Results from recent clinical trials of antibodies that target amyloid-β (Aβ) for Alzheimer's
disease have created excitement and have been heralded as corroboration of the amyloid …

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 …

This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

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 …

This review discusses one-dimensional supramolecular polymers that form in aqueous
media. First, naturally occurring supramolecular polymers are described, in particular …

Aggregation of amyloid-β peptides into fibrils or other self-assembled states is central to the
pathogenesis of Alzheimer's disease. Fibrils formed in vitro by 40-and 42-residue amyloid-β …

Alzheimer's disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that
depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here …

We describe the isolation and detailed structural characterization of stable toxic oligomers of
α-synuclein that have accumulated during the process of amyloid formation. Our approach …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …