@inbook{3ec97af982314350bbf86d637031776a,
title = "Protein Cysteinyl-S-Nitrosylation: Analysis and Quantification",
abstract = "The thiol moiety of cysteine residues can undergo a number of biologic modifications including oxidation, sulfenylation, nitrosylation, persulfidation, metalation, and other modifications. These modifications can control biological function, including gain as well as loss of function. Herein, we focus attention on the proteomic analysis of S-nitrosylation in health and disease. We describe a novel quantitative approach that combines accurate, sensitive fluorescence modification of cysteinyl-S-nitrosylation that leaves electrophoretic mobility unaffected (SNOFlo), and introduce unique concepts for measuring changes in S-nitrosylation status relative to protein abundance. We present several studies where suitability of this approach for investigating endogenous S-nitrosylation is addressed.",
keywords = "BODIPY Fl-maleimide, Cysteinyl-S-nitrosylation, Proteome",
author = "Wiktorowicz, {J. E.} and Stafford, {S. J.} and Garg, {N. J.}",
note = "Publisher Copyright: {\textcopyright} 2017 Elsevier Inc.",
year = "2017",
doi = "10.1016/bs.mie.2016.10.016",
language = "English (US)",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "1--14",
booktitle = "Methods in Enzymology",
}