Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation [PDF]
Molecules, 2021 S-glutathionylation and S-nitrosylation are reversible post-translational modifications on the cysteine thiol groups of proteins, which occur in cells under physiological conditions and oxidative/nitrosative stress both spontaneously and enzymatically ...
Elena Kalinina, Maria Novichkova
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Glutaredoxin 1 protects lens epithelial cells from epithelial-mesenchymal transition by preventing casein kinase 1α S-glutathionylation during posterior capsular opacification [PDF]
Redox Biology, 2023 Oxidative stress drives protein S-glutathionylation, which regulates the structure and function of target proteins and is implicated in the pathogenesis of many diseases.
Chenshuang Li +6 more
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Regulation of Mitochondrial Hydrogen Peroxide Availability by Protein S-glutathionylation [PDF]
Cells, 2022 Background: It has been four decades since protein S-glutathionylation was proposed to serve as a regulator of cell metabolism. Since then, this redox-sensitive covalent modification has been identified as a cell-wide signaling platform required for ...
Ryan J. Mailloux +2 more
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A novel approach for predicting protein S-glutathionylation [PDF]
BMC Bioinformatics, 2020 Background S-glutathionylation is the formation of disulfide bonds between the tripeptide glutathione and cysteine residues of the protein, protecting them from irreversible oxidation and in some cases causing change in their functions.
Anastasia A. Anashkina +6 more
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Alcohol Binge Drinking Selectively Stimulates Protein S-Glutathionylation in Aorta and Liver of ApoE−/− Mice [PDF]
Frontiers in Cardiovascular Medicine, 2021 Background: Binge drinking has become the most common and deadly pattern of excessive alcohol use in the United States, especially among younger adults. It is closely related to the increased risk of cardiovascular disease.
Kerstin Seidel +6 more
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S-glutathionylation of Hsp90 enhances its degradation and correlates with favorable prognosis of breast cancer [PDF]
Redox Biology, 2022 Heat shock protein 90 (Hsp90) is a ubiquitous chaperone to interact with numerous proteins to regulate multiple cellular processes, especially during cell proliferation and cell cycle progression.
Yu-Yin Shih +6 more
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Immunoprecipitation methods to identify S-glutathionylation in target proteins [PDF]
MethodsX, 2019 S-glutathionylation is a reversible post-translational modification of proteins that generate a mixed disulfide between glutathione to thiolate anion of cysteine residues in target proteins. In the last ten years, S-glutathionylation has been extensively
Elena Butturini +3 more
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Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle
Redox Biology, 2018 Protein S-glutathionylation is an important reversible post-translational modification implicated in redox signaling. Oxidative modifications to protein thiols can alter the activity of metabolic enzymes, transcription factors, kinases, phosphatases, and
Philip A Kramer +2 more
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Cell Reports, 2017 Reactive oxygen species (ROS)-induced cysteine S-glutathionylation is an important posttranslational modification (PTM) that controls a wide range of intracellular protein activities.
Xue Zhang, Fan Zhao, Hongbo Yu
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ROS-Driven STAT1 S-Glutathionylation Sustains IFNγ Signaling and Pro-Inflammatory Microglial Polarization [PDF]
AntioxidantsOxidative stress is a major driver of neuroinflammation, yet the molecular redox mechanisms that shape microglial activation remain incompletely defined.
Martina Brattini +8 more
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