Among the long list of age-related complications, Alzheimer's disease (AD) has the most
dreadful impact on the quality of life due to its devastating effects on memory and cognitive …

Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

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 …

The amylome is the universe of proteins that are capable of forming amyloid-like fibrils. Here
we investigate the factors that enable a protein to belong to the amylome. A major factor is …

In recent genome-wide association studies, the extracellular chaperone protein, clusterin,
has been identified as a newly-discovered risk factor in Alzheimer's disease. We have …

A major role for the intracellular post-translational modification O-GlcNAc appears to be the
inhibition of protein aggregation. Most of the previous studies in this area focused on O …

Mammalian small heat-shock proteins (sHSPs) are molecular chaperones that form
polydisperse and dynamic complexes with target proteins, serving as a first line of defense …

Small heat-shock proteins, including αB-crystallin (αB), play an important part in protein
homeostasis, because their ATP-independent chaperone activity inhibits uncontrolled …

How small heat shock proteins (sHsps) might empower proteostasis networks to control
beneficial prions or disassemble pathological amyloid is unknown. Here, we establish that …

Amyloid-like fibrils from food proteins possess unique functional properties for food and
many other uses. This study reports the effect of hydrolytic heating (pH 2.0, 85° C, 0–24 h) …