Transition of soluble proteins into insoluble amyloid fibrils is driven by self-propagating short
sequence stretches. However, accurate prediction of aggregation determinants remains …

Accurate prediction of amyloid-forming amino acid sequences remains an important
challenge. We here present an online database that provides open access to the largest set …

The establishment of rules that link sequence and amyloid feature is critical for our
understanding of misfolding diseases. To this end, we have performed a saturation …

Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a
functional role. The cross-β molecular architecture has been reported in increasing numbers …

Background Amyloidoses are a group of usually fatal diseases, probably caused by protein
misfolding and subsequent aggregation into amyloid fibrillar deposits. The mechanisms …

In amyloid fibrils, β-strand conformations of polypeptide chains, or segments thereof, are
perpendicular to the fibril axis, but knowledge of their three dimensional structure at atomic …

Numerous studies have shown that the ability to form amyloid fibrils is an inherent property
of the polypeptide chain. This has lead to the development of several computational …

Protein aggregation results in β-sheet–like assemblies that adopt either a variety of
amorphous morphologies or ordered amyloid-like structures. These differences in structure …

Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …

Amyloidogenic model peptides are invaluable for investigating assembly mechanisms in
disease related amyloids and in protein folding. During aggregation, such peptides can …