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Citation
Tags
HERO ID
196218
Reference Type
Journal Article
Subtype
Review
Title
Protein S-nitrosylation: Purview and parameters
Author(s)
Hess, DT; Matsumoto, A; Kim, SO; Marshall, HE; Stamler, JS
Year
2005
Is Peer Reviewed?
1
Journal
Nature Reviews. Molecular Cell Biology
ISSN:
1471-0072
EISSN:
1471-0080
Volume
6
Issue
2
Page Numbers
150-166
Language
English
PMID
15688001
DOI
10.1038/nrm1569
Web of Science Id
WOS:000226720500014
Abstract
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.
Tags
IRIS
•
Formaldehyde
Cited in text
Retroactive RIS import
Pre2013
Formaldehyde IRIS 2011
Old references
•
Methanol (Non-Cancer)
Cited in Final (2013)
Cited in External Review Draft (2013)
Cited in External Review Draft (2011)
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