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26,27-dehydrozymosterol
5beta-cholest-7-en-3beta-ol
-
-
?
26,27-dinorcholesta-8,24-dienol
26,27-dinorcholesta-7,24-dienol
-
-
?
26-homo-cholesta-8(9),23(24) E26(26')-trienol
26-homo-cholesta-7(8),23(24)E26(26')trienol
-
-
?
4alpha-methyl-5alpha-ergosta-8,24-dien-3beta-ol
24-methylenelophenol
-
-
i.e. 4alpha-methyl-5alpha-ergosta-7,24-dien-3beta-ol
-
?
4alpha-methyl-ergosta-8,24-dien-3beta-ol
?
-
-
-
-
?
4alpha-methyl-fecosterol
4alpha-methyl-ergosta-7,24-dien-3beta-ol
-
-
-
-
?
5alpha-Cholest-7-en-3beta-ol
5alpha-Cholest-8-en-3beta-ol
5alpha-cholest-7-en-3beta-ol
?
enzyme of the cholesterol biosynthetic pathway, mutations are associated with Conradi-Huenermann syndrome. The enzyme may be involved in liver function, since the mRNA is only detected in hepatocytes not in connective tissue or blood vessels. The expression of the SI gene is regulated transcriptionally in vitro and in vivo by widely known regulatory agents ranging from tamoxifen, an oestrogen receptor antagonist and SI-specific inhibitor, to cholesterol-lowering drugs
-
?
5alpha-cholesta-8,24-dien-3beta-ol
5alpha-cholesta-7,24-dien-3beta-ol
cholest-8-enol
cholest-7-enol
-
-
?
cholesta-8,24-dien-3beta-ol
?
-
-
-
-
?
DELTA8-sitostenol
stigmast-7-en-3beta-ol
-
-
-
-
?
dihydrozymosterol
lathosterol
-
-
-
-
?
fecosterol
24-methylene-5alpha-cholest-7-en-3beta-ol
-
-
?
stigmasta-8-en-3beta-ol
?
-
-
-
-
?
zymosterol
cholesta-7,24-dienol
additional information
?
-
5alpha-Cholest-7-en-3beta-ol
5alpha-Cholest-8-en-3beta-ol
-
-
-
?
5alpha-Cholest-7-en-3beta-ol
5alpha-Cholest-8-en-3beta-ol
-
r
-
?
5alpha-Cholest-7-en-3beta-ol
5alpha-Cholest-8-en-3beta-ol
-
r
-
?
5alpha-cholesta-8,24-dien-3beta-ol
5alpha-cholesta-7,24-dien-3beta-ol
-
-
-
-
?
5alpha-cholesta-8,24-dien-3beta-ol
5alpha-cholesta-7,24-dien-3beta-ol
-
-
-
?
zymostenol
lathosterol
-
-
-
-
?
zymostenol
lathosterol
-
-
-
-
?
zymostenol
lathosterol
-
-
-
-
?
zymostenol
lathosterol
-
-
-
-
?
zymosterol
cholesta-7,24-dienol
-
-
-
-
?
zymosterol
cholesta-7,24-dienol
preferred substrate for DELTA7-sterol production, the reaction equilibrium for double-bond isomerization favours the forward direction, DELTA8 to DELTA7
-
r
zymosterol
cholesta-7,24-dienol
-
primary substrate
-
-
?
zymosterol
cholesta-7,24-dienol
-
-
-
-
?
zymosterol
cholesta-7,24-dienol
-
primary substrate
-
-
?
zymosterol
cholesta-7,24-dienol
-
primary substrate
-
-
?
zymosterol
cholesta-7,24-dienol
-
-
-
-
?
zymosterol
cholesta-7,24-dienol
-
primary substrate
-
-
?
additional information
?
-
3-desoxyzymosterol is not an active substrate
-
?
additional information
?
-
-
4,4-dimethyl-cholesta-8,24-dien-3beta-ol, 4,4-dimethyl-ergosta-8,24-dien-3beta-ol, 4alpha,14aloha-dimethyl-ergosta-8,24-dien-3beta-ol, and cholest-8(14)-en-3beta-ol are no substrates
-
-
?
