Scientists have long known that amyloid plaques consist of more than just Aβ. With cryo-electron tomography, they can now zoom in on these aggregated jumbles, revealing in startling detail the mess ...

Thanks to cryo-electron microscopy, scientists have solved the structure of amyloid and tau fibrils—the hallmark protein pathologies of Alzheimer’s disease, and at the atomic level. As for Aβ42, they ...

This is a preview. Log in through your library . Abstract Amyloid-β (Aβ) fibrils exhibit self-propagating, molecular-level polymorphisms that may contribute to variations in clinical and pathological ...

Researchers found that peristaltic pump flow mechanically breaks supersaturation to induce amyloid formation by hen egg white lysozyme, a-synuclein, amyloid b 1-40, and b2-microglobulin. The high ...

Amyloid fibrils appear in many neurodegenerative diseases, and scientists are eager to understand how they form and spread. But amyloids—clumped aggregations of misfolded proteins—can be difficult to ...

Researchers have developed a potential new peptide-based drug delivery system by repurposing fibrils that contribute to Alzheimer’s disease pathogenesis. Researchers at the University of North ...