The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Open accessAbstract
Sirtuins are NAD(+)-dependent protein deacetylases. They mediate adaptive responses to a variety of stresses, including calorie restriction and metabolic stress. Sirtuin 3 (SIRT3) is localized in the mitochondrial matrix, where it regulates the acetylation levels of metabolic enzymes, including acetyl coenzyme A synthetase 2 (refs 1, 2). Mice lacking both Sirt3 alleles appear phenotypically normal under basal conditions, but show marked hyperacetylation of several mitochondrial proteins. Here we report that SIRT3 expression is upregulated during fasting in liver and brown adipose tissues. During fasting, livers from mice lacking SIRT3 had higher levels of fatty-acid oxidation intermediate products and triglycerides, associated with decreased levels of fatty-acid oxidation, compared to livers from wild-type mice. Mass spectrometry of mitochondrial proteins shows that long-chain acyl coenzyme A dehydrogenase (LCAD) is hyperacetylated at lysine 42 in the absence of SIRT3. LCAD is deacetylated in wild-type mice under fasted conditions and by SIRT3 in vitro and in vivo; and hyperacetylation of LCAD reduces its enzymatic activity. Mice lacking SIRT3 exhibit hallmarks of fatty-acid oxidation disorders during fasting, including reduced ATP levels and intolerance to cold exposure. These findings identify acetylation as a novel regulatory mechanism for mitochondrial fatty-acid oxidation and demonstrate that SIRT3 modulates mitochondrial intermediary metabolism and fatty-acid use during fasting.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Additionally, higher NAD+ levels can promote the deacetylase and deacylase activity of both nuclear SIRT1 and mitochondrial SIRT3, which regulate mitochondrial function and protect from high-fat diet-induced metabolic disease42,81,85–88.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [85]
Experimental — accuracy not yet measuredIn the citing paper
“Sirt3 is an established deacetylase whose targets include long chain acyl CoA dehydrogenase (LCAD), succinate dehydrogenase and Mn superoxide dismutase (SOD2) (Hirschey et al., 2010; Qiu et al., 2010).”
From Lipid-Induced Mitochondrial Stress and Insulin Action in Muscle (2012) · cites this paper as Hirschey et al., 2010
In the citing paper
“Loss of SIRT3 has been shown to inhibit fatty acid oxidation ((Hirschey et al. 2010)); the same study showed decreased gluconeogenic production of glucose in response to cold challenge and decreased production of the ketone body beta-hydroxybutyrate during fasting.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2010
In the citing paper
“Loss of SIRT3 has been shown to inhibit fatty acid oxidation ((Hirschey et al. 2010)); the same study showed decreased gluconeogenic production of glucose in response to cold challenge and decreased production of the ketone body beta-hydroxybutyrate during fasting.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2010
In the citing paper
“SIRT3 is upregulated during fasting (Hirschey et al. 2010) and more generally by PGC-1α (Kong et al. 2010), which allows it to best control the hyperacetylation caused by acetyl-CoA-dependent metabolic processes such as fatty acid oxidation and ketone body metabolism.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2010
In the citing paper
“These mice also share other characteristics of human disorders of fatty acid oxidation, including cold intolerance and reduced basal ATP levels ((Hirschey et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2010
In the citing paper
“SIRT3 promotes the efficient utilization of lipids as a primary source of acetyl-CoA during fasting by activating long-chain acyl-CoA dehydrogenase, a key enzyme in the β-oxidation of fatty acids, via deacetylation at K42 ((Hirschey et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2010
In the citing paper
“Mice lacking SIRT3 accumulate β-oxidation precursors and intermediates, including triglycerides and long-chain fatty acids.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2010
In the citing paper
“In mice, SIRT3 is normally upregulated during fasting in liver and brown fat where it plays a role in fatty-acid oxidation by maintaining the deacetylation of long-chain acyl coenzyme A dehydrogenase in mitochondria (175).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [175]
In the citing paper
“In its absence, SIRT3-deficient mice show reduced utilization of lipid stores during fasting: they have decreased fatty acid oxidation, accumulate triglycerides, and have diminished production of hepatic ATP.”
