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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 methods have been rapidly developed to study S-glutathionylation, thus expanding the dataset of experimentally determined glutathionylation sites.
(Chen et al., 2014) dbGSH: a database of S-glutathionylation. Bioinformatics.