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
|
| MeSH Number(s) |
D08.811.464.938
|
| 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.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2002 | 1 | 0 | 1 |
| 2007 | 0 | 1 | 1 |
| 2008 | 1 | 0 | 1 |
| 2009 | 2 | 0 | 2 |
| 2011 | 0 | 1 | 1 |
| 2017 | 0 | 1 | 1 |
| 2020 | 1 | 0 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "Ubiquitin-Protein Ligase Complexes" by people in Profiles.
-
Au WC, Zhang T, Mishra PK, Eisenstatt JR, Walker RL, Ocampo J, Dawson A, Warren J, Costanzo M, Baryshnikova A, Flick K, Clark DJ, Meltzer PS, Baker RE, Myers C, Boone C, Kaiser P, Basrai MA. Skp, Cullin, F-box (SCF)-Met30 and SCF-Cdc4-Mediated Proteolysis of CENP-A Prevents Mislocalization of CENP-A for Chromosomal Stability in Budding Yeast. PLoS Genet. 2020 02; 16(2):e1008597.
-
Escamilla CO, Filonova I, Walker AK, Xuan ZX, Holehonnur R, Espinosa F, Liu S, Thyme SB, L?pez-Garc?a IA, Mendoza DB, Usui N, Ellegood J, Eisch AJ, Konopka G, Lerch JP, Schier AF, Speed HE, Powell CM. Kctd13 deletion reduces synaptic transmission via increased RhoA. Nature. 2017 11 09; 551(7679):227-231.
-
Kong Y, Cui H, Zhang H. Smurf2-mediated ubiquitination and degradation of Id1 regulates p16 expression during senescence. Aging Cell. 2011 Dec; 10(6):1038-46.
-
Benanti JA, Matyskiela ME, Morgan DO, Toczyski DP. Functionally distinct isoforms of Cik1 are differentially regulated by APC/C-mediated proteolysis. Mol Cell. 2009 Mar 13; 33(5):581-90.
-
Torres MP, Lee MJ, Ding F, Purbeck C, Kuhlman B, Dokholyan NV, Dohlman HG. G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase. J Biol Chem. 2009 Mar 27; 284(13):8940-50.
-
Benanti JA, Toczyski DP. Cdc20, an activator at last. Mol Cell. 2008 Nov 21; 32(4):460-1.
-
Man C, Rosa J, Yip YL, Cheung AL, Kwong YL, Doxsey SJ, Tsao SW. Id1 overexpression induces tetraploidization and multiple abnormal mitotic phenotypes by modulating aurora A. Mol Biol Cell. 2008 Jun; 19(6):2389-401.
-
Tran K, Mahr JA, Choi J, Teodoro JG, Green MR, Spector DH. Accumulation of substrates of the anaphase-promoting complex (APC) during human cytomegalovirus infection is associated with the phosphorylation of Cdh1 and the dissociation and relocalization of APC subunits. J Virol. 2008 Jan; 82(1):529-37.
-
Vega LR, Phillips JA, Thornton BR, Benanti JA, Onigbanjo MT, Toczyski DP, Zakian VA. Sensitivity of yeast strains with long G-tails to levels of telomere-bound telomerase. PLoS Genet. 2007 Jun; 3(6):e105.
-
Medina R, van Wijnen AJ, Stein GS, Stein JL. The histone gene transcription factor HiNF-P stabilizes its cell cycle regulatory co-activator p220NPAT. Biochemistry. 2006 Dec 26; 45(51):15915-20.