Amyloid beta (Aβ), the hallmark of Alzheimer's Disease (AD), now appears to be deleterious
in its low number aggregate form as opposed to the macroscopic Aβ fibers historically seen …

Solid-state nuclear magnetic resonance (SSNMR) spectroscopy elucidates membrane
protein structures and dynamics in atomic detail to yield mechanistic insights. By …

Disruption of the neuronal membrane by toxic amyloid β oligomers is hypothesized to be the
major event associated with Alzheimer's disease's neurotoxicity. Misfolding of amyloid β is …

Background: The beta-amyloid peptide (Aβ) involved in Alzheimer's disease (AD) has been
described to associate/aggregate on the cell surface disrupting the membrane through pore …

Amyloid formation continues to be a widely studied area due to its association with
numerous diseases, such as Alzheimer's and Parkinson's diseases. Despite a large body of …

Aggregation and the formation of oligomeric intermediates of amyloid-β (Aβ) at the
membrane interface of neuronal cells are implicated in the cellular toxicity and pathology of …

Cellular membrane disruption induced by β-amyloid (Aβ) peptides has been considered one
of the major pathological mechanisms for Alzheimer disease. Mechanistic studies of the …

Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-β
(Aβ) toxicity associated with Alzheimer's disease; however, structural and mechanistic …

Molecular self-assembly, a phenomenon widely observed in nature, has been exploited
through organic molecules, proteins, DNA, and peptides to study complex biological …

The aggregation and deposition of amyloid β (Aβ) peptide onto neuronal cells, with
consequent cellular membrane perturbation, are central to the pathogenesis of Alzheimer's …