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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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
Glutathione S-Transferase P-Mediated Protein S-Glutathionylation of Resident Endoplasmic Reticulum Proteins Influences Sensitivity to Drug-Induced Unfolded Protein Response. [PDF]
Antioxid Redox Signal, 2017 Ye ZW +5 more
europepmc +2 more sources
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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Fluorescein-labeled glutathione to study protein S-glutathionylation [PDF]
Analytical Biochemistry, 2010 Numerous studies of S-glutathionylation of cysteine thiols indicate that this protein modification plays a key role in redox regulation of proteins. To facilitate the study of protein S-glutathionylation, we developed a synthesis and purification to produce milligram quantities of fluorescein-labeled glutathione.
Lisa M, Landino +6 more
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In Vivo Tagging and Characterization of S‐Glutathionylated Proteins by a Chemoenzymatic Method [PDF]
Angewandte Chemie, 2012 Glutathione (GSH), a sulfhydryl-containing tripeptide present in most organisms at millimolar levels, plays a crucial role in redox homeostasis.1 Reactive cysteine residues are vulnerable to reactive oxygen or nitrogen species and thus depend heavily on GSH to avoid irreversible oxidation.[1a], [2] Reversible conjugation of GSH to proteins through the ...
Chiang, Bing-Yu +8 more
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PLoS Pathogens, 2020 S-glutathionylation is an important post-translational modification (PTM) process that targets protein cysteine thiols by the addition of glutathione (GSH).
Zhengyi Li +6 more
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Redox Biology, 2016 Background: Oxidative stress is implicated in increased vascular permeability associated with metabolic disorders, but the underlying redox mechanism is poorly defined.
Jingyan Han +11 more
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Protein thiyl radical mediates S-glutathionylation of complex I [PDF]
Free Radical Biology and Medicine, 2012 Complex I is a critical site of O(2)(•-) production and the major host of reactive protein thiols in mitochondria. In response to oxidative stress, complex I protein thiols at the 51- and 75-kDa subunits are reversibly S-glutathionylated. The mechanism of complex I S-glutathionylation is mainly obtained from insight into GSSG-mediated thiol-disulfide ...
Patrick T, Kang +5 more
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New insights into posttranslational modifications of proteins during bull sperm capacitation
Cell Communication and Signaling, 2023 Background Due to the unique nature of spermatozoa, which are transcriptionally and translationally silent, the regulation of capacitation is based on the formation of posttranslational modifications of proteins (PTMs).
Agnieszka Mostek-Majewska +3 more
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