 Sumoylation
"Sumoylation" 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 type of POST-TRANSLATIONAL PROTEIN MODIFICATION by SMALL UBIQUITIN-RELATED MODIFIER PROTEINS (also known as SUMO proteins).
| Descriptor ID |
D058207
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| MeSH Number(s) |
G02.111.087.675.871.790.600.925.500 G02.111.087.693.600.775.500 G02.149.115.675.871.790.600.831.500 G02.149.115.693.600.850.500 G03.495.770.871.790.600.831.500 G05.355.315.670.600.831.500
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| Concept/Terms |
Sumoylation- Sumoylation
- Sumoylations
- SUMO-Conjugation
- SUMO Conjugation
- SUMO-Conjugations
|
Below are MeSH descriptors whose meaning is more general than "Sumoylation".
- 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]
- Sumoylation [G02.111.087.675.871.790.600.925.500]
- Protein Modification, Translational [G02.111.087.693]
- Protein Processing, Post-Translational [G02.111.087.693.600]
- Ubiquitination [G02.111.087.693.600.775]
- Sumoylation [G02.111.087.693.600.775.500]
- 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]
- Sumoylation [G02.149.115.675.871.790.600.831.500]
- Protein Modification, Translational [G02.149.115.693]
- Protein Processing, Post-Translational [G02.149.115.693.600]
- Ubiquitination [G02.149.115.693.600.850]
- Sumoylation [G02.149.115.693.600.850.500]
- 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]
- Sumoylation [G03.495.770.871.790.600.831.500]
- 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]
- Sumoylation [G05.355.315.670.600.831.500]
Below are MeSH descriptors whose meaning is more specific than "Sumoylation".
This graph shows the total number of publications written about "Sumoylation" by people in UAMS Profiles by year, and whether "Sumoylation" 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 |
|---|
| 2021 | 1 | 1 | 2 | | 2020 | 0 | 1 | 1 | | 2019 | 0 | 1 | 1 | | 2018 | 0 | 2 | 2 | | 2016 | 1 | 1 | 2 | | 2015 | 2 | 1 | 3 | | 2014 | 0 | 2 | 2 | | 2013 | 0 | 1 | 1 | | 2012 | 1 | 2 | 3 | | 2011 | 1 | 1 | 2 | | 2010 | 2 | 0 | 2 |
To return to the timeline, click here.
Below are the most recent publications written about "Sumoylation" by people in Profiles over the past ten years.
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Chen X, Zhang Y, Ren X, Su Q, Liu Y, Dang X, Qin Y, Yang X, Xing Z, Shen Y, Wang Y, Bai Z, Yeh ETH, Wu H, Qi Y. The SUMO-specific protease SENP2 plays an essential role in the regulation of Kv7.2 and Kv7.3 potassium channels. J Biol Chem. 2021 10; 297(4):101183.
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Chen X, Qin Y, Zhang Y, Yang X, Xing Z, Shen Y, Cheng J, Yeh ETH, Wu H, Qi Y. SENP2-PLC?4 signaling regulates neurogenesis through the maintenance of calcium homeostasis. Cell Death Differ. 2022 02; 29(2):337-350.
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Traver G, Sekhar KR, Crooks PA, Keeney DS, Freeman ML. Targeting NPM1 in irradiated cells inhibits NPM1 binding to RAD51, RAD51 foci formation and radiosensitizes NSCLC. Cancer Lett. 2021 03 01; 500:220-227.
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Abe JI, Ko KA, Kotla S, Wang Y, Paez-Mayorga J, Shin IJ, Imanishi M, Vu HT, Tao Y, Leiva-Juarez MM, Thomas TN, Medina JL, Won JH, Fujii Y, Giancursio CJ, McBeath E, Shin JH, Guzman L, Abe RJ, Taunton J, Mochizuki N, Faubion W, Cooke JP, Fujiwara K, Evans SE, Le NT. MAGI1 as a link between endothelial activation and ER stress drives atherosclerosis. JCI Insight. 2019 04 04; 4(7).
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Lao Y, Yang K, Wang Z, Sun X, Zou Q, Yu X, Cheng J, Tong X, Yeh ETH, Yang J, Yi J. DeSUMOylation of MKK7 kinase by the SUMO2/3 protease SENP3 potentiates lipopolysaccharide-induced inflammatory signaling in macrophages. J Biol Chem. 2018 03 16; 293(11):3965-3980.
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Li J, Lu D, Dou H, Liu H, Weaver K, Wang W, Li J, Yeh ETH, Williams BO, Zheng L, Yang T. Desumoylase SENP6 maintains osteochondroprogenitor homeostasis by suppressing the p53 pathway. Nat Commun. 2018 01 10; 9(1):143.
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Zhou Z, Wang M, Li J, Xiao M, Chin YE, Cheng J, Yeh ET, Yang J, Yi J. SUMOylation and SENP3 regulate STAT3 activation in head and neck cancer. Oncogene. 2016 11 10; 35(45):5826-5838.
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Huang C, Cheng J, Bawa-Khalfe T, Yao X, Chin YE, Yeh ETH. SUMOylated ORC2 Recruits a Histone Demethylase to Regulate Centromeric Histone Modification and Genomic Stability. Cell Rep. 2016 Apr 05; 15(1):147-157.
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Ferdaoussi M, Dai X, Jensen MV, Wang R, Peterson BS, Huang C, Ilkayeva O, Smith N, Miller N, Hajmrle C, Spigelman AF, Wright RC, Plummer G, Suzuki K, Mackay JP, van de Bunt M, Gloyn AL, Ryan TE, Norquay LD, Brosnan MJ, Trimmer JK, Rolph TP, Kibbey RG, Manning Fox JE, Colmers WF, Shirihai OS, Neufer PD, Yeh ET, Newgard CB, MacDonald PE. Isocitrate-to-SENP1 signaling amplifies insulin secretion and rescues dysfunctional ? cells. J Clin Invest. 2015 Oct 01; 125(10):3847-60.
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Ritho J, Arold ST, Yeh ET. A Critical SUMO1 Modification of LKB1 Regulates AMPK Activity during Energy Stress. Cell Rep. 2015 Aug 04; 12(5):734-42.
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Heo KS, Le NT, Cushman HJ, Giancursio CJ, Chang E, Woo CH, Sullivan MA, Taunton J, Yeh ET, Fujiwara K, Abe J. Disturbed flow-activated p90RSK kinase accelerates atherosclerosis by inhibiting SENP2 function. J Clin Invest. 2015 Mar 02; 125(3):1299-310.
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