Cancer cells are characterized by a higher rate of protein turnover and greater demand for
protein homeostasis compared to normal cells. In this scenario, the ubiquitin–proteasome …

The 26S proteasome is the most complex ATP-dependent protease machinery, of~ 2.5 MDa
mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated …

Remarkable progress has been achieved in multiple myeloma, and patient median survival
has been extended 3-to 4-fold. Specifically, there have been 18 newly approved treatments …

The ubiquitin/proteasome system is a primary conduit for selective intracellular protein
degradation. Since its discovery over 30 years ago, this highly regulated system continues to …

Despite all the other cells that have the potential to prevent cancer development and
metastasis through tumour suppressor proteins, cancer cells can upregulate the ubiquitin …

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

Simple Summary During the last two decades, collaborative translational studies utilizing
novel methodologies have dramatically advanced our understanding of multiple myeloma …

The proteasome is the central component of the main cellular protein degradation pathway.
During the past four decades, the critical function of the proteasome in numerous …

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

PSMD4/Rpn10 is a subunit of the 19S proteasome unit that is involved with feeding target
proteins into the catalytic machinery of the 26S proteasome. Because proteasome inhibition …