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Information on EC 1.3.1.21 - 7-dehydrocholesterol reductase and Organism(s) Homo sapiens
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1.3.1.21 7-dehydrocholesterol reductaseIUBMB Comments
The enzyme is part of the cholesterol biosynthesis pathway.
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Word Map
- 1.3.1.21
-
smith-lemli-opitz
- malformation
- cyp2r1
- anomaly
-
25-hydroxyvitamin
-
syndactyly
-
d-related
- desmosterol
- 8-dehydrocholesterol
- dhcr24
-
genitalia
- oxysterols
- holoprosencephaly
- rsh
- ecdysteroids
-
cholesterogenic
- medicine
- diagnostics
-
25-hydroxylase
- trazodone
- aripiprazole
- ebp
- hmgcs1
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
dhcr7, 7-dehydrocholesterol reductase, neverland, daf-36, sterol delta7-reductase, 7-dhc reductase, 3beta-hydroxysterol delta7-reductase, 7-dhcr, 3beta-hydroxysterol-delta7-reductase, 7-dehydrocholesterol delta7-reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7-DHC reductase
-
-
-
-
Dhcr7
Dwarf5 protein
-
-
-
-
reductase, 7-dehydrocholesterol
-
-
-
-
Sterol delta-7-reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
cholesterol:NADP+ DELTA7-oxidoreductase
The enzyme is part of the cholesterol biosynthesis pathway.
CAS REGISTRY NUMBER
COMMENTARY
9080-21-1
-
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
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
terminal step in desmosterol de novo biosynthesis, pathway and physiological role, overview
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
defect in cholesterol biosynthesis cause multiple congenital, developmental and morphogenic anomalies, e.g. the Smith-Lemli-Opitz syndrome due to a gene mutation, overview
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
defect in cholesterol biosynthesis cause multiple congenital, developmental and morphogenic anomalies, e.g. the Smith-Lemli-Opitz syndrome due to a gene mutation, overview
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol biosynthesis
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol biosynthesis
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
wide substrate spectrum
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
enzyme catalyzes the terminal step in cholesterol biosynthesis by reducing 7-dehydrocholesterol
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
final step in cholesterol biosynthesis
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
last step in cholesterol biosynthesis
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
terminal step in cholesterol de novo biosynthesis, pathway and physiological role, overview
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
terminal step in cholesterol de novo biosynthesis, physiological role, overview
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
i.e. 7-dehydrocholesterol
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
i.e. 7-dehydrocholesterol
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
i.e. 7-dehydrocholesterol
-
-
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
i.e. ergosterol
i.e. brassicasterol
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
i.e. ergosterol
i.e. brassicasterol
?
additional information
?
-
-
a mutational enzyme defect causes the Smith-Lemli-Opitz syndrome, a severe developmental disorder associated with multiple congenital anomalies, with low cholesterol and high precurosor 7-hydrocholesterol contents in plasma and tissues, clinical symptoms, overview
-
-
?
additional information
?
-
-
over 92% reduced enzyme activity, due to autosomal recessive mutational disorder, leads to the Smith-Lemli-Opitz syndrome in multiple cell types
-
-
?
additional information
?
-
reduced enzyme activity due to mutation leads to holoprosencephaly in vivo, phenotype
-
-
?
additional information
?
-
-
reduced enzyme activity due to mutation leads to holoprosencephaly in vivo, phenotype
-
-
?
additional information
?
-
-
several enzyme mutational defects cause the Smith-Lemli-Opitz syndrome, a severe developmental disorder associated with multiple congenital malformations and mental retardation, or desmosterolosis and lathosterolosis, rare autosomal recessive disorders, defect cholesterol synthesis, clinical symptoms, overview
-
-
?
