The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

Highlights•New structures have shown that there is a remarkable diversity and complexity of
the amyloid fold.•The same sequence forms different amyloid structures in different …

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

Amyloid proteins, which are considered 'villains' in many neurodegenerative diseases, form
enigmatic pathological strains that underlie disease pathogenesis and progression. Recent …

The hidden world of amyloid biology has suddenly snapped into atomic-level focus,
revealing over 80 amyloid protein fibrils, both pathogenic and functional. Unlike globular …

Proteins are occasionally converted from their normal soluble state to highly ordered fibrillar
aggregates (amyloids), which give rise to pathological conditions that range from …

Amyloid fibrils are filamentous protein aggregates implicated in several common diseases
such as Alzheimer's disease and type II diabetes. Similar structures are also the molecular …

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and
deposition into insoluble plaques and intracellular inclusions is the hallmark of several …

Many, perhaps most, proteins, are capable of forming self-propagating, β-sheet (amyloid)
aggregates. Amyloid-like aggregates are found in a wide range of diseases and underlie …

Protein amyloid fibrils are originally identified as pathological entities in a variety of
neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. Recent …