Evidence map›Paper›PMID 7657821›Full record

ArticleThe Journal of clinical investigation1995

The phosphorylation targets of p47phox, a subunit of the respiratory burst oxidase. Functions of the individual target serines as evaluated by site-directed mutagenesis.

L R Faust, J el Benna, B M Babior, S J Chanock

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of clinical investigation, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
8.6field-weighted citation impact, top 1% 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

47 citing papers in PubMed, 181 citations in OpenAlex.

  1. Review
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  8. Review
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  11. The oxidative burst reaction in mammalian cells depends on gravity.Cell communication and signaling : CCS · 2013
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. NADPH oxidases in heart failure: poachers or gamekeepers?Antioxidants & redox signaling · 2013
    Review
  17. Article
  18. Review
  19. Cell signaling through protein kinase C oxidation and activation.International journal of molecular sciences · 2012
    Review
  20. Article
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

4 authors at 2 institutions in 1 country.

L R FaustScripps Research Institute, La Jolla, California 92037, USA.
J el Benna
B M Babior
S J Chanock
National Institutes of Health · USScripps Research Institute · US

Funding

VPA 985 IN LIVER CIRRHOSIS &ASCITESM01RR000833 · NCRR · SCRIPPS RESEARCH INSTITUTE · PI BABIOR, BERNARD M · 1985 to 2004
$14.0M
THE FUNCTION OF NORMAL AND MALIGNANT PHAGOCYTESR01AI024227 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI CATZ, SERGIO DANIEL · 1985 to 2007
$4.0M
OXIDASE-RELATED 48K PHOSPHOPROTEIN OF HUMAN NEUTROPHILSR01AI028479 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI DEUEL, THOMAS F · 1989 to 2004
$2.0M
FUNCTION OF NORMAL AND MALIGNANT PHAGOCYTESR37AI024227 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI BABIOR, BERNARD M · 1988 to 1997
–
NCRR NIH HHS RR-00833NIAID NIH HHS AI-24227NIAID NIH HHS AI-28479
6 · The paper itself

Abstract

The respiratory burst oxidase of phagocytes and B lymphocytes catalyzes the reduction of oxygen to O2- at the expense of NADPH. Dormant in resting cells, the oxidase is activated by exposing the cells to appropriate stimuli. During activation, p47phox, a cytosolic oxidase subunit, becomes extensively phosphorylated on a number of serines located between S303 and S379. To determine whether this phosphorylation is necessary for oxidase activation, we examined phorbol-elicited oxidase activity in EBV-transformed B lymphoblasts deficient in p47phox after transfection with plasmids expressing various S-->A mutants of p47phox. The mutant containing S-->A mutations involving all serines between S303 and S379 [S(303-379)A] was not phosphorylated, did not translocate to plasma membrane during activation and was almost devoid of function. As to individual serines, S379 was of special interest because (a) p47 phox S379 was phosphorylated in phorbol-activated lymphoblasts expressing wild-type p47phox, and (b) p47phox S379A failed to translocate to the membrane, and was as functionless as p47phox S(303-379)A; other single S-->A mutations had little effect on oxidase activity. These findings suggest that the phosphorylation of S379 may be important for oxidase activation in whole cells.

Indexed as

NADPH OxidasesSerineAmino Acid SequenceBase SequenceB-LymphocytesCell MembraneCytosolEnzyme ActivationHumansKineticsMolecular Sequence DataMutagenesis, Site-DirectedNADH, NADPH OxidoreductasesNADPH DehydrogenaseOligonucleotides, AntisensePhagocytesNADH, NADPH OxidoreductasesNADPH DehydrogenaseNADPH Oxidasesneutrophil cytosolic factor 1Oligonucleotides, AntisensePhosphoproteinsRecombinant ProteinsSerinesuperoxide-forming enzyme

Identifiers

PMID7657821
PMCPMC185774
OpenAlexW2034453407

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.