Evidence map›Paper›PMID 17602947›Full record

ReviewFree radical biology & medicine2007

Regulation of Nox and Duox enzymatic activity and expression.

J David Lambeth, Tsukasa Kawahara, Becky Diebold

Open access · greenAbstract readReview
In one paragraph

Review in Free radical biology & medicine, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 246 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
246citing papers in PubMed, 1 pooled it
17.2field-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

246 citing papers in PubMed, 1 synthesis or guideline pooled it, 491 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Role of reactive oxygen species in myelodysplastic syndromes.Cellular & molecular biology letters · 2024
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. A Role for Second Messengers in Axodendritic Neuronal Polarity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Review
  19. Article
  20. Article

186 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

3 authors at 1 institution in 1 country.

J David LambethDepartment of Pathology and Laboratory Medicine, 148 Whitehead Biomedical Research Building, Emory University, 615 Michael Street, Atlanta, GA 30322, USA. noxdoc@mac.com
Tsukasa Kawahara
Becky Diebold
Emory University · US

Funding

Moxl as a Molecular Target for Cancer Drug DiscoveryR01CA084138 · NCI · EMORY UNIVERSITY · PI LAMBETH, JOHN DAVID · 2000 to 2011
$4.4M
Regulation of Nox Enzymes by Calcium and Novel SubunitsR01CA105116 · NCI · EMORY UNIVERSITY · PI LAMBETH, JOHN DAVID · 2004 to 2014
$2.4M
Dual Oxidases (Duox): Enzymology &Biological FunctionR01GM067717 · NIGMS · EMORY UNIVERSITY · PI LAMBETH, JOHN DAVID · 2003 to 2006
$1.1M
Regulation of Nox Enzymes by Calcium and Novel SubunitsR56CA105116 · NCI · EMORY UNIVERSITY · PI LAMBETH, JOHN DAVID · 2009 to 2009
$248k
NCI NIH HHS CA084138NCI NIH HHS CA105116NCI NIH HHS R01 CA084138NCI NIH HHS R01 CA105116NCI NIH HHS R56 CA105116NIGMS NIH HHS R01 GM067717
6 · The paper itself

Abstract

In recent years, it has become clear that reactive oxygen species (ROS, which include superoxide, hydrogen peroxide, and other metabolites) are produced in biological systems. Rather than being simply a by-product of aerobic metabolism, it is now recognized that specific enzymes--the Nox (NADPH oxidase) and Duox (Dual oxidase) enzymes--seem to have the sole function of generating ROS in a carefully regulated manner, and key roles in signal transduction, immune function, hormone biosynthesis, and other normal biological functions are being uncovered. The prototypical Nox is the respiratory burst oxidase or phagocyte oxidase, which generates large amounts of superoxide and other reactive species in the phagosomes of neutrophils and macrophages, playing a central role in innate immunity by killing microbes. This enzyme system has been extensively studied over the past two decades, and provides a basis for comparison with the more recently described Nox and Duox enzymes, which generate ROS in a variety of cells and tissues. This review first considers the structure and regulation of the respiratory burst oxidase, and then reviews recent studies relating to the regulation of the activity of the novel Nox/Duox enzymes. The regulation of Nox and Duox expression in tissues and by specific stimuli is also considered here. An accompanying review considers biological and pathological roles of the Nox family of enzymes.

Indexed as

AnimalsDual OxidasesFlavoproteinsGene Expression Regulation, EnzymologicHumansMembrane GlycoproteinsMembrane ProteinsNADPH Oxidase 1NADPH Oxidase 2NADPH Oxidase 4NADPH Oxidase 5NADPH OxidasesPhagocytesPhosphoproteinsPromoter Regions, GeneticProtein Structure, TertiaryCYBB protein, humanDual OxidasesDUOX1 protein, humanFlavoproteinsMembrane GlycoproteinsMembrane ProteinsNADPH Oxidase 1NADPH Oxidase 2NADPH Oxidase 4NADPH Oxidase 5NADPH Oxidasesneutrophil cytosol factor 67Kneutrophil cytosolic factor 1NOX1 protein, humanNox4 protein, mouseNOX5 protein, humanPhosphoproteinsProtein Subunitssuperoxide-forming enzyme

Identifiers

PMID17602947
PMCPMC1989153
OpenAlexW2032028059

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.