Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
20,22-hydroxylumisterol-3 + NADPH + H+
? + NADP+
-
-
-
?
20S-hydroxy-7-dehydrocholesterol + NADPH + H+
20S-hdroxycholesterol + NADP+
-
-
-
?
22-hydroxylumisterol-3 + NADPH + H+
? + NADP+
-
-
-
?
27-hydroxydehydrocholesterol + NADPH + H+
27-hydroxycholesterol + NADP+
-
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
7-dehydrodesmosterol + NADPH + H+
desmosterol + NADP+
-
-
-
?
7-dehydrositosterol + NADPH
sitosterol + NADP+
-
25% of that with 7-dehydrocholesterol
-
?
7-hydroxycholesterol + NADPH + H+
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
cholesta-5,7-dien-3alpha-ol + NADPH
epicholesterol + NADP+
-
i.e. 7-dehydroepicholesterol, 25% activity of that with 7-dehydrocholesterol
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
cholesterol + NADP+
-
-
-
-
?
cholesta-7-en-3beta-ol + NADPH
?
cholesterol + NADP+
cholesta-5,7-dien-3-beta-ol + NADPH + H+
-
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
cholesterol + O2 + NAD(P)H + H+
cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
desmosterol + NADP+
7-dehydrodesmosterol + NADPH + H+
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
ergosta-5,7-diene-3beta-ol + NADPH
ergosta-5-ene-3beta-ol + NADP+
ergosta-5,7-diene-3beta-ol + NADPH
ergosta-5-eneol + NADP+
-
-
?
ergosta-5,7-dienol + NADPH
ergosta-5-enol + NADP+
ergosterol + NADP+
?
-
-
-
-
r
ergosterol + NADPH + H+
brassicasterol + NADP+
-
-
-
?
lumisterol-3 + NADPH + H+
? + NADP+
-
-
-
?
additional information
?
-
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
-
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
terminal step in desmosterol de novo biosynthesis, pathway and physiological role, overview
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
desmosterol is cholesta-5,24-dienol
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
desmosterol is cholesta-5,24-dienol
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
-
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
highly regiospecific for DELTA7-bond reduction, but wide substrate specificity
-
?
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-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol formation outside myelin sheath
-
?
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-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol biosynthesis
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
reversibility of the reaction in vivo could not be proven
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
wide substrate spectrum
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
wide substrate spectrum
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
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
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
-
?
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+
-
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+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
-
isotope effects
-
?
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+
-
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+
-
-
-
?
cholesta-7-en-3beta-ol + NADPH
?
-
i.e. lathosterol
-
-
?
cholesta-7-en-3beta-ol + NADPH
?
-
low activity
-
-
?
cholesta-7-en-3beta-ol + NADPH
?
-
not:
-
-
?
cholesta-7-en-3beta-ol + NADPH
?
-
i.e. lathosterol
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
cholesterol + O2 + NAD(P)H + H+
cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
-
-
-
?
cholesterol + O2 + NAD(P)H + H+
cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
-
-
-
?
cholesterol + O2 + NAD(P)H + H+
cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
first committed step in biosynthesis of Caenorhabditis elegans bile acid-like steroids called dafachronic acids
-
-
?
desmosterol + NADP+
7-dehydrodesmosterol + NADPH + H+
-
-
-
-
?
desmosterol + NADP+
7-dehydrodesmosterol + NADPH + H+
-
-
-
-
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
i.e. ergosterol
-
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
i.e. ergosterol
-
?
