Mostrando 10 resultados de: 11
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Journal of Clinical Endocrinology and Metabolism(6)
Cytochrome P450: Structure, Mechanism, and Biochemistry, Fourth Edition(1)
Endocrine Research(1)
Journal of Biological Chemistry(1)
Molecular Endocrinology(1)
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Bioquímica(5)
Enfermedades(3)
Fisiología humana(2)
Medicina y salud(2)
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scopus(11)
Congenital adrenal hyperplasia due to steroid 21-hydroxylase deficiency: An endocrine society* clinical practice guideline
ArticleAbstract: Objective: To update the congenital adrenal hyperplasia due to steroid 21-hydroxylase deficiency cliPalabras claves:Autores:Arlt W., Baskin L.S., Conway G.S., Merke D.P., Meyer-Bahlburg H.F.L., Miller W.L., Murad M.H., Oberfield S.E., Richard J. Auchus, Speiser P.W., White P.C.Fuentes: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:scopusErratum: Congenital adrenal hyperplasia due to steroid 21-hydroxylase deficiency: An endocrine society clinical practice guideline (The Journal of Clinical Endocrinology and Metabolism (2018) 103:11 (4043-4088) DOI: 10.1210/jc.2018-01865)
OtherAbstract: The above-mentioned guideline by Speiser PW, Azziz R, Baskin LS, Ghizzoni L, Hensle TW, Merke DP, MePalabras claves:Autores:Arlt W., Baskin L.S., Conway G.S., Merke D.P., Meyer-Bahlburg H.F.L., Miller W.L., Murad M.H., Oberfield S.E., Richard J. Auchus, Speiser P.W., White P.C.Fuentes: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:scopusThe 17, 20-lyase activity of cytochrome P450c17 from human fetal testis favors the Δ<sup>5</sup> steroidogenic pathway
ArticleAbstract: Cytochrome P450c17 catalyzes both 17α-hydroxylation and 17,20-lyase conversion of 21-carbon steroidsPalabras claves:Autores:Flück C.E., Miller W.L., Richard J. AuchusFuentes:scopusThe regulation of 17,20 lyase activity
Conference ObjectAbstract: P450c17 is a single microsomal enzyme that catalyzes two distinct steroid biosynthetic activities: 1Palabras claves:17α-hydroxylase, adrenarche, molecular modeling, P450c17, serine phosphorylation, sex steroidAutores:Geller D.H., Miller W.L., Richard J. AuchusFuentes:scopus