"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,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2005 | 1 | 0 | 1 |
| 2006 | 1 | 0 | 1 |
| 2007 | 1 | 0 | 1 |
| 2008 | 1 | 0 | 1 |
| 2009 | 2 | 3 | 5 |
| 2010 | 1 | 0 | 1 |
| 2011 | 0 | 1 | 1 |
| 2012 | 2 | 0 | 2 |
| 2013 | 1 | 0 | 1 |
| 2014 | 1 | 0 | 1 |
| 2019 | 2 | 0 | 2 |
| 2020 | 0 | 1 | 1 |
| 2026 | 1 | 0 | 1 |
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Below are the most recent publications written about "Sirtuins" by people in Profiles.
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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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MDM2-mediated degradation of SIRT6 phosphorylated by AKT1 promotes tumorigenesis and trastuzumab resistance in breast cancer. Sci Signal. 2014 Jul 29; 7(336):ra71.
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Sirtuins in yeast: phenotypes and tools. Methods Mol Biol. 2013; 1077:11-37.
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SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation. Nature. 2012 Jul 05; 487(7405):114-8.
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Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation. Oncogene. 2012 Mar 22; 31(12):1546-57.
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Dietary restriction: standing up for sirtuins. Science. 2010 Aug 27; 329(5995):1012-3; author reply 1013-4.
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Identification and characterization of novel sirtuin inhibitor scaffolds. Bioorg Med Chem. 2009 Oct 01; 17(19):7031-41.
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Histone H4 lysine 16 acetylation regulates cellular lifespan. Nature. 2009 Jun 11; 459(7248):802-7.
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Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell. 2009 Mar 20; 136(6):1073-84.
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NAMPT is essential for the G-CSF-induced myeloid differentiation via a NAD(+)-sirtuin-1-dependent pathway. Nat Med. 2009 Feb; 15(2):151-8.