Journal
TRENDS IN NEUROSCIENCES
Volume 30, Issue 1, Pages 37-45Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tins.2006.11.004
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Funding
- NEI NIH HHS [R01 EY05477, R01 EY09024] Funding Source: Medline
- NICHD NIH HHS [P01 HD29587] Funding Source: Medline
- NINDS NIH HHS [R01 NS046994, R01 NS43242, P30 NS057096] Funding Source: Medline
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [P01HD029587] Funding Source: NIH RePORTER
- NATIONAL EYE INSTITUTE [R01EY005477, R01EY009024] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS043242, P30NS057096, R01NS046994] Funding Source: NIH RePORTER
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The importance of phosphorylation of key threonine, serine and tyrosine residues is a well known essential feature of many signal transduction pathways. A similar, highly conserved redox reaction involving cysteine thiols is now emerging as an important regulator of protein function. An example of this redox regulation is S-nitrosylation (the transfer of a nitric oxide group to a key protein thiol). Here, we review the chemical biology of an additional class of drugs, electrophiles (electrondeficient carbon centers), that react with key protein thiols, and provide insights into a broader class of reactions implicated in redox signaling. Interestingly, certain electrophilic compounds, including endogenous metabolites and natural products, seem to have neuroprotective effects, and this has resulted in the development of neuroprotective electrophilic drugs, including prostaglandin derivatives and hydroquinones, that exert their action through activating antioxidant-signaling cascades.
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