Evidence map›Paper›PMID 15293055›Full record

ReviewHistochemistry and cell biology2004

Assembly of the phagocyte NADPH oxidase.

William M Nauseef

Abstract readReview
PubMed Publisher
In one paragraph

Review in Histochemistry and cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 192 papers.

0numbers the graph read from it
0cells of the map it votes in
192citing papers in PubMed
10.8field-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

192 citing papers in PubMed, 419 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. 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
    Article
  10. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  11. Implications for neutrophils in cardiac arrhythmias.American journal of physiology. Heart and circulatory physiology · 2024
    Review
  12. Article
  13. NADPH Oxidase 3: Beyond the Inner Ear.Antioxidants (Basel, Switzerland) · 2024
    Review
  14. Perivascular Adipose Tissue Oxidative Stress in Obesity.Antioxidants (Basel, Switzerland) · 2023
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

132 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

1 author at 1 institution in 1 country.

William M NauseefInflammation Program and Department of Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, D160 MTF, 2501 Crosspark Road, Coralville, IA 52241, USA. william-nauseef@uiowa.edu
Iowa City VA Medical Center · US

Funding

Studies of the capsular-like antigen of F. tularensisP01AI044642 · NIAID · UNIVERSITY OF IOWA · PI ALLEN, LEE-ANN H · 1999 to 2014
$18.2M
The Submembranous Cytoskeleton in Neutrophil ActivationR01AI034879 · NIAID · UNIVERSITY OF IOWA · PI NAUSEEF, WILLIAM MICHAEL · 1996 to 2005
$1.3M
CHAPERONES AND PROTEIN BIOSYNTHESIS IN MYELOID CELLSR01HL053592 · NHLBI · UNIVERSITY OF IOWA · PI NAUSEEF, WILLIAM MICHAEL · 1997 to 2005
$1.2M
Biosynthesis, structural organization, and function of NOX proteinsR56AI034879 · NIAID · UNIVERSITY OF IOWA · PI NAUSEEF, WILLIAM M. · 2007 to 2007
$337k
Human neutrophils, phospholipase A2 and S.aureus: microbial targets and responsesI01BX000513 · VA · IOWA CITY VA MEDICAL CENTER · PI NAUSEEF, WILLIAM M. · 2009 to 2017
–
BLRD VA I01 BX000513NHLBI NIH HHS HL53592NIAID NIH HHS AI34879NIAID NIH HHS AI44642
6 · The paper itself

Abstract

Stimulated phagocytes undergo a burst in respiration whereby molecular oxygen is converted to superoxide anion through the action of an NADPH-dependent oxidase. The multicomponent phagocyte oxidase is unassembled and inactive in resting cells but assembles at the plasma or phagosomal membrane upon phagocyte activation. Oxidase components include flavocytochrome b558, an integral membrane heterodimer comprised of gp91phox and p22phox, and three cytosolic proteins, p47phox, p67phox, and Rac1 or Rac2, depending on the species and phagocytic cell. In a sense, the phagocyte oxidase is spatially regulated, with critical elements segregated in the membrane and cytosol but ready to undergo nearly immediate assembly and activation in response to stimulation. To achieve such spatial regulation, the individual components in the resting phagocyte adopt conformations that mask potentially interactive structural domains that might mediate productive intermolecular associations and oxidase assembly. In response to stimulation, post-translational modifications of the oxidase components release these constraints and thereby render potential interfaces accessible and interactive, resulting in translocation of the cytosolic elements to the membrane where the functional oxidase is assembled and active. This review summarizes data on the structural features of the phagocyte oxidase components and on the agonist-dependent conformational rearrangements that contribute to oxidase assembly and activation.

Indexed as

AnimalsCytochrome b GroupHumansNADPH OxidasesOxygenPhagocytesPhosphoproteinsProtein BindingProtein Conformationrac1 GTP-Binding ProteinRAC2 GTP-Binding Proteinrac GTP-Binding ProteinsSuperoxidescytochrome b558Cytochrome b GroupNADPH OxidasesOxygenPhosphoproteinsrac1 GTP-Binding ProteinRAC2 GTP-Binding Proteinrac GTP-Binding ProteinsSuperoxides

Identifiers

PMID15293055
OpenAlexW2048486951

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.