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(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-aminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
-
-
(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-N-methylaminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
-
-
(1'R,3a'R,7a'R,1''R)-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitro-5-[[2-(pyrrolidin-1yl)ethyl]aminomethyl]spiro[1,3-dioxane-2,4'-octahydroindene]
-
-
(1'R,3a'R,7a'R,1''R)-7a'-methyl-5-[N-(N,N-dimethylaminoeth-2-yl-aminomethyl)-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]]
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-[methyl(pent-4-en-1-yl)amino]octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(1R,3aR,4R,5S,7aR)-5-[benzyl(pent-4-en-1-yl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
(R,S)-1-cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydronaphthalen-1-yl)-n-propyl]piperazine
-
-
1',2',3',4'-tetrahydro-5-(N-benzylpiperidin-4-yl)-aminomethyl-5-nitro-6'-(4-methylpentyloxy)-spiro[1,3-dioxane-2,1'-naphthaline]
-
-
1',2',3',4'-tetrahydro-5-(N-benzylpiperidin-4-yl)-aminomethyl-6'-methoxy-5-nitrospiro[1,3-dioxane-2,1'-naphthaline]
-
-
1,3-di-2-tolylguanidine
-
-
1-cyclohexyl-4-[cis-4-(2,6-difluorophenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[cis-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[cis-4-(2-methoxyphenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[cis-4-(2-methylphenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[cis-4-(4-methoxyphenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[trans-4-(2,6-difluorophenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[trans-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[trans-4-(2-methoxyphenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[trans-4-(2-methylphenyl)cyclohexyl]piperazine
-
-
1-cyclohexyl-4-[trans-4-(4-methoxyphenyl)cyclohexyl]piperazine
-
-
1-[(6-methoxy-1,2,3,4-tetrahydronaphthalen-2-yl)methyl]-4-pyridin-2-ylpiperazine
-
-
1-[4-(3-methoxyphenyl)cyclohex-3-en-1-yl]-4-phenylpiperazine
-
-
1-[4-(3-methoxyphenyl)cyclohex-3-en-1-yl]-4-pyridin-2-ylpiperazine
-
-
1-[4-(3-methoxyphenyl)cyclohexyl]-4-phenylpiperazine
-
-
1-[cis-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
-
-
1-[cis-4-(2-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
1-[cis-4-(3-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
1-[cis-4-(4-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
1-[trans-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
-
-
1-[trans-4-(2-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
1-[trans-4-(3-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
1-[trans-4-(4-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
2-[4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy]-N,N-dimethylethanamine
-
noncompetitive, IC50: 0.00025 mM
3-[4-(4-naphthalen-1-ylpiperazin-1-yl)cyclohexyl]phenyl hydroperoxide
-
-
3beta-[2-(diethylamino)ethoxy]androst-5-en-17-one
IC50: 0.0042 mM
4-[1-(2,6-dimethylphenyl)-3-cyclohexen-4-yl]-1-(2-pyridinyl)piperazine
-
-
cis-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
-
-
cis-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
-
-
cis-4-(4-phenylcyclohexyl)-1-(2-pyridinyl)piperazine
-
-
cis-4-[4-(2,6-difluorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
cis-4-[4-(2,6-dimethylyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
cis-4-[4-(2-chlorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
cis-4-[4-(2-methylphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
N,N-dipropyl-2-[4-methoxy-3-(2-phenylethoxy)phenyl]ethylamine
-
-
N-(2-phenylethyl)piperidine
-
-
trans-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
-
-
trans-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
-
-
trans-2-[4-(1,2-diphenylbuten-1-yl)phenoxy]-N,N-dimethylethylamine
IC50: 0.0112 mM
trans-4-(4-phenylcyclohexyl)-1-(2-pyridinyl)piperazine
-
-
trans-4-[4-(2,6-difluorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
trans-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
trans-4-[4-(2-chlorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
trans-4-[4-(2-methylphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
(+)-emopamil
-
(+)-pentazocine
-
-
(+)-pentazocine
-
i.e. (+)-[2S-(2R,6R,11R)]-1,2,3,4,5,6-hexahydro-6,11-dimethyl-3-(3-methyl-2-butenyl)-2,6-methano-3-benzazocine-8-ol
(+)-verapamil
-
(-)-emopamil
IC50: 28 nM for the liver enzyme, IC50: 34 nM for the brain enzyme
(-)-verapamil
