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 |
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2009 | 0 | 1 | 1 | 2010 | 0 | 1 | 1 | 2011 | 0 | 1 | 1 | 2013 | 0 | 1 | 1 | 2014 | 0 | 1 | 1 | 2015 | 1 | 0 | 1 | 2016 | 0 | 2 | 2 | 2018 | 0 | 1 | 1 | 2020 | 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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Sorensen DW, Carreon D, Williams JM, Pearce WJ. Hypoxic modulation of fetal vascular MLCK abundance, localization, and function. Am J Physiol Regul Integr Comp Physiol. 2021 01 01; 320(1):R1-R18.
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Bianco AC, da Conceição RR. The Deiodinase Trio and Thyroid Hormone Signaling. Methods Mol Biol. 2018; 1801:67-83.
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Jeganathan N, Predescu D, Zhang J, Sha F, Bardita C, Patel M, Wood S, Borgia JA, Balk RA, Predescu S. Rac1-mediated cytoskeleton rearrangements induced by intersectin-1s deficiency promotes lung cancer cell proliferation, migration and metastasis. Mol Cancer. 2016 09 14; 15(1):59.
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Ozden O, Bishehsari F, Bauer J, Park SH, Jana A, Baik SH, Sporn JC, Staudacher JJ, Yazici C, Krett N, Jung B. Expression of an Oncogenic BARD1 Splice Variant Impairs Homologous Recombination and Predicts Response to PARP-1 Inhibitor Therapy in Colon Cancer. Sci Rep. 2016 05 20; 6:26273.
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Werneck de Castro JP, Fonseca TL, Ueta CB, McAninch EA, Abdalla S, Wittmann G, Lechan RM, Gereben B, Bianco AC. Differences in hypothalamic type 2 deiodinase ubiquitination explain localized sensitivity to thyroxine. J Clin Invest. 2015 Feb; 125(2):769-81.
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Li S, Shu B, Zhang Y, Li J, Guo J, Wang Y, Ren F, Xiao G, Chang Z, Chen D. Carboxyl terminus of Hsp70-interacting protein regulation of osteoclast formation in mice through promotion of tumor necrosis factor receptor-associated factor 6 protein degradation. Arthritis Rheumatol. 2014 Jul; 66(7):1854-63.
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Arrojo E Drigo R, Egri P, Jo S, Gereben B, Bianco AC. The type II deiodinase is retrotranslocated to the cytoplasm and proteasomes via p97/Atx3 complex. Mol Endocrinol. 2013 Dec; 27(12):2105-15.
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Arrojo E Drigo R, Bianco AC. Type 2 deiodinase at the crossroads of thyroid hormone action. Int J Biochem Cell Biol. 2011 Oct; 43(10):1432-41.
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Duan L, Raja SM, Chen G, Virmani S, Williams SH, Clubb RJ, Mukhopadhyay C, Rainey MA, Ying G, Dimri M, Chen J, Reddi AL, Naramura M, Band V, Band H. Negative regulation of EGFR-Vav2 signaling axis by Cbl ubiquitin ligase controls EGF receptor-mediated epithelial cell adherens junction dynamics and cell migration. J Biol Chem. 2011 Jan 07; 286(1):620-33.
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Zavacki AM, Arrojo E Drigo R, Freitas BC, Chung M, Harney JW, Egri P, Wittmann G, Fekete C, Gereben B, Bianco AC. The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase. Mol Cell Biol. 2009 Oct; 29(19):5339-47.
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