The structures of prion protein (PrP)–based mammalian prions have long been elusive. However, cryo-EM has begun to reveal the near-atomic resolution structures of fully …
B Caughey, HG Standke, E Artikis, F Hoyt… - PLoS …, 2022 - journals.plos.org
Numerous proteins are known to form ordered, self-propagating aggregates as underlying causes of neurodegeneration in proteinopathies such as Alzheimer's, Parkinson's, and prion …
BR Groveman, MA Dolan, LM Taubner, A Kraus… - Journal of Biological …, 2014 - ASBMB
Structures of the infectious form of prion protein (eg PrP Sc or PrP-Scrapie) remain poorly defined. The prevalent structural models of PrP Sc retain most of the native α-helices of the …
JR Requena, H Wille - Prion, 2014 - Taylor & Francis
The structures of the infectious prion protein, PrPSc, and that of its proteolytically truncated variant, PrP 27–30, have evaded experimental determination due to their insolubility and …
A Kraus, F Hoyt, CL Schwartz, B Hansen, AG Hughson… - BioRxiv, 2021 - biorxiv.org
Classical mammalian prions are assemblies of prion protein molecules that are extraordinarily transmissible, with a microgram of protein containing up to 108 lethal doses …
Prions, or infectious proteins, represent a major frontier in the study of infectious agents. The prions responsible for mammalian transmissible spongiform encephalopathies (TSEs) are …
The development of transmissible spongiform encephalopathies (TSEs) is associated with the conversion of the cellular prion protein (PrPC) into a misfolded, pathogenic isoform …
The conversion of the prion protein (PrP) into scrapie PrP (PrP Sc) is a central event in prion diseases. Several molecules work as cofactors in the conversion process, including …
Human (Hu) familial prion diseases are associated with about 40 point mutations of the gene coding for the prion protein (PrP). Most of the variants associated with these mutations …