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Information on EC 3.4.24.B4 - matrix metalloproteinase-13
for references in articles please use BRENDA:EC3.4.24.B4preliminary BRENDA-supplied EC number
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EC Tree
3.4.24.B4 matrix metalloproteinase-13Specify your search results
Word Map
- 3.4.24.B4
- cartilage
- chondrocytes
- osteoarthritis
- metalloproteinases
- joint
-
articular
- aggrecan
- degeneration
- mmp-2
- tnf
- knee
- timp-1
- arthritis
- synovial
- interleukin-1
- proteoglycans
-
degener
- cox-2
- osteoblast
- adamts-5
- ligament
-
intra-articular
- collagenases
-
col2a1
- thrombospondin
- pulposus
- runx2
-
cruciate
-
zymography
-
chondrogenic
- gelatinase
- meniscus
-
intervertebral
-
subchondral
-
disintegrin
-
endochondral
-
safranin
- synoviocytes
-
collagenolytic
-
matrix-degrading
-
chondroprotective
-
ossification
-
temporomandibular
- mt1-mmp
-
chondrogenesis
- medicine
- stromelysin-1
- diagnostics
-
cartilage-specific
-
condylar
- analysis
- osteophyte
- drug development
- aggrecanase
The enzyme appears in viruses and cellular organisms
Synonyms
mmp-13, mmp13, collagenase-3, matrix metalloproteinase-13, matrix metalloproteinase 13, collagenase 3, mmp13a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
collagenase
collagenase 3
collagenase-3
M10.013
matrix metalloproteinase 13
matrix metalloproteinase-13
MMP-13
MMP13
additional information
matrix metalloproteinase-13
-
-
MMP-13
-
-
649335, 650906, 651854, 651876, 652045, 677407, 677860, 682209, 682962, 691486, 693582, 693802, 707707, 708635, 710176, 711041, 711043, 711046, 711048, 711049, 711050, 711163, 711388, 711392, 711414, 711421, 711595, 711608, 711683, 711922, 712131, 712200, 712547, 712576, 712577, 712592, 712636, 712837, 712838, 712839, 712849, 713161, 713163, 713164, 713176, 713178, 713372, 713497, 713548, 719033, 719055, 719062, 719319, 720193
MMP-13
-
-
additional information
MMP-13 is the third member in the collagenase subfamily of proteases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
C-terminal and N-terminal part are involved in substrate and inhibitor binding
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CAS REGISTRY NUMBER
COMMENTARY
175449-82-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly-norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly + norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu + Gly-Leu-Dpa-Ala-Arg-NH2
-
-
-
-
?
2,4-dinitrophenyl-GPLGMRSGL-NH2 + H2O
2,4-dinitrophenyl-GPLGM + RSGL-NH2
-
-
-
?
alpha1-Antichymotrypsin + H2O
?
-
cleavage of peptide bond Ala362-Leu363
-
?
alpha2-antichymotrypsin + H2O
?
-
degradation, cleavage site is Ala362-Leu363
-
?
alpha2-chain of type IV collagen + H2O
?
-
cleavage sites at amino acid residues 881 and 1000 in the triple-helical region
-
?
alpha4-chain of type IV collagen + H2O
?
-
cleavage site at amino acid residue 86 in the triple-helical region
-
?
collagen II + H2O
?
complete degradation by the isolated catalytic domain
-
-
?
collagen type I beta1,2 chain + H2O
collagen type I alpha1,2 chain
-
wild-type enzyme and enzyme fragment 249-451
-
?
Collagen type III + H2O
?
-
5 to 6fold less active compared to substrate collagen type II
-
?
collagen type IV chain alpha1 + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type IV chain alpha2 + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type X + H2O
48 kDa fragment
-
wild-type enzyme and enzyme fragment 249-451
-
?
collagen type X + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
fibronectin + H2O
fragments of MW 100 kDa, 43 kDa, 35 kDa, and 29 kDa
-
native and recombinant substrate, whole substrate molecule and fragments, wild-type enzyme and enzyme fragment 249-451
from intact plasma fibronectin
?
interstitial collagen type II + H2O
?
-
fibrillar collagen, best substrate, cleavage sites are Gly906-Leu907, Gly909-Gln910, and Gly912-Ile913
-
?
Transforming growth factor + H2O
?
-
cleavage site at amino acid residue 150 in the latency-associated peptide
-
?
type-II collagen + H2O
?
-
the osteoarthritic cartilage type-II collagen is preferentially cleaved by the proinflammatory cytokine-induced MMP-13
-
-
?
Y(NO2)GGPAGLYEK(Abz)G + H2O
Y(NO2)GGPAG + LYEK(Abz)G
FRET substrate, cleavage rate is 0.468 nmoles/second
-
-
?
Y(NO2)GPLGMRGLK(Abz)G + H2O
Y(NO2)GPLG + MRGLK(Abz)G
FRET substrate, cleavage rate is 0.006 nmoles/second
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly-norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly + norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2
-
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly-norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Cha-Gly + norvaline-His-Ala-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-NH2
-
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
-
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2
-
-
-
?
Ac-PLG-[2-mercapto-4-methyl-pentanoyl]-LG-OC2H5 + H2O
?
-
colorimetric substrate
-
-
?
Ac-PLG-[2-mercapto-4-methyl-pentanoyl]-LG-OC2H5 + H2O
?
-
colorimetric substrate
-
-
?
aggrecan + H2O
?
-
cleavage site in the interglobular domain is PEN341-FFG
-
?
Collagen type I + H2O
?
-
fibrillar, 5 to 6fold less active compared to substrate collagen type II
-
?
Collagen type I + H2O
?
-
wild-type enzyme, substrate binding is mediated by the C-terminal domain, which is essential for the triple helicase activity
-
?
Collagen type I + H2O
?
-
Interstitial fibers of collagen type I in the plaque can be degraded by MMP13 specifically. MMP13 is capable of degrading collagen type I in the upstream atherosclerotic lesions
-
-
?
collagen type IV + H2O
?
-
substrate alpha2-chain and alpha1-chain, wild-type enzyme and enzyme fragment 249-451
-
?
collagen type IV + H2O
?
-
wild-type enzyme and enzyme fragment 249-451
-
?
collagen type IX + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
collagen type IX + H2O
?
-
wild-type enzyme and enzyme fragment 249-451
-
?
collagen type XIV + H2O
?
-
alpha3-chain, wild-type enzyme and enzyme fragment 249-451
-
?
collagen type XIV + H2O
?
-
fibrillar collagen, wild-type enzyme and truncated mutant
-
?
fibrillin-1 + H2O
?
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
fibrillin-2 + H2O
?
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
Fibronectin + H2O
?
partial degradation by the isolated catalytic domain
-
-
?
Gelatin + H2O
?
complete degradation by the isolated catalytic domain
-
-
?
large tenascin C isoform + H2O
?
-
no activity with the small isoform
-
?
large tenascin C isoform + H2O
?
-
wild-type enzyme and enzyme fragment 249-451
-
?
protein + H2O
peptides
-
substrate specificity and cleavage site determination via phage display approach
-
?
protein + H2O
peptides
enzyme is involved in human breast cancer pathology and in arthritic processes
-
?
protein + H2O
peptides
-
enzyme is involved in tumor progression, significant role in the turnover of connective tissue matrix constituents
-
?
protein + H2O
peptides
-
enzyme plays a key role in the matrix metalloproteinase activation cascade, and in tumor invasion and metastasis, and appears to be critical in bone metabolism and homeostasis
-
?
type II collagen + H2O
?
-
the hemopexin domain of the protease is critical for substrate specificity
-
-
?
additional information
?
-
-
plasmin-activated MMP-13 can functions as an angiogenic factor. Physiological role of MMP-13: associated with cartilage/bone resorption and collagen remodeling involved in the angiogenic cascade
-
-
?
additional information
?
-
-
collagen type XI is not cleaved by wild-type enzyme and truncated mutant
-
?
additional information
?
-
-
no activity with the minor cartilage collagen type XI
-
?
additional information
?
-
-
enzyme expression is limited to situations of rapid extracellular matrix remodeling, transcriptional regulatory mechansim, strict regulation of expression
-
?
additional information
?
-
-
role for enzyme in regulating dermal fibroblast survival, proliferation, and interaction in 3D collagen
-
-
?
additional information
?
-
-
MMP-13 has wide substrate specificity compared with other MMPs
-
-
?
additional information
?
-
-
MMP-13 interacts with tissue inhibitor of metalloproteinase-3, fibronectin 1, insulin-like growth factor binding protein 5, and FBJ murine osteosarcoma viral oncogene homologue
-
-
?
additional information
?
-
-
MMP-13 is basically capable of degrading all components of the extracellular matrix
-
-
?
additional information
?
-
MMP-13 preferentially hydrolyzes collagen type II, and has wide substrate specificity, allowing it to degrade several other forms of collagen and other extracellular matrix components
-
-
?
additional information
?
-
-
MMP-13 preferentially hydrolyzes collagen type II, and has wide substrate specificity, allowing it to degrade several other forms of collagen and other extracellular matrix components
-
-
?
additional information
?
-
-
stimulates bradykinin-induced tyrosine phosphorylation and activation of epidermal growth factor receptor
-
-
?
additional information
?
-
-
MMP-13 degrades intact collagen and participates in situations where rapid and effective remodeling of collagenous extracellular matrix is required
-
-
?
additional information
?
-
-
osteoblastic osteosarcoma cell line UMR 106-01, Ca2+-dependent binding in a two-step mechanism via the required specific 170 kDa enzyme receptor and the required 600 kDa LDL-receptor, internalization and degradation of the enzyme, modeling, the enzyme also binds to mouse fibroblastic cells
-
?
additional information
?
-
-
decrease in types I and III collagen with a concurrent increase in MMP-13 after elastase perfusion in males compared with females, overview
-
-
?
additional information
?
-
-
rat MMP13 is a better gelatinase than a collagenase. Injection of catalytically active recombinant MMP13 enzyme into a rat knee joint to induce cartilage damage
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Collagen type I + H2O
?
-
Interstitial fibers of collagen type I in the plaque can be degraded by MMP13 specifically. MMP13 is capable of degrading collagen type I in the upstream atherosclerotic lesions
-
-
?
fibrillin-1 + H2O
?
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
fibrillin-2 + H2O
?
-
enzyme affects microfibril organization and integrity, leadint ot loss of normal microfibril function
-
?
interstitial collagen type II + H2O
?
-
fibrillar collagen, best substrate, cleavage sites are Gly906-Leu907, Gly909-Gln910, and Gly912-Ile913
-
?
type-II collagen + H2O
?
-
the osteoarthritic cartilage type-II collagen is preferentially cleaved by the proinflammatory cytokine-induced MMP-13
-
-
?
protein + H2O
peptides
enzyme is involved in human breast cancer pathology and in arthritic processes
-
?
protein + H2O
peptides
-
enzyme is involved in tumor progression, significant role in the turnover of connective tissue matrix constituents
-
?
protein + H2O
peptides
-
enzyme plays a key role in the matrix metalloproteinase activation cascade, and in tumor invasion and metastasis, and appears to be critical in bone metabolism and homeostasis
-
?
additional information
?
-
-
plasmin-activated MMP-13 can functions as an angiogenic factor. Physiological role of MMP-13: associated with cartilage/bone resorption and collagen remodeling involved in the angiogenic cascade
-
-
?
additional information
?
-
-
enzyme expression is limited to situations of rapid extracellular matrix remodeling, transcriptional regulatory mechansim, strict regulation of expression
-
?
additional information
?
-
-
role for enzyme in regulating dermal fibroblast survival, proliferation, and interaction in 3D collagen
-
-
?
additional information
?
-
-
MMP-13 has wide substrate specificity compared with other MMPs
-
-
?
additional information
?
-
-
MMP-13 interacts with tissue inhibitor of metalloproteinase-3, fibronectin 1, insulin-like growth factor binding protein 5, and FBJ murine osteosarcoma viral oncogene homologue
-
-
?
additional information
?
-
-
MMP-13 is basically capable of degrading all components of the extracellular matrix
-
-
?
additional information
?
-
MMP-13 preferentially hydrolyzes collagen type II, and has wide substrate specificity, allowing it to degrade several other forms of collagen and other extracellular matrix components
-
-
?
additional information
?
-
-
MMP-13 preferentially hydrolyzes collagen type II, and has wide substrate specificity, allowing it to degrade several other forms of collagen and other extracellular matrix components
-
-
?
additional information
?
-
-
MMP-13 degrades intact collagen and participates in situations where rapid and effective remodeling of collagenous extracellular matrix is required
-
-
?
additional information
?
-
-
osteoblastic osteosarcoma cell line UMR 106-01, Ca2+-dependent binding in a two-step mechanism via the required specific 170 kDa enzyme receptor and the required 600 kDa LDL-receptor, internalization and degradation of the enzyme, modeling, the enzyme also binds to mouse fibroblastic cells
-
?
additional information
?
-
-
decrease in types I and III collagen with a concurrent increase in MMP-13 after elastase perfusion in males compared with females, overview
-
-
?
additional information
?
-
-
rat MMP13 is a better gelatinase than a collagenase. Injection of catalytically active recombinant MMP13 enzyme into a rat knee joint to induce cartilage damage
-
-
?
