A crucial step for transformation of the normal cellular isoform of the prion protein (PrPC) to
the infectious prion protein (PrPSc) is thought to entail a previously uncharacterized …

PrPSc is known to be the major, if not the only, component of the infectious prion. Limited
proteolysis of PrPSc produces an N-terminally truncated polypeptide of about 142 residues …

The infectious agents of prion diseases are composed primarily of an infectious protein
designated PrP Sc. In cells infected with prions, a host glycoprotein termed PrP C undergoes …

The conversion of prion helix 1 from an α-helical into an extended conformation is generally
assumed to be an essential step in the conversion of the cellular isoform PrP C of the prion …

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 prion protein (PrP) in a living cell is associated with cellular membranes. However, all
previous biophysical studies with the recombinant prion protein have been performed in an …

Prion diseases are assumed to be caused by the infectious isoform, PrPSc, of a single
cellular surface protein, PrPC. PrPScis an insoluble form of PrPCand is believed to possess …

Revised Manuscript Received January 11, 1995® abstract: The structures of synthetic
peptides corresponding to regions of putative secondarystructure in the cellular prion protein …

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