Any feedback?
No. of entries
Information on EC 1.14.19.1 - stearoyl-CoA 9-desaturase
for references in articles please use BRENDA:EC1.14.19.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
1.14.19.1 stearoyl-CoA 9-desaturase
IUBMB Comments
An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2).
The enzyme appears in viruses and cellular organisms
- 1.14.19.1
-
sickle
- cardiac
- children
- ventricular
- pain
- hemoglobin
- arrhythmia
-
vaso-occlusive
-
transfusion
- anemia
- infarct
- cardiomyopathy
- episode
- cardiovascular
- coronary
- myocardial
- artery
-
stratification
-
polyunsaturated
-
ejection
- hydroxyurea
- stroke
-
monounsaturated
- crises
- chest
-
defibrillator
-
desaturation
-
lipogenesis
-
arrhythmogenic
- tachycardia
- hemoglobinopathy
-
all-cause
-
cardioverter
-
pufas
-
cardioverter-defibrillator
-
desaturases
-
electrocardiogram
-
lipogenic
-
transfused
- pharmacology
- thalassemia
-
12-lead
-
palmitoleic
- agriculture
- tachyarrhythmias
-
caregiver
-
out-of-hospital
-
resynchronization
- medicine
-
transcranial
- syncope
- drug development
-
holter
-
alloimmunization
Reaction Schemes
show+
2
+
+
2
=
+
2
+
2
Synonyms
scd, stearoyl-coa desaturase, fatty acid desaturase, scd-1, stearoyl-coa desaturase 1, stearoyl-coa desaturase-1, stearoyl coa desaturase, stearoyl-coenzyme a desaturase, delta9-desaturase, delta9 desaturase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl coenzyme A desaturase
-
-
-
-
acyl-CoA desaturase
delta-9 desaturase
DELTA-9 fatty acyl desaturase
DELTA9 desaturase
DELTA9 fatty acid desaturase
DELTA9-acyl CoA desaturase
-
-
-
-
DELTA9-desaturase
DELTA9-FAD
DesA3
EC 1.14.99.5
-
-
formerly
-
eicosatrienoyl-CoA desaturase
-
-
-
-
Fad1
FAD9
fatty acid 9-desaturase
-
-
-
-
fatty acid DELTA9-desaturase
-
-
-
-
fatty acid desaturase
fatty acyl CoA DELTA9-desaturase
-
-
-
-
fatty acyl DELTA9-desaturase
-
-
-
-
fatty acyl-CoA desaturase
-
-
-
-
long-chain fatty acid DELTA9-desaturase
-
-
-
-
membrane-bound stearoyl-CoA DELTA9 desaturase
palmitoyl CoA desaturase
-
-
-
-
palmitoyl-CoA desaturase
-
-
-
-
RtFad1
SCD
SCD-1
SCD-2
SCD1
SCD2
SCD3
SCD4
SCD5
stearoyl coenzyme A desaturase
-
-
-
-
stearoyl coenzyme-A desaturase 1
stearoyl-CoA (DELTA8) desaturase
-
-
-
-
stearoyl-CoA desaturase
stearoyl-CoA desaturase 1
stearoyl-CoA desaturase 2
stearoyl-CoA desaturase 5
stearoyl-CoA desaturase-1
stearoyl-CoA desaturase-2
stearoyl-CoA desaturase-5
stearoyl-coenzyme A desaturase
stearyl coenzyme A desaturase
-
-
-
-
stearyl-CoA desaturase
-
-
-
-
TGGT1 238950
TgSCD
acyl-CoA desaturase
-
-
-
-
DELTA9-desaturase
-
-
-
-
fatty acid desaturase
-
-
-
-
SCD1
-
-
SCD1
-
-
SCD1
-
SCD1
-
-
stearoyl-CoA desaturase
-
-
-
-
stearoyl-CoA desaturase
-
-
stearoyl-CoA desaturase
-
-
stearoyl-CoA desaturase 1
-
-
stearoyl-CoA desaturase 1
-
-
stearoyl-CoA desaturase-1
-
-
stearoyl-CoA desaturase-1
-
stearoyl-CoA desaturase-1
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the possible mechanism would be that dioxygen has to bind to both irons for effective two-electron transfer to the half-occupied antibonding pi orbitals of dioxygen to give a peroxide level intermediate
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cold exposure leads to an induced activity, in vivo cooling causes an activity induction of up to 15 to 30fold. Increase of desaturase synthesis by means of activated gene transcription. Transfer of cells to 10°C causes a smaller increase in activity compared to cells maintained at 30°C
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
regioselectivity, substrate specificity, probably extra-plastidal
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the reducing equivalents required for the desaturation site seem to be supplied from NADPH via cytochrome b5 as electron carrier
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
existence of three highly homologous isoforms: SCD1, SCD2 and SCD3 which show different substrate specificities, here SCD1 is mainly analysed
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
presence of two desaturase genes, isomers CDS1 and CDS2. Cooling treatment of carp causes significant changes to the activity of the DELTA9-desaturase. Modest cooling of carp shows an increase in acticity without any increase in the amount of desaturase protein, suggesting the activation of the pre-existing inactive latent enzyme, possibly by a post-translational mechanism
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
increase of activity induced by cold is preceded by the activation of latent desaturase, probably by a posttranslational mechanism. Amounts of desaturase transcript are increased as a result of cold-induced gene transcription
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
SSI2 gene encodes a member of a family of soluble fatty acid desaturases
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
introduction of double bonds at fixed positions from the carboxyl group of the fatty acid. D-hydrogen atoms are removed during desaturation. Mixed-function oxidase, acting via hydroxy acid intermediates. Acetyl-CoA desaturase, carboxylase and fatty acid synthetase are all controlled together as a unit and influenced by dietary components
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cytochrome b5, cytochrome b5 reductase and lipid and/or detergent are needed for all assays. A cis-hydrogen abstraction mechanism is involved in desaturation
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the synthesis is transcriptionally regulated by fat-free diet and sterols. Cholesterol-supplemented media as well as the transient transfection induces the expression of stearoyl-CoA desaturase RNA
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the synthesis is transcriptionally regulated by fat-free diet and sterols. Cholesterol-supplemented media as well as the transient transfection induces the expression of stearoyl-CoA desaturase RNA
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
it is suggested that in HepG2 cells the trans-10,cis-12 conjugated linoleic acid isomer regulates human desaturase activity mainly by a posttranslational mechanism
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
isolation of a third fatty acid DELTA9-desaturase. Higher activity with longer chain fatty acid substrates. Desaturase expression is induced significantly by increasing the ratio of carbon to nitrogen
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
multienzyme, insertion of a double bond in 9,10 position
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
incorporation of fatty acid into phospholipid. Enzyme may contain an essential thiol group. Endogenous saturated phospholipid is desaturated rapidly in all experiments in contrast with exogenous saturated phospholipid, which generally is not desaturated
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
presence of an unusual microsomal electron transport system associated with the desaturase
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
significant amounts of DELTA8-isomers are present
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
electron flow from NADH to cytochrome b5, via cytochrome b5 reductase. Different types of acyl-CoA desaturation show immunological differences
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
introduction of double bond at position 9
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. Formerly EC 1.14.99.5
-
-
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
arginyl and tyrosyl residues expected in the active site of enzyme
-
-
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the DELTA9-desaturase SCD-1 introduces a cis-double bond into saturated fatty acids between carbons 9 and 10. Preferred substrates of SCD-1 are long-chain acyl-CoAs with 13 to 19 carbons, among them stearoyl-CoA and palmitoyl-CoA, the most abundant saturated fatty acid-CoA ester in mammalians. Dehydrogenation of the pro-R hydrogens at C9 and C10 requires molecular oxygen which is activated at the di-iron center and reduced to water. Two of the electrons transferred to molecular oxygen derive from the acyl-CoA substrate and two others from the di-iron center. The ferrous catalytic center is regenerated by electron transfer from cytochrome b5, which has been suggested to bind to a groove at the cytoplasmic domain and to transmit electrons via two histidine residues bridging the distance. Ferrocytochrome b5 is provided by cytochrome b5 reductase using NAD(P)H as co-substrate
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
the DELTA9-desaturase SCD-1 introduces a cis-double bond into saturated fatty acids between carbons 9 and 10. Preferred substrates of SCD-1 are long-chain acyl-CoAs with 13 to 19 carbons, among them stearoyl-CoA and palmitoyl-CoA, the most abundant saturated fatty acid-CoA ester in mammalians. Dehydrogenation of the pro-R hydrogens at C9 and C10 requires molecular oxygen which is activated at the di-iron center and reduced to water. Two of the electrons transferred to molecular oxygen derive from the acyl-CoA substrate and two others from the di-iron center. The ferrous catalytic center is regenerated by electron transfer from cytochrome b5, which has been suggested to bind to a groove at the cytoplasmic domain and to transmit electrons via two histidine residues (H157 and H298) bridging the distance. Ferrocytochrome b5 is provided by cytochrome b5 reductase using NAD(P)H as co-substrate
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
presence of two desaturase genes, isomers CDS1 and CDS2. Cooling treatment of carp causes significant changes to the activity of the DELTA9-desaturase. Modest cooling of carp shows an increase in acticity without any increase in the amount of desaturase protein, suggesting the activation of the pre-existing inactive latent enzyme, possibly by a post-translational mechanism
-
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cold exposure leads to an induced activity, in vivo cooling causes an activity induction of up to 15 to 30fold. Increase of desaturase synthesis by means of activated gene transcription. Transfer of cells to 10°C causes a smaller increase in activity compared to cells maintained at 30°C
-
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
isolation of a third fatty acid DELTA9-desaturase. Higher activity with longer chain fatty acid substrates. Desaturase expression is induced significantly by increasing the ratio of carbon to nitrogen
Mortierella alpina CBS 528.72 / ATCC 32222
-
-
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
cytochrome b5, cytochrome b5 reductase and lipid and/or detergent are needed for all assays. A cis-hydrogen abstraction mechanism is involved in desaturation
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
oleate biosynthesis II (animals and fungi), palmitoleate biosynthesis IV (fungi and animals), sorgoleone biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
stearoyl-CoA,ferrocytochrome-b5:oxygen oxidoreductase (9,10-dehydrogenating)
An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. The ferricytochrome b5 produced is reduced by NADH and cytochrome-b5 reductase (EC 1.6.2.2).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9014-34-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
18-fluoro-10-thiaoctadecanoyl-[acyl-carrier protein] + O2 + ferredoxin
?
-
Substrates: -
Products: -
Products: -
?
myristic acid + NADH + O2 + ATP + CoA
myristoleic acid + NAD+ + H2O + ?
-
Substrates: reaction in presence of fatty acid-binding proteins with mixing at speeds between 250 and 500 rpm
Products: -
Products: -
?
myristoyl-CoA + NADH + O2
?
-
Substrates: 59% activity of stearoyl-CoA
Products: -
Products: -
?
myristoyl-CoA + NADH + O2
myristoleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
palmitoyl-CoA + AH2 + O2
palmitoleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + ferrocytochrome b5 + O2
palmitoleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + ferricytochrome b5 + 2 H2O
palmitoyl-CoA + NAD(P)H + O2
palmitoleate + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + NADPH + O2
palmitoleoyl-CoA + NADP+ + H2O
-
Substrates: Angus and American Wagyu steers, corn-fed steers for 8 mo (short-fed) or 16 mo (long-fed), and hay-fed steers fed for 12 mo (short-fed) and 20 mo (long-fed)
Products: -
Products: -
?
palmitoyl-CoA + NADPH + O2 + H+
palmitoleoyl-CoA + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
stearoyl-CoA + ferrocytochrome b5 + H+ + O2
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
trans-2-hexadecenoyl-CoA + ferrocytochrome b5 + O2 + H+
?
-
Substrates: -
Products: -
Products: -
?
myristoyl-CoA + AH2 + O2
?
-
Substrates: 59% activity of the rate with stearoyl-CoA
Products: -
Products: -
?
N-hydroxy-benzenecarboximidamide + NADH + H+ + O2
benzamidine + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
N-hydroxy-benzenecarboximidamide + NADH + H+ + O2
benzamidine + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
palmitic acid + AH2 + O2
palmitoleic acid + A + H2O
-
Substrates: -
Products: -
Products: -
?
palmitic acid + AH2 + O2
palmitoleic acid + A + H2O
Mortierella alpina CBS 528.72 / ATCC 32222
-
Substrates: -
Products: -
Products: -
?
palmitic acid + AH2 + O2
palmitoleic acid + A + H2O
-
Substrates: -
Products: -
Products: -
?
palmitic acid + reduced acceptor + O2
palmitoleic acid + acceptor + H2O
Substrates: preferred substrate
Products: -
Products: -
?
palmitic acid + reduced acceptor + O2
palmitoleic acid + acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
palmitic acid + reduced acceptor + O2
palmitoleic acid + acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
palmitic acid + reduced acceptor + O2
palmitoleic acid + acceptor + H2O
-
Substrates: isozyme Sls-FL2, preferred substrate
Products: Z-isomer, both isozymes
Products: Z-isomer, both isozymes
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + AH2 + O2
palmitoleoyl-CoA + A
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + AH2 + O2
palmitoleoyl-CoA + A
-
Substrates: 62% activity of the rate with stearoyl-CoA
Products: -
Products: -
?
palmitoyl-CoA + AH2 + O2
palmitoleoyl-CoA + A
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + ferricytochrome b5 + 2 H2O
-
Substrates: a key step in triglyceride synthesis in the fatty acid metabolic network
Products: -
Products: -
?
palmitoyl-CoA + ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + NADH + H+ + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: main substrate
Products: -
Products: -
?
palmitoyl-CoA + NADH + H+ + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: 13% conversion
Products: -
Products: -
?
palmitoyl-CoA + NADH + H+ + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: SCD activity of microsomal fraction
Products: -
Products: -
?
palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: 62% activity of stearoyl-CoA
Products: -
Products: -
?
palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
Substrates: slight activity
Products: -
Products: -
?
palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearate + AH2 + O2
oleate + A + 2 H2O
Mortierella alpina CBS 528.72 / ATCC 32222
-
Substrates: -
Products: -
Products: -
?
stearate + AH2 + O2
oleate + A + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearate + AH2 + O2
oleate + A + 2 H2O
-
Substrates: maximum activity
Products: -
Products: -
?
stearate + AH2 + O2
oleate + A + 2 H2O
-
Substrates: biosynthesis of unsaturated fatty acid, synthesis of triacylglycerol from oleate
Products: -
Products: -
?
stearate + reduced acceptor + O2
oleate + acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
stearate + reduced acceptor + O2
oleate + acceptor + H2O
Substrates: -
Products: -
Products: -
?
stearate + reduced acceptor + O2
oleate + acceptor + H2O
-
Substrates: isozyme Sls-FL1, preferred substrate
Products: Z-isomer, both isozymes
Products: Z-isomer, both isozymes
?
stearic acid + AH2 + O2
oleic acid + A + H2O
Substrates: the enzyme shows a preference for C18 saturated fatty acids
Products: -
Products: -
?
stearic acid + reduced acceptor + O2
oleic acid + acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
stearic acid + reduced acceptor + O2
oleic acid + acceptor + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-acyl-carrier protein + AH2 + O2
oleoyl-acyl-carrier protein + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-acyl-carrier protein + AH2 + O2
oleoyl-acyl-carrier protein + A + H2O
-
Substrates: key regulator of fatty acid desaturation of carbons 9 and 10
Products: -
Products: -
?
stearoyl-acyl-carrier protein + AH2 + O2
oleoyl-acyl-carrier protein + A + H2O
-
Substrates: insertion of a cis double bond between the 9 and 10 position, essential step in fatty acid biosynthesis
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Rhodotorula toruloides NBRC 8766
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + H+ + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: oleic acid biosynthesis
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: also other fatty acyl-CoA substrates
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
Substrates: activity measured via the generation of tritium enriched water from the substrate 9,10-3H-steaoryl-CoA
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, which plays an important role in lipid metabolism and body weight control, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, hepatic SCD1 activity may regulate fat accumulation in the liver and possibly protects from insulin resistance in obesity, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: the enzyme catalyzes the desaturation from saturated to monounsaturated fatty acids
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: stearoyl-CoA desaturase converts saturated to monounsaturated fatty acids and is a key enzyme in lipogenesis, elevated levels of endogenous lipogenesis increase the risk of fracture and suggest a role for saturated fat in the pathogenesis of osteoporosis
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, it is also involved in familial combined hyperlipidemia, fatty acid desaturation index, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: a key step in triglyceride synthesis in the fatty acid metabolic network
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, key enzyme in lipid metabolism and energy expenditure in mammals, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: stearoyl-CoA desaturase 2 is uniquely and absolutely required for adipogenesis, SCD2 also controls the maintenance of adipocyte-specific gene expression in fully differentiated 3T3-L1 adipocytes, including the expression of SCD1, polysome profile analysis, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, deficiency of isozyme SCD1 leads to activation of the metabolic pathways that promote fatty acid beta-oxidation in mice, enzyme regulation in the heart in a hormone-dependent fashion, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: essential enzyme activity, regulation mechanism, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: DesA3 expressed as a fusion with either a C-terminal His6 or c-myc tag has consistently higher activity and stability than native DesA3 having the native C-terminal sequence of LAA
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: essential enzyme activity, regulation mechanism, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: DesA3 expressed as a fusion with either a C-terminal His6 or c-myc tag has consistently higher activity and stability than native DesA3 having the native C-terminal sequence of LAA
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NAD(P)H + O2
oleoyl-CoA + NAD(P)+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NAD(P)H + O2
oleoyl-CoA + NAD(P)+ + H2O
-
Substrates: fatty acid desaturation
Products: -
Products: -
?
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: main substrate
Products: -
Products: -
?
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: 45% conversion
Products: -
Products: -
?
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
Substrates: high activity
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: preferred substrate for SCD1
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: Scd-/- and wild-type mice are fed with 20% high fat diets, fat-free basal mix is supplemented with 20% by weight of tristearin or triolein and 1% by weight corn oil
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: maximal activity
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: terminal component in the enzyme system
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: terminal component in the enzyme system
Products: -
Products: -
?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADPH + H+ + O2
oleoyl-CoA + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADPH + H+ + O2
oleoyl-CoA + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADPH + H+ + O2
oleoyl-CoA + NADP+ + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + NADPH + O2
oleoyl-CoA + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: preference for 18-carbon versus 16-carbon chain length fatty acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: Angus and Wagyu steers consuming high-roughage diets exhibit large differences in adipose tissue fatty acid composition, but there are no differences in terminal measures of CD activity or gene expression, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also produces cis-9, trans-11 conjugated linoleic acid and palmitoleoyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also produces cis-9, trans-11 conjugated linoleic acid and palmitoleoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also produces cis-9, trans-11 conjugated linoleic acid and palmitoleoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in the synthesis of unsaturated fatty acyl-CoAs
Products: -
Products: -
?
additional information
?
-
-
Substrates: incorporation of the first unsaturation bond into saturated fatty acids
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: fatty acid binding proteins my regulate the accessibility of fatty acids in the desaturation reaction to the active site
Products: -
Products: -
?
additional information
?
-
-
Substrates: rate limiting-step in the cellular synthesis of monounsaturated fatty acids mainly oleate and palmitoleate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activity measured by conversion of 14C-stearic acid to 14C-oleic acid, reverse-phase HPLC
Products: -
Products: -
?
additional information
?
-
-
Substrates: due to a population-based, longitudinal cohort study of men, the risk of fracture is highest among men with the highest levels of SCD activity index, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: aging human orbitofrontal cortex includes decreasing of polyunsaturated fatty acid composition associates increases in lipogenic gene expression and stearoyl-CoA desaturase activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: role of SCD1 in fatty acid metabolism in HepG2 cells, the desaturation systems in Hep-G2 cells are strongly compartmentalized, effects of SCD1 inhibition on fatty acid composition in HepG2 cells occur through changes in the dynamics of the fatty acid metabolic network and not through transcriptional regulatory mechanisms, overview
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: preference for stearate as substrate for SCD5
Products: -
Products: -
?
additional information
?
-
-
Substrates: SCD1 activity relies on endoplasmic reticulum-bound cytochrome b5 reductase which accepts an electron from NADH and donate it to cytochrome b5 and then to the SCD1 prosthetic iron for its reduction. In the presence of oxygen, reduced SCD1 introduces a single double bond at the delta-9,10-position of long-chain acyl-CoAs
Products: -
Products: -
?
additional information
?
-
Substrates: SCD1 activity relies on endoplasmic reticulum-bound cytochrome b5 reductase which accepts an electron from NADH and donate it to cytochrome b5 and then to the SCD1 prosthetic iron for its reduction. In the presence of oxygen, reduced SCD1 introduces a single double bond at the delta-9,10-position of long-chain acyl-CoAs
Products: -
Products: -
?
additional information
?
-
-
Substrates: inhibition of the enzyme in cholesterol-fed hamsters leads to reduced overall body weight and adipose tissue deposition, while enzyme inhibition in absence of cholesterol does not. Enzyme inhibition induces hypercholesterinemia, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: long-chain polyunsaturated fatty acid biosynthetic pathway
Products: -
Products: -
?
additional information
?
-
Mortierella alpina CBS 528.72 / ATCC 32222
-
Substrates: long-chain polyunsaturated fatty acid biosynthetic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: SCD2 and SCD3 preferentially utilize palmitoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: rate-limiting enzyme in the biosynthesis of monounsaturated fatty acids
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: SCD1 catalyses the DELTA9 desaturation of 12-19 carbon saturated fatty acids to monounsaturated fatty acids
Products: -
Products: -
?
additional information
?
-
Substrates: wild-type isozyme SCD3 is an exclusive 16:0 desaturase, while SCD3 enzyme mutant I112A/E113L is also active with stearoyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: wild-type isozyme SCD3 is an exclusive 16:0 desaturase, while SCD3 enzyme mutant I112A/E113L is also active with stearoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: wild-type isozyme SCD3 is an exclusive 16:0 desaturase, while SCD3 enzyme mutant I112A/E113L is also active with stearoyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: the desaturation reaction is catalyzed by a diiron center in SCD1 in a highly regio- and stereo-specific manner. The double bond is formed at the 9th position (DELTA9) of the acyl chain (regiospecificity) and with the cis configuration (stereospecificity). SCD1 can utilize saturated acyl-CoAs with an acyl chain length of 14-19 carbons as substrates but favors stearoyl-CoA (18:0 CoA) over others. The conformation of the bound stearoyl-CoA provides a simple explanation for both the regioselectivity and stereospecificity imposed by SCD1s. Mechanism of SCD1 catalysis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: DesA3 is a membrane-bound stearoyl-CoA desaturase that works together with oxidoreductase Rv3230c, encoded by gene rv3230c, to produce oleic acid, an 55 essential constituent of mycobacterial membrane phospholipids and triglycerides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme reacts with oxidoreductase Rv3230c to produce oleic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: DesA3 is a membrane-bound stearoyl-CoA desaturase that works together with oxidoreductase Rv3230c, encoded by gene rv3230c, to produce oleic acid, an 55 essential constituent of mycobacterial membrane phospholipids and triglycerides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme reacts with oxidoreductase Rv3230c to produce oleic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: glycerolipid such as phosphatidylcholine is involved as an intermediate substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: temperature-dependent chain length change is not mediated by a temperature-dependent change in desaturase substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: not acyl-CoA as substrate but phospholipid
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of unsaturated fatty acids. Possible substrates: acyl-CoA, acyl-acyl-carrier and acyl chains of phospholipids. The substrate in vivo is saturated phospholipid
Products: -
Products: -
?
additional information
?
-
-
Substrates: 12-19 carbon fatty acyl chains undergo 9,10 desaturation. Dephospho-, deamino- and (1-N6-etheno)-CoA analogs of stearoyl-CoA are poorer substrates than stearoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: specific for C14-C19 fatty acyl-CoA substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in the synthesis of unsaturated fatty acyl-CoAs
Products: -
Products: -
?
additional information
?
-
Substrates: decreased degradation of SCD is responsible for the increase in palmitoyl-CoA chain elongase activity in addition to increased transcription of SCD1 in the rats treated with clofibric acid, overview
Products: -
Products: -
?
additional information
?
-
Substrates: decreased degradation of SCD is responsible for the increase in palmitoyl-CoA chain elongase activity in addition to increased transcription of SCD1 in the rats treated with clofibric acid, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 12-19 carbon fatty acyl chains undergo 9,10 desaturation. Dephospho-, deamino- and (1-N6-etheno)-CoA analogs of stearoyl-CoA are poorer substrates than stearoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: stearic and palmitic acids are no substrates
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
palmitoyl-CoA + AH2 + O2
palmitoleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + ferricytochrome b5 + 2 H2O
-
Substrates: a key step in triglyceride synthesis in the fatty acid metabolic network
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearate + AH2 + O2
oleate + A + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearate + AH2 + O2
oleate + A + 2 H2O
-
Substrates: biosynthesis of unsaturated fatty acid, synthesis of triacylglycerol from oleate
Products: -
Products: -
?
stearoyl-acyl-carrier protein + AH2 + O2
oleoyl-acyl-carrier protein + A + H2O
-
Substrates: key regulator of fatty acid desaturation of carbons 9 and 10
Products: -
Products: -
?
stearoyl-acyl-carrier protein + AH2 + O2
oleoyl-acyl-carrier protein + A + H2O
-
Substrates: insertion of a cis double bond between the 9 and 10 position, essential step in fatty acid biosynthesis
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Rhodotorula toruloides NBRC 8766
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: oleic acid biosynthesis
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: also other fatty acyl-CoA substrates
Products: -
Products: -
?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, which plays an important role in lipid metabolism and body weight control, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, hepatic SCD1 activity may regulate fat accumulation in the liver and possibly protects from insulin resistance in obesity, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: the enzyme catalyzes the desaturation from saturated to monounsaturated fatty acids
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: stearoyl-CoA desaturase converts saturated to monounsaturated fatty acids and is a key enzyme in lipogenesis, elevated levels of endogenous lipogenesis increase the risk of fracture and suggest a role for saturated fat in the pathogenesis of osteoporosis
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, it is also involved in familial combined hyperlipidemia, fatty acid desaturation index, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: a key step in triglyceride synthesis in the fatty acid metabolic network
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, key enzyme in lipid metabolism and energy expenditure in mammals, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: stearoyl-CoA desaturase 2 is uniquely and absolutely required for adipogenesis, SCD2 also controls the maintenance of adipocyte-specific gene expression in fully differentiated 3T3-L1 adipocytes, including the expression of SCD1, polysome profile analysis, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, deficiency of isozyme SCD1 leads to activation of the metabolic pathways that promote fatty acid beta-oxidation in mice, enzyme regulation in the heart in a hormone-dependent fashion, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: essential enzyme activity, regulation mechanism, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: essential enzyme activity, regulation mechanism, overview
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: Angus and Wagyu steers consuming high-roughage diets exhibit large differences in adipose tissue fatty acid composition, but there are no differences in terminal measures of CD activity or gene expression, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in the synthesis of unsaturated fatty acyl-CoAs
Products: -
Products: -
?
additional information
?
-
-
Substrates: incorporation of the first unsaturation bond into saturated fatty acids
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: heterologous expression in yeast shows that Dpu-DELTA9-KPSE produces E9 mono-unsaturated fatty acids of various chain lengths. When provided with the (7Z)-tetradec-7-enoate, it forms the (7Z,9E)-tetradec-7,9-dienoate unsaturated fatty acids, another biosynthetic intermediate that can be chain-shortened to (5Z,7Z)-dodeca-5,7-dienoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: rate limiting-step in the cellular synthesis of monounsaturated fatty acids mainly oleate and palmitoleate
Products: -
Products: -
?
additional information
?
-
-
Substrates: due to a population-based, longitudinal cohort study of men, the risk of fracture is highest among men with the highest levels of SCD activity index, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: aging human orbitofrontal cortex includes decreasing of polyunsaturated fatty acid composition associates increases in lipogenic gene expression and stearoyl-CoA desaturase activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: role of SCD1 in fatty acid metabolism in HepG2 cells, the desaturation systems in Hep-G2 cells are strongly compartmentalized, effects of SCD1 inhibition on fatty acid composition in HepG2 cells occur through changes in the dynamics of the fatty acid metabolic network and not through transcriptional regulatory mechanisms, overview
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
-
Substrates: inhibition of the enzyme in cholesterol-fed hamsters leads to reduced overall body weight and adipose tissue deposition, while enzyme inhibition in absence of cholesterol does not. Enzyme inhibition induces hypercholesterinemia, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: long-chain polyunsaturated fatty acid biosynthetic pathway
Products: -
Products: -
?
additional information
?
-
Mortierella alpina CBS 528.72 / ATCC 32222
-
Substrates: long-chain polyunsaturated fatty acid biosynthetic pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: rate-limiting enzyme in the biosynthesis of monounsaturated fatty acids
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
Products: -
Products: -
?
additional information
?
-
Substrates: SCD1 catalyses the DELTA9 desaturation of 12-19 carbon saturated fatty acids to monounsaturated fatty acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: DesA3 is a membrane-bound stearoyl-CoA desaturase that works together with oxidoreductase Rv3230c, encoded by gene rv3230c, to produce oleic acid, an 55 essential constituent of mycobacterial membrane phospholipids and triglycerides
Products: -
Products: -
?
additional information
?
-
-
Substrates: DesA3 is a membrane-bound stearoyl-CoA desaturase that works together with oxidoreductase Rv3230c, encoded by gene rv3230c, to produce oleic acid, an 55 essential constituent of mycobacterial membrane phospholipids and triglycerides
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of unsaturated fatty acids. Possible substrates: acyl-CoA, acyl-acyl-carrier and acyl chains of phospholipids. The substrate in vivo is saturated phospholipid
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme in the synthesis of unsaturated fatty acyl-CoAs
Products: -
Products: -
?
additional information
?
-
Substrates: decreased degradation of SCD is responsible for the increase in palmitoyl-CoA chain elongase activity in addition to increased transcription of SCD1 in the rats treated with clofibric acid, overview
Products: -
Products: -
?
additional information
?
