The prion (infectious protein) concept has evolved with the discovery of new self-
propagating protein states in organisms as diverse as mammals and fungi. The infectious …

Prions, the infectious agents of transmissible spongiform encephalopathies (TSEs), have
defied full characterization for decades. The dogma has been that prions lack nucleic acids …

The conformational change of a host protein, PrPC, into a disease-associated isoform,
PrPSc, appears to play a critical role in the pathogenesis of prion diseases such as …

Prions are thought to consist mainly or entirely of misfolded PrP, a constitutively expressed
host protein. Prions associated with the same PrP sequence may occur in the form of …

The “protein only” hypothesis holds that the infectious agent causing transmissible
spongiform encephalopathies is a conformational isomer of PrP, a host protein that is …

Little is currently known about the biochemical mechanism by which induced prion protein
(PrP) conformational change occurs during mammalian prion propagation. In this study, we …

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 …

We used ELISA and flow cytometry to study the binding of prion protein PrP to
glycosaminoglycans (GAGs). We found that recombinant human PrP (rPrP) binds GAGs …

Protein aggregation into dense filamentous inclusions is a characteristic feature of many
etiologically diverse neurodegenerative disorders including Alzheimer's disease (AD) …

The central pathogenic event of prion disease is the conformational conversion of a host
protein, PrP C, into a pathogenic isoform, PrP Sc. We previously showed that the protein …