The amyloid-β oligomer (AβO) hypothesis was introduced in 1998. It proposed that the brain
damage leading to Alzheimer's disease (AD) was instigated by soluble, ligand-like AβOs …

Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

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 …

Most neurodegenerative diseases are proteinopathies, which are characterized by the
aggregation of misfolded proteins. Although many proteins have an intrinsic propensity to …

Amyloid-β peptide (Aβ) forms metastable oligomers> 50 kDa, termed AβOs, that are more
effective than Aβ amyloid fibrils at triggering Alzheimer's disease-related processes such as …

Protein aggregation is common to dozens of diseases including prionoses, diabetes,
Parkinson's and Alzheimer's. Over the past 15 years, there has been a paradigm shift in …

Chaperone-mediated autophagy (CMA) is a lysosome-dependent selective degradation
pathway implicated in the pathogenesis of cancer and neurodegenerative diseases …

This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

A pathological hallmark of Alzheimer's disease is an accumulation of insoluble plaque
containing the amyloid-β peptide of 40–42 amino acid residues. Prefibrillar, soluble …