Amyloid-β (Aβ) is a 39–42 residue protein produced by the cleavage of the amyloid
precursor protein (APP), which subsequently aggregates to form cross-β amyloid fibrils that …

Pathological folding and oligomer formation of the amyloid β-protein (Aβ) are widely
perceived as central to Alzheimer's disease. Experimental approaches to study Aβ self …

The formation of amyloid deposits in human tissues is a defining feature of more than 50
medical disorders, including Alzheimer's disease. Strong genetic and histological evidence …

The deposition of β-amyloid peptide (Aβ) fibrils around neurons is an invariable feature of
Alzheimer's disease and there is increasing evidence that fibrillar deposits and/or prefibrillar …

The deposition of aggregated amyloid‐β (Aβ) peptides in the brain as senile plaques is a
pathological hallmark of Alzheimer's disease (AD). Several lines of evidence indicate that …

The relationship between amyloid deposition and cellular toxicity is still controversial. In
addition to fibril-forming oligomers, other soluble Aβ forms (amyloid β-derived diffusible …

We have applied in situ atomic force microscopy to directly observe the aggregation of
Alzheimer's β-amyloid peptide (Aβ) in contact with two model solid surfaces: hydrophilic …

Alzheimer's disease is characterized by extensive cerebral amyloid deposition. Amyloid
deposits associated with damaged neuropil and blood vessels contain abundant fibrils …

Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1–42)), rather than of the more abundant Aβ (1–40) …

Misfolding and aggregation of peptides and proteins is a characteristic of many
neurodegenerative disorders, including Alzheimer's disease (AD). In AD the β-amyloid …