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
Ca2+
Zn2+
additional information
-
Ca2+-dependent binding to the specific receptor of osteoblastic and fibroblastic cell lines via residue I125
Ca2+
three Zn2+ and three Ca2+ ions per crystallographically independent sununit
Zn2+
three Zn2+ and three Ca2+ ions per crystallographically independent sununit
Zn2+
-
dependent on. MMPs have a conserved active site motif, where a tris(histidine)-bound zinc(II) acts as the catalytic site for substrate hydrolysis
Zn2+
His201, His211, and His 205 are involved in metal ion binding, geometry from crystal structure
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-N,3-dihydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]propanamide
-
-
(2R)-N-hydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]-2-(tetrahydro-2H-pyran-4-yl)ethanamide
-
-
(2R)-N-hydroxy-4-(4-hydroxyphenyl)-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]butanamide
-
-
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
-
(2R)-[1-(tert-butoxycarbonyl)piperidin-4-yl][([5-[4-(dimethylamino)phenyl]thiophen-2-yl]sulfonyl)amino]ethanoic acid
-
-
(2R,3R)-4-[[4-(2-chloro-4-fluorophenoxy)phenyl]sulfonyl]-N,2-dihydroxy-2-methylmorpholine-3-carboxamide
-
-
(2R,4S)-1-((4-[(2-chlorobenzyl)oxy]phenyl)sulfonyl)-N,4-dihydroxypiperidine-2-carboxamide
-
i.e. rTACE, 50% inhibition at 12 nM
(2S,3R)-1-acetyl-N-hydroxy-2-methyl-4-[[4-(2-methylbenzyl)phenyl]sulfonyl]piperidine-3-carboxamide
-
-
(2S,3R)-2-[(cyclopropylmethyl)amino]-N1-hydroxy-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-3-methylbutanediamide
-
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(2-methoxybenzylidene)-1,3-thiazolidin-4-one
-
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(3-methoxybenzylidene)-1,3-thiazolidin-4-one
-
(3S)-N,3-dihydroxy-4-[(3'-methylbiphenyl-4-yl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 0.43 nM, not inhibitory to aggrecanase
(3S)-N,3-dihydroxy-4-[(4'-methylbiphenyl-4-yl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 0.39 nM, not inhibitory to aggrecanase
(3S)-N,3-dihydroxy-4-[(4-(2,4-dichlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition of enzyme at 0.95 nM, 50% inhibition of aggrecanase at 8.1 nM
(3S)-N,3-dihydroxy-4-[(4-(2-chlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 2.7 nM
(3S)-N,3-dihydroxy-4-[(4-(3-chlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 2.4 nM
(3S)-N,3-dihydroxy-4-[(4-(3-methylbenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 5 nM
(3S)-N,3-dihydroxy-4-[(4-(4-chlorobenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 0.88 nM, selective for enzyme
(3S)-N,3-dihydroxy-4-[(4-(4-methylbenzoxy)phenyl)sulfonyl]tetrahydro-2H-pyran-3-carboxamide
-
50% inhibition at 1.3 nM
(3S,3'S)-astaxanthin
i.e. 3S,3S-dihydoxy-beta, beta-carotene-4,4-dione, active metabolite of some soft drugs, binds to enzyme at or near active site
(4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]phenyl)acetic acid
-
-
(4R)-1-[4-(4-fluorophenoxy)benzyl]-N-hydroxy-2-oxoimidazolidine-4-carboxamide
-
-
(E)-2-(4-(2-(biphenyl-4-yl)vinyl)-N-isopropoxyphenylsulfonamido)-N-hydroxyacetamide
-
(R)-2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxy-3-methylbutanamide
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-cyclohexanecarbonyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-propylcarbamoyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropionyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2-methylpropane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(3,3-dimethylbutyryl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(methane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(phenylmethanesulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-2-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(tetrahydropyran-4-carbonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-benzylpiperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-iso-butylpiperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-diethylcarbamoylpiperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-butyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-isopropylcarbamoyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-tertbutylcarbamoyl-piperidin-4-yl)-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(toluene-4-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
(R)-[5-(4-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(butane-1-sulfonyl)-piperidin-4-yl]-acetic acid
-
-
1,5-anhydro-2,3-dideoxy-3-[[4-(2,4-dichlorophenoxy)phenyl]sulfonyl]-4-C-(hydroxycarbamoyl)-D-threo-pentitol
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(1-hydroxyethyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(1-methoxyethyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(2-methoxyphenyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(2-phenylethyl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(propan-2-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyrazin-2-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyridin-2-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyridin-4-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)-N,N-bis[4-(pyrimidin-4-yl)piperazin-1-yl]piperidine-4-carboxamide
-
-
1-(6-[4-[4-(4-fluorophenyl)-1,3-oxazol-2-yl]phenoxy]pyridin-3-yl)-1,7,9-triazaspiro[4.5]decane-6,8,10-trione
-
-
1-acetyl-4-hydroxypyrrolidine-2-carboxylic acid
-
binding structure, modelling, overview
1-cyclopropyl-4-[(4-[4-[(1,3-dibenzyl-1,3-dimethyltriazan-2-yl)carbonyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
1-cyclopropyl-4-[[4-(4-[[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxypiperidine-4-carboxamide
-
-
1-cyclopropyl-N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)piperidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
1-cyclopropyl-N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]piperidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
1-cyclopropyl-N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]piperidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
1-[4-((4-phenoxy)phenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
1-[4-(1,3-benzodioxol-5-yloxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
1-[4-(3-methoxyphenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
1-[4-(4-chlorophenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
2,3-dihydro-1,4-benzodioxine-2-carboxylic acid
-
binding structure, modelling, overview
2,3-dihydro-1,4-benzodioxine-5-carboxylic acid
-
binding structure, modelling, overview
2-(2-[(2-chlorobenzoyl)amino]-1,3-thiazol-4-yl)acetic acid
-
binding structure, modelling, overview
2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxyacetamide
-
2-(5-((4-butylphenyl)ethynyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
-
2-(5-(4-ethylphenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
-
2-(5-(4-fluorophenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
-
2-(benzo[d]isothiazol-3-ylimino)-5-(4-methoxybenzylidene)thiazolidin-4-one
potent and selective MMP-13 inhibitor
2-(ethyl[[4-(prop-1-yn-1-yloxy)phenyl]sulfonyl]amino)-5-phenylpentane(thioperox)ic O-acid
-
-
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
-
-
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
-
-
2-fluoro-N-hydroxy-6-([4-[4-(trifluoromethoxy)phenoxy]piperidin-1-yl]sulfonyl)benzamide
-
-
2-[benzyl[(4-methoxyphenyl)sulfonyl]amino]-N-hydroxy-3,5-dimethylbenzamide
-
WAY- 152177
2-[[(4'-chlorobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
-
-
2-[[(4'-cyanobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
-
-
2-[[(4'-[[(5-bromo-4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]methyl]-3-methylbutanoic acid
-
-
2-[[[4-(4-chlorophenoxy)phenyl]sulfonyl](methyl)amino]-N-hydroxy-3-[(4-methylpiperazin-1-yl)methyl]benzamide
-
-
3-(carboxymethyl)-2-methylenepentanedioic acid
-
binding structure, modelling, overview
4-((R)-carboxy-[5-[4'-(2-methoxyethoxy)-phenyl]-thiophene-2-sulfonylamino]-methyl)-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-(3-[3-[3-(3,4-difluorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]prop-2-yn-1-yl]phenyl)butanoic acid
-
-
4-(4-[[(3R)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(4-[[(3R)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-(4-[[(3S)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyridin-4-ylmethyl)benzamide
-
-
4-(4-[[(3S)-3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl]ethynyl]phenoxy)-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)-N-(2-fluorobenzyl)benzamide
-
50% inhibition at 01.1 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-8, MMP-12
4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)-N-(3-fluorobenzyl)benzamide
-
50% inhibition at 0.85 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-8, MMP-12
4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)-N-phenylbenzamide
-
50% inhibition at 0.84 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-8, MMP-12
4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)-N-pyridin-3-ylbenzamide
-
50% inhibition at 0.40 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-8, MMP-12
4-([(2-([(3-methoxyphenyl)methyl]carbamoyl)-4-oxo-3H,4H-thieno[2,3-d]pyrimidin-5-yl)methoxy]methyl)benzoic acid
highly potent and selective MMP-13 inhibitor. Compound shows shows more than 2600fold selectivity over the other related metalloenzymes. The disodium salt formulation is well absorbed in all species tested at the oral dose of 10-20 mg/kg. Compound is active in in bovine nasal cartilage explants assay
4-([4-[(5-[[4-(dimethylamino)phenyl]amino]-5-oxopentyl)oxy]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([4-[4-(2,4-dimethylphenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-ethoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(2-fluorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(4'-fluorobiphenyl-2-yl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(4-chlorophenyl)piperazin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([4-[4-(4-chlorophenyl)piperidin-1-yl]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)benzoic acid
-
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)cyclohexanecarboxylic acid
-
4-([6-[(4-methoxybenzyl)carbamoyl]-4-oxopyrido[3,4-d]pyrimidin-3(4H)-yl]methyl)benzoic acid
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-([[4-(4-fluorophenoxy)phenyl]sulfonyl]amino)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-oxo-N-[[40-([[(5-oxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)methyl]sulfonyl]methyl)biphenyl-3-yl]methyl]-3,4-dihydroquinazoline-2-carboxamide
compound exhibits excellent potency and selectivity (greater than 170fold) over MMP1, 2, 3, 7, 8, 9, 10, 12, and 14 and tumor necrosis factor-alpha converting enzyme
4-[(4-[3-[(2,2-dimethylpentanoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[3-[(2,4-dimethylbenzoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[3-[(cyclohexylcarbonyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[3-[4-(dimethylamino)phenyl]-3-oxopropoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[4-[(1,3-diethenyl-1,3-dimethyltriazan-2-yl)carbonyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[4-[4-(dimethylamino)benzoyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
MMP-13 selective
4-[(4-[4-[4-(dimethylamino)phenyl]-4-oxobutoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[(4-[4-[bis(3,5-dimethylpiperidin-1-yl)carbamoyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxy-1-(2-methoxyethyl)piperidine-4-carboxamide
-
-
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-chloro-4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-cyanobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-fluoro-3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluoro-3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluoro-3-methylbenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
-
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
-
4-[(R)-(benzofuran-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-(benzo[b]thiophene-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-dimethylamino-biphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-ethoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-fluorobiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-methoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(4'-methylbiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(5-phenylthiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(5-pyridin-2-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-(5-pyridin-4-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3',4'-difluorophenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3',4'-methylenedioxyphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3,4-dimethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(3-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 1-ethyl-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 4-tetrahydropyranyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid butyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid cyclohexyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid ethyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid methyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid neopentyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid propyl ester
-
-
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-hydroxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-iso-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-methylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
-
-
4-[(R)-carboxy-[5-(4'-n-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
-
-
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-trifluoromethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[(R)-carboxy-[5-phenylthiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
-
-
4-[([3-[2-(3-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
-
4-[([3-[2-(4-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
-
4-[([[5-(1H-indol-5-yl)-1-methyl-1H-pyrazol-3-yl]carbonyl]amino)methyl]benzoic acid
-
-
4-[2-([6-fluoro-2-[([[3-(methyloxy)phenyl]methyl]amino)-carbonyl]-4-oxo-3,4-dihydroquinazolin-5-yl]oxy)ethyl]-benzoic acid
inhibitor exhibits excellent potency and selectivity for MMP-13 over other MMPs. No overt toxicity is observed in a preliminary repeat dose oral toxicity study of compound in rats. A single oral dose of the monosodium salt significantly reduces degradation products released from articular cartilage into the joint cavity in a rat MIA model in vivo
4-[2-[4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)phenyl]-1,3-oxazol-4-yl]benzonitrile
-
-
4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoic acid
-
comparison of selectivity with other matrix metalloproteinases
4-[4-[(3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl)ethynyl]phenoxy]-N-(pyridin-4-ylmethyl)benzamide
-
-
4-[4-[(3-methoxy-1-azabicyclo[2.2.2]oct-3-yl)ethynyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[4-[(E)-2-(1-azabicyclo[2.2.2]oct-2-en-3-yl)ethenyl]phenoxy]-N-(pyridin-4-ylmethyl)benzamide
-
-
4-[4-[(E)-2-(1-azabicyclo[2.2.2]oct-2-en-3-yl)ethenyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[4-[(E)-2-(3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl)ethenyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[4-[2-(3-hydroxy-1-azabicyclo[2.2.2]oct-3-yl)ethyl]phenoxy]-N-(pyrimidin-4-ylmethyl)benzamide
-
-
4-[carboxy-[5-(4-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[carboxy-[5-(6-methoxy-pyridin-3-yl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
-
4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
-
-
4-[[([5-[2-(ethoxymethyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
-
-
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
4-[[4-(3-[[4-(dimethylamino)benzoyl]amino]propoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-(4-[[1-ethynyl-1,3-dimethyl-3-(prop-2-yn-1-yl)triazan-2-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-(4-[[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxy-1-(2-methoxyethyl)piperidine-4-carboxamide
-
-
4-[[4-(4-[[4-(2,3-dimethylphenyl)piperazin-1-yl]carbonyl]piperidin-1-yl)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-(4-[[4-(dimethylamino)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
-
4-[[4-([5-[4-(dimethylamino)phenyl]-5-oxopentyl]oxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
MMP-13 selective
4-[[5-(2-methyl-6-[[3-(propan-2-yloxy)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
-
4-[[5-(2-methyl-6-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
-
4-[[5-(2-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
-
4-[[5-(2-[[4-fluoro-3-(trifluoromethyl)benzyl]carbamoyl]-6-methylpyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
-
4-[[6-(2-[3-[3-(hydroxyamino)-3-oxopropoxy]phenyl]-1,3-oxazol-5-yl)-4-oxoquinazolin-3(4H)-yl]methyl]benzoic acid
-
-
5-(2-ethoxyethyl)-5-[4-[4-(1,3,4-oxadiazol-2-yl)phenoxy]phenoxy]pyrimidine-2,4,6(1H,3H,5H)-trione
-
-
5-(3,4-difluorobenzyl)-7-methyl-4,6-dioxo-N-[[2-(3-sulfanylpropoxy)pyridin-4-yl]methyl]-3a,4,5,6-tetrahydrothieno[3,2-c]pyridine-2-carboxamide
-
-
5-(5-chloropyridin-2-yl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
5-[3-[(4-carboxybenzyl)carbamoyl]-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylic acid
-
-
5-[3-[(acetylamino)methyl]phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
5-[4-(1-benzofuran-2-ylmethoxy)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
5-[4-(acetylamino)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
6-hydroxy-2-(methylsulfanyl)-4-pyrimidinecarboxylic acid
-
binding structure, modelling, overview
AG1296
-
a platelet-derived growth factor receptor inhibitor, shows several physiological effects, overview
alendronate
-
inhibits the in vitro invasion and random cell migration, 99% inhibition at 0.4 mM and physiological Ca2+-concentration, 67% inhibition at 0.4 mM and high Ca2+-concentration
BB94
-
a broadspectrum MMP inhibitor, significantly inhibits keratinocyte migration
benzyl 6-benzyl-5,7-dioxo-6,7-dihydro-5H-[1,3]thiazolo[3,2-c]pyrimidine-2-carboxylate
-
competitive, does not ligate the catalytic zinc, zinc binding is unnecessary to achieve nanomolar affinity, extremely selective for inhibition of MMP13 over all other MMPs
bone morphogenetic protein 2
-
down-regulation of enzyme expression in osteoblasts, can be overcome by noggin
-
bone morphogenetic protein 4
-
down-regulation of enzyme expression in osteoblasts, can be overcome by noggin
-
bone morphogenetic protein 6
-
down-regulation of enzyme expression in osteoblasts, can be overcome by noggin
-
cilostazol
docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
clodronate
-
77% inhibition at 0.4 mM and physiological Ca2+-concentration, 35.7% inhibition at 0.4 mM and high Ca2+-concentration
domperidone
docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
eltrombopag
docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
ethyl 5-(1-methyl-3-[[(6-oxo-1,6-dihydropyridin-3-yl)methyl]carbamoyl]-1H-pyrazol-5-yl)-1H-indole-2-carboxylate
-
-
ethyl 5-[1-methyl-3-[(pyridin-4-ylmethyl)carbamoyl]-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
-
-
ethyl 5-[3-(methoxycarbonyl)-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
-
-
ethyl 5-[5-methyl-2-[(pyridin-4-ylmethyl)carbamoyl]pyridin-4-yl]-1H-indole-2-carboxylate
-
-
hydroxamate inhibitor RS-113456
a diphenyl ether sulfon compound, complexing of the enzyme via His205 and Glu202
-
hydroxamic acid inhibitor CGS 27023
complex formation with the catalytic fragment of the enzyme, inhibitor binding mechanism
hydroxamic acid inhibitor WAY-151693
complex formation with the catalytic fragment of the enzyme
mannose-6-phosphate/insulin-like growth factor 2 receptor
-
inhibition of enzyme induction by TGFbeta1 in chondrocytes
-
methyl 4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoate
-
comparison of selectivity with other matrix metalloproteinases
N,N'-bis(4-fluoro-3-methylbenzyl)pyrimidine-4,6-dicarboxamide
50% inhibition at 8 nM
N,N-bis(2,6-dimethylmorpholin-4-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis(3,5-dimethylpiperidin-1-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis(4-acetylpiperazin-1-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis(7,8-dimethoxy-3,4-dihydroisoquinolin-2(1H)-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(2,4-dimethylphenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(2-fluorophenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(4-acetylphenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-(4-fluorophenyl)piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-bis[4-[1-(dimethylamino)ethyl]piperazin-1-yl]-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N,N-di(3,4-dihydroisoquinolin-2(1H)-yl)-1-(4-[[4-(hydroxycarbamoyl)tetrahydro-2H-pyran-4-yl]sulfonyl]phenyl)piperidine-4-carboxamide
-
-
N-(3-methoxybenzyl)-4-oxo-3,4-dihydroquinazoline-2-carboxamide
lead compound for the development of thieno[2,3-d]pyrimidine-2-carboxamide inhibitors