-
Substrates: decreased degradation of SCD is responsible for the increase in palmitoyl-CoA chain elongase activity in addition to increased transcription of SCD1 in the rats treated with clofibric acid, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome b5
a redox-active co-substrate reducing molecular oxygen to water. Ferrocytochrome b5 is regenerated by reduction of ferricytochrome b5 through cyt. b5 reductase using NADPH as electron donor
-
cytochrome b5
a redox-active co-substrate reducing molecular oxygen to water. Ferrocytochrome b5 is regenerated by reduction of ferricytochrome b5 through cyt. b5 reductase using NADPH as electron donor
-
cytochrome b5
enzyme SCD1 has a diiron center, and its proper function requires an electron transport chain composed of NADH (or NADPH), cytochrome b5 reductase (b5R), and cytochrome b5 (cyt b5)
-
ferrocytochrome b5
dependent on, the enzyme also requires the presence of NADH-cytochrome b5 reductase
NADPH
-
specifically required, seems not to be directly involved in the desaturation reaction but serves to keep another cofactor in the reduced state, maybe FADH
NADPH
SCD is mainly dependent on NADPH, no oleic acid is produced in the absence of NADPH
additional information
-
requires some other form of reduced cofactor than a reduced nicotinamide nucleotide, no special cofactor requirement
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mg2+
Zn2+
additional information
Fe2+
-
iron-sulfur protein(s) may act as electron carrier(s) in place of the cytchrome b5 and NADH cytochrome b5 reductase system associated with the mammalian desaturase systems
Fe2+
SCD-1 has a di-metal catalytic center consisting of two iron cations (in the crystal structures replaced by zinc cations) that are coordinated by histidine residues and a single water molecule
Fe2+
SCD-1 has a di-metal catalytic center consisting of two iron cations (in the crystal structures replaced by zinc cations) that are coordinated by histidine residues and a single water molecule
Fe2+
required, enzyme SCD1 has a diiron center. The redox state of the bound irons is tracked by precise spectroscopic studies such as UV-vis spectroscopy and electron paramagnetic resonance and by structural studies via X-ray crystallography
Fe2+
-
contains one atom of non-heme iron per enzyme molecule, catalytic function
Fe2+
-
each subunit of homodimer contains one binuclear non-heme iron active site. The reduced DELTA9-desaturase has two approximately equivalent 5-coordinate irons in a distorted square pyramidal geometry, a two-in-two-out equatorial distortion, the irons are rhombic, weakly antiferromagnetically coupled. Addition of substrate causes dramatic changes, first ion remains 5-coordinate but is distorted toward a trigonal bipyramidal structure, second iron changes to 4-coordinate
Zn2+
incorporation of zinc instead of iron into the protein is likely an artifact of protein overexpression, and zinc remains the predominant metal species even when the growth media and purification solutions are supplemented with iron. Coordination of both zinc ions is consistent with octahedral geometry with one missing ligand. The nine histidines are highly conserved, and eight of them belong to three histidine-containing motifs (two HXXHH motifs and one HX4H motif in SCD1) that are characteristic of integral membrane desaturases
additional information
the enzyme is inactive when Fe2+ is substituted for Zn2+. Although Zn2+ serves as a surrogate to maintain the structural integrity because of its similar ionic radius and charge property to a ferrous ion (Fe2+), misincorporation of Zn2+ renders the enzyme inactive and thus hampers further investigation of the enzymatic reaction mechanism. The misincorporation of Zn2+ is not unique to SCD1, and it has also been reported in the production of other enzymes such as yeast fatty acid alpha-hydroxylase and quinol-dependent nitric-oxide reductase. The most efficient way of replacing zinc ions is to dialyze SCD1 first against two strong zinc chelators, N,N,N',N'-tetrakis(2-pyridinylmethyl)-1,2-ethanediamine (TPEN, 100 microM) and dipicolinic acid (DPA, 10 mM), and then against high concentrations of ferrous ions (10 mM)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1-[6-[3-(3-hydroxybenzyl)-1,2,4-oxadiazol-5-yl]pyridazin-3-yl]piperidin-4-yl)[2-(trifluoromethyl)phenyl]methanone
(1-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-imidazol-4-yl)methanol
-
-
(1-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-4-yl)methanol
-
-
(2-(1-(3,4,5-trichlorobenzyl)-1H-1,2,3-triazol-4-yl)imidazo[1,2-a]pyridin-7-yl)methanol
-
(2-[(4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino)-thiazol-5-yl)-acetic acid
-
(2-[(5-([2-(3-methyl-butyl)-phenylamino]-methyl)-thiophene-2-carbonyl)-amino]-thiazol-4-yl)-acetic acid
(2-[[(5-[[(4-fluoro-2-heptylphenyl)amino]methyl]thiophen-2-yl)carbonyl]amino]-1,3-thiazol-4-yl)acetic acid
(2R)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
(2S)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
(3(2)R,3(5)S,5S)-5-(tert-butyl)-N-((1R,2S)-1-((cyclopropylsulfonyl)carbamoyl)-2-vinylcyclopropyl)-4,7-dioxo-2,8-dioxa-6-aza-1(1,7)-isoquinolina-3(2,1)-pyrrolidinacyclotridecaphane-3(5)-carboxamide
-
(3-[5-[(3S)-3-(2-bromo-5-fluorophenoxy)pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl]-1,2,4-oxadiazol-5-yl)methanol
(4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]phenyl)methanol
-
-
(5-(6-(3-(2-(trifluoromethyl)phenoxy)azetidin-1-yl)pyridazin-3-yl)-1,3,4-oxadiazol-2-yl)methanol
-
(5-(6-(4-(2-(trifluoromethyl)phenoxy)piperidin-1-yl)pyridazin-3-yl)-1,3,4-oxadiazol-2-yl)methanol
-
(5-(6-(4-(2-bromo-5-fluorophenoxy)piperidin-1-yl)pyridazin-3-yl)pyridin-3-yl)methanol
-
(5-[6-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
(5-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]pyridin-2-yl)methanol
-
-
(5R)-5-(hydroxymethyl)-3-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridin-3-yl)-1,3-oxazolidin-2-one
(E)-N-(2-cyclopropylethyl)-N2-(pyridin-2-yl[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]methylidene)glycinamide
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]amino)acetic acid
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]oxy)acetic acid
1'-[6-(3-methyl-1,2,4-thiadiazol-5-yl)pyridazin-3-yl]-2,3-dihydrospiro[indene-1,4'-piperidine]
1-(1-[6-[1-(2-ethoxyethyl)-1H-pyrazol-4-yl]pyridazin-3-yl]piperidin-4-yl)-6-fluoro-2,3-dihydro-1H-indole
-
-
1-(1-[6-[4-(ethoxymethyl)-1H-pyrazol-1-yl]pyridazin-3-yl]piperidin-4-yl)-6-fluoro-2,3-dihydro-1H-indole
-
-
1-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)urea
-
-
1-hydroxy-3-[5-(6-[3-[2-(trifluoromethyl)benzyl]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]propan-2-one
1-[1-[6-(1-ethyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-6-fluoro-2,3-dihydro-1H-indole
-
-
1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1H-indole
-
-
1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-6-(trifluoromethyl)-2,3-dihydro-1H-indole
-
-
1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
1-[5-(5-methyl-1,3,4-thiadiazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(benzylcarbamoyl)-4-methyl-1,3-thiazol-2-yl]-N-(4-fluorobenzyl)-1H-1,2,3-triazole-4-carboxamide
2,3-dihydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((6-(trifluoromethyl)pyridin-3-yl)methyl)-thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(piperidin-3-ylmethyl)thiazole-5-carboxamide trifluoroacetic acid salt
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
2-(1-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-4-yl)ethanol
-
-
2-(2'-fluorobiphenyl-4-yl)-1-methyl-5-(methylsulfonyl)-2,3-dihydro-1H-benzimidazole
-
-
2-(2-cyclopropylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1H-isoindole-1,3(2H)-dione
2-(3'-chloro-2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
-
-
2-(4-phenoxyphenyl)-N-(1,3-thiazol-2-ylmethyl)-1H-benzimidazole-5-carboxamide
-
-
2-(4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino)-thiazole-5-carboxylic acid
-
2-(4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-1-yl)-N-methylacetamide
-
-
2-(4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-1-yl)ethanol
-
-
2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxylic acid
-
-
2-(4-[[5-(hexylamino)-2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-N-pentylpyridine-4-carboxamide
2-(5'-chloro-2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
-
-
2-(5-[1-[(2,5-dichlorophenyl)carbonyl]piperidin-4-ylidene]-2,4-dioxo-1,3-thiazolidin-3-yl)-N-pentylacetamide
2-(thiophen-2-yl)-N-(2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1H-benzimidazol-5-yl)acetamide
-
-
2-([2-[4-(2-chloro-3,5-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylbenzamide
2-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-phenylbenzamide
-
-
2-acetyl-N-[1-(3,4-dichlorobenzyl)-1H-pyrazol-4-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
2-hydroxy-N-[2-[2-oxo-3-(trifluoromethyl)-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
2-hydroxy-N-[2-[3-(1-methylethyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
2-methyl-5-(6-(4-(2-(trifluoromethyl)phenoxy) piperidin-1-yl)pyridazin-3-yl)-1,3,4-thiadiazole
-
MF-438, known enzyme inhibitor
-
2-[1-[2-(4-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]-4-methyl-N-(pyridin-3-ylmethyl)-1,3-thiazole-5-carboxamide
2-[3-(4-fluorobenzyl)-2-oxo-2,3-dihydro-1H-imidazol-1-yl]-N-(pyridin-3-ylmethyl)-4-(trifluoromethyl)-1,3-thiazole-5-carboxamide
2-[4-(2-chlorophenoxy)phenyl]-N-(1,3-thiazol-2-ylmethyl)-1H-benzimidazole-5-carboxamide
-
-
2-[4-(2-chlorophenoxy)phenyl]-N-(2-cyclopropylethyl)-1H-benzimidazole-5-carboxamide
-
-
2-[4-(2-chlorophenoxy)phenyl]-N-(3-methylbutyl)-1H-benzimidazole-5-carboxamide
-
-
2-[4-(2-chlorophenoxy)phenyl]-N-[(5-chlorothiophen-2-yl)methyl]-1H-benzimidazole-5-carboxamide
-
-
2-[6-(benzyloxy)pyridazin-3-yl]-5-(1-[2-(trifluoromethyl)phenyl]ethenyl)-1,2,3,4,5,6-hexahydropyrrolo[3,4-c]pyrrole
-
i.e. SAR707, known enzyme inhibitor
-
2-[[4-(2-chlorophenoxy)piperidine-1-carbonyl]amino]-N-methylpyridine-4-carboxamide
-
2-[[4-(2-chlorophenoxy)piperidine-1-carbonyl]amino]-N-methylpyridine-4-carboxamide attenuates tumor progression and demonstrates excellent bioavailability
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-((1-methyl-1H-pyrazol-4-yl)methyl)-1H-pyrazole-5-carboxamide
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(oxazol-4-ylmethyl)-1H-pyrazole-5-carboxamide
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-4-ylmethyl)-1H-pyrazole-5-carboxamide
3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2,3-dihydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-(4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino)-thiazol-5-yl)-propionic acid
-
3-(2-hydroxy-2-methylpropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxy-ethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-4-methoxy-N-(5-[[3-(trifluoromethyl)phenyl]carbonyl]-1,3-thiazol-2-yl)benzamide
3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-4-[(methylsulfonyl)amino]-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
3-(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-propionic acid
-
3-(3-hydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
3-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazino[3,4-b][1,5]benzoxazepin-5(6H)-one
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[3-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
-
-
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
3-(5-[hydroxy[2-(trifluoromethyl)phenyl]methyl]-1H-benzimidazol-2-yl)-N-(1,3-thiazol-2-ylmethyl)benzamide
-
-
3-([2-[4-(2,3-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
-
-
3-([2-[4-(2,5-dichlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
-
-
3-([2-[4-(2-bromophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
-
-
3-([2-[4-(2-chloro-3,5-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
-
-
3-([2-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(2-hydroxyethyl)pyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(pyridin-2-ylmethyl)pyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(pyridin-3-ylmethyl)pyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(pyridin-4-ylmethyl)pyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-ethylpyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-phenylpyrazine-2-carboxamide
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carbaldehyde
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carbonitrile
-
-
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxamide
-
-
3-chloro-N-[2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]pyrazin-2-amine
-
-
3-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-(2-phenylethyl)pyridine-2-carboxamide
-
-
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-(pyridin-3-ylmethyl)pyridine-2-carboxamide
-
-
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-(pyridin-4-ylmethyl)pyridine-2-carboxamide
-
-
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-pentylpyridine-2-carboxamide
-
-
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-propylpyridine-2-carboxamide
-
-
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
-
-
3-[([4-[2-(acetylamino)ethyl]-2-(4-methoxyphenyl)-3-oxo-3,4-dihydropyrido[2,3-b]pyrazin-6-yl]amino)methyl]benzoic acid
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]-N-methylpropanamide
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
3-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]propanamide
3-[2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-7-oxo-6,7-dihydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]propanoic acid
3-[3-(2,6-dichloro-4-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-chloro-5-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
3-[3-[2-chloro-3-(trifluoromethyl)phenoxy]azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,2,4-oxadiazole-5-carboxamide
-
-
3-[6-(4'-chlorobiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
3-[6-(4'-methylbiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
3-[6-(4-methoxyphenyl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
3-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
3-[7-oxo-6-(4-pyridin-3-ylphenyl)-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
4-(1,2-benzoxazol-3-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
-
-
4-(1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
-
-
4-(1H-indol-1-yl)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(1H-indol-3-yl)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
15% inhibition at 0.001 mM
4-(2,3-dihydro-1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
-
-
4-(2,3-dihydro-1H-indol-1-yl)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-bromo-5-fluorophenoxy)-1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3,4-thiadiazol-2-yl]piperidine
4-(2-chloro-phenoxy)-piperidine-1-carboxylic acid tert-butyl ester
-
i.e. Abbott 10b
-
4-(2-chlorophenoxy)-N-[3-[(methylamino)carbonyl]phenyl]-1-piperidinecarboxamide
i.e. A939 or A939572, an SCD1 inhibitor, causes significantly delayed tumor growth, which is reversed by L-cycloserine, an inhibitor of ceramide biosynthesis. A939 can significantly inhibit LOVO cell proliferation, which can be dose-dependently reversed by oleic acid, but not by palmitic acid
4-(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-butyric acid
-
4-(3,4-dihydroquinolin-1(2H)-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl)piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4-oxo-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrazin-2-yl)piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(5-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(6-hydroxy-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl)piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[4-(2-hydroxyethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[4-(hydroxymethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[4-(methylcarbamoyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
-
20% inhibition at 0.001 mM
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(2-hydroxyethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(hydroxyacetyl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(hydroxymethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
-
-
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(methylcarbamoyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
-
-
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
4-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
4-hydroxymethyl-2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazole-5-carboxylic acid
-
4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
4-methyl-2-[2-oxo-3-[4-(trifluoromethyl)benzyl]-2,3-dihydro-1H-imidazol-1-yl]-N-(pyridin-3-ylmethyl)-1,3-thiazole-5-carboxamide
4-[(7-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-5,6,7,7a-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl)methoxy]benzoic acid
4-[2-(dimethylamino)ethoxy]-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]benzoic acid
-
-
5-(4-(2-bromo-5-fluorophenoxy)piperidin-1-yl)thiazolo[5,4-d]pyrimidin-2-amine
-
5-(hydroxymethyl)-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
5-chloro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
5-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
5-fluoro-3-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1,2-benzoxazole
-
-
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
5-[(2-hexyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid (4-hydroxymethyl-thiazol-2-yl)-amide
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
5-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-N,N-dimethylpyridin-2-amine
-
-
5-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-N-methylpyridine-2-carboxamide
-
-
6-(3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
6-(3-bromobenzyl)-5,7-dimethyl-N-(tetrahydrofuran-2-ylmethyl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxylic acid
-
-
6-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)pyridine-3-carboxylic acid
6-(methylsulfonyl)-2-[4-(3-methylthiophen-2-yl)phenyl]-1H-benzimidazole
-
-
6-chloro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-(1-[6-[4-(trifluoromethyl)phenyl]pyridazin-3-yl]piperidin-4-yl)-2,3-dihydro-1H-indole
-
-
6-fluoro-1-(1-[6-[6-(trifluoromethyl)pyridin-3-yl]pyridazin-3-yl]piperidin-4-yl)-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1H-indazole
-
-
6-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1H-indole
-
-
6-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(1-propyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(3-methyl-1,2,4-thiadiazol-5-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(4-fluorophenyl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(4-methyl-1,3-thiazol-2-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(4-methyl-1H-imidazol-1-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(4-methyl-1H-pyrazol-1-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(4-methylphenyl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(5-methyl-1,3-thiazol-2-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(5-methylthiophen-2-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(6-methoxypyridin-3-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-fluoro-1-[1-[6-(6-methylpyridin-3-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-methoxy-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-methyl-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
-
-
6-[(3,4-dichlorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
6-[(3-chloro-4-fluorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
6-[4-[(2-bromo-5-methoxyphenyl)carbonyl]piperazin-1-yl]-N-(3-phenylpropyl)pyridine-3-carboxamide
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
6-[5-chloro-2-(trifluoromethyl)benzyl]-N-hexyl-5,6,7,8-tetrahydro-1,6-naphthyridine-2-carboxamide
7-[(3-chlorobenzyl)amino]-1-(4-oxopentyl)-3-(3-pyridin-4-ylphenyl)pyrido[3,4-b]pyrazin-2(1H)-one
7-[(3-chlorobenzyl)amino]-3-(4-methoxyphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
7-[(3-chlorobenzyl)amino]-3-(4-methylphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
8-(trifluoromethyl)-2,5,21,24,25-pentaazatetracyclo[21.2.2.2-2,5.1-7,11]triaconta-1(25),7(28),8,10,23,26-hexaene-6,22-dione
ethyl 2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxylate
-
-
ethyl [5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-oxadiazol-2-yl]acetate
fenretinide
i.e. N-(4-hydroxyphenyl)retinamide, a synthetic retinoid, leads to an increase in C16 and C18 dihydroceramide substrate accumulation. Fenretinide induces degradation of SCD1 in human Rretinal pigment epithelium cells
methyl 3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxylate
-
-
methyl sterculate
inhibits the synthesis of oleic acid both with parasite lysates and infected erythrocytes, most likely by targeting SCD
methyl [5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-thiadiazol-2-yl]acetate
N,N-dimethyl-2-((4-((5-methylthiazol-2-yl)carbamoyl)benzyl)amino)benzamide
-
N,N-dimethyl-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
-
-
N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
N-(1,3-thiazol-2-yl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-(1,3-thiazol-2-ylmethyl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-(2-(7-((4-chloro-3-(trifluoromethyl)benzyl)amino)-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl)ethyl)acetamide
-
N-(2-cyclopropyl-2-hydroxyethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-2-(4-phenoxyphenyl)-1H-benzimidazole-5-carboxamide
-
-
N-(2-cyclopropylethyl)-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-4-carboxamide
-
-
N-(2-cyclopropylethyl)-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
N-(2-cyclopropylethyl)-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-(2-cyclopropylethyl)-3-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1H-pyrazole-5-carboxamide
N-(2-cyclopropylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3,4-thiadiazole-2-carboxamide
N-(2-cyclopropylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
N-(2-cyclopropylethyl)-6-(4-[[5-fluoro-2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
N-(2-cyclopropylethyl)-6-[(1-[[2-(trifluoromethyl)phenyl]carbonyl]azetidin-3-yl)amino]pyridazine-3-carboxamide
N-(2-cyclopropylethyl)-6-[4-[3-(trifluoromethyl)pyridin-2-yl]piperazin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-(2-hydroxyethyl)-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
-
-
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
N-(2-[2-[(3,4-dichlorobenzyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)benzamide
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)methanesulfonamide
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)propanamide
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)thiophene-3-carboxamide
N-(2-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]ethyl)acetamide
N-(2-[2-[(3-chloro-4-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
N-(2-[2-[(3-chlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
N-(2-[2-[(4-chloro-3-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
N-(2-[6-[(2-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2,2-dimethyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-methyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
N-(2-[6-[(3,4-dichlorobenzyl)amino]-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
N-(2-[6-[(3-chloro-4-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
N-(2-[6-[(3-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
N-(2-[6-[(3-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
N-(2-[6-[(3-methoxybenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
N-(2-[6-[(4-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxopyrido[3,4-b]pyrazin-1(2H)-yl]ethyl)acetamide
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
N-(2-[7-[(3,4-dimethylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
N-(2-[7-[(4-fluoro-3-methylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
N-(3-methylbutyl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-(3-methylbutyl)-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-(3-methylbutyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
N-(3-methylbutyl)-6-oxo-8-[[2-(trifluoromethyl)phenyl]carbonyl]-6,6a,7,8,9,10-hexahydro-5H-pyrazino[1',2':1,6]pyrazino[2,3-c]pyridazine-3-carboxamide
N-(3-methylbutyl)-6-[[2-(trifluoromethyl)phenyl]carbonyl]-4,5,6,7-tetrahydrofuro[2,3-c]pyridine-2-carboxamide
N-(3-phenylpropyl)-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-(4-carbamoyl-1,3-thiazol-2-yl)-4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
-
-
N-(4-methyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
-
N-(4-methylthiazol-2-yl)-4-(((2-(trifluoromethyl)phenyl)amino)methyl)piperidine-1-carboxamide
-
N-(4-methylthiazol-2-yl)-5-(((2-(trifluoromethyl)phenyl)amino)methyl)thiophene-2-carboxamide
-
N-(5-acetyl-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)-4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
-
46% inhibition at 0.001 mM
N-(5-carbamoyl-1,3-thiazol-2-yl)-4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
-
-
N-(5-hydroxymethyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
-
N-(6,7-dihydro-4H-pyrano[4,3-d][1,3]thiazol-2-yl)-4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
-
-
N-(cyclopentylmethyl)-6-[5-[[2-(trifluoromethyl)phenyl]carbonyl]-3,4,5,6-tetrahydropyrrolo[3,4-c]pyrrol-2(1H)-yl]pyridine-3-carboxamide
N-(cyclopropylmethyl)-2-(4-phenoxyphenyl)-1H-benzimidazole-5-carboxamide
-
-
N-(thiophen-2-ylmethyl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-benzyl-2-(3-(4-fluorobenzyl)-2-oxoimidazolidin-1-yl)-4-methylthiazole-5-carboxamide
-
N-benzyl-3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxamide
-
-
N-benzyl-3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyridine-2-carboxamide
-
-
N-benzyl-4-methyl-2-(1-[2-[methyl(phenyl)amino]ethyl]-1H-pyrazol-3-yl)-1,3-thiazole-5-carboxamide
N-benzyl-6-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
-
-
N-ethyl-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
-
-
N-methoxy-3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
N-methyl-2-(2-oxo-2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]ethoxy)benzamide
-
-
N-methyl-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
-
-
N-methyl-2-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-3-carboxamide
-
-
N-methyl-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-methyl-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
-
-
N-methyl-3-[[2-oxo-2-(4-phenoxypiperidin-1-yl)ethyl]amino]pyrazine-2-carboxamide
-
-
N-methyl-3-[[2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]pyrazine-2-carboxamide
-
-
N-methyl-3-[[2-oxo-2-(4-[[2-(trifluoromethyl)phenyl]amino]piperidin-1-yl)ethyl]amino]pyrazine-2-carboxamide
-
-
N-methyl-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-imidazo[4,5-c]pyridin-4-amine
N-tert-butyl-3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxamide
-
-
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
N-[(5-chlorothiophen-2-yl)methyl]-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-[(5-chlorothiophen-2-yl)methyl]-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
-
-
N-[(5-chlorothiophen-2-yl)methyl]-3-(5-[hydroxy[2-(trifluoromethyl)phenyl]methyl]-1H-benzimidazol-2-yl)benzamide
-
-
N-[(6-chloropyridin-3-yl)methyl]-2-[4-[(4-fluorobenzyl)oxy]-2-oxopyridin-1(2H)-yl]-4-methyl-1,3-thiazole-5-carboxamide
N-[1-[5-chloro-2-(cyclopropylmethoxy)benzyl]-5-methyl-1H-pyrazol-3-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
N-[2-(4-[[2-fluoro-5-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-2-oxoethyl]-5-(2-methoxyphenyl)-1H-pyrazole-3-carboxamide
N-[2-(4-[[2-fluoro-5-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-2-oxoethyl]biphenyl-4-carboxamide
N-[2-(5-chlorothiophen-2-yl)ethyl]-2-(4-phenoxyphenyl)-1H-benzimidazole-5-carboxamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[6-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(2,2,2-trifluoroethoxy)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[4-(2,2,2-trifluoroethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[2-(4-methoxyphenyl)-6-[(3-methylbenzyl)amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[2-(4-methoxyphenyl)-6-[[(5-methylisoxazol-3-yl)methyl]amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[2-oxo-3-pyridin-3-yl-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
N-[2-[3-(4-ethylphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)quinoxalin-1(2H)-yl]ethyl]acetamide
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
N-[2-[3-(4-methoxyphenyl)-7-[(3-methylbenzyl)amino]-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
N-[2-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[3-tert-butyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]-2-hydroxyacetamide
N-[2-[6-(benzylamino)-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[6-[[2-fluoro-5-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[6-[[3,5-bis(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[6-[[4-fluoro-3-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
N-[3-(methylcarbamoyl)phenyl]-4-(2-oxo-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
-
7% inhibition at 0.001 mM
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
N-[4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
N-[5-(2-hydroxy-ethyl)-4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
-
N-[5-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
-
N-[5-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
-
N-[5-methyl-1-[3-(trifluoromethyl)benzyl]-1H-pyrazol-3-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
N-[5-[(2-chlorophenoxy)methyl]-1,3,4-thiadiazol-2-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
N-[[2-(benzyloxy)pyridin-4-yl]methyl]-4-[2-(trifluoromethyl)benzoyl]piperazine-1-carboxamide
-
-
[(5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-5,7a-dihydro[1,3]thiazolo[4,5-d]pyrimidin-7-yl)oxy]acetic acid
[2-((5-[(2-benzyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
[2-((5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
[2-([[4-([[2-(2-cyclopentylethyl)phenyl]amino]methyl)phenyl]carbonyl]amino)-1,3-thiazol-4-yl]acetic acid
[2-([[4-([[2-(trifluoromethyl)phenyl]amino]methyl)piperidin-1-yl]carbonyl]amino)-1,3-thiazol-4-yl]acetic acid
[2-methoxy-4-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
[2-methoxy-5-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
[2-[4-(benzyloxy)phenyl]-1H-benzimidazol-5-yl][2-(trifluoromethyl)phenyl]methanol
-
-
[2-[4-(benzyloxy)phenyl]-1H-benzimidazol-5-yl][2-(trifluoromethyl)phenyl]methanone
-
-
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
[3-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)-1H-1,2,4-triazol-1-yl]acetic acid
[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl][2-(trifluoromethyl)phenyl]methanone
-
-
[5-(2-[3-[2-bromo-5-(trifluoromethyl)phenoxy]propoxy]-1,3-thiazol-5-yl)-2H-tetrazol-2-yl]acetic acid
[5-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)-1H-tetrazol-1-yl]acetic acid
[5-(6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
[5-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
[5-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazin-3-yl)-1,3,4-thiadiazol-2-yl]acetic acid
[5-[2-([(2S)-3-[2-bromo-5-(trifluoromethoxy)phenoxy]-2-methylpropyl]oxy)-1,3-thiazol-5-yl]-2H-tetrazol-2-yl]acetic acid
[5-[6-(benzyloxy)pyridazin-3-yl]-3,4,5,6-tetrahydropyrrolo[3,4-c]pyrrol-2(1H)-yl][2-(trifluoromethyl)phenyl]methanone
-
-
(1-[6-[3-(3-hydroxybenzyl)-1,2,4-oxadiazol-5-yl]pyridazin-3-yl]piperidin-4-yl)[2-(trifluoromethyl)phenyl]methanone
-
-
(1-[6-[3-(3-hydroxybenzyl)-1,2,4-oxadiazol-5-yl]pyridazin-3-yl]piperidin-4-yl)[2-(trifluoromethyl)phenyl]methanone
-
-
(2-(4-[(2-benzyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-benzyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-butyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-butyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-chloro-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-chloro-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-hexyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-hexyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-octyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-(4-[(2-octyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
-
(2-[(5-([2-(3-methyl-butyl)-phenylamino]-methyl)-thiophene-2-carbonyl)-amino]-thiazol-4-yl)-acetic acid
-
(2-[(5-([2-(3-methyl-butyl)-phenylamino]-methyl)-thiophene-2-carbonyl)-amino]-thiazol-4-yl)-acetic acid
-
(2-[4-(biphenyl-2-ylaminomethyl)-benzoylamino]-thiazol-4-yl)-acetic acid
-
(2-[4-(biphenyl-2-ylaminomethyl)-benzoylamino]-thiazol-4-yl)-acetic acid
-
(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-acetic acid
-
(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-acetic acid
-
(2-[[(5-[[(4-fluoro-2-heptylphenyl)amino]methyl]thiophen-2-yl)carbonyl]amino]-1,3-thiazol-4-yl)acetic acid
-
-
(2-[[(5-[[(4-fluoro-2-heptylphenyl)amino]methyl]thiophen-2-yl)carbonyl]amino]-1,3-thiazol-4-yl)acetic acid
-
-
(2E)-3-(4-methoxyphenyl)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]prop-2-enamide
-
-
(2E)-3-(4-methoxyphenyl)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]prop-2-enamide
-
-
(2R)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
(2R)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
(2R)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
-
-
(2R)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
-
-
(2S)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
(2S)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
(2S)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
-
-
(2S)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
-
-
(3-[5-[(3S)-3-(2-bromo-5-fluorophenoxy)pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl]-1,2,4-oxadiazol-5-yl)methanol
-
-
(3-[5-[(3S)-3-(2-bromo-5-fluorophenoxy)pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl]-1,2,4-oxadiazol-5-yl)methanol
-
-
(5-[6-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
-
-
(5-[6-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
-
-
(5-[6-[3-(2-bromophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
-
-
(5-[6-[3-(2-bromophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
-
-
(5R)-5-(hydroxymethyl)-3-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridin-3-yl)-1,3-oxazolidin-2-one
-
-
(5R)-5-(hydroxymethyl)-3-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridin-3-yl)-1,3-oxazolidin-2-one
-
-
(E)-N-(2-cyclopropylethyl)-N2-(pyridin-2-yl[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]methylidene)glycinamide
-
-
(E)-N-(2-cyclopropylethyl)-N2-(pyridin-2-yl[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]methylidene)glycinamide
-
-
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]amino)acetic acid
-
-
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]amino)acetic acid
-
-
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]oxy)acetic acid
-
-
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]oxy)acetic acid
-
-
1'-[6-(3-methyl-1,2,4-thiadiazol-5-yl)pyridazin-3-yl]-2,3-dihydrospiro[indene-1,4'-piperidine]
-
-
1'-[6-(3-methyl-1,2,4-thiadiazol-5-yl)pyridazin-3-yl]-2,3-dihydrospiro[indene-1,4'-piperidine]
-
-
1-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)pyrrolidin-2-one
-
-
1-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)pyrrolidin-2-one
-
-
1-hydroxy-3-[5-(6-[3-[2-(trifluoromethyl)benzyl]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]propan-2-one
-
-
1-hydroxy-3-[5-(6-[3-[2-(trifluoromethyl)benzyl]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]propan-2-one
-
-
1-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]urea
-
-
1-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]urea
-
-
1-[5-(1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(1,3,4-oxadiazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(1,3,4-oxadiazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(1,3-oxazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(1,3-oxazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
-
-
1-[5-(benzylcarbamoyl)-4-methyl-1,3-thiazol-2-yl]-N-(4-fluorobenzyl)-1H-1,2,3-triazole-4-carboxamide
-
-
1-[5-(benzylcarbamoyl)-4-methyl-1,3-thiazol-2-yl]-N-(4-fluorobenzyl)-1H-1,2,3-triazole-4-carboxamide
-
-
2,3-dihydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
2,3-dihydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((6-(trifluoromethyl)pyridin-3-yl)methyl)-thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((6-(trifluoromethyl)pyridin-3-yl)methyl)-thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(piperidin-3-ylmethyl)thiazole-5-carboxamide trifluoroacetic acid salt
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(piperidin-3-ylmethyl)thiazole-5-carboxamide trifluoroacetic acid salt
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
-
2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-imidazo[4,5-b]pyridine
-
-
2-(2-(5-(((2-butylphenyl)amino)methyl)thiophene-2-carboxamido)thiazol-4-yl)acetate
the thiazole-4-acetic acid analogue is a potent and liver-selective SCD1 inhibitor. It exhibits significant effects in rodent models of diabetes, hepatic steatosis, and obesity, with sufficient safety margins in a rat toxicology study with repeated dosing
2-(2-(5-(((2-butylphenyl)amino)methyl)thiophene-2-carboxamido)thiazol-4-yl)acetate
the thiazole-4-acetic acid analogue is a potent and liver-selective SCD1 inhibitor. It exhibits significant effects in rodent models of diabetes, hepatic steatosis, and obesity, with sufficient safety margins in a rat toxicology study with repeated dosing
2-(2-cyclopropylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1H-isoindole-1,3(2H)-dione
-
-
2-(2-cyclopropylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1H-isoindole-1,3(2H)-dione
-
-
2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
-
MF-152
2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
-
MF-152
2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
-
MF-152
2-(4-[[2-(trifluoromethyl)phenyl]sulfanyl]piperidin-1-yl)-1,3-thiazole-5-carboxamide
-
-
2-(4-[[2-(trifluoromethyl)phenyl]sulfanyl]piperidin-1-yl)-1,3-thiazole-5-carboxamide
-
-
2-(4-[[5-(hexylamino)-2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-N-pentylpyridine-4-carboxamide
-
-
2-(4-[[5-(hexylamino)-2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-N-pentylpyridine-4-carboxamide
-
-
2-(5-[1-[(2,5-dichlorophenyl)carbonyl]piperidin-4-ylidene]-2,4-dioxo-1,3-thiazolidin-3-yl)-N-pentylacetamide
-
-
2-(5-[1-[(2,5-dichlorophenyl)carbonyl]piperidin-4-ylidene]-2,4-dioxo-1,3-thiazolidin-3-yl)-N-pentylacetamide
-
-
2-([2-[4-(2-chloro-3,5-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylbenzamide
-
-
2-([2-[4-(2-chloro-3,5-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylbenzamide
-
-
2-acetyl-N-[1-(3,4-dichlorobenzyl)-1H-pyrazol-4-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
-
2-acetyl-N-[1-(3,4-dichlorobenzyl)-1H-pyrazol-4-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
-
2-hydroxy-N-[2-[2-oxo-3-(trifluoromethyl)-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
2-hydroxy-N-[2-[2-oxo-3-(trifluoromethyl)-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
2-hydroxy-N-[2-[3-(1-methylethyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
2-hydroxy-N-[2-[3-(1-methylethyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
CVT-12,012
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
CVT-12,012
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
2-hydroxy-N-[4-oxo-3-[3-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
-
-
2-hydroxy-N-[4-oxo-3-[3-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
-
-
2-hydroxy-N-[4-oxo-3-[4-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
-
-
2-hydroxy-N-[4-oxo-3-[4-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
-
-
2-[(2,5-dichlorophenoxy)methyl]-N-[4-(1H-pyrazol-1-ylmethyl)phenyl]pyridine-4-carboxamide
-
-
2-[(2,5-dichlorophenoxy)methyl]-N-[4-(1H-pyrazol-1-ylmethyl)phenyl]pyridine-4-carboxamide
-
-
2-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]benzamide
-
-
2-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]benzamide
-
-
2-[(3S)-3-[2-(trifluoromethyl)phenoxy]pyrrolidin-1-yl]-1,3-thiazole-5-carboxamide
-
-
2-[(3S)-3-[2-(trifluoromethyl)phenoxy]pyrrolidin-1-yl]-1,3-thiazole-5-carboxamide
-
-
2-[1-[2-(4-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]-4-methyl-N-(pyridin-3-ylmethyl)-1,3-thiazole-5-carboxamide
-
-
2-[1-[2-(4-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]-4-methyl-N-(pyridin-3-ylmethyl)-1,3-thiazole-5-carboxamide
-
-
2-[3-(4-fluorobenzyl)-2-oxo-2,3-dihydro-1H-imidazol-1-yl]-N-(pyridin-3-ylmethyl)-4-(trifluoromethyl)-1,3-thiazole-5-carboxamide
-
-
2-[3-(4-fluorobenzyl)-2-oxo-2,3-dihydro-1H-imidazol-1-yl]-N-(pyridin-3-ylmethyl)-4-(trifluoromethyl)-1,3-thiazole-5-carboxamide
-
-
2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
-
-
2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
-
-
2-[4-[2-(trifluoromethyl)benzyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-4-carboxamide
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-carboxamide
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-sulfonamide
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,4,5,9-tetrahydro-6H-purin-6-one
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,4,5,9-tetrahydro-6H-purin-6-one
