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Highly promiscuous nature of prion polymerization
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Converting the prion protein: What makes the protein infectious
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Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay
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Molecular structure of amyloid fibrils: insights from solid-state NMR
Robert Tycko
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Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation
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Structure of the cross-β spine of amyloid-like fibrils
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Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils
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Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob disease
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In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc
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Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro
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JOURNAL OF MOLECULAR BIOLOGY (2003)
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