Understanding the structure of PrPSc and its strain variation has been one of the major
challenges in prion disease biology. To study the strain-dependent conformations of PrPSc …

The scrapie prion protein (PrPSc) is formed from the cellular isoform (PrPC) by a post-
translational process that involves a profound conformational change. Linear epitopes for …

Prions are composed solely of the pathological isoform (PrP Sc) of the normal cellular prion
protein (PrP C). Identification of different PrP Sc structures is crucially important for …

Prion diseases are associated with accumulation of strain-dependent biochemically distinct,
disease-related isoforms (PrPSc) of host-encoded prion protein (PrPC). PrPSc is …

Native mammalian prions exist in self-propagating strains that exhibit distinctive clinical,
pathological and biochemical characteristics. Prion strain diversity is associated with …

The scrapie prion protein (PrPSc) is derived from a cellular isoform (PrPC) that acquires
protease resistance posttranslationally. We have used several different experimental …

Mammalian prion diseases involve conversion of normal prion protein, PrPC, to a
pathological aggregated state (PrPres). The three-dimensional structure of PrPres is not …

Although the protein-only hypothesis proposes that it is the conformation of abnormal prion
protein (PrPSc) that determines strain diversity, the molecular basis of strains remains to be …

The scrapie prion protein (PrPSc) is the major, and possibly the only, component of the
infectious prion; it is generated from the cellular isoform (PrPC) by a conformational change …

Prion diseases are associated with the conversion of the α-helix rich prion protein (PrPC)
into a β-structure-rich insoluble conformer (PrPSc) that is thought to be infectious. The …