Development and application of site-specific proteomic approach for study protein S-nitrosylation

Miao Liu, James E. Talmadge, Shi Jian Ding

Research output: Contribution to journalReview articlepeer-review

7 Scopus citations


Protein S-nitrosylation is the covalent redoxrelated modification of cysteine sulfhydryl groups with nitric oxide, creating a regulatory impact similar to phosphorylation. Recent studies have reported a growing number of proteins to be S-nitrosylated in vivo resulting in altered functions. These studies support S-nitrosylation as a critical regulatory mechanism, fine-tuning protein activities within diverse cellular processes and biochemical pathways. In addition, S-nitrosylation appears to have key roles in the etiology of a broad range of human diseases. In this review, we discuss recent advances in proteomic approaches for the enrichment, identification, and quantitation of cysteine S-nitrosylated proteins and peptides. These advances have provided analytical tools with the power to interpret the impact of S-nitrosylation at the system level, providing a new platform for drug discovery and the identification of diagnostic markers for human diseases.

Original languageEnglish (US)
Pages (from-to)1541-1551
Number of pages11
JournalAmino Acids
Issue number5
StatePublished - May 2012


  • Identification
  • Proteomics
  • Quantification
  • S-nitrosylation

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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