Evidence map›Paper›PMID 32933097›Full record

ArticleInternational journal of molecular sciences2020

Interaction Modes of Microsomal Cytochrome P450s with Its Reductase and the Role of Substrate Binding.

Francisco Esteves, Philippe Urban, José Rueff, Gilles Truan, Michel Kranendonk

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-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

12 citing papers in PubMed, 13 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

5 authors at 2 institutions in 2 countries.

Francisco EstevesCenter for Toxicogenomics and Human Health (ToxOmics), Genetics, Oncology and Human Toxicology, NOVA Medical School/Faculty of Medical Sciences, Universidade NOVA de Lisboa, 1169-056 Lisbon, Portugal.ORCID 0000-0002-3046-1313
Philippe UrbanTBI, Université de Toulouse, CNRS, INRAE, INSA, CEDEX 04, 31077 Toulouse, France.ORCID 0000-0003-0557-839X
José RueffCenter for Toxicogenomics and Human Health (ToxOmics), Genetics, Oncology and Human Toxicology, NOVA Medical School/Faculty of Medical Sciences, Universidade NOVA de Lisboa, 1169-056 Lisbon, Portugal.
Gilles TruanTBI, Université de Toulouse, CNRS, INRAE, INSA, CEDEX 04, 31077 Toulouse, France.ORCID 0000-0002-3560-8302
Michel KranendonkCenter for Toxicogenomics and Human Health (ToxOmics), Genetics, Oncology and Human Toxicology, NOVA Medical School/Faculty of Medical Sciences, Universidade NOVA de Lisboa, 1169-056 Lisbon, Portugal.ORCID 0000-0003-1362-0076
Universidade Nova de Lisboa · PTCentre National de la Recherche Scientifique · FR

Funding

Fundação para a Ciência e a Tecnologia FCTANR/BEXBCM/0002/2013L'Agence Nationale de la Recherche ANR-13-ISV5-0001
6 · The paper itself

Abstract

The activity of microsomal cytochromes P450 (CYP) is strictly dependent on the supply of electrons provided by NADPH cytochrome P450 oxidoreductase (CPR). The variant nature of the isoform-specific proximal interface of microsomal CYPs implies that the interacting interface between the two proteins is degenerated. Recently, we demonstrated that specific CPR mutations in the FMN-domain (FD) may induce a gain in activity for a specific CYP isoform. In the current report, we confirm the CYP isoform dependence of CPR's degenerated binding by demonstrating that the effect of four of the formerly studied FD mutants are indeed exclusive of a specific CYP isoform, as verified by cytochrome

Indexed as

Cytochrome P-450 Enzyme SystemCytochromes cEscherichia coliHumansMutationNADPH-Ferrihemoprotein ReductaseProtein BindingProtein IsoformsCytochrome P-450 Enzyme SystemCytochromes cNADPH-Ferrihemoprotein ReductaseProtein IsoformsCPR-FMN-domainCYP-substrateelectron transfermicrosomal cytochrome P450NADPH-cytochrome P450 reductaseprotein–protein interaction

Identifiers

PMID32933097
PMCPMC7555755
OpenAlexW3086561251

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.