Evidence map›Paper›PMID 36223700›Full record

ReviewCurrent opinion in chemical biology2022

Emerging chemistry and biology in protein glutathionylation.

Dhanushika S K Kukulage, Nadee N J Matarage Don, Young-Hoon Ahn

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Unravelling the Therapeutic Potential of Cysteine for Cardiovascular Health.International journal of molecular sciences · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Redox Regulation of Cell Migration via Nischarin S-glutathionylation.bioRxiv : the preprint server for biology · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023
    Review
  19. Article
  20. Review
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 1 country.

Dhanushika S K KukulageDepartment of Chemistry, Wayne State University, Detroit, MI 48202, USA.
Nadee N J Matarage DonDepartment of Chemistry, Wayne State University, Detroit, MI 48202, USA.
Young-Hoon AhnDepartment of Chemistry, Drexel University, Philadelphia, PA 19104, USA. Electronic address: ya426@drexel.edu.
Wayne State University · USDrexel University · US

Funding

Chemical Methods for Dissecting Protein Glutathionylation in SarcomereR01HL131740 · NHLBI · WAYNE STATE UNIVERSITY · PI AHN, YOUNG-HOON, BHAGWAT, ASHOK S · 2017 to 2021
$1.8M
Chemical Proteomic Strategy to Investigate Cysteine GlutathionylationR01GM143214 · NIGMS · WAYNE STATE UNIVERSITY · PI AHN, YOUNG-HOON · 2021 to 2024
$1.1M
NHLBI NIH HHS R01 HL131740NIGMS NIH HHS R01 GM143214
6 · The paper itself

Abstract

Protein S-glutathionylation serves a regulatory role in proteins and modulates distinct biological processes implicated in health and diseases. Despite challenges in analyzing the dynamic and reversible nature of S-glutathionylation, recent chemical and biological methods have significantly advanced the field of S-glutathionylation, culminating in selective identification and detection, structural motif analysis, and functional studies of S-glutathionylation. This review will highlight emerging studies of protein glutathionylation, beginning by introducing biochemical tools that enable mass spectrometric identification and live-cell imaging of S-glutathionylation. Next, it will spotlight recent examples of S-glutathionylation regulating physiology and inflammation. Lastly, we will feature two emerging lines of glutathionylation research in cryptic cysteine glutathionylation and protein C-glutathionylation.

Indexed as

CysteineGlutathioneBiologyOxidation-ReductionProtein Processing, Post-TranslationalProteinsCysteineGlutathioneProteinsC-glutathionylationCryptic cysteinesCysteineProteomicsRedox signalingS-glutathionylation

Identifiers

PMID36223700
PMCPMC9844265
OpenAlexW4303857481

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.