Evidence map›Paper›PMID 23639002›Full record

ReviewCritical reviews in biochemistry and molecular biology

Redox regulation of protein kinases.

Thu H Truong, Kate S Carroll

Abstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

95 citing papers in PubMed, 164 citations in OpenAlex.

  1. Article
  2. Nitration in cancer signaling.Redox biology · 2026
    Review
  3. Article
  4. Article
  5. A druggable redox switch on SHP1 controls macrophage inflammation.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Therapeutic advances of targeting receptor tyrosine kinases in cancer.Signal transduction and targeted therapy · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Alexander disease: the road ahead.Neural regeneration research · 2023
    Review

35 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 1 country.

Thu H TruongDepartment of Chemistry, University of Michigan, Ann Arbor, MI, USA.
Kate S Carroll
Scripps Research Institute · USUniversity of Michigan · US

Funding

Probing the role of cysteine sulfenylation in cell signalingR01GM102187 · NIGMS · UNIVERSITY OF FLORIDA · PI Kate Suzanne Carroll · 2012 to 2026
$4.6M
Nucleophilic Inhibitors for Targeting Redox-Sensitive KinasesR01CA174864 · NCI · SCRIPPS FLORIDA · PI CARROLL, KATE SUZANNE · 2014 to 2017
$1.6M
NCI NIH HHS R01 CA174864NIGMS NIH HHS GM102187NIGMS NIH HHS R01 GM102187
6 · The paper itself

Abstract

Protein kinases represent one of the largest families of genes found in eukaryotes. Kinases mediate distinct cellular processes ranging from proliferation, differentiation, survival, and apoptosis. Ligand-mediated activation of receptor kinases can lead to the production of endogenous hydrogen peroxide (H₂O₂) by membrane-bound NADPH oxidases. In turn, H₂O₂ can be utilized as a secondary messenger in signal transduction pathways. This review presents an overview of the molecular mechanisms involved in redox regulation of protein kinases and its effects on signaling cascades. In the first half, we will focus primarily on receptor tyrosine kinases (RTKs), whereas the latter will concentrate on downstream non-receptor kinases involved in relaying stimulant response. Select examples from the literature are used to highlight the functional role of H₂O₂ regarding kinase activity, as well as the components involved in H₂O₂ production and regulation during cellular signaling. In addition, studies demonstrating direct modulation of protein kinases by H₂O₂ through cysteine oxidation will be emphasized. Identification of these redox-sensitive residues may help uncover signaling mechanisms conserved within kinase subfamilies. In some cases, these residues can even be exploited as targets for the development of new therapeutics. Continued efforts in this field will further basic understanding of kinase redox regulation, and delineate the mechanisms involved in physiological and pathological H₂O₂ responses.

Indexed as

AnimalsHumansHydrogen PeroxideOxidation-ReductionProtein KinasesSignal TransductionHydrogen PeroxideProtein Kinases

Identifiers

PMID23639002
PMCPMC4358782
OpenAlexW2026772781

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.