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Unraveling the S ‐nitrosoproteome: Tools and strategies
Author(s) -
LópezSánchez Laura M.,
Muntané Jordi,
de la Mata Manuel,
RodríguezAriza Antonio
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800546
Subject(s) - proteome , nitrosation , lability , computational biology , proteomics , subcellular localization , chemistry , biochemistry , biology , cytoplasm , gene
Abstract One of the major tasks to be accomplished in the postgenomic era is the characterization of PTMs in proteins. The S ‐nitrosation of protein thiols is a redox‐based PTM that modulating enzymatic activity, subcellular localization, complex formation, and degradation of proteins, largely contributes to the complexity of cellular proteomes. Although the detection of S ‐nitrosated proteins is problematical due to the lability of S ‐nitrosothiols, with the improvement of molecular tools an increasing range of proteins has been shown to undergo S ‐nitrosation. We here review recent proteomic approaches for the systematic assessment of potential targets for protein S ‐nitrosation. The development of new analytical methods and strategies over the past several years now allows us to investigate the nitrosoproteome on a global scale.