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-b]pyridine
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-b]pyridine
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7-amine
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7-amine
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[5,4-c]pyridin-4(5H)-one
-
-
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[5,4-c]pyridin-4(5H)-one
-
-
3,4-bis(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3,4-bis(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-((1-methyl-1H-pyrazol-4-yl)methyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-((1-methyl-1H-pyrazol-4-yl)methyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(oxazol-4-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(oxazol-4-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-4-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-4-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-methyl-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-methyl-1H-pyrazole-5-carboxamide
-
3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2,3-dihydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2,3-dihydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxy-2-methylpropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxy-2-methylpropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-(5-[[3-(trifluoromethyl)phenyl]carbonyl]-1,3-thiazol-2-yl)benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-(5-[[3-(trifluoromethyl)phenyl]carbonyl]-1,3-thiazol-2-yl)benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
-
highly potent and orally bioavailable thiazole-based SCD-1 inhibitor
3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
-
highly potent and orally bioavailable thiazole-based SCD-1 inhibitor
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
potent and orally efficacious SCD-1 inhibitor
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
potent and orally efficacious SCD-1 inhibitor
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]thiophen-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]thiophen-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-{5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl}benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-{5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl}benzamide
-
-
3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-[(methylsulfonyl)amino]-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-[(methylsulfonyl)amino]-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
-
-
3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
-
-
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
-
-
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
-
-
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazine
-
-
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazine
-
-
3-(3-hydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(3-hydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
-
-
3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
-
-
3-(4-phenoxypiperidin-1-yl)-6-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]pyridazine
-
-
3-(4-phenoxypiperidin-1-yl)-6-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]pyridazine
-
-
3-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazino[3,4-b][1,5]benzoxazepin-5(6H)-one
-
-
3-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazino[3,4-b][1,5]benzoxazepin-5(6H)-one
-
-
3-(5-benzyl-1,3,4-oxadiazol-2-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
-
-
3-(5-benzyl-1,3,4-oxadiazol-2-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
-
-
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
-
-
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
-
-
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
-
-
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
-
-
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
-
MF-438
3-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
3-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
-
-
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-[([4-[2-(acetylamino)ethyl]-2-(4-methoxyphenyl)-3-oxo-3,4-dihydropyrido[2,3-b]pyrazin-6-yl]amino)methyl]benzoic acid
-
-
3-[([4-[2-(acetylamino)ethyl]-2-(4-methoxyphenyl)-3-oxo-3,4-dihydropyrido[2,3-b]pyrazin-6-yl]amino)methyl]benzoic acid
-
-
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]-N-methylpropanamide
-
-
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]-N-methylpropanamide
-
-
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
3-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]propanamide
-
-
3-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]propanamide
-
-
3-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]propanamide
-
-
3-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]propanamide
-
-
3-[2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-7-oxo-6,7-dihydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]propanoic acid
-
-
3-[2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-7-oxo-6,7-dihydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]propanoic acid
-
-
3-[3-(2-bromo-4-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-bromo-4-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-bromophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-bromophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-iodophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-(2-iodophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
3-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
3-[4-(2-benzylphenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
-
-
3-[4-(2-benzylphenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(1H-imidazol-1-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(1H-imidazol-1-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3,5-dimethyl-1H-pyrazol-1-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3,5-dimethyl-1H-pyrazol-1-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,2,4-oxadiazol-3-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,2,4-oxadiazol-3-yl)pyridazine
-
-
3-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,2-oxazole-5-carboxamide
-
-
3-[6-(4'-chlorobiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
3-[6-(4'-chlorobiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
3-[6-(4'-methylbiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
3-[6-(4'-methylbiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
3-[6-(4-methoxyphenyl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
3-[6-(4-methoxyphenyl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
3-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
3-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
3-[7-oxo-6-(4-pyridin-3-ylphenyl)-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
3-[7-oxo-6-(4-pyridin-3-ylphenyl)-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
-
-
4-(2-bromo-5-fluorophenoxy)-1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3,4-thiadiazol-2-yl]piperidine
-
-
4-(2-bromo-5-fluorophenoxy)-1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3,4-thiadiazol-2-yl]piperidine
-
-
4-(2-chloro-4-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-4-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-5-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-5-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-6-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-6-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-(3-(3-methylcarbamoyl)phenyl)piperidine-1-carboxamide
#1716, suppression of DENV1 replication without apparent cytotoxicity
-
4-(2-chlorophenoxy)-N-(3-(3-methylcarbamoyl)phenyl)piperidine-1-carboxamide
-
#1716, suppression of DENV2 replication without apparent cytotoxicity
-
4-(2-chlorophenoxy)-N-(3-(3-methylcarbamoyl)phenyl)piperidine-1-carboxamide
-
#1716, suppression of DENV3 replication without apparent cytotoxicity
-
4-(2-chlorophenoxy)-N-(3-(3-methylcarbamoyl)phenyl)piperidine-1-carboxamide
-
#1716, suppression of DENV4 replication without apparent cytotoxicity
-
4-(2-chlorophenoxy)-N-[3-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-[(1-methylethyl)carbamoyl]phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-[(1-methylethyl)carbamoyl]phenyl]piperidine-1-carboxamide
-
-
4-(2-hydroxyethoxy)-3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(2-hydroxyethoxy)-3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-ethoxy-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-ethoxy-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
-
-
4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
-
-
4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
4-methyl-2-[2-oxo-3-[4-(trifluoromethyl)benzyl]-2,3-dihydro-1H-imidazol-1-yl]-N-(pyridin-3-ylmethyl)-1,3-thiazole-5-carboxamide
-
-
4-methyl-2-[2-oxo-3-[4-(trifluoromethyl)benzyl]-2,3-dihydro-1H-imidazol-1-yl]-N-(pyridin-3-ylmethyl)-1,3-thiazole-5-carboxamide
-
-
4-[(2-butyl-phenylamino)-methyl]eN-(4-hydroxymethylthiazol-2-yl)-benzamide
-
4-[(2-butyl-phenylamino)-methyl]eN-(4-hydroxymethylthiazol-2-yl)-benzamide
-
4-[(2-butyl-phenylamino)-methyl]eN-[4-(2-hydroxyethyl)-thiazol-2-yl]-benzamide
-
4-[(2-butyl-phenylamino)-methyl]eN-[4-(2-hydroxyethyl)-thiazol-2-yl]-benzamide
-
4-[(2-chloro-phenylamino)-methyl]eN-(4-hydroxymethylthiazol-2-yl)-benzamide
-
4-[(2-chloro-phenylamino)-methyl]eN-(4-hydroxymethylthiazol-2-yl)-benzamide
-
4-[(2-chloro-phenylamino)-methyl]eN-[4-(2-hydroxyethyl)-thiazol-2-yl]-benzamide
-
4-[(2-chloro-phenylamino)-methyl]eN-[4-(2-hydroxyethyl)-thiazol-2-yl]-benzamide
-
4-[(7-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-5,6,7,7a-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl)methoxy]benzoic acid
-
-
4-[(7-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-5,6,7,7a-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl)methoxy]benzoic acid
-
-
4-[2-(dimethylamino)ethoxy]-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-[2-(dimethylamino)ethoxy]-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
5-(hydroxymethyl)-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
-
-
5-(hydroxymethyl)-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
-
-
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
-
-
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
-
-
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidine
-
-
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidine
-
-
5-[(2-hexyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
-
5-[(2-hexyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
-
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid (4-hydroxymethyl-thiazol-2-yl)-amide
-
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid (4-hydroxymethyl-thiazol-2-yl)-amide
-
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
-
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
-
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-1H-imidazo[4,5-b]pyrazine
-
-
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[4,5-b]pyrazin-2-amine
-
-
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[4,5-b]pyrazin-2-amine
-
-
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-oxadiazole-2-carboxamide
-
-
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazole-2-carboxamide
-
-
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazole-2-carboxamide
-
-
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-1,2,4-triazole-3-carboxamide
-
-
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-1,2,4-triazole-3-carboxamide
-
-
6'-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-2,3'-bipyridine-5-carboxylic acid
-
-
6'-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-2,3'-bipyridine-5-carboxylic acid
-
-
6-(3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
-
-
6-(3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
-
-
6-(3-bromobenzyl)-5,7-dimethyl-N-(tetrahydrofuran-2-ylmethyl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
-
-
6-(3-bromobenzyl)-5,7-dimethyl-N-(tetrahydrofuran-2-ylmethyl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
-
-
6-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)pyridine-3-carboxylic acid
-
-
6-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)pyridine-3-carboxylic acid
-
-
6-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
-
-
6-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
-
-
6-[(3,4-dichlorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
-
-
6-[(3,4-dichlorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
-
-
6-[(3-chloro-4-fluorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
-
-
6-[(3-chloro-4-fluorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
-
-
6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine-3-carbohydrazide
-
-
6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine-3-carboxamide
-
-
6-[4-[(2-bromo-5-methoxyphenyl)carbonyl]piperazin-1-yl]-N-(3-phenylpropyl)pyridine-3-carboxamide
-
-
6-[4-[(2-bromo-5-methoxyphenyl)carbonyl]piperazin-1-yl]-N-(3-phenylpropyl)pyridine-3-carboxamide
-
-
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
-
-
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
-
-
6-[5-chloro-2-(trifluoromethyl)benzyl]-N-hexyl-5,6,7,8-tetrahydro-1,6-naphthyridine-2-carboxamide
-
-
6-[5-chloro-2-(trifluoromethyl)benzyl]-N-hexyl-5,6,7,8-tetrahydro-1,6-naphthyridine-2-carboxamide
-
-
7-[(3-chlorobenzyl)amino]-1-(4-oxopentyl)-3-(3-pyridin-4-ylphenyl)pyrido[3,4-b]pyrazin-2(1H)-one
-
-
7-[(3-chlorobenzyl)amino]-1-(4-oxopentyl)-3-(3-pyridin-4-ylphenyl)pyrido[3,4-b]pyrazin-2(1H)-one
-
-
7-[(3-chlorobenzyl)amino]-3-(4-methoxyphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
-
-
7-[(3-chlorobenzyl)amino]-3-(4-methoxyphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
-
-
7-[(3-chlorobenzyl)amino]-3-(4-methylphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
-
-
7-[(3-chlorobenzyl)amino]-3-(4-methylphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
-
-
8-(trifluoromethyl)-2,5,21,24,25-pentaazatetracyclo[21.2.2.2-2,5.1-7,11]triaconta-1(25),7(28),8,10,23,26-hexaene-6,22-dione
-
-
8-(trifluoromethyl)-2,5,21,24,25-pentaazatetracyclo[21.2.2.2-2,5.1-7,11]triaconta-1(25),7(28),8,10,23,26-hexaene-6,22-dione
-
-
A939572
i.e. 4-(2-chlorophenoxy)-N-(3-(3-methylcarbamoyl)phenyl)piperidine-1-carboxamide
A939572
an SCD inhibitor, pharmacological inhibition of SCD1 by A939572 suppresses selfrenewal, migration, invasion and sorafenib resistance of hepatocellular carcinoma cells
benzyl [3-(2,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
-
-
benzyl [3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
-
-
benzyl [3-(3,4-dimethylbenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
-
-
benzyl [3-(3-chloro-4-fluorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
-
-
benzyl [3-(3-chloro-4-fluorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
-
-
benzyl [3-[(3,4-dichlorobenzyl)carbamoyl]-4-(pyridin-3-yloxy)phenyl]carbamate
-
-
benzyl [3-[(3,4-dichlorobenzyl)carbamoyl]-4-(pyridin-3-yloxy)phenyl]carbamate
-
-
Cu2+
-
and its complexes of tyrosine, histidine and lysine, act as superoxide scavengers, inhibition at low concentrations
cytochrome c
-
very low inhibitor concentrations of 10 mM lead to an almost complete inhibition of the SCD benzamidoxime reductase activity of porcine adipose tissue microsome
decanoyl-CoA
-
competitive inhibition of enzyme activity greater than 95% at 0.002 mM
dodecanoyl-CoA
-
competitive inhibition of enzyme activity greater than 90% at 0.002 mM
ethyl [5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-oxadiazol-2-yl]acetate
-
-
ethyl [5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-oxadiazol-2-yl]acetate
-
-
GSK-993
-
potent and orally available SCD1 inhibitor, almost complete inhibition at 0.01 mM
methyl (2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)carbamate
-
-
methyl (2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)carbamate
-
-
methyl [5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-thiadiazol-2-yl]acetate
-
-
methyl [5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-thiadiazol-2-yl]acetate
-
-
MK8245
EC50 value is 34 nm with serotype DENV1, MK8245 suppresses DENV1 replication in human lung carcinoma cells (A549) and baby hamster kidney cells (BHK-21), suppression of DENV1 replication without apparent cytotoxicity
-
MK8245
-
EC50 value is 58 nm with serotype DENV2, MK8245 suppresses DENV2 replication in human lung carcinoma cells (A549) and baby hamster kidney cells (BHK-21), suppression of DENV2 replication without apparent cytotoxicity
-
MK8245
-
EC50 value is 59 nm with serotype DENV3, MK8245 suppresses DENV3 replication in human lung carcinoma cells (A549) and baby hamster kidney cells (BHK-21), suppression of DENV3 replication without apparent cytotoxicity
-
MK8245
-
EC50 value is 81 nm with serotype DENV4, MK8245 suppresses DENV4 replication in human lung carcinoma cells (A549) and baby hamster kidney cells (BHK-21), suppression of DENV4 replication without apparent cytotoxicity
-
N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
-
N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
-
N-(2-amino-2-oxoethyl)-6-(2,3-dichlorobenzyl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
-
-
N-(2-amino-2-oxoethyl)-6-(2,3-dichlorobenzyl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
-
-
N-(2-cyclopropylethyl)-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
-
-
N-(2-cyclopropylethyl)-3-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1H-pyrazole-5-carboxamide
-
-
N-(2-cyclopropylethyl)-3-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1H-pyrazole-5-carboxamide
-
-
N-(2-cyclopropylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3,4-thiadiazole-2-carboxamide
-
-
N-(2-cyclopropylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3,4-thiadiazole-2-carboxamide
-
-
N-(2-cyclopropylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-6-(4-[[5-fluoro-2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-6-(4-[[5-fluoro-2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-6-[(1-[[2-(trifluoromethyl)phenyl]carbonyl]azetidin-3-yl)amino]pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-6-[(1-[[2-(trifluoromethyl)phenyl]carbonyl]azetidin-3-yl)amino]pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-6-[4-[3-(trifluoromethyl)pyridin-2-yl]piperazin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-cyclopropylethyl)-6-[4-[3-(trifluoromethyl)pyridin-2-yl]piperazin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-(phenylcarbonyl)piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-(phenylcarbonyl)piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-phenylethyl)-4-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)benzamide
-
-
N-(2-phenylethyl)-4-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)benzamide
-
-
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
-
-
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
-
-
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
-
-
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
-
-
N-(2-[2-[(3,4-dichlorobenzyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3,4-dichlorobenzyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)benzamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)benzamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)methanesulfonamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)methanesulfonamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)propanamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)propanamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)thiophene-3-carboxamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)thiophene-3-carboxamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3-chloro-4-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3-chloro-4-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3-chlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(3-chlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(4-chloro-3-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[2-[(4-chloro-3-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(2-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(2-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2,2-dimethyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2,2-dimethyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-methyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-methyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
-
-
N-(2-[6-[(3,4-dichlorobenzyl)amino]-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
-
-
N-(2-[6-[(3-chloro-4-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3-chloro-4-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3-methoxybenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(3-methoxybenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(4-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[6-[(4-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxopyrido[3,4-b]pyrazin-1(2H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxopyrido[3,4-b]pyrazin-1(2H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(3,4-dimethylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(3,4-dimethylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(4-fluoro-3-methylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
-
-
N-(2-[7-[(4-fluoro-3-methylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
-
-
N-(3-methylbutyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(3-methylbutyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(3-methylbutyl)-6-oxo-8-[[2-(trifluoromethyl)phenyl]carbonyl]-6,6a,7,8,9,10-hexahydro-5H-pyrazino[1',2':1,6]pyrazino[2,3-c]pyridazine-3-carboxamide
-
-
N-(3-methylbutyl)-6-oxo-8-[[2-(trifluoromethyl)phenyl]carbonyl]-6,6a,7,8,9,10-hexahydro-5H-pyrazino[1',2':1,6]pyrazino[2,3-c]pyridazine-3-carboxamide
-
-
N-(3-methylbutyl)-6-[[2-(trifluoromethyl)phenyl]carbonyl]-4,5,6,7-tetrahydrofuro[2,3-c]pyridine-2-carboxamide
-
-
N-(3-methylbutyl)-6-[[2-(trifluoromethyl)phenyl]carbonyl]-4,5,6,7-tetrahydrofuro[2,3-c]pyridine-2-carboxamide
-
-
N-(4-hydroxymethyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
-
N-(4-hydroxymethyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
-
N-(cyclopentylmethyl)-6-[5-[[2-(trifluoromethyl)phenyl]carbonyl]-3,4,5,6-tetrahydropyrrolo[3,4-c]pyrrol-2(1H)-yl]pyridine-3-carboxamide
-
-
N-(cyclopentylmethyl)-6-[5-[[2-(trifluoromethyl)phenyl]carbonyl]-3,4,5,6-tetrahydropyrrolo[3,4-c]pyrrol-2(1H)-yl]pyridine-3-carboxamide
-
-
N-benzyl-2-(5-hydroxy-1-oxoisoquinolin-2(1H)-yl)-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-benzyl-2-(5-hydroxy-1-oxoisoquinolin-2(1H)-yl)-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-benzyl-2-[3-(4-fluorobenzyl)-2-oxopyrrolidin-1-yl]-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-benzyl-2-[3-(4-fluorobenzyl)-2-oxopyrrolidin-1-yl]-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-benzyl-2-[3-(4-fluorophenoxy)-2-oxopiperidin-1-yl]-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-benzyl-2-[3-(4-fluorophenoxy)-2-oxopiperidin-1-yl]-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-benzyl-4-(morpholin-4-ylmethyl)-2-[(3-phenylpropanoyl)amino]-1,3-thiazole-5-carboxamide
-
-
N-benzyl-4-(morpholin-4-ylmethyl)-2-[(3-phenylpropanoyl)amino]-1,3-thiazole-5-carboxamide
-
-
N-benzyl-4-methyl-2-(1-[2-[methyl(phenyl)amino]ethyl]-1H-pyrazol-3-yl)-1,3-thiazole-5-carboxamide
-
-
N-benzyl-4-methyl-2-(1-[2-[methyl(phenyl)amino]ethyl]-1H-pyrazol-3-yl)-1,3-thiazole-5-carboxamide
-
-
N-benzyl-4-methyl-2-[6-(2-phenylethyl)pyrazin-2-yl]-1,3-thiazole-5-carboxamide
-
-
N-benzyl-4-methyl-2-[6-(2-phenylethyl)pyrazin-2-yl]-1,3-thiazole-5-carboxamide
-
-
N-methoxy-3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
N-methoxy-3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
-
-
N-methyl-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-imidazo[4,5-c]pyridin-4-amine
-
-
N-methyl-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-imidazo[4,5-c]pyridin-4-amine
-
-
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-[(6-chloropyridin-3-yl)methyl]-2-[4-[(4-fluorobenzyl)oxy]-2-oxopyridin-1(2H)-yl]-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-[(6-chloropyridin-3-yl)methyl]-2-[4-[(4-fluorobenzyl)oxy]-2-oxopyridin-1(2H)-yl]-4-methyl-1,3-thiazole-5-carboxamide
-
-
N-[1-[5-chloro-2-(cyclopropylmethoxy)benzyl]-5-methyl-1H-pyrazol-3-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
-
N-[1-[5-chloro-2-(cyclopropylmethoxy)benzyl]-5-methyl-1H-pyrazol-3-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
-
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(4-[[2-fluoro-5-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-2-oxoethyl]-5-(2-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
N-[2-(4-[[2-fluoro-5-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-2-oxoethyl]-5-(2-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
N-[2-(4-[[2-fluoro-5-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-2-oxoethyl]biphenyl-4-carboxamide
-
-
N-[2-(4-[[2-fluoro-5-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-2-oxoethyl]biphenyl-4-carboxamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[6-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[6-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(2,2,2-trifluoroethoxy)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(2,2,2-trifluoroethoxy)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[4-(2,2,2-trifluoroethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[4-(2,2,2-trifluoroethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-6-[(3-methylbenzyl)amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-6-[(3-methylbenzyl)amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-6-[[(5-methylisoxazol-3-yl)methyl]amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-(4-methoxyphenyl)-6-[[(5-methylisoxazol-3-yl)methyl]amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[2-oxo-3-pyridin-3-yl-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[2-oxo-3-pyridin-3-yl-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[2-[3-(4-ethylphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-(4-ethylphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-(4-methoxyphenyl)-7-[(3-methylbenzyl)amino]-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-(4-methoxyphenyl)-7-[(3-methylbenzyl)amino]-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[3-tert-butyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]-2-hydroxyacetamide
-
-
N-[2-[3-tert-butyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]-2-hydroxyacetamide
-
-
N-[2-[6-(benzylamino)-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[6-(benzylamino)-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[6-[[2-fluoro-5-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[6-[[2-fluoro-5-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[6-[[3,5-bis(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[6-[[3,5-bis(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[6-[[4-fluoro-3-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[6-[[4-fluoro-3-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
-
-
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
-
-
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
-
-
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
CVT-11,563
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
CVT-11,563
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-phenoxyacetamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-phenoxyacetamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-3-hydroxypropanamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-3-hydroxypropanamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
-
-
N-[3-(3-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
-
-
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-phenoxyacetamide
-
-
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
-
-
N-[3-(biphenyl-3-ylmethyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(biphenyl-3-ylmethyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
-
N-[3-(tert-butylcarbamoyl)phenyl]-4-(2-chlorophenoxy)piperidine-1-carboxamide
-
-
N-[3-(tert-butylcarbamoyl)phenyl]-4-(2-chlorophenoxy)piperidine-1-carboxamide
-
-
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
-
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
-
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
-
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
-
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[[2-(3-methylbutyl)-phenylamino]-methyl]-benzamide
-
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[[2-(3-methylbutyl)-phenylamino]-methyl]-benzamide
-
N-[4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
-
N-[4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
-
N-[5-(2,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(2,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,4-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,4-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,4-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,4-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,5-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,5-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-chloro-4-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-chloro-4-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-chlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-chlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-fluoro-4-methylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-fluoro-4-methylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-tert-butylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-tert-butylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-methyl-1-[3-(trifluoromethyl)benzyl]-1H-pyrazol-3-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
-
N-[5-methyl-1-[3-(trifluoromethyl)benzyl]-1H-pyrazol-3-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
-
N-[5-[(2-chlorophenoxy)methyl]-1,3,4-thiadiazol-2-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
complete inhibition at 0.1 mM
N-[5-[(2-chlorophenoxy)methyl]-1,3,4-thiadiazol-2-yl]-1,2,3,4-tetrahydroisoquinoline-6-carboxamide
-
-
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
p-chloromercuribenzoate
-
prevention by stearoyl-CoA; reversed by beta-mercaptoethanol
p-hydroxymercuribenzoate
-
potent inhibitor of the SCD benzamidoxime reductase activity of porcine adipose tissue microsomes
potassium cyanide
-
supplementation of potassium cyanide leads to a 65% inhibition of the microsomal benzamidoxime reductase activity of SCD in porcine adipose tissue
stearoyl-CoA
-
inhibits SCD activity in concentrations greater than 0.05 mM
Sterculic acid
-
inhibits the enzyme activity in a dose dependent manner with a calculated EC50 of 247 nM
Thenoyltrifluoroacetone
-
59% inhibition at 6 mM; i.e. 4,4,4-trifluoro-1-(2-thienyl)-1,3-butanedione
Thenoyltrifluoroacetone
-
i.e. 4,4,4-trifluoro-1-(2-thienyl)-1,3-butanedione
trans-10,cis-12 conjugated linoleic acid
-
inhibits stearate desaturation only, not that of palmitate
[(5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-5,7a-dihydro[1,3]thiazolo[4,5-d]pyrimidin-7-yl)oxy]acetic acid
-
-
[(5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-5,7a-dihydro[1,3]thiazolo[4,5-d]pyrimidin-7-yl)oxy]acetic acid
-
-
[2-((5-[(2-benzyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
-
[2-((5-[(2-benzyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
-
-
[2-((5-[(2-benzyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
-
[2-((5-[(2-hexyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetate
-
[2-((5-[(2-hexyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetate
-
[2-((5-[(2-octyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetate
-
[2-((5-[(2-octyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetate
-
[2-((5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
-
[2-((5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
-
[2-(4-([2-(3-methyl-butyl)-phenylamino]-methyl)-benzoylamino)-thiazol-4-yl]-acetic acid
-
[2-(4-([2-(3-methyl-butyl)-phenylamino]-methyl)-benzoylamino)-thiazol-4-yl]-acetic acid
-
[2-([[4-([[2-(2-cyclopentylethyl)phenyl]amino]methyl)phenyl]carbonyl]amino)-1,3-thiazol-4-yl]acetic acid
-
99% inhibition at 0.01 mM
[2-([[4-([[2-(2-cyclopentylethyl)phenyl]amino]methyl)phenyl]carbonyl]amino)-1,3-thiazol-4-yl]acetic acid
-
-
[2-([[4-([[2-(trifluoromethyl)phenyl]amino]methyl)piperidin-1-yl]carbonyl]amino)-1,3-thiazol-4-yl]acetic acid
-
complete inhibition at 0.01 mM
[2-([[4-([[2-(trifluoromethyl)phenyl]amino]methyl)piperidin-1-yl]carbonyl]amino)-1,3-thiazol-4-yl]acetic acid
-
-
[2-methoxy-4-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
-
-
[2-methoxy-4-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
-
-
[2-methoxy-5-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
-
-
[2-methoxy-5-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
-
-
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
-
-
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
EC50 value is 62 nM. SCD-1 inhibition with the inhibitor increases susceptibility of hepatitis C virus RNA to exogenously added nucleases in digitonin permeabilized cells. Low dose treatment with the inhibitor decreases the number of membranous webs and alters their structure while having no effect on lipid droplets in Huh7-SGR cells
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
-
-
[3-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)-1H-1,2,4-triazol-1-yl]acetic acid
-
-
[3-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)-1H-1,2,4-triazol-1-yl]acetic acid
-
-
[5-(2-[3-[2-bromo-5-(trifluoromethyl)phenoxy]propoxy]-1,3-thiazol-5-yl)-2H-tetrazol-2-yl]acetic acid
-
-
[5-(2-[3-[2-bromo-5-(trifluoromethyl)phenoxy]propoxy]-1,3-thiazol-5-yl)-2H-tetrazol-2-yl]acetic acid
-
-
[5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-oxadiazol-2-yl]methanol
-
-
[5-(4-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]phenyl)-1,3,4-oxadiazol-2-yl]methanol
-
-
[5-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)-1H-tetrazol-1-yl]acetic acid
-
-
[5-(5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazol-2-yl)-1H-tetrazol-1-yl]acetic acid
-
-
[5-(6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
-
-
[5-(6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
-
-
[5-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
-
-
[5-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
-
-
[5-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazin-3-yl)-1,3,4-thiadiazol-2-yl]acetic acid
-
-
[5-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazin-3-yl)-1,3,4-thiadiazol-2-yl]acetic acid
-
-
[5-[2-([(2S)-3-[2-bromo-5-(trifluoromethoxy)phenoxy]-2-methylpropyl]oxy)-1,3-thiazol-5-yl]-2H-tetrazol-2-yl]acetic acid
-
-
[5-[2-([(2S)-3-[2-bromo-5-(trifluoromethoxy)phenoxy]-2-methylpropyl]oxy)-1,3-thiazol-5-yl]-2H-tetrazol-2-yl]acetic acid
-
-
[[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]amino](oxo)acetic acid
-
-
[[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]amino](oxo)acetic acid
-
-
additional information
-
administering CoEDTA, ytterbium acetate and chromium-mordanted straw decrease in milk cis-9 10:1/10:0, cis-9 12:1/12:0, cis-9 14:1/14:0, cis-9 16:1/16:0, cis-9 17:1/17:0, cis-9 18:1/18:0 and cis-9,trans-11 conjugated linoleic acid/trans-11 18:1 concentration rations of 44.6,52.7, 58.7, 36.8, 37.2, 44.3 and 43.0%, cows are fed with incremental levels of fish oil
-
additional information
-
Co2+ has a reducing effect on the DELTA9-desaturase indices [(product of DELTA9-desaturase)/(product of DELTA9-desaturase + substrate of DELTA9-desaturase)] of milk for myristoleic acid, palmitoleic acid, oleic acid, and rumenic acid, there are no differences in DELTA9-desaturase indices between Co2+-EDTA and Co2+-acetate
-
additional information
SCD1 inhibitors inhibit replication of all DENV serotypes and other flaviviruses
-
additional information
-
SCD1 inhibitors inhibit replication of all DENV serotypes and other flaviviruses
-
additional information
-
SCD1 inhibitors inhibit replication of all DENV serotypes and other flaviviruses
-
additional information
-
SCD1 inhibitors inhibit replication of all DENV serotypes and other flaviviruses
-
additional information
-
N-ethylmaleimide and iodoacetamide have no inhibitory effect
-
additional information
-
design and synthesis of 1-(4-phenoxypiperidin-1-yl)-2-arylaminoethanone-based inhibitors, overview
-
additional information
-
design and synthesis of piperidine-aryl urea-based stearoyl-CoA desaturase1 inhibitors, overview
-
additional information
synthesis and structure-activity relationships of a series of triazolone derivatives as enzyme inhibitors, overview
-
additional information
no inhibition of the enzyme by N-[4-methoxyphenyl]retinamide and by non-retinoid RBP4 ligand A1120, RBP4 is a serum retinol-binding protein. The presence of fenretinide or 4-oxo-N-(4-hydroxyphenyl)retinamide leads to 2.7 and 3fold increases in ratio for C16 and C18 ceramides ratio respectively
-
additional information
no inhibition by NS3 protease inhibitor B. Palmitoleic acid or oleic acid treatment rescues SCD inhibitors' antiviral effect
-
additional information
combined treatment with SCD1 inhibitors and RSL3 results in a synergistic cytotoxic effect on FT-t cells as calculated by the Chou-Talalay method. The decrease in viability in cells treated with the combination of RSL3 and SCD1 inhibitors is characterized by an increased oxidation of membrane lipids consistent with an increase in ferroptotic cell death. Further, blockade of SCD using siRNA or shRNA similarly sensitizes cells to RSL3, ruling out nonspecific effects of SCD1 inhibitors on ferroptosis sensitization
-
additional information
screening for compounds that selectively inhibit SCD1 in the liver in an ex vivo assay, identification and synthesis of 4-aminopyridine-based SCD1 inhibitors
-
additional information
-
drug design, de novo compound library design, screening using a QSAR model, and analysis of several unique molecules, of which the lead compound SSI-4 demonstrates potent anti-tumor activity, with an excellent pharmacokinetic and toxicology profile. Composite Z-score for modeling of all de novo ligands designed using docking, shape, and QSAR for ligand-guided predictions of high affinity drug-like compounds. The experimental SCD1 inhibitors induce tumor endoplasmic reticulum stress
-
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
-
design and synthesis of piperidine-aryl urea-based stearoyl-CoA desaturase1 inhibitors, overview
-
additional information
synthesis and structure-activity relationships of a series of triazolone derivatives as enzyme inhibitors, overview
-
additional information
screening for compounds that selectively inhibit SCD1 in the liver in an ex vivo assay, identification and synthesis of 4-aminopyridine-based SCD1 inhibitors. Analysis of anti-diabetic and anti-obesity effects of the inhibitors in mice fed a high fat diet (HFD), percentage inhibition in eyelid and liver, overview
-
additional information
product inhibition occurs with the purified recombinant enzyme because of limited capacity of a detergent micelle around SCD1
-
additional information
-
phenylalanine, indolepyruvic acid and 2-amino-1-phenylethanol show no inhibitory effect
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-Cresol
-
as well as other phenols, interact with desaturase system causing a stimulation of oxidation of reduced cytochrome b5
stearoyl-CoA-binding protein
-
stimulates activity in the crude microsomal fraction
-
bovine serum albumin
-
stimulates activity in the microsomal fraction
-
cytochrome b5 reductase
-
NADH-specific, required, EC 1.6.2.2
-
protein
-
basic cytoplasmic protein from rat liver stimulates activity in crude extract, no activity of partially purified enzyme
additional information
-
desaturase expression is sensitive to hormonal manipulation
-
additional information
-
high carbohydrate diet over weeks increses the stearoyl-CoA desaturase level specifically in contrast to the other lipogenic enzyme which are not upregulated, overview
-
additional information
-
SCD-1 activity is increased in the non-alcoholic human fatty liver, hepatic SCD-1 activity index is positively related to the concebtrations of diacylglycerols
-
additional information
-
the enzyme expression is increased by feeding of cholesterol and sterculic oil in parallel, enzyme expression levels and metabolic effects, overview
-
additional information
-
SCD2 mRNA expression is elevated 44fold in adipose tissue upon feeding mice a high fat diet, whereas SCD1 shows little response
-
additional information
treatment of rats with 2-(4-chlorophenoxy)-2-methylpropionic acid, i.e. clofibric acid, or feeding of a fat-free diet markedly elevated hepatic activity of SCD by increasing the steady-state level of SCD1 mRNA and enhancing transcriptional rate, metabolic effects, overview
-
additional information
treatment of rats with 2-(4-chlorophenoxy)-2-methylpropionic acid, i.e. clofibric acid, or feeding of a fat-free diet markedly elevated hepatic activity of SCD by increasing the steady-state level of SCD1 mRNA and enhancing transcriptional rate, metabolic effects, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0105
stearoyl-CoA
-
in 150 mM KCl, 40 mM NaF, 100 mM sodium phosphate buffer, pH 7.4, at 37°C
0.0566
stearoyl-CoA
in 0.1 M potassium phosphate buffer pH 7.2, at 37°C
