Protein misfolding and aggregation are known to play a crucial role in a number of important
human diseases (Alzheimer's, Parkinson's, prion, diabetes, cataracts, etc.) as well as in a …

The key molecular event in the pathogenesis of prion diseases is the conformational
conversion of a cellular prion protein, PrP C, into a misfolded form, PrP Sc. In contrast to PrP …

Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but
structures observed to date have not been definitively correlated with infectivity and the three …

Prion diseases, also known as transmissible spongiform encephalopathies, make up a
group of fatal neurodegenerative disorders linked with the misfolding and aggregation of the …

Seeded polymerisation of proteins forming amyloid fibres and their spread in tissues has
been implicated in the pathogenesis of multiple neurodegenerative diseases: so called …

Methionine/valine polymorphism at position 129 of the human prion protein, huPrP, is tightly
associated with the pathogenic phenotype, disease progress, and age of onset of …

Prion diseases, like Alzheimer's disease and Parkinson disease, are rapidly progressive
neurodegenerative disorders caused by misfolding followed by aggregation and …

Prion diseases are associated with the structural conversion of prion protein (PrP) to a β-
sheet-rich aggregate, PrP Sc. Previous studies have indicated that a reduction of the …

The characterization of the structural dynamics of proteins, including those that present a
substantial degree of disorder, is currently a major scientific challenge. These dynamics are …

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 …