Evidence map›Paper›PMID 29371396›Full record

ArticleThe Journal of biological chemistry2018

The cytochrome P450 24A1 interaction with adrenodoxin relies on multiple recognition sites that vary among species.

D Fernando Estrada

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

D Fernando EstradaFrom the Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York 14214 dfestrad@buffalo.edu.
University at Buffalo, State University of New York · US

Funding

Crystallographic and NMR studies of the Human Cytochrome P450 enzyme responsible for inactivating vitamin DR00GM112862 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI ESTRADA, DAVID FERNANDO · 2016 to 2018
$747k
NIGMS NIH HHS R00 GM112862
6 · The paper itself

Abstract

Mitochondrial cytochromes P450 (P450s) are responsible for important metabolic reactions, including steps involved in steroid and vitamin D metabolism. The mitochondrial P450 24A1 (CYP24A1) is responsible for deactivation of the bioactive form of vitamin D, 1,25(OH)

Indexed as

AdrenodoxinAnimalsBinding SitesCattleCytochrome P450 Family 24HumansModels, MolecularMutagenesis, Site-DirectedMutationNuclear Magnetic Resonance, BiomolecularOpossumsOxidation-ReductionProtein ConformationRatsSpecies SpecificityAdrenodoxinCytochrome P450 Family 24adrenodoxinCYP24A1cytochrome P450ferredoxinmembrane proteinmitochondrianuclear magnetic resonance (NMR)P450-ferredoxin complexvitamin D

Identifiers

PMID29371396
PMCPMC5857985
OpenAlexW2784937745

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.