"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
|
| MeSH Number(s) |
D08.811.277.087.520.200.650 D08.811.913.400.725.115.961 D12.776.476.900
|
| Concept/Terms |
Sirtuins- Sirtuins
- Sir2-like Proteins
- Sir2 like Proteins
- Silent Mating Type Information Regulator 2-like Proteins
- Silent Mating Type Information Regulator 2 like Proteins
|
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,
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2005 | 1 | 0 | 1 |
| 2006 | 2 | 0 | 2 |
| 2007 | 3 | 0 | 3 |
| 2008 | 3 | 2 | 5 |
| 2009 | 3 | 3 | 6 |
| 2010 | 1 | 0 | 1 |
| 2011 | 0 | 1 | 1 |
| 2012 | 1 | 0 | 1 |
| 2013 | 3 | 1 | 4 |
| 2014 | 3 | 0 | 3 |
| 2016 | 0 | 1 | 1 |
| 2019 | 2 | 1 | 3 |
| 2020 | 0 | 1 | 1 |
| 2021 | 1 | 0 | 1 |
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Below are the most recent publications written about "Sirtuins" by people in Profiles.
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Metabolic Rewiring by Loss of Sirt5 Promotes Kras-Induced Pancreatic Cancer Progression. Gastroenterology. 2021 11; 161(5):1584-1600.
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SIRT7 slows down stem cell aging by preserving heterochromatin: a perspective on the new discovery. Protein Cell. 2020 07; 11(7):469-471.
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Synergy between SIRT1 and SIRT6 helps recognize DNA breaks and potentiates the DNA damage response and repair in humans and mice. Elife. 2020 06 15; 9.
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The DNA Endonuclease Mus81 Regulates ZEB1 Expression and Serves as a Target of BET4 Inhibitors in Gastric Cancer. Mol Cancer Ther. 2019 08; 18(8):1439-1450.
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SIRT6 Is Responsible for More Efficient DNA Double-Strand Break Repair in Long-Lived Species. Cell. 2019 04 18; 177(3):622-638.e22.
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Telomere Dysfunction Induces Sirtuin Repression that Drives Telomere-Dependent Disease. Cell Metab. 2019 06 04; 29(6):1274-1290.e9.
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LncPRESS1 Is a p53-Regulated LncRNA that Safeguards Pluripotency by Disrupting SIRT6-Mediated De-acetylation of Histone H3K56. Mol Cell. 2016 12 01; 64(5):967-981.
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SIRT6 deacetylates H3K18ac at pericentric chromatin to prevent mitotic errors and cellular senescence. Nat Struct Mol Biol. 2016 05; 23(5):434-40.
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The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites. Microbiologyopen. 2015 Feb; 4(1):66-83.
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MDM2-mediated degradation of SIRT6 phosphorylated by AKT1 promotes tumorigenesis and trastuzumab resistance in breast cancer. Sci Signal. 2014 Jul 29; 7(336):ra71.