 Sirtuin 3
"Sirtuin 3" 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 sirtuin family member found primarily in MITOCHONDRIA. It is a multifunctional enzyme that contains a NAD-dependent deacetylase activity that is specific for HISTONES and a mono-ADP-ribosyltransferase activity.
| Descriptor ID |
D056566
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| MeSH Number(s) |
D08.811.277.087.520.200.650.600 D08.811.913.400.725.115.961.600 D12.776.476.900.600 D12.776.575.875
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| Concept/Terms |
Sirtuin 3- Sirtuin 3
- Silent Mating Type Information Regulation 2 Homolog 3
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Below are MeSH descriptors whose meaning is more general than "Sirtuin 3".
Below are MeSH descriptors whose meaning is more specific than "Sirtuin 3".
This graph shows the total number of publications written about "Sirtuin 3" by people in this website by year, and whether "Sirtuin 3" 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 |
|---|
| 2011 | 4 | 0 | 4 | | 2012 | 1 | 0 | 1 | | 2013 | 2 | 0 | 2 | | 2014 | 0 | 2 | 2 | | 2015 | 1 | 0 | 1 | | 2016 | 1 | 0 | 1 | | 2017 | 1 | 1 | 2 | | 2018 | 1 | 0 | 1 | | 2019 | 2 | 1 | 3 | | 2020 | 0 | 2 | 2 |
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Below are the most recent publications written about "Sirtuin 3" by people in Profiles.
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Keller A, Hull SE, Elajaili H, Johnston A, Knaub LA, Chun JH, Walker L, Nozik-Grayck E, Reusch JEB. (-)-Epicatechin Modulates Mitochondrial Redox in Vascular Cell Models of Oxidative Stress. Oxid Med Cell Longev. 2020; 2020:6392629.
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Tyagi A, Mirita C, Taher N, Shah I, Moeller E, Tyagi A, Chong T, Pugazhenthi S. Metabolic syndrome exacerbates amyloid pathology in a comorbid Alzheimer's mouse model. Biochim Biophys Acta Mol Basis Dis. 2020 10 01; 1866(10):165849.
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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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Tyagi A, Nguyen CU, Chong T, Michel CR, Fritz KS, Reisdorph N, Knaub L, Reusch JEB, Pugazhenthi S. SIRT3 deficiency-induced mitochondrial dysfunction and inflammasome formation in the brain. Sci Rep. 2018 12 03; 8(1):17547.
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Harris PS, Gomez JD, Backos DS, Fritz KS. Characterizing Sirtuin 3 Deacetylase Affinity for Aldehyde Dehydrogenase 2. Chem Res Toxicol. 2017 03 20; 30(3):785-793.
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Pugazhenthi S. Metabolic Syndrome and the Cellular Phase of Alzheimer's Disease. Prog Mol Biol Transl Sci. 2017; 146:243-258.
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Bruce KD, Szczepankiewicz D, Sihota KK, Ravindraanandan M, Thomas H, Lillycrop KA, Burdge GC, Hanson MA, Byrne CD, Cagampang FR. Altered cellular redox status, sirtuin abundance and clock gene expression in a mouse model of developmentally primed NASH. Biochim Biophys Acta. 2016 Jul; 1861(7):584-93.
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Novgorodov SA, Riley CL, Keffler JA, Yu J, Kindy MS, Macklin WB, Lombard DB, Gudz TI. SIRT3 Deacetylates Ceramide Synthases: IMPLICATIONS FOR MITOCHONDRIAL DYSFUNCTION AND BRAIN INJURY. J Biol Chem. 2016 Jan 22; 291(4):1957-73.
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