Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

The condensation and aggregation of individual protein molecules into dense insoluble
phases is of relevance in such diverse fields as materials science, medicine, structural …

Fibrils associated with amyloid disease are molecular assemblies of key biological
importance, yet how cells respond to the presence of amyloid remains unclear. Cellular …

In this note we explain the use of the Akiake Information Criterion and its related model
comparison indices (usually derived for maximum likelihood estimator inverse problem …

It is still unclear why pathological amyloid deposition initiates in specific brain regions or why
some cells or tissues are more susceptible than others. Amyloid deposition is determined by …

The presence of amyloid fibrils is a hallmark of more than 50 human disorders, including
neurodegenerative diseases and systemic amyloidoses. A key unresolved challenge in …

Amyloid assemblies are associated with several debilitating human disorders.
Understanding the intra-and extracellular assembly of normally soluble proteins and …

We explore the long-time behavior and equilibrium properties of a system of linear filaments
growing through nucleated polymerisation. We show that the length distribution for …

Amyloid fibrils are highly polymorphic structures formed by many different proteins. They
provide biological function but also abnormally accumulate in numerous human diseases …

Amyloid fibrils are ordered, non-covalent polymers of proteins that are linked to a range of
diseases, as well as biological functions. Amyloid fibrils are often considered …