The proteasome and its subunits are of clinical significance for at least two reasons: (1) a compromised complex assembly or a dysfunctional proteasome can be associated with the underlying pathophysiology of specific diseases, and (2) they can be exploited as drug targets for therapeutic interventions.

The proteasome is a highly sophisticated protease complex designed to carry out selective, efficient and processive hydrolysis of client proteins. It is known to collaborate with ubiquitin, which polymerizes to form a marker for regulated ...

The proteasome is a multisubunit enzyme complex that plays a central role in the regulation of proteins that control cell-cycle progression and apoptosis, and has therefore become an important target for anticancer therapy.

Structure of the Proteasome in the Core Particle (CP) and the Regulatory Particle (RP) as shown in Figure 3.10.2. Figure 3.10.2: Simplified scheme of the proteosome complex. The core particle is made of 2 copies of each of 14 different proteins that are assembled in groups of 7 forming a ring.

As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic machine responsible for regulated protein degradation in eukaryotic cells.

The proteasome is a large multi-subunit protease responsible for the degradation and removal of oxidized, misfolded, and polyubiquitinated proteins. The proteasome plays critical roles in nervous system processes.

The proteasome is a highly sophisticated protease complex designed to carry out selective, efficient and processive hydrolysis of client proteins. It is known to collaborate with ubiquitin, which polymerizes to form a marker for regulated proteolysis in eukaryotic cells.

2003年5月1日 · This review summarizes the structure and function of the proteasome, its role in the cell, and the preclinical rationale for proteasome inhibition in the treatment of cancer.

A proteasome is a large protein complex in cells that degrades and recycles damaged, misfolded, or unneeded proteins. This process is essential for maintaining cellular homeostasis and regulating various cellular functions.

The structure of the proteasome from Thermoplasma acidophilum introduces threonine proteases as a fifth class of proteolytic enzymes, and offers insights into the catalytic activity of this complicated piece of molecular machinery with its 14 active sites.