▪ Abstract Many neurodegenerative diseases, including Alzheimer's and Parkinson's and the
transmissible spongiform encephalopathies (prion diseases), are characterized at autopsy …

There are a group of diseases associated with protein misfolding and accumulation into
amyloid fibers. Many of these diseases have a major impact on human health, in particular …

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

A change of the prion protein conformation results in a class of neurodegenerative diseases
called the transmissible spongiform encephalopathies (like mad cow and Creutzfeld–Jakob …

The prion protein (PrP) is a Cu 2+ binding cell surface glycoprotein that can misfold into a β-
sheet-rich conformation to cause prion diseases. The majority of copper binding studies …

Zoonotic Viruses of Northern Eurasia: Taxonomy and Ecology provides a review of modern
data of the taxonomy, distribution, and ecology of zoonotic viruses in the ecosystems of …

The prion protein (PrP) binds copper and under some conditions copper can facilitate its
folding into a more protease resistant form. Hence, copper levels may influence the …

Transmissible spongiform encephalopathies form a group of fatal neurodegenerative
disorders that have the unique property of being infectious, sporadic or genetic in origin …

Data from cell culture and animal models of prion disease support the separate involvement
of both heparan sulfate proteoglycans and copper (II) ions in prion (PrP) metabolism …

In recent studies, the amyloid fibrils produced in vitro from recombinant prion protein
encompassing residues 89− 230 (rPrP 89− 230) were shown to produce transmissible form …