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 …

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 …

The ability to relate bulk experimental measurements of amyloid formation to the
microscopic assembly processes that underlie protein aggregation is critical in order to …

Neurodegenerative diseases such as Alzheimer's, Parkinson's and the transmissible
spongiform encephalopathies (TSEs) are characterized by abnormal protein deposits, often …

We report the detailed mechanical characterization of individual amyloid fibrils by atomic
force microscopy and spectroscopy. These self-assembling materials, formed here from the …

Self-assembly processes resulting in linear structures are often observed in molecular
biology, and include the formation of functional filaments such as actin and tubulin, as well …

A principle that has emerged from studies of protein aggregation is that proteins typically can
misfold into a range of different aggregated forms. Moreover, the phenotypic and …

Abstract Changes in protein conformation drive most biological processes, but none have
seized the imagination of scientists and the public alike as have the self-replicating …

A review of the literature of kinetic and mechanistic studies of transition-metal nanocluster
nucleation and growth is presented; the focus is on nucleation processes. A brief survey of …

Amyloid is aggregated protein in the form of insoluble fibrils. Amyloid deposition in human
tissue—amyloidosis—is associated with a number of diseases including all common …