Results 11 to 20 of about 195,005 (265)
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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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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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
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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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Molecular Cell, 2011 Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and thereby are essential for many aspects of cellular function. Because the proteolytic sites are sequestered in a closed barrel-shaped structure, activators are required to facilitate substrate access.
Stadtmueller, Beth M. +1 more
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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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The capture proteasome assay (CAPA) to evaluate subtype-specific proteasome inhibitors
Data in Brief, 2015 We recently developed a new assay to measure proteasome activity in vitro (CAPA for capture proteasome assay) [1], based on proteasome capture on an antibody-coated plate.
Nathalie Vigneron +2 more
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Annual Review of Microbiology, 2015 Interest in bacterial proteasomes was sparked by the discovery that proteasomal degradation is required for the pathogenesis of Mycobacterium tuberculosis, one of the world's deadliest pathogens. Although bacterial proteasomes are structurally similar to their eukaryotic and archaeal homologs, there are key differences in their mechanisms of assembly,
Jordan B, Jastrab, K Heran, Darwin
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Frontiers in Molecular Biosciences, 2019 The proteasome is a multi-catalytic molecular machine that plays a key role in the degradation of many cytoplasmic and nuclear proteins. The proteasome is essential and proteasome malfunction is associated with various disease pathologies.
Sabine Schipper-Krom +6 more
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