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
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
25% activity of that with 7-dehydrocholesterol
-
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
i.e. ergosterol
-
-
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
i.e. ergosterol
-
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
i.e. ergosterol
-
?
ergosta-5,7,22-trien-3beta-ol + NADPH
ergosta-5,22-diene-3beta-ol + NADP+
-
enzyme activity diet-inducible: 2.6fold by 0.5% ergosterol and 5fold by 5.0% cholestyramine and 0.1% lovastatin
-
-
?
ergosta-5,7-diene-3beta-ol + NADPH
ergosta-5-ene-3beta-ol + NADP+
-
-
-
?
ergosta-5,7-diene-3beta-ol + NADPH
ergosta-5-ene-3beta-ol + NADP+
also ergosta-5,24(28)-, ergosta-5,22,24(28)-eneols and cholesta-5,24- or cholesta-5,22,24-eneols can be formed in vivo in the mutants of Saccharomyces cerevisiae
-
?
ergosta-5,7-dienol + NADPH
ergosta-5-enol + NADP+
-
-
-
?
ergosta-5,7-dienol + NADPH
ergosta-5-enol + NADP+
-
-
-
?
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
-
-
?
additional information
?
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing
-
-
?
additional information
?
-
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing
-
-
?
additional information
?
-
-
enzyme is essential for steroidogenesis, enzyme is not regulated by the luteinizing hormone LH
-
-
?
additional information
?
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing, enzyme is induced when sterols are depleted both in vivo and in vitro
-
-
?
additional information
?
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing, enzyme is induced when sterols are depleted both in vivo and in vitro
-
-
?
additional information
?
-
no substrates: 8-dehydrocholesterol or 20S-hydroxylumisterol
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
cholesterol + NADP+
-
-
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
cholesterol + O2 + NAD(P)H + H+
cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O
first committed step in biosynthesis of Caenorhabditis elegans bile acid-like steroids called dafachronic acids
-
-
?
desmosterol + NADP+
7-dehydrodesmosterol + NADPH + H+
ergosta-5,7-diene-3beta-ol + NADPH
ergosta-5-ene-3beta-ol + NADP+
additional information
?
-
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
terminal step in desmosterol de novo biosynthesis, pathway and physiological role, overview
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
-
-
-
?
7-dehydrodesmosterol + NADPH
desmosterol + NADP+
-
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
highly regiospecific for DELTA7-bond reduction, but wide substrate specificity
-
?
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-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol formation outside myelin sheath
-
?
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-3-beta-ol + NADPH
cholesterol + NADP+
-
cholesterol biosynthesis
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
reversibility of the reaction in vivo could not be proven
-
?
cholesta-5,7-dien-3-beta-ol + NADPH
cholesterol + NADP+
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
cholesta-5,7-dien-3beta-ol + NADPH
cholesterol + NADP+
enzyme catalyzes the terminal step in cholesterol biosynthesis by reducing 7-dehydrocholesterol
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
cholesterol + NADP+
cholesta-5,7-dien-3beta-ol + NADPH + H+
-
-
-
-
?
desmosterol + NADP+
7-dehydrodesmosterol + NADPH + H+
-
-
-
-
?
desmosterol + NADP+
7-dehydrodesmosterol + NADPH + H+
-
-
-
-
?
ergosta-5,7-diene-3beta-ol + NADPH
ergosta-5-ene-3beta-ol + NADP+
-
-
-
?
ergosta-5,7-diene-3beta-ol + NADPH
ergosta-5-ene-3beta-ol + NADP+
also ergosta-5,24(28)-, ergosta-5,22,24(28)-eneols and cholesta-5,24- or cholesta-5,22,24-eneols can be formed in vivo in the mutants of Saccharomyces cerevisiae
-
?
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
-
-
?
additional information
?
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing
-
-
?
additional information
?
-
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing
-
-
?
additional information
?
-
-
enzyme is essential for steroidogenesis, enzyme is not regulated by the luteinizing hormone LH
-
-
?
additional information
?
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing, enzyme is induced when sterols are depleted both in vivo and in vitro
-
-
?
additional information
?
