Steele, Andrew D. (2008) All quiet on the neuronal front: NMDA receptor inhibition by prion protein. Journal of Cell Biology, 181 (3). pp. 407-409. ISSN 0021-9525. PMCID PMC2364702. doi:10.1083/jcb.200803152. https://resolver.caltech.edu/CaltechAUTHORS:STEjcb08
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Abstract
The normal function of the prion protein (PrP)—the causative agent of mad cow or prion disease—has long remained out of reach. Deciphering PrP's function may help to unravel the complex chain of events triggered by PrP misfolding during prion disease. In this issue of the JCB, an exciting paper (Khosravani, H., Y. Zhang, S. Tsutsui, S. Hameed, C. Altier, J. Hamid, L. Chen, M. Villemaire, Z. Ali, F.R. Jirik, and G.W. Zamponi. 2008. J. Cell Biol. 181:551–565) connects diverse observations regarding PrP into a coherent framework whereby PrP dampens the activity of an N-methyl-D-aspartate (NMDA) receptor (NMDAR) subtype and reduces excitotoxic lesions. The findings of this study suggest that understanding the normal function of proteins associated with neurodegenerative disease may elucidate the molecular pathogenesis.
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| Additional Information: | © 2008 Steele. Submitted: 27 March 2008; Accepted: 1 April 2008. Published online April 28, 2008; doi:10.1083/jcb.200803152. A.D. Steele is supported by the Broad Fellows in Brain Circuitry program at the California Institute of Technology. | |||||||||
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| Issue or Number: | 3 | |||||||||
| PubMed Central ID: | PMC2364702 | |||||||||
| DOI: | 10.1083/jcb.200803152 | |||||||||
| Record Number: | CaltechAUTHORS:STEjcb08 | |||||||||
| Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:STEjcb08 | |||||||||
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | |||||||||
| ID Code: | 10514 | |||||||||
| Collection: | CaltechAUTHORS | |||||||||
| Deposited By: | Archive Administrator | |||||||||
| Deposited On: | 13 May 2008 | |||||||||
| Last Modified: | 08 Nov 2021 21:08 |
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