Evidence map›Paper›PMID 23861399›Full record

ReviewThe Journal of biological chemistry2013

Causes and consequences of cysteine S-glutathionylation.

Christina L Grek, Jie Zhang, Yefim Manevich, Danyelle M Townsend, Kenneth D Tew

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.

0numbers the graph read from it
0cells of the map it votes in
157citing papers in PubMed
–field-weighted citation impact
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

157 citing papers in PubMed.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Article
  6. Implication ofInternational journal of molecular sciences · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. The ascorbate-glutathione cycle coming of age.Journal of experimental botany · 2024
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

97 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

5 authors.

Christina L GrekFrom the Departments of Cell and Molecular Pharmacology and Experimental Therapeutics and.
Jie Zhang
Yefim Manevich
Danyelle M Townsend
Kenneth D Tew

Funding

GLUTATHIONE S TRANSFERASES IN DRUG AND STRESS RESPONSER01CA085660 · NCI · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI TEW, KENNETH D. · 2000 to 2014
$5.0M
SOUTH CAROLINA COBRE IN OXIDANTS, REDOX BALANCE AND STRESS SIGNALINGP20RR024485 · NCRR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI TEW, KENNETH D. · 2011 to 2011
$2.2M
MUSC FACIL EXPANSION &RENOV: SLE C06RR015455 · NCRR · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI RAYMOND, JOHN R · 2002 to 2002
$2.0M
PRECLINICAL DEVELOPMENT OF A GLUTATHIONE BASED CANCER DRUGR41CA117259 · NCI · CELLECTAR BIOSCIENCES, INC. · PI TEW, KENNETH D. · 2007 to 2007
$150k
NCI NIH HHS CA08660NCI NIH HHS CA117259NCI NIH HHS R01 CA085660NCI NIH HHS R41 CA117259NCRR NIH HHS C06 RR015455NCRR NIH HHS P20 RR024485
6 · The paper itself

Abstract

Post-translational S-glutathionylation occurs through the reversible addition of a proximal donor of glutathione to thiolate anions of cysteines in target proteins, where the modification alters molecular mass, charge, and structure/function and/or prevents degradation from sulfhydryl overoxidation or proteolysis. Catalysis of both the forward (glutathione S-transferase P) and reverse (glutaredoxin) reactions creates a functional cycle that can also regulate certain protein functional clusters, including those involved in redox-dependent cell signaling events. For translational application, S-glutathionylated serum proteins may be useful as biomarkers in individuals (who may also have polymorphic expression of glutathione S-transferase P) exposed to agents that cause oxidative or nitrosative stress.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsCysteineGlutaredoxinsGlutathioneGlutathione TransferaseHumansNitric OxideNitrogenOxidation-ReductionOxidative StressPeroxidasesProtein Processing, Post-TranslationalReactive Oxygen SpeciesSerpinsSulfhydryl CompoundsCysteineGlutaredoxinsGlutathioneGlutathione TransferaseNitric OxideNitrogenPeroxidasesReactive Oxygen SpeciesSerpinsSulfhydryl CompoundsCysteine-mediated Cross-linkingGlutathioneGlutathione S-TransferaseGlutathionylationKinase SignalingNitric OxideNitrosylationPeroxidasesPeroxiredoxinSerpin

Identifiers

PMID23861399
PMCPMC3772197

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.