Results 11 to 20 of about 8,445 (200)
S-glutathionylation reactions in mitochondrial function and disease [PDF]
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
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Glutathionylation pathways in drug response
Current Opinion in Pharmacology, 2007 Regulation of protein function through post-translational modifications (PTM) can be important pharmacological target, and there are drugs developed to modulate specific PTM such as protein kinase or histone deacetylase inhibitors. We are still far behind in considering protein glutathionylation as pharmacological target as the biological consequences ...
Ghezzi, Pietro, Di Simplicio, Paolo
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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
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Detection of Protein Glutathionylation
, 2009 Recent studies indicate that protein glutathionylation is an important regulatory mechanism. The develop-ment of redox proteomics techniques to identify proteins undergoing glutathionylation has a key role in defining the importance of this post-translational modification, although the available methods are not yet comparable to those for the study of ...
E. Gianazza, I. Eberini, P. Ghezzi
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Redox regulation of cyclophilin A by glutathionylation
PROTEOMICS, 2006 AbstractUsing redox proteomics techniques to characterize the thiol status of proteins in human T lymphocytes, we identified cyclophilin A (CypA) as a specifically oxidized protein early after mitogen activation. CypA is an abundantly expressed cytosolic protein, target of the immunosuppressive drug cyclosporin A (CsA), for which a variety of functions
Ghezzi, Pietro +14 more
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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-pKa cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative stress, but also occurs under basal (physiological) conditions. S-glutathionylation has now emerged as a potential mechanism for dynamic, posttranslational regulation
Dalle Donne, I. +4 more
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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
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Post-translational S-glutathionylation of cofilin increases actin cycling during cocaine seeking.
PLoS ONE, 2019 Neuronal defense against oxidative damage is mediated primarily by the glutathione redox system. Traditionally considered a mechanism to protect proteins from irreversible oxidation, mounting evidence supports a role for protein S-glutathionylation in ...
Anna Kruyer +4 more
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Immunoprecipitation methods to identify S-glutathionylation in target proteins [PDF]
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 +2 more sources
S-Glutathionylation of metallothioneins by nitrosative/oxidative stress
Experimental Gerontology, 2008 Cystein residues within metallothionein (MT) structure have been shown to be particularly prone to S-nitrosylation. The objective of this study was to examine the possibility that MTs undergo S-glutathionylation under nitrosative/oxidative stress. MT from rabbit liver was treated with different concentrations of GSNO, diamide plus GSH or H(2)O(2) plus ...
CASADEI M +4 more
core +7 more sources