This process involves the formation of amyloid fibrils, crystal-like collections of misfolded proteins that clump together when the proteins are highly concentrated (supersaturated) in liquids ...

Rather than seeking a single cure — a magic bullet — for Alzheimer’s disease, a shotgun blast of different drugs with ...

More than 20 unrelated proteins can form amyloid fibrils in vivo. All fibrils share cross-β core structure and pathognomonic red-green birefringence when viewed under cross-polarized light after ...

Intrinsically disordered proteins (IDPs) do not attain a stable secondary or tertiary structure and rapidly change their ...

A study originally focusing on cancer has shown that amyloids — proteins typically linked to neurodegenerative diseases like ...

Transthyretin (ATTR) amyloidosis is a life-threatening, gain-of-toxic-function disease characterised by extracellular deposition of amyloid fibrils composed of transthyretin (TTR). TTR protein ...

From a molecular perspective, the common hallmark of neurodegenerative disorders is the misfolding and aberrant aggregation of proteins in amyloid-like beta-sheet filaments. This feature is not only ...

Peristaltic pump-induced amyloid formation of proteins. (a) hen egg white lysozyme, (B) α-synuclein, (C) Aβ, and (D) β2microglobulin. Osaka, Japan – The factor that tips you over the edge ...