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 |
|---|
| 1995 | 0 | 1 | 1 |
| 1996 | 1 | 0 | 1 |
| 2000 | 1 | 0 | 1 |
| 2001 | 3 | 0 | 3 |
| 2002 | 3 | 0 | 3 |
| 2003 | 2 | 0 | 2 |
| 2005 | 0 | 1 | 1 |
| 2006 | 1 | 0 | 1 |
| 2022 | 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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A peroxisomal ubiquitin ligase complex forms a retrotranslocation channel. Nature. 2022 07; 607(7918):374-380.
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The Cdc34/SCF ubiquitination complex mediates Saccharomyces cerevisiae cell wall integrity. Genetics. 2006 Dec; 174(4):1825-39.
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Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Proc Natl Acad Sci U S A. 2005 Dec 27; 102(52):18890-5.
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Herpes simplex virus 1 mutant in which the ICP0 HUL-1 E3 ubiquitin ligase site is disrupted stabilizes cdc34 but degrades D-type cyclins and exhibits diminished neurotoxicity. J Virol. 2003 Dec; 77(24):13194-202.
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Cdc34 self-association is facilitated by ubiquitin thiolester formation and is required for its catalytic activity. Mol Cell Biol. 2003 Aug; 23(15):5388-400.
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Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0. Proc Natl Acad Sci U S A. 2002 Jun 11; 99(12):7889-94.
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Cytokinesis: regulated by destruction. Curr Biol. 2002 May 14; 12(10):R344-6.
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Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes. Proc Natl Acad Sci U S A. 2002 Jan 22; 99(2):631-6.
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APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Mol Biol Cell. 2001 Dec; 12(12):3839-51.
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Creation of a pluripotent ubiquitin-conjugating enzyme. Mol Cell Biol. 2001 Oct; 21(19):6537-48.