Evidence map›Paper›PMID 28684414›Full record

ArticleThe Journal of biological chemistry2017

Kinetic processivity of the two-step oxidations of progesterone and pregnenolone to androgens by human cytochrome P450 17A1.

Eric Gonzalez, F Peter Guengerich

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  14. CytochromeDrug metabolism and disposition: the biological fate of chemicals · 2021
    Article
  15. Article
  16. Steroidogenic cytochrome P450 17A1 structure and function.Molecular and cellular endocrinology · 2021
    Review
  17. Review
  18. Article
  19. Article
  20. Article
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 1 institution in 1 country.

Eric GonzalezFrom the Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
F Peter GuengerichFrom the Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146 f.guengerich@vanderbilt.edu.ORCID 0000-0002-7458-3048
Vanderbilt University · US

Funding

TRAINING PROGRAM IN ENVIRONMENTAL TOXICOLOGYT32ES007028 · NIEHS · VANDERBILT UNIVERSITY · PI F PETER Guengerich, Fiona Edith Harrison · 1985 to 2026
$15.7M
Vanderbilt/Meharry Initiative for Minority Student DvptR25GM062459 · NIGMS · VANDERBILT UNIVERSITY · PI VELEZ EDWARDS, DIGNA R · 2002 to 2020
$10.4M
Metabolism of Carcinogens and Drugs by Human P450sR01GM118122 · NIGMS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 2016 to 2023
$3.3M
Structure and Function of P450 Enzymes in Steroid Hormone BiosynthesisR01GM103937 · NIGMS · VANDERBILT UNIVERSITY · PI EGLI, MARTIN · 2013 to 2016
$1.6M
NIEHS NIH HHS T32 ES007028NIGMS NIH HHS R01 GM103937NIGMS NIH HHS R01 GM118122NIGMS NIH HHS R25 GM062459
6 · The paper itself

Abstract

Cytochrome P450 (P450, CYP) 17A1 plays a critical role in steroid metabolism, catalyzing both the 17α-hydroxylation of pregnenolone and progesterone and the subsequent 17α,20-lyase reactions to form dehydroepiandrosterone (DHEA) and androstenedione (Andro), respectively, critical for generating glucocorticoids and androgens. Human P450 17A1 reaction rates examined are enhanced by the accessory protein cytochrome

Indexed as

Models, Molecular17-alpha-HydroxypregnenoloneAndrostenedioneAnimalsBinding SitesBiocatalysisCytochrome P-450 Enzyme InhibitorsCytochromes b5DehydroepiandrosteroneHumansImidazolesKineticsLigandsNADPH-Ferrihemoprotein ReductaseNaphthalenesOxidation-Reduction17-alpha-HydroxypregnenoloneAndrostenedioneCYB5A protein, humanCYP17A1 protein, humanCytochrome P-450 Enzyme InhibitorsCytochromes b5DehydroepiandrosteroneImidazolesLigandsNADPH-Ferrihemoprotein ReductaseNaphthalenesorteronelPregnenoloneProgesteroneRecombinant ProteinsSteroid 17-alpha-Hydroxylasecytochrome P450enzyme kineticsoxidation-reduction (redox)pre-steady-state kineticssteady-state kineticssteroid metabolismsteroidogenesis

Identifiers

PMID28684414
PMCPMC5555180
OpenAlexW2725904614

What OpenQuestion holds

Textmetadata
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.