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-threonine
-
-
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
-
-
N-([4'-[([4-[(1-methoxy-2-methyl-1-oxopropan-2-yl)oxy]-3-methyl-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
-
-
N-([4'-[([4-[(2-carboxypropan-2-yl)oxy]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
-
-
N-([4'-[([5-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)valine
-
50% inhibition at 0.43 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N-hydroxy-1-(2-methoxyethyl)-4-([4-[4-(phenylcarbamoyl)piperidin-1-yl]phenyl]sulfonyl)piperidine-4-carboxamide
-
-
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-biphenylcarbonyl)piperazine-2-carboxamide
-
-
N-hydroxy-2,2-dimethyl-4-[[4-(pyridin-4-yloxy)phenyl]sulfonyl]thiomorpholine-3-carboxamide
-
-
N-hydroxy-2,6-dimethoxy-3-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]pyridine-4-carboxamide
-
-
N-hydroxy-2-(N-isopropoxy-4'-(methylthio)biphenyl-4-ylsulfonamido)acetamide
-
N-hydroxy-2-(N-isopropoxy-5-(4-methoxyphenyl)thiophene-2-sulfonamido)acetamide
-
N-hydroxy-2-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]-3-methylbenzamide
-
-
N-hydroxy-3-methyl-2-(methyl[[4-(pyridin-4-yloxy)phenyl]sulfonyl]amino)benzamide
-
-
N-hydroxy-3-methyl-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-4-([4-[(4-hydroxybut-2-yn-1-yl)oxy]phenyl]sulfonyl)-2,2-dimethylthiomorpholine-3-carboxamide
-
-
N-hydroxy-4-([4-[4-(2-hydroxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methoxyphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(3,3,6-trimethoxycyclohexa-1,5-dien-1-yl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(3-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4,4,6-trimethoxycyclohexa-1,5-dien-1-yl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4-methoxy-2-methylphenyl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4-methoxyphenoxy)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-([4-[4-(4-methoxyphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(4-methylphenyl)piperazin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-(naphthalen-1-yl)piperidin-1-yl]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-([4-[4-oxo-4-(piperidin-1-yl)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[(4-[3-[(4-methoxybenzoyl)amino]propoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[(4-[4-[(4-methoxyphenyl)amino]-4-oxobutoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[(4-[4-[2-(trifluoromethyl)phenyl]piperidin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[(4-[4-[2-methoxy-5-(propan-2-yl)phenyl]piperidin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[(4-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[(4-[4-[4-(trifluoromethyl)phenyl]piperazin-1-yl]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[[4-(3-[[4-(trifluoromethoxy)benzoyl]amino]propoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-oxo-4-[[4-(trifluoromethoxy)phenyl]amino]butoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(4-phenylpiperazin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[[4-(4-phenylpiperidin-1-yl)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
N-hydroxy-4-[[4-(4-[methyl[4-(trifluoromethoxy)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
-
-
N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]-1-(prop-2-yn-1-yl)piperidine-4-carboxamide
-
i.e. SC-276
N-hydroxy-N2-(3-methylbutyl)-N2-(2,3,3a,7a-tetrahydro-1-benzofuran-5-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-5-phenyl-D-norvalinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-[(6-propoxynaphthalen-2-yl)sulfonyl]-D-valinamide
-
-
N-hydroxy-N2-(3-methylbutyl)-N2-[[6-(2-methylpropoxy)naphthalen-2-yl]sulfonyl]-D-valinamide
-
-
N-hydroxy-N2-[(6-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[(6-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[(7-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[(7-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-hydroxy-N2-[2-(morpholin-4-yl)ethyl]-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N-hydroxy-N2-[[6-(3-methylbutoxy)naphthalen-2-yl]sulfonyl]-N2-(3-methylbutyl)-D-valinamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(3-[[(furan-2-ylcarbonyl)amino]methyl]phenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-ethoxyphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methoxyphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methylphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-phenoxyphenyl)furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[3-([[(2-methylfuran-3-yl)carbonyl]amino]methyl)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(1H-pyrazol-3-ylmethoxy)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylcarbamoyl)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylsulfamoyl)phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1,5-dimethyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(5-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(6-methylpyridin-2-yl)methoxy]phenyl]furan-2-carboxamide
-
-
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(methylsulfonyl)amino]phenyl]furan-2-carboxamide
-
-
N-[(4'-[[(3,4-dimethyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(3-methyl-4-phenoxy-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(3-methyl-4-phenyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-amino-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-ethenyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-ethoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-ethyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-hydroxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(4-methoxy-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]valine
-
50% inhibition at 2.33 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N-[(4'-[[(4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
-
-
N-[(4'-[[(5-amino-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]valine
-
50% inhibition at 1.5 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N-[(4'-[[(5-chloro-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]valine
-
50% inhibition at 0.6 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N-[(4'-[[(5-methoxy-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]valine
-
50% inhibition at 0.66 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N-[(4'-[[(5-nitro-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]valine
-
50% inhibition at 0.7 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-threonine
-
replacing a backbone benzene with a pyridine and valine with threonine results in greatly reduced plasma protein binding of the compound
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-valine
-
-
N-[2-(4-[benzyl[2-(hydroxycarbamoyl)-4,6-dimethylphenyl]sulfamoyl]phenoxy)ethyl]-1-benzofuran-2-carboxamide
-
WAY-170523
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1,5-dimethyl-1H-pyrazole-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-imidazole-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-methyl-1,3-thiazole-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylfuran-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylpyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-ethylpyridine-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-methylfuran-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-methylpyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-7-methylimidazo[1,2-a]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-8-methylimidazo[1,2-a]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]imidazo[1,2-a]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-2-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-3-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
-
-
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
-
-
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
-
-
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-benzofuran-2-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-methyl-1H-pyrazole-3-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-4,5-dimethylfuran-2-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methyl-1H-pyrazole-3-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methylfuran-2-carboxamide
-
-
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-6-methylpyridine-2-carboxamide
-
-
N-[[(3-phenyl-1,2-oxazol-5-yl)methyl]carbamothioyl]benzamide
-
competitive, is synergic with acetohydroxamic acid
N-[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]-L-phenylalanine
-
-
N-[[4'-([[3-methyl-4-(methylamino)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[3-methyl-4-(morpholin-4-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[3-methyl-4-(prop-1-yn-1-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(3-hydroxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(3-methoxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(acetylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(dimethylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[4-(furan-2-yl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
-
-
N-[[4'-([[5-(acetylamino)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]valine
-
50% inhibition at 0.98 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N-[[4-(4-fluorophenoxy)phenyl]sulfonyl]-N-[1-(hydroxycarbamoyl)cyclopentyl]-b-alanine
-
-
N-[[4-(5-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]pyridin-2-yl)phenyl]sulfonyl]-L-valine
-
-
N2,N5-bis(3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
compound shows about 75fold selectivity over metalloproteases MMP3, MMP12
N2,N5-bis(4-fluoro-3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
compound shows about 65fold and 47fold selectivity over metalloproteases MMP3, MMP12, respectively
N2-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-(3a,7a-dihydro-1-benzothiophen-5-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-({4'-[(4-chlorobenzyl)oxy]biphenyl-4-yl}sulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
-
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl]-N,3-dimethyl-L-valinamide
-
-
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-6-phenoxyhexanoyl]-N,3-dimethyl-L-valinamide
-
-
N2-[(3,4-dimethoxyphenyl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[(6-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[(6-ethylnaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[(7-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
N2-[2-(dimethylamino)ethyl]-N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
-
-
N2-[[6-(benzyloxy)naphthalen-2-yl]sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
-
-
O-tert-butyl-N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-serinamide
-
-
P53
-
down-regulation of enzyme expression, possibly contributes to the dysregulation of the enzyme observed in cancer
tissue matrix metalloproteinase inhibitor hybrid N.TIMP-1/C.TIMP-2
-
complex formation is not affected by the C-terminal domain of the enzyme, inhibition mechanism, wild-type enzyme and enzyme fragment 249-451
-
tissue matrix metalloproteinase inhibitor-1
-
in a ratio of enzyme to inhibitor of 1:1
-
tissue matrix metalloproteinase inhibitor-2
-
in a ratio of enzyme to inhibitor of 1:1
-
tissue matrix metalloproteinase inhibitor-3
-
fast inhibition, in a ratio of enzyme to inhibitor of 1:1
-
transforming growth factor-beta1
-
i.e. TGFbeta1, accelerates the decay of the enzymes mRNA and decreased enzyme expression in osteoblasts
-
1-(4-phenoxyphenyl)-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
comparison of selectivity with other matrix metalloproteinases
4-([6-[(4-methoxybenzyl)carbamoyl]-4-oxopyrido[3,4-d]pyrimidin-3(4H)-yl]methyl)benzoic acid
-
4-([6-[(4-methoxybenzyl)carbamoyl]-4-oxopyrido[3,4-d]pyrimidin-3(4H)-yl]methyl)benzoic acid
-
a less potent MMP13 inhibitor
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
inhibitor of MMP-13 having no activity against MMP-1 (collagenase-1) or tumor necrosis factor-R converting enzyme
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
orally active carboxylic acid-derived MMP-13 inhibitor with subnanomolar potency is identified and tested in a rat intraarticular injection model. Greater than 20000fold in vitro selectivity for MMP-13 over MMP-1 is achieved
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
-
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
-
noncompetitive, extremely selective for inhibition of MMP13 over all other MMPs
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
-
-
5-(4-chlorophenyl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
discovery and optimization of potency and selectivity of the non-Zn-chelating MMP-13 inhibitor with the aid of protein co-crystal structural information, binding mode, overview. 1 binds in the active site region despite not interacting with the catalytic zinc
5-(4-chlorophenyl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
-
-
CL-82198
-
a specific MMP-13 inhibitor, inhibits also the metastatic activity of chloramphenicol-treated cells
marimastat
the intact peptide backbone scaffold is optimum to fix the inhibitor into the rigid environment of the MMP13 binding site
N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide
50% inhibition at 72 nM
N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide
-
extremely selective for inhibition of MMP13 over all other MMPs
N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide
-
a MMP13-specific inhibitor
N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide
50% inhibition at 6600 nM
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
-
i.e. PF152, a potent and highly selective MMP-13 inhibitor, that binds the S1' active site pocket of the enzyme, is not a ligand to the catalytic zinc atom, and dose-dependently decreases cartilage degradation ex vivo. PF152 treatment of osteoarthritis dogs reduces cartilage lesions and decreased biomarkers of type II collagen and aggrecan degradation
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
-
i.e. PF152, a non-hydroxamic acid and a potent and highly selective MMP-13 inhibitor, that binds the S1' active site pocket of the enzyme and is not a ligand to the catalytic zinc atom
N-([4'-[(1-benzofuran-2-ylcarbonyl)amino]biphenyl-4-yl]sulfonyl)valine
-
50% inhibition at 1.3 nM, comparison with inhibition of matrix metalloproteinases MMP-2, MMP-14
N2-[(4'-bromobiphenyl-4-yl)sulfonyl]-N-hydroxy-D-valinamide
-
a nonselective inhibitor
RS 102,481
-
a small molecule preferential inhibitor of MMP13, the compound is able to potently inhibit the release of type II collagen degradation peptides from human osteoarthritis articular cartilage explants
tissue matrix metalloproteinase inhibitor TIMP-1
-
complex formation is promoted by the C-terminal domain of the enzyme, inhibition mechanism, wild-type enzyme and enzyme fragment 249-451
-
tissue matrix metalloproteinase inhibitor TIMP-2
-
complex formation is not affected by the C-terminal domain of the enzyme, inhibition mechanism, wild-type enzyme and enzyme fragment 249-451
-
tissue matrix metalloproteinase inhibitor TIMP-3
-
complex formation is promoted by the C-terminal domain of the enzyme, inhibition mechanism, wild-type enzyme and enzyme fragment 249-451
-
additional information
-
development of MMP-13 inhibitors mechanistically distinct from previously reported broad-spectrum MMP inhibitors with improved selectivity and pharmacokinetics. Chondroprotective effect of MMP-13-selective inhibitors
-
additional information
-
synthesis of a series of phenyl piperidine alpha-sulfone hydroxamate derivatives, utilizing a combination of solution-phase and resin-bound library technologies, to afford compounds that are potent and highly selective for MMP-13, selectivity analysis compared to other MMPs, overview
-
additional information
-
development of MMP-13 inhibitors mechanistically distinct from previously reported broad-spectrum MMP inhibitors with improved selectivity and pharmacokinetics. Chondroprotective effect of MMP-13-selective inhibitors
-
additional information
-
development and optimization of potent 3,4-disubstituted benzofuran P1' MMP-13 inhibitors, overview
-
additional information
-
development of MMP-13 selective isonipecotamide alpha-sulfone hydroxamate inhibitors, overview
-
additional information
-
selectivity and metabolic stability of non-zinc-chelating MMP-13 inhibitors, overview
-
additional information
discovery of (pyridin-4-yl)-2H-tetrazole as a scaffold to identify highly selective MMP-13 inhibitors for the treatment of osteoarthritis
-
additional information
design, synthesis and biological evaluation of selective matrix metalloproteinase-13 N-O-isopropyl sulfonamido-based hydroxamate inhibitors as potential therapeutic agents for osteoarthritis, docking study and molecular modelling, overview
-
additional information
-
MMP-13 activity is not directly inhibited by the imidazo[5,1-c][1,4]thiazine derivative ITZ-1
-
additional information
-
structure-function relationships of different inhibitor types, overview. No inhibition by 27, i.e. CGS27023A
-
additional information
-
selective inhibition of MMP-13 may be achieved by targeting the hemopexin domain of the protease, which is critical for substrate specificity, systematic cheminformatics-based drug design with virtual screening, overview
-
additional information
-
no inhibition of MMP-13 by MMP-3 inhibitor N-isobutyl-N-[4-methoxyphenylsulphonyl] glycyl hydroxamic acid or by doxycycline
-
additional information
-
orally active and specific matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis. Two series, quinazolinones and pyrido[3,4-d]pyrimidin-4-ones, that are potent and specific MMP-13 inhibitors, some of which are orally bioavailable. These specific MMP-13 inhibitors, occupying the unique S1'-specificity pocket, do not bind to the Zn2+ ion, effectively preventing cartilage damage in animal models of osteoarthritis without inducing musculoskeletal side effects when given at extremely high doses to rats
-
additional information
-
development of MMP-13 inhibitors mechanistically distinct from previously reported broad-spectrum MMP inhibitors with improved selectivity and pharmacokinetics. Chondroprotective effect of MMP-13-selective inhibitors. Effect of MMP-13 inhibition on cartilage degradation in the rat medial meniscal tear model of osteoarthritis, overview
-
additional information
-
MMP-13 activity is not directly inhibited by the imidazo[5,1-c][1,4]thiazine derivative ITZ-1
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12-O-tetradecanoyl phorbol 13-acetate
-
8fold activation of transcriptional activity in chondrocytes
hepatocyte growth factor
-
stimulation of enzyme expression in osteoarthritic chondrocytes
-
interleukin-1
-
alpha and beta form, induction of enzyme expression, which is inhibited by 15-deoxy-DELTA12,14-prostaglandin J2, induction of enzyme expression in chondrosarcoma cells requires nuclear factor-kappaB nuclear translocation, p38 MAPkinase activity, c-Jun N-terminal kinase activity
-
interleukin-1beta
-
activates, hyaluronan inhibits interleukin-1beta-stimulated MMP-13 via CD44 in arthritic chondrocytes
-
p-aminophenylmercuric acetate
-
purified proMMP-13 is activated using 1 mM amino phenyl mercuric acid for 20 h at 35°C
Smad
-
indirect stimulation via regulation of transforming growth factor-beta responsive genes
-
transforming growth factor-beta1
-
strong induction of enzyme expression in KMST fibroblasts, increase of enzyme expression by inhibition of p38 mitose-activated protein kinase
-
Tumor necrosis factor alpha
-
induction of enzyme expression, which is inhibited by 15-deoxy-DELTA12,14-prostaglandin J2
-
additional information
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
-
additional information
-
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
-
additional information
-
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
gelatin
Km value is 0.136 mg/ml, pH 8.0, 37°C
-
additional information
additional information
-
steady-state kinetics analysis, overview
-
additional information
additional information
-
steady-state kinetics analysis, overview
-
additional information
additional information
-
steady-state kinetics analysis, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
or above, pH not specified in the publication, temperature not specified in the publication
0.0029
(2S,3R)-2-[(cyclopropylmethyl)amino]-N1-hydroxy-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-3-methylbutanediamide
or above, pH not specified in the publication, temperature not specified in the publication
0.00000033
1-[4-((4-phenoxy)phenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.0000058
1-[4-(1,3-benzodioxol-5-yloxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.0000019
1-[4-(3-methoxyphenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.00000095
1-[4-(4-chlorophenoxy)phenyl]-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
-
-
0.0000223
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000313
