The prion glycoprotein (PrPC) is mostly located at the cell surface, tethered to the plasma
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …

Prion diseases, also known as transmissible spongiform encephalopathies, make up a
group of fatal neurodegenerative disorders linked with the misfolding and aggregation of the …

Protein phase separation by low-complexity, intrinsically disordered domains generates
membraneless organelles and links to neurodegeneration. Cellular prion protein (PrP C) …

Prions are fatal neurodegenerative transmissible agents causing several incurable illnesses
in humans and animals. Prion diseases are caused by the structural conversion of the …

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 …

A molecular understanding of the prion diseases requires delineation of the origin of
misfolding of the prion protein (PrP). An understanding of how different disease‐linked …

The prion protein (PrPC) is highly expressed within the nervous system. Similar to other GPI-
anchored proteins, PrPC is found in lipid rafts, membrane domains enriched in cholesterol …

The misfolding of the prion protein (PrP) to aggregated forms is linked to several
neurodegenerative diseases. Misfolded oligomeric forms of PrP are associated with …

The post-translational conversion of the ubiquitously expressed cellular form of the prion
protein, PrPC, into its misfolded and pathogenic isoform, known as prion or PrPSc, plays a …

Although prions are known as protein-only infectious particles, they exhibit lipid specificities,
cofactor dependencies and membrane-dependent activities. Such membrane interactions …