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

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 …

The accumulation of β-sheet–rich amyloid fibrils or aggregates is a complex, multistep
process that is associated with cellular toxicity in a number of human protein misfolding …

Several lines of evidence indicate that prefibrillar assemblies of amyloid-β (Aβ)
polypeptides, such as soluble oligomers or protofibrils, rather than mature, end-stage …

Background Amyloid-related degenerative diseases are associated with the accumulation of
misfolded proteins as amyloid fibrils in tissue. In Alzheimer disease (AD), amyloid …

Oligomeric intermediates are non-fibrillar polypeptide assemblies that occur during amyloid
fibril formation and that are thought to underlie the aetiology of amyloid diseases, such as …

Alzheimer disease is characterized by the abnormal aggregation of amyloid β peptide into
extracellular fibrillar deposits known as amyloid plaques. Soluble oligomers have been …

Neurodegenerative diseases typically involve deposits of inclusion bodies that contain
abnormal aggregated proteins. Therefore, it has been suggested that protein aggregation is …

Many peptides and proteins self-assemble into amyloidfibrils. Examples include mammalian
and fungal prion proteins, polypeptides associated with human amyloid diseases, and …

The conversion of proteins from their native state to misfolded oligomers is associated with,
and thought to be the cause of, a number of human diseases, including Alzheimer's disease …