Breakthroughs in molecular medicine have positioned the amyloid-β (Aβ) pathway at the
center of Alzheimer's disease (AD) pathophysiology. While the detailed molecular …

Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Natural biomolecular systems have evolved to form a rich variety of supramolecular
materials and machinery fundamental to cellular function. The assembly of these structures …

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 …

Amyloid diseases are global epidemics with profound health, social and economic
implications and yet remain without a cure. This dire situation calls for research into the …

The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

Abnormal assembly of tau, α-synuclein, TDP-43 and amyloid-β proteins into amyloid
filaments defines most human neurodegenerative diseases. Genetics provides a direct link …

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 …

The formation of amyloid fibrils is a general class of protein self-assembly behaviour, which
is associated with both functional biology and the development of a number of disorders …