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scopus(57)
A-ring modified steroidal azoles retaining similar potent and slowly reversible CYP17A1 inhibition as abiraterone
ArticleAbstract: Abiraterone acetate is a potent inhibitor of human cytochrome P450c17 (CYP17A1, 17α-hydroxylase/17,2Palabras claves:abiraterone, androgen, CYP17A1, Cytochrome p450, Enzymology, Prostate cancer, steroidogenesisAutores:Bratoeff E., Garrido M., Peng H.M., Richard J. Auchus, Upadhyay S.K., Yoshimoto F.K.Fuentes:scopusCofactors, redox state, and directional preferences of hydroxysteroid dehydrogenases
ReviewAbstract: The hydroxysteroid dehydrogenases (HSDs) interconvert pairs of weak and potent steroids, thus servinPalabras claves:androgen, Equilibrium, Estrogen, Glucocorticoid, Hydroxysteroid dehydrogenase, Nicotinamide cofactor, Redox stateAutores:Agarwal A.K., Andersson S., Brandmaier A., Chattopadhyay A., Khan N., Papari-Zareei M., Rambally S., Richard J. Auchus, Sharma K.K., Sherbet D.P.Fuentes:scopusComparison of the hamster and human adrenal P450c17 (17α-hydroxylase/17,20-lyase) using site-directed mutagenesis and molecular modeling
ArticleAbstract: In order to understand the activity specificity of the hamster cytochrome P450 17α-hydroxylase/17,20Palabras claves:17,20-Lyase, 17α-hydroxylase, 3D modeling, Adrenals, CYP17, Cytochrome P450c17, HÁMSTER, Human, Mutants, Site-directed mutagenesisAutores:LeHoux J.G., Mathieu A.P., Richard J. AuchusFuentes:scopusBiochemical factors governing the steady-state estrone/estradiol ratios catalyzed by human 17β-hydroxysteroid dehydrogenases types 1 and 2 in HEK-293 cells
ArticleAbstract: Human 17β-hydroxysteroid dehydrogenase types 1 and 2 (17βHSD1 and 17βHSD2) regulate estrogen potencyPalabras claves:Autores:Akbar S., Guryev O.L., Mizrachi D., Papari-Zareei M., Rambally S., Richard J. Auchus, Sherbet D.P.Fuentes:scopusAndrogens, estrogens, and hydroxysteroid dehydrogenases
ReviewAbstract: The task of regulating both production and activity of potent androgens and estrogens in human physiPalabras claves:androgen, Equilibrium, Estrogen, Glucocorticoid, Hydroxysteroid dehydrogenase, Nicotinamide cofactor, Redox stateAutores:Mizrachi D., Richard J. AuchusFuentes:scopusCYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding
ArticleAbstract: Cytochrome P450c17 (CYP17) converts the C21 steroids pregnenolone and progesterone to the C19 androgPalabras claves:Autores:Hochberg Z., Kwist K.W., Richard J. Auchus, Sherbet D.P., Tiosano D.Fuentes:scopusCardiac decompensation and promiscuous prenylation of small GTPases in cardiomyocytes in response to local mevalonate pathway disruption<sup>†</sup>
OtherAbstract: Investigations of major mevalonate pathway enzymes have demonstrated the importance of local isoprenPalabras claves:CAAX motif, farnesyl diphosphate synthase, farnesylation, geranylgeranylation, mevalonate pathway, prenylation, RAS, Rheb, small GTPases, statinsAutores:Brody M.J., Essandoh K., Richard J. AuchusFuentes:scopusCatalytic modulation of human cytochromes P450 17A1 and P450 11B2 by phospholipid
ArticleAbstract: Unlike most of the drug-metabolizing cytochrome P450s, microsomal P450 17A1 and mitochondrial P450 1Palabras claves:P450 11B2, P450 17A1, phospholipidAutores:Barlow C., Peng H.M., Richard J. AuchusFuentes:scopusCatalytically relevant electrostatic interactions of cytochrome P450c17 (CYP17A1) and cytochrome b<inf>5</inf>
ArticleAbstract: Background: Cytochrome b5 (b5) stimulates the 17,20-lyase activity of cytochrome P450c17 (CYP17A1).Palabras claves:Autores:Anderson S.M., Forsberg S.E., Liu J., Peng H.M., Richard J. Auchus, Tran H.T.Fuentes:scopusArginine 276 controls the directional preference of AKR1C9 (rat liver 3α-hydroxysteroid dehydrogenase) in human embryonic kidney 293 cells
ArticleAbstract: Rat liver AKR1C9 is the best-studied 3α-hydroxysteroid dehydrogenase (3αHSD) of the aldo-keto reductPalabras claves:Autores:Brandmaier A., Papari-Zareei M., Richard J. AuchusFuentes:scopus