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
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
terminal step in desmosterol de novo biosynthesis, pathway and physiological role, overview
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
defect in cholesterol biosynthesis cause multiple congenital, developmental and morphogenic anomalies, e.g. the Smith-Lemli-Opitz syndrome due to a gene mutation, overview
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
defect in cholesterol biosynthesis cause multiple congenital, developmental and morphogenic anomalies, e.g. the Smith-Lemli-Opitz syndrome due to a gene mutation, overview
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol biosynthesis
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol biosynthesis
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
enzyme catalyzes the terminal step in cholesterol biosynthesis by reducing 7-dehydrocholesterol
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
final step in cholesterol biosynthesis
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
last step in cholesterol biosynthesis
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
terminal step in cholesterol de novo biosynthesis, pathway and physiological role, overview
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
terminal step in cholesterol de novo biosynthesis, physiological role, overview
-
-
?
additional information
?
-
-
a mutational enzyme defect causes the Smith-Lemli-Opitz syndrome, a severe developmental disorder associated with multiple congenital anomalies, with low cholesterol and high precurosor 7-hydrocholesterol contents in plasma and tissues, clinical symptoms, overview
-
-
?
additional information
?
-
-
over 92% reduced enzyme activity, due to autosomal recessive mutational disorder, leads to the Smith-Lemli-Opitz syndrome in multiple cell types
-
-
?
additional information
?
-
reduced enzyme activity due to mutation leads to holoprosencephaly in vivo, phenotype
-
-
?
additional information
?
-
-
reduced enzyme activity due to mutation leads to holoprosencephaly in vivo, phenotype
-
-
?
additional information
?
-
-
several enzyme mutational defects cause the Smith-Lemli-Opitz syndrome, a severe developmental disorder associated with multiple congenital malformations and mental retardation, or desmosterolosis and lathosterolosis, rare autosomal recessive disorders, defect cholesterol synthesis, clinical symptoms, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[2-(4-chlorophenyl)ethyl]-6-hydroxy-7-methoxy-1,2,3,4-tetrahydroisoquinoline
-
strong and selective inhibition of 7-dehydrocholesterol reductase, stronger inhibition of overall cholesterol biosynthesis than BM 15.766, presently the most selective known inhibitor of 7-DHCR
trans-1,4-Bis-(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride
-
i.e. AY-9944, hypercholesterolaemic drug
AY9944
-
i.e. AY9944, competitive inhibitor of DHCR7 enzyme activity and inductor of DHCR7 expression. It blocks hedgehog signaling upstream of the Gli transcription factors, overview
cyclopamine
-
treatment of adult human epidermal keratinocytes with 0.01 mM cyclopamine results in a decrease in enzyme activity (50% of control activity at 3 h)
additional information
-
feed-back inhibition through 3-hydroxy-3-methylglutaryl-CoA reductase
-
additional information
-
feed-back inhibition through 3-hydroxy-3-methylglutaryl-CoA reductase
-
additional information
-
in enzyme deficiency, accumulated 7-dehydrocholesterol suppresses sterol biosynthesis in vivo
-
additional information
-
not inhibited by 1alpha,25-dihydroxyvitamin D3 and vitamin D3
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sterol regulatory element
-
two sterol regulatory elements that bind sterol regulatory element-binding protein-2 work in cooperation to synergistically activate the enzyme
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
2-[2-(4-chlorophenyl)ethyl]-6-hydroxy-7-methoxy-1,2,3,4-tetrahydroisoquinoline
Homo sapiens
-
whole-cell assay, pH not specified in the publication, temperature not specified in the publication
0.000022
3'-methoxy-4'-hydroxyclomiphene
Homo sapiens
-
pH and temperature not specified in the publication
0.0000023
BM 15.766
Homo sapiens
-
whole-cell assay, pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
relative activity levels in healthy persons, heterozygous persons, and Smith-Lemli-Opitz syndrome patients
