Aβ42 oligomers play key roles in the pathogenesis of Alzheimer disease, but their structures
remain elusive partly due to their transient nature. Here, we show that Aβ42 in a fusion …

When assembling as fibrils Aβ40 peptides can only assume U-shaped conformations while
Aβ42 can also arrange as S-shaped three-stranded chains. We show that this allows Aβ42 …

Amyloid-β (Aβ) peptides form assemblies that are pathological hallmarks of Alzheimer's
disease. Aβ oligomers are soluble, mobile, and toxic forms of the peptide that act in the …

The aggregation of the amyloid (Aβ) peptide of 39–43 amino acids into plaques is observed
in the brain of Alzheimer's disease (AD) patients, but the mechanisms underlying the …

Spontaneous aggregation of amyloid beta (Aβ) proteins leading to the formation of
oligomers and eventually into fibrils has been identified as a key pathological signature of …

Oligomeric amyloid-β aggregates (AβOs) effectively trigger Alzheimer's disease-related
toxicity, generating great interest in understanding their structures and formation …

A β amyloid fibrils, which are related to Alzheimer's disease, have a cross-β structure
consisting of two β-sheets: β 1 and β 2. The A β peptides are thought to be serially arranged …

Amyloid-β (Aβ) fibrillary plaques represent the main hallmarks of Alzheimer's disease (AD),
in addition to tau neurofibrillary tangles. Disrupting early-formed Aβ protofibrils is considered …

Alzheimer's disease (AD) is characterized by fibrillar deposits of amyloid-β (Aβ) peptides
and neurofibrillary tangles of Tau proteins. Aβ peptides are composed of 37–49 residues …

The complex self-assembly processes in three dimensions of Alzheimer's β-peptide (Aβ)
amyloid protofibrils into polymorphic mature fibrils, particularly the relative protofibril …