 Ubiquitination
"Ubiquitination" 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.
The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.
| Descriptor ID |
D054875
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| MeSH Number(s) |
G02.111.087.675.871.790.600.925 G02.111.087.693.600.775 G02.149.115.675.871.790.600.831 G02.149.115.693.600.850 G03.495.770.871.790.600.831 G05.355.315.670.600.831
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| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Ubiquitination".
- Biological Sciences [G]
- Chemical Phenomena [G02]
- Biochemical Phenomena [G02.111]
- Biochemical Processes [G02.111.087]
- Peptide Biosynthesis [G02.111.087.675]
- Protein Biosynthesis [G02.111.087.675.871]
- Protein Modification, Translational [G02.111.087.675.871.790]
- Protein Processing, Post-Translational [G02.111.087.675.871.790.600]
- Ubiquitination [G02.111.087.675.871.790.600.925]
- Protein Modification, Translational [G02.111.087.693]
- Protein Processing, Post-Translational [G02.111.087.693.600]
- Ubiquitination [G02.111.087.693.600.775]
- Chemical Processes [G02.149]
- Biochemical Processes [G02.149.115]
- Peptide Biosynthesis [G02.149.115.675]
- Protein Biosynthesis [G02.149.115.675.871]
- Protein Modification, Translational [G02.149.115.675.871.790]
- Protein Processing, Post-Translational [G02.149.115.675.871.790.600]
- Ubiquitination [G02.149.115.675.871.790.600.831]
- Protein Modification, Translational [G02.149.115.693]
- Protein Processing, Post-Translational [G02.149.115.693.600]
- Ubiquitination [G02.149.115.693.600.850]
- Metabolic Phenomena [G03]
- Metabolism [G03.495]
- Peptide Biosynthesis [G03.495.770]
- Protein Biosynthesis [G03.495.770.871]
- Protein Modification, Translational [G03.495.770.871.790]
- Protein Processing, Post-Translational [G03.495.770.871.790.600]
- Ubiquitination [G03.495.770.871.790.600.831]
- Genetic Phenomena [G05]
- Genetic Processes [G05.355]
- Gene Expression Regulation [G05.355.315]
- Protein Modification, Translational [G05.355.315.670]
- Protein Processing, Post-Translational [G05.355.315.670.600]
- Ubiquitination [G05.355.315.670.600.831]
Below are MeSH descriptors whose meaning is more specific than "Ubiquitination".
This graph shows the total number of publications written about "Ubiquitination" by people in this website by year, and whether "Ubiquitination" 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 |
|---|
| 2009 | 0 | 2 | 2 | | 2010 | 1 | 1 | 2 | | 2013 | 0 | 1 | 1 | | 2014 | 0 | 2 | 2 | | 2015 | 0 | 5 | 5 |
To return to the timeline, click here.
Below are the most recent publications written about "Ubiquitination" by people in Profiles.
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Canning P, Ruan Q, Schwerd T, Hrdinka M, Maki JL, Saleh D, Suebsuwong C, Ray S, Brennan PE, Cuny GD, Uhlig HH, Gyrd-Hansen M, Degterev A, Bullock AN. Inflammatory Signaling by NOD-RIPK2 Is Inhibited by Clinically Relevant Type II Kinase Inhibitors. Chem Biol. 2015 Sep 17; 22(9):1174-84.
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Krist DT, Statsyuk AV. Catalytically Important Residues of E6AP Ubiquitin Ligase Identified Using Acid-Cleavable Photo-Cross-Linkers. Biochemistry. 2015 Jul 28; 54(29):4411-4.
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Dulloo I, Phang BH, Othman R, Tan SY, Vijayaraghavan A, Goh LK, Martin-Lopez M, Marques MM, Li CW, Wang de Y, Marín MC, Xian W, McKeon F, Sabapathy K. Hypoxia-inducible TAp73 supports tumorigenesis by regulating the angiogenic transcriptome. Nat Cell Biol. 2015 Apr; 17(4):511-23.
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Murray AR, Vuong L, Brobst D, Fliesler SJ, Peachey NS, Gorbatyuk MS, Naash MI, Al-Ubaidi MR. Glycosylation of rhodopsin is necessary for its stability and incorporation into photoreceptor outer segment discs. Hum Mol Genet. 2015 May 15; 24(10):2709-23.
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Lee S, Lee TA, Lee E, Kang S, Park A, Kim SW, Park HJ, Yoon JH, Ha SJ, Park T, Lee JS, Cheon JH, Park B. Identification of a subnuclear body involved in sequence-specific cytokine RNA processing. Nat Commun. 2015 Jan 05; 6:5791.
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van den Boomen DJ, Timms RT, Grice GL, Stagg HR, Skødt K, Dougan G, Nathan JA, Lehner PJ. TMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I. Proc Natl Acad Sci U S A. 2014 Aug 05; 111(31):11425-30.
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An H, Krist DT, Statsyuk AV. Crosstalk between kinases and Nedd4 family ubiquitin ligases. Mol Biosyst. 2014 Jul; 10(7):1643-57.
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Mistry H, Hsieh G, Buhrlage SJ, Huang M, Park E, Cuny GD, Galinsky I, Stone RM, Gray NS, D'Andrea AD, Parmar K. Small-molecule inhibitors of USP1 target ID1 degradation in leukemic cells. Mol Cancer Ther. 2013 Dec; 12(12):2651-62.
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Schwarz LA, Hall BJ, Patrick GN. Activity-dependent ubiquitination of GluA1 mediates a distinct AMPA receptor endocytosis and sorting pathway. J Neurosci. 2010 Dec 08; 30(49):16718-29.
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Farmer LM, Book AJ, Lee KH, Lin YL, Fu H, Vierstra RD. The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis. Plant Cell. 2010 Jan; 22(1):124-42.
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