-
enzyme is regulated through tissue-specific transcription and differential alternative splicing, enzyme is induced when sterols are depleted both in vivo and in vitro
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
H190A
mutation within Rieske [2Fe-2S]-motif, complete loss of activity
H282A
mutation within non-heme Fe(II) binding motif, complete loss of activity
C122A
mutation within Rieske [2Fe-2S]-motif, complete loss of activity
D234A
mutation within non-heme Fe(II) binding motif, complete loss of activity
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
F174S
-
enzyme mutation in patients with Smith-Lemli-Opitz syndrome
F302L
-
the mutation is associated with Lemli-Opitz syndrome
G147D
-
the mutation is associated with Lemli-Opitz syndrome
G303R
-
the mutation is associated with Lemli-Opitz syndrome
G344D
site-directed mutagenesis, analogously to the naturally occurring mutation in holoprosencephaly, 50% reduced enzyme activity compared to the wild-type enzyme
H119L
-
the mutation is associated with Lemli-Opitz syndrome
H301Q
-
the mutation is associated with Lemli-Opitz syndrome
H301R
-
enzyme mutation in patients with Smith-Lemli-Opitz syndrome
H405Y
-
the mutation is associated with Lemli-Opitz syndrome
I251N
mutation isolated in patient with severe form of Smith-Lemli-Opitz syndrome, carrying additional heterozygous mutation E288K
L157P
-
the mutation is associated with Lemli-Opitz syndrome
N274K
-
enzyme mutation in patients with Smith-Lemli-Opitz syndrome
P51H
-
natural mutation present in patient with Smith-Lemli-Opitz syndrome
P51S
-
the mutation is associated with Lemli-Opitz syndrome
R242C
-
the mutation is associated with Lemli-Opitz syndrome
R352Q
-
the mutation is associated with Lemli-Opitz syndrome
R352W
-
the mutation is associated with Lemli-Opitz syndrome
R363C
-
the mutation is associated with Lemli-Opitz syndrome
R466Q
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 1.0% of wild-type enzyme activity, disease severity score is not directly correlated
R540L
-
natural mutation present in patient with Smith-Lemli-Opitz syndrome
S113C
-
the mutation is associated with Lemli-Opitz syndrome
T154M
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 8.2% of wild-type enzyme activity, disease severity score is not directly correlated
T154R
-
the mutation is associated with Lemli-Opitz syndrome
V326L
-
the mutation is associated with Lemli-Opitz syndrome
V326R
-
the mutation is associated with Lemli-Opitz syndrome
V330M
-
the mutation is associated with Lemli-Opitz syndrome
W151X
-
the mutation is associated with Lemli-Opitz syndrome
W182L
-
enzyme mutation in patients with Smith-Lemli-Opitz syndrome
E288K
mutation isolated in patient with severe form of Smith-Lemli-Opitz syndrome, carrying additional heterozygous mutation I251N
E288K
-
the mutation is associated with Lemli-Opitz syndrome
E448K
-
natural mutation present in patient with Smith-Lemli-Opitz syndrome
E448K
-
the mutation is associated with Lemli-Opitz syndrome
G410S
site-directed mutagenesis, analogously to the naturally occurring mutation in holoprosencephaly, inactive mutant
G410S
-
the mutation is associated with Lemli-Opitz syndrome
L99P
-
natural mutation present in patient with Smith-Lemli-Opitz syndrome
L99P
-
the mutation is associated with Lemli-Opitz syndrome
Q98X
-
enzyme mutation in patients with Smith-Lemli-Opitz syndrome
Q98X
-
the mutation is associated with Lemli-Opitz syndrome
R404C
site-directed mutagenesis, analogously to the naturally occurring mutation in holoprosencephaly, inactive mutant
R404C
-
the mutation is associated with Lemli-Opitz syndrome
S169L
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 6.2% of wild-type enzyme activity, disease severity score is not directly correlated
S169L
-
the mutation is associated with Lemli-Opitz syndrome
T93M
-
natural mutant, Smith-Lemli-Opitz syndrome patient, 7.0% of wild-type enzyme activity, disease severity score is not directly correlated
T93M
-
enzyme mutation in patients with Smith-Lemli-Opitz syndrome
T93M
-
natural mutation present in patient with Smith-Lemli-Opitz syndrome
T93M
-
the mutation is associated with Lemli-Opitz syndrome
T93M
-
naturally occuring mutation involved in Dhcr7 deficiency and the Smith-Lemli-Opitz syndrome, overview
T93M
-
naturally occuring mutation involved in Dhcr7 deficiency and the Smith-Lemli-Opitz syndrome, overview
-
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
additional information
-
enzyme knockdown by DHCR7 siRNA
additional information
-
ectopic and increased cholesterol formation achieved by overexpression of mural Dhcr7 in Xenopus laevis leads to an expansion of the embryonic brain, at least in part at the expense of eye formation
additional information
-
knock down of enzyme synthesis by an antisense morpholino oligonucleotide. Inhibition of enzyme synthesis results in disturbance of the expression of eyefield marker genes in the early neurula stage embryos, and alters brain development, as the expression of Xgsh1, which demarcates the intermediate neurons, and that of Xnkx2.2, a ventral forebrain marker, are significantly reduced. Overexpression of large isoform Xdhcr7-L results in an impairment of eye development
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Srikantaiah, M.V.; Assef, S.; Morin, R.J.
