Protein S-nitrosylation: purview and parameters

Nat Rev Mol Cell Biol. 2005 Feb;6(2):150-66. doi: 10.1038/nrm1569.

Abstract

S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an important mechanism for dynamic, post-translational regulation of most or all main classes of protein. S-nitrosylation thereby conveys a large part of the ubiquitous influence of nitric oxide (NO) on cellular signal transduction, and provides a mechanism for redox-based physiological regulation.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Membrane / metabolism
  • Cysteine / chemistry
  • GTP Phosphohydrolases / metabolism
  • Humans
  • Models, Biological
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Nitric Oxide / metabolism
  • Nitrogen / chemistry*
  • Oxidation-Reduction
  • Protein Processing, Post-Translational
  • Proteins / chemistry*
  • Signal Transduction
  • Sulfhydryl Compounds / chemistry

Substances

  • Proteins
  • Sulfhydryl Compounds
  • Nitric Oxide
  • GTP Phosphohydrolases
  • Cysteine
  • Nitrogen