Evidence map›Paper›PMID 25482340›Full record

ReviewThe Journal of steroid biochemistry and molecular biology2015

The diverse chemistry of cytochrome P450 17A1 (P450c17, CYP17A1).

Francis K Yoshimoto, Richard J Auchus

Abstract readReview
In one paragraph

Review in The Journal of steroid biochemistry and molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed, 1 pooled it
9.4field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed, 1 synthesis or guideline pooled it, 110 citations in OpenAlex.

  1. Pooled it
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  15. Biotransformation of ΔInternational journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Francis K YoshimotoDepartment of Biochemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, United States.
Richard J AuchusDivision of Metabolism, Diabetes, and Endocrinology, Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48019, United States. Electronic address: rauchus@med.umich.edu.
University of Michigan–Ann Arbor · USVanderbilt University · US

Funding

Activation of androgen biosynthesis and drug metabolism by cytochrome b5R01GM086596 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RICHARD J. AUCHUS · 2009 to 2026
$4.8M
NIGMS NIH HHS R01 GM086596NIGMS NIH HHS R01GM086596
6 · The paper itself

Abstract

The steroid hydroxylation and carbon-carbon bond cleavage activities of cytochrome P450 17A1 (CYP17A1) are responsible for the production of glucocorticoids and androgens, respectively. The inhibition of androgen synthesis is an important strategy to treat androgen-dependent prostate cancer. We discuss the different enzymatic activities towards the various substrates of CYP17A1, demonstrating its promiscuity. Additionally, a novel interhelical interaction is proposed between the F-G loop and the B'-helix to explain the 16α-hydroxylase activity of human CYP17A1 with progesterone as the substrate. The techniques used by biochemists to study this important enzyme are also summarized. This article is part of a Special Issue entitled 'Steroid/Sterol signaling'.

Indexed as

Steroid 17-alpha-HydroxylaseAnimalsCatalysisHumansSteroidsSubstrate SpecificityCYP17A1 protein, humanSteroid 17-alpha-HydroxylaseSteroids17,20-Lyase17-HydroxylaseAndrogenCytochrome P450HypertensionMetabolic switchingSteroidogenesis

Identifiers

PMID25482340
PMCPMC4456341
OpenAlexW1989552101

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.