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 UAMS Profiles 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 |
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2024 | 1 | 2 | 3 | 2021 | 1 | 2 | 3 | 2020 | 1 | 3 | 4 | 2019 | 1 | 3 | 4 | 2018 | 1 | 1 | 2 | 2016 | 1 | 2 | 3 | 2015 | 0 | 1 | 1 | 2013 | 1 | 0 | 1 | 2012 | 1 | 2 | 3 | 2011 | 0 | 2 | 2 | 2010 | 0 | 4 | 4 | 2008 | 0 | 1 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "Ubiquitination" by people in Profiles over the past ten years.
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Xiao Y, Yuan Y, Liu Y, Lin Z, Zheng G, Zhou D, Lv D. Targeted Protein Degradation: Current and Emerging Approaches for E3 Ligase Deconvolution. J Med Chem. 2024 Jul 25; 67(14):11580-11596.
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Kelliher JL, Folkerts ML, Shen KV, Song W, Tengler K, Stiefel CM, Lee SO, Dray E, Zhao W, Koss B, Pannunzio NR, Leung JW. Evolved histone tail regulates 53BP1 recruitment at damaged chromatin. Nat Commun. 2024 May 31; 15(1):4634.
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Espejo-Serrano C, Aitken C, Tan BF, May DG, Chrisopulos RJ, Roux KJ, Demmers JA, Mackintosh SG, Gribnau J, Bustos F, Gontan C, Findlay GM. Chromatin targeting of the RNF12/RLIM E3 ubiquitin ligase controls transcriptional responses. Life Sci Alliance. 2024 03; 7(3).
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Lee SO, Kelliher JL, Song W, Tengler K, Sarkar A, Dray E, Leung JWC. UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination and DNA repair. J Biol Chem. 2023 08; 299(8):105043.
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Lv D, Pal P, Liu X, Jia Y, Thummuri D, Zhang P, Hu W, Pei J, Zhang Q, Zhou S, Khan S, Zhang X, Hua N, Yang Q, Arango S, Zhang W, Nayak D, Olsen SK, Weintraub ST, Hromas R, Konopleva M, Yuan Y, Zheng G, Zhou D. Development of a BCL-xL and BCL-2 dual degrader with improved anti-leukemic activity. Nat Commun. 2021 11 25; 12(1):6896.
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Li C, Xia J, Franqui-Machin R, Chen F, He Y, Ashby TC, Teng F, Xu H, Liu D, Gai D, Johnson SK, van Rhee F, Janz S, Shaughnessy JD, Tricot G, Frech I, Zhan F. TRIP13 modulates protein deubiquitination and accelerates tumor development and progression of B cell malignancies. J Clin Invest. 2021 07 15; 131(14).
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Kelliher J, Ghosal G, Leung JWC. New answers to the old RIDDLE: RNF168 and the DNA damage response pathway. FEBS J. 2022 05; 289(9):2467-2480.
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Kang JW, Zhan Z, Ji G, Sang Y, Zhou D, Li Y, Feng H, Cheng T. PUMA facilitates EMI1-promoted cytoplasmic Rad51 ubiquitination and inhibits DNA repair in stem and progenitor cells. Signal Transduct Target Ther. 2021 03 31; 6(1):129.
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Gu C, Lu T, Wang W, Shao M, Wei R, Guo M, Li R, Qiao L, Hu Y, Zhan F, Seckinger A, Hose D, Yang Y. RFWD2 induces cellular proliferation and selective proteasome inhibitor resistance by mediating P27 ubiquitination in multiple myeloma. Leukemia. 2021 06; 35(6):1803-1807.
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He Y, Khan S, Huo Z, Lv D, Zhang X, Liu X, Yuan Y, Hromas R, Xu M, Zheng G, Zhou D. Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies. J Hematol Oncol. 2020 07 27; 13(1):103.
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Kelliher JL, West KL, Gong Q, Leung JWC. Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination. Nat Commun. 2020 05 18; 11(1):2462.
