The aggregation of proteins into structures known as amyloids is observed in many
neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of …

Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some
amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative …

Mammalian prions propagate as distinct strains and are composed of multichain assemblies
of misfolded host-encoded prion protein (PrP). Here, we present a near-atomic resolution …

Prion diseases are caused by the misfolding of prion protein (PrP). Misfolded PrP forms
protease-resistant aggregates in vivo (PrPSc) that are able to template the conversion of the …

Recent cryogenic electron microscopy (cryo-EM) studies of infectious, ex vivo, prion fibrils
from hamster 263K and mouse RML prion strains revealed a similar, parallel in-register …

Prions are notorious protein-only infectious agents that cause invariably fatal brain diseases
following silent incubation periods that can span a lifetime. These diseases can arise …

Highlights•Cryo-EM enables high resolution structure determination of ex vivo amyloid
fibres.•Patient derived tau fibrils adopt multiple folds and protofilament interactions.•β-helix …

The structure of the infectious prion protein (PrPSc), which is responsible for Creutzfeldt-
Jakob disease in humans and bovine spongiform encephalopathy, has escaped all attempts …

Self-templating assemblies of the human prion protein are clinically associated with
transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a …

Mammalian prions are lethal transmissible pathogens that cause fatal neurodegenerative
diseases in humans and animals. They consist of fibrils of misfolded, host-encoded prion …