"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 | 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 |
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Below are the most recent publications written about "Sirtuins" by people in Profiles.
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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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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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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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The controversial world of sirtuins. Drug Discov Today Technol. 2014 Jun; 12:e9-e17.
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Sirtuins in yeast: phenotypes and tools. Methods Mol Biol. 2013; 1077:11-37.
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A sirtuin link between metabolism and heart disease. Nat Med. 2012 Nov; 18(11):1617-9.
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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.