This book highlights proteasome structures and how they are related to different aspects of
proteasome function. Moreover, the book reports on the functional roles these highly …

Proteasomes are large, multisubunit proteolytic complexes presenting multiple targets for
therapeutic intervention. The 26S proteasome consists of a 20S proteolytic core and one or …

The presence of endoplasmic reticulum (ER) stress and impaired ubiquitin–proteasome
system (UPS) activity has been independently implicated in the pathophysiology of …

Proteasome inhibitors are used to treat blood cancers such as multiple myeloma (MM) and
mantle cell lymphoma. The efficacy of these drugs is frequently undermined by acquired …

Selective degradation of proteins by the ubiquitin-proteasome pathway is a critical
determinant for maintaining cellular homeostasis. Most intracellular proteins are degraded …

Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and
survival. Defects in this process are associated with diseases such as cancer and …

Targeting of the protein degradation pathway, in particular, the ubiquitin-proteasome system,
has emerged as an attractive novel cancer chemotherapeutic modality. Although …

Immunoproteasome is an emerging biological target that constitutes a key element not only
in antigen presentation but also in T cell and cytokine regulation as well as cellular …

Background: In eukaryotes, endoplasmic reticulum stress (ERS) and the unfolded protein
response (UPR) are coordinately regulated to maintain steady-state levels and activities of …

Significance: The proteasome is the essential protease that is responsible for regulated
cleavage of the bulk of intracellular proteins. Its central role in cellular physiology has been …