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

The generation of toxic oligomers during the aggregation of the amyloid-β (Aβ) peptide Aβ42
into amyloid fibrils and plaques has emerged as a central feature of the onset and …

The formation of amyloid fibrils and oligomers is a hallmark of several neurodegenerative
disorders, including Alzheimer's disease (AD), and contributes to the disease pathway. To …

The self-assembly of β-amyloid (Aβ) peptide into highly ordered amyloid fibril structures
represents one of the pathological hallmarks of Alzheimer's disease. This process leads to …

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 …

Oligomers and fibrils of the amyloid-β (Aβ) peptide are implicated in the pathology of
Alzheimer's disease. Here, we monitor the growth of individual Aβ40 fibrils by time-resolved …

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 conversion of the soluble, nontoxic amyloid-β (Aβ) peptide into an aggregated, toxic
form rich in β-sheets is considered a key step in the development of Alzheimer's disease …

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 …