Screening systems for the identification of S-nitrosylated proteins

被引:7
|
作者
Uehara, Takashi [1 ]
Nishiya, Tadashi [2 ]
机构
[1] Okayama Univ, Dept Med Pharmacol, Grad Sch Med Dent & Pharmaceut Sci, Okayama 7008530, Japan
[2] Hokkaido Univ, Dept Cellular Pharmacol, Grad Sch Med, Sapporo, Hokkaido 0600812, Japan
来源
NITRIC OXIDE-BIOLOGY AND CHEMISTRY | 2011年 / 25卷 / 02期
关键词
S-Nitrosylation; Nitric oxide; Screening; NITRIC-OXIDE; PROTEOMIC ANALYSIS; SITES; DENITROSYLATION; MECHANISM; KINASE;
D O I
10.1016/j.niox.2010.11.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
S-Nitrosylation is a well-characterized reaction involving the covalent binding of nitric oxide (NO) to cysteine residues (Cys) in a protein. Similar to protein phosphorylation, S-nitrosylation is a post-translational modification involved in the regulation of a large number of intracellular functions and signaling events. Moreover, like phosphorylation, S-nitrosylation is precisely regulated in time and space. A procedure known as the biotin-switch method that specifically detects S-nitrosylated proteins (SNO-P) was recently developed by Snyder's group. They found that many proteins are substrates for NO, and several groups have attempted to identify other SNO-P by improving this method. In this review, we describe the SNO-P identified using modified versions of the biotin-switch method. (C) 2010 Elsevier Inc. All rights reserved.
引用
收藏
页码:108 / 111
页数:4
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