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He Y, Li W, Lv D, Zhang X, Zhang X, Ortiz YT, Budamagunta V, Campisi J, Zheng G, Zhou D. Inhibition of USP7 activity selectively eliminates senescent cells in part via restoration of p53 activity. Aging Cell. 2020 03; 19(3):e13117.
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Balasubramaniam M, Parcon PA, Bose C, Liu L, Jones RA, Farlow MR, Mrak RE, Barger SW, Griffin WST. Interleukin-1? drives NEDD8 nuclear-to-cytoplasmic translocation, fostering parkin activation via NEDD8 binding to the P-ubiquitin activating site. J Neuroinflammation. 2019 Dec 27; 16(1):275.
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Miah S, Banks CAS, Ogunbolude Y, Bagu ET, Berg JM, Saraf A, Tettey TT, Hattem G, Dayebgadoh G, Kempf CG, Sardiu M, Napper S, Florens L, Lukong KE, Washburn MP. BRK phosphorylates SMAD4 for proteasomal degradation and inhibits tumor suppressor FRK to control SNAIL, SLUG, and metastatic potential. Sci Adv. 2019 10; 5(10):eaaw3113.
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Liang F, Miller AS, Longerich S, Tang C, Maranon D, Williamson EA, Hromas R, Wiese C, Kupfer GM, Sung P. DNA requirement in FANCD2 deubiquitination by USP1-UAF1-RAD51AP1 in the Fanconi anemia DNA damage response. Nat Commun. 2019 06 28; 10(1):2849.
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Cho JJ, Xu Z, Parthasarathy U, Drashansky TT, Helm EY, Zuniga AN, Lorentsen KJ, Mansouri S, Cho JY, Edelmann MJ, Duong DM, Gehring T, Seeholzer T, Krappmann D, Uddin MN, Califano D, Wang RL, Jin L, Li H, Lv D, Zhou D, Zhou L, Avram D. Hectd3 promotes pathogenic Th17 lineage through Stat3 activation and Malt1 signaling in neuroinflammation. Nat Commun. 2019 02 11; 10(1):701.
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Chen Y, Hou Y, Yang J, Du R, Chen C, Chen F, Wang H, Ge R, Chen J. P75 Involved in the Ubiquitination of a-synuclein in Rotenone-based Parkinson's Disease Models. Neuroscience. 2018 09 15; 388:367-373.
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Franqui-Machin R, Hao M, Bai H, Gu Z, Zhan X, Habelhah H, Jethava Y, Qiu L, Frech I, Tricot G, Zhan F. Destabilizing NEK2 overcomes resistance to proteasome inhibition in multiple myeloma. J Clin Invest. 2018 07 02; 128(7):2877-2893.
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Gulia R, Sharma R, Bhattacharyya S. A Critical Role for Ubiquitination in the Endocytosis of Glutamate Receptors. J Biol Chem. 2017 01 27; 292(4):1426-1437.
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Atanassov BS, Mohan RD, Lan X, Kuang X, Lu Y, Lin K, McIvor E, Li W, Zhang Y, Florens L, Byrum SD, Mackintosh SG, Calhoun-Davis T, Koutelou E, Wang L, Tang DG, Tackett AJ, Washburn MP, Workman JL, Dent SY. ATXN7L3 and ENY2 Coordinate Activity of Multiple H2B Deubiquitinases Important for Cellular Proliferation and Tumor Growth. Mol Cell. 2016 05 19; 62(4):558-71.
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Casta?eda CA, Dixon EK, Walker O, Chaturvedi A, Nakasone MA, Curtis JE, Reed MR, Krueger S, Cropp TA, Fushman D. Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins. Structure. 2016 Mar 01; 24(3):423-36.
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Ranek MJ, Zheng H, Huang W, Kumarapeli AR, Li J, Liu J, Wang X. Genetically induced moderate inhibition of 20S proteasomes in cardiomyocytes facilitates heart failure in mice during systolic overload. J Mol Cell Cardiol. 2015 Aug; 85:273-81.
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