Emerging chemistry and biology in protein glutathionylation |
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| Affiliation: | 1. Department of Chemistry, Wayne State University, Detroit, MI 48202, USA;2. Department of Chemistry, Drexel University, Philadelphia, PA 19104, USA;1. Department of Microbiology, The Ohio State University, Columbus OH 43210, USA;2. Division of Medicinal Chemistry and Pharmacognosy, The Ohio State University, Columbus OH 43210, USA;3. Infectious Diseases Institute, The Ohio State University, Columbus OH 43210, USA;4. Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA;5. Center for Biophysics and Quantitative Biology, University of Illinois, Urbana, IL 61801, USA;6. Carl Woese Institute for Genomic Biology, University of Illinois, Urbana, IL 61801, USA;1. Department of Pharmacology, University of California San Diego, USA;2. Department of Chemistry and Biochemistry, University of California Los Angeles, USA;3. Department of Bioengineering, University of California San Diego, USA;4. Department of Chemistry and Biochemistry, University of California San Diego, USA;1. Department of Chemistry, University of California, Berkeley, CA, 94720, USA;2. Department of Molecular & Cell Biology, University of California, Berkeley, CA, 94720, USA;3. Helen Wills Neuroscience Institute, University of California, Berkeley, CA, 94720, USA |
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| 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. |
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| Keywords: | Cysteine S-glutathionylation Proteomics Redox signaling Cryptic cysteines C-glutathionylation |
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