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Published online April 28, 2008
doi:10.1083/jcb.200803152
The Journal of Cell Biology, Vol. 181, No. 3, 407-409
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Steele
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 All quiet on the neuronal front: NMDA receptor inhibition by prion protein

Andrew D. Steele

Division of Biology, California Institute of Technology, Pasadena, CA 91125

Correspondence to Andrew D. Steele: andydsteele{at}alum.mit.edu

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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Related Article

Prion protein attenuates excitotoxicity by inhibiting NMDA receptors
Houman Khosravani, Yunfeng Zhang, Shigeki Tsutsui, Shahid Hameed, Christophe Altier, Jawed Hamid, Lina Chen, Michelle Villemaire, Zenobia Ali, Frank R. Jirik, and Gerald W. Zamponi
J. Cell Biol. 2008 181: 551-565. [Abstract] [Full Text] [PDF]



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