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 …

Amyloid and amyloid-like fibrils are self-assembling protein nanostructures, of interest for
their robust material properties and inherent biological compatibility as well as their putative …

Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid
results in numerous human diseases. Despite an increasing number of proteins and peptide …

Evolution has fine-tuned proteins to accomplish a variety of tasks. Yet, with aging, some
proteins assemble into harmful amyloid aggregates associated with neurodegenerative …

The formation of nanoscale amyloid fibrils from normally soluble peptides and proteins is a
common form of self-assembly phenomenon that has fundamental connections with …

Quantitative understanding of the kinetics of fibril formation and the molecular mechanism of
transition from monomers to fibrils is needed to obtain insights into the growth of amyloid …

The spontaneous assembly of proteins into amyloid fibrils is a phenomenon central to many
increasingly common and currently incurable human disorders, including Alzheimer's and …

Self-assembly of proteins into amyloid aggregates displays a broad diversity of
morphologies, both at the protofibrillar and final fibrillar species. These polymorphic species …

Protein oligomers have been implicated as toxic agents in a wide range of amyloid-related
diseases. However, it has remained unsolved whether the oligomers are a necessary step in …

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