4-([5-[2-(benzylcarbamoyl)-6-methylpyridin-4-yl]-2H-tetrazol-2-yl]methyl)cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.00000028
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
-
pH 7.5
0.0000036
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000075
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000434
4-[(5-[2-[(3,4-difluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.00000026
4-[(5-[2-[(3-chloro-4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000181
4-[(5-[2-[(3-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000067
4-[(5-[2-[(3-cyanobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000286
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000221
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000759
4-[(5-[2-[(3-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000015
4-[(5-[2-[(3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.00000018
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.00000016
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000021
4-[(5-[2-[(3-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.000227
4-[(5-[2-[(4-chlorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000014
4-[(5-[2-[(4-fluoro-3-hydroxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000003
4-[(5-[2-[(4-fluoro-3-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.00000022
4-[(5-[2-[(4-fluoro-3-methylbenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000053
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000044
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000653
4-[(5-[2-[(4-fluorobenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000044
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000042
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]-6-methylpyridin-4-yl]-2H-tetrazol-2-yl)methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000367
4-[(5-[2-[(4-methoxybenzyl)carbamoyl]pyridin-4-yl]-2H-tetrazol-2-yl)methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000005
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
-
pH 7.5
0.0000027
4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoic acid
-
-
0.00000127
4-[carboxy-[5-(4-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
-
pH 7.5
0.0000015
4-[[5-(2-methyl-6-[[3-(propan-2-yloxy)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000025
4-[[5-(2-methyl-6-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.0000165
4-[[5-(2-[[3-(trifluoromethyl)benzyl]carbamoyl]pyridin-4-yl)-2H-tetrazol-2-yl]methyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.00000062
4-[[5-(2-[[4-fluoro-3-(trifluoromethyl)benzyl]carbamoyl]-6-methylpyridin-4-yl)-2H-tetrazol-2-yl]methyl]cyclohexanecarboxylic acid
pH not specified in the publication, temperature not specified in the publication
0.0000003
marimastat
pH not specified in the publication, temperature not specified in the publication
0.0000042
methyl 4-[4-(2,6,8,10-tetraoxo-1,7,9-triazaspiro[4.5]dec-1-yl)phenoxy]benzoate
-
-
0.00000084 - 0.0000015
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
0.00000003
N-hydroxy-2,2-dimethyl-4-[[4-(pyridin-4-yloxy)phenyl]sulfonyl]thiomorpholine-3-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
0.0000058
N-hydroxy-2-(N-isopropoxy-4'-methoxybiphenyl-4-ylsulfonamido)acetamide
pH not specified in the publication, 25°C
0.0000015
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)-L-valinamide
pH not specified in the publication, 25°C
0.00002
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
pH not specified in the publication, 25°C
0.0000015
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
pH not specified in the publication, 25°C
0.0000082
N2-({4'-[(4-chlorobenzyl)oxy]biphenyl-4-yl}sulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
pH not specified in the publication, 25°C
0.00000078
ALS 1-0635
-
pH not specified in the publication, temperature not specified in the publication
-
0.00000078
ALS 1-0635
-
pH not specified in the publication, temperature not specified in the publication
-
0.00000078
ALS 1-0635
-
pH not specified in the publication, temperature not specified in the publication
-
0.00000084
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
0.0000015
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
tissue matrix metalloproteinase inhibitors and fragments
-
additional information
additional information
inhibition kinetics, overview
-
additional information
additional information
-
steady-state inhibition kinetics studies
-
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
0.0000013
(2R)-N,3-dihydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]propanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000012
(2R)-N-hydroxy-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]-2-(tetrahydro-2H-pyran-4-yl)ethanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000033
(2R)-N-hydroxy-3-methyl-2-[(naphthalen-2-ylsulfonyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000029
(2R)-N-hydroxy-3-methyl-2-[methyl(naphthalen-2-ylsulfonyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000028
(2R)-N-hydroxy-4-(4-hydroxyphenyl)-2-[(3-methylbutyl)(naphthalen-2-ylsulfonyl)amino]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
(2R)-[1-(tert-butoxycarbonyl)piperidin-4-yl][([5-[4-(dimethylamino)phenyl]thiophen-2-yl]sulfonyl)amino]ethanoic acid
Homo sapiens
-
pH 7.5
0.00000095
(2R,3R)-4-[[4-(2-chloro-4-fluorophenoxy)phenyl]sulfonyl]-N,2-dihydroxy-2-methylmorpholine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000003
(2S,3R)-1-acetyl-N-hydroxy-2-methyl-4-[[4-(2-methylbenzyl)phenyl]sulfonyl]piperidine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.1
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(2-methoxybenzylidene)-1,3-thiazolidin-4-one
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
(2Z,5E)-2-(1,2-benzothiazol-3-ylimino)-5-(3-methoxybenzylidene)-1,3-thiazolidin-4-one
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.000003
(4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]phenyl)acetic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000003
(4R)-1-[4-(4-fluorophenoxy)benzyl]-N-hydroxy-2-oxoimidazolidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000007
(4S)-4-[4-(4-fluorophenoxy)phenyl]-N-hydroxy-5-oxo-D-prolinamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000041
(E)-2-(4-(2-(biphenyl-4-yl)vinyl)-N-isopropoxyphenylsulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000003
(R)-2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxy-3-methylbutanamide
Homo sapiens
pH not specified in the publication, 25°C
0.0000009
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-cyclohexanecarbonyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000008
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-propylcarbamoyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.000008
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropionyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.000049
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2,2-dimethylpropyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000055
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(2-methylpropane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000036
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(3,3-dimethylbutyryl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000007
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000127
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(methane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000007
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(phenylmethanesulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000069
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.000004
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(propane-2-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000017
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(tetrahydropyran-4-carbonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000076
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-benzylpiperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.000028
(R)-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-iso-butylpiperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000028
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-diethylcarbamoylpiperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.000016
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-iso-butyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000016
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-isopropylcarbamoyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000014
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-(1-tertbutylcarbamoyl-piperidin-4-yl)-acetic acid
Homo sapiens
-
pH 7.5
0.0000012
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(benzenesulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000014
(R)-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-[1-(toluene-4-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000047
(R)-[5-(4-ethoxyphenyl)-thiophene-2-sulfonylamino]-[1-(butane-1-sulfonyl)-piperidin-4-yl]-acetic acid
Homo sapiens
-
pH 7.5
0.0000009
1,5-anhydro-2,3-dideoxy-3-[[4-(2,4-dichlorophenoxy)phenyl]sulfonyl]-4-C-(hydroxycarbamoyl)-D-threo-pentitol
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000033
1-(4-phenoxyphenyl)-1,7,9-triazaspiro[4.5]decane-2,6,8,10-tetrone
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000036
1-(6-[4-[4-(4-fluorophenyl)-1,3-oxazol-2-yl]phenoxy]pyridin-3-yl)-1,7,9-triazaspiro[4.5]decane-6,8,10-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000019
2-(4'-(4-chlorobenzyloxy)-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000015
2-(4'-butoxy-N-isopropoxybiphenyl-4-ylsulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.00026
2-(5-((4-butylphenyl)ethynyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000091
2-(5-(4-ethylphenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.0006
2-(5-(4-fluorophenyl)-N-isopropoxythiophene-2-sulfonamido)-N-hydroxyacetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000036
2-(benzo[d]isothiazol-3-ylimino)-5-(4-methoxybenzylidene)thiazolidin-4-one
Homo sapiens
pH and temperature not specified in the publication
0.0000045
2-(ethyl[[4-(prop-1-yn-1-yloxy)phenyl]sulfonyl]amino)-5-phenylpentane(thioperox)ic O-acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.5
2-butanoyl-1H-indole-5-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000027
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000003
2-chloro-N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000122
2-fluoro-N-hydroxy-6-([4-[4-(trifluoromethoxy)phenoxy]piperidin-1-yl]sulfonyl)benzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
2-[benzyl[(4-methoxyphenyl)sulfonyl]amino]-N-hydroxy-3,5-dimethylbenzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000000016
2-[[(4'-chlorobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000002
2-[[(4'-cyanobiphenyl-4-yl)oxy]methyl]-N-hydroxy-4-(4-oxo-1,2,3-benzotriazin-3(4H)-yl)butanamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000018
2-[[(4'-[[(5-bromo-4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]methyl]-3-methylbutanoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000008
2-[[[4-(4-chlorophenoxy)phenyl]sulfonyl](methyl)amino]-N-hydroxy-3-[(4-methylpiperazin-1-yl)methyl]benzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000009
4-((R)-carboxy-[5-[4'-(2-methoxyethoxy)-phenyl]-thiophene-2-sulfonylamino]-methyl)-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000000069
4-([(2-([(3-methoxyphenyl)methyl]carbamoyl)-4-oxo-3H,4H-thieno[2,3-d]pyrimidin-5-yl)methoxy]methyl)benzoic acid
Homo sapiens
pH 7.5, 37°C
0.0000018
4-([4-[(5-[[4-(dimethylamino)phenyl]amino]-5-oxopentyl)oxy]phenyl]sulfonyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00000672
4-([6-[(4-methoxybenzyl)carbamoyl]-4-oxopyrido[3,4-d]pyrimidin-3(4H)-yl]methyl)benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000003
4-([[4-(4-chlorophenoxy)phenyl]sulfonyl]methyl)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH 7.5
0.0000005 - 0.00000075
4-([[4-(4-fluorophenoxy)phenyl]sulfonyl]amino)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
0.000071
4-oxo-N-[[40-([[(5-oxo-4,5-dihydro-1H-1,2,4-triazol-3-yl)methyl]sulfonyl]methyl)biphenyl-3-yl]methyl]-3,4-dihydroquinazoline-2-carboxamide
Homo sapiens
pH 7.5, 37°C
0.0000082
4-[(4-[3-[(2,2-dimethylpentanoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
4-[(4-[3-[(2,4-dimethylbenzoyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000082
4-[(4-[3-[(cyclohexylcarbonyl)amino]propoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000009
4-[(4-[3-[4-(dimethylamino)phenyl]-3-oxopropoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
4-[(4-[4-[4-(dimethylamino)benzoyl]piperidin-1-yl]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
4-[(4-[4-[4-(dimethylamino)phenyl]-4-oxobutoxy]phenyl)sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.001325
4-[(R)-(benzofuran-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000145
4-[(R)-(benzo[b]thiophene-2-sulfonylamino)-carboxy-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000003
4-[(R)-carboxy-(4'-dimethylamino-biphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-(4'-ethoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000024
4-[(R)-carboxy-(4'-fluorobiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-(4'-methoxybiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000007
4-[(R)-carboxy-(4'-methylbiphenyl-4-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000068
4-[(R)-carboxy-(5-phenylthiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000018
4-[(R)-carboxy-(5-pyridin-2-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.00009
4-[(R)-carboxy-(5-pyridin-4-yl-thiophene-2-sulfonylamino)-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.009
4-[(R)-carboxy-[5-(3',4'-difluorophenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000197
4-[(R)-carboxy-[5-(3',4'-methylenedioxyphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000575
4-[(R)-carboxy-[5-(3,4-dimethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.001058
4-[(R)-carboxy-[5-(3-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000004
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 1-ethyl-propyl ester
Homo sapiens
-
pH 7.5
0.0000004
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid 4-tetrahydropyranyl ester
Homo sapiens
-
pH 7.5
0.0000008
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid cyclohexyl ester
Homo sapiens
-
pH 7.5
0.000002
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid ethyl ester
Homo sapiens
-
pH 7.5
0.0000006
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-butyl ester
Homo sapiens
-
pH 7.5
0.0000005
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000035
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid methyl ester
Homo sapiens
-
pH 7.5
0.0000009
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid neopentyl ester
Homo sapiens
-
pH 7.5
0.000001
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid propyl ester
Homo sapiens
-
pH 7.5
0.0000006
4-[(R)-carboxy-[5-(4'-ethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000033
4-[(R)-carboxy-[5-(4'-hydroxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.000004
4-[(R)-carboxy-[5-(4'-iso-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000006
4-[(R)-carboxy-[5-(4'-methoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000013
4-[(R)-carboxy-[5-(4'-methylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.000011
4-[(R)-carboxy-[5-(4'-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
Homo sapiens
-
pH 7.5
0.0000008
4-[(R)-carboxy-[5-(4'-n-propoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid
Homo sapiens
-
pH 7.5
0.0000013
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.00000075
4-[(R)-carboxy-[5-(4'-piperidin-1-yl-phenyl)-thiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000022
4-[(R)-carboxy-[5-(4'-trifluoromethoxyphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000615
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-furan-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.0000039
4-[(R)-carboxy-[5-(4'-trifluoromethylphenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0000121
4-[(R)-carboxy-[5-phenylthiophene-2-sulfonylamino]-methyl]piperidine-1-carboxylic acid iso-propyl ester
Homo sapiens
-
pH 7.5
0.0017
4-[([3-[(3-methoxybenzyl)carbamoyl]benzoyl]amino)methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00053
4-[([3-[2-(3-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00013
4-[([3-[2-(4-methoxybenzyl)-2H-tetrazol-5-yl]benzoyl]amino)methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.026
4-[([[5-(1H-indol-5-yl)-1-methyl-1H-pyrazol-3-yl]carbonyl]amino)methyl]benzoic acid
Homo sapiens
-
IC50 above 0.026 mM; in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0000000039
4-[2-([6-fluoro-2-[([[3-(methyloxy)phenyl]methyl]amino)-carbonyl]-4-oxo-3,4-dihydroquinazolin-5-yl]oxy)ethyl]-benzoic acid
Homo sapiens
pH 7.5, 37°C
0.00000036
4-[2-[4-(4-[[5-(2-ethoxyethyl)-2,4,6-trioxohexahydropyrimidin-5-yl]oxy]phenoxy)phenyl]-1,3-oxazol-4-yl]benzonitrile
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000019
4-[carboxy-[5-(4-N,N-dimethylaminophenyl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.00005
4-[carboxy-[5-(6-methoxy-pyridin-3-yl)-thiophene-2-sulfonylamino]-methyl]-piperidine-1-carboxylic acid tert-butyl ester
Homo sapiens
-
pH 7.5
0.000001
4-[[([5-[2-(ethoxycarbonyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00025
4-[[([5-[2-(ethoxymethyl)-1H-indol-5-yl]-1-methyl-1H-pyrazol-3-yl]carbonyl)amino]methyl]benzoic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00000067
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
0.0000016
4-[[4-(3-[[4-(dimethylamino)benzoyl]amino]propoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000017
4-[[4-(4-[[4-(dimethylamino)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
4-[[4-([5-[4-(dimethylamino)phenyl]-5-oxopentyl]oxy)phenyl]sulfonyl]-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00000154
4-[[4-oxo-6-(3-phenylprop-1-yn-1-yl)quinazolin-3(4H)-yl]methyl]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00001
5-(2-ethoxyethyl)-5-[4-[4-(1,3,4-oxadiazol-2-yl)phenoxy]phenoxy]pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00039
5-(4-chlorophenoxy)-5-methylpyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00043
5-(4-chlorophenyl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000245
5-(5-chloropyridin-2-yl)-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000078
5-hexyl-5-(4-phenoxyphenoxy)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000065
5-methyl-5-(4-phenoxyphenoxy)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.025
5-[3-[(4-carboxybenzyl)carbamoyl]-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylic acid
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0033
5-[3-[(acetylamino)methyl]phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000006
5-[4-(1-benzofuran-2-ylmethoxy)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00155
5-[4-(acetylamino)phenyl]-N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00003
benzyl 6-benzyl-5,7-dioxo-6,7-dihydro-5H-[1,3]thiazolo[3,2-c]pyrimidine-2-carboxylate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0025
ethyl 5-(1-methyl-1H-imidazol-5-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00012
ethyl 5-(1-methyl-3-[[(6-oxo-1,6-dihydropyridin-3-yl)methyl]carbamoyl]-1H-pyrazol-5-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0096
ethyl 5-(3-methylpyridin-4-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.031
ethyl 5-(acetylamino)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.5
ethyl 5-(pyridin-2-yl)-1H-indole-2-carboxylate
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.015
ethyl 5-(pyridin-3-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.082
ethyl 5-(pyridin-4-yl)-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.039
ethyl 5-carbamoyl-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.5
ethyl 5-phenyl-1H-indole-2-carboxylate
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.097
ethyl 5-[(methylsulfonyl)amino]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00009
ethyl 5-[1-methyl-3-[(pyridin-4-ylmethyl)carbamoyl]-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.0024
ethyl 5-[3-(methoxycarbonyl)-1-methyl-1H-pyrazol-5-yl]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.00015
ethyl 5-[5-methyl-2-[(pyridin-4-ylmethyl)carbamoyl]pyridin-4-yl]-1H-indole-2-carboxylate
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000012
N-(3-methoxybenzyl)-4-oxo-3,4-dihydroquinazoline-2-carboxamide
Homo sapiens
pH 7.5, 37°C
0.0000012 - 0.000002
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
0.0000013
N-([4'-[(1-benzofuran-2-ylcarbonyl)amino]biphenyl-4-yl]sulfonyl)valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000013
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-threonine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000013
