The self-assembly of amyloid-beta (Aβ) proteins in aqueous extracellular environments is
implicated in Alzheimer's disease. Among several alloforms of Aβ proteins differing in …

Aβ 16–22 is believed to have critical role in early aggregation of full length amyloids that are
associated with the Alzheimer's disease and can aggregate to form amyloid fibrils. However …

The nucleation of Alzheimer-associated Aβ peptide monomers can be catalyzed by
preexisting Aβ fibrils. This leads to autocatalytic amplification of aggregate mass and …

Extracellular deposition of amyloid‐beta (Aβ) protein, a fragment of membrane glycoprotein
called β‐amyloid precursor transmembrane protein (βAPP), is the major characteristic for the …

Understanding the key factors that govern the rate of protein aggregation is of immense
interest since protein aggregation is associated with a number of neurodegenerative …

The long lag times and subsequent rapid growth of Alzheimer's Aβ42 fibrils can be
explained by a secondary nucleation step, in which existing fibril surfaces are able to …

Amyloid aggregation is linked to a number of neurodegenerative syndromes, the most
prevalent one being Alzheimer's disease. In this pathology, the β‐amyloid peptides (Aβ) …

A novel computational approach to the structural analysis of ordered β-aggregation is
presented and validated on three known amyloidogenic polypeptides. The strategy is based …

The adsorption and aggregation of the amyloid-β (Aβ) peptides on the cell membrane plays
a causal role in the pathogenesis of Alzheimer's disease. Here, we report all-atom molecular …

Identifying the principles that describe the formation of protein oligomers and fibrils with
distinct morphologies is a daunting problem. Here we summarize general principles of …