Results 31 to 40 of about 8,445 (200)
Frontiers in Physiology, 2013 Our previous studies demonstrated a relation between glutathionylation of cardiac myosin binding protein C and diastolic dysfunction in a hypertensive mouse model stressed by treatment with salt, deoxycorticosterone acetate, and unilateral nephrectomy.
Bindiya G Patel +2 more
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Antioxidants, 2022 Mitochondrial complex I can produce large quantities of reactive oxygen species (ROS) by reverse electron transfer (RET) from the ubiquinone (UQ) pool.
Kevin Wang +3 more
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dbGSH: a database of S-glutathionylation [PDF]
Bioinformatics, 2014 Summary: S-glutathionylation, the reversible protein posttranslational modification (PTM) that generates a mixed disulfide bond between glutathione and cysteine residue, critically regulates protein activity, stability and redox regulation. Due to its importance in regulating oxidative/nitrosative stress and balance in cellular response, a number of ...
Yi-Ju Chen +3 more
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eLife, 2020 Peroxiredoxins are H2O2 scavenging enzymes that also carry out H2O2 signaling and chaperone functions. In yeast, the major cytosolic peroxiredoxin, Tsa1 is required for both promoting resistance to H2O2 and extending lifespan upon caloric restriction. We
Friederike Roger +14 more
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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
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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
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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
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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
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
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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
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