Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

Nucleation of new peptide and protein aggregates on the surfaces of amyloid fibrils of the
same peptide or protein has emerged in the past two decades as a major pathway for both …

It is widely accepted that β-amyloid oligomers (Aβos) play a key role in the progression of
Alzheimer's disease (AD) by inducing neuron damage and cognitive impairment, but Aβos …

The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …

Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the elderly.
Zinc (Zn) ion interacts with the pathogenic hallmark, amyloid-β (Aβ), and is enriched in …

The accumulation of the amyloid‐β peptides (Aβ) is central to the development of
Alzheimer's disease. The mechanism by which Aβ triggers a cascade of events that leads to …

Self-assembly of amyloid-β peptides leads to oligomers, protofibrils, and fibrils that are likely
instigators of neurodegeneration in Alzheimer's disease. We report results of time-resolved …

Neurodegeneration correlates with Alzheimer's disease (AD) symptoms, but the molecular
identities of pathogenic amyloid β-protein (Aβ) oligomers and their targets, leading to …

Self-assembly of amyloid-β (Aβ) peptides in human brain tissue leads to neurodegeneration
in Alzheimer's disease (AD). Amyloid fibrils, whose structures have been extensively …

The deposition of amyloid in brain tissue in the context of neurodegenerative diseases
involves the formation of intermediate species—termed oligomers—of lower molecular mass …