There is an enormous amount of interest in the structures and formation mechanisms of
amyloid fibers. In this Perspective, we review the most common structural motifs of amyloid …

Lung endothelia in the arteries, capillaries, and veins are heterogeneous in structure and
function. Lung capillaries in particular represent a unique vascular niche, with a thin yet …

PrPSc (scrapie isoform of the prion protein) prions are the infectious agent behind diseases
such as Creutzfeldt–Jakob disease in humans, bovine spongiform encephalopathy in cattle …

Biomolecular self‐assembly of hierarchical materials is a precise and adaptable bottom‐up
approach to synthesizing across scales with considerable energy, health, environment …

We report the results of solid state nuclear magnetic resonance (NMR) measurements on
amyloid fibrils formed by the full-length prion protein PrP (residues 23− 231, Syrian hamster …

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 …

The transmissible agent of prion disease consists of a prion protein in its abnormal, β-sheet
rich state (PrPSc), which is capable of replicating itself according to the template-assisted …

Structural variations in β-amyloid fibrils are potentially important to the toxicity of these fibrils
in Alzheimer's disease (AD). We describe a repeated seeding protocol that selects a …

The key molecular event in the pathogenesis of prion diseases is the conformational
conversion of a cellular prion protein, PrP C, into a misfolded form, PrP Sc. In contrast to PrP …

Prions are infective proteins, which can self-assemble into different strain conformations,
leading to different disease phenotypes. An increasing number of studies suggest that prion …