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NMR characterization of the pH 4 β-intermediate of the prion protein:: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility
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Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4
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Elongated oligomers assemble into mammalian PrP amyloid fibrils
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Protein conformation significantly influences immune responses to prion protein
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FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
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The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC
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DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid
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