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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Autores principales: 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.
Formato: Artigo
Lenguaje:Inglês
Publicado: 2013
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Article
Acceso en línea: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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