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-(pent-4-en-1-ylamino)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-[methyl(pent-4-en-1-yl)amino]octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-[methyl(pent-4-en-1-yl)amino]octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-[methyl(pent-4-en-1-yl)amino]octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)-5-[methyl(pent-4-en-1-yl)amino]octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(benzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-(dibenzylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-amino-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(methyl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(pent-4-en-1-yl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(pent-4-en-1-yl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(pent-4-en-1-yl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,4R,5S,7aR)-5-[benzyl(pent-4-en-1-yl)amino]-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
(1R,3aR,5S,7aR)-5-(dimethylamino)-3a,7a-dimethyl-1-(6-methylheptan-2-yl)octahydro-1H-inden-4-ol
-
-
amiodarone
-
AY9944
-
BM15766
-
CuCl2
IC50: 0.01 mM, ifenprodil-labeled enzyme
CuCl2
IC50: 0.0023 mM, ifenprodil-labeled enzyme
CuCl2
IC50: 0.0011 mM, ifenprodil-labled enzyme
CuCl2
-
IC50: 0.57 mM, ifenprodil-labeled enzyme
ditolylguanidine
IC50: 122 nM for the liver enzyme, IC50: 36 nM for the brain enzyme
enclomiphene
-
fenpropimorph
-
haloperidol
-
-
haloperidol
IC50: 6.8 nM for the liver enzyme, 23 nM for the brain enzyme
ifenprodil
-
-
ifenprodil
IC50: 2.4 nM for the liver enzyme, 1.7 nM for the brain enzyme
L690404
-
MDL28815
-
MDL5332
-
nafoxidine
-
naftifine
-
opipramol
-
SR31747
-
-
tamoxifen
-
terbinafine
-
tridemorph
-
Trifluoperazine
IC50: 11 nM for the liver enzyme, IC50: 13 nM for the brain enzyme
trifluperidol
-
Triparanol
-
U18666A
-
verapamil
-
-
ZnCl2
IC50: 0.001 mM, ifenprodil-labeled enzyme
ZnCl2
IC50: 0.0006 mM, ifenprodil-labeled enzyme
ZnCl2
IC50: 0.001 mM, ifenprodil-labeled enzyme
ZnCl2
-
IC50: 0.0044 mM, ifenprodil-labeled enzyme
zuclomiphene
-
additional information
-
not inhibited by N-benzamido-decalin, tamoxifen, N-benzyl-8-azadecalin, and AY9944
-
additional information
-
not inhibited by N-benzamido-decalin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Antley-Bixler Syndrome Phenotype
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Candidiasis
ERG2 and ERG24 Are Required for Normal Vacuolar Physiology as Well as Candida albicans Pathogenicity in a Murine Model of Disseminated but Not Vaginal Candidiasis.
cholestenol delta-isomerase deficiency
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Chondrodysplasia Punctata
A novel EBP c.224T>A mutation supports the existence of a male-specific disorder independent of CDPX2.
Chondrodysplasia Punctata
A novel X-linked multiple congenital anomaly syndrome associated with an EBP mutation.
Chondrodysplasia Punctata
Characterization of mutations in 22 females with X-linked dominant chondrodysplasia punctata (Happle syndrome).
Chondrodysplasia Punctata
Cloning of an emopamil-binding protein (EBP)-like protein that lacks sterol delta8-delta7 isomerase activity.
Chondrodysplasia Punctata
Conradi-Hünermann-Happle syndrome (X-linked dominant chondrodysplasia punctata) confirmed by plasma sterol and mutation analysis.
Chondrodysplasia Punctata
Gas chromatography-mass spectrometry and molecular genetic studies in families with the Conradi-Hünermann-Happle syndrome.
Chondrodysplasia Punctata
Male CDPX2 patient with EBP mosaicism and asymmetrically lateralized skin lesions with strict midline demarcation.
Chondrodysplasia Punctata
Prenatal testing for a novel EBP missense mutation causing X-linked dominant chondrodysplasia punctata.
Chondrodysplasia Punctata
Pustular Skin Lesions in an Adult Female Patient with X-linked Dominant Chondrodysplasia Punctata with a Novel Emopamil Binding Protein Mutation: A Rare Skin Manifestation.
Chondrodysplasia Punctata
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Chondrodysplasia Punctata
The Conradi-Hünermann-Happle syndrome (CDPX2) and emopamil binding protein: novel mutations, and somatic and gonadal mosaicism.
Chondrodysplasia Punctata
X-linked dominant chondrodysplasia punctata with severe phenotype in a female fetus: A case report.
Colorectal Neoplasms
A perspective on medicinal chemistry approaches towards adenomatous polyposis coli and Wnt signal based colorectal cancer inhibitors.
Demyelinating Diseases
[Mechanisms underlying remyelination with special focus on demyelination models of multiple sclerosis].
