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 …

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 …

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

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 …

Tauopathies feature progressive accumulation of tau amyloids. Pathology may begin when
these amplify from a protein template, or seed, whose structure is unknown. We have …

The development of atomic force microscopy (AFM) has opened up a wide range of novel
opportunities in nanoscience and new modalities of observation in complex biological …

Simple polyglutamine (polyQ) peptides aggregate in vitro via a nucleated growth pathway
directly yielding amyloid-like aggregates. We show here that the 17-amino-acid flanking …

Misfolded proteins associated with diverse aggregation disorders assemble not only into a
single toxic conformer but rather into a suite of aggregated conformers with unique …

Phase separation is thought to underlie spatial and temporal organization that is required for
controlling biochemical reactions in cells. Multivalence of interaction motifs, also known as …

Several hereditary neurological and neuromuscular diseases are caused by an abnormal
expansion of trinucleotide repeats. To date, there have been 10 of these trinucleotide repeat …