Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle [PDF]
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 +7 more
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Protein S-glutathionylation confers cellular resistance to ferroptosis induced by glutathione depletion [PDF]
Redox BiologyFerroptosis is one of the most critical biological consequences of glutathione depletion. Excessive oxidative stress, indicated by an elevated oxidized glutathione (GSSG)/reduced glutathione (GSH) ratio, is recognized as a key driver of ferroptosis ...
Yi Ju +20 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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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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Protein S-glutathionylation lowers superoxide/hydrogen peroxide release from skeletal muscle mitochondria through modification of complex I and inhibition of pyruvate uptake. [PDF]
PLoS ONE, 2018 Protein S-glutathionylation is a reversible redox modification that regulates mitochondrial metabolism and reactive oxygen species (ROS) production in liver and cardiac tissue.
Robert M Gill +4 more
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Temporal changes in glutaredoxin 1 and protein s-glutathionylation in allergic airway inflammation. [PDF]
PLoS ONE, 2015 Asthma is a chronic inflammatory disorder of the airways, involving oxidative stress. Upon oxidative stress, glutathione covalently binds to protein thiols to protect them against irreversible oxidation.
Kanako Maki +5 more
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Activation of Nrf2 at Critical Windows of Development Alters Tissue-Specific Protein S-Glutathionylation in the Zebrafish (Danio rerio) Embryo [PDF]
AntioxidantsActivation of Nrf2—the master regulator of antioxidative response—at different stages of embryonic development has been shown to result in changes in gene expression, but the tissue-specific and downstream effects of Nrf2 activation during development ...
Emily S. Marques +4 more
doaj +2 more sources
Sputum Glutaredoxin 1 and Protein S-Glutathionylation in COPD [PDF]
AntioxidantsAlterations in glutathione and its metabolism contribute to oxidative stress in COPD, but the role of S-glutathionylation (PSSG) and its major regulator glutaredoxin 1 (Grx1) remains unclear.
Ine Kuipers +7 more
doaj +2 more sources
Identification of DUOX1-dependent redox signaling through protein S-glutathionylation in airway epithelial cells [PDF]
Redox Biology, 2014 The NADPH oxidase homolog dual oxidase 1 (DUOX1) plays an important role in innate airway epithelial responses to infection or injury, but the precise molecular mechanisms are incompletely understood and the cellular redox-sensitive targets for DUOX1 ...
Milena Hristova +7 more
doaj +2 more sources