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- W2074668880 abstract "The prion diseases, including Creutzfeldt–Jakob disease (CJD) and Gerstmann–Straussler–Scheinker disease (GSS) in humans, and bovine spongiform encephalopathy (BSE) in cattle, can exhibit inherited, infectious and sporadic presentations. Moreover, inherited forms of these diseases can be infectious. Obviously, infectious diseases imply an exogenous exposure to a pathogen, whereas inherited diseases are associated with alterations to genomic DNA. To unify these apparently conflicting observations, Prusiner proposed that an endogenous prion protein was the infectious agent, and that mutated forms of this protein were responsible for inherited diseases. Subsequent work has identified the genomic sequence of the prion protein, the nature of the mutations associated with inherited disease, and the conformational distinction between the normal cellular isoform of the prion protein (PrPC) and its disease causing counterpart (PrPSc) (Reviewed in 1 Cohen F.E. Prusiner S.B. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 1998; 67: 793-819 Crossref PubMed Scopus (472) Google Scholar )." @default.
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- W2074668880 date "2000-07-01" @default.
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- W2074668880 title "Prions, peptides and protein misfolding" @default.
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- W2074668880 doi "https://doi.org/10.1016/s1357-4310(00)01740-8" @default.
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