Pathological folding and oligomer formation of the amyloid β-protein (Aβ) are widely
perceived as central to Alzheimer's disease. Experimental approaches to study Aβ self …

The self-assembly of amyloid (Aβ) proteins into nano-aggregates is a hallmark of
Alzheimer's disease (AD) development, yet the mechanism of how disordered monomers …

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 …

Experimental findings suggest that oligomeric forms of the amyloid β protein (Aβ) play a
critical role in Alzheimer's disease. Thus, elucidating their structure and the mechanisms of …

The aggregation of amyloid beta (Aβ) peptides plays an important role in the development of
Alzheimer's disease. Despite extensive effort, it has been difficult to characterize the …

Oligomers of amyloid β-protein (Aβ) play a central role in the pathology of Alzheimer's
disease. Of the two predominant Aβ alloforms, Aβ1− 40 and Aβ1− 42, Aβ1− 42 is more …

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 …

Amyloid-β (Aβ) peptides can elongate in the fibril axis and associate in the lateral direction.
We present detailed atomic Aβ models with different in-register intermolecular β-sheet-β …

One of the main research topics related to Alzheimer's disease is the aggregation of the
amyloid-β peptide, which was shown to follow different pathways for the two major alloforms …

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 …