The prion protein, PrPC, is a small, cell-surface glycoprotein notable primarily for its critical
role in pathogenesis of the neurodegenerative disorders known as prion diseases. A …

Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to
conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer …

Prions are the causative agent of the transmissible spongiform encephalopathies, such as
Creutzfeldt-Jakob disease in humans. In these prion diseases the normal cellular form of the …

The mode of internalization of glycosylphosphatidylinositol‐anchored proteins, lacking any
cytoplasmic domain by which to engage adaptors to recruit them into coated pits, is …

In Trypanosoma brucei, the plasma membrane is dominated by glycosylphosphatidylinositol
(GPI)‐anchored proteins. Endocytic activity correlates with expression levels of the clathrin …

Dementia with Lewy bodies (DLB), Parkinson's disease (PD) and multiple system atrophy
are characterized by the deposition of disease-associated α-synuclein. In the present study …

The normal function of prion protein (PrP) is usually disregarded at the expense of the more
fascinating role of PrP in transmissible prion diseases. However, the normal PrP may play …

Prion diseases are fatal, neurodegenerative disorders in humans and animals and are
characterized by the accumulation of an abnormally folded isoform of the cellular prion …

Cell biological studies of PrP have contributed enormously to our understanding of prion
diseases. Like other membrane proteins, PrPC is post-translationally processed in the …

Prions are defined as infectious agents that comprise only proteins and are responsible for
transmissible spongiform encephalopathies (TSEs)–fatal neurodegenerative diseases that …