 Proteasome Endopeptidase Complex
"Proteasome Endopeptidase Complex" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
| Descriptor ID |
D046988
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| MeSH Number(s) |
D05.500.562.500 D08.811.277.656.918 D08.811.600.730
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| Concept/Terms |
Proteasome Endopeptidase Complex- Proteasome Endopeptidase Complex
- Complex, Proteasome Endopeptidase
- Endopeptidase Complex, Proteasome
- Macropain
- Macroxyproteinase
- Multicatalytic Proteinase
- Proteinase, Multicatalytic
- Prosome
- Proteasome
- 20S Proteasome
- Proteasome, 20S
- Multicatalytic Endopeptidase Complex
- Complex, Multicatalytic Endopeptidase
- Endopeptidase Complex, Multicatalytic
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Below are MeSH descriptors whose meaning is more general than "Proteasome Endopeptidase Complex".
Below are MeSH descriptors whose meaning is more specific than "Proteasome Endopeptidase Complex".
This graph shows the total number of publications written about "Proteasome Endopeptidase Complex" by people in this website by year, and whether "Proteasome Endopeptidase Complex" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
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| 1995 | 1 | 0 | 1 | | 1996 | 0 | 1 | 1 | | 1997 | 0 | 1 | 1 | | 2000 | 0 | 7 | 7 | | 2001 | 1 | 0 | 1 | | 2002 | 0 | 2 | 2 | | 2003 | 0 | 3 | 3 | | 2004 | 1 | 4 | 5 | | 2005 | 0 | 2 | 2 | | 2006 | 1 | 5 | 6 | | 2007 | 0 | 3 | 3 | | 2008 | 2 | 4 | 6 | | 2009 | 6 | 2 | 8 | | 2010 | 3 | 2 | 5 | | 2011 | 2 | 6 | 8 | | 2012 | 0 | 8 | 8 | | 2013 | 1 | 2 | 3 | | 2014 | 1 | 4 | 5 | | 2015 | 1 | 5 | 6 | | 2016 | 0 | 2 | 2 | | 2017 | 0 | 3 | 3 | | 2019 | 3 | 1 | 4 | | 2020 | 1 | 3 | 4 | | 2022 | 3 | 2 | 5 |
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Below are the most recent publications written about "Proteasome Endopeptidase Complex" by people in Profiles.
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Hogrel G, Marino-Puertas L, Laurent S, Ibrahim Z, Covès J, Girard E, Gabel F, Fenel D, Daugeron MC, Clouet-d'Orval B, Basta T, Flament D, Franzetti B. Characterization of a small tRNA-binding protein that interacts with the archaeal proteasome complex. Mol Microbiol. 2022 07; 118(1-2):16-29.
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Nahar A, Sokolova V, Sekaran S, Orth JD, Park S. Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones. Cell Rep. 2022 06 07; 39(10):110918.
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Song A, Wen AQ, Wen YE, Dzieciatkowska M, Kellems RE, Juneja HS, D'Alessandro A, Xia Y. p97 dysfunction underlies a loss of quality control of damaged membrane proteins and promotes oxidative stress and sickling in sickle cell disease. FASEB J. 2022 05; 36(5):e22246.
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Tencer AH, Liu J, Zhu J, Burkholder NT, Zhang Y, Wu W, Strahl BD, Ohta T, Kutateladze TG. The ZZ domain of HERC2 is a receptor of arginylated substrates. Sci Rep. 2022 04 11; 12(1):6063.
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Galvin J, Curran E, Arteaga F, Goossens A, Aubuchon-Endsley N, McMurray MA, Moore J, Hansen KC, Chial HJ, Potter H, Brodsky JL, Coughlan CM. Proteasome activity modulates amyloid toxicity. FEMS Yeast Res. 2022 03 09; 22(1).
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Whiteley AM, Prado MA, de Poot SAH, Paulo JA, Ashton M, Dominguez S, Weber M, Ngu H, Szpyt J, Jedrychowski MP, Easton A, Gygi SP, Kurz T, Monteiro MJ, Brown EJ, Finley D. Global proteomics of Ubqln2-based murine models of ALS. J Biol Chem. 2021 Jan-Jun; 296:100153.
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Tzounakas VL, Dzieciatkowska M, Anastasiadi AT, Karadimas DG, Vergaki A, Siourounis P, Stamoulis K, Papassideri IS, Kriebardis AG, D'Alessandro A, Antonelou MH. Red cell proteasome modulation by storage, redox metabolism and transfusion. Blood Transfus. 2022 01; 20(1):27-39.
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Moon SL, Morisaki T, Stasevich TJ, Parker R. Coupling of translation quality control and mRNA targeting to stress granules. J Cell Biol. 2020 08 03; 219(8).
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Zavortink M, Rutt LN, Dzitoyeva S, Henriksen JC, Barrington C, Bilodeau DY, Wang M, Chen XXL, Rissland OS. The E2 Marie Kondo and the CTLH E3 ligase clear deposited RNA binding proteins during the maternal-to-zygotic transition. Elife. 2020 06 23; 9.
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Ferdoush J, Sen R, Durairaj G, Barman P, Kaja A, Guha S, Bhaumik SR. An F-Box Protein, Mdm30, Interacts with TREX Subunit Sub2 To Regulate Cellular Abundance Cotranscriptionally in Orchestrating mRNA Export Independently of Splicing and Mitochondrial Function. Mol Cell Biol. 2020 03 16; 40(7).
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