Evidence map›Paper›PMID 20592030›Full record

ArticleThe Journal of biological chemistry2010

p47phox molecular activation for assembly of the neutrophil NADPH oxidase complex.

Julien Marcoux, Petr Man, Isabelle Petit-Haertlein, Corinne Vivès, Eric Forest, Franck Fieschi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 43 citations in OpenAlex.

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  10. Suppressed ubiquitination of Nrf2 by p47Free radical biology & medicine · 2017
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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

6 authors at 3 institutions in 2 countries.

Julien MarcouxLaboratoire des Protéines Membranaires, Institut de Biologie Structurale (IBS), 41 rue Jules Horowitz, Grenoble, F-38027, France.
Petr Man
Isabelle Petit-Haertlein
Corinne Vivès
Eric Forest
Franck Fieschi
Institut de Biologie Structurale · FRCentre National de la Recherche Scientifique · FRUniversité Grenoble Alpes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The p47(phox) cytosolic factor from neutrophilic NADPH oxidase has always been resistant to crystallogenesis trials due to its modular organization leading to relative flexibility. Hydrogen/deuterium exchange coupled to mass spectrometry was used to obtain structural information on the conformational mechanism that underlies p47(phox) activation. We confirmed a relative opening of the protein with exposure of the SH3 Src loops that are known to bind p22(phox) upon activation. A new surface was shown to be unmasked after activation, representing a potential autoinhibitory surface that may block the interaction of the PX domain with the membrane in the resting state. Within this surface, we identified 2 residues involved in the interaction with the PX domain. The double mutant R162A/D166A showed a higher affinity for specific phospholipids but none for the C-terminal part of p22(phox), reflecting an intermediate conformation between the autoinhibited and activated forms.

Indexed as

Amino Acid SubstitutionAnimalsEnzyme ActivationHumansMutation, MissenseNADPH OxidasesNeutrophilsProtein Structure, Secondarysrc Homology DomainsCYBA protein, humanNADPH Oxidasesneutrophil cytosolic factor 1

Identifiers

PMID20592030
PMCPMC2937925
OpenAlexW2068639567

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.