Several neurodegenerative disorders arise from the abnormal protein aggregation in the
nervous tissue leading tointracellular inclusions or extracellular aggregates in specific brain …

This article reviews recent molecular dynamics simulations of the Alzheimer's amyloid-β
protein, the primary component of the amyloid plaques found in the brain of Alzheimer's …

In amyloid aggregation diseases soluble proteins coalesce into a wide array of undesirable
structures, ranging through oligomers and prefibrillar assemblies to highly ordered amyloid …

The progress toward understanding the molecular basis of Alzheimers's disease is strongly
connected to elucidating the early aggregation events of the amyloid-β (Aβ) peptide …

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 …

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 …

Amyloid β‐proteins spontaneously aggregate and build plaques in the brains of Alzheimer's
disease patients. The polypeptide has been the subject of extensive in vitro and …

Pathological folding and aggregation of the amyloid β-protein (Aβ) are widely perceived as
central to understanding Alzheimer's disease (AD) at the molecular level. Experimental …

Protein aggregation into highly structured amyloid fibrils is associated with various diseases
including Alzheimer's disease, Parkinson's disease, and type II diabetes. Amyloids can also …

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 …