From Redox regulation of mitochondrial function (2012) · cites this paper as [175]
In the citing paper
“Upon fasting, SIRT3 expression is rapidly induced and deacetylates key residues on mitochondrial proteins (Hirschey et al, 2010).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Hirschey et al, 2010
In the citing paper
“One week of HFD enhanced SIRT3 levels and prevented mitochondrial hyperacetylation despite the higher levels of lipid substrates (Hirschey et al, 2010).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Hirschey et al, 2010
In the citing paper
“Dietary excess of lipids also dramatically changes mitochondrial protein acetylation.”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Hirschey et al, 2010
In the citing paper
“Conversely, prolonged HFD dramatically decreases SIRT3 expression, correlating with the appearance of mitochondrial hyperacetylation and mitochondrial dysfunction (Hirschey et al, 2010).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Hirschey et al, 2010
In the citing paper
“For instance, acetylation of long-chain fatty acyl-CoA dehydrogenase, one of the four enzymes involved in the mitochondrial fat oxidation pathway, causes its inactivation, leading to fat accumulation [154], [155].”
In the citing paper
“SIRT3 has been reported to regulate mitochondrial fatty acid β-oxidation via deacetylation of long-chain acyl-CoA dehydrogenase, which, when dysregulated, results in defective fatty acid oxidation (Hirschey et al., 2010).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Hirschey et al., 2010
In the citing paper
“which represents a key regulator of mitochondrial energy metabolism (Palacios et al., 2009; Hirschey et al., 2010, 2011; Anderson and Hirschey, 2012).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Hirschey et al., 2010
In the citing paper
“Interestingly, SIRT3 is present in mitochondria, where it regulates the acetylation and activity of a variety of metabolic enzymes, suggesting additional ways that it might affect mitochondrial ROS production 73.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [73]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Complementary roles of IRS-1 and IRS-2 in the hepatic regulation of metabolism
Taniguchi, C. M., Ueki, K., & Kahn, C. R. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23187 · Cited by 286
Self-citationRetractedA SIMPLE METHOD FOR THE ISOLATION AND PURIFICATION OF TOTAL LIPIDES FROM ANIMAL TISSUES
Folch, J., Lees, M., & Stanley, G. H. S. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64849-5 · Cited by 65,189
A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
Bligh, E. G., & Dyer, W. J. (1959) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o59-099 · Cited by 54,751
Preparation of fatty acid methyl esters and dimethylacetals from lipids with boron fluoride–methanol
Morrison, W. R., & Smith, L. M. (1964) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)40190-7 · Cited by 6,005
A Flexible System of Enzymatic Analysis
Lowry, O. H., & Passonneau, J. V. (1972) · Elsevier eBooks · doi:10.1016/b978-0-12-457950-7.x5001-3 · Cited by 4,050
Global Survey of Phosphotyrosine Signaling Identifies Oncogenic Kinases in Lung Cancer
Rikova, K., Guo, A., Zeng, Q., Possemato, A., Yu, J., Haack, H., Nardone, J., Lee, K., Reeves, C., Li, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.11.025 · Cited by 2,317
Self-citationSrere, P. A. (1969) · Methods in Enzymology · doi:10.1016/0076-6879(69)13005-0 · Cited by 2,005
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487
Regulation of hepatic fatty acid oxidation and ketone body production
McGarry, J. D., & Foster, D. W. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.002143 · Cited by 1,460
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291
Cited by
Sorted by citations
Items 601–700 of 1,000