Foot-and-Mouth Disease
Single-cell analysis reveals the relevance of foot-and-mouth disease virus persistence to emopamil-binding protein gene expression in host cells.
Infections
ERG2 and ERG24 Are Required for Normal Vacuolar Physiology as Well as Candida albicans Pathogenicity in a Murine Model of Disseminated but Not Vaginal Candidiasis.
Neoplasms
Cholesterol epoxide hydrolase and cancer.
Neoplasms
Isolation of differentially expressed genes in NPM-ALK-positive anaplastic large cell lymphoma.
Neoplasms
Prenatal diagnosis of fetal skeletal dysplasia using targeted next-generation sequencing: an analysis of 30 cases.
Nevus
Male CDPX2 patient with EBP mosaicism and asymmetrically lateralized skin lesions with strict midline demarcation.
Protein Deficiency
Radiographic features of the skeleton in disorders of post-squalene cholesterol biosynthesis.
Psoriasis
Emopamil binding protein mutation in conradi-hünermann-happle syndrome representing plaque-type psoriasis.
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0.0000023 - 0.000077
(+)-emopamil
0.01
(+)-pentazocine
-
Ki above 0.01 mM
0.00089 - 0.00407
(+)-verapamil
0.0000147 - 0.0000164
(+/-)-ifenprodil
0.00001 - 0.000023
(-)-emopamil
0.00152 - 0.0029
(-)-verapamil
0.00766
1,3-di-2-tolylguanidine
-
-
0.000016
1-cyclohexyl-4-[cis-4-(2,6-difluorophenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000076
1-cyclohexyl-4-[cis-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000041
1-cyclohexyl-4-[cis-4-(2-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.000009
1-cyclohexyl-4-[cis-4-(2-methylphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.00000651
1-cyclohexyl-4-[cis-4-(4-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.000018
1-cyclohexyl-4-[trans-4-(2,6-difluorophenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.000011
1-cyclohexyl-4-[trans-4-(2,6-dimethoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000107
1-cyclohexyl-4-[trans-4-(2-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.00000973
1-cyclohexyl-4-[trans-4-(2-methylphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000136
1-cyclohexyl-4-[trans-4-(4-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000321
1-[(6-methoxy-1,2,3,4-tetrahydronaphthalen-2-yl)methyl]-4-pyridin-2-ylpiperazine
-
-
0.00046
1-[4-(3-methoxyphenyl)cyclohex-3-en-1-yl]-4-phenylpiperazine
-
-
0.00264
1-[4-(3-methoxyphenyl)cyclohex-3-en-1-yl]-4-pyridin-2-ylpiperazine
-
-
0.00171
1-[4-(3-methoxyphenyl)cyclohexyl]-4-phenylpiperazine
-
-
0.0000169
1-[cis-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
-
pH and temperature not specified in the publication
0.00000815
1-[cis-4-(2-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
0.0000454
1-[cis-4-(3-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
0.0000328
1-[cis-4-(4-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
0.0000206
1-[trans-4-(2-chlorophenyl)cyclohexyl]-4-cyclohexylpiperazine
-
pH and temperature not specified in the publication
0.0000135
1-[trans-4-(2-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
0.0000162
1-[trans-4-(3-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
0.0000716
1-[trans-4-(4-methoxyphenyl)cyclohexyl]-4-pyridin-2-ylpiperazine
-
-
0.021
25-Azacholesterol
-
0.0000167
3-[4-(4-naphthalen-1-ylpiperazin-1-yl)cyclohexyl]phenyl hydroperoxide
-
-
0.0000467
4-[1-(2,6-dimethylphenyl)-3-cyclohexen-4-yl]-1-(2-pyridinyl)piperazine
-
-
0.000016 - 0.00006
amiodarone
0.0000123
cis-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
-
pH and temperature not specified in the publication
0.0000126
cis-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000492
cis-4-(4-phenylcyclohexyl)-1-(2-pyridinyl)piperazine
-
-
0.00014
cis-4-[4-(2,6-difluorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.00000495
