 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
- Sir2-like Proteins
- Sir2 like Proteins
- Silent Mating Type Information Regulator 2-like Proteins
- Silent Mating Type Information Regulator 2 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 |
|---|
| 2003 | 0 | 1 | 1 | | 2005 | 0 | 1 | 1 | | 2008 | 1 | 0 | 1 | | 2009 | 0 | 3 | 3 | | 2010 | 1 | 1 | 2 | | 2011 | 1 | 0 | 1 | | 2016 | 1 | 1 | 2 | | 2017 | 1 | 0 | 1 | | 2018 | 0 | 1 | 1 | | 2019 | 3 | 1 | 4 | | 2021 | 1 | 0 | 1 | | 2022 | 1 | 0 | 1 | | 2024 | 1 | 0 | 1 |
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Below are the most recent publications written about "Sirtuins" by people in Profiles.
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Affandi T, Haas A, Ohm AM, Wright GM, Black JC, Reyland ME. PKCd Regulates Chromatin Remodeling and DNA Repair through SIRT6. Mol Cancer Res. 2024 02 01; 22(2):181-196.
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McGinnis CD, Jennings EQ, Harris PS, Galligan JJ, Fritz KS. Biochemical Mechanisms of Sirtuin-Directed Protein Acylation in Hepatic Pathologies of Mitochondrial Dysfunction. Cells. 2022 06 28; 11(13).
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Rodriguez-Iturbe B, Johnson RJ, Lanaspa MA, Nakagawa T, Garcia-Arroyo FE, S?nchez-Lozada LG. Sirtuin deficiency and the adverse effects of fructose and uric acid synthesis. Am J Physiol Regul Integr Comp Physiol. 2022 05 01; 322(5):R347-R359.
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Huang Z, Zhao J, Deng W, Chen Y, Shang J, Song K, Zhang L, Wang C, Lu S, Yang X, He B, Min J, Hu H, Tan M, Xu J, Zhang Q, Zhong J, Sun X, Mao Z, Lin H, Xiao M, Chin YE, Jiang H, Shen H, Xu Y, Chen G, Zhang J. Reply to: Binding site for MDL-801 on SIRT6. Nat Chem Biol. 2021 05; 17(5):522-523.
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Mills CA, Wang X, Bhatt DP, Grimsrud PA, Matson JP, Lahiri D, Burke DJ, Cook JG, Hirschey MD, Emanuele MJ. Sirtuin 5 Is Regulated by the SCFCyclin F Ubiquitin Ligase and Is Involved in Cell Cycle Control. Mol Cell Biol. 2021 01 25; 41(2).
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Shang J, Zhu Z, Chen Y, Song J, Huang Y, Song K, Zhong J, Xu X, Wei J, Wang C, Cui L, Liu CY, Zhang J. Small-molecule activating SIRT6 elicits therapeutic effects and synergistically promotes anti-tumor activity of vitamin D3 in colorectal cancer. Theranostics. 2020; 10(13):5845-5864.
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Yan D, Franzini A, Pomicter AD, Halverson BJ, Antelope O, Mason CC, Ahmann JM, Senina AV, Vellore NA, Jones CL, Zabriskie MS, Than H, Xiao MJ, van Scoyk A, Patel AB, Clair PM, Heaton WL, Owen SC, Andersen JL, Egbert CM, Reisz JA, D'Alessandro A, Cox JE, Gantz KC, Redwine HM, Iyer SM, Khorashad JS, Rajabi N, Olsen CA, O'Hare T, Deininger MW. SIRT5 IS A DRUGGABLE METABOLIC VULNERABILITY IN ACUTE MYELOID LEUKEMIA. Blood Cancer Discov. 2021 05; 2(3):266-287.
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Nahomi RB, Nandi SK, Rakete S, Michel C, Fritz KS, Nagaraj RH. Lysine malonylation and propionylation are prevalent in human lens proteins. Exp Eye Res. 2020 01; 190:107864.
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Nandi SK, Nahomi RB, Harris PS, Michel CR, Fritz KS, Nagaraj RH. The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of a-crystallin in mouse lenses. Exp Eye Res. 2019 05; 182:1-9.
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Ali HR, Assiri MA, Harris PS, Michel CR, Yun Y, Marentette JO, Huynh FK, Orlicky DJ, Shearn CT, Saba LM, Reisdorph R, Reisdorph N, Hirschey MD, Fritz KS. Quantifying Competition among Mitochondrial Protein Acylation Events Induced by Ethanol Metabolism. J Proteome Res. 2019 04 05; 18(4):1513-1531.
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