The brain is a singular organ of unique biological complexity that serves as the command
center for cognitive and motor function. As such, this specialized system also possesses a …

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 composed of an isoform of a normal sialoglycoprotein called PrP c, whose
physiological role has been under investigation, with focus on the screening for ligands. Our …

To test for a role for the cellular prion protein (PrP c) in cell death, we used a PrP c-binding
peptide. Retinal explants from neonatal rats or mice were kept in vitro for 24 h, and …

The fundamental physiological function of native cellular prion (PrPC) remains unknown.
Herein, the most salient observations as regards prion physiology are critically evaluated …

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 …

The cellular prion protein (PrPC) is essential for the pathogenesis and transmission of prion
diseases. Although PrPC is known to be located in detergent-insoluble lipid rafts at the …

PrPC (cellular prion protein) is located at the surface of neuronal cells in detergent-insoluble
lipid rafts, yet is internalized by clathrin-dependent endocytosis. As PrPC is glycosyl …