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 …

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 …

Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Formation of amyloid fibrils underlies a wide range of human disorders, including
Alzheimer's and prion diseases. The amyloid fibrils can be readily detected thanks to …

Cryoelectron microscopy (cryo-EM) has provided unprecedented insights into amyloid fibril
structures, including those associated with disease. However, these structures represent the …

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 …

The formation of amyloid fibrils by the intrinsically disordered protein α-synuclein is a
hallmark of Parkinson disease. To characterize the microscopic steps in the mechanism of …

Abstract α-Synuclein (α-syn) is a 140-residue intrinsically disordered protein that is involved
in neuronal and synaptic vesicle plasticity, but its aggregation to form amyloid fibrils is the …

Self-assembly provides an attractive route to functional organic materials, with properties
and hence performance depending sensitively on the organization of the molecular building …

Protein instability caused by exposure to external additives or severe stress may result in
different diseases. Of these diseases, many are triggered by protein misfolding and …