Results 11 to 20 of about 248,818 (307)
Microbial Cell, 2015 Ornithine decarboxylase (ODC), a ubiquitin-independent substrate of the proteasome, is a homodimeric protein with a rate-limiting function in polyamine biosynthesis.
R. Roshini Beenukumar +3 more
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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
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The ubiquitin‐proteasome pathway and proteasome inhibitors [PDF]
Medicinal Research Reviews, 2001 AbstractThe ubiquitin‐proteasome pathway has emerged as a central player in the regulation of several diverse cellular processes. Here, we describe the important components of this complex biochemical machinery as well as several important cellular substrates targeted by this pathway and examples of human diseases resulting from defects in various ...
J, Myung, K B, Kim, C M, Crews
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Fluorescence-based proteasome activity profiling [PDF]
, 2011 With the proteasome emerging as a therapeutic target for cancer treatment, accurate tools for monitoring proteasome (inhibitor) activity are in demand.
Jong, A. +9 more
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Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]
, 2014 The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G. +20 more
core +1 more source
Assembly of the Drosophila 26 S proteasome is accompanied by extensive subunit rearrangements [PDF]
, 2002 The subunit contacts in the regulatory complex of the Drosophila 26 S proteasome were studied through the cross-linking of closely spaced subunits of the complex, and analysis of the cross-linking pattern in an immunoblot assay with the use of subunit ...
Kapelari, Barbara +13 more
core +2 more sources
Interplay between RNA Viruses and Promyelocytic Leukemia Nuclear Bodies
Veterinary Sciences, 2021 Promyelocytic leukemia nuclear bodies (PML NBs) are nuclear membrane-less sub structures that play a critical role in diverse cellular pathways including cell proliferation, DNA damage, apoptosis, transcriptional regulation, stem cell renewal ...
Sabari Nath Neerukonda
doaj +1 more source
Proteasome as a Molecular Target of Microcystin-LR
Toxins, 2015 Proteasome degrades proteins in eukaryotic cells. As such, the proteasome is crucial in cell cycle and function. This study proved that microcystin-LR (MC-LR), which is a toxic by-product of algal bloom, can target cellular proteasome and selectively ...
Zhu Zhu, Li Zhang, Guoqing Shi
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Assembly and disassembly of branched ubiquitin chains
Frontiers in Molecular Biosciences, 2023 Protein ubiquitylation is an essential post-translational modification that regulates nearly all aspects of eukaryotic cell biology. A diverse collection of ubiquitylation signals, including an extensive repertoire of polymeric ubiquitin chains, leads to
Justin B. Gregor +3 more
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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
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