In vivo self-assembly of proteins into aggregates known as amyloids is related to many
diseases. Although a large number of studies have been performed on the formation of …

As an important neuropathological hallmark of Alzheimer's disease (AD), the oligomerization
of amyloid-β (Aβ) peptides has been intensively investigated in both theoretical and …

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 …

Aggregation of amyloid β (Aβ) peptide is implicated in fatal Alzheimer's disease, for which no
cure is available. Understanding the mechanisms responsible for this aggregation is …

A limitation of the amyloid hypothesis in explaining the development of neurodegenerative
diseases is that the level of amyloidogenic polypeptide in vivo is below the critical …

We studied the oligomerization of Alzheimer amyloid beta peptide (Aβ) using a replica
exchange molecular dynamics (REMD) simulation. The simulation was performed with Aβ10 …

The aggregation of monomeric amyloid β protein (Aβ) peptide into oligomers and amyloid
fibrils in the mammalian brain is associated with Alzheimer's disease. Insight into the …

Oligomers of amyloid-β peptides (Aβ) are formed during the early stage of the
amyloidogenesis process and exhibit neurotoxicity. The oligomer formation process of Aβ …

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 aggregation of amyloid-β protein (1–42) is studied at experimental concentrations using
all-atom molecular dynamics simulations. We observe a fast aggregation into oligomers …