Proline cis/trans isomerization governs protein local conformational changes via its local
mechanical rigidity. The amyloid-disrupting capacity of proline is widely acknowledged; …

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 …

Aggregation-prone proteins often misfold into multiple distinct amyloid conformations that
dictate different physiological impacts. Although amyloid formation is triggered by a transient …

Conformational switching of the prion protein (PrP) from an α-helical normal cellular form
(PrPC) to an aggregation-prone and self-propagating β-rich scrapie form (PrPSc) underlies …

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

Prion protein aggregation into amyloid fibrils is associated with the onset and progression of
prion diseases—a group of neurodegenerative amyloidoses. The process of such aggregate …

Misfolding and aggregation of the prion protein (PrP) are responsible for the development of
fatal transmissible neurodegenerative diseases. PrP undergoes structural conversion from a …

Human prion diseases are neurodegenerative disorders associated to the misfolding of the
prion protein (PrP). Common features of prion disorders are the fibrillar amyloid deposits …

Soluble oligomeric species of the amyloid-β (Aβ) peptide exhibit pronounced neurotoxic
effects in Alzheimer's disease. Recent studies have indicated that the prion protein (PrP) is …

Transmissive spongiform encephalopathies (TSE) are a group of neurodegenerative
diseases caused by infectious protein particles, known as prions. Prions are formed from …