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

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

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Main Authors: Kong, Qingzhong, Mills, Jeffrey L., Kundu, Bishwajit, Li, Xinyi, Qing, Liuting, Surewicz, Krystyna, Cali, Ignazio, Huang, Shenghai, Zheng, Mengjie, Swietnicki, Wieslaw, Sönnichsen, Frank D., Gambetti, Pierluigi, Surewicz, Witold K.
格式: Artigo
語言:Inglês
出版: 2013
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Article
在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC3766954/
https://ncbi.nlm.nih.gov/pubmed/23871665
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.celrep.2013.06.030
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