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of healthy persons, heterozygous persons, and Smith-Lemli-Opitz syndrome patients
-
of healthy persons, heterozygous persons, and Smith-Lemli-Opitz syndrome patients
-
of healthy persons, heterozygous persons, and Smith-Lemli-Opitz syndrome patients
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Dhcr7 is a nine-pass transmembrane protein in the endoplasmic reticulum
-
9 putative transmembrane segments, predicted membrane topology of the enzyme
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
enzyme absence leads to the devastating fetal developmental disorder Smith-Lemli-Opitz syndrome
malfunction
-
mutations in the enzyme gene lead to the developmental disease Smith-Lemli-Opitz syndrome which can also result in fetal mortality
malfunction
-
the Lemli-Opitz syndrome results from mutations in the 7-dehydrocholesterol reductase gene
metabolism
-
the enzyme catalyzes the final step of cholesterol synthesis via the Kandutsch-Russell pathway, and is crucial in maintaining cellular cholesterol levels
metabolism
-
the enzyme exerts complex biological effects, involved in both cholesterol and vitamin D production
metabolism
-
the enzyme is important for both cholesterol and vitamin D synthesis
physiological function
-
Dhcr7 inhibits hedgehog signaling in a Smo-independent manner, overview
physiological function
-
interaction with endothelial cells for 48 h down-regulates expression of genes in vascular smooth muscle cells controlling rate-limiting steps of the cholesterol biosynthesis such as HMG-CoA reductase, HMG-CoA-synthase-1, 24-dehydrocholesterol reductase and DHCR7. A decrease in the abundance of 24-dehydrocholesterol reductase and lower cholesterol levels in vascular smooth muscle cells cocultured with endothelial cells is observed
physiological function
upon DNA and RNA viral infection, macrophages reduce 7-dehydrocholesterol reductase (DHCR7) expression. DHCR7 deficiency or treatment with 7-dehydrocholesterol (7-DHC) can specifically promote phosphorylation of IRF3 and enhance type I interferon production in macrophages. Viral infection or 7-DHC treatment enhances AKT3 expression and activation. Deletion of DHCR7 and the DHCR7 inhibitors including AY9944 and the chemotherapy drug tamoxifen promote clearance of Zika virus and multiple viruses in vitro or in vivo
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). DHCR7_HUMAN
475
6
54489
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A247V
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 3.1% of wild-type enzyme activity, disease severity score is not directly correlated
C380Y
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 1.7% of wild-type enzyme activity, disease severity score is not directly correlated
E288K
E448K
G344D
site-directed mutagenesis, analogously to the naturally occurring mutation in holoprosencephaly, 50% reduced enzyme activity compared to the wild-type enzyme
G410S
I251N
mutation isolated in patient with severe form of Smith-Lemli-Opitz syndrome, carrying additional heterozygous mutation E288K
L99P
Q98X
R404C
R466Q
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 1.0% of wild-type enzyme activity, disease severity score is not directly correlated
S169L
T154M
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 8.2% of wild-type enzyme activity, disease severity score is not directly correlated
T93M
additional information
E288K
mutation isolated in patient with severe form of Smith-Lemli-Opitz syndrome, carrying additional heterozygous mutation I251N
G410S
site-directed mutagenesis, analogously to the naturally occurring mutation in holoprosencephaly, inactive mutant
R404C
site-directed mutagenesis, analogously to the naturally occurring mutation in holoprosencephaly, inactive mutant
S169L
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 6.2% of wild-type enzyme activity, disease severity score is not directly correlated
T93M
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 7.0% of wild-type enzyme activity, disease severity score is not directly correlated
additional information
-
91 naturally occurring mutations, expression study, analysis of genotypes and phenotypes, e.g. the Smith-Lemli-Opitz syndrome, resulting from diverse naturally occurring mutations in gene dhcr7, biochemical and physiological effects, e.g. low cholesterol and high precurosor 7-hydrocholesterol contents, overview
additional information
-
