Journal article
Chemistry and biology of enzymes in protein glutathionylation
Current opinion in chemical biology, v 75, 102326
01 Aug 2023
PMID: 37245422
Featured in Collection : UN Sustainable Development Goals @ Drexel
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.
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Details
- Title
- Chemistry and biology of enzymes in protein glutathionylation
- Creators
- Daniel Oppong - Drexel UniversityWilliam Schiff - Drexel University, ChemistryMadhu C Shivamadhu - Drexel UniversityYoung-Hoon Ahn - Drexel University, Chemistry
- Publication Details
- Current opinion in chemical biology, v 75, 102326
- Publisher
- Elsevier
- Grant note
- R01 GM143214 / NIGMS NIH HHS R01 HL131740 / NHLBI NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:001008673000001
- Scopus ID
- 2-s2.0-85160404433
- Other Identifier
- 991022024011104721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics