 Sirtuin 2
"Sirtuin 2" 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 sirtuin family member found primarily in the CYTOPLASM. It is a multifunctional enzyme that contains a NAD-dependent deacetylase activity that is specific for HISTONES and a mono-ADP-ribosyltransferase activity.
| Descriptor ID |
D056565
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| MeSH Number(s) |
D08.811.277.087.520.200.650.200 D08.811.913.400.725.115.961.200 D12.776.476.900.200
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| Concept/Terms |
Sirtuin 2- Sirtuin 2
- Silent Mating Type Information Regulation 2 Homolog 2
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Below are MeSH descriptors whose meaning is more general than "Sirtuin 2".
Below are MeSH descriptors whose meaning is more specific than "Sirtuin 2".
This graph shows the total number of publications written about "Sirtuin 2" by people in this website by year, and whether "Sirtuin 2" 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 |
|---|
| 1997 | 0 | 1 | 1 | | 2012 | 1 | 0 | 1 | | 2014 | 2 | 0 | 2 | | 2016 | 1 | 0 | 1 | | 2018 | 3 | 0 | 3 |
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Below are the most recent publications written about "Sirtuin 2" by people in Profiles.
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Huang H, Zhang D, Wang Y, Perez-Neut M, Han Z, Zheng YG, Hao Q, Zhao Y. Lysine benzoylation is a histone mark regulated by SIRT2. Nat Commun. 2018 08 28; 9(1):3374.
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Sarikhani M, Mishra S, Maity S, Kotyada C, Wolfgeher D, Gupta MP, Singh M, Sundaresan NR. SIRT2 deacetylase regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation. Elife. 2018 03 05; 7.
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Sarikhani M, Mishra S, Desingu PA, Kotyada C, Wolfgeher D, Gupta MP, Singh M, Sundaresan NR. SIRT2 regulates oxidative stress-induced cell death through deacetylation of c-Jun NH2-terminal kinase. Cell Death Differ. 2018 09; 25(9):1638-1656.
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Ai T, Wilson DJ, More SS, Xie J, Chen L. 5-((3-Amidobenzyl)oxy)nicotinamides as Sirtuin 2 Inhibitors. J Med Chem. 2016 Apr 14; 59(7):2928-41.
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Cui H, Kamal Z, Ai T, Xu Y, More SS, Wilson DJ, Chen L. Discovery of potent and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach. J Med Chem. 2014 Oct 23; 57(20):8340-57.
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Ming M, Qiang L, Zhao B, He YY. Mammalian SIRT2 inhibits keratin 19 expression and is a tumor suppressor in skin. Exp Dermatol. 2014 Mar; 23(3):207-9.
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Narayan N, Lee IH, Borenstein R, Sun J, Wong R, Tong G, Fergusson MM, Liu J, Rovira II, Cheng HL, Wang G, Gucek M, Lombard D, Alt FW, Sack MN, Murphy E, Cao L, Finkel T. The NAD-dependent deacetylase SIRT2 is required for programmed necrosis. Nature. 2012 Dec 13; 492(7428):199-204.
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Gossett AJ, Lieb JD. In vivo effects of histone H3 depletion on nucleosome occupancy and position in Saccharomyces cerevisiae. PLoS Genet. 2012; 8(6):e1002771.
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Deshmukh AS, Srivastava S, Herrmann S, Gupta A, Mitra P, Gilberger TW, Dhar SK. The role of N-terminus of Plasmodium falciparum ORC1 in telomeric localization and var gene silencing. Nucleic Acids Res. 2012 Jul; 40(12):5313-31.
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Hickman MA, Froyd CA, Rusche LN. Reinventing heterochromatin in budding yeasts: Sir2 and the origin recognition complex take center stage. Eukaryot Cell. 2011 Sep; 10(9):1183-92.
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