 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 |
|---|
| 2007 | 0 | 1 | 1 | | 2008 | 0 | 3 | 3 | | 2009 | 1 | 6 | 7 | | 2010 | 2 | 2 | 4 | | 2011 | 3 | 6 | 9 | | 2012 | 1 | 6 | 7 | | 2013 | 1 | 3 | 4 | | 2014 | 0 | 6 | 6 | | 2015 | 3 | 3 | 6 | | 2016 | 0 | 5 | 5 | | 2017 | 1 | 3 | 4 | | 2018 | 0 | 5 | 5 | | 2019 | 0 | 1 | 1 | | 2020 | 0 | 3 | 3 | | 2021 | 1 | 3 | 4 | | 2022 | 0 | 1 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "Ubiquitination" by people in Profiles.
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Stormo AED, Shavarebi F, FitzGibbon M, Earley EM, Ahrendt H, Lum LS, Verschueren E, Swaney DL, Skibinski G, Ravisankar A, van Haren J, Davis EJ, Johnson JR, Von Dollen J, Balen C, Porath J, Crosio C, Mirescu C, Iaccarino C, Dauer WT, Nichols RJ, Wittmann T, Cox TC, Finkbeiner S, Krogan NJ, Oakes SA, Hiniker A. The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its localization, degradation, and toxicity. J Cell Biol. 2022 04 04; 221(4).
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Wei J, Harada BT, Lu D, Ma R, Gao B, Xu Y, Montauti E, Mani N, Chaudhuri SM, Gregory S, Weinberg SE, Zhang DD, Green R, He C, Fang D. HRD1-mediated METTL14 degradation regulates m6A mRNA modification to suppress ER proteotoxic liver disease. Mol Cell. 2021 12 16; 81(24):5052-5065.e6.
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Pan M, Zheng Q, Wang T, Liang L, Mao J, Zuo C, Ding R, Ai H, Xie Y, Si D, Yu Y, Liu L, Zhao M. Structural insights into Ubr1-mediated N-degron polyubiquitination. Nature. 2021 12; 600(7888):334-338.
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Yu Y, Zheng Q, Erramilli SK, Pan M, Park S, Xie Y, Li J, Fei J, Kossiakoff AA, Liu L, Zhao M. K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle. Nat Chem Biol. 2021 08; 17(8):896-905.
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Tokamov SA, Su T, Ullyot A, Fehon RG. Negative feedback couples Hippo pathway activation with Kibra degradation independent of Yorkie-mediated transcription. Elife. 2021 02 08; 10.
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Wu L, Crawley CD, Garofalo A, Nichols JW, Campbell PA, Khramtsova GF, Olopade OI, Weichselbaum RR, Yamini B. p50 mono-ubiquitination and interaction with BARD1 regulates cell cycle progression and maintains genome stability. Nat Commun. 2020 10 06; 11(1):5007.
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Kang T, Boland BB, Jensen P, Alarcon C, Nawrocki A, Grimsby JS, Rhodes CJ, Larsen MR. Characterization of Signaling Pathways Associated with Pancreatic ß-cell Adaptive Flexibility in Compensation of Obesity-linked Diabetes in db/db Mice. Mol Cell Proteomics. 2020 06; 19(6):971-993.
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Kong D, Wan Q, Li J, Zuo S, Liu G, Liu Q, Wang C, Bai P, Duan SZ, Zhou B, Gounari F, Lyu A, Lazarus M, Breyer RM, Yu Y. DP1 Activation Reverses Age-Related Hypertension Via NEDD4L-Mediated T-Bet Degradation in T Cells. Circulation. 2020 02 25; 141(8):655-666.
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Serman TM, Gack MU. FBXO38 Drives PD-1 to Destruction. Trends Immunol. 2019 02; 40(2):81-83.
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Full F, van Gent M, Sparrer KMJ, Chiang C, Zurenski MA, Scherer M, Brockmeyer NH, Heinzerling L, Stürzl M, Korn K, Stamminger T, Ensser A, Gack MU. Centrosomal protein TRIM43 restricts herpesvirus infection by regulating nuclear lamina integrity. Nat Microbiol. 2019 01; 4(1):164-176.
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