Evidence map›Paper›PMID 20050630›Full record

ReviewBiochemistry2010

Signaling functions of reactive oxygen species.

Henry Jay Forman, Matilde Maiorino, Fulvio Ursini

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 342 papers.

0numbers the graph read from it
0cells of the map it votes in
342citing papers in PubMed
34.8field-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

342 citing papers in PubMed, 811 citations in OpenAlex.

  1. Trial
  2. PRX5 as a critical driver of colorectal cancer stemness and tumorigenicity.Redox report : communications in free radical research · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Protein oxidation in crowded environments.The Biochemical journal · 2026
    Review
  10. Curcumin in High Doses Reverses the UV-B-InducedPharmaceuticals (Basel, Switzerland) · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. BH4 Oxidation-Derived HJournal of neurochemistry · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Review

282 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 2 institutions in 2 countries.

Henry Jay FormanUniversity of California, 5200 North Lake Road, Merced, California 95344, USA. hjforman@gmail.com
Matilde Maiorino
Fulvio Ursini
University of Padua · ITUniversity of California, Merced · US

Funding

REGULATION OF GLUTATHIONE SYNTHESIS IN OXIDATIVE STRESSR01ES005511 · NIEHS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FORMAN, HENRY JAY · 1991 to 2010
$2.9M
Reactive oxygen species in alveolar macrophage signalingR01HL037556 · NHLBI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FORMAN, HENRY JAY · 1986 to 2004
$1.4M
Hydroxynonenal induces glutathione synthesis through JNKR56ES005511 · NIEHS · UNIVERSITY OF CALIFORNIA, MERCED · PI FORMAN, HENRY JAY · 2006 to 2006
$75k
NHLBI NIH HHS R01 HL037556NIEHS NIH HHS ES05511NIEHS NIH HHS R01 ES005511NIEHS NIH HHS R56 ES005511
6 · The paper itself

Abstract

We review signaling by reactive oxygen species, which is emerging as a major physiological process. However, among the reactive oxygen species, H(2)O(2) best fulfills the requirements of being a second messenger. Its enzymatic production and degradation, along with the requirements for the oxidation of thiols by H(2)O(2), provide the specificity for time and place that are required in signaling. Both thermodynamic and kinetic considerations suggest that among possible oxidation states of cysteine, formation of sulfenic acid derivatives or disulfides can be relevant as thiol redox switches in signaling. In this work, the general constraints that are required for protein thiol oxidation by H(2)O(2) to be fast enough to be relevant for signaling are discussed in light of the mechanism of oxidation of the catalytic cysteine or selenocysteine in thiol peroxidases. While the nonenzymatic reaction between thiol and H(2)O(2) is, in most cases, too slow to be relevant in signaling, the enzymatic catalysis of thiol oxidation by these peroxidases provides a potential mechanism for redox signaling.

Indexed as

AnimalsCysteineHumansHydrogen PeroxidePeroxiredoxinsReactive Oxygen SpeciesSecond Messenger SystemsSignal TransductionCysteinecysteine sulfinic acidHydrogen PeroxidePeroxiredoxinsReactive Oxygen Species

Identifiers

PMID20050630
PMCPMC4226395
OpenAlexW2101444644

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.