Results 41 to 50 of about 8,996 (206)
Glutathionyl systems and metabolic dysfunction in obesity [PDF]
Nutrition Reviews, 2015 Oxidative stress is associated with obesity. However, glutathione (GSH), one of the body's most abundant antioxidants, plays dual and seemingly contradictory roles in the development of obesity and its comorbidities. Glutathione has complex metabolic and biochemical fates and is a cofactor for several enzymes that function in modifying obesity-related ...
Matthew J, Picklo +2 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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S-glutathionylation reactions in mitochondrial function and disease
Frontiers in Cell and Developmental Biology, 2014 Mitochondria are highly efficient energy-transforming organelles that convert energy stored in carbon bonds into the universal energy currency ATP. The production of ATP by mitochondria is dependent on oxidation of nutrients and coupling of exergonic ...
Ryan J. Mailloux, William G. Willmore
doaj +1 more source
Causes and Consequences of Cysteine S-Glutathionylation [PDF]
Journal of Biological Chemistry, 2013 Post-translational S-glutathionylation occurs through the reversible addition of a proximal donor of glutathione to thiolate anions of cysteines in target proteins, where the modification alters molecular mass, charge, and structure/function and/or prevents degradation from sulfhydryl overoxidation or proteolysis.
Christina L, Grek +4 more
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mBio, 2021 Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent for coronavirus disease 2019 (COVID-19), encodes two proteases required for replication.
David A. Davis +9 more
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Glutathionylation of the Na K Pump [PDF]
Biophysical Journal, 2014 Reversible oxidative modifications of proteins are of importance for the normal cell functioning, e.g. for the receptor-coupled signaling. The formation of a disulfide bond between a protein and a glutathione tripeptide (Glu-Cys-Gly,) is an oxidative, posttranslational modification that might be involved in the cellular signaling.
Kopec, Wojciech +2 more
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Molecular mechanisms and potential clinical significance of S-glutathionylation
, 2008 Protein S-glutathionylation, the reversible binding of glutathione to protein thiols (PSH), is involved in protein redox regulation, storage of glutathione, and protection of PSH from irreversible oxidation.
DALLE DONNE I +11 more
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Cysteine-based redox regulation and signalling in plants
Frontiers in Plant Science, 2013 Living organisms are subjected to oxidative stress conditions which are characterized by the production of reactive oxygen (ROS), nitrogen (RNS) and sulfur (RSS) species.
Jérémy eCouturier +3 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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Glutathionylation of
mBio, 2017 Glutathionylation, the formation of reversible mixed disulfides between glutathione and protein cysteine residues, is a posttranslational modification previously observed for intracellular proteins of bacteria.
Anthony Mitchell +7 more
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