Formation of intracellular plaques and small oligomeric species of amyloid β (Aβ) peptides
inside neurons is a hallmark of Alzheimer's disease. The most abundant Aβ species in the …

Amyloid-β (Aβ) oligomers play a central role in Alzheimer's disease (AD). Plaques of AD
patients consist of Aβ40 and Aβ42 peptides and truncated Aβ peptides. The Aβ24 peptide …

The glycine zipper motif at the C-terminus of the β-amyloid (Aβ) peptide have been shown to
strongly influence the formation of neurotoxic aggregates. A previous study showed that the …

It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …

Alzheimer's disease is presumed to be caused by the formation of intracellular plaques of
amyloid β (Aβ) peptides inside neurons. The most abundant Aβ forms are Aβ40 and Aβ42 …

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 …

Alzheimer's disease (AD) is characterized by the abnormal aggregation of amyloid-β peptide
(Aβ) in extracellular deposits known as senile plaques. The tyrosine residue (Tyr-10) is …

A mechanistic understanding of Aβ aggregation and high-resolution structures of Aβ fibrils
and oligomers are vital to elucidating relevant details of neurodegeneration in Alzheimer's …

The aggregation of amyloid-β protein (Aβ) into oligomers and amyloid fibrils is closely
related to Alzheimer's disease (AD). Aβ40 and Aβ42, as two most prominent isoforms of Aβ …

Aβ peptide aggregation is known to be an important factor in the cause of Alzheimer's
disease (AD). Smaller oligomers, the intermediates during the process of aggregation, are …