Detection of protein S-nitrosylation with the biotin-switch technique |
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Authors: | Forrester Michael T Foster Matthew W Benhar Moran Stamler Jonathan S |
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Institution: | Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA. |
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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. |
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