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
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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 |
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| 2004 | 1 | 1 | 2 | | 2006 | 1 | 0 | 1 | | 2008 | 0 | 1 | 1 | | 2012 | 0 | 1 | 1 | | 2015 | 0 | 1 | 1 | | 2022 | 0 | 1 | 1 | | 2025 | 0 | 1 | 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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Oguh AU, Haemmerle MW, Sen S, Rozo AV, Shrestha S, Cartailler JP, Fazelinia H, Ding H, Preza S, Yang J, Yang X, Sussel L, Alvarez-Dominguez JR, Doliba N, Spruce LA, Arrojo E Drigo R, Stoffers DA. E3 ligase substrate adaptor SPOP fine-tunes the UPR of pancreatic ß cells. Genes Dev. 2025 Feb 03; 39(3-4):261-279.
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Wang Q, Li H, Tajima K, Verkerke ARP, Taxin ZH, Hou Z, Cole JB, Li F, Wong J, Abe I, Pradhan RN, Yamamuro T, Yoneshiro T, Hirschhorn JN, Kajimura S. Post-translational control of beige fat biogenesis by PRDM16 stabilization. Nature. 2022 09; 609(7925):151-158.
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Hai L, Szwarc MM, He B, Lonard DM, Kommagani R, DeMayo FJ, Lydon JP. Uterine function in the mouse requires speckle-type poz protein. Biol Reprod. 2018 06 01; 98(6):856-869.
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Kearns CA, Ravanelli AM, Cooper K, Appel B. Fbxw7 Limits Myelination by Inhibiting mTOR Signaling. J Neurosci. 2015 Nov 04; 35(44):14861-71.
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Snyder JL, Kearns CA, Appel B. Fbxw7 regulates Notch to control specification of neural precursors for oligodendrocyte fate. Neural Dev. 2012 May 03; 7:15.
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Homer H, Gui L, Carroll J. A spindle assembly checkpoint protein functions in prophase I arrest and prometaphase progression. Science. 2009 Nov 13; 326(5955):991-4.
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Killian DJ, Harvey E, Johnson P, Otori M, Mitani S, Xue D. SKR-1, a homolog of Skp1 and a member of the SCF(SEL-10) complex, regulates sex-determination and LIN-12/Notch signaling in C. elegans. Dev Biol. 2008 Oct 15; 322(2):322-31.
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McNatt MW, McKittrick I, West M, Odorizzi G. Direct binding to Rsp5 mediates ubiquitin-independent sorting of Sna3 via the multivesicular body pathway. Mol Biol Cell. 2007 Feb; 18(2):697-706.
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Yamamoto TM, Iwabuchi M, Ohsumi K, Kishimoto T. APC/C-Cdc20-mediated degradation of cyclin B participates in CSF arrest in unfertilized Xenopus eggs. Dev Biol. 2005 Mar 15; 279(2):345-55.
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Macdonald M, Wan Y, Wang W, Roberts E, Cheung TH, Erickson R, Knuesel MT, Liu X. Control of cell cycle-dependent degradation of c-Ski proto-oncoprotein by Cdc34. Oncogene. 2004 Jul 22; 23(33):5643-53.
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