{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10(4)"],"submitter":["Chen YJ"],"pubmed_abstract":["S-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, is a selective and reversible protein post-translational modification (PTM) that regulates protein activity, localization, and stability. Despite its implication in the regulation of protein functions and cell signaling, the substrate specificity of cysteine S-glutathionylation remains unknown. Based on a total of 1783 experimentally identified S-glutathionylation sites from mouse macrophages, this work presents an informatics investigation on S-glutathionylation sites including structural factors such as the flanking amino acids composition and the accessible surface area (ASA). TwoSampleLogo presents that positively charged amino acids flanking the S-glutathionylated cysteine may influence"],"journal":["PloS one"],"pagination":["e0118752"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4388702"],"repository":["biostudies-literature"],"pubmed_title":["GSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity."],"pmcid":["PMC4388702"],"pubmed_authors":["Huang KY","Lee TY","Chen YJ","Lu CT","Wu HY"],"additional_accession":[]},"is_claimable":false,"name":"GSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity.","description":"S-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, is a selective and reversible protein post-translational modification (PTM) that regulates protein activity, localization, and stability. Despite its implication in the regulation of protein functions and cell signaling, the substrate specificity of cysteine S-glutathionylation remains unknown. Based on a total of 1783 experimentally identified S-glutathionylation sites from mouse macrophages, this work presents an informatics investigation on S-glutathionylation sites including structural factors such as the flanking amino acids composition and the accessible surface area (ASA). TwoSampleLogo presents that positively charged amino acids flanking the S-glutathionylated cysteine may influence","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015","modification":"2025-04-19T02:51:55.884Z","creation":"2019-03-26T23:31:54Z"},"accession":"S-EPMC4388702","cross_references":{"pubmed":["25849935"],"doi":["10.1371/journal.pone.0118752"]}}