 Ubiquitin-Protein Ligases
"Ubiquitin-Protein Ligases" 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 diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
| Descriptor ID |
D044767
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| MeSH Number(s) |
D08.811.464.938.750
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| Concept/Terms |
Ubiquitin-Protein Ligases- Ubiquitin-Protein Ligases
- Ligases, Ubiquitin-Protein
- Ubiquitin Protein Ligases
- Ubiquitin-Protein Ligase E3
- Ligase E3, Ubiquitin-Protein
- Ubiquitin Protein Ligase E3
- Ubiquitin Ligase E3
- E3, Ubiquitin Ligase
- Ligase E3, Ubiquitin
- Ubiquitin-Protein Ligase
- Ligase, Ubiquitin-Protein
- Ubiquitin Protein Ligase
- E3 Ligase
- Ligase, E3
- E3 Ubiquitin Ligase
- Ligase, E3 Ubiquitin
- Ubiquitin Ligase, E3
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Below are MeSH descriptors whose meaning is more general than "Ubiquitin-Protein Ligases".
Below are MeSH descriptors whose meaning is more specific than "Ubiquitin-Protein Ligases".
This graph shows the total number of publications written about "Ubiquitin-Protein Ligases" by people in this website by year, and whether "Ubiquitin-Protein Ligases" 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 |
|---|
| 2003 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 | | 2008 | 2 | 0 | 2 | | 2011 | 1 | 0 | 1 | | 2015 | 1 | 0 | 1 | | 2018 | 1 | 0 | 1 |
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Below are the most recent publications written about "Ubiquitin-Protein Ligases" by people in Profiles.
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Oser MG, Fonseca R, Chakraborty AA, Brough R, Spektor A, Jennings RB, Flaifel A, Novak JS, Gulati A, Buss E, Younger ST, McBrayer SK, Cowley GS, Bonal DM, Nguyen QD, Brulle-Soumare L, Taylor P, Cairo S, Ryan CJ, Pease EJ, Maratea K, Travers J, Root DE, Signoretti S, Pellman D, Ashton S, Lord CJ, Barry ST, Kaelin WG. Cells Lacking the RB1 Tumor Suppressor Gene Are Hyperdependent on Aurora B Kinase for Survival. Cancer Discov. 2019 02; 9(2):230-247.
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Andreoletti G, Shakhnovich V, Christenson K, Coelho T, Haggarty R, Afzal NA, Batra A, Petersen BS, Mort M, Beattie RM, Ennis S. Exome Analysis of Rare and Common Variants within the NOD Signaling Pathway. Sci Rep. 2017 04 19; 7:46454.
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Kathania M, Zeng M, Yadav VN, Moghaddam SJ, Yang B, Venuprasad K. Ndfip1 regulates itch ligase activity and airway inflammation via UbcH7. J Immunol. 2015 Mar 01; 194(5):2160-7.
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Pant V, Xiong S, Iwakuma T, Quint?s-Cardama A, Lozano G. Heterodimerization of Mdm2 and Mdm4 is critical for regulating p53 activity during embryogenesis but dispensable for p53 and Mdm2 stability. Proc Natl Acad Sci U S A. 2011 Jul 19; 108(29):11995-2000.
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Barboza JA, Iwakuma T, Terzian T, El-Naggar AK, Lozano G. Mdm2 and Mdm4 loss regulates distinct p53 activities. Mol Cancer Res. 2008 Jun; 6(6):947-54.
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Perry JM, Li L. Self-renewal versus transformation: Fbxw7 deletion leads to stem cell activation and leukemogenesis. Genes Dev. 2008 May 01; 22(9):1107-9.
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Bittel DC, Kibiryeva N, Talebizadeh Z, Driscoll DJ, Butler MG. Microarray analysis of gene/transcript expression in Angelman syndrome: deletion versus UPD. Genomics. 2005 Jan; 85(1):85-91.
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Iwakuma T, Parant JM, Fasulo M, Zwart E, Jacks T, de Vries A, Lozano G. Mutation at p53 serine 389 does not rescue the embryonic lethality in mdm2 or mdm4 null mice. Oncogene. 2004 Oct 07; 23(46):7644-50.
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Park TJ, Hamanaka H, Ohshima T, Watanabe N, Mikoshiba K, Nukina N. Inhibition of ubiquitin ligase Siah-1A by disabled-1. Biochem Biophys Res Commun. 2003 Mar 21; 302(4):671-8.
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Hermida-Matsumoto ML, Chock PB, Curran T, Yang DC. Ubiquitinylation of transcription factors c-Jun and c-Fos using reconstituted ubiquitinylating enzymes. J Biol Chem. 1996 Mar 01; 271(9):4930-6.
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