additional information
additional information
-
substrates with 14-19 carbon fatty acyl chains show similar Km values of 0.0045-0.005 mM
-
additional information
additional information
stopped-flow and Michaelis-Menten kinetics, recombinant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.35
stearoyl-CoA
-
fatty acyl-CoA substrates with chain length of 14-19 carbon atoms show similar turnover number of about 22
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
(1-[6-[3-(3-hydroxybenzyl)-1,2,4-oxadiazol-5-yl]pyridazin-3-yl]piperidin-4-yl)[2-(trifluoromethyl)phenyl]methanone
Homo sapiens
-
IC50 below 0.0001 mM
0.000011
(1-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-imidazol-4-yl)methanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000017
(1-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-4-yl)methanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000055
(2-(4-[(2-benzyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000055
(2-(4-[(2-butyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000013
(2-(4-[(2-chloro-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000003
(2-(4-[(2-hexyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000045
(2-(4-[(2-octyl-phenylamino)-methyl]-benzoylamino)-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000058
(2-[(4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino)-thiazol-5-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000067
(2-[(5-([2-(3-methyl-butyl)-phenylamino]-methyl)-thiophene-2-carbonyl)-amino]-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000087
(2-[4-(biphenyl-2-ylaminomethyl)-benzoylamino]-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000051
(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-acetic acid
0.000002 - 0.000003
(2E)-3-(4-methoxyphenyl)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]prop-2-enamide
0.008
(2R)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
Rattus norvegicus
-
-
0.03
(2R)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
0.000038
(2S)-2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
Rattus norvegicus
-
-
0.03
(2S)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
0.000022
(4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]phenyl)methanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000034 - 0.0000056
(5-[6-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
0.0000049 - 0.00005
(5-[6-[3-(2-bromophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
0.000009
(5-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]pyridin-2-yl)methanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00014
(5R)-5-(hydroxymethyl)-3-(6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridin-3-yl)-1,3-oxazolidin-2-one
Rattus norvegicus
-
-
0.000004 - 0.000168
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]amino)acetic acid
0.000007 - 0.000053
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]oxy)acetic acid
0.003
1-(1,3-thiazol-2-yl)-4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazine
Rattus norvegicus
-
-
0.000012
1-(1-[6-[1-(2-ethoxyethyl)-1H-pyrazol-4-yl]pyridazin-3-yl]piperidin-4-yl)-6-fluoro-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000008
1-(1-[6-[4-(ethoxymethyl)-1H-pyrazol-1-yl]pyridazin-3-yl]piperidin-4-yl)-6-fluoro-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000164 - 0.000174
1-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)pyrrolidin-2-one
0.00015
1-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)urea
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000017
1-[1-[6-(1-ethyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-6-fluoro-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000422
1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000394
1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000173
1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-6-(trifluoromethyl)-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000268 - 0.001
1-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]urea
0.000004 - 0.000016
1-[5-(1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
0.000034 - 0.000065
1-[5-(1,3,4-oxadiazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
0.000014 - 0.000055
1-[5-(1,3-oxazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
0.000015 - 0.000039
1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
0.00075
1-[5-(5-methyl-1,3,4-thiadiazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000068 - 0.0011
2,3-dihydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
0.0036
2-((4-((5-methylthiazol-2-yl)carbamoyl)benzyl)amino)benzoic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000055 - 0.000306
2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.00003 - 0.000066
2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
0.000009 - 0.000015
2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.000019 - 0.000125
2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.000027 - 0.000504
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
0.000019 - 0.000477
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
0.000024 - 0.000032
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
0.000009 - 0.00028
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
0.000015 - 0.000194
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
0.001722
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((6-(trifluoromethyl)pyridin-3-yl)methyl)-thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000022 - 0.000214
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
0.000012 - 0.000039
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
0.01
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(piperidin-3-ylmethyl)thiazole-5-carboxamide trifluoroacetic acid salt
Mus musculus
pH and temperature not specified in the publication
0.000022 - 0.000067
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
0.00002 - 0.000268
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.000009 - 0.000012
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
0.000065 - 0.000945
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
0.000098 - 0.00014
2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.00002
2-(1-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-4-yl)ethanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.002488
2-(2'-fluorobiphenyl-4-yl)-1-methyl-5-(methylsulfonyl)-2,3-dihydro-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000697
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfanyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000113 - 0.000156
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-imidazo[4,5-b]pyridine
0.000528
2-(2'-fluorobiphenyl-4-yl)-N,N-dimethyl-1H-benzimidazole-6-sulfonamide
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.003863
2-(2'-methylbiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0000088
2-(2-(5-(((2-butylphenyl)amino)methyl)thiophene-2-carboxamido)thiazol-4-yl)acetate
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000095
2-(3'-chloro-2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000319
2-(3'-methylbiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000025
2-(4'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00651
2-(4-phenoxyphenyl)-N-(1,3-thiazol-2-ylmethyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0283
2-(4-phenoxyphenyl)-N-(2-phenylethyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000081
2-(4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino)-thiazole-5-carboxylic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000015
2-(4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-1-yl)-N-methylacetamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000022
2-(4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-1H-pyrazol-1-yl)ethanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0001
2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
-
0.007
2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxylic acid
Rattus norvegicus
-
-
0.000004 - 0.000024
2-(4-[[2-(trifluoromethyl)phenyl]sulfanyl]piperidin-1-yl)-1,3-thiazole-5-carboxamide
0.000278
2-(5'-chloro-2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0032
2-(thiophen-2-yl)-N-(2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1H-benzimidazol-5-yl)acetamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00025
2-([2-[4-(2-chloro-3,5-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylbenzamide
Rattus norvegicus
-
-
0.00058
2-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-phenylbenzamide
Homo sapiens
-
-
0.0000027 - 0.000015
2-hydroxy-N-[2-[2-oxo-3-(trifluoromethyl)-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
0.0000019
2-hydroxy-N-[2-[3-(1-methylethyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.0000061 - 0.000162
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
0.00136
2-hydroxy-N-[4-oxo-3-[3-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
0.00342
2-hydroxy-N-[4-oxo-3-[4-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
0.0002
2-[(2,5-dichlorophenoxy)methyl]-N-[4-(1H-pyrazol-1-ylmethyl)phenyl]pyridine-4-carboxamide
Homo sapiens
-
-
0.000037
2-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]benzamide
Homo sapiens
-
-
0.000012 - 0.000084
2-[(3S)-3-[2-(trifluoromethyl)phenoxy]pyrrolidin-1-yl]-1,3-thiazole-5-carboxamide
0.000115 - 0.000212
2-[4-(2-chlorophenoxy)phenyl]-N-(1,3-thiazol-2-ylmethyl)-1H-benzimidazole-5-carboxamide
0.000966
2-[4-(2-chlorophenoxy)phenyl]-N-(2-cyclopropylethyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00272
2-[4-(2-chlorophenoxy)phenyl]-N-(3-methylbutyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000832
2-[4-(2-chlorophenoxy)phenyl]-N-[(5-chlorothiophen-2-yl)methyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.01
2-[4-(o-tolylamino-methyl)-benzoylamino]-thiazole-4-carboxylic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000106 - 0.000254
2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
0.000076 - 0.000153
2-[4-[2-(trifluoromethyl)benzyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
0.000676 - 0.006523
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-4-carboxamide
0.000003 - 0.00001
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-carboxamide
0.000041 - 0.001019
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-sulfonamide
0.000097 - 0.000378
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,4,5,9-tetrahydro-6H-purin-6-one
0.000083 - 0.000755
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-b]pyridine
0.000007 - 0.000029
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
0.000056
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7-amine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000085 - 0.000268
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[5,4-c]pyridin-4(5H)-one
0.000227
2-[5-(2-fluorophenyl)pyridin-2-yl]-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000019 - 0.000058
2-[6-(2-fluorophenyl)pyridin-3-yl]-6-(methylsulfonyl)-1H-benzimidazole
0.000016 - 0.000022
3,4-bis(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.000076 - 0.000145
3,4-dimethoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.008218
3,4-dimethyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000147
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-((1-methyl-1H-pyrazol-4-yl)methyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000165
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(oxazol-4-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000023 - 0.00072
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
0.000007 - 0.000103
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
0.002673
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-4-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000385
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-methyl-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.002162 - 0.00217
3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.009999
3-(2,3-dihydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00057
3-(2-(4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino)-thiazol-5-yl)-propionic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.009999
3-(2-hydroxy-2-methylpropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000006 - 0.000003
3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.001
3-(2-hydroxyethoxy)-4-methoxy-N-(5-[[3-(trifluoromethyl)phenyl]carbonyl]-1,3-thiazol-2-yl)benzamide
Mus musculus
-
IC50 above 0.001 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000828 - 0.000836
3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.000002 - 0.000003
3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
0.000003 - 0.000059
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
0.000008 - 0.00001
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
0.000002 - 0.000015
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.000076 - 0.000145
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]thiophen-2-yl]benzamide
0.001
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
0.000006 - 0.000012
3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.009999
3-(2-hydroxyethoxy)-4-[(methylsulfonyl)amino]-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000276 - 0.000884
3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
0.0000063
3-(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-propionic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000026 - 0.000201
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
0.0000074 - 0.000397
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazine
0.009999
3-(3-hydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000085 - 0.00171
3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
0.00133
3-(4-phenoxypiperidin-1-yl)-6-(5-propyl-1,2,4-oxadiazol-3-yl)pyridazine
Mus musculus
-
pH 7.5
0.00082 - 0.00705
3-(4-phenoxypiperidin-1-yl)-6-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]pyridazine
0.000035 - 0.00004
3-(5-benzyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
0.000012 - 0.000041
3-(5-benzyl-1,3,4-oxadiazol-2-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
0.000009 - 0.000027
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
0.001992
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[3-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.0000023 - 0.000021
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
0.0013
3-(5-[hydroxy[2-(trifluoromethyl)phenyl]methyl]-1H-benzimidazol-2-yl)-N-(1,3-thiazol-2-ylmethyl)benzamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00047
3-([2-[4-(2,3-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
Homo sapiens
-
-
0.000038
3-([2-[4-(2,5-dichlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
Homo sapiens
-
-
0.000058
3-([2-[4-(2-bromophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
Homo sapiens
-
-
0.000035
3-([2-[4-(2-chloro-3,5-difluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
Homo sapiens
-
-
0.000051
3-([2-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
Homo sapiens
-
-
0.0001
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(2-hydroxyethyl)pyrazine-2-carboxamide
Homo sapiens
-
-
0.00011
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(pyridin-2-ylmethyl)pyrazine-2-carboxamide
Homo sapiens
-
-
0.000099
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(pyridin-3-ylmethyl)pyrazine-2-carboxamide
Homo sapiens
-
-
0.00011
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-(pyridin-4-ylmethyl)pyrazine-2-carboxamide
Homo sapiens
-
-
0.000039
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-ethylpyrazine-2-carboxamide
Homo sapiens
-
-
0.000051
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-methylpyrazine-2-carboxamide
Homo sapiens
-
-
0.00055
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)-N-phenylpyrazine-2-carboxamide
Homo sapiens
-
-
0.00021
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carbaldehyde
Homo sapiens
-
-
0.00034
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carbonitrile
Homo sapiens
-
-
0.000094
3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxamide
Homo sapiens
-
-
0.00003
3-chloro-N-[2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]pyrazin-2-amine
Homo sapiens
-
-
0.0039
3-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
Rattus norvegicus
-
-
0.000528 - 0.001402
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.00078
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-(2-phenylethyl)pyridine-2-carboxamide
Homo sapiens
-
-
0.00043
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-(pyridin-3-ylmethyl)pyridine-2-carboxamide
Homo sapiens
-
-
0.00035
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-(pyridin-4-ylmethyl)pyridine-2-carboxamide
Homo sapiens
-
-
0.01
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-pentylpyridine-2-carboxamide
Homo sapiens
-
above
0.00039
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]-N-propylpyridine-2-carboxamide
Homo sapiens
-
-
0.00009
3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
Homo sapiens
-
-
0.03
3-[([4-[2-(acetylamino)ethyl]-2-(4-methoxyphenyl)-3-oxo-3,4-dihydropyrido[2,3-b]pyrazin-6-yl]amino)methyl]benzoic acid
Rattus norvegicus
-
IC50 above 0.03 mM
0.00012 - 0.00036
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]-N-methylpropanamide
0.0000028 - 0.000027
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
0.000177
3-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]propanamide
0.000513
3-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]propanamide
0.000266 - 0.02434
3-[2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-7-oxo-6,7-dihydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]propanoic acid
0.008167
3-[3-(2,6-dichloro-4-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.00004 - 0.000067
3-[3-(2-bromo-4-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
0.000019 - 0.000028
3-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
0.000021 - 0.000023
3-[3-(2-bromophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
0.000163
3-[3-(2-chloro-5-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.0000072 - 0.000022
3-[3-(2-iodophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
0.03
3-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
Rattus norvegicus
-
-
0.003385
3-[3-[2-chloro-3-(trifluoromethyl)phenoxy]azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.0000053 - 0.00014
3-[4-(2-benzylphenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
0.000004 - 0.000014
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(1H-imidazol-1-yl)pyridazine
0.000017
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.0000045 - 0.000037
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
0.000004 - 0.000208
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
0.00037
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(1H-tetrazol-5-yl)pyridazine
Mus musculus
-
pH 7.5
0.00002 - 0.000091
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
0.000032 - 0.000712
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3,5-dimethyl-1H-pyrazol-1-yl)pyridazine
0.00002 - 0.00007
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
0.00001 - 0.000076
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,2,4-oxadiazol-3-yl)pyridazine
0.000209
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Homo sapiens
-
pH 7.5
0.001634
3-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,2,4-oxadiazole-5-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000008 - 0.000014
3-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,2-oxazole-5-carboxamide
0.00033 - 0.0033
3-[6-(4'-chlorobiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
0.000134 - 0.00134
3-[6-(4'-methylbiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
0.000145
3-[6-(4-methoxyphenyl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
0.000016 - 0.000029
3-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
0.00189
3-[7-oxo-6-(4-pyridin-3-ylphenyl)-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
0.000336
4'-[6-(methylsulfonyl)-1H-benzimidazol-2-yl]biphenyl-2-ol
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000018
4-(((3-chlorophenyl)amino)methyl)eN-(5-methylthiazol-2-yl)benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.00076
4-(((4-chlorophenyl)amino)methyl)eN-(5-methylthiazol-2-yl)benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.14
4-(1,2-benzoxazol-3-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.538
4-(1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.17
4-(1H-indol-1-yl)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.153
4-(2,3-dihydro-1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.151
4-(2,3-dihydro-1H-indol-1-yl)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000004 - 0.00003
4-(2-bromophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.000006 - 0.000058
4-(2-chloro-4-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.000004 - 0.000018
4-(2-chloro-5-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.00033 - 0.0097
4-(2-chloro-6-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.00001 - 0.00036
4-(2-chlorophenoxy)-N-[3-(1H-imidazol-2-yl)phenyl]piperidine-1-carboxamide
0.000008 - 0.00011
4-(2-chlorophenoxy)-N-[3-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl]piperidine-1-carboxamide
0.000008 - 0.00015
4-(2-chlorophenoxy)-N-[3-(ethylcarbamoyl)phenyl]piperidine-1-carboxamide
0.000004 - 0.000037
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.00081 - 0.0071
4-(2-chlorophenoxy)-N-[3-[(1-methylethyl)carbamoyl]phenyl]piperidine-1-carboxamide
0.000098 - 0.00068
4-(2-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.000003 - 0.00001
4-(2-hydroxyethoxy)-3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.000081 - 0.0019
4-(2-methoxyphenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.0027
4-(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-butyric acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.491
4-(3,4-dihydroquinolin-1(2H)-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00002 - 0.00027
4-(3-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
0.347
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.029
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000026 - 0.026
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
0.018
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4-oxo-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrazin-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.082
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(5-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.014
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(6-hydroxy-4,5,6,7-tetrahydro-1,3-benzothiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.02
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[4-(2-hydroxyethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.052
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[4-(hydroxymethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.008
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(2-hydroxyethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.096
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(hydroxyacetyl)-4,5,6,7-tetrahydro[1,3]thiazolo[5,4-c]pyridin-2-yl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.088
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(hydroxymethyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.093
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-[5-(methylcarbamoyl)-1,3-thiazol-2-yl]piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000008 - 0.000011
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.000004
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.000007 - 0.000015
4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.00000004 - 0.0000004
4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.000022
4-([6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazin-3-yl]ethynyl)phenol
Rattus norvegicus
-
-
0.000002
4-ethoxy-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
0.00000004 - 0.0000004
4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
0.000678
4-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000022
4-hydroxymethyl-2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazole-5-carboxylic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.001218
4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000007 - 0.000008
4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.000021 - 0.000398
4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.000014 - 0.000227
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
0.000016 - 0.000046
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
0.0000032
4-[(2-butyl-phenylamino)-methyl]eN-(4-hydroxymethylthiazol-2-yl)-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000003
4-[(2-butyl-phenylamino)-methyl]eN-[4-(2-hydroxyethyl)-thiazol-2-yl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000043
4-[(2-chloro-phenylamino)-methyl]eN-(4-hydroxymethylthiazol-2-yl)-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000092
4-[(2-chloro-phenylamino)-methyl]eN-(4-methyl-thiazol-2-yl)-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000064
4-[(2-chloro-phenylamino)-methyl]eN-[4-(2-hydroxyethyl)-thiazol-2-yl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.009999
4-[2-(dimethylamino)ethoxy]-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
IC50 above 0.009999 mM
0.000349
4-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]benzoic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000002 - 0.000016
5-(hydroxymethyl)-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
0.000181
5-chloro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000165
5-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000125
5-fluoro-3-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1,2-benzoxazole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000008 - 0.000059
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
0.000054 - 0.000182
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidine
0.0000045
5-[(2-hexyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000051
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid (4-hydroxymethyl-thiazol-2-yl)-amide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000039
5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carboxylic acid [4-(2-hydroxy-ethyl)-thiazol-2-yl]-amide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000003 - 0.000047
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-1H-imidazo[4,5-b]pyrazine
0.000001 - 0.000017
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[4,5-b]pyrazin-2-amine
0.000083 - 0.000199
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-oxadiazole-2-carboxamide
0.000003 - 0.000007
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazole-2-carboxamide
0.000127 - 0.002823
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-1,2,4-triazole-3-carboxamide
0.000017
5-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-N,N-dimethylpyridin-2-amine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000035
5-[6-[4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidin-1-yl]pyridazin-3-yl]-N-methylpyridine-2-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.001
6-(3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
Homo sapiens
-
IC50 below 0.001 mM
10
6-(3-bromobenzyl)-5,7-dimethyl-N-(tetrahydrofuran-2-ylmethyl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
Rattus norvegicus
-
IC50 below 10 mM
0.0007
6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Rattus norvegicus
-
-
0.1
6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxylic acid
Rattus norvegicus
-
IC50 above 0.1 mM
0.000401
6-(cyclopropylsulfonyl)-2-(2'-fluorobiphenyl-4-yl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000489
6-(methylsulfonyl)-2-(2-phenylpyrimidin-5-yl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000472
6-(methylsulfonyl)-2-[4-(3-methylthiophen-2-yl)phenyl]-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000425
6-(methylsulfonyl)-2-[4-(pyridin-3-yl)phenyl]-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000104
6-(methylsulfonyl)-2-[4-(thiophen-3-yl)phenyl]-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000035
6-chloro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00009
6-fluoro-1-(1-[6-[4-(trifluoromethyl)phenyl]pyridazin-3-yl]piperidin-4-yl)-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000016
6-fluoro-1-(1-[6-[6-(trifluoromethyl)pyridin-3-yl]pyridazin-3-yl]piperidin-4-yl)-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000038
6-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1H-indazole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000023
6-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000037
6-fluoro-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000022
6-fluoro-1-[1-[6-(1-propyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000011
6-fluoro-1-[1-[6-(3-methyl-1,2,4-thiadiazol-5-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000777
6-fluoro-1-[1-[6-(4-fluorophenyl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000007
6-fluoro-1-[1-[6-(4-methyl-1,3-thiazol-2-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000016
6-fluoro-1-[1-[6-(4-methyl-1H-imidazol-1-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000021
6-fluoro-1-[1-[6-(4-methyl-1H-pyrazol-1-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000079
6-fluoro-1-[1-[6-(4-methylphenyl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000031
6-fluoro-1-[1-[6-(5-methyl-1,3-thiazol-2-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000121
6-fluoro-1-[1-[6-(5-methylthiophen-2-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000012
6-fluoro-1-[1-[6-(6-methoxypyridin-3-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000013
6-fluoro-1-[1-[6-(6-methylpyridin-3-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000317
6-methoxy-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000005 - 0.000009
6-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
0.000286
6-methyl-1-[1-[6-(1-methyl-1H-pyrazol-4-yl)pyridazin-3-yl]piperidin-4-yl]-2,3-dihydro-1H-indole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000015 - 0.000127
6-[(3,4-dichlorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
0.000013 - 0.000333
6-[(3-chloro-4-fluorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
0.000074 - 0.000118
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
0.000021 - 0.000157
7-[(3-chlorobenzyl)amino]-1-(4-oxopentyl)-3-(3-pyridin-4-ylphenyl)pyrido[3,4-b]pyrazin-2(1H)-one
0.000034 - 0.00019
7-[(3-chlorobenzyl)amino]-3-(4-methoxyphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
0.00004 - 0.000343
7-[(3-chlorobenzyl)amino]-3-(4-methylphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
0.00088
conjugated linoleic acid
Rattus norvegicus
-
in 150 mM KCl, 40 mM NaF, 100 mM sodium phosphate buffer, pH 7.4, at 37°C
0.0383
ethyl 2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxylate
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00075 - 0.000775
methyl (2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)carbamate
0.000039
methyl 3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxylate
Homo sapiens
-
-
0.041
methyl 8-methoxy-8-(2-octylcycloprop-1-en-1-yl)octanoate
Plasmodium falciparum
in 0.1 M potassium phosphate buffer pH 7.2, at 37°C
0.08
methyl 9-(2-octylcycloprop-1-en-1-yl)nonanoate
Plasmodium falciparum
in 0.1 M potassium phosphate buffer pH 7.2, at 37°C
0.167
methyl malvalate
Plasmodium falciparum
in 0.1 M potassium phosphate buffer pH 7.2, at 37°C
0.087
methyl sterculate
Plasmodium falciparum
in 0.1 M potassium phosphate buffer pH 7.2, at 37°C
0.0027
N,N-dimethyl-2-((4-((5-methylthiazol-2-yl)carbamoyl)benzyl)amino)benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.01
N,N-dimethyl-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
Homo sapiens
-
above
0.000046 - 0.000105
N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
0.00452
N-(1,3-thiazol-2-yl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000078
N-(1,3-thiazol-2-ylmethyl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
10
N-(2-amino-2-oxoethyl)-6-(2,3-dichlorobenzyl)pyrazolo[1,5-a]pyrimidine-3-carboxamide
Rattus norvegicus
-
IC50 below 10 mM
0.0025
N-(2-cyclopropyl-2-hydroxyethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Rattus norvegicus
-
-
0.0249
N-(2-cyclopropylethyl)-2-(4-phenoxyphenyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.1
N-(2-cyclopropylethyl)-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-4-carboxamide
Rattus norvegicus
-
IC50 above 0.1 mM
0.037
N-(2-cyclopropylethyl)-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
-
0.000539
N-(2-cyclopropylethyl)-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000005 - 0.00001
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
0.000002 - 0.000007
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
0.000153 - 0.000292
N-(2-hydroxy-2-phenylethyl)-6-[4-(phenylcarbonyl)piperidin-1-yl]pyridazine-3-carboxamide
0.000052 - 0.000311
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000007 - 0.000015
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000095 - 0.00018
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000028 - 0.000037
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000034 - 0.000187
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000007 - 0.000044
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000003 - 0.000007
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.00012
N-(2-hydroxyethyl)-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
Homo sapiens
-
-
0.00015 - 0.00082
N-(2-phenylethyl)-4-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)benzamide
0.00025 - 0.00037
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
0.000006 - 0.000009
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
0.000099 - 0.000194
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
0.00028
N-(2-[2-[(3,4-dichlorobenzyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.00021
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
0.00056
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)benzamide
0.0028
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)methanesulfonamide
0.0028
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)propanamide
0.00047
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)thiophene-3-carboxamide
0.00027
N-(2-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]ethyl)acetamide
0.00075
N-(2-[2-[(3-chloro-4-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
0.0013
N-(2-[2-[(3-chlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
0.0009
N-(2-[2-[(4-chloro-3-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
0.000549
N-(2-[6-[(2-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.000012
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2,2-dimethyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
Rattus norvegicus
-
-
0.000081 - 0.00022
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
0.00008
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-methyl-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
Rattus norvegicus
-
-
0.0000005 - 0.0000014
N-(2-[6-[(3,4-dichlorobenzyl)amino]-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
0.000047 - 0.00466
N-(2-[6-[(3-chloro-4-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
0.0001 - 0.000376
N-(2-[6-[(3-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
0.0176
N-(2-[6-[(3-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.00076
N-(2-[6-[(3-methoxybenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.0000078 - 0.00011
N-(2-[6-[(4-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
0.0000001
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxopyrido[3,4-b]pyrazin-1(2H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.0000086 - 0.00011
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
0.000026 - 0.00013
N-(2-[7-[(3,4-dimethylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
0.0000005 - 0.0000031
N-(2-[7-[(4-fluoro-3-methylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
0.0216
N-(3-methylbutyl)-2-(4-phenoxyphenyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00386
N-(3-methylbutyl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000434
N-(3-methylbutyl)-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.1
N-(3-phenylpropyl)-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.682
N-(4-carbamoyl-1,3-thiazol-2-yl)-4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000038
N-(4-hydroxymethyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
0.0000041
N-(4-methyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.00003
N-(4-methylthiazol-2-yl)-4-(((2-(trifluoromethyl)phenyl)amino)methyl)piperidine-1-carboxamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000097
N-(4-methylthiazol-2-yl)-5-(((2-(trifluoromethyl)phenyl)amino)methyl)thiophene-2-carboxamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000046
N-(4-methylthiazol-2-yl)-5-((o-tolylamino)methyl)picolinamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.00031
N-(4-methylthiazol-2-yl)-6-((o-tolylamino)methyl)nicotinamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.02 - 2
N-(5-carbamoyl-1,3-thiazol-2-yl)-4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000028
N-(5-hydroxymethyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000089
N-(5-methylthiazol-2-yl)-4-(((2-propylphenyl)amino)methyl)benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000095
N-(5-methylthiazol-2-yl)-4-((phenylamino)methyl)benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.204
N-(6,7-dihydro-4H-pyrano[4,3-d][1,3]thiazol-2-yl)-4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0166
N-(cyclopropylmethyl)-2-(4-phenoxyphenyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000099
N-(thiophen-2-ylmethyl)-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00014
N-benzyl-3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxamide
Homo sapiens
-
-
0.00056
N-benzyl-3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyridine-2-carboxamide
Homo sapiens
-
-
0.0073
N-benzyl-6-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
Homo sapiens
-
-
0.00011
N-ethyl-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
Homo sapiens
-
-
0.00093
N-methoxy-3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
Rattus norvegicus
-
-
0.002
N-methyl-2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
-
0.001
N-methyl-2-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-3-carboxamide
Homo sapiens
-
above
0.0272
N-methyl-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000097
N-methyl-3-[(2-oxo-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]ethyl)amino]pyridine-2-carboxamide
Homo sapiens
-
-
0.0063
N-methyl-3-[[2-oxo-2-(4-phenoxypiperidin-1-yl)ethyl]amino]pyrazine-2-carboxamide
Homo sapiens
-
-
0.001
N-methyl-3-[[2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]pyrazine-2-carboxamide
Homo sapiens
-
above
0.0001
N-methyl-3-[[2-oxo-2-(4-[[2-(trifluoromethyl)phenyl]amino]piperidin-1-yl)ethyl]amino]pyrazine-2-carboxamide
Homo sapiens
-
-
0.00026
N-tert-butyl-3-([2-[4-(2-chlorophenoxy)piperidin-1-yl]-2-oxoethyl]amino)pyrazine-2-carboxamide
Homo sapiens
-
-
0.000025
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
0.000066 - 0.000081
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
0.000136
N-[(5-chlorothiophen-2-yl)methyl]-2-[4-[2-(trifluoromethyl)benzoyl]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000142
N-[(5-chlorothiophen-2-yl)methyl]-2-[4-[2-(trifluoromethyl)phenoxy]phenyl]-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00221
N-[(5-chlorothiophen-2-yl)methyl]-3-(5-[hydroxy[2-(trifluoromethyl)phenyl]methyl]-1H-benzimidazol-2-yl)benzamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000009 - 0.000022
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000005 - 0.000006
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.000005 - 0.000007
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
0.00037
N-[2-(5-chlorothiophen-2-yl)ethyl]-2-(4-phenoxyphenyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.00018 - 0.00033
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.01379
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[6-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00021 - 0.00026
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(2,2,2-trifluoroethoxy)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.000047 - 0.000206
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.00205 - 0.0025
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[4-(2,2,2-trifluoroethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.000096 - 0.00038
N-[2-[2-(4-methoxyphenyl)-6-[(3-methylbenzyl)amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.03
N-[2-[2-(4-methoxyphenyl)-6-[[(5-methylisoxazol-3-yl)methyl]amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
IC50 above 0.03 mM
0.000013 - 0.000168
N-[2-[2-oxo-3-pyridin-3-yl-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
0.000044 - 0.00032
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.0000032 - 0.000056
N-[2-[3-(4-ethylphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
0.0000065 - 0.000025
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)quinoxalin-1(2H)-yl]ethyl]acetamide
0.0000033 - 0.000093
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
0.000013 - 0.000018
N-[2-[3-(4-methoxyphenyl)-7-[(3-methylbenzyl)amino]-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
0.000261
N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00012 - 0.0014
