ABSTRACT A majority of thousands of intracellular mammalian proteins are recognized by
proteasome only being conjugated with ubiquitin (Ub), representing a universal degradation …

Emerging data reveal that besides degrading proteins tagged with ubiquitin, the proteasome
plays a more varied and decisive role in cellular regulation than previously imagined. In this …

The proteasome is an intricate molecular machine, which serves to degrade proteins
following their conjugation to ubiquitin. Substrates dock onto the proteasome at its 19 …

Regulated cellular proteolysis is mediated largely by the ubiquitin–proteasome system
(UPS). It is a highly specific process that is time-(eg cell cycle), compartment-(eg nucleus or …

To determine the minimum requirements for substrate recognition and processing by
proteasomes, the functional elements of a ubiquitin‐independent degradation tag were …

The 26S proteasome is responsible for regulated proteolysis in eukaryotic cells. Its
substrates are diverse in structure, function, sequence length, and amino acid composition …

The proteasome plays a role in a myriad of intracellular processes from cell-cycle control to
antigen presentation. Central to these processes is the targeting of selected proteins for …

Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and
survival. Defects in this process are associated with diseases such as cancer and …

In the ubiquitin-proteasome system, substrates fated for destruction first acquire covalent
modification by ubiquitin, and are subsequently destroyed by the proteasome. Traditionally …

Most proteasome substrates are marked for degradation by ubiquitin conjugation, but some
are targeted by other means. The properties of these exceptional cases provide insights into …