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 …

The assembly of proteins into amyloid fibrils, a phenomenon central to several currently
incurable human diseases, is a process of high specificity that commonly tolerates only a …

Aβ42 peptides associate into soluble oligomers and protofibrils in the process of forming the
amyloid fibrils associated with Alzheimer's disease. The oligomers have been reported to be …

Assemblyof the amyloid-β peptide (Aβ) into fibrils and its deposition in distinct brain areas is
considered responsible for the pathogenesis of Alzheimer's disease (AD). Thus, inhibition of …

Amyloid β-protein (Aβ) is linked to neuronal injury and death in Alzheimer's disease (AD). Of
particular relevance for elucidating the role of Aβ in AD is new evidence that oligomeric …

Formation of toxic oligomeric and fibrillar structures by the amyloid β-protein (Aβ) is linked to
Alzheimer's disease (AD). To facilitate the targeting and design of assembly inhibitors …

The nucleation of Alzheimer-associated Aβ peptide monomers can be catalyzed by
preexisting Aβ fibrils. This leads to autocatalytic amplification of aggregate mass and …

A macrocyclic β-sheet peptide containing two nonapeptide segments based on Aβ15–23
(QKLVFFAED) forms fibril-like assemblies of oligomers in the solid state. The X-ray …

Recent studies suggest that deposition of amyloid β (Aβ) into oligomeric aggregates and
fibrils, hallmarks of Alzheimer's disease, may be initiated by the aggregation of Aβ species …

Self-assembly of amyloid-β peptides leads to oligomers, protofibrils, and fibrils that are likely
instigators of neurodegeneration in Alzheimer's disease. We report results of time-resolved …