Evidence map›Paper›PMID 7964505›Full record

ArticleThe Journal of experimental medicine1994

156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox.

J H Leusen, B G Bolscher, P M Hilarius, R S Weening, W Kaulfersch, R A Seger, D Roos, A J Verhoeven

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of experimental medicine, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 107 citations in OpenAlex.

  1. Review
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  3. Structural basis for EROS binding to human phagocyte NADPH oxidase NOX2.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  18. Assembly of the phagocyte NADPH oxidase.Histochemistry and cell biology · 2004
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

J H LeusenCentral Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam.
B G Bolscher
P M Hilarius
R S Weening
W Kaulfersch
R A Seger
D Roos
A J Verhoeven
Dutch Blood Transfusion Society · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Src homology 3 (SH3) domains have been suggested to play an important role in the assembly of the superoxide-forming nicotinamide adenine dinucleotide phosphate (NADPH) oxidase upon activation of phagocytes, which involves the association of membrane-bound and cytosolic components. We studied the translocation of the cytosolic proteins to the plasma membrane in neutrophils of a patient with a point mutation in the gene encoding the light chain of cytochrome b558. This mutation leads to a substitution at residue 156 of a proline into a glutamine in a putative SH3 binding domain of p22-phox (Dinauer, M., E. A. Pierce, R. W. Erickson, T. Muhlebach, H. Messner, R. A. Seger, S. H. Orkin, and J. T. Curnutte. 1991. Proc. Natl. Acad. Sci. 88:11231). In PMA-stimulated neutrophils and in a cell-free translocation assay with neutrophil membranes and cytosol, association of the cytosolic proteins p47-phox and p67-phox with the membrane fraction of the patient's neutrophils was virtually absent. In contrast, when solubilized membranes of the patient's neutrophils were activated with phospholipids in the absence of cytosol (Koshkin, V., and E. Pick. 1993. FEBS [Fed. Eur. Biochem. Soc.] Lett. 327:57), the rate of NADPH-dependent oxygen uptake was observed at a rate similar to that of control membranes. We suggest that the binding of an SH3 domain of p47-phox to p22-phox, and thus activation of the oxidase, does not occur in the neutrophils of this patient, although under artificial conditions, electron flow from NADPH to oxygen in cytochrome b558 is possible.

Indexed as

GlutamineMembrane Transport ProteinsProlineBlotting, WesternCytochrome b GroupCytosolGranulomatous Disease, ChronicHumansMacromolecular SubstancesNADH, NADPH OxidoreductasesNADPH DehydrogenaseNADPH OxidasesNeutrophilsOxygen ConsumptionPhosphoproteinsPoint MutationCYBA protein, humancytochrome b558Cytochrome b GroupGlutamineMacromolecular SubstancesMembrane Transport ProteinsNADH, NADPH OxidoreductasesNADPH DehydrogenaseNADPH Oxidasesneutrophil cytosol factor 67Kneutrophil cytosolic factor 1PhosphoproteinsProline

Identifiers

PMID7964505
PMCPMC2191792
OpenAlexW2134557029

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.