Effects of Tween 80 on liver microsomal 7-dehydrocholesterol reductase
Biochem. Biophys. Res. Commun.
81
1087-1090
1978
Rattus norvegicus
brenda
Bjrkhem, I.; Holmberg, I.
Mechanism of enzymatic reduction of steroid double bonds
Eur. J. Biochem.
33
364-367
1973
Rattus norvegicus
brenda
Banik, N.L.; Davison, A.N.
Exchange of sterols between myelin and other membranes of developing rat brain
Biochem. J.
122
751-758
1971
Rattus norvegicus
brenda
Kandutsch, A.A.
Enzymatic reduction of the DELTA7 bond of 7-dehydrocholesterol
J. Biol. Chem.
237
358-362
1962
Mus musculus
brenda
Dempsey, M.E.; Seaton, J.D.; Schroepfer, G.J.; Trockman, R.W.
The intermediary role of DELTA5,7-cholestadien-3beta-ol in cholesterol biosynthesis
J. Biol. Chem.
239
1381-1387
1964
Rattus norvegicus
brenda
Niemiro, R.; Fumagalli, R.
Studies on the inhibitory mechanism of some hypocholesterolemic agents on 7-dehydrocholesterol DELTA-7-bond reductase activity
Biochim. Biophys. Acta
98
624-631
1965
Rattus norvegicus
brenda
Dempsey, M.E.
Pathways of enzymic synthesis and conversion to cholesterol of DELTA-5,7,24-cholestatrien-3beta-ol and other naturally occurring sterols
J. Biol. Chem.
240
4176-4188
1965
Rattus norvegicus
brenda
Trzaskos, J.M.; Gaylor, J.L.
Cytosolic modulators of activities of microsomal enzymes of cholesterol biosynthesis. Purification and characterization of a non-specific lipid-transfer protein
Biochim. Biophys. Acta
751
52-65
1983
Rattus norvegicus
brenda
Wilton, D.C.; Munday, K.A.; Skinner, S.J.M.; Akhtar, M.
The biological conversion of 7-dehydrocholesterol into cholesterol and comments on the reduction of double bonds
Biochem. J.
106
803
1968
Rattus norvegicus
brenda
Lecain, E.; Chenivesse, X.; Spagnoli, R.; Pompon, D.
Cloning by metabolic interference in yeast and enzymic characterization of Arabidopsis thaliana sterol DELTA7-reductase
J. Biol. Chem.
271
10866-10873
1996
Arabidopsis thaliana (Q9LDU6)
brenda
Lee, J.N.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: development of a novel assay method, characterization, and solubilization of rat hepatic microsomal sterol DELTA7-reductase
J. Biochem. Mol. Biol.
30
370-377
1997
Rattus norvegicus
-
brenda
Rahier, A.; Taton, M.
