Amyloid fibrils have traditionally been considered only as pathological aggregates in human
neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form …

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 …

Thioflavin T (ThT) has been widely used to investigate amyloid formation since 1989. While
concerns have recently been raised about its use as a probe specific for amyloid, ThT still …

This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …

Amyloid fibrils formed from different proteins, each associated with a particular disease,
contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming …

Background Protein aggregation correlates with the development of several debilitating
human disorders of growing incidence, such as Alzheimer's and Parkinson's diseases. On …

Amyloid fibrils are ordered aggregates of peptides or proteins that are fibrillar in structure
and contribute to the complications of many diseases (eg, type 2 diabetes mellitus …

Recent reports give strong support to the idea that amyloid fibril formation and the
subsequent development of protein deposition diseases originate from conformational …

The ability of proteins to fold to their functional states following synthesis in the intracellular
environment is one of the most remarkable features of biology. Substantial progress has …

Nanofiber structures of some peptides and proteins as biological materials have been
studied extensively, but their molecular mechanism of self-assembly and reassembly still …