Evidence map›Paper›PMID 35287432›Full record

ArticleBiochemistry2022

Importance of Asparagine 202 in Manipulating Active Site Structure and Substrate Preference for Human CYP17A1.

Yilin Liu, Ilia Denisov, Michael Gregory, Stephen G Sligar, James R Kincaid

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Fully automated virtual screening pipeline of FDA-approved drugs using Caver Web.Computational and structural biotechnology journal · 2022
    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

5 authors at 2 institutions in 1 country.

Yilin LiuDepartment of Chemistry, Marquette University, Milwaukee, Wisconsin 53233, United States.
Ilia DenisovDepartments of Chemistry and Biochemistry, University of Illinois, Urbana, Illinois 61801, United States.
Michael GregoryDepartments of Chemistry and Biochemistry, University of Illinois, Urbana, Illinois 61801, United States.
Stephen G SligarDepartments of Chemistry and Biochemistry, University of Illinois, Urbana, Illinois 61801, United States.
James R KincaidDepartment of Chemistry, Marquette University, Milwaukee, Wisconsin 53233, United States.ORCID 0000-0001-6050-1438
University of Illinois Urbana-Champaign · USMarquette University · US

Funding

Nanoscale Approaches to Understanding Membrane Protein FunctionR35GM118145 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI STEPHEN G. SLIGAR · 2016 to 2026
$7.5M
Mechanisms and control of multifunctional cytochromes P450R01GM125303 · NIGMS · MARQUETTE UNIVERSITY · PI KINCAID, JAMES ROBERT · 2017 to 2020
$1.0M
Human Steroid Metabolism by Cytochrome P450R01GM110428 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SLIGAR, STEPHEN G. · 2015 to 2016
$805k
NIGMS NIH HHS R01 GM110428NIGMS NIH HHS R01 GM125303NIGMS NIH HHS R35 GM118145
6 · The paper itself

Abstract

The multifunctional cytochrome P450 17A1 (CYP17A1) plays a crucial role in human steroid hormone synthesis (UniProtKB─P05093). It first carries out standard monooxygenase chemistry, converting pregnenolone (PREG) and progesterone (PROG) into 17OH-PREG and 17OH-PROG, utilizing a "Compound I" to initiate hydrogen abstraction and radical recombination in the classic "oxygen rebound" mechanism. Additionally, these hydroxylated products also serve as substrates in a second oxidative cycle which cleaves the 17-20 carbon-carbon bond to form dehydroepiandrosterone and androstenedione, which are key precursors in the generation of powerful androgens and estrogens. Interestingly, in humans, with 17OH-PREG, this so-called lyase reaction is more efficient than with 17OH-PROG, based on

Indexed as

AsparagineSteroid 17-alpha-HydroxylaseAndrostenedioneCatalytic DomainHumansPregnenoloneProgesteroneAndrostenedioneAsparagineCYP17A1 protein, humanPregnenoloneProgesteroneSteroid 17-alpha-Hydroxylase

Identifiers

PMID35287432
PMCPMC9972851
OpenAlexW4221023270

What OpenQuestion holds

Textmetadata
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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.