 Ubiquitin
"Ubiquitin" 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.
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
| Descriptor ID |
D025801
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| MeSH Number(s) |
D12.776.947.500
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| Concept/Terms |
Ubiquitin- Ubiquitin
- HMG-20
- High Mobility Protein 20
- APF-1
- ATP-Dependent Proteolysis Factor 1
- ATP Dependent Proteolysis Factor 1
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Below are MeSH descriptors whose meaning is more general than "Ubiquitin".
Below are MeSH descriptors whose meaning is more specific than "Ubiquitin".
This graph shows the total number of publications written about "Ubiquitin" by people in UAMS Profiles by year, and whether "Ubiquitin" 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 |
|---|
| 2020 | 1 | 1 | 2 | | 2019 | 0 | 2 | 2 | | 2018 | 0 | 2 | 2 | | 2015 | 0 | 1 | 1 | | 2014 | 0 | 1 | 1 | | 2013 | 1 | 2 | 3 | | 2012 | 0 | 1 | 1 | | 2011 | 2 | 0 | 2 | | 2010 | 2 | 0 | 2 | | 2008 | 2 | 1 | 3 | | 2007 | 1 | 0 | 1 | | 2006 | 2 | 1 | 3 | | 2005 | 3 | 1 | 4 | | 2004 | 1 | 1 | 2 | | 2003 | 0 | 3 | 3 | | 2002 | 1 | 0 | 1 |
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Below are the most recent publications written about "Ubiquitin" by people in Profiles over the past ten years.
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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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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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Zhao M, Nanbo A, Becnel D, Qin Z, Morris GF, Li L, Lin Z. Ubiquitin Modification of the Epstein-Barr Virus Immediate Early Transactivator Zta. J Virol. 2020 10 27; 94(22).
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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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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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Wang L, Howell MEA, Sparks-Wallace A, Hawkins C, Nicksic CA, Kohne C, Hall KH, Moorman JP, Yao ZQ, Ning S. p62-mediated Selective autophagy endows virus-transformed cells with insusceptibility to DNA damage under oxidative stress. PLoS Pathog. 2019 04; 15(4):e1007541.
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Balasubramaniam M, Ayyadevara S, Shmookler Reis RJ. Structural insights into pro-aggregation effects of C. elegans CRAM-1 and its human ortholog SERF2. Sci Rep. 2018 10 05; 8(1):14891.
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Hyer ML, Milhollen MA, Ciavarri J, Fleming P, Traore T, Sappal D, Huck J, Shi J, Gavin J, Brownell J, Yang Y, Stringer B, Griffin R, Bruzzese F, Soucy T, Duffy J, Rabino C, Riceberg J, Hoar K, Lublinsky A, Menon S, Sintchak M, Bump N, Pulukuri SM, Langston S, Tirrell S, Kuranda M, Veiby P, Newcomb J, Li P, Wu JT, Powe J, Dick LR, Greenspan P, Galvin K, Manfredi M, Claiborne C, Amidon BS, Bence NF. A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment. Nat Med. 2018 02; 24(2):186-193.
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O'Connor HF, Lyon N, Leung JW, Agarwal P, Swaim CD, Miller KM, Huibregtse JM. Ubiquitin-Activated Interaction Traps (UBAITs) identify E3 ligase binding partners. EMBO Rep. 2015 Dec; 16(12):1699-712.
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Penthala NR, Crooks PA, Freeman ML, Sekhar KR. Development and validation of a novel assay to identify radiosensitizers that target nucleophosmin 1. Bioorg Med Chem. 2015 Jul 01; 23(13):3681-6.
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Ayyadevara S, Balasubramaniam M, Gao Y, Yu LR, Alla R, Shmookler Reis R. Proteins in aggregates functionally impact multiple neurodegenerative disease models by forming proteasome-blocking complexes. Aging Cell. 2015 Feb; 14(1):35-48.
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