Altered protein S-glutathionylation identifies a potential mechanism of resistance to acetaminophen-induced hepatotoxicity. [PDF]
J Pharmacol Exp Ther, 2015 Acetaminophen (APAP) is the most commonly used over-the-counter analgesic. However, hepatotoxicity induced by APAP is a major clinical issue, and the factors that define sensitivity to APAP remain unclear. We have previously demonstrated that mice nulled
McGarry DJ +3 more
europepmc +3 more sources
Protein S -Glutathionylation Mediates Macrophage Responses to Metabolic Cues from the Extracellular Environment [PDF]
Antioxidants and Redox Signaling, 2016 Sarah L Ullevig +2 more
exaly +2 more sources
Glutathione S -Transferase P-Mediated Protein S-Glutathionylation of Resident Endoplasmic Reticulum Proteins Influences Sensitivity to Drug-Induced Unfolded Protein Response [PDF]
Antioxidants and Redox Signaling, 2017 Zhi-Wei Ye +2 more
exaly +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
doaj +1 more source
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
openaire +2 more sources
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
openaire +4 more sources
Quantitative Profiling of Protein S-Glutathionylation Reveals Redox-Dependent Regulation of Macrophage Function during Nanoparticle-Induced Oxidative Stress. [PDF]
ACS Nano, 2016 Engineered nanoparticles (ENPs) are increasingly utilized for commercial and medical applications; thus, understanding their potential adverse effects is an important societal issue.
Duan J +8 more
europepmc +2 more sources
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
doaj +1 more source