Protein instability caused by exposure to external additives or severe stress may result in
different diseases. Of these diseases, many are triggered by protein misfolding and …

The increasing use of recombinantly expressed therapeutic proteins in the pharmaceutical
industry has highlighted issues such as their stability during long-term storage and means of …

Necrosis can be induced by stimulating death receptors with tumor necrosis factor (TNF) or
other agonists; however, the underlying mechanism differentiating necrosis from apoptosis …

Amyloids are highly organized cross–β-sheet–rich protein or peptide aggregates that are
associated with pathological conditions including Alzheimer's disease and type II diabetes …

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

The covalent modification of therapeutic biomolecules has been broadly explored, leading
to a number of clinically approved modified protein drugs. These modifications are typically …

OBJECTIVE To minimize hypoglycemia in subjects with type 1 diabetes by automated
glucagon delivery in a closed-loop insulin delivery system. RESEARCH DESIGN AND …

Amyloid fibril formation plays a role in more than 20 diseases including Alzheimer's disease.
In vitro detection of these fibrils is often performed using Thioflavin T (ThT), though the ThT …

When blood is exposed to negatively charged surface materials such as glass, an enzymatic
cascade known as the contact system becomes activated. This cascade is initiated by …

An increasing body of evidence suggests that soluble assemblies of amyloid proteins are
the predominant neurotoxic species in many amyloid-related diseases. Consequently, the …