Sterol biosynthesis: Strong inhibition of maize DELTA5,7-sterol DELTA7-reductase by novel 6-aza-B-homosteroids and other analogs of a presumptive carbocationic intermediate of the reduction reaction
Biochemistry
35
7069-7076
1996
Zea mays
brenda
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
brenda
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
brenda
Shefer, S.; Salen, G.; Honda, A.; Batta, A.K.; Nguyen, L.B.; Tint, G.S.; Ioannou, Y.A.; Desnick, R.
Regulation of rat hepatic 3beta-hydroxysterol DELTA7-reductase: substrate specificity, competitive and non-competitive inhibition, and phosphorylation/dephosphorylation
J. Lipid Res.
39
2471-2476
1998
Rattus norvegicus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Anbalagan, M.; Yashwanth, R.; Jagannadha Rao, A.
DD-RT-PCR identifies 7-dehydrocholesterol reductase as a key marker of early Leydig cell steroidogenesis
Mol. Cell. Endocrinol.
219
37-45
2004
Rattus norvegicus
brenda
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
brenda
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
brenda
Lin, X.; Chen, Z.; Yue, P.; Averna, M.; Ostlund, R.E.; Watson, M.A.; Schonfeldt, G.
A targeted apoB38.9 mutation in mice is associated with reduced hepatic cholesterol synthesis and enhanced lipid peroxidation
Am. J. Physiol. Gastrointest. Liver Physiol.
290
1170-1176
2006
Mus musculus
-
brenda
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
brenda
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
brenda
Tadjuidje, E.; Hollemann, T.
Cholesterol homeostasis in development: The role of Xenopus 7-dehydrocholesterol reductase (Xdhcr7) in neural development
Dev. Dyn.
235
2095-2110
2006
Mus musculus, Xenopus laevis
brenda
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
brenda
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
brenda
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
brenda
Zhang, S.; Sakuradani, E.; Shimizu, S.
Identification of a sterol DELTA7 reductase gene involved in desmosterol biosynthesis in Mortierella alpina 1S-4
Appl. Environ. Microbiol.
73
1736-1741
2007
Mortierella alpina (A4F244), Mortierella alpina 1S-4 (A4F244), Mortierella alpina 1S-4
brenda
Hagiwara, K.; Nakamura, Y.; Nishijima, M.; Yamakawa, Y.
Prevention of prion propagation by dehydrocholesterol reductase inhibitors in cultured cells and a therapeutic trial in mice
Biol. Pharm. Bull.
30
835-838
2007
Mus musculus
brenda
Marcos, J.; Shackleton, C.H.; Buddhikot, M.M.; Porter, F.D.; Watson, G.L.
Cholesterol biosynthesis from birth to adulthood in a mouse model for 7-dehydrosterol reductase deficiency (Smith-Lemli-Opitz syndrome)
Steroids
72
802-808
2007
Mus musculus
brenda
Serra, M.; Matabosch, X.; Ying, L.; Watson, G.; Shackleton, C.
Hair and skin sterols in normal mice and those with deficient dehydrosterol reductase (DHCR7), the enzyme associated with Smith-Lemli-Opitz syndrome
J. Steroid Biochem. Mol. Biol.
122
318-325
2010
Mus musculus, Mus musculus C57BL/6
brenda
Jiang, X.S.; Backlund, P.S.; Wassif, C.A.; Yergey, A.L.; Porter, F.D.
Quantitative proteomics analysis of inborn errors of cholesterol synthesis: identification of altered metabolic pathways in DHCR7 and SC5D deficiency
Mol. Cell. Proteomics
9
1461-1475
2010
Mus musculus
brenda
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
brenda
Wollam, J.; Magomedova, L.; Magner, D.B.; Shen, Y.; Rottiers, V.; Motola, D.L.; Mangelsdorf, D.J.; Cummins, C.L.; Antebi, A.
The Rieske oxygenase DAF-36 functions as a cholesterol 7-desaturase in steroidogenic pathways governing longevity
Aging Cell
10
879-884
2011
Caenorhabditis elegans (Q17938)
brenda
Yoshiyama-Yanagawa, T.; Enya, S.; Shimada-Niwa, Y.; Yaguchi, S.; Haramoto, Y.; Matsuya, T.; Shiomi, K.; Sasakura, Y.; Takahashi, S.; Asashima, M.; Kataoka, H.; Niwa, R.
