Abstract
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 language | English (US) |
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Pages (from-to) | 1541-1551 |
Number of pages | 11 |
Journal | Amino Acids |
Volume | 42 |
Issue number | 5 |
DOIs | |
State | Published - May 2012 |
Keywords
- Identification
- Proteomics
- Quantification
- S-nitrosylation
ASJC Scopus subject areas
- Biochemistry
- Clinical Biochemistry
- Organic Chemistry