Results 11 to 20 of about 393,592 (390)
Modelling Proteasome and Proteasome Regulator Activities [PDF]
Biomolecules, 2014 Proteasomes are key proteases involved in a variety of processes ranging from the clearance of damaged proteins to the presentation of antigens to CD8+ T-lymphocytes.
Juliane Liepe +4 more
doaj +7 more sources
Deubiquitination Reactions on the Proteasome for Proteasome Versatility [PDF]
International Journal of Molecular Sciences, 2020 The 26S proteasome, a master player in proteolysis, is the most complex and meticulously contextured protease in eukaryotic cells. While capable of hosting thousands of discrete substrates due to the selective recognition of ubiquitin tags, this protease complex is also dynamically checked through diverse regulatory mechanisms.
Ji Yeong Shin +5 more
openaire +4 more sources
Cells, 2021 Cerebral hypoxia-ischemia (HI) compromises the proteasome in a clinically relevant neonatal piglet model. Protecting and activating proteasomes could be an adjunct therapy to hypothermia.
Nagat El Demerdash +6 more
doaj +1 more source
Proteasome Inhibitors for the Treatment of Multiple Myeloma
Cancers, 2020 Use of proteasome inhibitors (PIs) has been the therapeutic backbone of myeloma treatment over the past decade. Many PIs are being developed and evaluated in the preclinical and clinical setting.
S. Ito
semanticscholar +1 more source
Targeted Protein Degradation: Principles and Applications of the Proteasome
Cells, 2023 The proteasome is a multi-catalytic protease complex that is involved in protein quality control via three proteolytic activities (i.e., caspase-, trypsin-, and chymotrypsin-like activities).
Yosup Kim +4 more
doaj +1 more source
Ubiquitin–proteasome system (UPS) as a target for anticancer treatment
Archives of pharmacal research, 2020 The ubiquitin–proteasome system (UPS) plays an important role in the cellular processes for protein quality control and homeostasis. Dysregulation of the UPS has been implicated in numerous diseases, including cancer.
Jinyoung Park, Jinhong Cho, E. J. Song
semanticscholar +1 more source
Annual Review of Pharmacology and Toxicology, 2020 Proteasomes are large, multicatalytic protein complexes that cleave cellular proteins into peptides. There are many distinct forms of proteasomes that differ in catalytically active subunits, regulatory subunits, and associated proteins.
L. Fricker
semanticscholar +1 more source
Proteasome in action: substrate degradation by the 26S proteasome [PDF]
Biochemical Society Transactions, 2021 Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S proteasome. Additionally, a disordered segment on the substrate — either intrinsic or induced — is critical for proteasome engagement. The proteasome is geared to interact with both of these substrate features and prepare it for degradation.
Indrajit Sahu, Michael H. Glickman
openaire +3 more sources
Cell Chemical Biology, 2017 While proteasome inhibitors are now well-established research tools and chemotherapeutics, proteasome activators are much less explored. In this issue of Cell Chemical Biology, in a study from the groups of Berkers and Ovaa (Leestemaker et al., 2017), a chemical screen was used to identify a p38 MAPK inhibitor as a proteasome activator.
Krahn, Jan +2 more
openaire +4 more sources
Wiggle and Shake: Managing and Exploiting Conformational Dynamics during Proteasome Biogenesis
Biomolecules, 2023 The 26S proteasome is the largest and most complicated protease known, and changes to proteasome assembly or function contribute to numerous human diseases.
Daniel Betancourt +2 more
doaj +1 more source