ArticleThe Journal of steroid biochemistry and molecular biology2021
Characterization of human adrenal cytochrome P450 11B2 products of progesterone and androstenedione oxidation.
Article in The Journal of steroid biochemistry and molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 10 citations in OpenAlex.
- Cannabis consumption is associated with altered steroid metabolism in young men.Communications medicine · 2026Article
- The Role of Cytochrome P450 Enzymes in COVID-19 Pathogenesis and Therapy.Frontiers in pharmacology · 2022Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome P450 (P450) 11B1 and 11B2 both catalyze the 11β-hydroxylation of 11-deoxycorticosterone and the subsequent 18-hydroxylation of the product. P450 11B2, but not P450 11B1, catalyzes a further C-18 oxidation to yield aldosterone. 11-Oxygenated androgens are of interest, and 11-hydroxy progesterone has been reported to be a precursor of these. Oxidation of progesterone by purified recombinant P450 11B2 yielded a mono-hydroxy derivative as the major product, and co-chromatography with commercial standards and 2-D NMR spectroscopy indicated 11β-hydroxylation. 18-Hydroxyprogesterone and a dihydroxyprogesterone were also formed. Similarly, oxidation of androstenedione by P450 11B2 yielded 11β-hydroxyandrostenedione, 18-hydroxyandrostenedione, and a dihydroxyandrostenedione. The steady-state kinetic parameters for androstenedione and progesterone 11β-hydroxylation were similar to those reported for the classic substrate 11-deoxycorticosterone. The source of 11α-hydroxyprogesterone in humans remains unresolved.
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Registered trials
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