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All quiet on the neuronal front: NMDA receptor inhibition by prion protein

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. http://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.


Item Type:Article
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.
Record Number:CaltechAUTHORS:STEjcb08
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:STEjcb08
Alternative URL:http://dx.doi.org/10.1083/jcb.200803152
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:26 Dec 2012 10:01

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