Cellular prion protein (PrPC) is a glycosylphosphatidylinositol (GPI)-anchored protein most
abundantly found in the outer membrane of neurons. Due to structural characteristics (a …

Proteolytic processing of the cellular and disease-associated form of the prion protein leads
to generation of bioactive soluble prion protein fragments and modifies the structure and …

A variety of physiological functions, not only restricted to the nervous system, are discussed
for the cellular prion protein (PrP C). A prominent, non-physiological property of PrPC is the …

The prion protein (PrP C) is subjected to several conserved endoproteolytic events
producing bioactive fragments that are of increasing interest for their physiological functions …

Brain iron-dyshomeostasis is an important cause of neurotoxicity in prion disorders, a group
of neurodegenerative conditions associated with the conversion of prion protein (PrP C) …

The cellular form of the prion protein, PrPC, undergoes extensive proteolysis at the α site
(109K↓ H110). Expression of non-cleavable PrPC mutants in transgenic mice correlates …

An increasing number of scrapie cases with atypical characteristics, designated Nor98, have
recently been recognized. Here, the proteinase K (PK)-resistant prion protein (PrP) …

The prion protein (PrP) sequence of European moose, reindeer, roe deer and fallow deer in
Scandinavia has high homology to the PrP sequence of North American cervids. Variants in …

The cellular prion protein (PrPC) is attached to the cell membrane via its
glycosylphosphatidylinositol (GPI)-anchor and is constitutively shed into the extracellular …

The cellular prion protein (PrPc) is a glycosyl‐phosphatidylinositol (GPI)‐anchored protein
trafficking in the secretory and endocytic pathway and localized mainly at the plasma …