Prion propagation involves a conformational transition of the cellular form of prion protein
(PrP C) to a disease-specific isomer (PrP Sc), shifting from a predominantly α-helical …

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 …

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 …

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) …

Prion diseases are associated with the misfolding of the endogenously expressed prion
protein (designated PrP C) into an abnormal isoform (PrP Sc) that has infectious properties …

Structural information regarding normal prion protein (PrP C) and the scrapie isoform (PrP
Sc) is of vital importance for elucidating the pathogenesis of prion diseases (PDs). Despite …

A recombinant protein corresponding to the human prion protein domain encompassing
residues 90–231 (huPrP (90–231)) was expressed in Escherichia coli in a soluble form and …

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 …

The process of prion conversion is not yet well understood at the molecular level. The
regions critical for the conformational change of PrP remain mostly debated and the extent of …