| Literature DB >> 18977293 |
Michael T Forrester1, Matthew W Foster, Moran Benhar, Jonathan S Stamler.
Abstract
Protein S-nitrosylation, the posttranslational modification of cysteine thiols to form S-nitrosothiols, is a principle mechanism of nitric oxide-based signaling. Studies have demonstrated myriad roles for S-nitrosylation in organisms from bacteria to humans, and recent efforts have greatly advanced our scientific understanding of how this redox-based modification is dynamically regulated during physiological and pathophysiological conditions. The focus of this review is the biotin-switch technique (BST), which has become a mainstay assay for detecting S-nitrosylated proteins in complex biological systems. Potential pitfalls and modern adaptations of the BST are discussed, as are future directions for this assay in the burgeoning field of protein S-nitrosylation.Entities:
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Year: 2008 PMID: 18977293 PMCID: PMC3120222 DOI: 10.1016/j.freeradbiomed.2008.09.034
Source DB: PubMed Journal: Free Radic Biol Med ISSN: 0891-5849 Impact factor: 7.376