biostudies-literatureUnknown3(12)Zhang XS-Nitros(yl)ation is a ubiquitous redox-based post-translational modification of protein cysteine thiols by nitric oxide or its derivatives, which transduces the bioactivity of nitric oxide (NO) by regulation of protein conformation, activity, stability, localization and protein-protein interactions. These years, more and more S-nitrosated proteins were identified in physiological and pathological processes and the number is still growing. Here we developed a database named SNObase ( http://www.nitrosation.org ), which collected S-nitrosation targets extracted from literatures up to June 1st, 2012. SNObase contained 2561 instances, and provided information about S-nitrosation targets, sites, biological model, related diseases, trends of Protein & cell929-33https://www.ebi.ac.uk/biostudies/studies/S-EPMC4875383biostudies-literatureSNObase, a database for S-nitrosation modification.PMC4875383Qiao XZhang YGuo XZhang XZhang LChen CHuang BZhao YfalseSNObase, a database for S-nitrosation modification.S-Nitros(yl)ation is a ubiquitous redox-based post-translational modification of protein cysteine thiols by nitric oxide or its derivatives, which transduces the bioactivity of nitric oxide (NO) by regulation of protein conformation, activity, stability, localization and protein-protein interactions. These years, more and more S-nitrosated proteins were identified in physiological and pathological processes and the number is still growing. Here we developed a database named SNObase ( http://www.nitrosation.org ), which collected S-nitrosation targets extracted from literatures up to June 1st, 2012. SNObase contained 2561 instances, and provided information about S-nitrosation targets, sites, biological model, related diseases, trends of 2012-01-01T00:00:00Z2012 Dec2025-04-22T06:18:35.498Z2019-03-27T02:14:14ZS-EPMC48753832312922010.1007/s13238-012-2094-6