Amyloid beta peptide (Aβ) is produced through the proteolytic processing of a
transmembrane protein, amyloid precursor protein (APP), by β-and γ-secretases. Aβ …

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 …

We describe the isolation and detailed structural characterization of stable toxic oligomers of
α-synuclein that have accumulated during the process of amyloid formation. Our approach …

We describe solid-state nuclear magnetic resonance (NMR) measurements on fibrils formed
by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1-40) that …

Self-assembled peptide nanostructures have been increasingly exploited as functional
materials for applications in biomedicine and energy. The emergent properties of these …

Because understanding amyloid fibrillation in molecular detail is essential for development
of strategies to control amyloid formation and overcome neurodegenerative disorders …

Current interest in amyloid fibrils stems from their involvement in neurodegenerative and
other diseases and from their role as an alternative structural state for many peptides and …

Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs
and tissues. Amyloid is insoluble and is structurally dominated by β‑sheet structure. Unlike …

Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but
are also implicated in important physiological functions (functional amyloids). The …

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) …