Results 31 to 40 of about 8,996 (206)
Proteomic Identification of Protein Glutathionylation in Cardiomyocytes [PDF]
Journal of Proteome Research, 2019 Reactive oxygen species (ROS) are important signaling molecules, but their overproduction is associated with many cardiovascular diseases, including cardiomyopathy. ROS induce various oxidative modifications, among which glutathionylation is one of the significant protein oxidations that occur under oxidative stress.
Garrett C. VanHecke +2 more
openaire +2 more sources
Interplay among Oxidative Stress, Methylglyoxal Pathway and S-Glutathionylation
Antioxidants, 2020 Reactive oxygen species (ROS) are produced constantly inside the cells as a consequence of nutrient catabolism. The balance between ROS production and elimination allows to maintain cell redox homeostasis and biological functions, avoiding the occurrence
Lidia de Bari +5 more
doaj +1 more source
Temporal changes in glutaredoxin 1 and protein s-glutathionylation in allergic airway inflammation. [PDF]
PLoS ONE, 2015 Asthma is a chronic inflammatory disorder of the airways, involving oxidative stress. Upon oxidative stress, glutathione covalently binds to protein thiols to protect them against irreversible oxidation.
Kanako Maki +5 more
doaj +1 more source
Protein Glutathionylation in the Pathogenesis of Neurodegenerative Diseases [PDF]
Oxidative Medicine and Cellular Longevity, 2017 Protein glutathionylation is a redox‐mediated posttranslational modification that regulates the function of target proteins by conjugating glutathione with a cysteine thiol group on the target proteins. Protein glutathionylation has several biological functions such as regulation of metabolic pathways, calcium homeostasis, signal transduction ...
Sun Joo Cha +4 more
openaire +2 more sources
Protein S-glutathionylation: a regulatory device from bacteria to humans
, 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.
A. Milzani +4 more
core +2 more sources
Immunoprecipitation methods to identify S-glutathionylation in target proteins
MethodsX, 2019 S-glutathionylation is a reversible post-translational modification of proteins that generate a mixed disulfide between glutathione to thiolate anion of cysteine residues in target proteins. In the last ten years, S-glutathionylation has been extensively
Elena Butturini +3 more
doaj +1 more source
Oxidative stress (glutathionylation) and Na,K-ATPase activity in rat skeletal muscle. [PDF]
PLoS ONE, 2014 Changes in ion distribution across skeletal muscle membranes during muscle activity affect excitability and may impair force development. These changes are counteracted by the Na,K-ATPase. Regulation of the Na,K-ATPase is therefore important for skeletal
Carsten Juel
doaj +1 more source
Regulation of Mitochondrial Hydrogen Peroxide Availability by Protein S-glutathionylation
Cells, 2022 Background: It has been four decades since protein S-glutathionylation was proposed to serve as a regulator of cell metabolism. Since then, this redox-sensitive covalent modification has been identified as a cell-wide signaling platform required for ...
Ryan J. Mailloux +2 more
doaj +1 more source
Glutathionylation of Trypanosomal Thiol Redox Proteins [PDF]
Journal of Biological Chemistry, 2007 Trypanosomatids, the causative agents of several tropical diseases, lack glutathione reductase and thioredoxin reductase but have a trypanothione reductase instead. The main low molecular weight thiols are trypanothione (N(1),N(8)-bis-(glutathionyl)spermidine) and glutathionyl-spermidine, but the parasites also contain free glutathione.
Johannes, Melchers +3 more
openaire +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