N-([4'-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-([4'-[([4-[(1-methoxy-2-methyl-1-oxopropan-2-yl)oxy]-3-methyl-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000149
N-([4'-[([4-[(2-carboxypropan-2-yl)oxy]-1-benzofuran-2-yl]carbonyl)amino]biphenyl-4-yl]sulfonyl)-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000047
N-hydroxy-2,6-dimethoxy-3-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]pyridine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000072
N-hydroxy-2-(N-isopropoxy-4'-(methylthio)biphenyl-4-ylsulfonamido)acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.00001
N-hydroxy-2-(N-isopropoxy-4'-methoxybiphenyl-4-ylsulfonamido)acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000063
N-hydroxy-2-(N-isopropoxy-4-phenoxyphenylsulfonamido)-acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000025
N-hydroxy-2-(N-isopropoxy-5-(4-methoxyphenyl)thiophene-2-sulfonamido)acetamide
Homo sapiens
pH not specified in the publication, 25°C
0.000008
N-hydroxy-2-[(2-methylpropyl)(naphthalen-2-ylsulfonyl)amino]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00018
N-hydroxy-2-[(naphthalen-2-ylsulfonyl)amino]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
N-hydroxy-2-[[(4-methoxyphenyl)sulfonyl](pyridin-3-ylmethyl)amino]-3-methylbenzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000004
N-hydroxy-3-methyl-2-(methyl[[4-(pyridin-4-yloxy)phenyl]sulfonyl]amino)benzamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000034
N-hydroxy-3-methyl-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
N-hydroxy-4-([4-[(4-hydroxybut-2-yn-1-yl)oxy]phenyl]sulfonyl)-2,2-dimethylthiomorpholine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000009
N-hydroxy-4-([4-[4-(4-methoxyphenoxy)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000012
N-hydroxy-4-([4-[4-oxo-4-(piperidin-1-yl)butoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000016
N-hydroxy-4-[(4-[3-[(4-methoxybenzoyl)amino]propoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
N-hydroxy-4-[(4-[4-[(4-methoxyphenyl)amino]-4-oxobutoxy]phenyl)sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00000066
N-hydroxy-4-[[4-(3-[[4-(trifluoromethoxy)benzoyl]amino]propoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000002
N-hydroxy-4-[[4-(4-oxo-4-[[4-(trifluoromethoxy)phenyl]amino]butoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000033
N-hydroxy-4-[[4-(4-[methyl[4-(trifluoromethoxy)phenyl]amino]-4-oxobutoxy)phenyl]sulfonyl]tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
N-hydroxy-4-[[4-(phenylsulfanyl)phenyl]sulfonyl]-1-(prop-2-yn-1-yl)piperidine-4-carboxamide
Homo sapiens
-
IC50 below 1 nM, pH and temperature not specified in the publication
0.000007
N-hydroxy-N2-(2-methylpropyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000006
N-hydroxy-N2-(3-methylbutyl)-N2-(2,3,3a,7a-tetrahydro-1-benzofuran-5-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000026
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-5-phenyl-D-norvalinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000006
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-leucinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000032
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-threoninamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000003
N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000361
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-3-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000012
N-hydroxy-N2-(3-methylbutyl)-N2-(quinolin-6-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
N-hydroxy-N2-(3-methylbutyl)-N2-[(6-propoxynaphthalen-2-yl)sulfonyl]-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000013
N-hydroxy-N2-(3-methylbutyl)-N2-[[6-(2-methylpropoxy)naphthalen-2-yl]sulfonyl]-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000002
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(2-phenylethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000024
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(3-phenylpropyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000022
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-2-ylmethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000015
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-3-ylmethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000007
N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-N2-(pyridin-4-ylmethyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000004
N-hydroxy-N2-methyl-3-[(4-phenoxyphenyl)sulfonyl]-L-alaninamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000001
N-hydroxy-N2-[(6-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000013
N-hydroxy-N2-[(6-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000242
N-hydroxy-N2-[(7-hydroxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00048
N-hydroxy-N2-[(7-methoxynaphthalen-2-yl)sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000018
N-hydroxy-N2-[2-(morpholin-4-yl)ethyl]-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000176
N-hydroxy-N2-[[6-(3-methylbutoxy)naphthalen-2-yl]sulfonyl]-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000075
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(3-[[(furan-2-ylcarbonyl)amino]methyl]phenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000032
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-ethoxyphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00022
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methoxyphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00029
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-methylphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.05
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-(4-phenoxyphenyl)furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[3-([[(2-methylfuran-3-yl)carbonyl]amino]methyl)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000006
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(1H-pyrazol-3-ylmethoxy)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.006
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylcarbamoyl)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00048
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-(methylsulfamoyl)phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000004
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1,5-dimethyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(1-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000002
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(5-methyl-1H-pyrazol-3-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00004
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(6-methylpyridin-2-yl)methoxy]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00046
N-[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]-5-[4-[(methylsulfonyl)amino]phenyl]furan-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000048
N-[(4'-[[(3,4-dimethyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000019
N-[(4'-[[(3-methyl-4-phenoxy-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
N-[(4'-[[(3-methyl-4-phenyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000043
N-[(4'-[[(4-amino-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000037
N-[(4'-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000061
N-[(4'-[[(4-ethenyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000074
N-[(4'-[[(4-ethoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000023
N-[(4'-[[(4-ethyl-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000061
N-[(4'-[[(4-hydroxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000095
N-[(4'-[[(4-methoxy-3-methyl-1-benzofuran-2-yl)carbonyl]amino]biphenyl-4-yl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000035
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-threonine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00004
N-[(4-[5-[([3-methyl-4-[(methylsulfonyl)amino]-1-benzofuran-2-yl]carbonyl)amino]pyridin-2-yl]phenyl)sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.22
N-[2-(4,5-dihydro-1,3-oxazol-2-yl)-1H-indol-5-yl]acetamide
Homo sapiens
-
in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000017
N-[2-(4-[benzyl[2-(hydroxycarbamoyl)-4,6-dimethylphenyl]sulfamoyl]phenoxy)ethyl]-1-benzofuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000072
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1,5-dimethyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00031
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-imidazole-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00014
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-1-methyl-1H-pyrazole-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000007
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-methyl-1,3-thiazole-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00018
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-3-methylpyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000029
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-ethylpyridine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000011
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-5-methylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000009
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000004
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-methylpyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00014
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-7-methylimidazo[1,2-a]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00011
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-8-methylimidazo[1,2-a]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]imidazo[1,2-a]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000042
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000031
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyridine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00001
N-[3-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000036
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000028
N-[3-(5-[[1-cyclopropyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000002
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000002
N-[3-(5-[[2-(methylamino)-2-oxo-1-(tetrahydro-2H-pyran-4-yl)ethyl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000005
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-[3-(5-[[3-hydroxy-3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000009
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-2-(trifluoromethyl)pyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000006
N-[3-(5-[[3-methyl-1-(methylamino)-1-oxobutan-2-yl]carbamoyl]furan-2-yl)benzyl]-6-(trifluoromethyl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00062
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-benzofuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000031
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-1-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000063
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-4,5-dimethylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000088
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000057
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-5-methylfuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000017
N-[4-(5-[[(1S)-1-cyclohexyl-2-(methylamino)-2-oxoethyl]carbamoyl]furan-2-yl)phenyl]-6-methylpyridine-2-carboxamide
Homo sapiens
-
above, pH not specified in the publication, temperature not specified in the publication
0.01
N-[4-(morpholin-4-yl)butyl]-1-benzofuran-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N-[[4'-([[3-methyl-4-(methylamino)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000032
N-[[4'-([[3-methyl-4-(morpholin-4-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000095
N-[[4'-([[3-methyl-4-(prop-1-yn-1-yl)-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000071
N-[[4'-([[4-(3-hydroxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000011
N-[[4'-([[4-(3-methoxypropyl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000025
N-[[4'-([[4-(acetylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000065
N-[[4'-([[4-(dimethylamino)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000064
N-[[4'-([[4-(furan-2-yl)-3-methyl-1-benzofuran-2-yl]carbonyl]amino)biphenyl-4-yl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000009
N-[[4-(4-fluorophenoxy)phenyl]sulfonyl]-N-[1-(hydroxycarbamoyl)cyclopentyl]-b-alanine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000014
N-[[4-(5-[[(4-cyano-3-methyl-1-benzofuran-2-yl)carbonyl]amino]pyridin-2-yl)phenyl]sulfonyl]-L-valine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000096
N2,N5-bis(3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
Homo sapiens
pH 7.5, 22°C
0.000068
N2,N5-bis(4-fluoro-3-methylbenzyl)-6-oxo-1,6-dihydropyrimidine-2,5-dicarboxamide
Homo sapiens
pH 7.5, 22°C
0.00000005
N2-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000018
N2-(3a,7a-dihydro-1-benzothiophen-5-ylsulfonyl)-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000039
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(2-methylpropyl)glycinamide
Homo sapiens
pH not specified in the publication, 25°C
0.000045
N2-(biphenyl-4-ylsulfonyl)-N-hydroxy-N2-(propan-2-yloxy)glycinamide
Homo sapiens
pH not specified in the publication, 25°C
0.0000028
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
Homo sapiens
pH not specified in the publication, 25°C
0.000038
N2-benzyl-N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
N2-ethyl-1H-indole-2,5-dicarboxamide
Homo sapiens
-
IC50 above 0.5 mM, in 100 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM CaCl2, and 0.05% (v/v) Brij 35, and 1% (v/v) DMSO, at 28°C
0.000014
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl]-N,3-dimethyl-L-valinamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
N2-[(2S)-2-[[(4-benzylbenzyl)(hydroxy)phosphoryl]methyl]-6-phenoxyhexanoyl]-N,3-dimethyl-L-valinamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.003892
N2-[(3,4-dimethoxyphenyl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000036
N2-[(6-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000003
N2-[(6-ethylnaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000603
N2-[(7-ethoxynaphthalen-2-yl)sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000032
N2-[2-(dimethylamino)ethyl]-N-hydroxy-N2-(naphthalen-2-ylsulfonyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000165
N2-[[6-(benzyloxy)naphthalen-2-yl]sulfonyl]-N-hydroxy-N2-(3-methylbutyl)-D-valinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0000022
O-tert-butyl-N-hydroxy-N2-(3-methylbutyl)-N2-(naphthalen-2-ylsulfonyl)-D-serinamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000001
SC-276
Homo sapiens
-
IC50 above 1 nM, pH and temperature not specified in the publication
0.0000005
4-([[4-(4-fluorophenoxy)phenyl]sulfonyl]amino)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000075
4-([[4-(4-fluorophenoxy)phenyl]sulfonyl]amino)-N-hydroxytetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000067
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00000067
4-[[1-methyl-2,4-dioxo-6-(3-phenylprop-1-yn-1-yl)-1,4-dihydroquinazolin-3(2H)-yl]methyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0000066
N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000008
N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000012
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication, versus full-length bovine type II collagen
0.000002
N-(4-fluoro-3-methoxybenzyl)-6-(2-(((2S,5R)-5-(hydroxymethyl)-1,4-dioxan-2-yl)methyl)-2H-tetrazol-5-yl)-2-methylpyrimidine-4-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication, versus full-length bovine type II gelatin
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity of enzyme and enzyme fragment with synthetic peptide substrates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
-
712837, 712838, 712839, 712849, 712933, 713161, 713163, 713164, 713176, 713178, 713372, 713497, 713548, 719033, 719055, 719056, 719062
-
-
brenda
-
SwissProt
brenda
recombinant procollagnase expressed in NSO mouse myeloma cells and secreted to the medium
SwissProt
brenda
-
-
-
brenda
mice deficient in apolipopotein E (apoE -/-) in a C57BL/6J background
-
-
brenda
-
-
-
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
-
healthy and elastase-perfused aortas. Increased MMP-13 in experimental abdominal aortic aneurysms in males compared with females, while there are no differences in aortic diameter, collagen, and MMP-13 levels in baseline males versus females, MMP-13 expression analysis, overview
brenda
-
myoblast cell line, expression of enzyme and tissue inhibitor of matrix metalloproteinase, TIMP-1, is regulated by Wnt signaling combined with bone morphogenic protein BMP-2 in osteoblastic differentiation
brenda
-
MMP-13 is the only enzyme whose induction and expression coincides with the onset of angiogenesis and blood vessel formation. MMP-13-positive cells appear shortly after angiogenic stimulation and then accumulate in the collagen onplant tissue. Morphologically, the chMMP-13-containing cells appear as hematopoietic cells of monocyte/macrophage lineage
brenda
-
from maxillary and mandibular jaws, semi-quantitative RT-PCR analysis, overview
brenda
-
MMP-13 real-time RT-PCR expression analysis, overview
brenda
-
expression of MMP-13 increases following the gonadotropin surge. MMP-13 is localized to granulosal and thecal layers
brenda
-
from keratocyst odontogenic tumours, stromal tissue and mesenchymal cells, distribution of MMP-13 expression, overview
brenda
-
MMP-13 expression in the tissues around in vivo developing oral sulcus at E11, 12, and 13, immunohistochemic analysis
brenda
-
MMP-13 is mainly produced by neurons, but also by oligodendrocytes
brenda
-
MMP-13 in perivascular cells may be involved in removal of cartilage matrix proteins such as type II collagen and aggrecan
brenda
-
expression of MMP13 in the synovial membrane of patients with rheumatoid and osteoarthritis
brenda
-
high expression of MMP13 in rheumatoid arthritis synovial tissue
brenda
-
nearly all chondrocyte-like cells are immunopositive, whereas fibroblast-like cells and fibrochondrocytes are more rarely labelled
brenda
additional information
-
enzyme is expressed during both intramembranous ossification in skull and endochondral ossification in long bones during gestation
brenda
-
subchondral bone, mRNA expressions of matrix metalloproteinase-13 is significantly enhanced in osteoarthritis subchondral bone osteoblasts compared to subchondral bone osteoblasts without osteoarthritis. The expression of these gene is greater in patients with severe cartilage damage than in those with mild cartilage damage
brenda
-
mRNA encoding MMP13 is present in multiple cell types involved in human fetal bone development
brenda
-
MMP13 is expressed by hypertrophic chondrocytes and osteoblasts in the fracture callus
brenda
-
surfaces under the ruffled borders and some clear zones of osteoclasts. MMP-13 may play an important role in the degradation of type I collagen in bone matrix, acting in concert with cathepsin K and MMP-9 produced by osteoclasts
brenda
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upregulation of active MMP-13 in rat brains after 90 min of cerebral ischemia
brenda
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upregulation of active MMP-13 in rat brains after 90 min of cerebral ischemia
brenda
-
femoral condyles and tibial plateaus, preferential expression of MMP-13 in the deep zone
brenda
-
articular, from osteoarthritis and rheumatoid arthritis patients
brenda
-
obtained from patients with rheumatoid arthritis and osteoarthritis. CCAAT/enhancer binding protein beta, i.e. C/EBPbeta, and MMP-13 expressions are colocalized in chondrocytes in arthritic cartilage
brenda
-
healthy and osteoarthritic, MMP-13 RT-PCR expression analysis, overview
brenda
hypertrophic, enzyme expression during bone development
brenda
-
expression by fibroblasts inadult gingival and in fetal skin wounds characterized by rapid collagen remodeling and scarless healing
brenda
-
during experimental gastric ulcer healing induced by acetic acid injection MMP-3 and MMP-3 expression is increased in stromal cells of the gastric mucosa bordering the ulcer. MMP-13 RNAs are confined to the upper layers of the granulation tissue
brenda
MMP-13 is the principal proteinase expressed by the mesenchymal stromal cells of giant cell tumor
brenda
-
from healthy subjects, patients with gingivitis, and with periodontitis, immunohistochemic analysis, overview
brenda
-
scar-associated macrophages are a major source of hepatic matrix metalloproteinase-13
brenda
-
MMP-13 is mainly produced by neurons, but also by oligodendrocytes
brenda
-
arthritic, from osteoarthritis and rheumatoid arthritis patients, the level of MMP-13 is higher in rheumatoid arthritis than in osteoarthritis samples. MMP-13 levels are highly associated with vascular endothelial growth factor levels in both osteoarthritis and rheumatoid arthritis fluids
