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 …

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

Alloform-specific differences in structural dynamics between amyloid β-protein (Aβ) 40 and
Aβ42 appear to underlie the pathogenesis of Alzheimer's disease. To elucidate these …

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 …

Aggregation of the full‐length amyloid‐β (Aβ) and β2‐microglobulin (β2m) proteins is
associated with Alzheimer's disease and dialysis‐related amyloidosis, respectively. This …

Folding and self‐assembly of the 42‐residue amyloid β‐protein (Aβ) are linked to
Alzheimer's disease (AD). The 21–30 region of Aβ, Aβ (21–30), is resistant to proteolysis …

Amyloid fibrils formed from unrelated proteins often share morphological similarities,
suggesting common biophysicalmechanisms for amyloidogenesis. Biochemical studies 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 …

The β amyloid (Aβ) peptide aggregates to form β-rich structures that are known to trigger
Alzheimer's disease. Experiments suggest that an α-helical intermediate precedes the …

Despite much progress in understanding the folding and the aggregation processes of
proteins, the rules defining their interplay have yet to be fully defined. This problem is of …