Extracellular deposits of amyloid β (Aβ) aggregates in the brain is the hallmark of
Alzheimer's disease. We present the configurations (location and conformation) and the …

Numerous studies have concluded that the interaction of the amyloid β-peptide (Aβ) and
cellular membranes contributes to the toxicity and cell death observed in the progression of …

The mechanisms of interfacial folding and membrane insertion of the Alzheimer's amyloid‐β
fragment Aβ (25–35) and its less toxic mutant, N27A‐Aβ (25–35) and more toxic mutant …

The aggregation cascade and peptide-membrane interactions of the amyloid β-peptide (Aβ)
have been implicated as toxic events in the development and progression of Alzheimer's …

The aggregation of amyloid-β (Aβ) on neuronal membranes is implicated in both neuronal
toxicity and the progression of Alzheimer's disease. Unfortunately, the heterogeneous …

Growing evidence suggests that the β-amyloid (Aβ) peptides of Alzheimer's disease are
generated in early endosomes and that small oligomers are the principal toxic species. We …

Perturbation of cell membranes by amyloid β (Ab) peptide oligomers is one possible
mechanism of cytotoxicity in Alzheimer's disease, but the structure of such Ab–membrane …

Amyloid-β (Aβ) peptides are thought to be involved in neurodegenerative diseases such as
Alzheimer's disease and Down's syndrome. They form a large number of polymorphic …

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 …

A potential mechanism of cytotoxicity attributed to Alzheimer's A β peptides postulates that
their aggregation disrupts membrane structure causing uncontrollable permeation of Ca2+ …