The conserved Rieske oxygenase DAF-36/Neverland is a novel cholesterol-metabolizing enzyme
J. Biol. Chem.
286
25756-25762
2011
Caenorhabditis elegans (Q17938), Bombyx mori (Q1JUZ2)
brenda
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
brenda
Matabosch, X.; Ying, L.; Serra, M.; Wassif, C.A.; Porter, F.D.; Shackleton, C.; Watson, G.
Increasing cholesterol synthesis in 7-dehydrosterol reductase (DHCR7) deficient mouse models through gene transfer
J. Steroid Biochem. Mol. Biol.
122
303-309
2010
Mus musculus
brenda
Zou, L.; Li, L.; Porter, T.D.
7-Dehydrocholesterol reductase activity is independent of cytochrome P450 reductase
J. Steroid Biochem. Mol. Biol.
127
435-438
2011
Mus musculus
brenda
Najle, S.R.; Nusblat, A.D.; Nudel, C.B.; Uttaro, A.D.
The sterol-C7 desaturase from the ciliate Tetrahymena thermophila is a Rieske oxygenase, which is highly conserved in animals
Mol. Biol. Evol.
30
1630-1643
2013
Tetrahymena thermophila (I7ML19), Tetrahymena thermophila
brenda
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
brenda
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
1842
1431-1439
2014
Homo sapiens
brenda
Kim, H.Y.; Korade, Z.; Tallman, K.A.; Liu, W.; Weaver, C.D.; Mirnics, K.; Porter, N.A.
Inhibitors of 7-dehydrocholesterol reductase: screening of a collection of pharmacologically active compounds in Neuro2a cells
Chem. Res. Toxicol.
29
892-900
2016
Mus musculus
brenda
Liu, W.; Xu, L.; Lamberson, C.; Haas, D.; Korade, Z.; Porter, N.A.
A highly sensitive method for analysis of 7-dehydrocholesterol for the study of Smith-Lemli-Opitz syndrome
J. Lipid Res.
55
329-337
2014
Mus musculus
brenda
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
brenda
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
brenda
Prabhu, A.V.; Luu, W.; Sharpe, L.J.; Brown, A.J.
Phosphorylation regulates activity of 7-dehydrocholesterol reductase (DHCR7), a terminal enzyme of cholesterol synthesis
J. Steroid Biochem. Mol. Biol.
165
363-368
2017
Mesocricetus auratus
brenda
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
brenda
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
brenda
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
brenda
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
109-122.e6
2020
Homo sapiens (Q9UBM7)
brenda
Tuckey, R.; Tang, E.; Chen, Y.; Slominski, A.
Selective ability of rat 7-dehydrocholesterol reductase (DHCR7) to act on some 7-dehydrocholesterol metabolites but not on lumisterol metabolites
J. Steroid Biochem. Mol. Biol.
212
105929
2021
Rattus norvegicus (Q9Z2Z8)
brenda
Genaro-Mattos, T.C.; Allen, L.B.; Anderson, A.; Tallman, K.A.; Porter, N.A.; Korade, Z.; Mirnics, K.
Maternal aripiprazole exposure interacts with 7-dehydrocholesterol reductase mutations and alters embryonic neurodevelopment
Mol. Psychiatry
24
491-500
2019
Mus musculus (O88455), Mus musculus
brenda
Zhang, M.; Song, M.; Cheng, F.; Yang, Z.; Davoudi, M.; Chen, J.; Lou, Q.
Identification of a putative candidate gene encoding 7-dehydrocholesterol reductase involved in brassinosteroids biosynthesis for compact plant architecture in Cucumber (Cucumis sativus L.)
Theor. Appl. Genet.
134
2023-2034
2021
Cucumis sativus (A0A0A0KC98), Cucumis sativus
brenda