Williams, A. S., Koves, T. R., Davidson, M. T., Crown, S. B., Fisher‐Wellman, K. H., Torres, M. J., Draper, J. A., Narowski, T. M., Slentz, D. H., Lantier, L., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.11.003 · Cited by 55
Dessai, A. S., Domínguez, M. P., Chen, U.-I., Hasper, J., Prechtl, C., Yu, C. R., Katsuta, E., Dai, T., Zhu, B., Jung, S. Y., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-1708 · Cited by 59
The role of SIRT3 in homeostasis and cellular health
Trinh, D., Halabi, L. A., Brar, H., Kametani, M., & Nash, J. E. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1434459 · Cited by 57
Sun, Y., Tian, Z., Liu, N., Zhang, L., Gao, Z., Sun, X., Yu, M., Wu, J., Yang, F., Zhao, Y., et al. (2018) · Journal of Molecular Medicine · doi:10.1007/s00109-017-1616-3 · Cited by 54
Gaucher, J., Kinouchi, K., Ceglia, N., Montellier, E., Peleg, S., Greco, C. M., Schmidt, A., Forné, I., Masri, S., Baldi, P., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911189116 · Cited by 59
Simic, Z., Weiwad, M., Schierhorn, A., Steegborn, C., & Schutkowski, M. (2015) · ChemBioChem · doi:10.1002/cbic.201500364 · Cited by 55
Ethanol Metabolism Modifies Hepatic Protein Acylation in Mice
Fritz, K. S., Green, M. F., Petersen, D. R., & Hirschey, M. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075868 · Cited by 53
Self-citationCell Death and Heart Failure in Obesity: Role of Uncoupling Proteins
Ruiz‐Ramírez, A., López-Acosta, O., Barrios-Maya, M. A., & El‐Hafidi, M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9340654 · Cited by 55
Xu, L., Hao, L., Ma, J. Q., Liu, J. K., & Hasim, A. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-019-03644-2 · Cited by 54
Mielke, C., Lefort, N., McLean, C. G., Cordova, J. M., Langlais, P. R., Bordner, A. J., Te, J. A., Ozkan, S. B., Willis, W. T., & Mandarino, L. J. (2014) · Biochemistry · doi:10.1021/bi401651e · Cited by 53
Mitochondrial proteins in heart failure: The role of deacetylation by SIRT3
Wang, C., Wang, Y., & Shen, L. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105802 · Cited by 52
Zhang, L., Shi, J., Du, D., Niu, N., Liu, S., Yang, X., Lu, P., Shen, X., Shi, N., Yao, L., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.103959 · Cited by 54
L-Carnitine and Male Fertility: Is Supplementation Beneficial?
Mateus, F. G., Moreira, S., Martins, A. D., Oliveira, P. F., Alves, M. G., & Pereira, M. D. L. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12185796 · Cited by 59
Buler, M., Aatsinki, S., Izzi, V., & Hakkola, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049863 · Cited by 54
Valdecantos, M. P., Pérez‐Matute, P., González‐Muniesa, P., Prieto-Hontoria, P. L., Moreno-Aliaga, M. J., & Martínez, J. A. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.11.011 · Cited by 54
Wu, Y., Wu, S., & Wei, Y. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140306103401 · Cited by 55
SIRT3 controls brown fat thermogenesis by deacetylation regulation of pathways upstream of UCP1
Sebaa, R., Johnson, J. R., Pileggi, C. A., Norgren, M., Xuan, J. Y., Sai, Y., Tong, Q., Krystkowiak, I., Bondy‐Chorney, E., Davey, N. E., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.04.008 · Cited by 56
Advances in characterization of SIRT3 deacetylation targets in mitochondrial function
Wang, S., Zhang, J., Deng, X., Zhao, Y., & Xu, K. (2020) · Biochimie · doi:10.1016/j.biochi.2020.08.021 · Cited by 52
Phosphatidylserine synthase regulates cellular homeostasis through distinct metabolic mechanisms
Yang, X. N., Liang, J., Ding, L., Li, X., Lam, S. M., Shui, G., Ding, M., & Huang, X. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008548 · Cited by 56
Zhang, L., Du, Z., He, L., Liang, W., Liu, K., & Gong, S. (2022) · Neural Plasticity · doi:10.1155/2022/5567174 · Cited by 52
Wei, Z., Xia, J., Li, J., Cai, J., Shan, J., Zhang, C., Zhang, L., Wang, T., Qian, C., & Liu, L. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.76704 · Cited by 52
