Proteomic analysis of protein S-nitrosylation

Federico Torta, Vera Usuelli, Antonio Malgaroli, Angela Bachi

Research output: Contribution to journalArticlepeer-review

Abstract

Nitric oxide (NO) produces covalent PTMs of specific cysteine residues, a process known as S-nitrosylation. This route is dynamically regulated and is one of the major NO signalling pathways known to have strong and dynamic interactions with redox signalling. In agreement with this scenario, binding of NO to key cysteine groups can be linked to a broad range of physiological and pathological cellular events, such as smooth muscle relaxation, neurotransmission and neurodegeneration. The characterization of S-nitrosylated residues and the functional relevance of this protein modification are both essential information needed to understand the action of NO in living organisms. In this review, we focus on recent advances in this field and on state-of-the-art proteomic approaches which are aimed at characterizing the S-nitrosylome in different biological backgrounds.

Original languageEnglish
Pages (from-to)4484-4494
Number of pages11
JournalProteomics
Volume8
Issue number21
DOIs
Publication statusPublished - Nov 2008

Keywords

  • Cellular signalling
  • Nitric oxide
  • Posttranslational modifications
  • S-nitrosylation

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

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