 Sirtuins
"Sirtuins" 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 homologous family of regulatory enzymes that are structurally related to the protein silent mating type information regulator 2 (Sir2) found in Saccharomyces cerevisiae. Sirtuins contain a central catalytic core region which binds NAD. Several of the sirtuins utilize NAD to deacetylate proteins such as HISTONES and are categorized as GROUP III HISTONE DEACETYLASES. Several other sirtuin members utilize NAD to transfer ADP-RIBOSE to proteins and are categorized as MONO ADP-RIBOSE TRANSFERASES, while a third group of sirtuins appears to have both deacetylase and ADP ribose transferase activities.
| Descriptor ID |
D037761
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| MeSH Number(s) |
D08.811.277.087.520.200.650 D08.811.913.400.725.115.961 D12.776.476.900
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| Concept/Terms |
Sirtuins- Sirtuins
- Silent Mating Type Information Regulator 2-like Proteins
- Silent Mating Type Information Regulator 2 like Proteins
- Sir2-like Proteins
- Sir2 like Proteins
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Below are MeSH descriptors whose meaning is more general than "Sirtuins".
Below are MeSH descriptors whose meaning is more specific than "Sirtuins".
This graph shows the total number of publications written about "Sirtuins" by people in this website by year, and whether "Sirtuins" 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 | | 2005 | 1 | 0 | 1 | | 2006 | 0 | 1 | 1 | | 2007 | 0 | 1 | 1 | | 2008 | 2 | 0 | 2 | | 2009 | 2 | 0 | 2 | | 2011 | 1 | 1 | 2 | | 2012 | 2 | 0 | 2 | | 2013 | 2 | 1 | 3 | | 2014 | 5 | 0 | 5 | | 2015 | 0 | 1 | 1 | | 2016 | 2 | 2 | 4 | | 2017 | 1 | 1 | 2 | | 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "Sirtuins" by people in Profiles.
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Samant SA, Pillai VB, Gupta MP. Cellular mechanisms promoting cachexia and how they are opposed by sirtuins 1. Can J Physiol Pharmacol. 2019 Apr; 97(4):235-245.
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Samant SA, Kanwal A, Pillai VB, Bao R, Gupta MP. The histone deacetylase SIRT6 blocks myostatin expression and development of muscle atrophy. Sci Rep. 2017 09 19; 7(1):11877.
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Guo Y, Li P, Gao L, Zhang J, Yang Z, Bledsoe G, Chang E, Chao L, Chao J. Kallistatin reduces vascular senescence and aging by regulating microRNA-34a-SIRT1 pathway. Aging Cell. 2017 08; 16(4):837-846.
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Bindu S, Pillai VB, Gupta MP. Role of Sirtuins in Regulating Pathophysiology of the Heart. Trends Endocrinol Metab. 2016 08; 27(8):563-573.
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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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Pillai VB, Bindu S, Sharp W, Fang YH, Kim G, Gupta M, Samant S, Gupta MP. Sirt3 protects mitochondrial DNA damage and blocks the development of doxorubicin-induced cardiomyopathy in mice. Am J Physiol Heart Circ Physiol. 2016 Apr 15; 310(8):H962-72.
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Xiong X, Wang G, Tao R, Wu P, Kono T, Li K, Ding WX, Tong X, Tersey SA, Harris RA, Mirmira RG, Evans-Molina C, Dong XC. Sirtuin 6 regulates glucose-stimulated insulin secretion in mouse pancreatic beta cells. Diabetologia. 2016 Jan; 59(1):151-160.
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Colak G, Pougovkina O, Dai L, Tan M, Te Brinke H, Huang H, Cheng Z, Park J, Wan X, Liu X, Yue WW, Wanders RJ, Locasale JW, Lombard DB, de Boer VC, Zhao Y. Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Mol Cell Proteomics. 2015 Nov; 14(11):3056-71.
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Hu S, Liu H, Ha Y, Luo X, Motamedi M, Gupta MP, Ma JX, Tilton RG, Zhang W. Posttranslational modification of Sirt6 activity by peroxynitrite. Free Radic Biol Med. 2015 Feb; 79:176-85.
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Ming M, Han W, Zhao B, Sundaresan NR, Deng CX, Gupta MP, He YY. SIRT6 promotes COX-2 expression and acts as an oncogene in skin cancer. Cancer Res. 2014 Oct 15; 74(20):5925-33.
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