This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

Soluble oligomers of the amyloid-β (1-42)(Aβ42) peptide, widely considered to be among
the relevant neurotoxic species involved in Alzheimer's disease, were characterized with a …

Several cell-surface receptors for neurotoxic forms of amyloid-β (Aβ) have been described,
but their molecular interactions with Aβ assemblies and their relative contributions to …

Alzheimer's disease (AD) is a neurodegenerative disease characterized by severe brain
damage and dementia. There are currently few therapeutics to treat this disease, and they …

Perturbation of cell membranes by amyloid β (Ab) peptide oligomers is one possible
mechanism of cytotoxicity in Alzheimer's disease, but the structure of such Ab–membrane …

Cerebral amyloid angiopathy (CAA), which involves amyloid deposition in blood vessels
leading to fatal cerebral hemorrhage and recurring strokes, is present in the majority …

Intermediates along the fibrillation pathway are generally considered to be the toxic species
responsible for the pathologies of amyloid diseases. However, structural studies of these …

Human PrP (huPrP) is a high-affinity receptor for oligomeric amyloid β (Aβ) protein
aggregates. Binding of Aβ oligomers to membrane-anchored huPrP has been suggested to …

Formation of Aβ oligomers and fibrils plays a central role in the pathogenesis of Alzheimer's
disease. There are two major forms of Aβ in the brain: Aβ42 and Aβ40. Aβ42 is the major …