Thermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in Vivo

Thermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in Vivo

Prion diseases, or transmissible spongiform encephalopathies (TSEs), are associated with the conformational conversion of the cellular prion protein, PrPC, into a protease-resistant form, PrPSc. Here, we show that mutation-induced thermodynamic stabilization of the folded, α-helical domain of PrPC...

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Bibliographic Details
Main Authors: Qingzhong Kong, Jeffrey L. Mills, Bishwajit Kundu, Xinyi Li, Liuting Qing, Krystyna Surewicz, Ignazio Cali, Shenghai Huang, Mengjie Zheng, Wieslaw Swietnicki, Frank D. Sönnichsen, Pierluigi Gambetti, Witold K. Surewicz
Format: Article
Language:English
Published: Elsevier 2013-07-01
Series:Cell Reports
Online Access:http://www.sciencedirect.com/science/article/pii/S2211124713003227

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http://www.sciencedirect.com/science/article/pii/S2211124713003227

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