N-[2-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.0028
N-[2-[3-tert-butyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.00084
N-[2-[6-(benzylamino)-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00148
N-[2-[6-[[2-fluoro-5-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000051 - 0.000217
N-[2-[6-[[3,5-bis(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.000016 - 0.00002
N-[2-[6-[[4-fluoro-3-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
0.00000005 - 0.00005
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
0.000032 - 0.000049
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
0.000208
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
0.00258
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
0.000017 - 0.00012
N-[3-(methylcarbamoyl)phenyl]-4-(2-methylphenoxy)piperidine-1-carboxamide
0.00011 - 0.00019
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
0.0000042
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
0.0000053
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[[2-(3-methylbutyl)-phenylamino]-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000052
N-[4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
0.000009 - 0.000429
N-[5-(2,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.000031
N-[5-(2-hydroxy-ethyl)-4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000038
N-[5-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000008 - 0.000013
N-[5-(3,4-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.000002 - 0.000034
N-[5-(3,4-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.0000007 - 0.000013
N-[5-(3,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.0000001 - 0.000116
N-[5-(3,5-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.000001 - 0.000017
N-[5-(3-chloro-4-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.000001 - 0.000009
N-[5-(3-chlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.000022 - 0.000639
N-[5-(3-fluoro-4-methylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.000002 - 0.000034
N-[5-(3-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.00026
N-[5-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.001307
N-[5-(3-tert-butylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000003 - 0.000026
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.01
N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
Mus musculus
-
IC50 above 0.01 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000002 - 0.000008
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
0.00012
Sterculic acid
Rattus norvegicus
-
in 150 mM KCl, 40 mM NaF, 100 mM sodium phosphate buffer, pH 7.4, at 37°C
0.0000075
[2-((5-[(2-benzyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
Homo sapiens
pH 7.4, 22°C,ex vivo
0.0000048
[2-((5-[(2-hexyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetate
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000017
[2-((5-[(2-octyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetate
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000009
[2-((5-[(2-trifluoromethyl-phenylamino)-methyl]-thiophene-2-carbonyl)-amino)-thiazol-4-yl]-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000048
[2-(4-([2-(3-methyl-butyl)-phenylamino]-methyl)-benzoylamino)-thiazol-4-yl]-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.1
[2-(biphenyl-4-yl)-1H-benzimidazol-5-yl](phenyl)methanone
Rattus norvegicus
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.004377
[2-methoxy-4-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.009999
[2-methoxy-5-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
Mus musculus
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0158
[2-[4-(benzyloxy)phenyl]-1H-benzimidazol-5-yl](phenyl)methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000082
[2-[4-(benzyloxy)phenyl]-1H-benzimidazol-5-yl][2-(trifluoromethyl)phenyl]methanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0133
[2-[4-(benzyloxy)phenyl]-1H-benzimidazol-5-yl][2-(trifluoromethyl)phenyl]methanone
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000001
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
0.1
[4-(5-benzoyl-1H-benzimidazol-2-yl)phenyl][2-(trifluoromethyl)phenyl]methanone
Rattus norvegicus
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.000026
[5-(2-[3-[2-bromo-5-(trifluoromethyl)phenoxy]propoxy]-1,3-thiazol-5-yl)-2H-tetrazol-2-yl]acetic acid
Homo sapiens
-
-
0.0000023 - 0.000013
[5-(6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
0.00009
[5-[2-([(2S)-3-[2-bromo-5-(trifluoromethoxy)phenoxy]-2-methylpropyl]oxy)-1,3-thiazol-5-yl]-2H-tetrazol-2-yl]acetic acid
Homo sapiens
-
-
0.000014
(2-[4-(o-tolylamino-methyl)-benzoylamino]-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000014
(2-[4-(o-tolylamino-methyl)-benzoylamino]-thiazol-4-yl)-acetic acid
Mus musculus
pH 7.4, 22°C, ex vivo
0.0000051
(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-acetic acid
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000051
(2-[4-[(2-trifluoromethyl-phenylamino)-methyl]-benzoylamino]-thiazol-4-yl)-acetic acid
Mus musculus
pH 7.4, 22°C, ex vivo
0.000002
(2E)-3-(4-methoxyphenyl)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]prop-2-enamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000003
(2E)-3-(4-methoxyphenyl)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]prop-2-enamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.03
(2R)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
Rattus norvegicus
-
IC50 above 0.03 mM
0.03
(2R)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
Homo sapiens
-
IC50 above 0.03 mM
0.03
(2S)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
Rattus norvegicus
-
IC50 above 0.03 mM
0.03
(2S)-N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxypropanamide
Homo sapiens
-
IC50 above 0.03 mM
0.0000034
(5-[6-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.0000056
(5-[6-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.0000049
(5-[6-[3-(2-bromophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.00005
(5-[6-[3-(2-bromophenoxy)azetidin-1-yl]pyridazin-3-yl]-1,3,4-oxadiazol-2-yl)methanol
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000004
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]amino)acetic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000168
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]amino)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000007
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]oxy)acetic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000053
([5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[5,4-d]pyrimidin-2-yl]oxy)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000164
1-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)pyrrolidin-2-one
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000174
1-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)pyrrolidin-2-one
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000268
1-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]urea
Rattus norvegicus
-
-
0.001
1-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]urea
Homo sapiens
-
IC50 above 0.001 mM
0.000004
1-[5-(1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000016
1-[5-(1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000034
1-[5-(1,3,4-oxadiazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000065
1-[5-(1,3,4-oxadiazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000014
1-[5-(1,3-oxazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000055
1-[5-(1,3-oxazol-2-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000015
1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000039
1-[5-(5-methyl-1,2,4-oxadiazol-3-yl)-1,3-thiazol-2-yl]-4-[2-(trifluoromethyl)phenoxy]piperidine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000068
2,3-dihydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
Homo sapiens
-
-
0.0011
2,3-dihydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]propanamide
Rattus norvegicus
-
-
0.000055
2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000306
2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00003
2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000066
2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000009
2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000015
2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000019
2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000125
2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000027
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000504
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000019
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000477
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000024
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000032
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000009
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.00028
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000015
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000194
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000022
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000214
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000012
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000039
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000022
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000067
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00002
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000268
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000009
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000012
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000065
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000945
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000098
2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.00014
2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000255
2-(2'-chlorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004489
2-(2'-chlorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000074
2-(2'-fluorobiphenyl-4-yl)-1H-benzimidazole-6-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000343
2-(2'-fluorobiphenyl-4-yl)-1H-benzimidazole-6-sulfonamide
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000096
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfinyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000472
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfinyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000027
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000065
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000113
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-imidazo[4,5-b]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000156
2-(2'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-imidazo[4,5-b]pyridine
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000015
2-(3'-chlorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000148
2-(3'-chlorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-(3'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00003
2-(3'-fluorobiphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000004
2-(4-[[2-(trifluoromethyl)phenyl]sulfanyl]piperidin-1-yl)-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000024
2-(4-[[2-(trifluoromethyl)phenyl]sulfanyl]piperidin-1-yl)-1,3-thiazole-5-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.00002
2-(biphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000024
2-(biphenyl-4-yl)-6-(methylsulfonyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000042
2-(biphenyl-4-yl)-7-(methylsulfonyl)imidazo[1,2-a]pyridine
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00006
2-(biphenyl-4-yl)-7-(methylsulfonyl)imidazo[1,2-a]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000027
2-hydroxy-N-[2-[2-oxo-3-(trifluoromethyl)-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000015
2-hydroxy-N-[2-[2-oxo-3-(trifluoromethyl)-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.0000061
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000162
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00136
2-hydroxy-N-[4-oxo-3-[3-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
Rattus norvegicus
-
-
0.00136
2-hydroxy-N-[4-oxo-3-[3-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
Homo sapiens
-
-
0.00342
2-hydroxy-N-[4-oxo-3-[4-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
Rattus norvegicus
-
-
0.00342
2-hydroxy-N-[4-oxo-3-[4-(trifluoromethyl)benzyl]-3,4-dihydroquinazolin-6-yl]acetamide
Homo sapiens
-
-
0.000012
2-[(3S)-3-[2-(trifluoromethyl)phenoxy]pyrrolidin-1-yl]-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000084
2-[(3S)-3-[2-(trifluoromethyl)phenoxy]pyrrolidin-1-yl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000477
2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-1,3-benzothiazole
Rattus norvegicus
-
pH and temperature not specified in the publication
0.01064
2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-1,3-benzothiazole
Homo sapiens
-
pH and temperature not specified in the publication
0.000115
2-[4-(2-chlorophenoxy)phenyl]-N-(1,3-thiazol-2-ylmethyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000212
2-[4-(2-chlorophenoxy)phenyl]-N-(1,3-thiazol-2-ylmethyl)-1H-benzimidazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000395
2-[4-(furan-3-yl)phenyl]-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.001705
2-[4-(furan-3-yl)phenyl]-6-(methylsulfonyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000106
2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000106
2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000253
2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000254
2-[4-[2-(trifluoromethyl)benzoyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000076
2-[4-[2-(trifluoromethyl)benzyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000153
2-[4-[2-(trifluoromethyl)benzyl]piperazin-1-yl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000676
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-4-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.006523
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-4-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000003
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.00001
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000041
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-sulfonamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.001019
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazole-5-sulfonamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000097
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,4,5,9-tetrahydro-6H-purin-6-one
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000378
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,4,5,9-tetrahydro-6H-purin-6-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000038
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purin-8-ol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000319
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purin-8-ol
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000257
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purine
Homo sapiens
-
pH and temperature not specified in the publication
0.000083
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-b]pyridine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000755
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-b]pyridine
Homo sapiens
-
pH and temperature not specified in the publication
0.000007
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000029
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000085
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[5,4-c]pyridin-4(5H)-one
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000268
2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[5,4-c]pyridin-4(5H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000019
2-[6-(2-fluorophenyl)pyridin-3-yl]-6-(methylsulfonyl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000058
2-[6-(2-fluorophenyl)pyridin-3-yl]-6-(methylsulfonyl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000016
3,4-bis(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000022
3,4-bis(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000076
3,4-dimethoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000145
3,4-dimethoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000023
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.00072
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000007
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000103
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.002162
3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00217
3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000006
3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000003
3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000828
3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000836
3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
Mus musculus
-
in 250 mM sucrose, 150 mM KCl, 40 mM NaF, 5 mM MgCl2, 100 mM sodium phosphate, pH 7.4, at 37°C
0.000003
3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
Homo sapiens
-
in 250 mM sucrose, 150 mM KCl, 40 mM NaF, 5 mM MgCl2, 100 mM sodium phosphate, pH 7.4, at 37°C
0.000003
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000059
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000008
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00001
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000003
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000015
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000076
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]thiophen-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000145
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]thiophen-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.001
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
IC50 above 0.001 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.001
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
IC50 above 0.001 mM, n 100 mM sodium phosphate, pH 7.4, at 37°C
0.000006
3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000012
3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000276
3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000884
3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00001
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.00486
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.000026
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.000201
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
Homo sapiens
-
pH 7.5
0.0000074
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.000397
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazine
Homo sapiens
-
pH 7.5
0.000085
3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.00171
3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
Homo sapiens
-
pH 7.5
0.00082
3-(4-phenoxypiperidin-1-yl)-6-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]pyridazine
Mus musculus
-
pH 7.5
0.00705
3-(4-phenoxypiperidin-1-yl)-6-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]pyridazine
Homo sapiens
-
pH 7.5
0.000035
3-(5-benzyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.00004
3-(5-benzyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000012
3-(5-benzyl-1,3,4-oxadiazol-2-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.000041
3-(5-benzyl-1,3,4-oxadiazol-2-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
Homo sapiens
-
pH 7.5
0.00022
3-(5-methyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.00581
3-(5-methyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.000009
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000027
3-(5-methyl-1,3,4-oxadiazol-2-yl)-6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.0000023
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.0000023
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000021
3-(5-methyl-1,3,4-thiadiazol-2-yl)-6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]pyridazine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000528
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.001402
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000193
3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000915
3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00012
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]-N-methylpropanamide
Homo sapiens
-
-
0.00036
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]-N-methylpropanamide
Rattus norvegicus
-
-
0.0000028
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
Homo sapiens
-
-
0.000027
3-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
Rattus norvegicus
-
-
0.000177
3-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]propanamide
Rattus norvegicus
-
-
0.000177
3-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]propanamide
Homo sapiens
-
-
0.000513
3-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]propanamide
Rattus norvegicus
-
-
0.000513
3-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]propanamide
Homo sapiens
-
-
0.000266
3-[2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-7-oxo-6,7-dihydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]propanoic acid
Rattus norvegicus
-
pH and temperature not specified in the publication
0.02434
3-[2-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-7-oxo-6,7-dihydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
3-[3-(2-bromo-4-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000067
3-[3-(2-bromo-4-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000019
3-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000028
3-[3-(2-bromo-5-fluorophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000021
3-[3-(2-bromophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000023
3-[3-(2-bromophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.0000072
3-[3-(2-iodophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000022
3-[3-(2-iodophenoxy)azetidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.0000053
3-[4-(2-benzylphenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
Mus musculus
-
pH 7.5
0.00014
3-[4-(2-benzylphenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
Homo sapiens
-
pH 7.5
0.000004
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(1H-imidazol-1-yl)pyridazine
Mus musculus
-
below, pH 7.5
0.000014
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(1H-imidazol-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.0000045
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Mus musculus
-
pH 7.5
0.000026
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Homo sapiens
-
pH 7.5
0.000037
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Homo sapiens
-
-
0.000004
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
Mus musculus
-
pH 7.5
0.000208
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
Homo sapiens
-
pH 7.5
0.00001
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(1H-pyrrol-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000076
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(1H-pyrrol-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.00002
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000091
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.000032
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3,5-dimethyl-1H-pyrazol-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000712
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3,5-dimethyl-1H-pyrazol-1-yl)pyridazine
Homo sapiens
-
pH 7.5
0.00002
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
Mus musculus
-
pH 7.5
0.00007
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
Homo sapiens
-
pH 7.5
0.00001
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,2,4-oxadiazol-3-yl)pyridazine
Mus musculus
-
pH 7.5
0.000076
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,2,4-oxadiazol-3-yl)pyridazine
Homo sapiens
-
pH 7.5
0.000004
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-pyridin-3-ylpyridazine
Mus musculus
-
below, pH 7.5
0.000028
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-pyridin-3-ylpyridazine
Homo sapiens
-
pH 7.5
0.000008
3-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,2-oxazole-5-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000014
3-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,2-oxazole-5-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.00033
3-[6-(4'-chlorobiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Homo sapiens
-
-
0.0033
3-[6-(4'-chlorobiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Rattus norvegicus
-
-
0.000134
3-[6-(4'-methylbiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Homo sapiens
-
-
0.00134
3-[6-(4'-methylbiphenyl-4-yl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Rattus norvegicus
-
-
0.000145
3-[6-(4-methoxyphenyl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Rattus norvegicus
-
-
0.000145
3-[6-(4-methoxyphenyl)-7-oxo-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Homo sapiens
-
-
0.000016
3-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
Homo sapiens
-
-
0.000029
3-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]propanamide
Rattus norvegicus
-
-
0.00189
3-[7-oxo-6-(4-pyridin-3-ylphenyl)-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Rattus norvegicus
-
-
0.00189
3-[7-oxo-6-(4-pyridin-3-ylphenyl)-2-[[3-(trifluoromethyl)phenyl]amino]pteridin-8(7H)-yl]propanamide
Homo sapiens
-
-
0.000342
4'-[6-(methylsulfonyl)-1H-benzimidazol-2-yl]biphenyl-3-ol
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000396
4'-[6-(methylsulfonyl)-1H-benzimidazol-2-yl]biphenyl-3-ol
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000304
4'-[6-(methylsulfonyl)-1H-benzimidazol-2-yl]biphenyl-4-ol
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.002326
4'-[6-(methylsulfonyl)-1H-benzimidazol-2-yl]biphenyl-4-ol
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015
4-((2-chlorophenoxy)methyl)eN-(pyridin-4-yl)benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.00051
4-((2-chlorophenoxy)methyl)eN-(pyridin-4-yl)benzamide
Mus musculus
pH 7.4, 22°C, ex vivo
0.0014
4-((2-chlorophenoxy)methyl)eN-(pyridin-4-yl)benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.000004
4-(2-bromophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
below
0.00003
4-(2-bromophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000006
4-(2-chloro-4-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000058
4-(2-chloro-4-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000004
4-(2-chloro-5-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
below
0.000018
4-(2-chloro-5-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.00033
4-(2-chloro-6-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.0097
4-(2-chloro-6-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.00001
4-(2-chlorophenoxy)-N-[3-(1H-imidazol-2-yl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.00036
4-(2-chlorophenoxy)-N-[3-(1H-imidazol-2-yl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000008
4-(2-chlorophenoxy)-N-[3-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.00011
4-(2-chlorophenoxy)-N-[3-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000008
4-(2-chlorophenoxy)-N-[3-(ethylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.00015
4-(2-chlorophenoxy)-N-[3-(ethylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000004
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
below
0.0000078
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Rattus norvegicus
-
-
0.000037
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.00081
4-(2-chlorophenoxy)-N-[3-[(1-methylethyl)carbamoyl]phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.0071
4-(2-chlorophenoxy)-N-[3-[(1-methylethyl)carbamoyl]phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000098
4-(2-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.00068
4-(2-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000003
4-(2-hydroxyethoxy)-3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00001
4-(2-hydroxyethoxy)-3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000081
4-(2-methoxyphenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.0019
4-(2-methoxyphenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.00002
4-(3-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.00027
4-(3-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Homo sapiens
-
-
0.000026
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.026
4-(6-fluoro-2,3-dihydro-1H-indol-1-yl)-N-(4-methyl-1,3-thiazol-2-yl)piperidine-1-carboxamide
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000008
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000011
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000004
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000004
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000007
4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000015
4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00000004
4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000004
4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
4-ethoxy-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
4-ethoxy-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00000004
4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
Homo sapiens
-
in 250 mM sucrose, 150 mM KCl, 40 mM NaF, 5 mM MgCl2, 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000004
4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
Mus musculus
-
in 250 mM sucrose, 150 mM KCl, 40 mM NaF, 5 mM MgCl2, 100 mM sodium phosphate, pH 7.4, at 37°C
0.000007
4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000008
4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000021
4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000398
4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000014
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000227
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000016
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000046
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000002
5-(hydroxymethyl)-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000016
5-(hydroxymethyl)-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000059
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidin-7(6H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000054
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000182
5-methyl-2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl][1,3]thiazolo[4,5-d]pyrimidine
Homo sapiens
-
pH and temperature not specified in the publication
0.000003
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-1H-imidazo[4,5-b]pyrazine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000047
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-1H-imidazo[4,5-b]pyrazine
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[4,5-b]pyrazin-2-amine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000017
5-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl][1,3]thiazolo[4,5-b]pyrazin-2-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.000083
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-oxadiazole-2-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000199
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-oxadiazole-2-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000003
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazole-2-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000007
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3,4-thiadiazole-2-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000127
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-1,2,4-triazole-3-carboxamide
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.002823
5-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1H-1,2,4-triazole-3-carboxamide
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.001248
6-(ethylsulfonyl)-2-(2'-fluorobiphenyl-4-yl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.001308
6-(ethylsulfonyl)-2-(2'-fluorobiphenyl-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.001713
6-(methylsulfonyl)-2-[4-(pyridin-2-yl)phenyl]-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00176
6-(methylsulfonyl)-2-[4-(pyridin-2-yl)phenyl]-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002473
6-(methylsulfonyl)-2-[4-(pyridin-4-yl)phenyl]-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.004246
6-(methylsulfonyl)-2-[4-(pyridin-4-yl)phenyl]-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000097
6-(methylsulfonyl)-2-[4-(thiophen-2-yl)phenyl]-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000231
6-(methylsulfonyl)-2-[4-(thiophen-2-yl)phenyl]-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000005
6-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000009
6-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000175
6-tert-butyl-2-(2'-fluorobiphenyl-4-yl)-1H-benzimidazole
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000731
6-tert-butyl-2-(2'-fluorobiphenyl-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
6-[(3,4-dichlorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
Homo sapiens
-
-
0.000127
6-[(3,4-dichlorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
Rattus norvegicus
-
-
0.000013
6-[(3-chloro-4-fluorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
Homo sapiens
-
-
0.000333
6-[(3-chloro-4-fluorobenzyl)amino]-4-(4-oxopentyl)-2-pyridin-3-ylpyrido[2,3-b]pyrazin-3(4H)-one
Rattus norvegicus
-
-
0.000001
6-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-9H-purine
Rattus norvegicus
-
IC50 less than 0.000039 mM, pH and temperature not specified in the publication
0.000039
6-[4-(2-bromo-5-fluorophenoxy)piperidin-1-yl]-9H-purine
Homo sapiens
-
IC50 less than 0.000039 mM, pH and temperature not specified in the publication
0.000074
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000118
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
Homo sapiens
-
-
0.00001
6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000048
6-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purine
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
7-[(3-chlorobenzyl)amino]-1-(4-oxopentyl)-3-(3-pyridin-4-ylphenyl)pyrido[3,4-b]pyrazin-2(1H)-one
Homo sapiens
-
-
0.000157
7-[(3-chlorobenzyl)amino]-1-(4-oxopentyl)-3-(3-pyridin-4-ylphenyl)pyrido[3,4-b]pyrazin-2(1H)-one
Rattus norvegicus
-
-
0.000034
7-[(3-chlorobenzyl)amino]-3-(4-methoxyphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
Homo sapiens
-
-
0.00019
7-[(3-chlorobenzyl)amino]-3-(4-methoxyphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
Rattus norvegicus
-
-
0.00004
7-[(3-chlorobenzyl)amino]-3-(4-methylphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
Homo sapiens
-
-
0.000343
7-[(3-chlorobenzyl)amino]-3-(4-methylphenyl)-1-(4-oxopentyl)pyrido[3,4-b]pyrazin-2(1H)-one
Rattus norvegicus
-
-
0.000039
8-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purin-6-amine
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000162
8-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-9H-purin-6-amine
Homo sapiens
-
pH and temperature not specified in the publication
0.03
benzyl [3-(2,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Rattus norvegicus
-
IC50 above 0.03 mM
0.03
benzyl [3-(2,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Homo sapiens
-
IC50 above 0.03 mM
0.000251
benzyl [3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Rattus norvegicus
-
-
0.000251
benzyl [3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Homo sapiens
-
-
0.00025
benzyl [3-(3,4-dimethylbenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Rattus norvegicus
-
-
0.00025
benzyl [3-(3,4-dimethylbenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Homo sapiens
-
-
0.000865
benzyl [3-(3-chloro-4-fluorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Rattus norvegicus
-
-
0.000865
benzyl [3-(3-chloro-4-fluorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Homo sapiens
-
-
0.00026
benzyl [3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Rattus norvegicus
-
-
0.00026
benzyl [3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]carbamate
Homo sapiens
-
-
0.0032
benzyl [3-[(3,4-dichlorobenzyl)carbamoyl]-4-(pyridin-3-yloxy)phenyl]carbamate
Rattus norvegicus
-
-
0.0032
benzyl [3-[(3,4-dichlorobenzyl)carbamoyl]-4-(pyridin-3-yloxy)phenyl]carbamate
Homo sapiens
-
-
0.00075
methyl (2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)carbamate
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000775
methyl (2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)carbamate
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000046
N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000105
N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000005
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.00001
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
Homo sapiens
-
-
0.000002
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000007
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
Homo sapiens
-
-
0.000153
N-(2-hydroxy-2-phenylethyl)-6-[4-(phenylcarbonyl)piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000292
N-(2-hydroxy-2-phenylethyl)-6-[4-(phenylcarbonyl)piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000052
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000311
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000007
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000015
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000095
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.00018
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000028
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000037
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000034
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000187
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000007
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000044
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000003
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000007
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.00015
N-(2-phenylethyl)-4-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)benzamide
Mus musculus
-
-
0.00082
N-(2-phenylethyl)-4-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)benzamide
Homo sapiens
-
-
0.00025
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
Homo sapiens
-
-
0.00037
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
Mus musculus
-
-
0.000006
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000006
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000009
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Homo sapiens
-
-
0.000099
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
Homo sapiens
-
-
0.000194
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
Mus musculus
-
-
0.00021
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.00021
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.00056
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)benzamide
Rattus norvegicus
-
-
0.00056
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)benzamide
Homo sapiens
-
-
0.0028
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)methanesulfonamide
Rattus norvegicus
-
-
0.0028
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)methanesulfonamide
Homo sapiens
-
-
0.0028
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)propanamide
Rattus norvegicus
-
-
0.0028
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)propanamide
Homo sapiens
-
-
0.00047
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)thiophene-3-carboxamide
Rattus norvegicus
-
-
0.00047
N-(2-[2-[(3,4-dichlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)thiophene-3-carboxamide
Homo sapiens
-
-
0.00027
N-(2-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.00027
N-(2-[2-[(3,4-dichlorophenyl)amino]-7-oxo-6-(4-pyridin-3-ylphenyl)pteridin-8(7H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.00075
N-(2-[2-[(3-chloro-4-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.00075
N-(2-[2-[(3-chloro-4-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.0013
N-(2-[2-[(3-chlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.0013
N-(2-[2-[(3-chlorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.0009
N-(2-[2-[(4-chloro-3-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.0009
N-(2-[2-[(4-chloro-3-fluorophenyl)amino]-6-(4-methoxyphenyl)-7-oxopteridin-8(7H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.000081
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.00022
N-(2-[6-[(3,4-dichlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.0000005
N-(2-[6-[(3,4-dichlorobenzyl)amino]-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
Homo sapiens
-
-
0.0000014
N-(2-[6-[(3,4-dichlorobenzyl)amino]-3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl]ethyl)-2-hydroxyacetamide
Rattus norvegicus
-
-
0.000047
N-(2-[6-[(3-chloro-4-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.00466
N-(2-[6-[(3-chloro-4-fluorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.0001
N-(2-[6-[(3-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.000376
N-(2-[6-[(3-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.0000078
N-(2-[6-[(4-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.00011
N-(2-[6-[(4-chlorobenzyl)amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.0000086
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.00011
