The 26S proteasome is involved in degrading and regulating the majority of proteins in
eukaryotic cells, which requires a sophisticated balance of specificity and promiscuity. In this …

Large contact surfaces of protein–protein interactions (PPIs) remain to be an ongoing issue
in the discovery and design of small molecule modulators. Peptides are intrinsically capable …

The proteasome has key roles in neuronal proteostasis, including the removal of misfolded
and oxidized proteins, presynaptic protein turnover, and synaptic efficacy and plasticity …

Abstract Ubiquitin Proteasome System (UPS) is an adaptable and finely tuned system that
sustains proteostasis network under a large variety of physiopathological conditions. Its …

While neurodegenerative diseases affect millions of patients worldwide, there are
insufficient available therapeutics to halt or slow down the progression of these diseases. A …

Aging and age-related diseases are associated with a decline in the capacity of protein
turnover. Intrinsically disordered proteins, as well as proteins misfolded and oxidatively …

Metal terpyridine complexes have gained substantial interest in many application fields,
such as catalysis and supramolecular chemistry. In recent years, the biological activity of …

The proteasome degrades proteins, which is essential for cellular homeostasis. Ubiquitin
independent proteolysis degrades highly disordered and misfolded proteins. A decline of …

The balance between protein degradation and protein synthesis is a highly choreographed
process generally called proteostasis. Most intracellular protein degradation occurs through …

The proteolytic active sites of the 26S proteasome are sequestered within the catalytic
chamber of its 20S core particle (CP). Access to this chamber is through a narrow channel …