It is now well established that the blood-clotting protein fibrinogen can polymerise into an
anomalous form of fibrin that is amyloid in character; the resultant clots and microclots entrap …

Within the extensive range of self-propagating pathologic protein aggregates of mammals,
prions are the most clearly infectious (eg,∼ 10 9 lethal doses per milligram). The structures …

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

Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å)
resolution cryo-electron microscopy-based structure of infectious brain-derived fibrils of the …

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 …

Prion strains in a given type of mammalian host are distinguished by differences in clinical
presentation, neuropathological lesions, survival time, and characteristics of the infecting …

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 …

Prion diseases are caused by the conformational conversion of prion protein (PrP). Forty-two
different mutations were identified in human PrP, leading to genetic prion diseases with …

Recent computational advancements in the simulation of biochemical processes allow
investigating the mechanisms involved in protein regulation with realistic physics-based …

The ever increasing computer power, together with the improved accuracy of atomistic force
fields, enables researchers to investigate biological systems at the molecular level with …