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United States Department of Agriculture

Agricultural Research Service


item Nicholson, Eric
item Greenlee, Justin
item Richt, Juergen
item Hamir, Amirali
item Kunkle, Robert
item Kehrli Jr, Marcus

Submitted to: Association of Analytical Communities International Midwest Section
Publication Type: Abstract Only
Publication Acceptance Date: 4/9/2005
Publication Date: 5/24/2005
Citation: Nicholson, E.M., Greenlee, J.J., Richt, J., Hamir, A.N., Kunkle, R.A., Kehrli, Jr., M.E. 2005. Biochemistry of prion diseases. Association of Analytical Communities International, Midwest Section [abstract]. Abstract No. 601. p. 38.

Interpretive Summary:

Technical Abstract: The nucleation-polymerization and template assistance models for conversion of the normal cellular form of the prion protein, PrP**C, to the disease associated, protease resistant conformation, PrP**d, will be discussed. Attention will be paid to a recent model of PrP**d fibril structure, the implications such a conformation has on the inactivation of prion infectivity, and the methods to detect inactivation.

Last Modified: 09/25/2017
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