Evidence map›Paper›PMID 24974182›Full record

ArticleAdvances in cancer research2014

A comparison of reversible versus irreversible protein glutathionylation.

Danyelle M Townsend, Volodymyr I Lushchak, Arthur J L Cooper

Open access · greenAbstract readComparative Study
In one paragraph

Article in Advances in cancer research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Antioxidants: a comprehensive review.Archives of toxicology · 2025
    Review
  3. Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023
    Review
  4. Article
  5. Article
  6. Emerging chemistry and biology in protein glutathionylation.Current opinion in chemical biology · 2022
    Review
  7. Article
  8. Article
  9. The Role of BRG1 in Antioxidant and Redox Signaling.Oxidative medicine and cellular longevity · 2020
    Review
  10. Differential regulation of CaScience signaling · 2019
    Article
  11. Article
  12. The Journal of biological chemistry · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
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 3 institutions in 2 countries.

Danyelle M TownsendDepartment of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, South Carolina, USA.
Volodymyr I LushchakDepartment of Biochemistry and Biotechnology, Vassyl Stefanyk Precarpathian National University, Ivano-Frankivsk, Ukraine.
Arthur J L CooperDepartment of Biochemistry and Molecular Biology, New York Medical College, Valhalla, New York, USA. Electronic address: arthur_cooper@nymc.edu.
Medical University of South Carolina · USNew York Medical College · USVasyl Stefanyk Precarpathian National University · UA

Funding

SOUTH CAROLINA COBRE IN OXIDANTS, REDOX BALANCE AND STRESS SIGNALINGP20GM103542 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI TEW, KENNETH D. · 2012 to 2020
$20.2M
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
PRECLINICAL DEVELOPMENT OF A GLUTATHIONE BASED CANCER DRUGR41CA117259 · NCI · CELLECTAR BIOSCIENCES, INC. · PI TEW, KENNETH D. · 2007 to 2007
$150k
RNS Mediated Regulation of Protein Disulfide Isomerase in Neuronal CellsR56ES017453 · NIEHS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI TOWNSEND, DANYELLE M. · 2010 to 2010
$108k
NCI NIH HHS CA08660NCI NIH HHS CA117259NCI NIH HHS R41 CA117259NCRR NIH HHS 5P20RR024485-02NCRR NIH HHS P20 RR024485NIEHS NIH HHS R56 ES017453NIGMS NIH HHS 8 P20 GM103542-02NIGMS NIH HHS P20 GM103542
6 · The paper itself

Abstract

Glutathionylation is generally a reversible posttranslational modification that occurs to cysteine residues that have been exposed to reactive oxygen species (P-SSG). This cyclical process can regulate various clusters of proteins, including those involved in critical cellular signaling functions. However, certain conditions can favor the formation of dehydroamino acids, such as 2,3-didehydroalanine (2,3-dehydroalanine, DHA) and 2,3-didehydrobutyrine (2,3-dehydrobutyrine), which can act as Michael acceptors. In turn, these can form Michael adducts with glutathione (GSH), resulting in the formation of a stable thioether conjugate, an irreversible process referred to as nonreducible glutathionylation. This is predicted to be prevalent in nature, particularly in more slowly turning over proteins. Such nonreducible glutathionylation can be distinguished from the more facile cycling signaling processes and is predicted to be of gerontological, toxicological, pharmacological, and oncological relevance. Here, we compare reversible and irreversible glutathionylation.

Indexed as

AlanineAminobutyratesEnzymesGene Expression Regulation, NeoplasticGlutaredoxinsGlutathioneGlutathione DisulfideGlutathione TransferaseHumansLens, CrystallineNeoplasmsPeptidesProteinsReactive Oxygen SpeciesSignal TransductionAlanineAminobutyratesdehydroalaninedehydrobutyrineEnzymesGlutaredoxinsGlutathioneGlutathione DisulfideGlutathione TransferasePeptidesProteinsReactive Oxygen SpeciesDehydroalanineGlutaredoxinGlutathioneGlutathione disulfideGlutathione S-transferasesIrreversible protein glutathionylationLanthionineReversible glutathionylationγ-Glutamyl-L-cysteine

Identifiers

PMID24974182
PMCPMC4603650
OpenAlexW2418353212

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.