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
exaly +3 more sources
The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26 [PDF]
BiomoleculesThe oxidation of cysteines in crystallins is a major age-related modification associated with cataract formation. The purpose of this research was to determine the susceptibility of γS-crystallin to glutathionylation-induced oxidation and disulfide bond ...
Kate Halverson-Kolkind +5 more
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Carbon monoxide induces heme oxygenase-1 to modulate STAT3 activation in endothelial cells via S-glutathionylation. [PDF]
PLoS ONE, 2014 IL-6/STAT3 pathway is involved in a variety of biological responses, including cell proliferation, differentiation, apoptosis, and inflammation.
Yan-Chang Yang +4 more
doaj +1 more source
The effect of oxidant and the non-oxidant alteration of cellular thiol concentration on the formation of protein mixed-disulfides in HEK 293 cells. [PDF]
PLoS ONE, 2008 Cellular molecules possess various mechanisms in responding to oxidant stress. In terms of protein responses, protein S-glutathionylation is a unique post-translational modification of protein reactive cysteines forming disulfides with glutathione ...
Jasen Lee Gilge +2 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
doaj +1 more source
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
doaj +1 more source
GSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity. [PDF]
PLoS ONE, 2015 S-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, is a selective and reversible protein post-translational modification (PTM) that regulates protein activity, localization, and stability.
Yi-Ju Chen +5 more
doaj +1 more source
Prediction of S-glutathionylation sites based on protein sequences. [PDF]
PLoS ONE, 2013 S-glutathionylation, the reversible formation of mixed disulfides between glutathione(GSH) and cysteine residues in proteins, is a specific form of post-translational modification that plays important roles in various biological processes, including ...
Chenglei Sun +4 more
doaj +1 more source
High glutathionylation of placental endothelial nitric oxide synthase in preeclampsia
Redox Biology, 2019 Decreased nitric oxide (NO) bioavailability plays a critical role in the pathophysiology of preeclampsia (PE). Recent evidence indicates that S-glutathionylation may occur on the endothelial nitric oxide synthase (eNOS), leading to eNOS uncoupling ...
Paul Guerby +7 more
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