The cascade of amyloid formation relates to multiple complex events at the molecular level.
Previous research has established amyloid plaque deposition as the leading cause of …

The link between bio-metals, Alzheimer's disease (AD), and its associated protein, amyloid-
β (Aβ), is very complex and one of the most studied aspects currently. Alzheimer's disease, a …

Amyloid fibrils from plant-based food protein sources bear a large unexploited potential for
applications in food and other biomaterials due to their techno-functional features. However …

Amyloid fibrils are associated with a number of neurodegenerative diseases, including fibrils
of amyloid β42 peptide (Aβ42) in Alzheimer's disease. These fibrils are a source of toxicity to …

The misfolding and aberrant aggregation of proteins into fibrillar structures is a key factor in
some of the most prevalent human diseases, including diabetes and dementia. Low …

Amyloid plaques composed of Aβ fibrils are a hallmark of Alzheimer's disease (AD).
However, the molecular architecture of amyloid plaques in the context of fresh mammalian …

Recent structural studies show distinct morphologies for the fibrils of Aβ (1–42) and Aβ (1–
40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1: 1 …

Development of therapeutic interventions for Alzheimer's over the past three decades has
been guided by the amyloid hypothesis, which puts Aβ deposition as the initiating event of a …

The accumulation of pathogenic protein oligomers and aggregates is associated with
several devastating amyloid diseases. As protein aggregation is a multi-step nucleation …

Amyloids share a common architecture but play disparate biological roles in processes
ranging from bacterial defense mechanisms to protein misfolding diseases. Their structures …