N-(2-[7-[(3,4-dichlorobenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.000026
N-(2-[7-[(3,4-dimethylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.00013
N-(2-[7-[(3,4-dimethylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.0000005
N-(2-[7-[(4-fluoro-3-methylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
Rattus norvegicus
-
-
0.0000031
N-(2-[7-[(4-fluoro-3-methylbenzyl)amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl)acetamide
Homo sapiens
-
-
0.0000038
N-(4-hydroxymethyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000038
N-(4-hydroxymethyl-thiazol-2-yl)-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
Mus musculus
pH 7.4, 22°C, ex vivo
0.0000064
N-(4-methyl-thiazol-2-yl)-4-(o-tolylamino-methyl)-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000064
N-(4-methyl-thiazol-2-yl)-4-(o-tolylamino-methyl)-benzamide
Mus musculus
pH 7.4, 22°C, ex vivo
0.000025
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000025
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Homo sapiens
-
-
0.000066
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000081
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Homo sapiens
-
-
0.000009
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000022
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000005
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000006
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000005
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Homo sapiens
-
-
0.000007
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.00018
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.00033
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00021
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(2,2,2-trifluoroethoxy)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.00026
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(2,2,2-trifluoroethoxy)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000047
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000206
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00205
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[4-(2,2,2-trifluoroethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.0025
N-[2-[2-(4-methoxyphenyl)-3-oxo-6-[[4-(2,2,2-trifluoroethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000096
N-[2-[2-(4-methoxyphenyl)-6-[(3-methylbenzyl)amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.00038
N-[2-[2-(4-methoxyphenyl)-6-[(3-methylbenzyl)amino]-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000013
N-[2-[2-oxo-3-pyridin-3-yl-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000168
N-[2-[2-oxo-3-pyridin-3-yl-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000044
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00032
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000032
N-[2-[3-(4-ethylphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000056
N-[2-[3-(4-ethylphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.0000065
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)quinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000025
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-([[4-(trifluoromethyl)pyridin-2-yl]methyl]amino)quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.0000033
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000033
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000093
N-[2-[3-(4-methoxyphenyl)-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000013
N-[2-[3-(4-methoxyphenyl)-7-[(3-methylbenzyl)amino]-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000018
N-[2-[3-(4-methoxyphenyl)-7-[(3-methylbenzyl)amino]-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00012
N-[2-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.0014
N-[2-[3-oxo-2-pyridin-3-yl-6-[[3-(trifluoromethyl)benzyl]amino]pyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000051
N-[2-[6-[[3,5-bis(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000217
N-[2-[6-[[3,5-bis(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000016
N-[2-[6-[[4-fluoro-3-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.00002
N-[2-[6-[[4-fluoro-3-(trifluoromethyl)benzyl]amino]-2-(4-methoxyphenyl)-3-oxopyrido[2,3-b]pyrazin-4(3H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.00000005
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.0000006
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
Rattus norvegicus
-
-
0.000034
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.00005
N-[2-[7-[[4-chloro-3-(trifluoromethyl)benzyl]amino]-3-(4-methoxyphenyl)-2-oxoquinoxalin-1(2H)-yl]ethyl]acetamide
Homo sapiens
-
-
0.000032
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000049
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000208
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.000208
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.000261
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.000261
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.000268
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-phenoxyacetamide
Rattus norvegicus
-
-
0.000268
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-phenoxyacetamide
Homo sapiens
-
-
0.0116
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-3-hydroxypropanamide
Rattus norvegicus
-
-
0.0116
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-3-hydroxypropanamide
Homo sapiens
-
-
0.00386
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]acetamide
Rattus norvegicus
-
-
0.00386
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]acetamide
Homo sapiens
-
-
0.000348
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.000348
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.00269
N-[3-(3-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.00269
N-[3-(3-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.00258
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.00258
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydropyrido[2,3-d]pyrimidin-6-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.00117
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.00117
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.00797
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-phenoxyacetamide
Rattus norvegicus
-
-
0.00797
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-phenoxyacetamide
Homo sapiens
-
-
0.00312
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.00312
N-[3-(4-chlorobenzyl)-4-oxo-3,4-dihydroquinazolin-7-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.00385
N-[3-(biphenyl-3-ylmethyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.00385
N-[3-(biphenyl-3-ylmethyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.000017
N-[3-(methylcarbamoyl)phenyl]-4-(2-methylphenoxy)piperidine-1-carboxamide
Mus musculus
-
-
0.00012
N-[3-(methylcarbamoyl)phenyl]-4-(2-methylphenoxy)piperidine-1-carboxamide
Homo sapiens
-
-
0.01
N-[3-(tert-butylcarbamoyl)phenyl]-4-(2-chlorophenoxy)piperidine-1-carboxamide
Homo sapiens
-
above
0.01
N-[3-(tert-butylcarbamoyl)phenyl]-4-(2-chlorophenoxy)piperidine-1-carboxamide
Mus musculus
-
above
0.00011
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.00019
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.00019
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Homo sapiens
-
-
0.00019
N-[3-[4-chloro-3-(trifluoromethyl)benzyl]-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
Rattus norvegicus
-
-
0.0000042
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000042
N-[4-(2-hydroxy-ethyl)-thiazol-2-yl]-4-[(2-trifluoromethylphenylamino)-methyl]-benzamide
Mus musculus
pH 7.4, 22°C, ex vivo
0.0000052
N-[4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
Homo sapiens
pH 7.4, 22°C, recombinant enzyme
0.0000052
N-[4-(3-hydroxy-propyl)-thiazol-2-yl]-4-[(2-trifluoromethyl-phenylamino)-methyl]-benzamide
Mus musculus
pH 7.4, 22°C, ex vivo
0.000009
N-[5-(2,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000429
N-[5-(2,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000008
N-[5-(3,4-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000013
N-[5-(3,4-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
N-[5-(3,4-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000034
N-[5-(3,4-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000007
N-[5-(3,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000013
N-[5-(3,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000001
N-[5-(3,5-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000116
N-[5-(3,5-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000001
N-[5-(3-chloro-4-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000017
N-[5-(3-chloro-4-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000001
N-[5-(3-chlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000009
N-[5-(3-chlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000022
N-[5-(3-fluoro-4-methylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000639
N-[5-(3-fluoro-4-methylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
N-[5-(3-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000034
N-[5-(3-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000003
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000006
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000026
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000002
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000008
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Homo sapiens
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000001
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000001
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.000001
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000001
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
[3-(2-[4-[2-(trifluoromethyl)phenoxy]piperidin-1-yl]-1,3-thiazol-5-yl)-1,2,4-oxadiazol-5-yl]methanol
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000023
[5-(6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
Rattus norvegicus
-
rat liver microsomal enzyme assay, pH not specified in the publication, temperature not specified in the publication
0.000013
[5-(6-[3-[2-(trifluoromethyl)phenoxy]azetidin-1-yl]pyridazin-3-yl)-1,3,4-oxadiazol-2-yl]methanol
Homo sapiens
-
HepG2 whole cell assay, pH not specified in the publication, temperature not specified in the publication
0.00089
[[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]amino](oxo)acetic acid
Rattus norvegicus
-
-
0.00089
[[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]amino](oxo)acetic acid
Homo sapiens
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0002
-
129S6/SvEvTac mice under low-fat diet, liver microsomes, stearoyl-CoA as substrate
0.0004
0.0011
-
C57Bl/B6 mice under low-fat diet, liver microsomes, stearoyl-CoA as substrate
0.0016
-
C57Bl/B6 mice under high-fat diet, liver microsomes, stearoyl-CoA as substrate
additional information
0.0004
-
129S6/SvEvTac mice under high-fat diet, liver microsomes, stearoyl-CoA as substrate
additional information
-
administering CoEDTA, ytterbium acetate and chromium-mordanted straw decrease in milk cis-9 10:1/10:0, cis-9 12:1/12:0, cis-9 14:1/14:0, cis-9 16:1/16:0, cis-9 17:1/17:0, cis-9 18:1/18:0 and cis-9,trans-11 conjugated linoleic acid/trans-11 18:1 concentration rations of 44.6,52.7, 58.7, 36.8, 37.2, 44.3 and 43.0%, cowsare fed with incremental levels of fish oil
additional information
-
enzyme activity in interfascicular adipose tissue ranges from 14.4 to 23.9, in subcutaneous adipose tissue from 32.5 to 44.4, in duodenal mucosal cells from 4.34 to 5.29 and in liver from 0.342 to 0.786 nmol/mg protein/7 min under diets based on corn, flaxseed, sorghum or whole cotton seed, respectively
additional information
-
higher enzyme activity in subcutaneous adipose tissue from long-fed than in short-fed steers
additional information
-
SCD enzyme activities in interfascicular and subcutaneous adipose tissue, duodenal mucosal cells and liver are not affected by dietary whole cottonseed or grain source
additional information
-
enzyme activities of 33 to 39 nmol/g tissue/7 min in subcutaneous adipose tissue, 61 to 89 nmol/g tissue/7 min in interfascicular adipose tissue, 118 to 141 nmol/g tissue/7 min in duodenal mucosal cells and 9 to 21 nmol/g tissue/7 min in liver of Angus steers fed with whole cottonseed or grain source, respectively
additional information
enzyme activity and fatty acid composition in response to different feeding conditions, overview, stearoyl-CoA desaturase activity in the s.c. adipose from the tail-head region do not differ among corn oil supplementation levels. Similarly, SCD mRNA level do not differ among oilsupplementation levels
additional information
-
Angus and Wagyu steers consuming high-roughage diets exhibit large differences in adipose tissue fatty acid composition, but there are no differences in terminal measures of SCD activity or gene expression
additional information
-
cold induces an 8 to 10fold increase in specific activity
additional information
-
enzyme activity is highest in microsomes from cells grown at 37°C and lowest in cells grown at 15°C
additional information
-
enzyme activity is reduced by feeding 2.5% and 5% conjugated linoleic acid
additional information
-
14C-labeled stearoyl-CoA as substrate, microsomal fraction, similar desaturase activity of hSCD1 and GFP-hSCD1, thin layer chromatography
additional information
14C-labeled stearoyl-CoA as substrate, microsomal fraction, similar desaturase activity of hSCD1 and GFP-hSCD1, thin layer chromatography
additional information
-
SV40-transformed WI38 fibroblasts exhibit a 2.2fold higher enzyme activity compared to normal WI38 cells
additional information
-
induction of apoptosis with 40 microM etoposide leads to a 20% decrease in enzyme activity in SV40-transformed WI38 fibroblasts compared to normal WI38 fibroblasts, which are resistant to etoposide-induced apoptosis
additional information
-
incubation of A-549 cells with 25 microM C6-ceramide for 6 h and 24 h leads to a 45% and 25% decrease in enzyme activity
additional information
-
mean SCD1 enzyme activity is 2.1fold higher in muscle microsomes prepared from obese compred to lean donors, microsomal preparations from rectus abdominus muscle
additional information
-
14C-labeled steaoryl-CoA as substrate, microsomal fraction, similar desaturase activity of hSCD5 and GFP-hSCD5, thin layer chromatography
additional information
14C-labeled steaoryl-CoA as substrate, microsomal fraction, similar desaturase activity of hSCD5 and GFP-hSCD5, thin layer chromatography
additional information
-
indirect measurement of SCD activity by plasma palmitoleic acid content determination of 138 samples, plasma triglycerides and fatty acid compositions, overview
additional information
-
fatty acid compositions in presence and absence of inhibitors
additional information
-
40% increase in enzyme activity in hepatic microsomes in tristearin-fed compared with trioleate-fed mice
additional information
-
enzyme activity increased by HF feeding and decreased after treatment with Scd1 sequence-specific antisense oligodeoxynucleotide compared with animals treated with scrambled antisense oligodeoxynucleotide
additional information
-
antisense oligodeoxynucleotide-mediated inhibition SCD1 in C57BL/6J mice results in resistance to high-fat diet-induced obesity and hepatic steatosis, also lower levels of postprandial glucose and insulin, increased oxygen consumption, increased physical activity and reduced lipogenic gene expression
additional information
-
10fold suppression in 24 microg/day leptin-treated ob/ob mice with or without exogenous insulin treatment
additional information
fasting reduces hepatic SCD1 protein expression and activity, and refeeding a high-carbohydrate or a high-sucrose diet increases both
additional information
fasting reduces hepatic SCD1 protein expression and activity, and refeeding a high-carbohydrate or a high-sucrose diet increases both
additional information
fasting reduces hepatic SCD1 protein expression and activity, and refeeding a high-carbohydrate or a high-sucrose diet increases both
additional information
fasting reduces hepatic SCD1 protein expression and activity, and refeeding a high-carbohydrate or a high-sucrose diet increases both
additional information
-
maximal activity at a concentration of 0.03 mM stearoyl-CoA
additional information
-
enzyme activity decreases by 50% in the liver after treatment with Scd1 sequence-specific antisense oligodeoxynucleotide compared with animals treated with scrambled antisense oligodeoxynucleotide
additional information
-
long-term glucose oversupply induces rapid increase in SCD expression and enzyme activity
additional information
-
short time (3 weeks) of sucrose feeding decreases mRNA level and enzyme activity, whereas long term (6 months) of sucrose feeding increases enzyme activity and mRNA level
additional information
Sprague-Dawley rats are food restricted at 50% of their spontaneous food intake for 2 weeks and than are refeeded, enzyme activity is significantly elevated at the end of 2 weeks of semistarvation, +72%, and remains higher on day 7 of refeeding, +44%
additional information
-
a reduced protein diet significantly increases protein expression and activity in muscle but not in subcutaneous adipose tissue
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7.5
8.7
-
but assay at pH 7.4, to standardize the experiments in vitro with those carried out with intact bacteria
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
pH 5.5: about 80% of maximum activity, pH 9.0: about 45% of maximum activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
25
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
milk fish, enzyme activity increases significantly in the beginning of cold acclimation, peaks at day 4 and then decreases constantly. Change of enzyme activity parllels the change of DELTA9 desaturation in the animal
-
-
brenda
grass carp, enzyme activity increases gradually in the first week of cold acclimation, increases dramatically afterward and the maintains a very high level. Change of enzyme activity parllels the change of DELTA9 desaturation in the animal
-
-
brenda
collected in a tidal pool near the King Sejong Station, King George Island, Antarctica
-
-
brenda
higher enzymic acitivity in Jersey-sired cattle than in Limousin-sired cattle, positive relationship between adipose tissue beta-carotene and desaturation
-
-
brenda
short- and long-fed Angus and Wagyu steers with corn-based or hay-based diets
-
-
brenda
transient upregulation of isoform Cps2 during first days of cold acclimation, no substantial response of isoform activity to diet of saturated fatty acids
SwissProt
brenda
-
695468, 695567, 696671, 696680, 696683, 696684, 696685, 696702, 697028, 697558, 697559, 697777, 697824, 697825, 699187, 699984, 701346
-
-
brenda
-
UniProt
brenda
-
674542, 675062, 675626, 676252, 684339, 685606, 687766, 688248, 695472, 696441, 696445, 696684, 696685, 696702, 697181, 698917, 698977, 726658, 727586, 727982
-
-
brenda
enzyme inhibition by specific antisense oligonucleotide inhibitors, reduction of enzyme expression, reduction of fatty acid synthesis and secretion, increase in fatty acid oxidation
-
-
brenda
ob/ob mice, isoform SCD4, tissue-specific regulation by leptin and dietary factors
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the level of SCD protein expression in cumulus cells does not change when cumulus-oocyte complexes (COCs) are exposed to saturated stearic acid during maturation
brenda
enzyme SCD1 is upregulated in enriched liver tumor-initiating cell populations and sporadically expressed in human hepatocellular carcinoma specimens, elevated SCD1 expression in hepatocellular carcinoma tumors
brenda
stably expressing the full-length HCV genotype 1b replicon with a S2204I adaptive mutation in NS5A (Huh7.5 FGR)
brenda
upregulation of SCD1 of self-renewing liver cancer cells in chemoresistant hepatospheres
brenda
-
normal lung fibroblasts WI38 and the derived SV40-tranformed strain cells SV40-WI38, SCD protein content 3.3fold increased in SV40-WI38 cells compared to WI38 cells
brenda
SCD2 is the predominant SCD isoform expressed in oligodendrocytes
brenda
additional information
isozyme SCD1 is dramatically induced during 3T3L1 differentiation
brenda
-
subcutaneous, gene expression very low in tissue from the short-fed steers fed the corn-based diet
brenda
-
Angus and Wagyu steers consuming high-roughage diets exhibit large differences in adipose tissue fatty acid composition, but there are no differences in terminal measures of SCD activity or gene expression
brenda
SCD1 is highly expressed in subcutaneous and visceral fat, peaking at 2 days after differentiation in bovine stromal vascular fraction (SVF) cells, SVF cells are isolated from inguinal adipose tissue with the type I collagenase method
brenda
hSCD1, sevenfold higher mRNA level in adipose tissue than in liver, real-time PCR
brenda
-
mRNA levels increases after 8 mg/day rosiglitazone treatment
brenda
-
injection of Scd1 sequence-specific antisense oligodeoxynucleotides decreases Scd1 gene expression in brown and white adipose tissue as well as in liver
brenda
-
a reduced protein diet does not change protein expression and activity in subcutaneous adipose tissue
brenda
specific high expression level of isozyme SCD5, equally distributed between white and gray matter
brenda
equivalent levels of hSCD1 and hSCD5 mRNA in adult brain, real-time PCR
brenda
-
post mortem brains, gender- and age-related quantitative expression analysis of SCD in brains in relation to the fatty acid composition, overview
brenda
high expression level of isozyme SCD2
brenda
exclusively expressed in heart, no repression by dietary polyunsaturated fatty acids, induction in SCD1-deficient animals
brenda
isozyme SCD4 is expressed mainly in the heart
brenda
-
-
brenda
harboring the pFKI389neo/NS3-39/5.1 subgenomic replicon (Huh7 SGR, genotype 1b)
brenda
hSCD1, sevenfold higher mRNA level in adipose tissue than in liver, real-time PCR
brenda
-
hepatic SCD1 activity index correlates negatively with liver fat and positively with insulin sensitivity, overview
brenda
high expression level of isozyme SCD1
brenda
-
5fold higher expression and 40% increase in enzyme activity in hepatic microsomes in tristearin-fed compared with trioleate-fed mice
brenda
-
treatment with Scd1 sequence-specific antisense oligodeoxynucleotide decreases mRNA and protein, real-time PCR
brenda
-
injection of Scd1 sequence-specific antisense oligodeoxynucleotides decreases Scd1 gene expression in brown and white adipose tissue as well as in liver
brenda
-
on a high-fat diet the livers of wild-type mice become steatotic, stearoyl-CoA desaturase deficiency protects against liver steatosis, on a chow diet the livers of wild-type and SCD1-/- mice are normal and of similar mass
brenda
-
24 microg/day leptin treatment for 4 days with or without exogenous insulin treatment of ob/ob mice suppresses mRNA, SCD protein undetectable in leptin-treated ob/ob mice with or without exogenous insulin treatment
brenda
SCD1 is highly expressed and significantly changed by various diets, where part of the medium chain triacylglycerol oil in control diet was replaced with 1.1% fungal oil, 1.9% fish oil or both 1.1% fungal and 1.9% fish oil
brenda
-
treatment with Scd1 sequence-specific antisense oligodeoxynucleotide decreases mRNA and protein, real-time PCR
-
brenda
-
SCD1 is highly expressed and significantly changed by various diets, where part of the medium chain triacylglycerol oil in control diet was replaced with 1.1% fungal oil, 1.9% fish oil or both 1.1% fungal and 1.9% fish oil
-
brenda
-
-
brenda
-
mRNA decreased by 80% following 2 injections of Scd1 sequence-specific antisense oligodeoxynucleotide over 5 days, real-time PCR
brenda
-
-
brenda
-
a reduced protein diet significantly increases protein expression and activity
brenda
-
a reduced protein diet increases SCD protein expression and activity
brenda
-
immunocytochemistry of day 8 myotubes using an anti-SCD1 antibody, SCD1 mRNA levels are increased 2.8fold and protein levels are increased 5.7fold in myotubes from obese compared to lean subjects
brenda
-
C57Bl/B6 mice under low-fat diet have 3 to 4 times more SCD1 transcript than 129S6/SvEvTac mice under low-fat diet, mRNA increased 3fold by high-fat feeding of 129S6/SvEvTac mice and 1.5fold by high-fat feeding of C57Bl/B6 mice
brenda
-
long-term glucose oversupply induces rapid increase in SCD expression and enzyme activity
brenda
-
increased relative expression level in obese insulin-resistent ZDF rats compared to lean insulin-sensitive rats
brenda
high expression level of isozyme SCD1
brenda
additional information
-
no activity in liver and perirenal adipose microsomes
brenda
additional information
expression level of SCD1 is highest in subcutaneous and visceral fat, followed by the longissimus dorsi muscle, heart, lung, large intestine, kidney, abomasum, liver, rumen, small intestine, reticulum, spleen, and omasum. Expression level of SCD1 in high marbling is significantly higher than that in low marbling
brenda
additional information
-
limited expression in adult tissues, detected in normal fibroblasts and cancer cell
brenda
additional information
isozyme SCD1 is abundantly expressed in lipogenic tissues
brenda
additional information
isozyme SCD1 is abundantly expressed in lipogenic tissues
brenda
additional information
isozyme SCD5 is predominantly expressed in the brain and pancreas
brenda
additional information
isozyme SCD5 is predominantly expressed in the brain and pancreas
brenda
additional information
mRNA expression levels of SCD1 in tumor tissues markedly elevated compared to that in adjacent non-tumor tissues
brenda
additional information
SCD1 is highly expressed in ovarian cancer tissue, cell lines, and a genetic model of ovarian cancer stem cells
brenda
additional information
human SCD5 is primarily found in fetal brain, and in adult brain and pancreas, adrenal gland, gonads, and to a lesser degree in kidney, lung, and normal and obese human adipose tissue, it has a different expression pattern of SCD5 compared to SCD1. The desaturase transcript levels increase with nuclear maturity and are thought to predict the quality of oocytes and viability of embryos. SCD5 expression has also been observed in several human oncogene-transformed and cancer cells
brenda
additional information
-
SCD1 is ubiquitously expressed but most abundant in liver and adipose
brenda
additional information
SCD1 is ubiquitously expressed but most abundant in liver and adipose
brenda
additional information
SCD5 expression is high in brain and pancreas
brenda
additional information
isozyme tissue expression analysis, isoyzme SCD3 shows expression in several tissues
brenda
additional information
isozyme tissue expression analysis, isoyzme SCD3 shows expression in several tissues
brenda
additional information
isozyme tissue expression analysis, isoyzme SCD3 shows expression in several tissues
brenda
additional information
-
isozyme tissue expression analysis, isoyzme SCD3 shows expression in several tissues
brenda
additional information
-
stearoyl-CoA desaturase deficient mice have very low levels of triglycerides in the VLDL and LDL fractions relative to the wild-type
brenda
additional information
SCD2 isoform is ubiquitously expressed in most tissues except liver
brenda
additional information
SCD2 isoform is ubiquitously expressed in most tissues except liver
brenda
additional information
SCD2 isoform is ubiquitously expressed in most tissues except liver
brenda
additional information
SCD2 isoform is ubiquitously expressed in most tissues except liver
brenda
additional information
isozyme SCD1 is ubiquitously expressed and shows higher expression in metabolic tissues
brenda
additional information
isozyme SCD1 is ubiquitously expressed and shows higher expression in metabolic tissues
brenda
additional information
isozyme SCD1 is ubiquitously expressed and shows higher expression in metabolic tissues
brenda
additional information
isozyme SCD1 is ubiquitously expressed and shows higher expression in metabolic tissues
brenda
additional information
isozyme SCD2 is ubiquitously expressed in most tissues except adult mouse liver
brenda
additional information
isozyme SCD2 is ubiquitously expressed in most tissues except adult mouse liver
brenda
additional information
isozyme SCD2 is ubiquitously expressed in most tissues except adult mouse liver
brenda
additional information
isozyme SCD2 is ubiquitously expressed in most tissues except adult mouse liver
brenda
additional information
isozyme SCD3 is mainly expressed in Harderian gland, preputial gland, and in mature sebocytes of skin
brenda
additional information
isozyme SCD3 is mainly expressed in Harderian gland, preputial gland, and in mature sebocytes of skin
brenda
additional information
isozyme SCD3 is mainly expressed in Harderian gland, preputial gland, and in mature sebocytes of skin
brenda
additional information
isozyme SCD3 is mainly expressed in Harderian gland, preputial gland, and in mature sebocytes of skin
brenda
additional information
the enzyme is highly expressed in lipogenic tissues, such as liver and adipose tissue
brenda
additional information
-
decreased mRNA levels in epididymal fat pads after 2 injections of Scd1 sequence-specific antisense oligodeoxynucleotide over 5 days
brenda
additional information
expression level of stearoyl-CoA desaturase (SCD) and three transcriptional factors in various adipose depots from piglets and adult pigs, the enzyme is significantly upregulated in differentiated porcine adipocytes
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
hSCD1 fused to GFP and expressed in HEK-293 cells
brenda
hSCD5 fused to GFP and expressed in HEK-293 cells
brenda
an integral protein anchored in the endoplasmic reticulum membrane
brenda
isozyme SCD1 has four transmembrane helices (TM1-TM4) arranged in a cone-like shape with TM4 sandwiched between TM1 and TM2. Residues in the membrane-spanning region are largely hydrophobic, with the notable exception of a conserved arginine (Arg249) located on TM4 in the center of the cone
brenda
an integral membrane enzyme
brenda
an integral protein anchored in the endoplasmic reticulum membrane
brenda
SCD1 protein consists of four transmembrane domains with both NH2(N) and C-termini directed to cytosol. It contains 8 histidine (His) residues. They form three His regions, one of which is located in C-terminus and the other two in the cytoplasmatic loop
brenda
-
-
-
685575, 688248, 696680, 696683, 696685, 696684, 697777, 697824, 696702, 696671, 714418, 714406, 767654
brenda
-
from liver, 40% increase in enzyme activity in hepatic microsomes in tristearin-fed compared with trioleate-fed mice
-
brenda
-
-
-
brenda
-
-
-
brenda
additional information
SCD-1 consists of a cytosolic domain containing a di-metal active center and four alpha-helices forming a tight hydrophobic core, which is situated in the endoplasmic reticulum membrane
-
brenda
additional information
-
in L6GLUT4myc myoblasts localized in endoplasmic reticulum-like subcellular structures, laser scanning microscopy
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
isozymes SCD1 and SCD3 share 89% primary sequence identity, but they yield remarkably different total fatty acid profiles in the recombinant yeast host cells, likely reflecting differences in their preferences for reaction with 16:0 and 18:0 substrates
evolution
although SCD5 has been initially thought to be present exclusively in primates, SCD5 orthologues have also been found in a variety of vertebrates, including ruminants, pigs, dogs, and birds. Several phylogenetic analyses of mammalian SCD variants hint at the possibility that a primordial DELTA9-desaturase gene diverged into scd1 and scd5 as independently duplicated genes early in vertebrate evolution. The pattern of gene expression after gene duplication may have resulted in functional specialization of SCD5, which may help explain its distinct expression profile in tissues and organs when compared to SCD1
malfunction
-
alterations in expression reported in several prevalent metabolic diseases, such as diabetes, obesity and atherosclerosis
malfunction
-
stearoyl-CoA desaturase 1 deficiency is coupled with an extreme cold sensitivity and significantly increased skin inflammation
malfunction
-
enzyme inhibition by genetic and chemical tools is detrimental for parasite development. The partial ablation of the enzyme inhibits drastically the parasite growth
malfunction
-
the ablation of enzyme activity has an immediate and profound impact on the fatty acid content of cell lipids. Enzyme inhibition alters the epidermal growth factor-dependent signaling mechanism, decreases the mobility of fluid domains in plasma membranes, and reduces EGF-induced proliferation in lung cancer cells
malfunction
loss of SCD-1 activity induces complex changes in the fatty acid composition of membrane lipids which are not restricted to the MUFA/SFA ratio. SCD-1 deficiency induces insulin signaling in peripheral tissues, namely phosphorylation of insulin receptor and insulin receptor substrates (IRS)1 and 2. Association of IRS isoforms with the regulatory subunit of phosphatidylinositol-3-kinase (PI3K) promotes the synthesis of phosphatidylinositol-3,4,5-trisphoshates (PIP3) as membrane anchor sites for the serine/threonine kinase Akt. SCD-1 inhibition suppressed starvation-induced autophagy in mouse embryonic fibroblasts and palmitate-induced autophagy in rat pancreatic beta-cells apparently by disturbing autophagosome-lysosome fusion
malfunction
chemical SCD1 inhibition in the presence of stearic acid results in a significant induction of apoptosis in cumulus cells of matured cumulus-oocyte complexes. SCD1 inhibition does not affect the levels of palmitic acid and its desaturated form, palmitoleic acid
malfunction
inhibition of SCD1 activity represents a potential novel approach for the treatment of metabolic diseases such as obesity, type 2 diabetes and dyslipidemia, as well as skin diseases, acne and cancer
malfunction
inhibition of SCD1 activity represents a potential novel approach for the treatment of metabolic diseases such as obesity, type 2 diabetes and dyslipidemia, as well as skin diseases, acne and cancer
malfunction
targeting SCD1 synergizes the effect of sorafenib both in vitro and in vivo. The endoplasmic reticulum stress-induced unfolded protein response is upregulated in SCD1-knockdown cells. Suppression of SCD1 forces liver cancer stem cells to differentiate via the induction of endoplasmic reticulum stress, which results in their enhanced sensitivity to sorafenib both in vitro and in vivo. SCD1 knockdown reduces stem/progenitor characteristics of hepatocellular carcinoma cells
malfunction
reduced SCD1 activity in the liver causes endoplasmic reticulum stress that is only normalized by exogenous or endogenous oleate but not palmitoleate. SCD1 deficiency-mediated glucose uptake in skeletal muscle and brown adipose tissue feeds toward glycogen synthesis. Localized and systemic SCD1 deficiency increases glucose uptake in white adipose tissue through apparently different mechanisms involving GLUT1 and GLUT4, respectively
malfunction
reduced SCD1 activity in the liver causes endoplasmic reticulum stress that is only normalized by exogenous or endogenous oleate but not palmitoleate. SCD1 deficiency-mediated glucose uptake in skeletal muscle and brown adipose tissue feeds toward glycogen synthesis. Localized and systemic SCD1 deficiency increases glucose uptake in white adipose tissue through apparently different mechanisms involving GLUT1 and GLUT4, respectively. Liver-specific SCD1 KO mice exhibit different phenotypes compared to skin-specific SCD1 KO mice, suggesting that SCD1 products, monounsaturated fatty acids, carry out different functions in different tissues. Global SCD1 KO mice are protected against high carbohydrate diet and high fat diet-induced adiposity and hepatic steatosis. Liver-specific SCD1 knockout mice fed high-fat diet show a significant reduction of white adipose tissue weights compared with control mice. Hepatic SCD1 deficiency causes a significant reduction in hepatic lipogenic gene expression and reduced de novo lipogenesis associated with reduced hepatic triglyceride secretion. Skin-specific knockout mice show protection against high-fat diet-induced adiposity along with increased energy expenditure expected to be sufficient to counter increased calorie intake associated with feeding high-fat diet. In addition, similar to SCD1 global KO mice, skin-specific KO mice are hyperphagic and maintain lean phenotype accompanied by protection against extended high-fat diet feeding-induced insulin resistance. Skin-specific KO mice exhibit increased cold sensitivity and died within 3 h of cold exposure due to hypoglycemia. SCD1 isozyme-specific knockout phenotypes with respect to the other isozymes, detailed overview
malfunction
dysregulation of stearoyl-CoA desaturase 1 likely contributes to obesity associated metabolic disturbances. Effect of genetic ablation of SCD1 in 3T3-L1 adipocytes on membrane microdomain lipid composition at the species-specific level, overview. 90% reduction in scd1 mRNA expression, caused by siRNA expression, leads to altered cellular lipid composition, SCD1 knockout modifies the acyl chain composition of lipids, as well as the lipid composition per se of membrane microdomains in 3T3-L1 adipocytes.The effects of SCD1 knockout are not limited to alterations in 16:0 and 18:0 fatty acids. Cholesterol content is unchanged although decreases in other lipids result in cholesterol accounting for a higher proportion of lipid in the membranes. This is associated with decreased membrane lateral diffusion. An increased ratio of 24:0 to 24:1 in ceramide, mono- and dihexosylceramide, and sphingomyelin likely also contributes to this decrease in lateral diffusion. Lipidomic profiling is targeted to specific membrane microdomains, overview. A decrease in phospholipids containing arachidonic acid is observed. Given the high degree of structural flexibility of this acyl chain this will influence membrane lateral diffusion, and is likely responsible for the transcriptional activation of Lands' cycle enzymes lpcat3 and mboat7
malfunction
stearoyl-CoA desaturase 1 (SCD-1) inhibition blocks hepatitis C virus replication and formation of hepatitis C virus-induced specialized membranes. Inhibition of stearoyl-CoA desaturase 1 halts the biosynthesis of unsaturated fatty acids, such as oleic acid, and negatively modulates HCV replication. Unsaturated fatty acids play key roles in membrane curvature and fluidity, SCD-1 inhibition disrupts the integrity of membranous HCV replication complexes and renders HCV RNA susceptible to nuclease-mediated degradation
malfunction
reduction of SCD1 activity and mRNA expression impaired the formation of cell membrane lipids with the decrease of fatty acid biosynthesis and desaturation, leading to cease cancer cell proliferation and induction of cell apoptosis. Inhibition of stearoyl-CoA desaturase 1 (SCD1) effectively suppresses tumor cell proliferation and induce apoptosis in numerous neoplastic lesions, SCD1-mediated anti-tumor effect. Endo-lipid messenger ceramides play a critical role in tumor fate modulated by SCD1 inhibition. Inhibition of SCD1 activity promotes apoptosis attributed to mitochondria dysfunctions, upregulation of reaction oxygen species (ROS), alteration of mitochondrial transmembrane potential, and translocation of mitochondrial protein cytochrome C in colorectal cancer cells. These effects are mediated by intracellular ceramide signals through induction of ceramide biosynthesis, rather than exclusive saturated fatty acid accumulation. Inhibitor A939 dramatically increases intracellular long-chain saturated ceramide levels including C18:0 ceramide, C20:0 ceramide, C22:0 ceramide, and C24:0 ceramide, while it slightly increases middle-chain saturated ceramide C16:0 and does not affect monounsaturated C24:1 ceramide
malfunction
loss of SCD-1 activity induces complex changes in the fatty acid scomposition of membrane lipids which are not restricted to the MUFA/SFA ratio. SCD-1 deficiency induces insulin signaling in peripheral tissues, namely phosphorylation of insulin receptor and insulin receptor substrates (IRS)1 and 2. Association of IRS isoforms with the regulatory subunit of phosphatidylinositol-3-kinase (PI3K) promotes the synthesis of phosphatidylinositol-3,4,5-trisphoshates (PIP3) as membrane anchor sites for the serine/threonine kinase Akt
malfunction
-
SCD1 inhibitors (MK8245 and #1716) dramatically suppress DENV replication in a dose-dependent manner without cytotoxicity. This anti-DENV efficacy is observed against all four DENV serotypes and other flaviviruses, including Zika virus and Japanese encephalitis virus. A subgenomic replicon system of DENV is used to confirm that SCD1 inhibitor suppressed viral RNA replication. Exogenous supplementation of unsaturated fatty acids results in recovery of the DENV titer even in the presence of SCD1 inhibitor, suggesting that fatty acid biosynthesis contributes to DENV genome replication
malfunction
-
