Many calpain orthologues in parasites or microorganisms ... than proteases such as caspases and those involved in the ubiquitin–proteasome system. Consequently, the biological functions and ...

The newfound relationship between the ubiquitin and calpain pathways may lead to pharmaceuticals and dietary approaches that can prolong the function of the relevant pathways and delay the onset ...

Found in most known organisms, the proteasome is the crucial component of ubiquitin-mediated protein degradation. It complements the numerous proteases that degrade proteins in the cell. Protease ...

Protein turnover is crucial in maintaining cellular homeostasis and this process is largely controlled by the Ubiquitin Proteasome Pathway (UPP). The pathway consists of an enzymatic cascade that ...

Polyubiquitination targets proteins for recognition and processing by the 26S proteasome, a cylindrical organelle that recognizes ubiquitinated proteins, degrades the proteins, and recycles ubiquitin.

Success as An Anti-Cancer Agent Has Fueled Efforts to Discover Proteasome Inhibitors That Raise Proteins Levels with Beneficial Effects The ubiquitin proteasome system (UPS) provides a mechanism ...

The protein tagged with ubiquitins is referred to as a polyubiquitin chain and this is bound by the proteasome for degradation. This overall process of protein degradation is termed the ubiquitin ...

Ubiquitin can be thought of as a “tag” that bonds to substrate proteins that should be degraded by the proteasome. It acts as a signal and, once bound, the protein is usually directed towards ...

This occurs through interactions with the protein FBXO31. On binding CTAPs, FBXO31 summons a ubiquitin ligase to tag the modified proteins for dismantling by the proteasome. Curiously, loss of FBXO31 ...

For more than a decade, medical providers have treated multiple myeloma (MM) with proteasome inhibitors (PIs). This important drug therapy has helped improve survival rates of people with MM.