Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

Amyloidosis affects millions of people, as a cause of Alzheimer's disease or a complication
of dialysis, and also causes rare conditions. The many forms of the disorder have one …

Nanoparticles present enormous surface areas and are found to enhance the rate of protein
fibrillation by decreasing the lag time for nucleation. Protein fibrillation is involved in many …

Real-time monitoring of fibril growth is essential to clarify the mechanism of amyloid fibril
formation. Thioflavin T (ThT) is a reagent known to become strongly fluorescent upon …

Over the past two decades, there has been considerable research interest in the use of
nanoparticles in the study of protein and peptide aggregation, and of amyloid-related …

Amyloids can have normal biological functions. 1r3 However, amyloidogenic proteins can
also form unwanted oligomeric or polymeric aggregates when disturbed from their native …

Amyloid fibrils are self‐assembled fibrous protein aggregates that are associated with a
number of presently incurable diseases such as Alzheimer's and Parkinson's disease …

Since amyloid beta fibrillation (AβF) plays an important role in the development of
neurodegenerative diseases, we investigated the effect of graphene oxide (GO) and their …

We describe a kindred with slowly progressive gastrointestinal symptoms and autonomic
neuropathy caused by autosomal dominant, hereditary systemic amyloidosis. The amyloid …

Although most proteins can assemble into amyloid-like fibrils in vitro under extreme
conditions, how proteins form amyloid fibrils in vivo remains unresolved. Identifying rare …