Abstract The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led
to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic …

Immunoproteasomes contain replacements for the three catalytic subunits of standard
proteasomes. In most cells, oxidative stress and proinflammatory cytokines are stimuli that …

Constitutive proteasomes and immunoproteasomes shape the peptide repertoire presented
by major histocompatibility complex class I (MHC-I) molecules by harboring different sets of …

The immunoproteasome, a distinct class of proteasome found predominantly in monocytes
and lymphocytes, is known to shape the antigenic repertoire presented on class I major …

When cells are stimulated with pro-inflammatory cytokines, most of their constitutively
expressed proteasomes are replaced with immunoproteasomes, which increase the …

Rising interest in the mechanism and function of the proteasomes and the ubiquitin system
revealed that it is hard to find any aspect of the cellular metabolic network that is not directly …

The ubiquitin–proteasome system (UPS) degrades intracellular proteins into peptide
fragments that can be presented by major histocompatibility complex (MHC) class I …

During viral infection, proper regulation of immune responses is necessary to ensure
successful viral clearance with minimal host tissue damage. Proteasomes play a crucial role …

The life of every organism is dependent on the fine-tuned mechanisms of protein synthesis
and breakdown. The degradation of most intracellular proteins is performed by the ubiquitin …

Proteasomes perform the majority of proteolysis that occurs in the cytosol and nucleus of
eukaryotic cells and, thereby, perform crucial roles in cellular regulation and homeostasis …