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
0.0000331
cis-4-[4-(2,6-dimethylyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.0000851
cis-4-[4-(2-chlorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.000005
cis-4-[4-(2-methylphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.0043 - 0.0144
ditolylguanidine
0.00000069
enclomiphene
-
0.000035 - 0.000435
haloperidol
0.000001 - 0.0000023
L690404
0.00000067 - 0.000054
MDL5332
0.0000146
N,N-dipropyl-2-[4-methoxy-3-(2-phenylethoxy)phenyl]ethylamine
-
-
0.000595
N-(2-phenylethyl)piperidine
-
-
0.0000009 - 0.000232
nafoxidine
0.00031 - 0.0015
naftifine
0.0000038 - 0.000047
opipramol
0.0000028 - 0.001
tamoxifen
0.0000142
trans-1-cyclohexyl-4-(4-phenylcyclohexyl)piperazine
-
pH and temperature not specified in the publication
0.0000004
trans-1-cyclohexyl-4-[(3-methoxyphenyl)cyclohexyl]piperazine
-
pH and temperature not specified in the publication
0.0000168
trans-4-(4-phenylcyclohexyl)-1-(2-pyridinyl)piperazine
-
-
0.000106
trans-4-[4-(2,6-difluorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.000007
trans-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.00000721
trans-4-[4-(2-chlorophenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.00000904
trans-4-[4-(2-methylphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.0000013 - 0.001
tridemorph
0.0000036 - 0.0000077
Trifluoperazine
0.0000039
trifluoroperazine
-
0.0000001 - 0.0019
U18666A
0.0000023
(+)-emopamil
-
0.00089
(+)-verapamil
-
0.0000147
(+/-)-ifenprodil
-
pH and temperature not specified in the publication
0.0000164
(+/-)-ifenprodil
-
-
0.00001
(-)-emopamil
-
0.00152
(-)-verapamil
-
0.000016
amiodarone
-
0.01648
BM15766
-
-
0.00000495
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
-
0.00000495
cis-4-[4-(2,6-dimethoxyphenyl)cyclohexyl]-1-(2-pyridinyl)piperazine
-
pH and temperature not specified in the publication
0.0043
ditolylguanidine
-
0.0106
ditolylguanidine
-
0.0144
ditolylguanidine
-
0.000035
haloperidol
-
0.000001
L690404
-
0.00000067
MDL5332
-
-
0.0000009
nafoxidine
-
0.00031
naftifine
-
-
0.0000038
opipramol
-
0.0000028
tamoxifen
-
0.0000013
tridemorph
-
0.0000036
Trifluoperazine
-
0.0000077
Trifluoperazine
-
0.0000001
U18666A
-
-
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0.000028 - 0.000034
(-)-emopamil
0.0017
(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-aminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
(1'R,3a'R,7a'R,1''R)-5-(N-benzylpiperidin-4-yl)-N-methylaminomethyl-7a'-methyl-1'-(1,5-dimethylhexyl)-5-nitrospiro[1,3-dioxane-2,4'-octahydroindene]
Homo sapiens
-
pH and temperature not specified in the publication
0.0045
1',2',3',4'-tetrahydro-5-(N-benzylpiperidin-4-yl)-aminomethyl-5-nitro-6'-(4-methylpentyloxy)-spiro[1,3-dioxane-2,1'-naphthaline]
Homo sapiens
-
pH and temperature not specified in the publication
0.00025
2-[4-[(1Z)-1,2-diphenylbut-1-en-1-yl]phenoxy]-N,N-dimethylethanamine
Rattus norvegicus
-
noncompetitive, IC50: 0.00025 mM
0.0042
3beta-[2-(diethylamino)ethoxy]androst-5-en-17-one
Rattus norvegicus
IC50: 0.0042 mM
0.0001
AY9944
Zea mays
-
-
0.000036 - 0.000122
ditolylguanidine
0.00003 - 0.00021
fenpropimorph
0.0000068 - 0.000023
haloperidol
0.0000017 - 0.0000024
ifenprodil
0.0085
tamoxifen
Zea mays
-
-
0.0112
trans-2-[4-(1,2-diphenylbuten-1-yl)phenoxy]-N,N-dimethylethylamine
Rattus norvegicus
IC50: 0.0112 mM
0.00085 - 0.001
tridemorph
0.000011 - 0.5
Trifluoperazine
0.000028
(-)-emopamil
Cavia porcellus
IC50: 28 nM for the liver enzyme
0.000034
(-)-emopamil
Cavia porcellus
IC50: 34 nM for the brain enzyme
0.0011
CuCl2
Mus musculus
IC50: 0.0011 mM, ifenprodil-labled enzyme
0.0023
CuCl2
Homo sapiens
IC50: 0.0023 mM, ifenprodil-labeled enzyme
0.01
CuCl2
Cavia porcellus
IC50: 0.01 mM, ifenprodil-labeled enzyme
0.57
CuCl2
