Neurodegenerative diseases constitute a set of pathological conditions originating from the
slow, irreversible, and systematic cell loss within the various regions of the brain and/or the …

J. Neurochem.(2012) 120, 853–868. Abstract The physiological function of the prion protein
(PrPC) and its conversion into its infectious form (PrPSc) are central issues to understanding …

We report the results of solid state nuclear magnetic resonance (NMR) measurements on
amyloid fibrils formed by the full-length prion protein PrP (residues 23− 231, Syrian hamster …

Protein misfolding cyclic amplification (PMCA) provides faithful replication of mammalian
prions in vitro and has numerous applications in prion research. However, the low efficiency …

In Alzheimer's disease (AD), soluble amyloid-β oligomers (AβOs) trigger neurotoxic
signaling, at least partially, via the cellular prion protein (PrPC). However, it is unknown …

Posttranslational modifications are a common feature of proteins associated with
neurodegenerative diseases including prion protein (PrPC), tau, and α-synuclein …

The presence of partially structured helices in natively unfolded amyloid-β42 (Aβ42) and α-
synuclein (αS) has been shown to accelerate fibrillation in the onset of Alzheimer's and …

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 …

A key structural component of amyloid fibrils is a highly ordered, crystalline-like cross-β-
sheet core. Conformationally different amyloid structures can be formed within the same …

Prion diseases are infectious and belong to the group of protein misfolding
neurodegenerative diseases. In these diseases, neuronal dysfunction and death are caused …