Dikalov, S., Panov, A. V., & Dikalova, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126498 · Cited by 52
Kwon, D.-N., Park, W.-J., Choi, Y.-J., Gurunathan, S., & Kim, J.-H. (2015) · Aging · doi:10.18632/aging.100800 · Cited by 45
The sirtuin class of histone deacetylases: Regulation and roles in lipid metabolism
Fiorino, E., Giudici, M., Ferrari, A., Mitro, N., Caruso, D., Fabiani, E. D., & Crestani, M. (2014) · IUBMB Life · doi:10.1002/iub.1246 · Cited by 54
Mitochondrial response to controlled nutrition in health and disease
Schiff, M., Bénit, P., Coulibaly, A., Loublier, S., El‐Khoury, R., & Rustin, P. (2011) · Nutrition Reviews · doi:10.1111/j.1753-4887.2010.00363.x · Cited by 53
Approach to assessing determinants of glucose homeostasis in the conscious mouse
Hughey, C. C., Wasserman, D. H., Lee, R. S., & Lantier, L. (2014) · Mammalian Genome · doi:10.1007/s00335-014-9533-z · Cited by 51
Protein lysine acetylation guards metabolic homeostasis to fight against cancer
Xu, W., Li, Y., LIU, C., & Zhao, S. (2013) · Oncogene · doi:10.1038/onc.2013.163 · Cited by 53
Self-citationMitochondrial Acetylation and Diseases of Aging
Wagner, G. R., & Payne, R. M. (2011) · Journal of Aging Research · doi:10.4061/2011/234875 · Cited by 52
SIRT3 in cardiovascular diseases: Emerging roles and therapeutic implications
Lü, Y., Wang, Y., Wang, X., Chen, H., Cai, Z., & Xiang, M. (2016) · International Journal of Cardiology · doi:10.1016/j.ijcard.2016.06.236 · Cited by 52
Altered mitochondrial acetylation profiles in a kainic acid model of temporal lobe epilepsy
Gano, L. B., Liang, L.-P., Ryan, K., Michel, C. R., Gomez, J., Vassilopoulos, A., Reisdorph, N. A., Fritz, K. S., & Patel, M. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.063 · Cited by 54
Fernández‐Tussy, P., Fernández‐Ramos, D., Lopitz‐Otsoa, F., Simón, J., Barbier‐Torres, L., Gómez‐Santos, B., Núñez-García, M., Azkargorta, M., Juan, V. G., Serrano‐Maciá, M., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.08.008 · Cited by 52
Role of the mitochondrial stress response in human cancer progression
Wang, S., Chen, S., Tseng, L., & Lee, H. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220920558 · Cited by 51
Chen, T., Ma, C., Fan, G., Liu, H., Xie, L. Y., Li, J., Li, N., Wang, S., Zeng, M., Zhang, Y., et al. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118724 · Cited by 51
nNOS and Neurological, Neuropsychiatric Disorders: A 20-Year Story
Zhu, L., Li, F. Y., & Zhu, D. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01060-7 · Cited by 51
The Physiological and Pathological Role of Acyl-CoA Oxidation
Szrok-Jurga, S., Czumaj, A., Turyn, J., Hebanowska, A., Świerczyński, J., Śledziński, T., & Stelmańska, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914857 · Cited by 58
Ryder, D. J., Judge, S. M., Beharry, A. W., Farnsworth, C. L., Silva, J. C., & Judge, A. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136247 · Cited by 51
de Moura, M. B., Uppala, R., Zhang, Y., Houten, B. V., & Goetzman, E. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106028 · Cited by 51
Self-citationEffect of Dietary Bioactive Compounds on Mitochondrial and Metabolic Flexibility
Serrano, J. C. E., Cassanyé, A., Martin‐Garí, M., Granado‐Serrano, A. B., & Portero‐Otín, M. (2016) · Diseases · doi:10.3390/diseases4010014 · Cited by 53
Fisher‐Wellman, K. H., Draper, J. A., Davidson, M. T., Williams, A. S., Narowski, T. M., Slentz, D. H., Ilkayeva, O., Stevens, R. D., Wagner, G. R., Najjar, R. S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.057 · Cited by 49
Self-citationEpigenetic Regulation of Metabolism and Inflammation by Calorie Restriction
Hernández‐Saavedra, D., Moody, L., Xu, G. B., Chen, H., & Pan, Y. (2018) · Advances in Nutrition · doi:10.1093/advances/nmy129 · Cited by 52
