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
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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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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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Fusaric acid-mediated S-glutathionylation of MaAKT1 channel confers the virulence of Foc TR4 to banana. [PDF]
PLoS PathogensOur previous studies have demonstrated that the phytotoxin fusaric acid (FSA), secreted by several Fusarium species, acts as a key factor in the development of plant diseases; however, the underlying mechanism remains unknown.
Jun Zhang +7 more
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S-glutathionylation in cancer: from fundamental mechanisms to clinical applications
Pharmacological ResearchGlutathione (GSH) is a thiol-containing antioxidant composed of glutamic acid, cysteine and glycine. GSH can form a disulfide bond with the cysteine sulfhydryl group of a protein, resulting in S-glutathionylation (-SSG).
Desheng Xiao, Yongguang Tao
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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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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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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
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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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