"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 |
|---|
| 1997 | 0 | 1 | 1 |
| 2005 | 1 | 0 | 1 |
| 2006 | 0 | 1 | 1 |
| 2007 | 0 | 1 | 1 |
| 2008 | 2 | 0 | 2 |
| 2009 | 3 | 0 | 3 |
| 2011 | 4 | 1 | 5 |
| 2012 | 3 | 0 | 3 |
| 2013 | 6 | 1 | 7 |
| 2014 | 7 | 0 | 7 |
| 2015 | 1 | 1 | 2 |
| 2016 | 7 | 2 | 9 |
| 2017 | 2 | 1 | 3 |
| 2018 | 1 | 1 | 2 |
| 2019 | 5 | 0 | 5 |
| 2020 | 1 | 0 | 1 |
| 2021 | 3 | 1 | 4 |
| 2022 | 2 | 0 | 2 |
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Below are the most recent publications written about "Sirtuins" by people in Profiles.
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Substrate-selective small-molecule modulators of enzymes: Mechanisms and opportunities. Curr Opin Chem Biol. 2023 Feb; 72:102231.
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Histone H2B Deacylation Selectivity: Exploring Chromatin's Dark Matter with an Engineered Sortase. J Am Chem Soc. 2022 03 02; 144(8):3360-3364.
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NAD+-consuming enzymes in immune defense against viral infection. Biochem J. 2021 12 10; 478(23):4071-4092.
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The nuclear sirtuin SIRT6 protects the heart from developing aging-associated myocyte senescence and cardiac hypertrophy. Aging (Albany NY). 2021 05 02; 13(9):12334-12358.
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Understanding the Function of Mammalian Sirtuins and Protein Lysine Acylation. Annu Rev Biochem. 2021 06 20; 90:245-285.
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Pharmacological and genetic perturbation establish SIRT5 as a promising target in breast cancer. Oncogene. 2021 03; 40(9):1644-1658.
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Is nuclear sirtuin SIRT6 a master regulator of immune function? Am J Physiol Endocrinol Metab. 2021 03 01; 320(3):E399-E414.
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The nuclear and mitochondrial sirtuins, Sirt6 and Sirt3, regulate each other's activity and protect the heart from developing obesity-mediated diabetic cardiomyopathy. FASEB J. 2019 10; 33(10):10872-10888.
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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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Updates on the epigenetic roles of sirtuins. Curr Opin Chem Biol. 2019 08; 51:18-29.