The central event in the pathogenesis of prion diseases is a profound conformational
change of the prion protein (PrP) from an α-helical (PrPC) to a β-sheet-rich isoform (PrPSc) …

According to the “protein-only” hypothesis, the critical step in the pathogenesis of prion
diseases is the conformational transition between the normal (PrPC) and pathological …

The conversion of the α-helical, cellular isoform of the prion protein (PrPC) to the insoluble, β-
sheet-rich, infectious, disease-causing isoform (PrPSc) is the fundamental event in the prion …

The conversion of a monomeric α-helix-rich isoform to multimeric β-sheet-rich isoforms is a
prominent feature of the conversion between PrPC and PrPSC. We mimicked this process in …

The self-association of prion protein (PrP) is a critical step in the pathology of prion diseases.
It is increasingly recognized that small non-fibrillar β-sheet-rich oligomers of PrP may be of …

Misfolding of the mammalian prion protein (PrP) is implicated in the pathogenesis of prion
diseases. We analyzed wild type PrP in comparison with different PrP mutants and identified …

Prion diseases are associated with a conformational switch in the prion protein (PrP) from its
normal cellular form (denoted PrPC) to a disease-associated “scrapie” form (PrPSc). A …

Prion propagation is associated with accumulation of a conformational isomer of host
encoded cellular prion protein, PrPC. Solution structures of several mammalian PrPs have …

Individual variations in structure and morphology of amyloid fibrils produced from a single
polypeptide are likely to underlie the molecular origin of prion strains and control the …

Three novel conformational isomers of mouse prion protein mPrP (23− 231) were prepared
by incubating the reduced mPrP (23− 231) in the presence of urea at mild acidic conditions …