Amyloid plaques in brain tissue are a hallmark of Alzheimer's disease. Primary components
of these plaques are 40-and 42-residue peptides, denoted Aβ (1− 40) and Aβ (1− 42), that …

Some of the pathological hallmarks of the Alzheimer's disease brain are senile plaques
composed of insoluble amyloid-β protein (Aβ) fibrils. However, much of the recent emphasis …

Accumulation of aggregated amyloid-β peptide (Aβ) in the brain is a pathological hallmark of
Alzheimer's disease (AD). In vitro studies indicate that the 40-to 42-residue Aβ peptide in …

Spontaneous conversion of β-amyloid peptide (Aβ) from soluble monomer to insoluble
fibrillar precipitate may underlie the neurodegeneration associated with Alzheimer's …

Extensive data suggest that the conversion of the amyloid-β (Aβ) peptide from soluble to
insoluble forms is a key factor in the pathogenesis of Alzheimer's disease (AD). In recent …

The pathology of Alzheimer's disease is connected to the aggregation of β-amyloid (Aβ)
peptide, which in vivo exists as a number of length-variants. Truncations and extensions are …

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 …

The deposition of amyloid βA4 in the brain is a major pathological hallmark of Alzheimer's
disease. Amyloid βA4 is a peptide composed of 42 or 43 amino acid residues. In brain, it …

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 …

Deposition of amyloid β (Aβ) fibrils has been suggested to play a central role in Alzheimer's
disease. In clarifying the mechanism by which fibrils form and moreover in developing new …