Evidence map›Paper›PMID 19438290›Full record

ReviewAntioxidants & redox signaling2009

Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases.

Thomas L Leto, Stanislas Morand, Darrell Hurt, Takehiko Ueyama

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers.

0numbers the graph read from it
0cells of the map it votes in
161citing papers in PubMed
9.8field-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

161 citing papers in PubMed, 341 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Tetrahydrocurcumin Attenuates NaIOAntioxidants (Basel, Switzerland) · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Nox3 expression and function in retinal ganglion cells and Amacrine cells.Cellular and molecular life sciences : CMLS · 2025
    Article
  12. Review
  13. Review
  14. Redox Control in Platelet Activity and Therapy.Antioxidants (Basel, Switzerland) · 2025
    Review
  15. Review
  16. Mechanisms of host-bacterial interactions duringFrontiers in veterinary science · 2025
    Article
  17. Review
  18. Frontiers in cell and developmental biology · 2025
    Article
  19. Article
  20. Review

101 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

4 authors at 3 institutions in 2 countries.

Thomas L LetoLaboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA. tleto@nih.gov
Stanislas Morand
Darrell Hurt
Takehiko Ueyama
National Institute of Allergy and Infectious Diseases · USKobe University · JPNational Institutes of Health · US

Funding

NOX family NADPH oxidases: roles in innate immunity and inflammatory diseaseZIAAI000614 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI LETO, THOMAS · 2009 to 2024
$16.2M
Intramural NIH HHS ZIA AI000614
6 · The paper itself

Abstract

Nox family NADPH oxidases serve a variety of functions requiring reactive oxygen species (ROS) generation, including antimicrobial defense, biosynthetic processes, oxygen sensing, and redox-based cellular signaling. We explored targeting, assembly, and activation of several Nox family oxidases, since ROS production appears to be regulated both spatially and temporally. Nox1 and Nox3 are similar to the phagocytic (Nox2-based) oxidase, functioning as multicomponent superoxide-generating enzymes. Factors regulating their activities include cytosolic activator and organizer proteins and GTP-Rac. Their regulation varies, with the following rank order: Nox2 > Nox1 > Nox3. Determinants of subcellular targeting include: (a) formation of Nox-p22(phox) heterodimeric complexes allowing plasma membrane translocation, (b) phospholipids-binding specificities of PX domain-containing organizer proteins (p47(phox) or Nox organizer 1 (Noxo1 and p40(phox)), and (c) variably splicing of Noxo1 PX domains directing them to nuclear or plasma membranes. Dual oxidases (Duox1 and Duox2) are targeted by different mechanisms. Plasma membrane targeting results in H(2)O(2) release, not superoxide, to support extracellular peroxidases. Human Duox1 and Duox2 have no demonstrable peroxidase activity, despite their extensive homology with heme peroxidases. The dual oxidases were reconstituted by Duox activator 2 (Duoxa2) or two Duoxa1 variants, which dictate maturation, subcellular localization, and the type of ROS generated by forming stable complexes with Duox.

Indexed as

Amino Acid SequenceAnimalsCell LineEnzyme ActivationHumansIsoenzymesModels, MolecularMolecular Sequence DataNADPH OxidasesPhagocytosisProtein ConformationProtein Structure, TertiaryReactive Oxygen SpeciesSequence AlignmentSequence Homology, Amino AcidIsoenzymesNADPH OxidasesReactive Oxygen Species

Identifiers

PMID19438290
PMCPMC2782575
OpenAlexW2059240598

What OpenQuestion holds

Textmetadata
LicenceTDM
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.