Saccharomyces cerevisiae
-
IC50: 0.57 mM, ifenprodil-labeled enzyme
0.000036
ditolylguanidine
Cavia porcellus
IC50: 36 nM for the brain enzyme
0.000122
ditolylguanidine
Cavia porcellus
IC50: 122 nM for the liver enzyme
0.00003
fenpropimorph
Saccharomyces cerevisiae
-
-
0.00021
fenpropimorph
Zea mays
-
-
0.0000068
haloperidol
Cavia porcellus
IC50: 6.8 nM for the liver enzyme
0.000023
haloperidol
Cavia porcellus
23 nM for the brain enzyme
0.0000017
ifenprodil
Cavia porcellus
1.7 nM for the brain enzyme
0.0000024
ifenprodil
Cavia porcellus
IC50: 2.4 nM for the liver enzyme
0.0001
SR31747
Zea mays
-
-
0.0006
SR31747
Saccharomyces cerevisiae
-
-
0.00085
tridemorph
Zea mays
-
-
0.001
tridemorph
Saccharomyces cerevisiae
-
-
0.000011
Trifluoperazine
Cavia porcellus
IC50: 11 nM for the liver enzyme
0.000013
Trifluoperazine
Cavia porcellus
IC50: 13 nM for the brain enzyme
0.001
Trifluoperazine
Zea mays
-
-
0.5
Trifluoperazine
Saccharomyces cerevisiae
-
IC50 above 0.5 mM
0.0006
ZnCl2
Homo sapiens
IC50: 0.0006 mM, ifenprodil-labeled enzyme
0.001
ZnCl2
Mus musculus
IC50: 0.001 mM, ifenprodil-labeled enzyme
0.001
ZnCl2
Cavia porcellus
IC50: 0.001 mM, ifenprodil-labeled enzyme
0.0044
ZnCl2
Saccharomyces cerevisiae
-
IC50: 0.0044 mM, ifenprodil-labeled enzyme
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C121A
mutant enzyme with 95% of the in vivo activity of the wild-type enzyme
C128A
mutant enzyme with 81% of the in vivo activity of the wild-type enzyme
C68A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
C73A
mutant enzyme with 83% of the in vivo activity of the wild-type enzyme
E123A
mutant enzyme with 10% of the in vivo activity of the wild-type enzyme
E123D
mutant enzyme does not bind the inhibitor ifenprodil
E81A
mutant enzyme with 5% of the in vivo activity of the wild-type enzyme
E81D
mutant enzyme still binds the inhibitor ifenprodil
F186A
mutant enzyme with 56% of the in vivo activity of the wild-type enzyme
F188A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
F190A
mutant enzyme with 21% of the in vivo activity of the wild-type enzyme
F192A
mutant enzyme with 92% of the in vivo activity of the wild-type enzyme
F37A
mutant enzyme with 74% of the in vivo activity of the wild-type enzyme
F70A
mutant enzyme with 95% of the in vivo activity of the wild-type enzyme
F75A
mutant enzyme with 88% of the in vivo activity of the wild-type enzyme
F84A
mutant enzyme with 72% of the in vivo activity of the wild-type enzyme
G131A
mutant enzyme with 69% of the in vivo activity of the wild-type enzyme
G41A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
G82A/F84V
mutant enzyme with 56% of the in vivo activity of the wild-type enzyme
H31A
mutant enzyme with 69% of the in vivo activity of the wild-type enzyme
H77A
mutant enzyme with 9% of the in vivo activity of the wild-type enzyme
H77N
mutant enzyme does not bind the inhibitor ifenprodil
I125A
mutant enzyme with 78% of the in vivo activity of the wild-type enzyme
I139A
mutant enzyme with 90% of the in vivo activity of the wild-type enzyme
I32A
mutant enzyme with 73% of the in vivo activity of the wild-type enzyme
I76A
mutant enzyme with 33% of the in vivo activity of the wild-type enzyme
I76L/L78A
mutant enzyme with 74% of the in vivo activity of the wild-type enzyme
L129A
mutant enzyme with 81% of the in vivo activity of the wild-type enzyme
L133A
mutant enzyme with 77% of the in vivo activity of the wild-type enzyme
L135A
mutant enzyme with 92% of the in vivo activity of the wild-type enzyme
L196A
mutant enzyme with 62% of the in vivo activity of the wild-type enzyme
L198A
mutant enzyme with 50% of the in vivo activity of the wild-type enzyme
L204A
mutant enzyme with 77% of the in vivo activity of the wild-type enzyme
L33A
mutant enzyme with 47% of the in vivo activity of the wild-type enzyme