SCD1 inhibitors (MK8245 and #1716) dramatically suppress DENV replication in a dose-dependent manner without cytotoxicity. This anti-DENV efficacy is observed against all four DENV serotypes and other flaviviruses, including Zika virus and Japanese encephalitis virus. A subgenomic replicon system of DENV is used to confirm that SCD1 inhibitor suppressed viral RNA replication. Exogenous supplementation of unsaturated fatty acids results in recovery of the DENV titer even in the presence of SCD1 inhibitor, suggesting that fatty acid biosynthesis contributes to DENV genome replication
malfunction
inhibition of SCD1 induces lipid oxidation and cell death, while overexpression of SCD or exogenous administration of its C16:1 and C18:1 products, palmitoleic acid or oleate, protects cells from death. Inhibition of SCD1 induces both ferroptosis and apoptosis. Inhibition of SCD1 decreases CoQ10, an endogenous membrane antioxidant whose depletion has been linked to ferroptosis, while concomitantly decreasing unsaturated fatty acyl chains in membrane phospholipids and increasing long-chain saturated ceramides, changes previously linked to apoptosis. Simultaneous triggering of two death pathways suggests SCD1 inhibition may be an effective component of antitumor therapy, because overcoming this dual mechanism of cell death may present a significant barrier to the emergence of drug resistance. Inhibition of SCD1 significantly potentiates the antitumor effect of ferroptosis inducers in both ovarian cancer cell lines and a mouse orthotopic xenograft model
malfunction
SCD1 inhibitors have potential effects on obesity, diabetes, acne, and cancer, but the adverse effects associated with SCD1 inhibition in the skin and eyelids are impediments to clinical development
malfunction
SCD1 inhibitors have potential effects on obesity, diabetes, acne, and cancer, but the adverse effects associated with SCD1 inhibition in the skin and eyelids are impediments to clinical development
malfunction
-
vitamin A deficiency results in the reduction of stearoyl-CoA desaturase 1 (SCD1) and monounsaturated fatty acid (MUFA) levels, which corroborated with attenuation of high fructose-induced hepatic steatosis, with decreased triglyceride accumulation in the liver. Unlike liver, the reduction in SCD1 and MUFA levels in the pancreas exerts deleterious effects on its functions and perturb the overall cellular metabolism
malfunction
when SCD1 is overexpressed in bovine stromal vascular fraction (SVF) cells, lipid droplets accumulation is increased, overexpression of SCD1 accelerates lipid accumulation in bovine SVF cells. Overexpression of SCD1 does not improve the expression of PPARgamma or C/EBPalpha, but it activates the PPARgamma receptor. Overexpression of SCD1 leads to adipocyte hypertrophy
malfunction
-
experimental SCD1 inhibitors induce tumor endoplasmic reticulum stress
malfunction
both Gba deficient (GBAKO) and Dgat2 deficient mice (DGAT2KO) exhibit skin barrier defects and high neonatal lethality similar to the SCD2KO mice. SCD2KO mice have decreased bone mineral density (BMD) and bone mineral content (BMC). In the C57BL/6 genetic background, Scd2 deficiency is 100% embryonic lethal. In the 129/SV genetic background, over 70% of SCD2KO mice die within 24 h of birth. Newborn SCD2KO mice are smaller than wild-type mice, have kinky tails, and their skin appears dry and cracked. The SCD2KO mice that survive to adulthood are fertile, retain their kinky tail phenotype, and remain smaller than wild-type mice. Scd2+/- mice are haplosufficient and resemble wild-type mice phenotypically. In the 129/SV genetic background, deletion of Scd2 creates a defective skin barrier which results in trans-epidermal water loss and ultimately leads to the death of newborn mice. Skin structure analysis shows a decreased number of lamellar bodies forming in the epidermis layer of the SCD2KO mice. Lamellar bodies are secreted by the keratinocytes, the most abundant cell type in the epidermis, to produce a lipid-containing membrane that serves as a water barrier. Scd2 deficiency decreases the contents of lamellar bodies and changes the lipid composition of the epidermis. siRNA mediated knockdown of SCD2 inhibits the transcription of peroxisome proliferator-activated receptor gamma (Pparg), reduces PPARgamma protein levels by 90%, and suppressed adipocyte lipid accumulation. PPARgamma is a nuclear lipogenic transcription factor and master regulator of adipogenesis. Primary preadipocytes from SCD2KO mice fail to differentiate and form lipid droplets compared to those from SCD1KO and wild-type mice. SCDKO phenotype, detailed overview
malfunction
a missense mutation in the scd5 gene is identified in a large family whose members were diagnosed with hearing loss of autosomal dominant inheritance. Although the molecular mechanisms by which SCD5 activity modulates the auditory pathways are unknown, the desaturase may be essential not only for the integrity and functionality of spiral ganglion cells in the cochlea but also for the auditory processes in brain cells, which express high levels of SCD5
malfunction
-
overexpression of RtFAD1 is downregulated in the RtFAD1 and RtFAD2 co-overexpressing strains, suggesting that the elevated linoleic acid content may function as a key regulator of RtFAD1 expression to control C18 fatty-acid synthesis in Rhodotorula toruloides
malfunction
SCD1 inhibition/deficiency causes DNA hypomethylation and changes the methyl group distribution within chromosomes in beta-cells. Lower levels of DNA methylation in SCD1-deficient beta-cells are followed by lower levels of DNA methyltransferase 1 (DNMT1). The downregulation of SCD1 in pancreatic beta-cells leads to the activation of adenosine monophosphate-activated protein kinase (AMPK) and an increase in the activity of the NAD-dependent deacetylase sirtuin-1 (SIRT1). The physical association between DNMT1 and SIRT1 stimulates the deacetylation of DNMT1 under conditions of SCD1 inhibition/downregulation, suggesting a mechanism by which SCD1 exerts control over DNMT1. SCD1-deficient beta-cells that are treated with compound c, an inhibitor of AMPK, are characterized by higher levels of both global DNA methylation and DNMT1 protein expression compared with untreated cells. Activation of the AMPK/SIRT1 signaling pathway mediates the effect of SCD1 inhibition/deficiency on DNA methylation status in pancreatic beta-cells. The level of global DNA (gDNA) methylation in pancreatic islets that were isolated from SCD1-/- mice significantly decreases by 40% compared with wild-type islets. Severity of the SCD1 deficiency-related stress response in insulin-secreting MIN6 cells
malfunction
the loss of SCD leads to dramatically decreased transdifferentiation efficiency, as evidenced by the decreased expression of known lipid synthesis-related genes, lower levels of oil red O staining, and significantly lower levels of triglyceride content. SCD knockout inhibites PEF transdifferentiation into mature adipocytes
malfunction
RNA interference (RNAi) silencing of SCD1 and administration of sterculic acid (SA), a small molecule inhibitor of SCD1, significantly impact on the survival and reproduction of female mosquitoes following blood feeding. The mosquito thorax is quickly filled with blood, a phenomenon likely caused by the collapse of midgut epithelial cell membranes, and epithelial cells are depleted of lipid droplets and oocytes fail to mature. Transcriptional profiling shows that genes involved in protein, lipid and carbohydrate metabolism and immunity-related genes are the most affected by SCD1 knock down (KD) in blood-fed mosquitoes. Metabolic profiling reveals that these mosquitoes exhibit increased amounts of saturated fatty acids and TCA cycle intermediates, highlighting the biochemical framework by which the SCD1 KD phenotype manifests as a result of a detrimental metabolic syndrome
malfunction
the SCD-overexpressing tachyzoites propagate slower than the parental strain, with a decreased invasion capability and weaker pathogenicity in mice. The TgIF2alpha phosphorylation and the expression changes of several genes demonstrate that endoplasmic reticulum stress is triggered in the SCD-overexpressing parasites, which are more apt toward autophagy and apoptosis. Lower mortality rate in SCD overexpressing-infected mice
malfunction
SCD1 inhibitors (MK8245 and #1716) dramatically suppress DENV replication in a dose-dependent manner without cytotoxicity. This anti-DENV efficacy is observed against all four DENV serotypes and other flaviviruses, including Zika virus and Japanese encephalitis virus. A subgenomic replicon system of DENV is used to confirm that SCD1 inhibitor suppressed viral RNA replication. Exogenous supplementation of unsaturated fatty acids results in recovery of the DENV titer even in the presence of SCD1 inhibitor, suggesting that fatty acid biosynthesis contributes to DENV genome replication
malfunction
enzyme-deficient mice show decreased hepatic triacylglycerol content, reduced body adiposity, increased insulin sensitivity, and resistance to diet-induced weight gain. However, liver-specific enzyme-deficient mice are not protected from high-fat diet-induced adiposity and hepatic steatosis, indicating that enzyme inhibition in the extrahepatic tissues is required for protection from high-fat-diet-induced obesity and insulin resistance
malfunction
-
SCD1 inhibitors (MK8245 and #1716) dramatically suppress DENV replication in a dose-dependent manner without cytotoxicity. This anti-DENV efficacy is observed against all four DENV serotypes and other flaviviruses, including Zika virus and Japanese encephalitis virus. A subgenomic replicon system of DENV is used to confirm that SCD1 inhibitor suppressed viral RNA replication. Exogenous supplementation of unsaturated fatty acids results in recovery of the DENV titer even in the presence of SCD1 inhibitor, suggesting that fatty acid biosynthesis contributes to DENV genome replication
malfunction
-
both Gba deficient (GBAKO) and Dgat2 deficient mice (DGAT2KO) exhibit skin barrier defects and high neonatal lethality similar to the SCD2KO mice. SCD2KO mice have decreased bone mineral density (BMD) and bone mineral content (BMC). In the C57BL/6 genetic background, Scd2 deficiency is 100% embryonic lethal. In the 129/SV genetic background, over 70% of SCD2KO mice die within 24 h of birth. Newborn SCD2KO mice are smaller than wild-type mice, have kinky tails, and their skin appears dry and cracked. The SCD2KO mice that survive to adulthood are fertile, retain their kinky tail phenotype, and remain smaller than wild-type mice. Scd2+/- mice are haplosufficient and resemble wild-type mice phenotypically. In the 129/SV genetic background, deletion of Scd2 creates a defective skin barrier which results in trans-epidermal water loss and ultimately leads to the death of newborn mice. Skin structure analysis shows a decreased number of lamellar bodies forming in the epidermis layer of the SCD2KO mice. Lamellar bodies are secreted by the keratinocytes, the most abundant cell type in the epidermis, to produce a lipid-containing membrane that serves as a water barrier. Scd2 deficiency decreases the contents of lamellar bodies and changes the lipid composition of the epidermis. siRNA mediated knockdown of SCD2 inhibits the transcription of peroxisome proliferator-activated receptor gamma (Pparg), reduces PPARgamma protein levels by 90%, and suppressed adipocyte lipid accumulation. PPARgamma is a nuclear lipogenic transcription factor and master regulator of adipogenesis. Primary preadipocytes from SCD2KO mice fail to differentiate and form lipid droplets compared to those from SCD1KO and wild-type mice. SCDKO phenotype, detailed overview
-
malfunction
-
vitamin A deficiency results in the reduction of stearoyl-CoA desaturase 1 (SCD1) and monounsaturated fatty acid (MUFA) levels, which corroborated with attenuation of high fructose-induced hepatic steatosis, with decreased triglyceride accumulation in the liver. Unlike liver, the reduction in SCD1 and MUFA levels in the pancreas exerts deleterious effects on its functions and perturb the overall cellular metabolism
-
malfunction
-
enzyme inhibition by genetic and chemical tools is detrimental for parasite development. The partial ablation of the enzyme inhibits drastically the parasite growth
-
malfunction
-
the SCD-overexpressing tachyzoites propagate slower than the parental strain, with a decreased invasion capability and weaker pathogenicity in mice. The TgIF2alpha phosphorylation and the expression changes of several genes demonstrate that endoplasmic reticulum stress is triggered in the SCD-overexpressing parasites, which are more apt toward autophagy and apoptosis. Lower mortality rate in SCD overexpressing-infected mice
-
malfunction
Rhodotorula toruloides NBRC 8766
-
overexpression of RtFAD1 is downregulated in the RtFAD1 and RtFAD2 co-overexpressing strains, suggesting that the elevated linoleic acid content may function as a key regulator of RtFAD1 expression to control C18 fatty-acid synthesis in Rhodotorula toruloides
-
malfunction
-
overexpression of RtFAD1 is downregulated in the RtFAD1 and RtFAD2 co-overexpressing strains, suggesting that the elevated linoleic acid content may function as a key regulator of RtFAD1 expression to control C18 fatty-acid synthesis in Rhodotorula toruloides
-
metabolism
-
SCD is critical in the biosynthesis of triglycerides, cholesterol esters, wax esters, and 1-alkyl-2,3-diacylglycerol
metabolism
sex-pheromone biosynthesis
metabolism
-
the enzyme is necessary for proper liver, adipose tissue, and skeletal muscle lipid metabolism
metabolism
-
stearoyl-CoA desaturase 1 is the rate-limiting enzyme in the biosynthesis of monounsaturated fatty acids and a risk factor of diabetes
metabolism
survival and stress-activated signaling pathways are regulated by SCD-1, molecular link between SCD-1 activity and cell signaling, overview
metabolism
stearoyl-CoA desaturase-1 (SCD1) plays an important role in lipid metabolism
metabolism
stearoyl-CoA desaturase-1 (SCD1) plays an important role in lipid metabolism
metabolism
isozyme SCD1 has a role in adipogenesis and lipid biosynthesis
metabolism
isozyme SCD1 has a role in adipogenesis and lipid biosynthesis
metabolism
cross-talk of SCD1-mediated lipid pathway and endo-ceramide biosynthesis pathway, indicating roles of ceramide signals in SCD1-mediated anti-tumor property
metabolism
survival and stress-activated signaling pathways are regulated by SCD-1, molecular link between SCD-1 activity and cell signaling, overview
metabolism
pathway of the SCD1-promoting adipogenesis, overview. SREBP1 promotes the transcription of SCD1. SCD1 mainly catalyzes palmitate (C16:0) and stearate (C18:0) into palmitoleate (C16:1) and oleate (C18:1), respectively. Oleate as a strong ligand activated the PPARgamma receptor and then upregulates the downstream target genes (FASN, ACCalpha, and FABP4). Finally, lipid droplets begins to accumulate
metabolism
role of SCD5 in metabolism, and in cell proliferation, differentiation and survival, overview. Isozyme SCD5, similar to isozyme SCD1, may not only determine the MUFA:SFA ratio but also the rate of polar and neutral lipid synthesis in fast-replicating cells. Further supporting a role for SCD5 in lipid regulation, it is observed that in mice with a global SCD1 knockout the liver-specific expression of human SCD5 fully reverses the decreased levels of hepatic triacylglycerol observed in SCD1-ablated animals
metabolism
enzyme SCD plays a role in porcine adipocyte differentiation and fat deposition
physiological function
-
Scd1 null mice are more susceptible to dextran sulfate sodium treatment than wild type mice, while oleic acid feeding and in vivo SCD1 rescue with SCD1 adenovirus alleviates the dextran sulfate sodium-induced phenotype
physiological function
-
SCD-1 knockout mice show reduced body adiposity, increased insulin sensitivity, leanness, increased metabolic rate, and resistance to diet-induced obesity
physiological function
-
mice with a skin-specific deletion of SCD1 (SKO) have significantly increased energy expenditure, are protected from high fat diet-induced obesity, and display marked sebaceous gland hypoplasia and depletion of sebaceous lipids. SKO mice display severe cold intolerance because of rapid depletion of fuel substrates, including hepatic glycogen, to maintain core body temperature. Unlike mice globally deficient in SCD1, SKO mice have an intact hepatic lipogenic response to acute high carbohydrate feeding
physiological function
-
SCD1 knockout mice on the methionine-choline-deficient diet have decreased steatosis and markedly increased hepatocellular apoptosis, liver injury, and fibrosis compared with the SCD-expressing mice
physiological function
-
absence of stearoyl-CoA desaturase-1 leads to chronic inflammation of the skin and increased susceptibility to atherosclerosis, while also increasing plasma inflammatory markers, but does not promote dextran sulfate sodium-induced acute colitis
physiological function
-
mice lacking Scd1 are protected from obesity and insulin resistance and are characterized by decreased fatty acid synthesis and increased fatty acid oxidation
physiological function
-
skin stearoyl-CoA desaturase 1 regulates skin integrity and energy balance
physiological function
-
enzyme expression is important in regulating lipid bilayer fluidity, increasing triglyceride formation, and enabling lipogenesis and may protect against saturated fatty acids-induced lipotoxicity
physiological function
-
the enzyme activity is the most critical determinant of the monounsaturated/saturated fatty acid balance in cancer cells
physiological function
stearoyl-CoA desaturase (SCD), the central enzyme in the biosynthesis of monounsaturated fatty acids, introduces a cis-DELTA9 double bond into saturated fatty acids. SCD-1 induces adaptive stress signaling that maintains cellular persistence and fosters survival and cellular functionality under distinct pathological conditions. Function, regulation, structure and mechanism of SCD-1, molecular mechanisms and potential lipid factors that link SCD-1 activity with initial signal transduction, overview. SCD-1 is the major isoenzyme responsible for monounsaturated fatty acid biosynthesis in most rodent tissues. SCD-1 is critical for cell proliferation, especially in hyperproliferative cells, such as cancer cells. Another mechanism bywhich SCD-1 modulates overall lipid metabolism depends on the negative regulation of the lipogenic transcription factor SREBP-1c, thereby reducing lipid biosynthesis and enhancing beta-oxidation of fatty acids. SCD-1 has a dual function in the regulation of autophagy by either promoting or inhibiting autophagy depending on the experimental settings and stress conditions
physiological function
cumulus cells can desaturate the potentially toxic stearic acid into oleic acid via stearoyl-CoA desaturase (SCD) activity, cumulus cells protect the oocyte against toxicity by saturated fatty acids. Stearoyl-CoA desaturase 1 activity is related with increased lipid storage in cumulus cells. The level of SCD protein expression in cumulus cells does not change when cumulus-oocyte complexes (COCs) are exposed to saturated stearic acid during maturation
physiological function
stearoyl-CoA desaturase regulates liver tumorinitiating cells and resistance to sorafenib, a drug in treatment of hepatocellular carcinoma, via modulation of endoplasmic reticulum stress-induced differentiation, functional roles of SCD1 in regulating liver tumor-initiating cells and sorafenib resistance, SCD1 maintains liver tumor-initiating cells by suppressing differentiation intervening in the differentiation process, overview
physiological function
stearoyl-CoA desaturase (SCD) introduces the first double bond into saturated fatty acyl-CoAs. Since the monounsaturated products of SCD are key precursors of membrane phospholipids, cholesterol esters, and triglycerides, SCD is pivotal in fatty acid metabolism
physiological function
stearoyl-coenzyme A desaturase 1 (SCD1) is a central regulator of fuel metabolism. SCD1 catalyzes the synthesis of monounsaturated fatty acids (MUFAs), mainly oleate and palmitoleate, which are important in controlling weight gain in response to feeding high carbohydrate diets, role of SCD1 isoform in the regulation of lipid and glucose metabolism in metabolic tissues. SCD1 products, oleate and palmitoleate, have different metabolic properties. Palmitoleate reduces hepatic lipogenesis and improves insulin sensitivity, while oleate promotes ectopic fat accumulation and increases glucose intolerance. Hepatic oleate, but not palmitoleate, regulates body weight. Exercise increases SCD1 activity in skeletal muscle, indicating increased fatty acid synthesis, and is proposed to be protective against weight gain
physiological function
stearoyl-coenzyme A desaturase 1 (SCD1) is a central regulator of fuel metabolism. SCD1 catalyzes the synthesis of monounsaturated fatty acids (MUFAs), mainly oleate and palmitoleate, which are important in controlling weight gain in response to feeding high carbohydrate diets, role of SCD1 isoform in the regulation of lipid and glucose metabolism in metabolic tissues. SCD1 products, oleate and palmitoleate, have different metabolic properties. Palmitoleate reduces hepatic lipogenesis and improves insulin sensitivity, while oleate promotes ectopic fat accumulation and increases glucose intolerance. Hepatic oleate, but not palmitoleate, regulates body weight. Exercise increases SCD1 activity in skeletal muscle, indicating increased fatty acid synthesis, and is proposed to be protective against weight gain
physiological function
stearoyl-CoA desaturase-1, SCD1, is an enzyme that desaturates satruated fatty acids (SFA), converting them to monounsaturated fatty acids (MUFAs), leading to the formation of neutral lipid droplets. SCD1 activity protects cells against lipotoxicity-mediated apoptosis in proximal tubular cells. In culture, retrovirus-mediated overexpression of SCD1 or MUFA treatment significantly ameliorates saturated fatty acid-induced apoptosis in proximal tubular epithelial cells by enhancing intracellular lipid droplet formation. Both overexpression of SCD1 and monounsaturated fatty acid treatment reduces SFA-induced apoptosis via reducing endoplasmic reticulum stress in cultured proximal tubular epithelial cells
physiological function
-
both SCD genes from an Antarctic marine copepod encode a functional desaturase that is capable of increasing the amounts of palmitoleic acid and oleic acid in a prokaryotic expression system
physiological function
oleic acid stimulation of motility of human extravillous trophoblast cells is mediated by stearoyl-CoA desaturase-1 activity. SCD1 is a key enzyme involved in oleic acid-induced migration of HTR8/SVneo cells. Regulatory effects of oleic acid and SCD1 on oxidative stress in HTR8/SVneo cells, effects of oleic acid and elaidic acid on proliferation and migration of HTR8/SVneo cell lines, overview
physiological function
stearoyl-CoA desaturase 1 is a lipogenic enzyme important for the regulation of membrane lipid homeostasis. The enzyme catalyses the insertion of a cis double bond in 12-19 carbon saturated fatty acids, thereby converting them to monounsaturated fatty acids. Through this activity, SCD1 helps to regulate the ratio of saturated to monounsaturated acyl chains in membrane lipids influencingmembrane fluidity and functionality, both essential for maintaining cellular integrity. Adaptive homeostatic mechanisms to ensure partial maintenance of the biophysical properties of membranes likely occur at a post-transcriptional level
physiological function
stearoyl-CoA desaturase is a key enzyme in the biosynthesis of oleic acid, role of SCD-1 in the fatty acid biosynthesis pathway, schematic overview. SCD-1 catalyzes the fatty acids desaturation at carbon-9 forming a cis-double bond. The SCD-1 produced products, palmitoleoyl-CoA (C16:1) and oleoyl-CoA (C18:1), are directly incorporated in triglycerides, cholesterol esters, and phospholipids. These lipids are crucial to the formation of cytosolic lipid droplets, luminal lipid domains, and lipid-rich membranes, which are platforms for hepatitis C virus replication and assembly. Analysis of the influence of SCD-1 on the nuclease and detergent resistant properties of viral RNA at replication complexes
physiological function
stearoyl-CoA desaturase-1 (SCD1) catalyzes saturated fatty acids to DELTA-9 monounsaturated fatty acids, e.g. converting palmitic acid (C16:0) to palmitoleic acid (C16:1) or converting stearic acid (C18:0) to oleic acid (C18:1). SCD1 is necessary to stimulate lipid biosynthesis to supply new phospholipids for cell membrane biogenesis in cell cycle process of mitosis
physiological function
stearoyl-CoA desaturase (SCD), the central enzyme in the biosynthesis of monounsaturated fatty acids, introduces a cis-DELTA9 double bond into saturated fatty acids. SCD-1 induces adaptive stress signaling that maintains cellular persistence and fosters survival and cellular functionality under distinct pathological conditions. The enzyme is a key player that links lipid metabolism with adaptive stress signaling and multiple diseases such as metabolic syndrome, skin disorders, cardiovascular disease and cancer. Function, regulation, structure and mechanism of SCD-1, molecular mechanisms and potential lipid factors that link SCD-1 activity with initial signal transduction, overview. SCD-1 is the major isoenzyme responsible for monounsaturated fatty acid biosynthesis in most human tissues. SCD-1 is critical for cell proliferation, especially in hyperproliferative cells, such as cancer cells. Another mechanism bywhich SCD-1 modulates overall lipid metabolism depends on the negative regulation of the lipogenic transcription factor SREBP-1c, thereby reducing lipid biosynthesis and enhancing beta-oxidation of fatty acids. SCD-1 has a dual function in the regulation of autophagy by either promoting or inhibiting autophagy depending on the experimental settings and stress conditions
physiological function
-
stearoyl-CoA desaturase-1 is required for Dengue virus and other flavivirus RNA replication, it is involved in monounsaturated FAS and a key factor that regulates DENV replication efficiency
physiological function
-
stearoyl-CoA desaturase-1 is required for Dengue virus and other flavivirus RNA replication, it is involved in monounsaturated FAS and a key factor that regulates DENV replication efficiency
physiological function
stearoyl-CoA desaturase 1 (SCD1) catalyzes the rate-limiting step in monounsaturated fatty acid synthesis in ovarian cancer cells and protects ovarian cancer cells from ferroptotic cell death. Sterol CoA desaturase (SCD1, SCD) is a lipid-modifying enzyme that is upregulated in numerous malignancies, including prostate, liver, and breast cancers. SCD1 catalyzes the desaturation of saturated fatty acids, principally stearic acid (18:0) and palmitic acid (16:0), to their DELTA9-monounsaturated counterparts, oleic acid (18:1) and palmitoleic acid (16:1)
physiological function
SCD1 is a rate-limiting enzyme in the conversion of saturated fatty acids to monounsaturated fatty acids
physiological function
SCD1 is a rate-limiting enzyme in the conversion of saturated fatty acids to monounsaturated fatty acids
physiological function
-
enzyme stearoyl-CoA desaturase 1 (SCD1) is an endoplasmic reticulum-bound enzyme, involved in the endogenous synthesis of monounsaturated fatty acid (MUFA), palmitoleic (C16:1) and oleic (C18:1) acids from their respective saturated fatty acid (SFA) precursors, palmitic (C16:0) and stearic (C18:0) acids. The ratio of SFA to MUFA is critical for structural integrity and cellular functions, as it determines the membrane fluidity
physiological function
stearoyl-CoA desaturase 1 (SCD1) is a rate-limiting enzyme that mainly catalyzes the saturated fatty acids (SFAs) into the monounsaturated fatty acids (MUFAs). Bovine stearoyl-CoA desaturase 1 promotes adipogenesis by activating the PPARgamma receptor. Functional mechanism of SCD1 in adipogenesis, overview
physiological function
stearoyl-CoA desaturase 1 (SCD1) is a membrane-embedded metalloenzyme that catalyzes formation of a double-bond on a saturated acyl-CoA. It converts saturated acyl-CoAs to monounsaturated acyl-CoAs which are precursors for the biosynthesis of phospholipids, cholesterol esters, and triglycerides. SCD1 is a key regulator in fat metabolism and is required for survival of cancer cells
physiological function
enzyme SCD2 is required for the survival, development, and de novo synthesis of MUFAs in young mice, SCD2 is a critical enzyme in murine development, metabolism, and disease. SCD2 is required to differentiate 3T3-L1 preadipocytes into mature adipocytes in vitro
physiological function
the expression of SCD5 was found elevated in lymphocytes from patients with vasodilator-responsive pulmonary artery hypertension when compared to the non-responsive phenotype, indicating the desaturase may be implicated in the mechanisms of hypertension. The desaturase activity, by providing substrate for protein acylation, has been linked to mechanisms of Wnt activation, putative functional association of SCD5 and Wnt activity in pulmonary artery hypertension. Enzyme SCD5 activity appears to be crucial in the processes of neuronal proliferation and differentiation. SCD5 mRNA expression is elevated in the brain of patients with Alzheimer's disease. Schizophrenia, bipolar disorder, and major depressive disorder, clinical entities that are thought to be genetically connected, display few susceptibility genes located on chromosome 4, including scd5. Role of SCD5 in craniofacial formation. Regulation of SCD5, overview
physiological function
-
the RtFAD1 expression levels may be regulated by the linoleic acid (LA) content and lead to the suppression of LA production in Rhodotorula toruloides
physiological function
stearoyl-CoA desaturase (SCD) generates monounsaturated fatty acids (MUFAs) which contribute to cell growth, survival, differentiation, metabolic regulation and signal transduction. Overexpression of SCD is evident and implicated in metabolic diseases such as diabetes and non-alcoholic fatty liver disease. SCD also stimulates canonical Wnt pathway and YAP activation in support of stemness and tumorigenesis. SCD facilitates metabolic reprogramming in cancer which is mediated, at least in part, by regulation of AKT, AMPK, and NF-kappaB via MUFAs. Mechanisms of SCD-mediated tumor promotion, detailed overview
physiological function
stearoyl-CoA desaturase 1 (SCD1) is a rate-limiting enzyme that is involved in monounsaturated fatty acid synthesis, which protects pancreatic beta-cells against lipotoxicity. Stearoyl-CoA desaturase 1 activity determines the maintenance of DNMT1-mediated DNA methylation patterns in pancreatic beta-cells. Metabolic stress, such as lipotoxicity, affects the DNA methylation profile in pancreatic beta -cells and thus contributes to beta-cell failure and the progression of type 2 diabetes (T2D). SCD1 is a gatekeeper that protects beta-cells against the lipid-derived loss of DNA methylation and provide mechanistic insights into the mechanism by which SCD1 regulates DNA methylation patterns in beta-cells and T2D-relevant tissues
physiological function
stearoyl-CoA desaturase (SCD) is a well recognized rate-limiting enzyme in the biogenesis of endogenous monounsaturated fatty acids (MUFAs), mainly oleate and palmitoleate. Stearoyl-CoA desaturase is essential for porcine adipocyte differentiation and a key enzyme that catalyzes the conversion of saturated fatty acids into monounsaturated fatty acids, and it is associated with fatty acid composition in pigs. Bama native Chinese pig breed have a high capacity for fat deposition and show increased SCD expression levels
physiological function
Anopheles coluzzii stearoyl-CoA desaturase is essential for adult female survival and reproduction upon blood feeding. Vitellogenesis and oocyte maturation require anautogenous female Anopheles mosquitoes to obtain a bloodmeal from a vertebrate host. The bloodmeal is rich in proteins that are readily broken down into amino acids in the midgut lumen and absorbed by the midgut epithelial cells where they are converted into lipids and then transported to other tissues including ovaries. The stearoyl-CoA desaturase (SCD) plays a pivotal role in this process by converting saturated (SFAs) to unsaturated (UFAs) fatty acids, the latter being essential for maintaining cell membrane fluidity amongst other housekeeping functions. Stearoyl-CoA desaturase is a rate limiting key enzyme regulating the ratio of saturated to unsaturated fatty acids (SFAs to UFAs) that is essential in the maintenance of cell membrane fluidity, proliferation, lipid accumulation and signaling
physiological function
SCD might be involved in tachyzoite autophagy and apoptosis. TgSCD might also be involved in the further modification of fatty acids in both the endoplasmic reticulum and apicoplast
physiological function
stearoyl-CoA desaturase-1 is required for Dengue virus and other flavivirus RNA replication, it is involved in monounsaturated FAS and a key factor that regulates DENV replication efficiency
physiological function
the enzyme is dispensable for tachyzoite growth and proliferation and is involved in tachyzoite autophagy and apoptosis
physiological function
-
elevated enzyme activity is associated with increased iron storage inside the human body
physiological function
the enzyme plays a pivotal role in hepatic lipogenesis
physiological function
-
stearoyl-CoA desaturase-1 is required for Dengue virus and other flavivirus RNA replication, it is involved in monounsaturated FAS and a key factor that regulates DENV replication efficiency
physiological function
-
enzyme SCD2 is required for the survival, development, and de novo synthesis of MUFAs in young mice, SCD2 is a critical enzyme in murine development, metabolism, and disease. SCD2 is required to differentiate 3T3-L1 preadipocytes into mature adipocytes in vitro
-
physiological function
-
enzyme stearoyl-CoA desaturase 1 (SCD1) is an endoplasmic reticulum-bound enzyme, involved in the endogenous synthesis of monounsaturated fatty acid (MUFA), palmitoleic (C16:1) and oleic (C18:1) acids from their respective saturated fatty acid (SFA) precursors, palmitic (C16:0) and stearic (C18:0) acids. The ratio of SFA to MUFA is critical for structural integrity and cellular functions, as it determines the membrane fluidity
-
physiological function
-
the enzyme is dispensable for tachyzoite growth and proliferation and is involved in tachyzoite autophagy and apoptosis
-
physiological function
-
SCD might be involved in tachyzoite autophagy and apoptosis. TgSCD might also be involved in the further modification of fatty acids in both the endoplasmic reticulum and apicoplast
-
physiological function
Rhodotorula toruloides NBRC 8766
-
the RtFAD1 expression levels may be regulated by the linoleic acid (LA) content and lead to the suppression of LA production in Rhodotorula toruloides
-
physiological function
-
the RtFAD1 expression levels may be regulated by the linoleic acid (LA) content and lead to the suppression of LA production in Rhodotorula toruloides
-
additional information
structure-function analysis and catalytic mechanism of SCD-1, overview. SCD-1 consists of a cytosolic domain containing a di-metal active center and four alpha-helices forming a tight hydrophobic core, which is situated in the endoplasmic reticulum membrane. Acyl-CoA substrates bind to the surface of the cytoplasmic domain by forming multiple hydrogen bonds via the adenosine group, the panthothenate group and the carbonyl-group of the fatty acid. The substrate is fixed by ionic interactions between the phosphates of CoA and a positively charged surface of the enzyme and by a cation-Pi-interaction between adenosine and Lys194. The acyl-chain enters a hydrophobic tunnel extending to the interface of the cytoplasmic and transmembrane domain. The substrate tunnel has a kink, which is considered to hold the substrate and thereby determining regiospecificity of the enzyme and cis-conformation of the product. The catalytic center for dehydrogenation is located adjacent to the kink in the hydrophobic tunnel and adjacent to carbons 9 and 10 of stearoyl-CoA
additional information
the structure of isozyme SCD1 shows a fold comprising four transmembrane helices capped by a cytosolic domain, and a plausible pathway for lateral substrate access and product egress. The acyl chain of the bound stearoyl-CoA is enclosed in a tunnel buried in the cytosolic domain, and the geometry of the tunnel and configuration of the bound acyl chain provide a structural basis for the regioselectivity and stereospecificity of the desaturation reaction. The dimetal center is coordinated by a unique configuration of nine conserved histidine residues that implies a potentially distinct metal center and mechanism for oxygen activation, isozyme SCD1 structure analysis and modelling, overview. In SCD1, Ala108, Leu109, Ala288 and Val289 line the distal end of the substrate binding channel, Ala115 is near the position of double bond formation, while Gln277 and Ser278 are on the cytoplasmic surface opposite to the CoA binding site. Structural role of Arg249
additional information
the structure of isozyme SCD1 shows a fold comprising four transmembrane helices capped by a cytosolic domain, and a plausible pathway for lateral substrate access and product egress. The acyl chain of the bound stearoyl-CoA is enclosed in a tunnel buried in the cytosolic domain, and the geometry of the tunnel and configuration of the bound acyl chain provide a structural basis for the regioselectivity and stereospecificity of the desaturation reaction. The dimetal center is coordinated by a unique configuration of nine conserved histidine residues that implies a potentially distinct metal center and mechanism for oxygen activation, isozyme SCD1 structure analysis and modelling, overview. In SCD1, Ala108, Leu109, Ala288 and Val289 line the distal end of the substrate binding channel, Ala115 is near the position of double bond formation, while Gln277 and Ser278 are on the cytoplasmic surface opposite to the CoA binding site. Structural role of Arg249
additional information
-
the structure of isozyme SCD1 shows a fold comprising four transmembrane helices capped by a cytosolic domain, and a plausible pathway for lateral substrate access and product egress. The acyl chain of the bound stearoyl-CoA is enclosed in a tunnel buried in the cytosolic domain, and the geometry of the tunnel and configuration of the bound acyl chain provide a structural basis for the regioselectivity and stereospecificity of the desaturation reaction. The dimetal center is coordinated by a unique configuration of nine conserved histidine residues that implies a potentially distinct metal center and mechanism for oxygen activation, isozyme SCD1 structure analysis and modelling, overview. In SCD1, Ala108, Leu109, Ala288 and Val289 line the distal end of the substrate binding channel, Ala115 is near the position of double bond formation, while Gln277 and Ser278 are on the cytoplasmic surface opposite to the CoA binding site. Structural role of Arg249
additional information
in SCD3, Ile112, Glu113, Ser292 and Met293 line the distal end of the substrate binding channel, Val119 is near the position of double bond formation, while Asp281 and Pro282 are on the cytoplasmic surface opposite to the CoA binding site
additional information
in SCD3, Ile112, Glu113, Ser292 and Met293 line the distal end of the substrate binding channel, Val119 is near the position of double bond formation, while Asp281 and Pro282 are on the cytoplasmic surface opposite to the CoA binding site
additional information
-
in SCD3, Ile112, Glu113, Ser292 and Met293 line the distal end of the substrate binding channel, Val119 is near the position of double bond formation, while Asp281 and Pro282 are on the cytoplasmic surface opposite to the CoA binding site
additional information
stearoyl-CoA desaturase-1 (SCD1) expression level significantly decreases in the kidneys of high-fat diet (HFD)-induced diabetic mice, compared with non-diabetic mice
additional information
-
a second transmembrane domain integrated in the membrane seems to be critical for desaturase activity
additional information
lipid and ceramide content analysis in untreated and inhibitor-treated ARPE-19 cells, overview
additional information
structure-function analysis and catalytic mechanism of SCD-1, overview. SCD-1 consists of a cytosolic domain containing a di-metal active center and four alpha-helices forming a tight hydrophobic core, which is situated in the endoplasmic reticulum membrane. Acyl-CoA substrates bind to the surface of the cytoplasmic domain by forming multiple hydrogen bonds via the adenosine group, the panthothenate group and the carbonyl-group of the fatty acid. The substrate is fixed by ionic interactions between the phosphates of CoA and a positively charged surface of the enzyme and by a cation-Pi-interaction between adenosine and Lys194. The acyl-chain enters a hydrophobic tunnel extending to the interface of the cytoplasmic and transmembrane domain. The substrate tunnel has a kink, which is considered to hold the substrate and thereby determining regiospecificity of the enzyme and cis-conformation of the product. The catalytic center for dehydrogenation is located adjacent to the kink in the hydrophobic tunnel and adjacent to carbons 9 and 10 of stearoyl-CoA. Active site structure