brenda
-
from healthy persons and rheumatoid arthritis patients, the latter show a higher MMP-13 level
brenda
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epithelial-myoepithelial, immunohistochemic determination of MMP-13 and other MMPs, overview. The overall level of MMP-13 is low, thereby the average indices of MMP-13 in epithelial cells are higher than in myoepithelial cells
brenda
-
expression by fibroblasts in adult gingival and in fetal skin wounds characterized by rapid collagen remodeling and scarless healing
brenda
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MMP-13 expression is negligible in the normal unwounded skin at day 0, but it increases on days 1 to 7 upon wounding, diminishes on day 14 and disappears on day 28
brenda
-
high levels of MMP13 mRNA only in malignant squamous epithelium of the skin, while premalignant and benign tumors are mostly negative for MMP13
brenda
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enzyme expression is related to tumor aggresiveness
brenda
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induced tumors, stromal MMP13 is associated with vascular endothelial growth factor receptor-2 on endothelial cells in invasive areas. Tumour invasion was downregulated in Mmp13-/- animals. Kinetics of angiogenesis and tumour growth in surface transplants, overview
brenda
-
from healthy persons and rheumatoid arthritis patients, the latter show a higher MMP-13 level
brenda
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interleukin-1beta-stimulated rheumatoid arthritis fibroblast-like, semi-quantitative RTPCR MMP-13 expression analysis
brenda
additional information
immunohistochemic MMP13 expression analysis
brenda
additional information
-
MMP-13 is expressed in osteoarthritis and rheumatoid arthritis patients, but not in normal adult tissues
brenda
additional information
-
MMP-13 quantitative real-time PCR expression analysis, overview
brenda
additional information
-
MMP-13 real-time PCR expression analysis, overview
brenda
additional information
Mmp13 is expressed in human neovascular membranes
brenda
additional information
-
Mmp13 is expressed in human neovascular membranes
brenda
additional information
-
no MMP-13 expression in THP-1 cells, HL-60 cells, and Jurkat cells
brenda
additional information
-
quantitative real-time PCR MMP-13 expression analysis
brenda
additional information
-
the levels of MMP-13 in gingival crevicular fluid samples are not influenced by diabetes mellitus type 2, overview
brenda
additional information
MMP-13 pattern of expression in various healthy tissues and during embryogenesis, MMP-13 expression is slightly increased in the first day post-fertilization and sharply up-regulated from 1-day postfertilization through hatching, quantitative RT-PCR analysis, overview
brenda
additional information
-
MMP-13 pattern of expression in various healthy tissues and during embryogenesis, MMP-13 expression is slightly increased in the first day post-fertilization and sharply up-regulated from 1-day postfertilization through hatching, quantitative RT-PCR analysis, overview
brenda
additional information
-
expression analysis of MMP13 in healthy and wounded skin, overview
brenda
additional information
-
MMP-13 mRNA abundance is greatly enhanced in Hdac4-deficient mice compared with wild-type or heterozygous littermates. MMP-13 staining in the tibiae of knockout mice is strongly detected in late hypertrophic chondrocytes and bone regions compared with wild-type or heterozygous mice
brenda
additional information
-
Mmp13 is expressed in mouse choroidal neovascular lesions induced by laser burn
brenda
additional information
-
MMP13 is upregulated at the breast tumor-bone interface, gene expression profiling, overview
brenda
additional information
-
realtime RT-PCR MMP13 expression analysis, overview
brenda
additional information
-
Mmp13 is expressed in mouse choroidal neovascular lesions induced by laser burn
-
brenda
additional information
-
osteoblastic osteosarcoma cell line UMR 106-01, Ca2+-dependent binding in a two-step mechanism via the required specific enzyme receptor and LDL-receptor-related protein, internalization and degradation of the enzyme, also binding to fibroblastic cells
brenda
additional information
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ibuprofen upregulates expressions of MMP-13 both at mRNA and protein levels
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
gold-labeled MMP-13 is closely associated with collagen fibrils
-
brenda
additional information
-
interleukin-1 at 2 ng/ml stimulates the secretion of MMP-13 in both osteoarthritis or rheumatoid arthritis chondrocytes
-
brenda
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secretion of MMP-13 protein to the culture supernatant of chondrocytes
-
brenda
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hypoxia increases MMP-13 protein secretion from astrocytes
-
brenda
-
-
brenda
-
-
brenda
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MMP-13 activation and its nuclear translocation is an early consequence of an ischemic stimulus
brenda
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MMP-13 activation and its nuclear translocation is an early consequence of an ischemic stimulus
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
metabolism
-
interleukin-1beta treatment induces COX-2 and MMP-13 expressions in association with activation of ERKs, p38 MAPK, JNKs, and NF-kappaB in skin fibroblasts. Phorbol-12-myristate-13-acetate treatment also induces COX-2 and MMP-13 expressions in association with p38 MAPK activation. Glucosamine-hydrochloride differentially downregulates COX-2 andMMP-13 expression in the interleukin-1beta- or phorpbol-12-myristate-13-acetate-treated skin fibroblasts via the p38 MAPK-independent COX-2 translational inhibition and the p38 MAPK-dependent MMP-13 transcriptional suppression, respectively
metabolism
-
the activation of MMP-13 expression by T3 is in a competitive balance with the regulation of osteocalcin expression, overview
metabolism
-
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
metabolism
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
physiological function
-
functional role of MMP13 in tumor-induced osteolysis, MMP-13 regulates mammary tumor-induced osteolysis by activating MMP9 and transforming growth factor-beta signaling at the tumor-bone interface
physiological function
-
inhibition of MMP-13 reduces resorptive activity of the cells indicating that MMP-13 likely plays an important role in bone giant cell tumor. Mesenchymal stromal cells and the multinucleated giant cells cell-cell cooperation involves giant cell-derived cytokine up-regulation of MMP-13 in the stromal cells, which in turn assists the giant cells in bone resorption
physiological function
-
inhibition of MMP-13 reduces resorptive activity of the cells indicating that MMP-13 likely plays an important role in bone giant cell tumor. Mesenchymal stromal cells and the multinucleated giant cells cell-cell cooperation involves giant cell-derived cytokine up-regulation of MMP-13 in the stromal cells, which in turn assists the giant cells in bone resorption
physiological function
-
involvement of MMP-13 and upregulation in the Cyr61-directed chondrosarcoma cells migration, the upregulation of MMP-13 is antagonized by decoy agonist AP-1-binding site, AP-1 oligonucleotide, but not by NF-kappaB oligonucleotide or scrambled oligonucleotide, as well as by RGD, PD98059 and FAK(Y397F) and ERK2 mutant
physiological function
-
MMP-13 acts as an inflammatory mediator in age-related osteoarthritis
physiological function
-
MMP-13 can initiate bone resorption and activate proMMP-9 in vitro, and both these MMPs are widely implicated in tissue destruction associated with chronic periodontitis, with proteolytic roles of MMP-13 during progression of chronic periodontitis, overview
physiological function
-
MMP-13 efficiently degrades proteoglycans and type II collagen in articular cartilage and may therefore play a central role in articular cartilage degradation
physiological function
MMP-13 is a key enzyme implicated in the degradation of the extracellular matrix in osteoarthritis
physiological function
-
MMP-13 is a key regulator involved in cancer, cellular movement, connective tissue disorders, and in cellular growth and proliferation, cellular assembly and organization, cellular movement, hierarchical cluster analysis of key regulator genes, overview
physiological function
-
MMP-13 is a matrix metalloproteinase that is important for bone development and remodelling
physiological function
MMP-13 is a proteolytic enzyme that plays a key role in degradation and remodelling of host extracellular matrix proteins
physiological function
MMP-13 is involved in extracellular matrix remodeling
physiological function
-
MMP-13 is involved in the degradation of extracellular matrix in many kinds of tissues. MMP-13 is an important factor leading to the disorganization of ZO-1, destruction of ZO-1 tight junction protein, and hyperpermeablility of blood-brain barrier in response to hypoxia. Hypoxia-induced MMP-13 expression in astrocytes enhances paracellular permeability of brain endothelial cells
physiological function
-
MMP-13 is involved in the mechano-transduction in periodontal ligament cells, that is crucial for physiological and orthodontic tooth movement-associated periodontal remodelling
physiological function
-
MMP-13 loss associated with impaired extracellular matrix remodeling disrupts chondrocyte differentiation by concerted effects on multiple regulatory factors. MMP-13 loss alone impedes the differentiation of primary chondrocyte micromasses by inhibiting the expression or activation of multiple regulatory factors including runt-related transcription factor 2, RUNX-2, vascular endothelial growth factor, VEGF, and beta-catenin, and enhances chondrocyte viability. The inhibitory effects of MMP-13 ablation on several principal regulators of chondrocyte maturation toward a hypertrophic-like state occurr in conjunction with diminished type X collagen expression
physiological function
-
MMP-13 participate in the bone-remodeling mechanism involving the platelet-derived growth factor receptor
physiological function
-
MMP-13 plays a critical role in parathyroid hormone-induced bone resorption
physiological function
-
MMP13 affects the keratinocyte migration in the skin, overview. Connective tissue growth factor, CTGF, blocks angiogenic activity of vascular epithelial growth factor, VEGF, by complex formation, and MMP13 re-activates VEGF activity through selective cleavage of CTGF in the complex
physiological function
MMP13 catalyzes the degradation of extracellular matrix components in the growth plate and at the same time cleaves and releases biologically active molecules stored in the extracellular matrix, such as the vascular endothelial growth factor A
physiological function
-
MMP13 catalyzes the degradation of extracellular matrix components in the growth plate and at the same time cleaves and releases biologically active molecules stored in the extracellular matrix, such as the vascular endothelial growth factor A. In mice, ablation of Mmp9, Mmp13, or both Mmp9 and Mmp13 causes severe distortion of the metaphyseal growth plate
physiological function
-
MMP13 has an essential role in highly malignant and invasive growth in skin squamous cell carcinoma. Lack of host MMP13 strongly impairs implanted tumour growth of malignant skin squamous cell carcinoma cells, leading to small, mostly avascular cysts. MMP13 is essential for maintenance of angiogenesis and for invasion
physiological function
-
MMP13 plays a critical role in the redifferentiation phase of kidney development. Potential role of MMP13 in endochondral and intramembranous ossification, with a functional role in skeletal development. MMP13 plays a significant role in the cartilage collagen degradation that occurs in osteoarthritis, and a pathological role of the degradative MMP13 enzyme in rheumatoid arthritis. The catalytic activity of MMP13 may play a role in the high invasion capacity of these cancer cells. Degradation of basement membrane is thought to be an early and critical event influencing tumor invasion and metastasis. MMP13 plays a role in proteolytic activity in invasive malignant growth
physiological function
-
MMPs are important regulators of tissue remodeling and repair
physiological function
-
the MMP-13 knockout phenotype, which is due to an inability of chondrocytes to exit the growth plate, resolves completely by 12 weeks of age, suggesting that other (collagen degrading) proteases can at least partially functionally substitute for MMP13 in this developmental role
physiological function
-
tMMP-13 is responsible for cartilage proteoglycan degradation in rat synovial joints
physiological function
-
MMP-13 activity is necessary for normal skeletal development and plays a central role in cartilage degeneration associated with osteoarthritis
physiological function
-
MMP13 mediates cell proliferation in melanocytes and melanoma cells. Growth stimuli are mediated via MMP13 in melanocytes and melanoma
physiological function
-
MMP13 mediates cell proliferation in melanocytes and melanoma cells. Growth stimuli are mediated via MMP13 in melanocytes and melanoma
physiological function
-
in a larval zebrafish model, glucose treatment induces sensory axon degeneration, which is mediated by ROS formation in the skin, and ROS-dependent MMP13 activation. Glucose-induced sensory axon degeneration is prevented upon pharmacological inhibition of ROS with N-acetylcysteine, and upon pharmacological MMP13 inhibition
physiological function
neuropathy is reversed upon injection of MMP13 inhibitor into obese mice on a high-fat/high sugar diet
additional information
-
age-related accumulation of advanced glycation end products can activate chondrocytes and induce the production of proinflammatory cytokines and matrix metalloproteinases
additional information
-
ALK1 and Alk5 are involved in MMP-13 activity regulation, age-related shift in ALK1/ALK5 ratio in murine cartilage. A change in balance between ALK5 and ALK1 receptors in chondrocytes causes changes in MMP-13 expression, thereby causing an osteoarthritis-like phenotype
additional information
-
angiotensin II promotes a stable fibrotic phenotype by inducing severe intra-plaque hemorrhages, characterized by increased degradation of interstitial collagen I via an MMP13 or MMP8-mediated mechanism, overview
additional information
-
cartilage ALK1 is highly correlated with MMP-13 expression, whereas ALK5 correlates with aggrecan and collagen type II expression. Strong correlation between ALK1 and MMP-13 expression in human cartilage
additional information
-
cartilage structural damage in osteoarthritis in mice is dependent on MMP13 activity
additional information
-
chloramphenicol-induced MMP-13 expression is strongly associated with metastatic capacity of solid-tumor cells
additional information
-
clinical outcomes of periodontal treatment and gingival crevicular fluid MMP-13 levels in MMP-13 genotype subjects, overview
additional information
-
down-regulation of MMP13, Birc2, or Birc3 results in reduced tumor growth when transplanted into immunodeficient recipient mice, high MMP13 expression enhances osteosarcoma cell survival
additional information
-
down-regulation of MMP13, Birc2, or Birc3 results in reduced tumor growth, while high MMP13 expression enhances osteosarcoma cell survival
additional information
-
high MMP13 expression is correlated with poor prognosis and reduced median overall survival in patients with head and neck cancer. High MMP13 levels in patients with salivary gland cancer are also associated with poor survival. And high levels of tumor-derived MMP13 correlate with poor prognosis in invasive breast cancer and reduced overall survival
additional information
-
in addition to phosphorylation of Elk-1, dynamic posttranslational modification of Elk-1 by small ubiquitin-related modifier, SUMO, serves as an important mechanism through which MMP-13 gene expression is regulated
additional information
-
interleukin-1beta-induced activation of signal transduction pathways associated with the expression of MMP-13 downregulates the expression of miR-27b micro-RNA. Thus, miR-27b may play a role in regulating the expression of MMP-13 in human chondrocytes, with negative regulation of miR-27b expression by activation of NF-kappaB
additional information
-
kinetics of MMP13 mRNA expression and tumor-induced osteolysis
additional information
-
lack of transcription-translation coupling on MMP-13 expression in experimental periodontal disease
additional information
-
matrix metalloproteinase-13 expression associates to cisplatin resistance in head and neck cancer cell lines
additional information
-
miRNAs miR-140 and miR-27a act as regulators of the MMP-13 and IGFBP-5 genes, expression regulation in normal and osteoarthritic chondrocytes, detailed overview
additional information
-
MMP-13 expression is increased in rheumatoid arthritis and osteoarthritis
additional information
-
MMP-13 levels in vitro and extracellular matrix remodeling in vitro and in vivo are linked to changes in SOX9 subcellular localization, loss of MMP-13 or IKKalpha leads to the nuclear localization of SOX9. IKKalpha ablation in articular chondrocytes stabilizes their extracellular matrix by posttranscriptionally suppressing MMP-13 activity, thereby blocking their differentiation and maintaining them in an early periarticular-like state
additional information
-
MMP-13 overexpression in stromal tissue of non-nevoid basal cell carcinoma syndrome-associated keratocyst odontogenic tumours explains the higher aggressiveness of these cysts
additional information
MMP13 involvement in age-related macular degeneration
additional information
-
Obedience in the expression of MMP-13 as extracellular matrix remodelling executioner from the activation state of mechano-transducing molecules. The transcription factor c-fos is a constituent of the AP1-complex addressing the MMP-13 promotor. Role of activated MAP-kinases pp38 and pp42/44 in strain-induced expression of the active form of MMP-13, activated, phosphorylated p42/44 and p38 are responsible for the expression of MMP-13, overview
additional information
osteoarthritis, involving MMP-13, is a degenerative joint disease characterized by the erosion of articular cartilage leading to pain and reduced mobility
additional information
-
potential role of MMP13 in choroidal angiogenesis in a murine model of laser-induced ocular neovascularisation. Deficiency of Mmp13 impaires choroidal neovascularization formation which is fully restored by wild-type bone marrow engraftment and partially rescued by several injections of wild-type mesenchymal stem cells. Mmp13 deficiency not only affects vessel recruitment, but also impairs their maturation through pericyte coverage
additional information
-
protective effects of tetracycline compounds are more pronounced in synoviocytes than cartilage, and following minocycline compared to doxycycline, molecular mechanism of action, overview
additional information
-
the ING2-HDAC1-mSin3A complex members regulates expression of MMP13. Upregulation of ING2 is associated with colon cancer and MMP13-dependent cellular invasion
additional information
-
potential role of MMP13 in choroidal angiogenesis in a murine model of laser-induced ocular neovascularisation. Deficiency of Mmp13 impaires choroidal neovascularization formation which is fully restored by wild-type bone marrow engraftment and partially rescued by several injections of wild-type mesenchymal stem cells. Mmp13 deficiency not only affects vessel recruitment, but also impairs their maturation through pericyte coverage
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A142EHU4_CERNI
179
0
20063
TrEMBL
other Location (Reliability: 5)
MMP13_RAT
466
0
53375
Swiss-Prot
Chloroplast (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 35000, enzyme fragment 249-451, SDS-PAGE, x * 24000, mature enzyme, SDS-PAGE
35000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 35000, enzyme fragment 249-451, SDS-PAGE, x * 24000, mature enzyme, SDS-PAGE
48000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 48000, mature enzyme, SDS-PAGE
50000
60000
50000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 35000, enzyme fragment 249-451, SDS-PAGE, x * 24000, mature enzyme, SDS-PAGE
50000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 48000, mature enzyme, SDS-PAGE
60000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 35000, enzyme fragment 249-451, SDS-PAGE, x * 24000, mature enzyme, SDS-PAGE
60000
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 48000, mature enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 35000, enzyme fragment 249-451, SDS-PAGE, x * 24000, mature enzyme, SDS-PAGE
?
