Aggregation of amyloidogenic proteins into insoluble amyloid fibrils is implicated in various
neurodegenerative diseases. This process involves protein assembly into oligomeric …

One of the hallmarks of Alzheimer's disease is the self‐aggregation of the amyloid β peptide
(Aβ) in extracellular amyloid fibrils. Among the different forms of Aβ, the 42‐residue fragment …

Individual Alzheimer's disease (AD) patients have been shown to have structurally distinct
amyloid-β (Aβ) aggregates, including fibrils, in their brain. These findings suggest the …

Abstract Amyloid-Β (A Β) is the major protein component of neuritic plaques found in
Alzheimer's disease. Evidence suggests that the physical aggregation state of A Β directly …

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 …

We report the use of atomic force microscopy to observe the initial stages of β-amyloid
fibrillization in situ. The growth of individual β-amyloid protofibrils on a mica substrate was …

Extensive data suggest that the conversion of the amyloid-β (Aβ) peptide from soluble to
insoluble forms is a key factor in the pathogenesis of Alzheimer's disease (AD). In recent …

Soluble oligomers and protofibrils are widely thought to be the toxic forms of the Aβ42
peptide associated with Alzheimer's disease. We have investigated the structure and …

Late-onset diabetes is typically associated with amyloid deposits of fibrillar amylin in the
pancreatic islets. Aqueous synthetic human amylin spontaneously forms polymorphic fibrils …

Evidence suggests that oligomers of the 42-residue form of the amyloid β-protein (Aβ), Aβ42,
play a critical role in the etiology of Alzheimer's disease (AD). Here we use high resolution …