Mostrando 10 resultados de: 17
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Journal of Clinical Endocrinology and Metabolism(5)
Endocrine Research(2)
Journal of Biological Chemistry(2)
Molecular Endocrinology(2)
Cytochrome P450: Structure, Mechanism, and Biochemistry, Fourth Edition(1)
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Farmacología y terapéutica(9)
Bioquímica(8)
Fisiología humana(6)
Enfermedades(5)
Química orgánica(2)
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scopus(17)
Clinical, biochemical, and molecular characterization of macronodular adrenocortical hyperplasia of the zona reticularis: A new syndrome
ArticleAbstract: Context: Macronodular adrenocortical hyperplasia classically presents with progressive hypercortisolPalabras claves:Autores:Carrick K., Ghayee H.K., Miller W.L., Nwariaku F.E., Rainey W.E., Rege J., Richard J. Auchus, Watumull L.Fuentes:scopusCytochrome b<inf>5</inf> augments the 17,20-lyase activity of human P450c17 without direct electron transfer
ArticleAbstract: In the biosynthesis of steroid hormones, P450c17 is the single enzyme that catalyzes both the 17α-hyPalabras claves:Autores:Lee T.C., Miller W.L., Richard J. AuchusFuentes:scopusEnzymatic activities of P450c17 stably expressed in fibroblasts from patients with the polycystic ovary syndrome
ArticleAbstract: Polycystic ovary syndrome (PCOS) is a common endocrine disorder affecting approximately 5-10% of womPalabras claves:Autores:Arlt W., Dunaif A., Geller D.H., Martens J.W.M., Miller W.L., Ossovskaya V.S., Richard J. Auchus, Rodriguez H.Fuentes:scopusMolecular evolution of adrenarche: Structural and functional analysis of P450c17 from four rimate species
ArticleAbstract: Adrenarche is the prepubertal onset of increased adrenal secretion of 19-carbon steroids, especiallyPalabras claves:Autores:Arlt W., Martens J.W.M., Miller W.L., Richard J. Auchus, Song M., Wang J.Fuentes:scopusMolecular modeling of human p450c17 (17α-hydroxylase/ 17,20-lyase) insights into reaction mechanisms and effects of mutations
ArticleAbstract: P450c17 (17α-hydroxylase/17,20-lyase) catalyzes steroid 17α-hydroxylase and 17,20-lyase activities iPalabras claves:Autores:Miller W.L., Richard J. AuchusFuentes:scopusP450 enzymes in steroid processing
Book PartAbstract: Steroid hormones are a group of biomolecules with similar structures derived from the common four-riPalabras claves:Autores:Miller W.L., Richard J. AuchusFuentes:scopusP450c17 mutations R347H and R358Q selectively disrupt 17,20-lyase activity by disrupting interactions with P450 oxidoreductase and cytochrome b<inf>5</inf>
ArticleAbstract: Cytochrome P450c17 catalyzes steroid 17α-hydroxylase and 17,20-lyase activities and hence is a key ePalabras claves:Autores:Geller D.H., Miller W.L., Richard J. AuchusFuentes:scopusMedroxyprogesterone acetate and dexamethasone are competitive inhibitors of different human steroidogenic enzymes
ArticleAbstract: Medroxyprogesterone acetate (MPA), a widely used progestin, can suppress the hypothalamic-pituitary-Palabras claves:Autores:Lee T.C., Miller W.L., Richard J. AuchusFuentes:scopusRole of cytochrome b<inf>5</inf> in the 17,20-lyase activity of P450c17 [3]
OtherAbstract:Palabras claves:Autores:Miller W.L., Richard J. AuchusFuentes:scopusProbing structural and functional domains of human P450c17
Conference ObjectAbstract: Human P450c17 performs at least six chemical transformations, but this spectrum of activity is diffePalabras claves:Autores:Geller D.H., Miller W.L., Richard J. Auchus, Worthy K.Fuentes:scopus