The proteasome degrades most cellular proteins in a controlled and tightly regulated
manner and thereby controls many processes, including cell cycle, transcription, signalling …

The ubiquitin proteasome pathway was discovered in the 1980s to be a central component
of the cellular protein-degradation machinery with essential functions in homeostasis, which …

Critical cellular processes are regulated, in part, by maintaining the appropriate intracellular
levels of proteins. Whereas de novo protein synthesis is a comparatively slow process …

In E. coli, protein degradation plays important roles in regulating the levels of specific
proteins and in eliminating damaged or abnormal proteins. E. coli possess a very large …

▪ Abstract Proteasomes are large multisubunit proteases that are found in the cytosol, both
free and attached to the endoplasmic reticulum, and in the nucleus of eukaryotic cells. Their …

A protein that greatly stimulates the multiple peptidase activities of the 20 S proteasome
(also known as macropain, the multicatalytic protease complex, and 20 S protease) has …

We have identified and purified a protein complex from human red blood cells that activates
the multicatalytic protease (MCP). The complex, which we call the regulator, sediments at 11 …

Proteins presented to the immune system must first be cleaved to small peptides by
intracellular proteinases. Proteasomes are proteolytic complexes that degrade cytosolic and …

The autophagic clearance of 26S proteasomes (proteaphagy) is an important homeostatic
mechanism within the ubiquitin system that modulates proteolytic capacity and eliminates …

Exposure to various forms of mild oxidative stress significantly increased the intracellular
degradation of both" short-lived" and" long-lived," metabolically radiolabeled, cell proteins in …