Metastable oligomeric and protofibrillar forms of amyloidogenic proteins have been
implicated as on-pathway assembly intermediates in amyloid formation and as the major …

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 …

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 …

Soluble oligomeric aggregates of the amyloid-β peptide (Aβ) have been implicated in the
pathogenesis of Alzheimer's disease (AD). Although the conformation adopted by Aβ within …

Alzheimer's disease (AD) is characterized by large numbers of senile plaques in the brain
that consist of fibrillar aggregates of 40-and 42-residue amyloid-β (Aβ) peptides. However …

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 …

Several lines of evidence indicate that prefibrillar assemblies of amyloid-β (Aβ)
polypeptides, such as soluble oligomers or protofibrils, rather than mature, end-stage …

Proteins adopt an amazing array of sequence-dependent struc-tures that enable them to
perform the many chemical functions critical to life. Over the past decade, however, it has …

Amyloid fibrils comprising primarily the peptides Aβ40 and Aβ42 are a defining feature of the
Alzheimer's disease (AD) brain, and convergent evidence suggests that the process of their …

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 …