additional information
-
SCD1 protein consists of four transmembrane domains with both NH2(N) and C-termini directed to cytosol. It contains 8 histidine (His) residues. They form three His regions, one of which is located in C-terminus and the other two in the cytoplasmatic loop. These regions collectively configure a His box, which serves to form a prosthetic group by binding nonheme iron as the catalytic center of SCD1
additional information
SCD1 protein consists of four transmembrane domains with both NH2(N) and C-termini directed to cytosol. It contains 8 histidine (His) residues. They form three His regions, one of which is located in C-terminus and the other two in the cytoplasmatic loop. These regions collectively configure a His box, which serves to form a prosthetic group by binding nonheme iron as the catalytic center of SCD1
additional information
-
the enzyme possesses a typicalx02DELTA9-desaturase domain
additional information
the enzyme possesses a typicalx02DELTA9-desaturase domain
additional information
-
the enzyme possesses a typicalx02DELTA9-desaturase domain
-
Show AA Sequence and Transmembrane Helices (3938 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
40000
41000
53000
58000
additional information
-
SCD protein undetectable in 24 microg/day leptin-treated ob/ob mice with or without exogenous insulin treatment
41000
-
Myc or HA epitope tagged proteins expressed in HeLa cells, immunoblot using anti-Myc and ant-HA antibodies
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
the gene encodes a 355 amino acid-long protein with a single transmembrane domain and a putative acyl-CoA desaturase domain (IPR015876, 68-309 aa)
additional information
-
SCD1 protein is a short-lived protein with a half-life of 2-4 hours and is stabilized by the PPAR agonist clofibric acid. Human SCD1 may gain the stability by forming dimers and oligomers
additional information
SCD1 protein is a short-lived protein with a half-life of 2-4 hours and is stabilized by the PPAR agonist clofibric acid. Human SCD1 may gain the stability by forming dimers and oligomers
additional information
-
human SCD5 may gain the stability by forming dimers and oligomers
additional information
human SCD5 may gain the stability by forming dimers and oligomers
additional information
-
N and C termini are oriented toward the cytosol, loop between the first and second transmembrane domain is oriented toward the ER lumen, the loop between the second and third transmembrane domain is oriented toward the cytosol, the loop between the third and fourth transmembrane domain is oriented toward the ER lumen, indirect immunofluorescence of transiently transfected HeLa cells
additional information
isozyme SCD1 has four transmembrane helices (TM1-TM4) arranged in a cone-like shape with TM4 sandwiched between TM1 and TM2, the N- and C-termini are on the cytosolic side of the membrane. On the cytosolic side, TM2 and TM4 protrude three helical turns out of the membrane and provide some of the coordinating residues for the dimetal active site. The cytosolic domain comprises 93 residues between TM2 and TM3 (C1) and the 90-residue C-terminus (C2). The C1 and C2 domains contain six and five alpha-helices, respectively. Three of the alpha-helices (AH1 on C1 and AH7 and AH9 on C2) are amphipathic and likely provide interactions between the cytosolic domain and the lipid bilayer. Structure analysis and modelling, overview. Structural role of Arg249. Structure of the SCD1 cytoplasmic domain, model
additional information
isozyme SCD1 has four transmembrane helices (TM1-TM4) arranged in a cone-like shape with TM4 sandwiched between TM1 and TM2, the N- and C-termini are on the cytosolic side of the membrane. On the cytosolic side, TM2 and TM4 protrude three helical turns out of the membrane and provide some of the coordinating residues for the dimetal active site. The cytosolic domain comprises 93 residues between TM2 and TM3 (C1) and the 90-residue C-terminus (C2). The C1 and C2 domains contain six and five alpha-helices, respectively. Three of the alpha-helices (AH1 on C1 and AH7 and AH9 on C2) are amphipathic and likely provide interactions between the cytosolic domain and the lipid bilayer. Structure analysis and modelling, overview. Structural role of Arg249. Structure of the SCD1 cytoplasmic domain, model
additional information
-
isozyme SCD1 has four transmembrane helices (TM1-TM4) arranged in a cone-like shape with TM4 sandwiched between TM1 and TM2, the N- and C-termini are on the cytosolic side of the membrane. On the cytosolic side, TM2 and TM4 protrude three helical turns out of the membrane and provide some of the coordinating residues for the dimetal active site. The cytosolic domain comprises 93 residues between TM2 and TM3 (C1) and the 90-residue C-terminus (C2). The C1 and C2 domains contain six and five alpha-helices, respectively. Three of the alpha-helices (AH1 on C1 and AH7 and AH9 on C2) are amphipathic and likely provide interactions between the cytosolic domain and the lipid bilayer. Structure analysis and modelling, overview. Structural role of Arg249. Structure of the SCD1 cytoplasmic domain, model
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospholipoprotein
additional information
phospholipoprotein
-
tightly bound phospholipid is removed during purification
phospholipoprotein
-
tightly bound phospholipid is removed during purification
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with its substrate stearoyl-CoA, X-ray diffraction structure determination and analysis at 3.25 A resolution. The two iron cations are replaced by zinc cations in the crystal structure
purified DELTA223 N-terminally truncated recombinant isozyme SCD1 bound to stearoyl-CoA and two ions of Zn2+ instead of Fe2+, X-ray diffraction structure determination and analysis at 2.6 A resolution, single-wavelength anomalous dispersion
purified free enzyme, X-ray diffraction structure determination and analysis at 2.6 A resolution. The two iron cations are replaced by zinc cations in the crystal structure
purified recombinant enzyme with native diiron center and bound oleoyl-CoA, 30-50 mg/ml protein solution is mixed with crystallization solution containing 100 mM Tris, pH 7.8-8.2, 37-42% PEG 400, 20 mM Mg(Ace)2, and 50 mM MgCl2, method optimization to consistently produce iron-containing SCD1, overview. X-ray diffraction structure determination and analysis at 3.5 A resolution, molecular replacement using the previous SCD1 structure as a search model, modeling
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C222S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C233S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C322S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C92S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C92S/C97S/C222S/C322S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity 5fold increased compared with cells transfected with the empty vector, clear ER pattern
C97S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
I112A/E113L
site-directed mutagenesis, the mutation is able to convert isozyme SCD3 from exclusively a 16:0 desaturase into a predominantly 18:0 desaturase
V119A/D281Q/P282S E113L
site-directed mutagenesis, the mutation of the residues which are located away from the end of the substrate tunnel, causes no change in the reaction specificity of isozyme SCD3
Y104G
the mutant enzyme acquires the ability to desaturate 24C and 26C acyl-CoAs while maintaining its DELTA9-regioselectivity
additional information
additional information
siRNA mediated enzyme silencing and knockout in malaria mosquitos, phenotype and metabolomic profile of SCD1 KD mosquitoes, overview. SCD1 silencing affects midgut epithelial integrity and egg development, blockage of SCD1-catalyzed MUFA synthesis appears to inhibit TAG and phospholipid biosynthesis from bloodmeal-derived carbon in the midgut cells. SCD1 KD phenotype manifests as a result of a detrimental metabolic syndrome, overview. Analysis of the subcellular basis of the SCD1 knockdown phenotype using transmission electron microscopy (TEM) on midgut tissues. Ovaries are a major target tissue of Lp-carried lipids synthesized in the midgut from bloodmeal-derived carbon. SCD1 KD mosquitoes show no signs of egg maturation following a bloodmeal. SCD1 KD triggers a robust immune response
additional information
-
fusion protein of enzyme isoform ADS1 or ADS2 with plastid targeting sequence of palmitic acid DELTA7 desaturase targets enzymes to plastid and shifts regiospecificity of enzymes from DELTA9 desaturase to DELTA7 desaturase
additional information
overexpression of SCD1 increases the expression levels of FABP4, FASN, and ACCalpha, while the expression of PPARgamma or C/EBPalpha is not changed at mRNA or protein level. Dual-luciferase reporter assay shows that the activity of the PPARgamma receptor is enhanced by 3.69 times. When SCD1 is overexpressed in bovine stromal vascular fraction (SVF) cells, lipid droplets accumulation is increased
additional information
near complete transfer of the in vitro expressed enzyme integral membrane protein into the liposomes, followed by single step purification via centrifugation in a density gradient yielded proteoliposomes with the desaturase in high purity as judged by capillary electrophoresis, overview
additional information
-
near complete transfer of the in vitro expressed enzyme integral membrane protein into the liposomes, followed by single step purification via centrifugation in a density gradient yielded proteoliposomes with the desaturase in high purity as judged by capillary electrophoresis, overview
additional information
inhibition of SCD1 modulates lipid content of ovarian cancer cells. A blockade of SCD1 enhances sensitivity to ferroptosis inducers both in a genetic model of ovarian cancer stem cells and in ovarian cancer cell lines. Sensitization to ferroptosis inducers is observed both in vitro and in vivo
additional information
in mice with a global SCD1 knockout the liver-specific expression of human SCD5 fully reverses the decreased levels of hepatic triacylglycerol observed in SCD1-ablated animals
additional information
-
Myc epitope at the C terminus and additional HA epitope at predicted loops, after amino acid 93, 138 or 241
additional information
-
activities of enzymes with HA epitope tagged to the N terminus and Myc epitope tagged to the C terminus expressed in HeLa cells are 23fold and 39fold higher than in cells transfected with an empty vector, acitivities of enzymes with HA epitope after amino acid 93 and 138 additionally Myc epitope tagged to the C terminus are 5.5fold and 5.9fold higher than in cells transfected with an empty vector, respectively
additional information
-
no activity when HA epitope is inserted after amino acid 241
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
-
silencing of SCD1 does not downregulate 3T3-L1 cell differentiation or gene expression, inhibition of adipogenesis caused by SCD2 depletion is associated with a decrease in peroxisome proliferator-activated receptor alpha mRNA and protein, whereas in mature adipocytes loss of SCD2 diminishes PPARalpha protein levels, with little change in mRNA levels and protein translation levels
additional information
-
SCD1 knockout mice show reduced levels of fatty acid transport proteins and lipid content on the heart, as well as decreased fatty acid beta-oxidation and a downregulated peroxisome proliferator-activated receptor-alpha, PPARalpha, pathway, the signalling pathways involved in glucose transport are affected, phenotype, overview
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
siRNA-mediated downregulation of stearoyl-coenzyme A desaturase-1 (SCD1) in diabetic proximal tubular epithelial cells
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
additional information
scd1 gene silencing by siRNA resulting in 90% reduction in scd1 mRNA expression, ceramide spectrum in the mutant, membrane microdomain lipid and acyl chain composition are altered in SCD1 knockdown mutant cells, phenotype, overview. Short range lateral diffusion, using 1-pyrenedecanoic acid, is highly reduced in mutant cell membranes. SCD1 knockout activates the expression of enzymes involved in the remodelling of phospholipids
additional information
assemblance of the entire electron transport chain using the purified soluble domains of cyt b5 and b5R, and the purified mouse SCD1 and the three proteins coordinate to produce proper products. These results establish an in vitro system that allows precise perturbations of the electron transport chain for the understanding of the catalytic mechanism in SCD1
additional information
generation of SCD2 knockout 3T3-L1 cells, and Scd2 deficient mice (SCD2KO) in both the C57BL/6 and 129/SV genetic backgrounds. In the C57BL/6 genetic background, Scd2 deficiency is 100% embryonic lethal. In the 129/SV genetic background, over 70% of SCD2KO mice die within 24 h of birth. Moreover, newborn SCD2KO mice are smaller than wild-type mice, have kinky tails, and their skin appears dry and cracked. The SCD2KO mice that survive to adulthood are fertile, retain their kinky tail phenotype, and remain smaller than wild-type mice. Scd2+/- mice are haplosufficient and resemble wild-type mice phenotypically. In the 129/SV genetic background, deletion of Scd2 creates a defective skin barrier which results in trans-epidermal water loss and ultimately leads to the death of newborn mice. Skin structure analysis shows a decreased number of lamellar bodies forming in the epidermis layer of the SCD2KO mice. Lamellar bodies are secreted by the keratinocytes, the most abundant cell type in the epidermis, to produce a lipid-containing membrane that serves as a water barrier. Scd2 deficiency decreases the contents of lamellar bodies and changes the lipid composition of the epidermis. The epidermis of SCD2KO mice displays significantly decreased MUFAs in the triglyceride (TG), cholesterol ester (CE), acylceramide (AC), phospholipid (PL), and free fatty acid (FFA) fractions. Linoleic acid (18:2n6) ACs are the major lipid species involved in protecting the epidermis from permeability. Although the total epidermal linoleic acid content is similar between SCD2KO and wild-type mice, Scd2 deficiency decreases the amount of linoleic acid (18:2n6) in the epidermal AC fraction, which is consistent with a defective skin barrier. In SCD2KO mice, linoleic acid from ACs is repartitioned to PLs to compensate for decreased MUFAs and to maintain proper membrane fluidity and cell structure
additional information
enzyme downregulation by 90% in INS-1E cells via siRNA transfection. Both SCD1 inhibition and the genetic ablation of SCD1 by siRNA decrease gDNA methylation levels by about 40% compared with control cells. The distribution of proteins and DNA within the chromosomes is similar in the SCD1 inhibitor-treated and control samples, but the inhibition of SCD1 activity in INS-1E cells affects the spatial spreading and location of -CH3 groups over an area of chromosome 1. SCD1 inhibition/downregulation is related to an increase in the deacetylation of DNMT1 by SIRT1. In INS-1E cells that are treated with the SCD1 inhibitor, H4K16 acetylation levels decrease by over 40%, whereas the downregulation of SCD1 gene expression decreases H4K16 acetylation levels by nearly 60%. Treatment with palmitate itself reduces the level of H4K16 acetylation by approximately 40%. Similar to SIRT1 protein levels, no significant difference in the level of H4K16 acetylation is observed between INS-1E cells that are treated with the SCD1 inhibitor or siRNA against SCD1 and SCD1-deficient INS-1E cells subjected to palmitate treatment. DNMT1 undergoes hypoacetylation in SCD1-inhibited INS-1E cells. The inhibition of AMPK substantially increases DNMT1 protein levels in INS-1E cells that are incubated with palmitate and the SCD1 inhibitor or the siRNA against SCD1
additional information
-
generation of SCD2 knockout 3T3-L1 cells, and Scd2 deficient mice (SCD2KO) in both the C57BL/6 and 129/SV genetic backgrounds. In the C57BL/6 genetic background, Scd2 deficiency is 100% embryonic lethal. In the 129/SV genetic background, over 70% of SCD2KO mice die within 24 h of birth. Moreover, newborn SCD2KO mice are smaller than wild-type mice, have kinky tails, and their skin appears dry and cracked. The SCD2KO mice that survive to adulthood are fertile, retain their kinky tail phenotype, and remain smaller than wild-type mice. Scd2+/- mice are haplosufficient and resemble wild-type mice phenotypically. In the 129/SV genetic background, deletion of Scd2 creates a defective skin barrier which results in trans-epidermal water loss and ultimately leads to the death of newborn mice. Skin structure analysis shows a decreased number of lamellar bodies forming in the epidermis layer of the SCD2KO mice. Lamellar bodies are secreted by the keratinocytes, the most abundant cell type in the epidermis, to produce a lipid-containing membrane that serves as a water barrier. Scd2 deficiency decreases the contents of lamellar bodies and changes the lipid composition of the epidermis. The epidermis of SCD2KO mice displays significantly decreased MUFAs in the triglyceride (TG), cholesterol ester (CE), acylceramide (AC), phospholipid (PL), and free fatty acid (FFA) fractions. Linoleic acid (18:2n6) ACs are the major lipid species involved in protecting the epidermis from permeability. Although the total epidermal linoleic acid content is similar between SCD2KO and wild-type mice, Scd2 deficiency decreases the amount of linoleic acid (18:2n6) in the epidermal AC fraction, which is consistent with a defective skin barrier. In SCD2KO mice, linoleic acid from ACs is repartitioned to PLs to compensate for decreased MUFAs and to maintain proper membrane fluidity and cell structure
-
additional information
-
stability and activity of several GFP-fusion mutant enzymes variants, resistance os sensitivity to mycobacterial proteases, overview
additional information
-
stability and activity of several GFP-fusion mutant enzymes variants, resistance os sensitivity to mycobacterial proteases, overview
-
additional information
-
yeast expression strain carries a mutation in the stearoyl-CoA desaturase gene
additional information
-
overexpression of RtFAD1 is downregulated in the RtFAD1 and RtFAD2 co-overexpressing strains, suggesting that the elevated linoleic acid content may function as a key regulator of RtFAD1 expression to control C18 fatty-acid synthesis in Rhodotorula toruloides. RtFAD2 (EC 1.14.19.6) gene expression and coexpression of RtFAD2 and RtFAD1 genes increase the lipid production significantly in Rhodotorula toruloides strains, overview. Although cooverexpression of the RtFAD1 and RtFAD2 in TK16 and L1-1 cell lines yield higher linoleic acid percentages compared to wild-type, the LA contents are slightly decreased in comparison to the RtFAD2-overexpressing strains. The expression levels of RtFAD1 are drastically decreased in the RtFAD1 and RtFAD2 co-overexpressing strains in TK16 and L1-1. Overexpression of the RtFAD2 achieves a higher level of lipid production in Rhodotorula toruloides than overexpression of RtFAD1. Fatty acid composition in total lipid in the transformants and wild-type strains, overview
additional information
Rhodotorula toruloides NBRC 8766
-
overexpression of RtFAD1 is downregulated in the RtFAD1 and RtFAD2 co-overexpressing strains, suggesting that the elevated linoleic acid content may function as a key regulator of RtFAD1 expression to control C18 fatty-acid synthesis in Rhodotorula toruloides. RtFAD2 (EC 1.14.19.6) gene expression and coexpression of RtFAD2 and RtFAD1 genes increase the lipid production significantly in Rhodotorula toruloides strains, overview. Although cooverexpression of the RtFAD1 and RtFAD2 in TK16 and L1-1 cell lines yield higher linoleic acid percentages compared to wild-type, the LA contents are slightly decreased in comparison to the RtFAD2-overexpressing strains. The expression levels of RtFAD1 are drastically decreased in the RtFAD1 and RtFAD2 co-overexpressing strains in TK16 and L1-1. Overexpression of the RtFAD2 achieves a higher level of lipid production in Rhodotorula toruloides than overexpression of RtFAD1. Fatty acid composition in total lipid in the transformants and wild-type strains, overview
-
additional information
-
overexpression of RtFAD1 is downregulated in the RtFAD1 and RtFAD2 co-overexpressing strains, suggesting that the elevated linoleic acid content may function as a key regulator of RtFAD1 expression to control C18 fatty-acid synthesis in Rhodotorula toruloides. RtFAD2 (EC 1.14.19.6) gene expression and coexpression of RtFAD2 and RtFAD1 genes increase the lipid production significantly in Rhodotorula toruloides strains, overview. Although cooverexpression of the RtFAD1 and RtFAD2 in TK16 and L1-1 cell lines yield higher linoleic acid percentages compared to wild-type, the LA contents are slightly decreased in comparison to the RtFAD2-overexpressing strains. The expression levels of RtFAD1 are drastically decreased in the RtFAD1 and RtFAD2 co-overexpressing strains in TK16 and L1-1. Overexpression of the RtFAD2 achieves a higher level of lipid production in Rhodotorula toruloides than overexpression of RtFAD1. Fatty acid composition in total lipid in the transformants and wild-type strains, overview
-
additional information
generation of SCD-KO porcine embryonic fibroblasts (PEFs) using the CRISPR/Cas9 method, generation of SCD-/- porcine embryo fibroblasts, enzyme expression analysis in 7-weeks-old and in 4-months-old piglets in comparison to SCD knockout piglets, overview
additional information
-
based on CRISPR/Cas9 gene editing technology, SCD conditional knockout mutants in the Toxoplasma gondii TATi strain are obtained. The growth in vitro and pathogenicity in mice of the mutants suggests that SCD might be dispensable for tachyzoite growth and proliferation. The SCD-overexpressing line is constructed to further explore SCD function. The portions of palmitoleic acid and oleic acid are increased in SCD overexpressing parasites, compared to the RH parental strain. Deletion of SCD in tachyzoites does not affect the phenotype in vitro and in vivo
additional information
based on CRISPR/Cas9 gene editing technology, SCD conditional knockout mutants in the Toxoplasma gondii TATi strain are obtained. The growth in vitro and pathogenicity in mice of the mutants suggests that SCD might be dispensable for tachyzoite growth and proliferation. The SCD-overexpressing line is constructed to further explore SCD function. The portions of palmitoleic acid and oleic acid are increased in SCD overexpressing parasites, compared to the RH parental strain. Deletion of SCD in tachyzoites does not affect the phenotype in vitro and in vivo
additional information
-
based on CRISPR/Cas9 gene editing technology, SCD conditional knockout mutants in the Toxoplasma gondii TATi strain are obtained. The growth in vitro and pathogenicity in mice of the mutants suggests that SCD might be dispensable for tachyzoite growth and proliferation. The SCD-overexpressing line is constructed to further explore SCD function. The portions of palmitoleic acid and oleic acid are increased in SCD overexpressing parasites, compared to the RH parental strain. Deletion of SCD in tachyzoites does not affect the phenotype in vitro and in vivo
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
30 min in distilled water or 0.1 M phosphate buffer, pH 7.2 causes in almost complete loss of activity
additional information
additional information
-
50% loss of activity after repeated freezing and thawing
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SCD1 protein is a short-lived protein with a half-life of 2-4 hours and is stabilized by the PPAR agonist clofibric acid
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, sedimented enzyme, 0.25 M sucrose, 2 weeks, without significant loss of activity
-
-30°C, freeze-dried microsomal preparation, 12 months stable, activity is retained
-
-60°C, 0.12 M sodium phosphate buffer, pH 8.0, 0.5% Triton X-100, stable for several months
-
4°C, 1 mM or 10 mM potassium phosphate buffer, pH 7.2, 24 hours, activity irreversibly lost
-
4°C, microsomes, 24 hours, inhibition of desaturase by the cytosolic fraction rather than stimulation
-
enzyme cannot be stored overnight without loss of 20-50% of activity before fraction 5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, gel filtration, ultra filtration, ion-exchange
-
near complete transfer of the in vitro expressed enzyme integral membrane protein into the liposomes, followed by single step purification via centrifugation in a density gradient yielded proteoliposomes with the desaturase in high purity as judged by capillary electrophoresis, method optimization of cell-free translation to the assembly and purification of integral membrane protein complexes, overview
recombinant isozyme SCD1 from Saccharomyces cerevisiae monounsaturated fatty acid auxotroph L8-14C, incorporation of zinc instead of iron into the protein is likely an artifact of protein overexpression, and zinc remains the predominant metal species even when the growth media and purification solutions are supplemented with iron
recombinant isozyme SCD1 partially from transfected HEL-293 cells by microsome preparation
recombinant isozyme SCD2 partially from transfected HEL-293 cells by microsome preparation
recombinant isozyme SCD3 partially from transfected HEL-293 cells by microsome preparation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA fragment corresponding to bp 278-2005 of the sequence was subcloned into a pcDNA3 vector in antisense orientation and stably transfected into SV40-WI38 lung fibroblasts cells, enzyme activity reduced in these stable cell clones, reduced protein level, reduced enzyme expression slows the rate of cell proliferation and suppresses anchorage-independent proliferation, SCD deficiency promotes apoptosis in a ceramide-independent manner
coexpression of acyl carrier protein isoform I gene and holo-acyl carrier protein synthase of Escherichia coli
-
expressed in HeLa cells, tagged with myc epitope at the C terminus or HA epitope
-
expressed in L6GLUT4myc myoblasts, localized in endoplasmic reticulum-like subcellular structures, laser scanning microscopy
-
expressed in primary human skeletal muscle cells from obese and lean donors, SCD1 mRNA levels are increased 2.8fold, protein levels are increased 5.7fold in myotubes from obese compared to lean subjects
-
expressed in Saccharomyces cerevisiae
expression in Escherichia coli, transfection of Arabidopsis by Agrobacterium tumefaciens clones
-
gender- and age-related quantitative expression analysis of SCD in brains in relation to the fatty acid composition, overview
-
gene complements genetic disruption of OLE1 of Saccharomyces cerevisiae
gene FAD1, recombinant co-overexpression with Rhodotorula toruloides RtFAD2 encoding DELTA12-desaturase in Rhodotorula toruloides strain DMKU3-TK16 (a thermotolerant derivative of strain TK16 (L1-1)). The expression levels of RtFAD1 are drastically decreased in the RtFAD1 and RtFAD2 co-overexpressing strains in TK16 and L1-1
-
gene rv3229c, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli as c-Myc and/or His-tagged protein, DesA3 expressed as a fusion with either a C-terminal His6 or c-myc tag has consistently higher activity and stability than native DesA3 having the native C-terminal sequence of LAA. The native C-terminal sequence of LAA apparently serves as a binding determinant for a mycobacterial protease/degradation system directed at DesA3. Fusion of only the last 12 residues of native DesA3 to the C-terminal of GFP is sufficient to make GFP unstable
-
gene scd, lentiviral-based overexpression and knockdown of SCD in tumor-initiating cells
gene SCD, quantitative real-time PCR enzyme expression analysis, enzyme expression analysis in 7-weeks-old and in 4-months-old piglets, expression level of stearoyl-CoA desaturase (SCD) and three transcriptional factors in various adipose depots from piglets and adult pigs
gene SCD, semiquantitative and quantitative RT-PCR enzyme expression analysis
gene SCD-1, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli srain BL21(DE3)
-
gene SCD-2, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli srain BL21(DE3)
-
gene SCD1, DNA and amino acid analysis, sequence comparisons, quantitative RT-PCR enzyme expression analysis and gene expression profiling
gene SCD1, phylogenetic tree, sequence comparisons with other isozymes and enzymes from other organisms, overview
gene SCD1, recombinant expression in Spodoptera frugiperda SF9 cells, the recombinant enzyme contains artificial Zn2+ ions, which are replaced for Fe2+. Recombinant expression of codon-optimized mouse SCD1 gene with deletion of residue 2-23 at the N-terminus (mDELTASCD1) in HEK-293 cells as C-terminally GFP-tagged enzyme
gene scd1, recombinant expression of isozyme SCD1 in Saccharomyces cerevisiae monounsaturated fatty acid auxotroph L8-14C, which allows growth in media lacking unsaturated fatty acids. Optimization of enzyme expression method
gene scd3, recombinant expression of wild-type and mutant isozymes SCD3 in Saccharomyces cerevisiae monounsaturated fatty acid auxotroph L8-14C, wild-type exxpression allows growth in media lacking unsaturated fatty acids
gene SCD5, DNA and amino acid sequence determination and analysis, phylogenetic tree, sequence comparisons with other isozymes and enzymes from other organisms, overview
gene scd5, located on chromosome 4, recombinant expression of human SCD5 in mouse 3T3-L1 preadipocytes leading to elevation of oleic acid without modifying the content of palmitoleic acid. Lentivirus-mediated expression of SCD5 in human melanoma and murine mammary carcinoma cells markedly increase the oleic acid/stearic acid ratio with minimal changes in the palmitoleic acid/palmitic acid ratio. Liver-specific overexpression of human SCD5 in mice with global SCD1 depletion increases the levels of oleic acid, but not palmitoleic acid
gene TGGT1 238950, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of C-terminally HA3-tagged enzyme in Toxoplasma gondii mutant DELTAKu80
heterologously expressed in Saccharomyces cerevisiae
identified of positive clones by screening with hybridization of cDNA of carp with rat DELTA9-desaturase cDNA
-
in vitro translation using a wheat germ cell-free extract in the presence of unilamelar liposomes, method optimization of cell-free translation to the assembly and purification of integral membrane protein complexes
isozyme SCD1, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in HEK-293 cell microsomes
isozyme SCD2, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in HEK-293 cell microsomes
isozyme SCD3, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in HEK-293 cell microsomes
isozyme SCD5 liver-specific overexpression in isozyme SCD1 global knockout mutants
overexpression in CHO cells results in a significant increase in the rate of triglyceride synthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
C-reactive protein concentrations are positively associated with estimated SCD-1 activity
-
chronic food restriction and chronic food restriction/refeeding cause increased expression
-
elanocortin receptor agonist MT II and leptin suppress the liver Scd1 independently of insulin and SREBP-1c
enzyme SCD is observed to be significantly induced in 3T3-L1 preadipocytes differentiation. SCD and lipogenesis-related genes are induced significantly in differentiated porcine adipocytes
enzyme SCD1 is 28fold upregulated in enriched liver tumor-initiating cell populations and sporadically expressed in human hepatocellular carcinoma specimens, upregulation of SCD1 of self-renewing liver cancer cells in chemoresistant hepatospheres
hepatic SCD1 expression increases in experimental steatosis resulting from high fat diet and decreases in a methionine-choline-deficient dietary model of steatohepatitis resulting in the latter situation in significantly increased hepatic saturated fatty acid levels
-
higher levels of stearoyl lysophosphatidylcholine and lower levels of oleoyl lysophosphatidylcholine in dextran sulfate sodium-treated mice compared to controls lead to the identification of dextran sulfate sodium-elicited inhibition of SCD1 expression in liver, Citrobacter rodentium-induced colitis and lipopolysaccharide treatment also suppresses SCD1 expression in liver
-
intracerebroventricular glucose administration strongly decreases hepatic Scd1
-
isoform SCD-1 expression is dramatically induced in liver and heart in response to high-carbohydrate diet, SCD-1 expression is also induced by nuclear sterol regulatory element-binding protein-1 via the sterol regulatory element in its promoter, in aortic endothelial cells liver X receptor beta activation increases SCD-1 mRNA and protein expression
-
linolenic acid and eicosapentaenoic acid decrease SCD mRNA (EC50 of 0.50 and 1.67 mM), whereas alpha-linolenic acid does not, GW-9662 at a pan-peroxisome proliferation activator receptor antagonistic dose does not obviate the effects of linolenic acid and eicosapentaenoic acid on SCD mRNA
-
SCD-1 expression is about 2fold upregulated in coronary artery smooth muscle cells, myotubes, and Hep-G2 cells at 0.5 mM palmitate, SCD-1 is upregulated using 0.01 mM TO-901317 in HAEC cells, inhibition of SCD-1 with cis-10,trans-12-conjugated linoleic acid blocks the upregulating effect of TO-901317
-
SCD1 expression is induced by palmitate, high SCD1 inducibility is associated with a low inflammatory and endoplasmic reticulum stress response to palmitate exposure
-
Scd1 is both transcriptionally and post-transcriptionally regulated. Scd1 transcription is induced by binding of liver X receptor (LXR) to LXR response element (LXRE) and that of sterol regulatory-element binding protein-1c (SREBP-1c) to the SREBP element (SRE). As LXR activates Srebp-1c transcription, LXR is capable of activating Scd1 directly and indirectly. Dietary carbohydrate such as glucose, fructose and sucrose, increases the expression of liver Scd1 in both SREBP-1c dependent and independent manners and the latter is caused by carbohydrate-induced LXR and the activation of carbohydrate response-element binding protein (ChREBP). Scd1 is upregulated by activation of the xenobiotic nuclear receptor pregnane-X-receptor (PXR), but this regulation may be mediated by the ability of PXR agonists to activate both PXR and LXR and to induce CD36 which takes up native lipoproteins, oxidized LDL, oxidized phospholipids, and long-chain fatty acids (FA). Toll-like receptor 2 (TLR2)-NF-kappaB activation transcriptionally induces SCD1 in human sebocytes and this underlies antimicrobial defense facilitated by MUFA in skin. SCD1 protein is a short-lived protein with a half-life of 2-4 hours and is stabilized by the PPAR agonist clofibric acid, which also stimulates Scd1 transcription
Scd1 is both transcriptionally and post-transcriptionally regulated. Scd1 transcription is induced by binding of liver X receptor (LXR) to LXR response element (LXRE) and that of sterol regulatory-element binding protein-1c (SREBP-1c) to the SREBP element (SRE). As LXR activates Srebp-1c transcription, LXR is capable of activating Scd1 directly and indirectly. Dietary carbohydrate such as glucose, fructose and sucrose, increases the expression of liver Scd1 in both SREBP-1c dependent and independent manners and the latter is caused by carbohydrate-induced LXR and the activation of carbohydrate response-element binding protein (ChREBP). Scd1 is upregulated by activation of the xenobiotic nuclear receptor pregnane-X-receptor (PXR), but this regulation may be mediated by the ability of PXR agonists to activate both PXR and LXR and to induce CD36 which takes up native lipoproteins, oxidized LDL, oxidized phospholipids, and long-chain fatty acids (FA). Toll-like receptor 2 (TLR2)-NF-kappaB activation transcriptionally induces SCD1 in human sebocytes and this underlies antimicrobial defense facilitated by MUFA in skin. SCD1 protein is a short-lived protein with a half-life of 2-4 hours and is stabilized by the PPAR agonist clofibric acid, which also stimulates Scd1 transcription. Human SCD1/5 may gain the stability by forming dimers and oligomers
the enzyme level is dramatically increased in high-fat diet-fed myeloid differentiation factor 88-deficient mice liver
-
the expression level of SCD1 is positively correlated with the marbling score
there is a 53fold increase of SCD transcript expression level between 18 and 36 h during the late trophozoite stage
vitamin A deficiency decreases SCD1 protein and its product, oleic acid (C18:1)
vitamin A deficiency decreases SCD1 protein and its product, oleic acid (C18:1)
-
vitamin A deficiency decreases SCD1 protein and its product, oleic acid (C18:1)
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
in vitro reconstitution of the non-heme iron and heme active sites to a functional reconstituted enzyme complex after in vitro translation and protein integration into liposomes, method optimization, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
drug development
medicine
pharmacology
agriculture
-
higher enzymic acitivity in Jersey-sired cattle than in Limousin-sired cattle, positive relationship between adipose tissue beta-carotene and desaturation
drug development
SCD-1 is a promising target for the treatment of cancer, skin disorders and metabolic diseases, development of clinical drug candidates
drug development
isozyme SCD1 may represent a therapeutic target to control obesity and the progression of related metabolic diseases including type 2 diabetes and hepatic steatosis
drug development
SCD-1 is a promising target for the treatment of cancer, skin disorders and metabolic diseases, development of clinical drug candidates
drug development
SCD1 is a drug target for various metabolic diseases and cancers
drug development
-
accelerated bottom-up drug design platform enables the discovery of stearoyl-CoA desaturase 1 inhibitors for cancer therapy
medicine
-
potential use of SCD1 as a target in the treatment of some eye diseases
medicine
-
treatment with enzyme-specific antisense oligonucleotide inhibitors results in prevention of diet-induced obesity with reductions in the ratio of oleate to stearoyl-CoA in tissues and plasma. Correlation with reduced body adiposity, hepatomegaly and steatosis
medicine
-
DELTA9 desaturase and abdominal adiposity are positively associated independently of insulin resistance and dietary saturated fatty acids intake, DELTA9 desaturase is positively associated with blood lipids independent of the insulin resistance, abdominal adiposity, and dietary saturated fatty acid intake
medicine
the gene combination of macrophage migration inhibitory factor and stearoyl-CoA desaturase 1 is a prognostic marker for the overall outcome of soft tissue sarcomas
medicine
targeting SCD1 in combination with sorafenib may be another therapeutic strategy against liver cancer. SCD1 may be a biomarker for sorafenib response and personalized medicine for hepatocellular carcinoma
medicine
isozyme SCD1 may represent a therapeutic target to control obesity and the progression of related metabolic diseases including type 2 diabetes and hepatic steatosis
medicine
the use of combined treatment with SCD1 inhibitors and ferroptosis inducers may provide a therapeutic strategy for patients with ovarian cancer. Combined treatment with SCD1 inhibitors and RSL3 results in a synergistic cytotoxic effect on FT-t cells as calculated by the Chou-Talalay method. The decrease in viability in cells treated with the combination of RSL3 and SCD1 inhibitors is characterized by an increased oxidation of membrane lipids consistent with an increase in ferroptotic cell death. Further, blockade of SCD using siRNA or shRNA similarly sensitizes cells to RSL3, ruling out nonspecific effects of SCD1 inhibitors on ferroptosis sensitization
medicine
prospect for SCD-mediated signaling crosstalk as a potential therapeutic target for cancer
pharmacology
targeting SCD1 in combination with sorafenib may be another therapeutic strategy against liver cancer. Clinically, SCD1 serves as a good predictive marker for patient responses to sorafenib treatment. Targeting SCD1 synergizes the effect of sorafenib both in vitro and in vivo
pharmacology
enhancing SCD1-mediated desaturation of saturated fatty acids and subsequent formation of neutral lipid droplets may become a promising therapeutic target to reduce saturated fatty acid-induced lipotoxicity in the pathogenesis of diabetic nephropathy
pharmacology
-
SCD1 inhibitor is a potential candidate for treating dengue fever
pharmacology
-
SCD1 inhibitor is a potential candidate for treating dengue fever
pharmacology
SCD1 inhibitor is a potential candidate for treating dengue fever
pharmacology
-
SCD1 inhibitor is a potential candidate for treating dengue fever
EXTERNAL LINKS (specific for EC-Number 1.14.19.1)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
