The structural transition of the prion protein from α-helical-to β-sheet-rich underlies its
conversion into infectious and disease-associated isoforms. Here we describe the crystal …

Misfolding and aggregation of the prion protein is responsible for multiple
neurodegenerative diseases. Works from several laboratories on folding of both the WT and …

A molecular understanding of prion diseases requires an understanding of the mechanism
of amyloid fibril formation by the prion protein. In particular, it is necessary to define the …

The conformational transition of the human prion protein from an α-helical to a β-sheet-rich
structure is believed to be the critical event in prion pathogenesis. The molecular …

Transmissible spongiform encephalopathies (TSEs) represent a group of fatal
neurodegenerative diseases that are associated with conformational conversion of the …

It has been well established that a single amino acid sequence can give rise to several
conformationally distinct amyloid states. The extent to which amyloid structures formed …

Understanding how structure develops during the course of amyloid fibril formation by the
prion protein is important for understanding prion diseases. Determining how conformational …

Protein conformational transition from α-helices to β-sheets precedes aggregation of
proteins implicated in many diseases, including Alzheimer and prion diseases. Direct …

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 key event in prion diseases. In …

Neurodegenerative diseases associated with the human prion protein are characterized by
structural rearrangement in the domains of the benign monomeric form of the prion protein …