L35A
mutant enzyme with 62% of the in vivo activity of the wild-type enzyme
L43A
mutant enzyme with 103% of the in vivo activity of the wild-type enzyme
L49A
mutant enzyme with 108% of the in vivo activity of the wild-type enzyme
L50A
mutant enzyme with 96% of the in vivo activity of the wild-type enzyme
L65A
mutant enzyme with 82% of the in vivo activity of the wild-type enzyme
L67A
mutant enzyme with 63% of the in vivo activity of the wild-type enzyme
M122A
mutant enzyme with 28% of the in vivo activity of the wild-type enzyme
M193A
mutant enzyme with 53% of the in vivo activity of the wild-type enzyme
N194Q
mutant enzyme still binds the inhibitor ifenprodil
S134A
mutant enzyme with 101% of the in vivo activity of the wild-type enzyme
S38A
mutant enzyme with 74% of the in vivo activity of the wild-type enzyme
T124A
mutant enzyme with 91% of the in vivo activity of the wild-type enzyme
T126A
mutant enzyme with 4% of the in vivo activity of the wild-type enzyme
T126S
mutant enzyme still binds the inhibitor ifenprodil
V120A
mutant enzyme with 62% of the in vivo activity of the wild-type enzyme
V138A
mutant enzyme with 94% of the in vivo activity of the wild-type enzyme
V191A
mutant enzyme with 91% of the in vivo activity of the wild-type enzyme
V199A
mutant enzyme with 76% of the in vivo activity of the wild-type enzyme
V203A
mutant enzyme with 71% of the in vivo activity of the wild-type enzyme
V39A
mutant enzyme with 80% of the in vivo activity of the wild-type enzyme
V44A
mutant enzyme with 76% of the in vivo activity of the wild-type enzyme
V45A
mutant enzyme with 79% of the in vivo activity of the wild-type enzyme
V72A
mutant enzyme with 93% of the in vivo activity of the wild-type enzyme
V79A
mutant enzyme with 75% of the in vivo activity of the wild-type enzyme
V85A
mutant enzyme with 68% of the in vivo activity of the wild-type enzyme
W130A
mutant enzyme with 70% of the in vivo activity of the wild-type enzyme
W136A
mutant enzyme with 104% of the in vivo activity of the wild-type enzyme
W187A
mutant enzyme with 56% of the in vivo activity of the wild-type enzyme
W197A
mutant enzyme with 5% of the in vivo activity of the wild-type enzyme
W197F
mutant enzyme still binds the inhibitor ifenprodil
W48A
mutant enzyme with 87% of the in vivo activity of the wild-type enzyme
W69A
mutant enzyme with 17% of the in vivo activity of the wild-type enzyme
W83A
mutant enzyme with 97% of the in vivo activity of the wild-type enzyme
Y185A
mutant enzyme with 64% of the in vivo activity of the wild-type enzyme
Y189A
mutant enzyme with 32% of the in vivo activity of the wild-type enzyme
E116V
-
mutant exhibits 72% of wild type activity
E73V
-
mutant exhibits 100% of wild type activity
H69L
-
mutant exhibits 70% of wild type activity
T124I
-
mutant exhibits 10% of wild type activity
additional information
-
functional complementation by C-8,7 sterol isomerase of the corresponding sterol mutant in yeast and its characterization by exposure to sigma ligands. The full-length Arabidosis thaliana cDNA encoding C-8,7 sterol isomerase complements the erg2 mutation
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Lee, W.H.; Kammereck, R.; Lutsky, B.N.; McCloskey, J.A.; Schroepfer, G.J.Jr.
Studies on the mechanism of the enzymatic conversion of DELTA8-cholesten-3beta-ol to DELTA7-cholesten-3beta-ol
J. Biol. Chem.
244
2033-2040
1969
Rattus norvegicus
brenda
Wilton, D.C.; Rahimtula, A.D.; Akhtar, M.
The reversibility of the DELTA8-cholestenol-DELTA7-cholestenol isomerase reaction in cholesterol biosynthesis
Biochem. J.
114
71-73
1969
Rattus norvegicus
brenda
Scala, A.; Galli-Kienle, M.; Anastasia, M.; Galli, G.
The reversibility of the isomerization of the DELTA8 to DELTA7 bond in cholesterol biosynthesis
Eur. J. Biochem.
