A Narrative Review of the Role of S-Glutathionylation in Bacteria. [PDF]
MicroorganismsProtein glutathionylation is defined as a reversible, ubiquitous post-translational modification, resulting in the formation of mixed disulfides between glutathione and proteins’ cysteine residues. Glutathionylation has been implicated in several cellular mechanisms ranging from protection from oxidative stress to the control of cellular homeostasis ...
Federici L +3 more
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Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease [PDF]
International Journal of Molecular Sciences, 2020 Yuh-Cherng Chai
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Causes and Consequences of Cysteine S-Glutathionylation [PDF]
Journal of Biological Chemistry, 2013 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.
Christina L, Grek +4 more
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Redox regulation of cell migration via Nischarin S-glutathionylation. [PDF]
Free Radic Biol MedAbstract Reactive oxygen species (ROS) are central players in redox signaling, controlling all biological processes in human health. Many reports demonstrated that ROS play essential roles in regulating cell migration and invasion, while contributing to cancer progression and metastasis, potentially via inducing protein cysteine ...
Shivamadhu MC +7 more
europepmc +8 more sources
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
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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
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S-Glutathionylation Regulates Inflammatory Activities of S100A9 [PDF]
Journal of Biological Chemistry, 2010 Reactive oxygen species generated by activated neutrophils can cause oxidative stress and tissue damage. S100A8 (A8) and S100A9 (A9), abundant in neutrophil cytoplasm, are exquisitely sensitive to oxidation, which may alter their functions. Murine A8 is a neutrophil chemoattractant, but it suppresses leukocyte transmigration in the microcirculation ...
Su Yin, Lim +3 more
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S-Glutathionylation in Monocyte and Macrophage (Dys)Function [PDF]
International Journal of Molecular Sciences, 2013 Atherosclerosis is a chronic inflammatory disease involving the accumulation of monocytes and macrophages in the vascular wall. Monocytes and macrophages play a central role in the initiation and progression of atherosclerotic lesion development. Oxidative stress, which occurs when reactive oxygen species (ROS) overwhelm cellular antioxidant systems ...
Ullevig, Sarah +2 more
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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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