The aggregation and accumulation of amyloidogenic peptides and proteins are observed as
pathological features in the brains of patients suffering from neurodegenerative disorders …

Conformational conversion of the α-helix-rich cellular prion protein into the misfolded, β-rich,
aggregated, scrapie form underlies the molecular basis of prion diseases that represent a …

Two normally occurring polymorphisms of the human PRNP gene, methionine (M)/valine (V)
at codon 129 and glutamic acid (E)/lysine (K) at codon 219, can affect the susceptibility to …

Loss of pancreatic β-cell mass is deleterious for type 2 diabetes patients since it reduces
insulin production, critical for glucose homeostasis. The main research axis developed over …

The spontaneous aggregation of infectious or misfolded forms of prion protein is known to
be responsible for neurotoxicity in brain cells, which ultimately leads to the progression of …

Prion diseases are caused by the propagation of misfolded cellular prion proteins (PrPs). A
completely prion disease-resistant genotype, V127M129, has been identified in Papua New …

Breeding programmes to promote resistance to classical scrapie, similar to those for sheep
in existing transmissible spongiform encephalopathies (TSE) regulations, have not been …

The cellular prion protein (PrPC) is a mainly α-helical 208-residue protein located in the pre-
and postsynaptic membranes. For unknown reasons, PrPC can undergo a structural …

The accumulation of abnormal prion protein (PrP Sc) converted from the normal cellular
isoform of PrP (PrP C) is assumed to induce pathogenesis in prion diseases. Therefore, drug …

The large chronic wasting disease (CWD)-affected cervid population in the USA and
Canada, and the risk of the disease being transmitted to humans through intermediate …