Alzheimer's disease and Creutzfeldt–Jakob disease are the best‐known examples of a
group of diseases known as the amyloidoses. They are characterized by the extracellular …

Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs
and tissues. Amyloid is insoluble and is structurally dominated by β‑sheet structure. Unlike …

Disaggregation of amyloid fibrils is a fundamental biological process required for amyloid
propagation. However, due to the lack of experimental systems, the molecular mechanism of …

Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both
'natively unfolded'and globular proteins have been shown to initiate fibrillization by adopting …

The deposition of amyloid-and amyloid-like fibrils is the main pathological hallmark of
numerous protein misfolding diseases including Alzheimer's disease, transmissible …

Despite the difficulties associated with determining atomic-level structures for materials that
are fibrous, structural biologists are making headway in understanding the architecture of …

Misfolding and subsequent self‐assembly of protein molecules into various aggregates is a
common molecular mechanism for a number of important human diseases. Curing protein …

Protein aggregation refers to the process by which misfolded or partially folded proteins self-
assemble into supramolecular assemblies. This process is often associated with disease as …

One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

The formation of amyloid fibrils is associated with various human medical disorders of
unrelated origin. Recent research indicates that self‐assembled amyloid fibrils are also …