Screening systems for the identification of S-nitrosylated proteins

Takashi Uehara, Tadashi Nishiya

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)108-111
Number of pages4
JournalNitric Oxide - Biology and Chemistry
Volume25
Issue number2
DOIs
Publication statusPublished - Aug 1 2011

Keywords

  • Nitric oxide
  • S-Nitrosylation
  • Screening

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Clinical Biochemistry
  • Cancer Research

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