An In Vitro Study of Protein S-Glutathionylation by Members of the CLIC Protein Family [PDF]
BiomoleculesIncreasing evidence points to members of the chloride intracellular ion channel (CLIC) protein family performing a variety of functions within cells—classifying them as moonlighting proteins—and serving as natural cellular antioxidant protective agents ...
Wendy El Khoury +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
doaj +5 more sources
Identification of DUOX1-dependent redox signaling through protein S-glutathionylation in airway epithelial cells [PDF]
Redox Biology, 2014 The NADPH oxidase homolog dual oxidase 1 (DUOX1) plays an important role in innate airway epithelial responses to infection or injury, but the precise molecular mechanisms are incompletely understood and the cellular redox-sensitive targets for DUOX1 ...
Milena Hristova +7 more
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Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease. [PDF]
Int J Mol Sci, 2020 S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage.
Musaogullari A, Chai YC.
europepmc +3 more sources
Isotopically Labeled Clickable Glutathione to Quantify Protein S-Glutathionylation. [PDF]
Chembiochem, 2020 AbstractProtein S‐glutathionylation is one of the important cysteine oxidation events that regulate various redox‐mediated biological processes. Despite several existing methods, there are few proteomic approaches to identify and quantify specific cysteine residues susceptible to S‐glutathionylation.
VanHecke GC +3 more
europepmc +5 more sources
The Role of S-Nitrosylation and S-Glutathionylation of Protein Disulphide Isomerase in Protein Misfolding and Neurodegeneration [PDF]
International Journal of Cell Biology, 2013 Neurodegenerative diseases involve the progressive loss of neurons, and a pathological hallmark is the presence of abnormal inclusions containing misfolded proteins.
M. Halloran, S. Parakh, J. D. Atkin
doaj +5 more sources
S-glutathionylation in protein redox regulation
Free Radical Biology and Medicine, 2007 Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and low-pK, cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative stress, but also occurs under basal (physiological) conditions.
D. Giustarini +9 more
core +6 more sources
S-Glutathionylation of Protein Disulfide Isomerase Regulates Estrogen Receptor α Stability and Function [PDF]
International Journal of Cell Biology, 2012 S-Glutathionylation of cysteine residues within target proteins is a posttranslational modification that alters structure and function. We have shown that S-glutathionylation of protein disulfide isomerase (PDI) disrupts protein folding and leads to the ...
Ying Xiong +3 more
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Protein S-glutathionylation: a regulatory device from bacteria to humans
Trends in Biochemical Sciences, 2009 S-Glutathionylation is the specific post-translational modification of protein cysteine residues by the addition of the tripeptide glutathione, the most abundant and important low-molecular-mass thiol within most cell types.
Dalle Donne, I. +3 more
core +6 more sources
Dicarbonyl Stress and S-Glutathionylation in Cerebrovascular Diseases: A Focus on Cerebral Cavernous Malformations [PDF]
Antioxidants, 2020 Dicarbonyl stress is a dysfunctional state consisting in the abnormal accumulation of reactive α-oxaldehydes leading to increased protein modification.
Cinzia Antognelli +4 more
doaj +2 more sources