Evidence map›Paper›PMID 27566228›Full record

ReviewMolecular and cellular endocrinology2017

Structural insights into the function of steroidogenic cytochrome P450 17A1.

Rahul Yadav, Elyse M Petrunak, D Fernando Estrada, Emily E Scott

Abstract readReview
In one paragraph

Review in Molecular and cellular endocrinology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.3field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
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  12. Article
  13. Associations BetweenFrontiers in genetics · 2021
    Article
  14. Article
  15. Alternative modes of OJournal of inorganic biochemistry · 2020
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Spectroscopic studies of the cytochrome P450 reaction mechanisms.Biochimica et biophysica acta. Proteins and proteomics · 2018
    Review
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

4 authors at 1 institution in 1 country.

Rahul YadavDepartment of Medicinal Chemistry, 1251 Wescoe Hall Dr., The University of Kansas, Lawrence, KS 66045, USA.
Elyse M PetrunakDepartment of Medicinal Chemistry, 1251 Wescoe Hall Dr., The University of Kansas, Lawrence, KS 66045, USA.
D Fernando EstradaDepartment of Medicinal Chemistry, 1251 Wescoe Hall Dr., The University of Kansas, Lawrence, KS 66045, USA.
Emily E ScottDepartment of Medicinal Chemistry, 1251 Wescoe Hall Dr., The University of Kansas, Lawrence, KS 66045, USA. Electronic address: eescott@ku.edu.
University of Kansas · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI LOVELL, SCOTT W. · 2014 to 2018
$5.6M
Structural Basis of Cytochrome P450 Activity-Equipment SupplementR37GM076343 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCOTT, EMILY E · 2015 to 2024
$3.7M
Structural Basis of Cytochrome P450 ActivityR01GM076343 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI SCOTT, EMILY E · 2006 to 2014
$2.9M
Protein Structure and FunctionP20GM103420 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2012 to 2012
$2.0M
Structure and Function of Cytochrome P450 17A1R01GM102505 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI AUBE, JEFFREY, SCOTT, EMILY E · 2012 to 2015
$1.2M
Application of solution NMR to (human) membrane cytochrome P450 17A1F32GM103069 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI ESTRADA, DAVID FERNANDO · 2012 to 2014
$102k
NIGMS NIH HHS F32 GM103069NIGMS NIH HHS P20 GM103420NIGMS NIH HHS P30 GM110761NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R01 GM076343NIGMS NIH HHS R01 GM102505NIGMS NIH HHS R37 GM076343
6 · The paper itself

Abstract

Cytochrome P450 17A1 (CYP17A1) operates at the core of human steroidogenesis, directing precursors into mineralocorticoids, glucocorticoids, or sex steroids. Although the 17α-hydroxylase and 17,20-lyase activities of this dual function enzyme have been investigated extensively, until recently no CYP17A1 structures were available to inform our understanding. Structures of CYP17A1 with a range of steroidal inhibitors and substrates are now available. This review relates functional knowledge of this enzyme to structural features defining the selective differentiation between its various substrates. While both hydroxylase and lyase substrates have similar orientations with respect to the heme, subtle differences in hydrogen bonding between CYP17A1 and the C3 substituent at the opposite end of ligands appear to correlate with differential substrate utilization and product formation. Complementary structural information from solution NMR supports cytochrome b

Indexed as

AnimalsHumansHydroxylationPregnenoloneProgesteroneStereoisomerismSteroid 17-alpha-HydroxylaseSubstrate SpecificityPregnenoloneProgesteroneSteroid 17-alpha-Hydroxylase17,20-Lyase17α−hydroxylaseCytochrome P450 17A1SteroidogenesisX-ray crystallography

Identifiers

PMID27566228
PMCPMC5235955
OpenAlexW2518031329

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.