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 …

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 progressive deposition of the amyloid β peptide (Aβ) in fibrillar form is a key feature in
the development of the pathology in Alzheimer's disease (AD). We have characterized the …

The Aβ peptide assembles into a variety of distinct types of structures in vitro and in the brain
which have different biological consequences. Differential effects of inhibitory small …

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 …

Soluble oligomers and protofibrils of the Aβ42 peptide are neurotoxic intermediates in the
conversion of monomeric Aβ42 into the amyloid fibrils associated with Alzheimer's disease …

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 amyloid β peptide (Aβ), composed of 40 or 42 amino acids, is a critical component in the
etiology of the neurodegenerative Alzheimer disease. Aβ is prone to aggregate and forms …

Neurotoxic assemblies of the amyloid β‐protein (Aβ) have been linked strongly to the
pathogenesis of Alzheimer's disease (AD). Here, we sought to monitor the earliest step in Aβ …

Amyloid‐β peptide (Aβ) isoforms of different lengths and aggregation propensities coexist in
vivo. These different isoforms are able to nucleate or frustrate the assembly of each other. N …