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S-glutathionylation in protein redox regulation
Free Radical Biology and Medicine, 2007Protein 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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Determination of site-specificity of S-glutathionylated cellular proteins
Biochemical and Biophysical Research Communications, 2005Redox modification by S-glutathionylation is an expanding field within cell signalling research. However, the methods available for analysis of S-glutathionylated proteins in complex mixtures are not sufficiently accurate to specifically and in a high-throughput manner on a structural level establish the effects of S-glutathionylation on the individual
Ylva, Hamnell-Pamment +4 more
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Catalase and estradiol inhibit mitochondrial protein S-glutathionylation
Molecular and Cellular Biochemistry, 2012Regulation and downstream effects of mitochondrial protein S-glutathionylation in response to oxidative stress are poorly understood. The study aim was to determine whether anti-oxidants such as catalase and estradiol alter mitochondrial protein S-glutathionylation and in turn affect apoptosis following ultraviolet B (UV-B) light irradiation.
Bin, Hu +4 more
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Protein Glutathionylation in Cardiovascular Diseases
International Journal of Molecular Sciences, 2013 The perturbation of thiol-disulfide homeostasis is an important consequence of many diseases, with redox signals implicated in several physio-pathological processes.
Anna Pastore +2 more
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Detection of S-glutathionylated proteins by glutathione S-transferase overlay
Archives of Biochemistry and Biophysics, 2005Oxidative and nitrosative stress lead to the S-glutathionylation of proteins and subsequent functional impairment. Glutathione S-transferase (GST) from Schistosoma japonicum was found to bind to the glutathione moiety of S-glutathionylated proteins, thus establishing a convenient method for detecting S-glutathionylated proteins by biotinylated GST ...
Guang, Cheng +3 more
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Protein S-glutathionylation correlates to selective stress gene expression and cytoprotection
Archives of Biochemistry and Biophysics, 2002During situations of oxidative stress phenotypic adaptation to altered redox state is achieved by changes in expression of selected genes. The mechanisms regulating this may involve reversible S-glutathionylation of cellular proteins. In this study we compared and contrasted changes in gene expression patterns in human type II lung epithelial A549 ...
Tiziana, Dandrea +3 more
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