Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

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 …

Alzheimer's disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

Highlights•New structures have shown that there is a remarkable diversity and complexity of
the amyloid fold.•The same sequence forms different amyloid structures in different …

This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …

Organic materials naturally lend themselves to the crafting of structure and function using the
strategies of self-assembly and supramolecular chemistry employed so effectively by …

Neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD),
Huntington's disease (HD), amyotrophic lateral sclerosis (ALS) and prion diseases are …

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

We present a structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide
associated with Alzheimer's disease (Aβ1–40), based on a set of experimental constraints …