Protein S-nitrosylation: purview and parameters.
Publication
, Journal Article
Hess, DT; Matsumoto, A; Kim, S-O; Marshall, HE; Stamler, JS
Published in: Nat Rev Mol Cell Biol
February 2005
S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an important mechanism for dynamic, post-translational regulation of most or all main classes of protein. S-nitrosylation thereby conveys a large part of the ubiquitous influence of nitric oxide (NO) on cellular signal transduction, and provides a mechanism for redox-based physiological regulation.
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Published In
Nat Rev Mol Cell Biol
DOI
ISSN
1471-0072
Publication Date
February 2005
Volume
6
Issue
2
Start / End Page
150 / 166
Location
England
Related Subject Headings
- Sulfhydryl Compounds
- Signal Transduction
- Proteins
- Protein Processing, Post-Translational
- Oxidation-Reduction
- Nitrogen
- Nitric Oxide
- Molecular Sequence Data
- Models, Molecular
- Models, Chemical
Citation
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Chicago
ICMJE
MLA
NLM
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005). Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol, 6(2), 150–166. https://doi.org/10.1038/nrm1569
Hess, Douglas T., Akio Matsumoto, Sung-Oog Kim, Harvey E. Marshall, and Jonathan S. Stamler. “Protein S-nitrosylation: purview and parameters.” Nat Rev Mol Cell Biol 6, no. 2 (February 2005): 150–66. https://doi.org/10.1038/nrm1569.
Hess DT, Matsumoto A, Kim S-O, Marshall HE, Stamler JS. Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol. 2005 Feb;6(2):150–66.
Hess, Douglas T., et al. “Protein S-nitrosylation: purview and parameters.” Nat Rev Mol Cell Biol, vol. 6, no. 2, Feb. 2005, pp. 150–66. Pubmed, doi:10.1038/nrm1569.
Hess DT, Matsumoto A, Kim S-O, Marshall HE, Stamler JS. Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol. 2005 Feb;6(2):150–166.
Published In
Nat Rev Mol Cell Biol
DOI
ISSN
1471-0072
Publication Date
February 2005
Volume
6
Issue
2
Start / End Page
150 / 166
Location
England
Related Subject Headings
- Sulfhydryl Compounds
- Signal Transduction
- Proteins
- Protein Processing, Post-Translational
- Oxidation-Reduction
- Nitrogen
- Nitric Oxide
- Molecular Sequence Data
- Models, Molecular
- Models, Chemical