Quantification of cysteinyl S-nitrosylation by fluorescence in unbiased proteomic studies.

@article{Wiktorowicz2011QuantificationOC,
  title={Quantification of cysteinyl S-nitrosylation by fluorescence in unbiased proteomic studies.},
  author={John E. Wiktorowicz and Susan J. Stafford and Harriett C. Rea and Petri Urvil and Kizhake V. Soman and Alexander Kurosky and J. Regino Perez-polo and Tor C. Savidge},
  journal={Biochemistry},
  year={2011},
  volume={50 25},
  pages={
          5601-14
        }
}
Cysteinyl S-nitrosylation has emerged as an important post-translational modification affecting protein function in health and disease. Great emphasis has been placed on global, unbiased quantification of S-nitrosylated proteins because of physiologic and oxidative stimuli. However, current strategies have been hampered by sample loss and altered protein electrophoretic mobility. Here, we describe a novel quantitative approach that uses accurate, sensitive fluorescence modification of cysteine… 

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