Ubiquitin-Protein Ligase Complexes
"Ubiquitin-Protein Ligase Complexes" 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.
Complexes of enzymes that catalyze the covalent attachment of UBIQUITIN to other proteins by forming a peptide bond between the C-terminal GLYCINE of UBIQUITIN and the alpha-amino groups of LYSINE residues in the protein. The complexes play an important role in mediating the selective-degradation of short-lived and abnormal proteins. The complex of enzymes can be broken down into three components that involve activation of ubiquitin (UBIQUITIN-ACTIVATING ENZYMES), conjugation of ubiquitin to the ligase complex (UBIQUITIN-CONJUGATING ENZYMES), and ligation of ubiquitin to the substrate protein (UBIQUITIN-PROTEIN LIGASES).
| Descriptor ID |
D043743
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| MeSH Number(s) |
D08.811.464.938
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| Concept/Terms |
Ubiquitin-Protein Ligase Complexes- Ubiquitin-Protein Ligase Complexes
- Complexes, Ubiquitin-Protein Ligase
- Ligase Complexes, Ubiquitin-Protein
- Ubiquitin Protein Ligase Complexes
|
Below are MeSH descriptors whose meaning is more general than "Ubiquitin-Protein Ligase Complexes".
Below are MeSH descriptors whose meaning is more specific than "Ubiquitin-Protein Ligase Complexes".
This graph shows the total number of publications written about "Ubiquitin-Protein Ligase Complexes" by people in this website by year, and whether "Ubiquitin-Protein Ligase Complexes" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2005 | 1 | 1 | 2 |
| 2006 | 0 | 1 | 1 |
| 2007 | 0 | 1 | 1 |
| 2008 | 1 | 0 | 1 |
| 2009 | 1 | 0 | 1 |
| 2013 | 1 | 0 | 1 |
| 2021 | 1 | 0 | 1 |
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Below are the most recent publications written about "Ubiquitin-Protein Ligase Complexes" by people in Profiles.
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Chen X, Liao S, Makaros Y, Guo Q, Zhu Z, Krizelman R, Dahan K, Tu X, Yao X, Koren I, Xu C. Molecular basis for arginine C-terminal degron recognition by Cul2FEM1 E3 ligase. Nat Chem Biol. 2021 03; 17(3):254-262.
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Pozzebon ME, Varadaraj A, Mattoscio D, Jaffray EG, Miccolo C, Galimberti V, Tommasino M, Hay RT, Chiocca S. BC-box protein domain-related mechanism for VHL protein degradation. Proc Natl Acad Sci U S A. 2013 Nov 05; 110(45):18168-73.
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van Leuken R, Clijsters L, van Zon W, Lim D, Yao X, Wolthuis RM, Yaffe MB, Medema RH, van Vugt MA. Polo-like kinase-1 controls Aurora A destruction by activating APC/C-Cdh1. PLoS One. 2009; 4(4):e5282.
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Kaplow ME, Korayem AH, Venkatesh TR. Regulation of glia number in Drosophila by Rap/Fzr, an activator of the anaphase-promoting complex, and Loco, an RGS protein. Genetics. 2008 Apr; 178(4):2003-16.
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Zhang N, Liu J, Ding X, Aikhionbare F, Jin C, Yao X. FBXL5 interacts with p150Glued and regulates its ubiquitination. Biochem Biophys Res Commun. 2007 Jul 20; 359(1):34-9.
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Eng CH, Huckaba TM, Gundersen GG. The formin mDia regulates GSK3beta through novel PKCs to promote microtubule stabilization but not MTOC reorientation in migrating fibroblasts. Mol Biol Cell. 2006 Dec; 17(12):5004-16.
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Luo K, Xiao Z, Ehrlich E, Yu Y, Liu B, Zheng S, Yu XF. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc Natl Acad Sci U S A. 2005 Aug 09; 102(32):11444-9.
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Liu B, Sarkis PT, Luo K, Yu Y, Yu XF. Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol. 2005 Aug; 79(15):9579-87.