Adult rodents picked up by the tail and slowly descending towards a horizontal surface
extend all four limbs in anticipation of contact. Mouse mutants with pathologies in various …

Soluble oligomers of the amyloid-β (Aβ) peptide cause neurotoxicity, synaptic dysfunction,
and memory impairments that underlie Alzheimer disease (AD). The cellular prion protein …

Amyloid aggregation starts with the initial misfolding of peptide/protein precursors, with
subsequent structural rearrangement into oligomers and protofibrils; the latter eventually …

Research on prions, the infectious agents of devastating neurological diseases in humans
and animals, has been in the forefront of developing the concept of protein aggregation …

The prion hypothesis is strongly supported by the fact that prion infectivity and the
pathogenic conformer of prion protein (PrP) are simultaneously propagated in vitro by the …

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

The structurally disordered N-terminal half of the prion protein (PrP C) is constitutively
released into the extracellular space by an endogenous proteolytic cleavage event. Once …

Protein targeting to specified cellular compartments is essential to maintain cell function and
homeostasis. In eukaryotic cells, two major pathways rely on N‐terminal signal peptides to …

Prion diseases in humans and animals are characterized by progressive neurodegeneration
and the formation of infectious particles called prions. Both features are intimately linked to a …

Prion diseases are fatal transmissible neurodegenerative diseases of various mammalian
species. Central to these conditions is the conversion of the normal host prion protein PrPC …