-
x * 60000, proform, SDS-PAGE, x * 50000, intermediate partially processed form, SDS-PAGE, x * 48000, mature enzyme, SDS-PAGE
additional information
recombinant catalytic enzyme fragment complexed with a hydroxamic acid inhibitor, NMR structure determination
additional information
-
recombinant catalytic enzyme fragment complexed with a hydroxamic acid inhibitor, NMR structure determination
additional information
recombinant catalytic enzyme fragment complexed with a non-peptidic sulfonamide, hydroxamic acid inhibitor CGS 27023, NMR structure determination
additional information
-
recombinant catalytic enzyme fragment complexed with a non-peptidic sulfonamide, hydroxamic acid inhibitor CGS 27023, NMR structure determination
additional information
structure and peptide organization, three-dimensional modeling
additional information
-
structure and peptide organization, three-dimensional modeling
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
autoproteolysis resulting in two N-glycosylated 29 kDa fragments and one 27 kDa fragment, processing of enzyme proform via a short-living intermediate form to the active form with Tyr85 at its N-terminus
proteolytic modification
-
cleavage by trypsin is not effective, processing of the 60 kDa procollagenase 3 by stromelysin or by p-aminophenylmercuric acetate to form an intermediate of 50 kDa, further processing by cleavage of the peptide bond Glu84-Tyr85 resuls in the active 48 kDa mature form, overview
proteolytic modification
-
stromelysin-1 can activate the enzyme by cleavage of the Glu57-Leu58 bond of the proform resulting in formation of an intermediate of 50 kDa which is further processed to the 48 kDa active mature form, inactive proform can be activated in 3 different ways: 1. autoproteolytically, 2. via cleavage by several other matrix metalloproteases, 3. in a three-step process using aminophenylmercuric acetate
proteolytic modification
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
proteolytic modification
-
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a complex of human MMP-13 with bovine TIMP-2 is crystallized using the sitting-drop vapour diffusion method in 100 mM MES (pH 6.5), 200 mM magnesium acetate, 20% (w/v) PEG 8000
comparison of more than 40 X-ray co-crystal structures of the human MMP-13 with bound inhibitors to gain the structural insights such as conserved direct interactions with binding site residues, namely Ala-238, Thr-245 and Thr-247. Docking-based screening of existing drugs and binding free-energy calculation suggests eltrombopag, cilostazol and domperidone as potential MMP-13 inhibitors
crystal structures of catalytically inactive full-length MMP-13 mutant E223A in complex with peptides of 14-26 amino acids derived from the cleaved prodomain during activation. Peptides are bound to the active site of the enzyme by forming an extended beta-strand with Glu40 or Tyr46 inserted into the S1' specificity pocket
enzyme catalytic domain in complex with inhibitor N,N'-bis(pyridin-3-ylmethyl)pyrimidine-4,6-dicarboxamide, N,N'-bis(3-methylbenzyl)pyrimidine-4,6-dicarboxamide or N,N'-bis(4-fluoro-3-methylbenzyl)pyrimidine-4,6-dicarboxamide
hanging drop vapor diffusion method, using 10% (w/v) PEG4000, 1 M ammonium formate, and 100 mM Tris, pH 8.0
-
in complex with inhibitor SM-25453, comparison with structure of EC 3.4.24.17 with inhibitor
molecular dynamics simulations and multiway explorative data analysis on MMP13 complexed with Marimastat and two cis-1(S)2(R)-amino-2-indanol ligands, and comparison with proteases ADAMTS4, ADAMTS5. Determinant characteristics for ligand binding and selectivity among the three enzymes are to be found in the different protein conformation flexibility
molecular modeling of binding of homochiral (3S,3S)-astaxanthin to enzyme
recombinant enzyme, hanging-drop vapour diffusion method, 20 mM Tris-HCl, pH 7.3, 5 mM CaCl2, 300 mM NaCl, addition of 1 M ammonium sulfate solution, pH 9.0, equilibrated against ammonium sulfate at 1.2 M, 20°C, 1 week, X-ray structure determination at 2.7 A resolution and analyis of the C-terminal haemopexin-like domain
enzyme complexed with a hydroxamate inhibitor, hanging-drop vapour diffusion method, 17 mg/ml protein in 10 mM HEPES, pH 7.5, with ammonium sufate to saturation, 18°C, 60 days, X-ray diffraction structure determination at 2.0 A resolution, and analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F55S
naturally occuring dominant mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
H213N
naturally occuring recessive mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
M1K
naturally occuring recessive mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
M72T
naturally occuring dominant mutation and cloning by site-directed mutagenesis, the mutation is involved in metaphyseal anadysplasia
additional information
additional information
-
truncated enzyme form comprising the amino acid residues 249-451 shows no triple helicase activity against collagen type I and II
additional information
-
identification of MMP-13 promoter polymorphisms in severe, generalized chronic periodontitis patients, genotypes and gingival crevicular fluid MMP-13 level with MMP-13 genotype correlation, overview
additional information
identification of mutations in MMP13 as the molecular basis of metaphyseal anadysplasia, MAD, overview. Recessive MAD is caused by homozygous loss of function of either MMP9 or MMP13, whereas dominant MAD is associated with missense mutations in the prodomain of MMP13 that determine autoactivation of MMP13 and intracellular degradation of both MMP13 and MMP9, resulting in a double enzymatic deficiency, phenotypes, overview
additional information
-
identification of mutations in MMP13 as the molecular basis of metaphyseal anadysplasia, MAD, overview. Recessive MAD is caused by homozygous loss of function of either MMP9 or MMP13, whereas dominant MAD is associated with missense mutations in the prodomain of MMP13 that determine autoactivation of MMP13 and intracellular degradation of both MMP13 and MMP9, resulting in a double enzymatic deficiency, phenotypes, overview
additional information
-
knockdown of MMP-13 by stable retrotransduction of short hairpin RNA leads to impaired ECM remodeling and suppressed differentiation in conjunction with reduced levels of RUNX-2, beta-catenin, and vascular endothelial growth factor, VEGF
additional information
-
enzyme-null mice show profound defects in growth plate cartilage with markedly increased hyperthrophic domains and delay in indochondrial ossification and formation and vascularization of primary ossification centers. Cartilaginous growth plate abnormalities persist in adult animals and phenocopy defects observed in human hereditary chondrodysplasis
additional information
-
generation of MMP13 and MMP13/MMP9 knockout mice, that all show delayed wound closure compared to wild-type mice. The rate of re-epithelialization is significantly delayed in MMP-9 KO and MMP-13 KO mice and remarkably delayed in MMP-9/13 double KO mice, phenotype, overview
additional information
-
identification of mutations in MMP13 as the molecular basis of metaphyseal anadysplasia, MAD, overview. Recessive MAD is caused by homozygous loss of function of either MMP9 or MMP13, whereas dominant MAD is associated with missense mutations in the prodomain of MMP13 that determine autoactivation of MMP13 and intracellular degradation of both MMP13 and MMP9, resulting in a double enzymatic deficiency
additional information
-
knockdown of MMP13 expression at the tumor-bone interface leads to significant reduction in bone destruction and in the number of activated osteoclasts at the tumor-bone interface
additional information
-
MMP13 knockout mice are viable, healthy, and grossly normal. The absence of MMP13, however, delays the endochondral ossification process of skeletal development, knockout phenotype, overview. The mutant mice show hypertrophic chondrocytes within the articular cartilage of trabecular bone that is due to impaired remodeling of the extracellular matrix, and they show reduced apoptosis of the hypertrophic chondrocytes. Tibial cartilage erosion does not progress with time in MMP13 knockout mice
additional information
-
generation of a -148 rat MMP-13 promoter construct and a mutation construct of pGL2-MMP-13 promoter by site-directed mutagenesis. MMP-13 knockout by siRNA in UMR106-01 cells
additional information
-
hypoxia-induced MMP-13 overexpression is antagonized by transfection with antisense oligodeoxynucleotides of c-Fos or c-Jun. Transfection of MMP-13-shRNA markedly antagonizes the proteolysis of ZO-1 induced by hypoxic-conditioned medium
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the recombinant catalytic enzyme fragment complexed with a non-peptidic sulfonamide inhibitor CGS 27023 is stable up to 45°C, denaturation and precipitation occurs at temperatures exceeding 50°C
additional information
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the recombinant catalytic enzyme fragment complexed with a non-peptidic sulfonamide inhibitor CGS 27023 is stable up to 45°C, denaturation and precipitation occurs at temperatures exceeding 50°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a fragment of human MMP-13 corresponding to residues 104-274 is expressed in Escherichia coli BL21(DE3) cells
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activation by aminophenylmercuric acetate, expression of procollagenase 3 and a C-terminal truncated form of procollagenase 3 comprising amino acid residues 249-451 in mouse myeloma cells, secretion to the cell culture medium
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DNA and amino acid sequence determination and analysis, quantitative RT-PCR analysis expression analysis, overview. Phylogenetic analysis
expression in Escherichia coli
expression of procollagenase 3 in NSO mouse myeloma cells, secretion to the medium
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expression of the catalytic enzyme fragment in Escherichia coli BL21(DE3)
matrix metalloproteinase gene MMP13 and the antiapoptotic genes Birc2, cIAP1, and Birc3, cIAP2, form an amplicon located on chromosome 11q22, and show elevated expression in osteosarcomas
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matrix metalloproteinase gene MMP13 and the antiapoptotic genes Birc2, cIAP1, and Birc3, cIAP2, form an amplicon located on chromosome 9A1, and show elevated expression in osteosarcomas
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overexpression in Escherichia coli BL21(DE3)
real-time quantitative PCR MMP-13 expression analysis, overview
reverse transcription-PCR expression analysis of MMP13 in wild-type and mutant mice, overview
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semi-quantitative RT-PCR expression analysis of MMP-13 in gingiva, lack of transcription-translation coupling on MMP-13 expression in experimental periodontal disease
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the MMP-13 gene is localized on chromosome 11q22.3, MMP13 DNA and amino acid sequence determination and analysis, genotyping
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transient expression of a -148 rat MMP-13 promoter construct, subcloned upstream of a CAT reporter gene in pSV0, and of the mutant pGL2-MMP-13 promoter construct in UMR106-01 cells, real time quantitative RT-PCR expression analysis, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
(Z)-1-[N-methyl-N-[6-(N-methylammoniohexyl)amino]]diazen-1-ium-1,2-diolate, i.e. MAHMA-NONOate, induces the expression of MMP-13 via release of NO, which induces MMP-13 expression by JNK and NF-kappaB activation in chondrocytes, mechanism, overview. NO-induced MMP-13 expression is not suppressed by extracellular signal-regulated kinase inhibitor PD98059, or inhibitors of p38 kinase, i.e. SB203580, but is inhibited by a c-jun terminal kinase inhibitor SP600125 and inhibitors of NF-kappaB, i.e. SN-50
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1,25-dihydroxy vitamin D3, 1,25D3, and T3 hormones induce MMP-13 expression in osteoblasts and are important for enzyme regulation in bone. The activation of MMP-13 expression by T3 is in a competitive balance with the regulation of osteocalcin expression, overview. PKA inhibitor HA1004 stimulates 1,25D3 activation of MMP-13 expression and reduces the stimulation by T3
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adiponectin and interleukin-1beta induce MMP-13 expression and secretion in cell cultures, adiponectin plays a role in the pathogenesis of arthritis as a proinflammatory mediator
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after epidermal growth factor stimulation MMP13 is up-regulated
avocado/soybean unsaponifiables reduce the expression of MMP-13 in cartilage
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BMP-2 siRNA induces a 60% increase in the expression of MMP-13 protein and a marked increase in the staining intensity for MMP-13 in the epithelial region of the BMP-2 siRNA treated mandibles
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both the JNK inhibitor SP 600125 and PI-3K/Akt inhibitor LY 294002 can inhibit chloramphenicol-induced c-Jun phosphorylation, MMP-13 expression, and cell invasion
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chloramphenicol causes mitochondrial stress, decreases ATP biosynthesis, and induces MMP-13 expression, and solid-tumor cell invasion. Chloramphenicol also activated c-Jun N-terminal kinases, JNK, and PI-3K/Akt signaling, leading to c-Jun protein phosphorylation. The activated c-Jun protein activates binding to the MMP-13 promoter and also upregulates the amount of MMP-13. Other antibiotics that cause mitochondrial stress and a decrease in ATP biosynthesis also induce MMP-13 expression. Chloramphenicol-induction of MMP-13 expression is observed in nine solid-tumor cell lines, including H1299, HepG2, A549, CL-10, NCI-N87, Huh7, SAS, GBM8401, and Hep1, but not in leukemia suspensions, including THP-1, HL-60, and Jurkat cells
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connective tissue growth factor, CTGF, a secreted protein that binds to integrins, increases the migration and expression of MMP-13 in chondrosarcoma JJ012 cells through the alphanybeta3 integrin, FAK, ERK, and NF-kappaB signal transduction pathway. The induction is inhibited by MAPK kinase inhibitors PD98059 and U0126, but not by RAD peptide. Also treatment of JJ012 cells with NF-kappaB inhibitor PDTC or IkappaB protease inhibitor TPCK inhibits CTGF-induced cell migration and MMP-13 up-regulation, overview
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Cyr61 increases the binding of c-Fos and c-Jun to the activator protein-1 element on the MMP-13 promoter, and Cyr61 enhances the migration of chondrosarcoma cells by increasing MMP-13 expression through the alphanybeta3 integrin receptor, FAK, ERK, c-Fos/c-Jun and activator protein-1 signal transduction pathway. The upregulation of MMP-13 is antagonized by decoy agonist AP-1-binding site, AP-1 oligonucleotide, but not by NF-kappaB oligonucleotide or scrambled oligonucleotide, as well as by RGD, PD98059 and FAK(Y397F) and ERK2 mutant. Pretreatment with RGD and PD98059 or transfection with FAK and ERK2 mutant of JJ012 cells inhibits the Cyr61-induced increase in AP-1 promoter activity
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epigallocatechin-3-gallate, EGCG, from Camellia sinensis inhibits advanced glycation end product-induced expression of matrix metalloproteinase-13 in chondrocytes involving suppression of p38-MAPK and JNK activation, overview
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ER-alpha upregulates MMP-13 expression and acts via an AP-1 regulatory site on the MMP-13 promoter, ER-alpha influences the MMP-13 activity mediated by two separate transcriptional activation domains, AF-1 and AF-2, overview. Both AF-1 and AF-2 domains of ER-alpha are required for regulation of MMP-13 promoter activity