48
263-269
1974
Rattus norvegicus
brenda
Bae, S.H.; Seong, J.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: molecular cloning, chromosomal localization, functional expression and liver-specific gene regulation of rat sterol DELTA8-isomerase, a cholesterogenic enzyme with multiple functions
Biochem. J.
353
689-699
2001
Rattus norvegicus (Q9JJ46)
brenda
Nes, W.D.; Zhou, W.; Dennis, A.L.; Li, H.; Jia, Z.; Keith, R.A.; Piser, T.M.; Furlong, S.T.
Purification, characterization and catalytic properties of human sterol 8-isomerase
Biochem. J.
367
587-599
2002
Homo sapiens (Q15125)
brenda
Moebius, F.F.; Soellner, K.E.M.; Fiechtner, B.; Huck, C.W.; Bonn, G.; Glossmann, H.
Histidine77, glutamic acid81, glutamic acid123, threonine126, asparagine194, and tryptophan197 of the human emopamil binding protein are required for in vivo sterol DELTA8-DELTA7 isomerization
Biochemistry
38
1119-1127
1999
Homo sapiens (Q15125), Homo sapiens
brenda
Cho, S.Y.; Kim, J.H.; Paik, Y.K.
Cholesterol biosynthesis from lanosterol: differential inhibition of sterol DELTA8-isomerase and other lanosterol-converting enzymes by tamoxifen
Mol. Cells
8
233-239
1998
Rattus norvegicus
brenda
Moebius, F.F.; Reiter, R.J.; Bermoser, K.; Glossmann, H.; Cho, S.Y.; Paik, Y.K.
Pharmacological analysis of sterol DELTA8-DELTA7-isomerase proteins with [3H]ifenprodil
Mol. Pharmacol.
54
591-598
1998
Saccharomyces cerevisiae, Mus musculus (P70245), Homo sapiens (Q15125), Homo sapiens, Cavia porcellus (Q60490)
brenda
Grebenok, R.J.; Ohnmeiss, T.E.; Yamamoto, A.; Huntley, E.D.; Galbraith, D.W.; Della Penna, D.
Isolation and characterization of an Arabidopsis thaliana C-8,7 sterol isomerase: functional and structural similarities to mammalian C-8,7 sterol isomerase/emopamil-binding protein
Plant Mol. Biol.
38
807-815
1998
Arabidopsis thaliana
brenda
Kedjouar, B.; de Medina, P.; Oulad-Abdelghani, M.; Payre, B.; Silvente-Poirot, S.; Favre, G.; Faye, J.C.; Poirot, M.
Molecular characterization of the microsomal tamoxifen binding site
J. Biol. Chem.
279
34048-34061
2004
Homo sapiens
brenda
Rahier, A.; Pierre, S.; Riveill, G.; Karst, F.
Identification of essential amino acid residues in a sterol 8,7-isomerase from Zea mays reveals functional homology and diversity with the isomerases of animal and fungal origin
Biochem. J.
414
247-259
2008
Saccharomyces cerevisiae, Zea mays
brenda
Berardi, F.; Abate, C.; Ferorelli, S.; de Robertis, A.F.; Leopoldo, M.; Colabufo, N.A.; Niso, M.; Perrone, R.
Novel 4-(4-aryl)cyclohexyl-1-(2-pyridyl)piperazines as DELTA8-DELTA7 sterol isomerase (emopamil binding protein) selective ligands with antiproliferative activity
J. Med. Chem.
51
7523-7531
2008
Homo sapiens
brenda
Abate, C.; Niso, M.; Contino, M.; Colabufo, N.A.; Ferorelli, S.; Perrone, R.; Berardi, F.
1-Cyclohexyl-4-(4-arylcyclohexyl)piperazines: Mixed sigma and human DELTA8-DELTA7 sterol isomerase ligands with antiproliferative and P-glycoprotein inhibitory activity
ChemMedChem
6
73-80
2011
Homo sapiens
brenda
Krojer, M.; Mueller, C.; Bracher, F.
Steroidomimetic aminomethyl spiroacetals as novel inhibitors of the enzyme DELTA8,7-sterol isomerase in cholesterol biosynthesis
Arch. Pharm.
347
108-122
2014
Homo sapiens
brenda
Koenig, M.; Mueller, C.; Bracher, F.
Stereoselective synthesis of a new class of potent and selective inhibitors of human DELTA8,7-sterol isomerase
Bioorg. Med. Chem.
21
1925-1943
2013
Saccharomyces cerevisiae, [Candida] glabrata, Yarrowia lipolytica, Homo sapiens
brenda