This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Amyloid fibrils formed from different proteins, each associated with a particular disease,
contain a common cross-β spine. The atomic architecture of a spine, from the fibril-forming …

We describe a full structural model for amyloid fibrils formed by the 40-residue β-amyloid
peptide associated with Alzheimer's disease (Aβ1–40), based on numerous constraints from …

Abnormal aggregation of proteins into filamentous aggregates commonly associates with
many diseases, such as Alzheimer's disease, Parkinson's disease and type-2 diabetes …

Amyloid–a fibrillar, cross β-sheet quaternary structure–was first discovered in the context of
human disease and tissue damage, and was thought to always be detrimental to the host …

Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional
structure, which is therefore of paramount importance for the prion function. However, no …

Protein molecules have the ability to form a rich variety of natural and artificial structures and
materials. We show that amyloid fibrils, ordered supramolecular nanostructures that are self …

The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative
diseases. In Parkinson's disease it is believed that the aggregation of α-synuclein (α-syn) …

The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are
the main peptide or protein component of amyloid that develops in the pancreas of type 2 …