Evidence map›Paper›PMID 37245422›Full record

ReviewCurrent opinion in chemical biology2023

Chemistry and biology of enzymes in protein glutathionylation.

Daniel Oppong, William Schiff, Madhu C Shivamadhu, Young-Hoon Ahn

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Redox Regulation of Cell Migration via Nischarin S-glutathionylation.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Natural variation in age-related dopamine neuron degeneration is glutathione dependent and linked to life span.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Glutathione-Dependent Pathways in Cancer Cells.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Article
  12. A Prognostic Activity of Glutaredoxin 1 Protein (Grx1) in Colon Cancer.International journal of molecular sciences · 2024
    Article
  13. Article
  14. Robust AMBER Force Field Parameters for Glutathionylated Cysteines.International journal of molecular sciences · 2023
    Article
  15. Article
  16. 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

4 authors at 1 institution in 1 country.

Daniel OppongDepartment of Chemistry, Drexel University, Philadelphia, PA 19104, USA.
William SchiffDepartment of Chemistry, Drexel University, Philadelphia, PA 19104, USA.
Madhu C ShivamadhuDepartment of Chemistry, Drexel University, Philadelphia, PA 19104, USA.
Young-Hoon AhnDepartment of Chemistry, Drexel University, Philadelphia, PA 19104, USA. Electronic address: ya426@drexel.edu.
Drexel 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 is emerging as a central oxidation that regulates redox signaling and biological processes linked to diseases. In recent years, the field of protein S-glutathionylation has expanded by developing biochemical tools for the identification and functional analyses of S-glutathionylation, investigating knockout mouse models, and developing and evaluating chemical inhibitors for enzymes involved in glutathionylation. This review will highlight recent studies of two enzymes, glutathione transferase omega 1 (GSTO1) and glutaredoxin 1 (Grx1), especially introducing their glutathionylation substrates associated with inflammation, cancer, and neurodegeneration and showcasing the advancement of their chemical inhibitors. Lastly, we will feature protein substrates and chemical inducers of LanC-like protein (LanCL), the first enzyme in protein C-glutathionylation.

Indexed as

GlutathioneProtein SAnimalsBiologyMiceOxidation-ReductionProtein Processing, Post-TranslationalGlutathioneProtein SC-glutathionylationCysteineGlutaredoxinGlutathione transferase omegaLanC-like proteinS-glutathionylation

Identifiers

PMID37245422
PMCPMC10524987
OpenAlexW4378449678

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.