Standard Article

S-nitrosylation and thiolation

Part 3. Proteomics

3.5. Proteome Diversity

Short Specialist Review

  1. Yunfei Huang,
  2. Solomon H. Snyder

Published Online: 15 APR 2005

DOI: 10.1002/047001153X.g305319

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

How to Cite

Huang, Y. and Snyder, S. H. 2005. S-nitrosylation and thiolation. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics. 3:3.5:68.

Author Information

  1. Johns Hopkins University, Baltimore, MD, USA

Publication History

  1. Published Online: 15 APR 2005

Abstract

Cysteine, one of the most reactive residues, is indispensable to the biological functions of many proteins. It constitutes the reactive centers of crucial enzymes and maintains protein confirmation of key cellular regulators. The posttranslational modifications of reactive cysteine residues, S-nitrosylation and thiolation, have now emerged as evolutionally conserved fundamental cell signals in all species.

Keywords:

  • S-nitrosylation;
  • thiolation;
  • nitric oxide;
  • redox signaling;
  • posttranslational modification