analysis of dhcr7 gene structure and naturally occurring mutations in the dhcr7 gene leading to formation of several congenital disorders with diverse symptoms, mutant genotypes and phenotypes, overview
additional information
-
mutation analysis and population study of patients with Smith-Lemli-Opitz syndrome, overview
additional information
-
expression of enzyme in Caenorhabditis elegans which is suspected to be defective in 7-dehydrocholesterol reductase activity. Caenorhabditis elegans expressing enzyme contains 80% more cholesterol than wild-type control. Brood size is reduced by 40%, although the growth rate is not significantly changed. Mean life span is increased up to 131% in sterol-deficient medium, probably resulting from acquired resisitance against both UV irradiation and thermal stress
additional information
-
identification of seven distinct enzyme mutations in patients with Smith-Lemli-Opitz syndrome
additional information
-
splice site mutation at the intron 8 - exon 9 splice junction, natural mutation present in patient with Smith-Lemli-Opitz syndrome
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and polymorphism analysis of DNA from fetae with holoprosencephaly, naturally occurring mutations involved in pathogenesis are G344D, R404C, and G410S, overexpression of wild-type and mutant enzymes in Saccharomyces cerevisiae as myc-tagged proteins
DNA and amino acid sequence determination, gene structure and organization, gene dhcr7 maps to chromosome 11q12-13
-
full length cDNA and 5'-terminal truncated cDNA, for the latter M59 is the first encountered, gene characterization
-
gene Dhcr7, DNA and amino acid sequence determination and analysis, no alternative splicing
gene dhcr7, maps to chromosome 11q13, determination of gene structure and organisation, DNA sequence determination and analysis of wild-type and natural mutant genes
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
trans-1,4-bis(2-chlorobenzaminomethyl)cyclohexane dihydrochloride, i.e. AY9944, is a competitive inhibitor of DHCR7 enzyme activity and inductor of DHCR7 expression. The DHCR7 expression is also activated by antipsychotic drugs, e.g. clozapine, chlorpromazine, haloperidol, and antidepressants such as imipramine, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
diagnostics
-
enzyme activity measurement can be a tool for prognosis of the Smith-Lemli-Opitz syndrome
diagnostics
-
enzyme activity measurement is useful for distinguishing Smith-Lemli-Opitz syndrome from carrier or unaffected cells, diagnosis of atypical cases, overview
medicine
-
mutational analysis of the DHCR7 gene in individuals from five families with Smith-Lemli-Opitz syndrome. No single mutation is responsible for the photosensitivity which characterizes Smith-Lemli-Opitz syndrome
medicine
-
Smith-Lemli-Opitz syndrome is caused not only by disruption of the enzymatic role of 7-dehydrocholesterol reductase as a reductase in cholesterol biosynthesis, but may also involve defects in enzyme resulting in derepression of Sonic Hedgehog signaling
medicine
-
screening of patients diagnosed for elevated 7-dehydrocholesterol levels identified three individuals affected with Smith-Lemli-Opitz Syndrome, and 22 with elevated 7-dehydrocholesterol levels in the absence of Smith-Lemli-Opitz Syndrome. Seven of these individuals showed no mutation in the gene encoding 7-dehydrocholesterol reductase. The medication history of these individuals revealed aripiprazole and trazodone as common medications to all the false positive results
medicine
-
interaction with endothelial cells for 48 h down-regulates expression of genes in vascular smooth muscle cells controlling rate-limiting steps of the cholesterol biosynthesis such as HMG-CoA reductase, HMG-CoA-synthase-1, 24-dehydrocholesterol reductase and DHCR7. A decrease in the abundance of 24-dehydrocholesterol reductase and lower cholesterol levels in vascular smooth muscle cells cocultured with endothelial cells is observed
medicine
upon DNA and RNA viral infection, macrophages reduce 7-dehydrocholesterol reductase (DHCR7) expression. DHCR7 deficiency or treatment with 7-dehydrocholesterol (7-DHC) can specifically promote phosphorylation of IRF3 and enhance type I interferon production in macrophages. Viral infection or 7-DHC treatment enhances AKT3 expression and activation. Deletion of DHCR7 and the DHCR7 inhibitors including AY9944 and the chemotherapy drug tamoxifen promote clearance of Zika virus and multiple viruses in vitro or in vivo
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Waterham, H.R.; Wanders, R.J.A.
