The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Detection of protein S-nitrosylation with the biotin-switch technique
Open accessAbstract
Protein S-nitrosylation, the post-translational 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 the current 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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Cites
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InfluentialProtein S-nitrosylation: Purview and parameters
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Cited by
Protein S-nitrosylation in health and disease: a current perspective
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The chemical biology of S-nitrosothiols
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Frungillo, L., Skelly, M. J., Loake, G. J., Spoel, S. H., & Salgado, I. (2014) · Nature Communications · doi:10.1038/ncomms6401 · Cited by 256
Metadata
- Authors
- Forrester, M. T., Foster, M. W., Benhar, M., & Stamler, J. S.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 46
- Issue
- 2
- Pages
- 119-126
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2032672255
- Cited by
- 298
- References
- 13
- FWCI
- 5.21
- Type
- journal article
- Language
- en
- Open access
- green
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