Evidence map›Paper›PMID 10393079›Full record

ArticleThe Biochemical journal1999

The mechanism of activation of NADPH oxidase in the cell-free system: the activation process is primarily catalytic and not through the formation of a stoichiometric complex.

A R Cross, R W Erickson, J T Curnutte

Abstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Assembly of the phagocyte NADPH oxidase.Histochemistry and cell biology · 2004
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. 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

3 authors.

A R CrossDepartment of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. scross@scripps.edu
R W Erickson
J T Curnutte

Funding

REGULATION OF SUPEROXIDE PRODUCTION BY HUMAN NEUTROPHILSR01AI024838 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI FRIEDMAN, JEFFREY S · 1986 to 2007
$3.1M
NIAID NIH HHS AI24838
6 · The paper itself

Abstract

It is commonly assumed that activation of the superoxide-generating NADPH oxidase requires the formation of a stable complex between flavocytochrome b-245 (the gp91phox/p22phox heterodimer) and the cytosolic cofactors p47phox, p67phox and Rac2. This association is thought to convert flavocytochrome b-245, which contains the NADPH-binding site, flavin and haem centres, from an inactive into an active state. Here we provide evidence that, in the cell-free system, this activation process does not necessarily require the formation of a stable stoichiometric complex between the phox proteins. To explain this data we propose the hypothesis that p67phox (and possibly Rac2), are capable of activating flavocytochrome b-245 in a catalytic fashion, where a single molecule of p67phox (or Rac2) is capable of activating multiple flavocytochrome b-245 molecules.

Indexed as

AnimalsBinding SitesCell-Free SystemEnzyme ActivationHumansNADPNADPH OxidasesNeutrophilsPhosphoproteinsProtein BindingNADPNADPH Oxidasesneutrophil cytosol factor 67KPhosphoproteins

Identifiers

PMID10393079
PMCPMC1220353

What OpenQuestion holds

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Registered trials

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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.