Prion diseases are rapidly progressive, incurable neurodegenerative disorders caused by
misfolded, aggregated proteins known as prions, which are uniquely infectious. Remarkably …

Prion diseases are a group of inevitably fatal neurodegenerative disorders affecting
numerous mammalian species, including humans. The existence of heritable phenotypes of …

Tau aggregation underlies neurodegenerative tauopathies, and transcellular propagation of
tau assemblies of unique structure, ie, strains, may underlie the diversity of these disorders …

Prions, which cause fatal neurodegenerative disorders such as Creutzfeldt‐Jakob disease,
are misfolded and infectious protein aggregates. Currently, there are no treatments available …

Protein misfolding results in devastating degenerative diseases and cancer. Among the
culprits involved in these illnesses are prions and prion-like proteins, which can propagate …

Prion diseases affect a wide range of mammal species and are caused by a misfolded self-
propagating isoform (PrPSc) of the normal prion protein (PrPC). Distinct strains of prions …

Prions induce a fatal neurodegenerative disease in infected host brain based on the
refolding and aggregation of the host-encoded prion protein PrPC into PrPSc. Structurally …

Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a
group of fatal neurodegenerative disorders affecting humans and other mammalian species …

The prion protein is a multifunctional protein that exists in at least two different folding states.
It is subject to diverse proteolytic processing steps that lead to prion protein fragments some …

Recent studies have proposed that nucleic acids act as potential cofactors for protein
aggregation and prionogenesis. By means of sedimentation, transmission electron …