Evidence map›Paper›PMID 7938008›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets.

T L Leto, A G Adams, I de Mendez

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

74 citing papers in PubMed, 287 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. NADPH Oxidase 3: Beyond the Inner Ear.Antioxidants (Basel, Switzerland) · 2024
    Review
  6. ROCK2 interacts with p22phox to phosphorylate p47phox and to control NADPH oxidase activation in human monocytes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. NADPH Oxidases in Aortic Aneurysms.Antioxidants (Basel, Switzerland) · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. The role of NADPH oxidase in a mouse model of fetal alcohol syndrome.American journal of obstetrics and gynecology · 2014
    Article
  18. Redox signaling in cardiovascular health and disease.Free radical biology & medicine · 2013
    Review
  19. Article
  20. Review

14 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

T L LetoLaboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.
A G Adams
I de Mendez
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The NADPH oxidase responsible for generation of superoxide anion and related microbicidal oxidants by phagocytes is assembled from at least five distinct proteins. Two are cytosolic components (p47-phox and p67-phox) that contain Src homology 3 (SH3) domains and associate with a transmembrane cytochrome b558 upon activation. We show here that the SH3 domains of p47-phox bind to proline-rich sequences in p47-phox itself and the p22-phox subunit of cytochrome b558. Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox. Expression of mutated p22-phox did not restore oxidase activity to p22-phox-deficient B cells and did not enable p22-phox-dependent translocation of p47-phox to membranes in phorbol ester-stimulated cells. We also show that the cytosolic oxidase components associate with one another through the C-terminal SH3 domain of p67-phox and a proline-rich C-terminal sequence in p47-phox. These SH3 target sites conform to consensus features deduced from SH3 binding sites in other systems. We propose a model in which the oxidase complex assembles through a mechanism involving SH3 domains of both cytosolic proteins and cognate proline-rich targets in other oxidase components.

Indexed as

Amino Acid SequenceAnimalsBinding SitesB-LymphocytesCell LineConsensus SequenceCytochrome b GroupDNA PrimersEnzyme ActivationGenes, srcGranulomatous Disease, ChronicHumansMolecular Sequence DataMutagenesis, Site-DirectedNADH, NADPH OxidoreductasesNADPH Dehydrogenasecytochrome b558Cytochrome b GroupDNA PrimersNADH, NADPH OxidoreductasesNADPH DehydrogenaseNADPH Oxidasesneutrophil cytosol factor 67Kneutrophil cytosolic factor 1PhosphoproteinsProlineRecombinant Proteins

Identifiers

PMID7938008
PMCPMC45079
OpenAlexW2084643121

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.