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…
RedoxDB
Data

RedoxDB

Provides information about protein oxidative modification verified by…

Provides information about protein oxidative modification verified by experimental studies. For each modified cysteine, the exact position, modification type and flanking sequence are provided.…

GSHSite
Web

GSHSite

A web server for identifying S-glutathionylation sites. GSHSite is based on a…

A web server for identifying S-glutathionylation sites. GSHSite is based on a statistical method for identifying S-glutathionylation sites and potential consensus motifs by maximal dependence…

dbGSH
Data

dbGSH

A public resource to allow efficient access to experimentally validated…

A public resource to allow efficient access to experimentally validated S-glutathionylation sites and comprehensive bioinformatics analyses, including functional annotations, structural…

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