Amyloid fibrils are elongated, insoluble protein aggregates deposited in vivo in amyloid
diseases, and amyloid‐like fibrils are formed in vitro from soluble proteins. Both of these …

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

Recent publications strongly support the hypothesis that conformational changes in
amyloidogenic proteins lead to amyloid fibril formation and cause disease. Biophysical …

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 …

In amyloid related diseases, proteins form fibrillar aggregates with highly ordered β-sheet
structure regardless of their native conformations. Formation of such amyloid fibrils can be …

Although we know a significant amount about amyloid structure from low-resolution
methods, the nature of the fundamental amyloid fibril folding motif remains unknown. Recent …

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 …

Protein aggregation is a process in which proteins self-associate into imperfectly ordered
macroscopic entities. Such aggregates are generally classified as either amorphous or …

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

The problem of determining and understanding the molecular structures of amyloid fibrils
has attracted considerable attention and effort over the past several years. Although …