Biochemical and genetic aspects of 7-dehydrocholesterol reductase and Smith-Lemli-Opitz syndrome
Biochim. Biophys. Acta
1529
340-356
2000
Arabidopsis thaliana, Homo sapiens, Rattus norvegicus
Honda, A.; Salen, G.; Nguyen, L.B.; Tint, G.S.; Batta, A.K.; Shefer, S.
Down-regulation of cholesterol biosynthesis in sitosterolemia: diminished activities of acetoacetyl-CoA thiolase, 3-hydroxy-3-methylglutaryl-CoA synthase, reductase, squalene synthase, and 7-dehydrocholesterol DELTA7-reductase in liver and mononuclear leukocytes
J. Lipid Res.
39
44-50
1998
Homo sapiens
Honda, A.; Salen, G.; Shefer, S.; Batta, A.K.; Honda, M.; Xu, G.; Tint, G.S.; Matsuzaki, Y.; Shoda, J.; Tanaka, N.
Bile acid synthesis in the Smith-Lemli-Opitz syndrome: effects of dehydrocholesterols on cholesterol 7.alpha-hydroxylase and 27-hydroxylase activities in rat liver
J. Lipid Res.
40
1520-1528
1999
Homo sapiens, Rattus norvegicus
Jira, P.E.; Waterham, H.R.; Wanders, R.J.; Smeitink, J.A.; Sengers, R.C.; Wevers, R.A.
Smith-Lemli-Opitz syndrome and the DHCR7 gene
Ann. Hum. Genet.
67
269-280
2003
Homo sapiens
Shim, Y.H.; Bae, S.H.; Kim, J.H.; Kim, K.R.; Kim, C.J.; Paik, Y.K.
A novel mutation of the human 7-dehydrocholesterol reductase gene reduces enzyme activity in patients with holoprosencephaly
Biochem. Biophys. Res. Commun.
315
219-223
2004
Homo sapiens (Q9UBM7), Homo sapiens
Lee, J.N.; Bae, S.H.; Paik, Y.K.
Structure and alternative splicing of the rat 7-dehydrocholesterol reductase gene
Biochim. Biophys. Acta
1576
148-156
2002
Mus musculus (O88455), Mus musculus, Rattus norvegicus (Q9E2H5), Rattus norvegicus (Q9Z2Z8), Homo sapiens (Q9UBM7), Homo sapiens
Ginat, S.; Battaile, K.P.; Battaile, B.C.; Maslen, C.; Gibson, K.M.; Steiner, R.D.
Lowered DHCR7 activity measured by ergosterol conversion in multiple cell types in Smith-Lemli-Opitz syndrome
Mol. Genet. Metab.
83
175-183
2004
Homo sapiens
Correa-Cerro, L.S.; Porter, F.D.
3beta-hydroxysterol DELTA7-reductase and the Smith-Lemli-Opitz syndrome
Mol. Genet. Metab.
84
112-126
2005
Homo sapiens, Mus musculus, Rattus norvegicus
Lee, E.Y.; Shim, Y.H.; Chitwood, D.J.; Hwang, S.B.; Lee, J.; Paik, Y.K.
Cholesterol-producing transgenic Caenorhabditis elegans lives longer due to newly acquired enhanced stress resistance
Biochem. Biophys. Res. Commun.
328
929-936
2005
Homo sapiens
Anstey, A.V.; Azurdia, R.M.; Rhodes, L.E.; Pearse, A.D.; Bowden, P.E.
Photosensitive Smith-Lemli-Opitz syndrome is not caused by a single gene mutation: analysis of the gene encoding 7-dehydrocholesterol reductase in five U.K. families
Br. J. Dermatol.
153
774-779
2005
Homo sapiens
Koide, T.; Hayata, T.; Cho, K.W.Y.
Negative regulation of Hedgehog signaling by the cholesterogenic enzyme 7-dehydrocholesterol reductase
Development
133
2395-2405
2006
Homo sapiens, Xenopus laevis
Romano, F.; fiore, B.; Pezzino, F.M.; Longombardo, M.T.; Cefalu, A.B.; Noto, D.; Puglisi, A.; Brogna, A.; Mattina, T.; Averna, M.; Travali, S.
