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 …

Two decades into the twenty-first century, a confluence of breakthrough technologies
wielded at the molecular level is presenting biologists with unique opportunities to unravel …

Hijacking the cellular protein degradation system offers unique opportunities for drug
discovery, as exemplified by proteolysis-targeting chimeras. Despite their great promise for …

Molecular machines, such as polymerases, ribosomes, or proteasomes, fulfill complex tasks
requiring the thermal energy of their environment. They achieve this by restricting random …

Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S
proteasome. Additionally, a disordered segment on the substrate—either intrinsic or induced …

Four proteasome subtypes are commonly present in mammalian tissues: standard
proteasomes, which contain the standard catalytic subunits β1, β2 and β5; …

Protein degradation occurs through proteasomal, endosomal, and lysosomal pathways.
Technological advancements have allowed for the determination of protein copy numbers …

The linkage, length, and architecture of ubiquitin (Ub) chains are all important variables in
providing tight control over many biological paradigms. There are clear roles for branched …

The ubiquitin-proteasome system (UPS) is critical for protein quality control and regulating
protein lifespans. Following ubiquitination, UPS substrates bind multidomain receptors that …

Proteasome is the principal hydrolytic machinery responsible for the great majority of protein
degradation. The past three decades have testified prominent advances about proteasome …