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In many cases this reversible post\u2010translational modification is accompanied by altered protein function and aberrant <jats:italic>S<\/jats:italic>\u2010nitrosylation of proteins, caused by altered production of NO and\/or impaired SNO homeostasis, has been repeatedly reported in a variety of pathophysiological settings. A growing number of studies are directed to the identification and characterization of those proteins that undergo <jats:italic>S<\/jats:italic>\u2010nitrosylation and the analysis of <jats:italic>S<\/jats:italic>\u2010nitrosoproteomes under pathological conditions is beginning to be reported. The study of these <jats:italic>S<\/jats:italic>\u2010nitrosoproteomes has been fueled by advances in proteomic technologies that are providing researchers with improved tools for exploring this post\u2010translational modification. Here we review novel refinements and improvements to these methods, and some recent studies of the <jats:italic>S<\/jats:italic>\u2010nitrosoproteome in disease. \u00a9 2013 Wiley Periodicals, Inc. 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