Recent studies suggest that both soluble oligomers and insoluble fibrils have toxic effects in
cell cultures, raising the interest in determining the first steps of the assembly process. We …

Pathogenesis of Alzheimer's disease (AD) is associated with aggregation of the amyloid-β
(Aβ) peptide into oligomeric and fibrillar assemblies; however, little is known about the …

Background: Brain amyloid plaque, a diagnostic feature of Alzheimer's disease (AD),
contains an insoluble fibrillar core that is composed primarily of variants of the β-amyloid …

Assembly of monomeric amyloid β-protein (Aβ) into oligomeric structures is an important
pathogenetic feature of Alzheimer's disease. The oligomer size distributions of aggregate …

Extensive research causally links amyloid-β peptide (Aβ) to Alzheimer's disease, although
the pathologically relevant Aβ conformation remains unclear. Aβ spontaneously aggregates …

A limitation of the amyloid hypothesis in explaining the development of neurodegenerative
diseases is that the level of amyloidogenic polypeptide in vivo is below the critical …

Oligomeric and protofibrillar aggregates formed by the amyloid‐β peptide (Aβ) are believed
to be involved in the pathology of Alzheimer's disease. Central to Alzheimer pathology is …

Oligomeric species populated during the aggregation of the Aβ42 peptide have been
identified as potent cytotoxins linked to Alzheimer's disease, but the fundamental molecular …

Since early oligomeric intermediates in amyloid assembly are often transient and difficult to
distinguish, characterize and quantify, the mechanistic basis of the initiation of spontaneous …

Background: Amyloid plaques composed of the fibrillar form of the amyloid-β protein (Aβ)
are the defining neuropathological feature of Alzheimer's disease (AD). A detailed …