Evidence map›Paper›PMID 20361926›Full record

ReviewArchives of biochemistry and biophysics2010

NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1), a multifunctional antioxidant enzyme and exceptionally versatile cytoprotector.

Albena T Dinkova-Kostova, Paul Talalay

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 332 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
332citing papers in PubMed, 1 pooled it
15.7field-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

332 citing papers in PubMed, 1 synthesis or guideline pooled it, 707 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Cell type diversification and phenotype convergence underlying white fin-ornamentation of cyprinid fishes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. A Potent Quinone Reductase Encoded byMolecules (Basel, Switzerland) · 2026
    Article
  15. Review
  16. Article
  17. An Antioxidant Cocktail ofAntioxidants (Basel, Switzerland) · 2026
    Article
  18. Article
  19. PeerJ · 2026
    Article
  20. Article

272 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

2 authors at 2 institutions in 2 countries.

Albena T Dinkova-KostovaBiomedical Research Institute, University of Dundee, Dundee, Scotland, UK.
Paul Talalay
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

Translational Research Central ServicesP30CA006973 · NCI · JOHNS HOPKINS UNIVERSITY · PI Rosalie Wollett · 1985 to 2026
$208.6M
Isolation &Evaluation of Anticarcinogenic GlucosinolateR01CA093780 · NCI · JOHNS HOPKINS UNIVERSITY · PI TALALAY, PAUL · 2002 to 2011
$2.9M
Cancer Research UK C20953/A10270Medical Research CouncilNCI NIH HHS CA06973NCI NIH HHS CA93780NCI NIH HHS P30 CA006973NCI NIH HHS R01 CA093780
6 · The paper itself

Abstract

NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1) is a widely-distributed FAD-dependent flavoprotein that promotes obligatory 2-electron reductions of quinones, quinoneimines, nitroaromatics, and azo dyes, at rates that are comparable with NADH or NADPH. These reductions depress quinone levels and thereby minimize opportunities for generation of reactive oxygen intermediates by redox cycling, and for depletion of intracellular thiol pools. NQO1 is a highly-inducible enzyme that is regulated by the Keap1/Nrf2/ARE pathway. Evidence for the importance of the antioxidant functions of NQO1 in combating oxidative stress is provided by demonstrations that induction of NQO1 levels or their depletion (knockout, or knockdown) are associated with decreased and increased susceptibilities to oxidative stress, respectively. Furthermore, benzene genotoxicity is markedly enhanced when NQO1 activity is compromised. Not surprisingly, human polymorphisms that suppress NQO1 activities are associated with increased predisposition to disease. Recent studies have uncovered protective roles for NQO1 that apparently are unrelated to its enzymatic activities. NQO1 binds to and thereby stabilizes the important tumor suppressor p53 against proteasomal degradation. Indeed, NQO1 appears to regulate the degradative fate of other proteins. These findings suggest that NQO1 may exercise a selective "gatekeeping" role in regulating the proteasomal degradation of specific proteins, thereby broadening the cytoprotective role of NQO1 far beyond its highly effective antioxidant functions.

Indexed as

AnimalsAntioxidantsEstrogensGene Knockdown TechniquesGene Knockout TechniquesHumansIntracellular Signaling Peptides and ProteinsKelch-Like ECH-Associated Protein 1Models, BiologicalNAD(P)H Dehydrogenase (Quinone)Oxidative StressPolymorphism, GeneticProteasome Endopeptidase ComplexProtein BindingProtein StabilityQuinonesAntioxidantsEstrogensIntracellular Signaling Peptides and ProteinsKEAP1 protein, humanKelch-Like ECH-Associated Protein 1NAD(P)H Dehydrogenase (Quinone)NQO1 protein, humanProteasome Endopeptidase ComplexQuinonesTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID20361926
PMCPMC2930038
OpenAlexW2022582116

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.