A novel mutation of the DHCR7 gene in a Sicilian compound heterozygote with Smith-Lemli-Optiz syndrome
Mol. Diagn.
9
201-204
2005
Homo sapiens (Q9UBM7), Homo sapiens
Cardoso, M.L.; Balreia, A.; Martins, E.; Nunes, L.; Cabral, A.; Marques, M.; Reis Lima, M.; Marques, J.S.; Medeira, A.; Cordeiro, I.; Pedro, S.; Mota, M.C.; Dionisi-Vici, C.; Santorelli, F.M.; Jakobs, C.; Clayton, P.T.; Vilarinho, L.
Molecular studies in Portuguese patients with Smith-Lemli-Opitz syndrome an report of three new mutations in DHCR7
Mol. Genet. Metab.
85
228-235
2005
Homo sapiens
Lauth, M.; Rohnalter, V.; Bergstroem, A.; Kooshesh, M.; Svenningsson, P.; Toftgard, R.
Antipsychotic drugs regulate hedgehog signaling by modulation of 7-dehydrocholesterol reductase levels
Mol. Pharmacol.
78
486-496
2010
Homo sapiens
Horling, A.; Mueller, C.; Barthel, R.; Bracher, F.; Imming, P.
A new class of selective and potent 7-dehydrocholesterol reductase inhibitors
J. Med. Chem.
55
7614-7622
2012
Homo sapiens
Hall, P.; Michels, V.; Gavrilov, D.; Matern, D.; Oglesbee, D.; Raymond, K.; Rinaldo, P.; Tortorelli, S.
Aripiprazole and trazodone cause elevations of 7-dehydrocholesterol in the absence of Smith-Lemli-Opitz Syndrome
Mol. Genet. Metab.
110
176-178
2013
Homo sapiens
Prabhu, A.V.; Sharpe, L.J.; Brown, A.J.
The sterol-based transcriptional control of human 7-dehydrocholesterol reductase (DHCR7): Evidence of a cooperative regulatory program in cholesterol synthesis
Biochim. Biophys. Acta
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1431-1439
2014
Homo sapiens
Luu, W.; Hart-Smith, G.; Sharpe, L.J.; Brown, A.J.
The terminal enzymes of cholesterol synthesis, DHCR24 and DHCR7, interact physically and functionally
J. Lipid Res.
56
888-897
2015
Homo sapiens
Zou, L.; Porter, T.D.
Rapid suppression of 7-dehydrocholesterol reductase activity in keratinocytes by vitamin D
J. Steroid Biochem. Mol. Biol.
148
64-71
2015
Homo sapiens
Boland, M.R.; Tatonetti, N.P.
Investigation of 7-dehydrocholesterol reductase pathway to elucidate off-target prenatal effects of pharmaceuticals: a systematic review
Pharmacogenomics J.
16
411-429
2016
Homo sapiens
Prabhu, A.V.; Luu, W.; Li, D.; Sharpe, L.J.; Brown, A.J.
DHCR7: A vital enzyme switch between cholesterol and vitamin D production
Prog. Lipid Res.
64
138-151
2016
Homo sapiens
Kohlhaas, J.; Jaeger, M.; Lust, L.; De La Torre, C.; Hecker, M.; Korff, T.
Endothelial cells control vascular smooth muscle cell cholesterol levels by regulating 24-dehydrocholesterol reductase expression
Exp. Cell Res.
399
112446
2021
Homo sapiens
Xiao, J.; Li, W.; Zheng, X.; Qi, L.; Wang, H.; Zhang, C.; Wan, X.; Zheng, Y.; Zhong, R.; Zhou, X.; Lu, Y.; Li, Z.; Qiu, Y.; Liu, C.; Zhang, F.; Zhang, Y.; Xu, X.; Yang, Z.; Chen, H.; Zhai, Q.; Wei, B.; Wang, H.
Targeting 7-dehydrocholesterol reductase integrates cholesterol metabolism and IRF3 activation to eliminate infection
Immunity
52
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2020
Homo sapiens (Q9UBM7)
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