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Expert Rev Proteomics. 2012;9(1):59-69. doi: 10.1586/epr.11.74.

Proteomics insights into deregulated protein S-nitrosylation and disease.

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Cell Biology Department, Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), Hospital Reina Sofía, Universidad de Córdoba, Spain.


Nitric oxide (NO) can modulate cell function by the coupling of a nitroso moiety to a reactive cysteine in target proteins leading to the formation of a S-nitrosothiol (SNO), a process commonly known as S-nitrosylation. Aberrant S-nitrosylation of proteins, caused by altered production of NO and/or impaired SNO homeostasis, constitutes a mechanism that has been recently postulated in numerous pathophysiological settings. The thiol microenvironment, cellular redox environment, and activity of transnitrosylases and denitrosylases have been proposed as determinant factors for the specificity of S-nitrosylation. A number of methodological approaches have recently been developed for the proteomic identification of S-nitrosylated proteins and/or the identification of specific sites of nitrosylation. This review will consider novel aspects of SNO homeostasis and S-nitrosylation, the latest proteomic methods for the identification of S-nitrosylated cysteines in proteins, and how these novel technologies will impact our current knowledge of the role of deregulated S-nitrosylation in disease.

[Indexed for MEDLINE]

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