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GDNF-induced MMP-13 expression and glioma migration are attenuated by MEK/extracellular signal-regulating kinase and c-Jun N-terminal protein kinase inhibitors, PD98059 and SP600125, as well as ERK and JNKdominant-negative mutants. AP-1 inhibitors, tanshinone IIA and curcumin, also reduce GDNF-induced glioma cell migration
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glial cell line-derived neurotrophic factor, GDNF, induces cell migration and MMP-13 expression in glioma cells
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glucosamine-hydrochloride differentially downregulates COX-2 andMMP-13 expression in the interleukin-1beta-treated or phorpbol-12-myristate-13-acetate-treated skin fibroblasts via the p38 MAPK-independent COX-2 translational inhibition and the p38 MAPK-dependent MMP-13 transcriptional suppression, respectively
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HDAC4 represses MMP-13 transcription in osteoblastic cells, and parathyroid hormone controls this repression
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HDAC4 represses MMP-13 transcription in osteoblastic cells, and parathyroid hormone controls this repression. HDAC4 interacts with Runx2 on the RD site of the MMP-13 promoter. Binding of HDAC4 to Runx2 is decreased after PTH stimulation
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hypoxia increases MMP-13 protein and mRNA levels in primary rat astrocyte cultures. c-Fos and c-Jun are involved in hypoxia-induced up-regulation of MMP-13 expression in primary cultured astrocytes
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ibuprofen upregulates expressions of MMP-13 both at mRNA and protein levels
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in the chondrocytes pretreated with the JNK inhibitor SP600125, stimulation with interleukin-1beta shows an 88% increase in miR-27b expression and an 14fold increase in MMP-13 mRNA expression compared with controls. Pretreatment of osteoarthritic chondrocytes with the p38 MAPK inhibitor SB202190 suppresses interleukin-1beta-induced MMP-13 mRNA expression by 90%
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inhibitor of growth 2, ING2, upregulates expression of MMP13, which enhances cancer invasion and metastasis. MMP13 expression is further enhanced by combination of the synergistically acting ING2 and HDAC1
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interleukin-1 and oncostatin M induce MMP-13 expression
interleukin-1beta and FN-f stimulate MMP-13 expression, dependent on AP-1 activation
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interleukin-1beta and tumor necrosis factor-alpha induce MMP-13 expression. When CCAAT/enhancer binding protein beta, i.e. C/EBPbeta and liver-enriched activator protein, LAP, are overexpressed in C-28/I2 cells, endogenous MMP-13 expression is stimulated up to 32fold. Both C/EBPbeta and AP-1 are essential regulators of the MMP-13 promoter
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interleukin-1beta induces MMP-13 expression, mediated by extracellular signal-regulated protein kinase, p38 kinase, and c-Jun N-terminal kinase of the MAPK family signal transduction molecules. The interleukin-1beta-induced expression of MMP-13 is selectively inhibited by ERK MAPK pathway inhibitor U0126 and by the imidazo[5,1-c][1,4]thiazine derivative ITZ-1 in vivo, overview
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interleukin-1beta induces MMP-13 expression, mediated by extracellular signal-regulated protein kinase, p38 kinase, and c-Jun N-terminal kinase of the MAPK family signal transduction molecules. The interleukin-1beta-induced expression of MMP-13 is selectively inhibited by ERK MAPK pathway inhibitor U0126, and by the imidazo[5,1-c][1,4]thiazine derivative ITZ-1, overview. It is also less selectively inhibited by the p38 kinase inhibitor SB203580 and the JNK inhibitor SP600125
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interleukin-1beta induces MMP-13 expression, which is potently inhibited by interferon-gamma healthy chondrocytes mediated by STAT1
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interleukin-1beta treatment induces COX-2 and MMP-13 expressions in association with activation of ERKs, p38 MAPK, JNKs, and NF-kappaB in skin fibroblasts. Phorbol-12-myristate-13-acetate treatment also induces COX-2 and MMP-13 expressions in association with p38 MAPK activation
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keratinocytes transfected with siRNA for MMP-13 exhibit downregulation of mRNA and protein expression of the MMP
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mechanical strain induction of MMP-13 by high mechanical forces, with receptor of platelet-derived growth factor receptor alpha, PDGFR-alpha, as a potential mechanoreceptor in the MMP-13 induction, inhibited by platelet-derived growth factor receptor inhibitor AG1296, overview. The receptor performs autophosphorylation under mechanical stress
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MMP-13 expression is induced by advanced glycation end products, e.g. pentosidine or N3-carboxymethyllysine, the induction is significantly inhibited by SB202190 and SP600125
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MMP-13 gene expression is upregulated in fish groups kept at 16°C around smoltification. MMP-13 gene expression is significantly higher at 6 and 9 weeks in the 16°C compared to 6 and 9 weeks respectively in the 10°C group
MMP-13-shRNA for 24 h significantly inhibits hypoxia-stimulated MMP-13 mRNA expression in cell lysate and enzyme activity in supernatant
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MMP13 expression is transiently induced by wounding, MMP-13 expression is negligible in the normal unwounded skin at day 0, but it increases on days 1 to 7 upon wounding, diminishes on day 14 and disappears on day 28
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MMP13 is a direct target of osteoblast-specific transcription factor Osx in osteoblasts. Calvaria obtained from Osx-null embryos display dramatic reductions in MMP13 expression compared to wild-type calvaria. Stable overexpression of Osx stimulates MMP13 expression in C2C12 mesenchymal cells. Inhibition of Osx expression by siRNA leads to downregulation of MMP13 expression. Osx directly activates a 1 kb fragment of the MMP13 promoter in a dose-dependent manner
p38gamma mitogen-activated protein kinase suppresses chondrocyte production of MMP-13 in response to catabolic stimulation. Inhibition of both p38alpha and p38gamma with BIRB796 results in less inhibition of MMP-13 production in response to interleukin-1beta or FN-f than does inhibition of only p38alpha with SB203580
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parathyroid hormone acts via protein kinase A to phosphorylate and stimulate the transactivation of Runx2 for MMP-13 promoter. Runx2 is phosphorylated on Ser28 and Thr340 after 8-bromo cyclic adenosine monophosphate treatment. Runx2 construct having mutations at three phosphorylation sites, S28, S347 and T340, is unable to stimulate MMP-13 promoter activity
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parathyroid hormone, PTH, stimulation of the MMP-13 promoter in the osteosarcoma cell line UMR-106-01, as well as in primary osteoblastic cells. Trichostatin A, an HDAC inhibitor, markedly stimulated basal transcription from the MMP-13 promoter in UMR 106-01 cells
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pyrrolidine dithiocarbamate, a NF-kappaB inhibitor, upregulates MMP-1 and MMP-13 in interleukin-1beta-stimulated rheumatoid arthritis fibroblast-like synoviocytes in a stimuli-specific manner or by an NF-kappaB independent mechanism
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Roxithromycin suppresses the expression of MMP-13 mRNA not only in Ca9-22 cells, but also in other human epithelial cell lines. Roxithromycin strongly inhibits the expression of Runx2 mRNA. Furthermore, Runx2 siRNA inhibits the induction of MMP-13 in Ca9-22 cells
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significantly elevated levels of MMP-13 mRNA and protein in case of lipopolysaccharide-induced inflammation throughout 30 days
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siRNA knockdown of transcription factor Runx2 decreases MMP-13 expression in giant cell tumor stromal cells
strong stimulus of a combination of interleukin-1alpha plus oncostatin M, inducing MMP13 expression
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the bFGF-ERK-Elk-1 signaling axis is responsible for the potent induction of MMP-13 in primary articular chondrocytes. Phosphorylation renders Elk-1 competent for induction of MMP-13 gene transcription, while sumoylation has the opposite effect. Unphosphorylatable Elk-1 S383A mutant and unphosphorylated Elk-1 are inactive, while mutation of the SUMO modification site of Elk-1 to GAL4-Elk-1K230R/K249R increases its activity. bFGF-mediated activation of Elk-1 is regulated by the SUMO pathway
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the NF-kappaB inhibitors fenofibrate, N-acetylcysteine and MG132 decrease MMP-13 expression in interleukin-1beta-stimulated fibroblast-like synoviocytes
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the Runx2 transcription factor is known to have a binding site in the MMP-13 promoter region and activates MMP-13 expression constitutively in giant cell tumor cells. Inhibition of the ERK and JNK signaling pathways inhibits the upregulation of MMP-13 in these cells
transfection of chondrocytes with adenovirus overexpressing constitutive active ALK1 increased MMP-13 expression, while small interfering RNA against ALK1 decreases MMP-13 expression to nondetectable levels
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
a chromatographic method is used to refold the Histidine-tagged (His-tagged) catalytic domain of MMP-13. After the optimization of gradient elution modes and chromatographic conditions, the recovery yield reaches 83% with a relative activity of 92%. Addition of small molecule inhibitors to prevent slight autoproteolytic degradation does not affect the secondary structure of the protein
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in 50 mM MES, pH 6.5, 500 mM NaCl, 10 mM CaCl2, 1.0 mM ZnCl2, and decreasing concentrations of urea (4-0 M)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
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MMP-13 is a predictive markers for cisplatin resistance in head and neck squamous cell cancer
drug development
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the enzyme is a target for design of tetracycline-based drugs
medicine
analysis
MMP-13 expression might be an indicator for increased extracellular matrix remodeling and early signs of vertebral compression in farmed Atlantic salmon
analysis
generation of a neutralizing antibody specifc for the active form of MMP-13, but not for the latent form, or other MMPs. antibody can be used to measure active MMP-13 selectively by an enzyme-linked immunosorbet assay. The antibody suppresses the cleavage of type II collagen in human articular chondrocyte cultures, and is thought to inhibit MMP-13 activity effectively
medicine
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abundant expression of enzyme and of matrix metalloproteinase 10 in keratoacanthoma. Frequent expression of transformation-specific enzyme suggests that keratoacanthomas are incomplete squamous cell carcinomas
medicine
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cartilaginous growth plate abnormalities result from enzyme deficiency in mice phenocopy defects observed in human hereditary chondrodysplasis
medicine
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change of enzyme expression in response to caries attack. Extremely high enzyme mRNA expression in pooled pulp samples of sound and carious teeth, downregulation of enzyme expression during caries progression
medicine
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during gastric ulcer healing, enzyme expression as well as matrix metalloproteinase MMP-2 and MMP-3 are induced in stromal cells of the gastric mucosa bordering the ulcer. Enzyme mRNA is confined to the upper layers of the granulation tissue
medicine
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expression of enzyme and tissue inhibitor of matrix metalloproteinase, TIMP-1, is regulated by Wnt signaling combined with bone morphogenic protein BMP-2 in osteoblastic differentiation
medicine
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high level of enzyme expression by fibroblasts achieved by adenoviral gene delivery results in potent enhancement of remodeling and contraction of 3D collagen
medicine
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percentage of enzyme-positive cutaneous malignant melanomas correlates significantly and positively with the mitotic index in invasive cutaneous malignant melanoma. No significant association between tumoral enzyme expression and relapse-free survival in patients with invasive cutaneous malignant melanoma
medicine
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selective inhibition of enzyme to inhibit cleavage of fibromodulin as a treatment for patients suffering from arthritis
medicine
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selective inhibitors for enzyme for potential use in treatment of osteoarthritis
medicine
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mRNA expressions of matrix metalloproteinase-13 is significantly enhanced in osteoarthritis subchondral bone osteoblasts compared to subchondral bone osteoblasts without osteoarthritis. The expressions of this gene is greater in patients with severe cartilage damage than in those with mild cartilage damage
medicine
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orally active and specific matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis. Two series, quinazolinones and pyrido[3,4-d]pyrimidin-4-ones, that are potent and specific MMP-13 inhibitors, some of which are orally bioavailable. These specific MMP-13 inhibitors, occupying the unique S1'-specificity pocket, do not bind to the Zn2+ ion, effectively preventing cartilage damage in animal models of osteoarthritis without inducing musculoskeletal side effects when given at extremely high doses to rats
medicine
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tumor-derived, but not stromal fibroblast-derived, MMP-13 correlates with aggressive tumor phenotypes, and inversely correlated with the overall survival of breast cancer patients. MMP-13 may serve as an independent prognostic factor for invasive breast cancer patients. MMP-13 may be particularly useful as a prognostic marker when evaluated along with Her-2/neu and lymph node status
medicine
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MMP13 is a potential therapeutic target for breast cancer bone metastasis
medicine
in a collagen-induced arthritis model, MMP-12 and MMP-13 activity probes based on derived from substrates Y(NO2)GPLG-LEEAK(Abz)G-NH2 and Y(NO2)GPAG-LYEK(Abz)G-NH2, respectively, discriminate between the activities of the 2 enzymes. In the disease model, MMP13 activity probe activation increases gradually after disease onset and correlates with disease severity over a longer period of 15 days
medicine
patients with alcoholic liver cirrhosis (stage A, B, C) display increased blood serum levels of MMP13 and reduced concentrations of glutamic acid and glutamine compared to the control group. No significant differences are observed in the activity of MMP1 in alcoholics with or without liver cirrhosis or in controls
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Release 2023.1 (January 2023)
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