The assembly and misassembly of normally soluble proteins into fibrilar structures is thought
to be a causative agent in a variety of human amyloid and prion diseases. Structural and …

Amyloid fibrils are found in association with at least two dozen fatal diseases. The tendency
of numerous proteins to convert into amyloid-like fibrils poses fundamental questions for …

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 …

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

The conformational change hypothesis postulates that tertiary structural changes under
partially denaturing conditions convert one of 17 normally soluble and functional human …

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 …

Amyloid diseases are characterized by the accumulation of insoluble, β‐strand‐rich
aggregates. The underlying structural conversions are closely associated with cellular …

Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …

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 …