Causes and consequences of cysteine S-glutathionylation
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Post-translational S-glutathionylation occurs through the reversible addition of a proximal donor of glutathione to thiolate anions of cysteines in target proteins, where the modification alters molecular mass, charge, and structure/function and/or prevents degradation from sulfhydryl overoxidation or proteolysis. Catalysis of both the forward (glutathione S-transferase P) and reverse (glutaredoxin) reactions creates a functional cycle that can also regulate certain protein functional clusters, including those involved in redox-dependent cell signaling events. For translational application, S-glutathionylated serum proteins may be useful as biomarkers in individuals (who may also have polymorphic expression of glutathione S-transferase P) exposed to agents that cause oxidative or nitrosative stress.
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Reversible oxidation of Cys residues of complex I, ALDH2, and Prx3 seems protective, despite temporary inactivation, against further tissue damage from irreversible hyper-oxidation of Cys followed by proteolytic degradation.
“For instance, reversible oxidation of Cys residues of mitochondrial NADH-dependent ubiquinone oxidoreductase (complex I), ALDH2, and Prx3 seem to be protective, despite temporary inactivation, against further tissue damage from irreversible hyper-oxidation of Cys to Cys-sulfinic acid (Cys-SO2) and Cys-sulfonic acid (Cys-SO3) followed by proteolytic degradation [67], [68], as in the case of I/R”
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Self-citationTargeting biomolecules with reversible covalent chemistry
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One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates
Trujillo, M., Alvarez, B., & Radi, R. (2016) · Free Radical Research · doi:10.3109/10715762.2015.1089988 · Cited by 142 · see citing works
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“For instance, reversible oxidation of Cys residues of mitochondrial NADH-dependent ubiquinone oxidoreductase (complex I), ALDH2, and Prx3 seem to be protective, despite temporary inactivation, against further tissue damage from irreversible hyper-oxidation of Cys to Cys-sulfinic acid (Cys-SO2) and Cys-sulfonic acid (C…”
BackgroundVaradharaj, S., Kelly, O. J., Khayat, R. N., Kumar, P. S., Ahmed, N., & Zweier, J. L. (2017) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2017.00064 · Cited by 101 · see citing works
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Thiol regulation by Mn porphyrins, commonly known as SOD mimics
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How widespread is stable protein S-nitrosylation as an end-effector of protein regulation?
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Wang, Y.-T., Piyankarage, S. C., Williams, D. L., & Thatcher, G. R. J. (2014) · ACS Chemical Biology · doi:10.1021/cb400547u · Cited by 33 · see citing works
- Authors
- Grek, C. L., Zhang, J., Manevich, Y., Townsend, D. M., & Tew, K. D.
- Affiliations
- Medical University of South Carolina (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 288
- Issue
- 37
- Pages
- 26497-26504
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3772197
- OpenAlex
- W1964891414
- Cited by
- 312
- References
- 104
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 15 · 2023: 19 · 2022: 16 · 2021: 14 · 2020: 35 · 2019: 28 · 2018: 35 · 2017: 30 · 2016: 38 · 2015: 26 · 2014: 29 · 2013: 6
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1c06rr015455-01a1)
- National Cancer Institute (R01CA085660, R41CA117259, CA08660, CA117259)
- National Center for Research Resources (C06 RR-015455, P20RR024485)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- post-translational modification, glutathione S-transferase pi, glutaredoxin, thiolate anion, protein redox regulation, oxidative stress, nitrosative stress, serum protein biomarkers, proteolysis
- MeSH terms
- Animals, Cysteine, Glutathione, Glutathione Transferase, Humans, Nitric Oxide, Nitrogen, Oxidation-Reduction, Peroxidases, Protein Processing, Post-Translational, Sulfhydryl Compounds, Serpins, Gene Expression Regulation, Enzymologic, Reactive Oxygen Species, Oxidative Stress, Glutaredoxins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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