SUMOylation-Mediated Response to Mitochondrial Stress
He, J., Cheng, J., & Wang, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165657 · Cited by 56
Honokiol attenuates lipotoxicity in hepatocytes via activating SIRT3-AMPK mediated lipophagy
Liu, J.-X., Zhang, T., Zhu, J.-Z., Ruan, S., Li, R.-S., Guo, B., & Lin, L.-G. (2021) · Chinese Medicine · doi:10.1186/s13020-021-00528-w · Cited by 34
Neuroprotection in Glaucoma: NAD+/NADH Redox State as a Potential Biomarker and Therapeutic Target
Petriti, B., Williams, P. A., Lascaratos, G., Chau, K., & Garway‐Heath, D. F. (2021) · Cells · doi:10.3390/cells10061402 · Cited by 52
Sirtuins in kidney health and disease
Perico, L., Remuzzi, G., & Benigni, A. (2024) · Nature Reviews Nephrology · doi:10.1038/s41581-024-00806-4 · Cited by 52
Rouble, A. N., & Storey, K. B. (2015) · Cryobiology · doi:10.1016/j.cryobiol.2015.08.009 · Cited by 50
Therapeutic potential of activators and inhibitors of sirtuins
Balcerczyk, A., & Pirola, L. (2010) · BioFactors · doi:10.1002/biof.112 · Cited by 49
Yang, L., Zhang, J., Xing, W., Zhang, X., Xu, J., Zhang, H., Chen, L., Ning, X., Ji, G., Li, J., et al. (2016) · Scientific Reports · doi:10.1038/srep23366 · Cited by 50
Sirtuin 3: A Janus face in cancer (Review)
Xiong, Y., Wang, M., Zhao, J., Han, Y., & Jia, L. (2016) · International Journal of Oncology · doi:10.3892/ijo.2016.3767 · Cited by 50
Díaz‐Ruiz, A., Lanasa, M., Garcia, J., Mora, H., Fan, F., Martín‐Montalvo, A., Francesco, A. D., Calvo‐Rubio, M., Salvador‐Pascual, A., Aon, M. A., et al. (2018) · Aging Cell · doi:10.1111/acel.12767 · Cited by 52
Parodi‐Rullán, R. M. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00439 · Cited by 50
Maissan, P., Mooij, E., & Barberis, M. (2021) · Biology · doi:10.3390/biology10030194 · Cited by 52
Berberine prevents NAFLD and HCC by modulating metabolic disorders
Lin, X., Zhang, J., Chu, Y., Nie, Q., & Zhang, J. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108593 · Cited by 56
Redox signaling and skeletal muscle adaptation during aerobic exercise
Zhou, Y., Zhang, X., Baker, J. S., Davison, G. W., & Yan, X. (2024) · iScience · doi:10.1016/j.isci.2024.109643 · Cited by 52
Targeting aberrant cancer metabolism – The role of sirtuins
Kleszcz, R., Paluszczak, J., & Baer‐Dubowska, W. (2015) · Pharmacological Reports · doi:10.1016/j.pharep.2015.03.021 · Cited by 51
Regulation of mitochondrial trifunctional protein modulates nonalcoholic fatty liver disease in mice
Nassir, F., Arndt, J. J., Johnson, S. A., & Ibdah, J. A. (2018) · Journal of Lipid Research · doi:10.1194/jlr.m080952 · Cited by 49
Theacrine protects against nonalcoholic fatty liver disease by regulating acylcarnitine metabolism
Wang, G.-E., Li, Y.-F., Zhai, Y.-J., Gong, L., Tian, J., Hong, M., Yao, N., Wu, Y., Kurihara, H., & He, R. (2018) · Metabolism · doi:10.1016/j.metabol.2018.04.011 · Cited by 49
Self-citationBerberine promotes glucose uptake and inhibits gluconeogenesis by inhibiting deacetylase SIRT3
Zhang, B., Pan, Y., Xu, L., Tang, D., Dorfman, R. G., Zhou, Q., Yin, Y., Yang, L., Zhou, L., Zhao, S., et al. (2018) · Endocrine · doi:10.1007/s12020-018-1689-y · Cited by 52
Kundu, A. B., Dey, P. K., Park, J. H., Kim, I. S., Kwack, S. J., & Kim, H. S. (2020) · Cells · doi:10.3390/cells9051101 · Cited by 50
Xie, H., Heier, C., Kien, B., Vesely, P. W., Tang, Z., Sexl, V., Schoiswohl, G., Strießnig-Bina, I., Höefler, G., Zechner, R., et al. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158737 · Cited by 48
Afzaal, A., Rehman, K., Kamal, S., & Akash, M. S. H. (2022) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23047 · Cited by 49
Emerging Roles of SIRT3 in Cardiac Metabolism
Murugasamy, K., Munjal, A., & Sundaresan, N. R. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.850340 · Cited by 48
Singhal, A., Arora, G., Virmani, R., Kundu, P., Khanna, T., Sajid, A., Misra, R., Joshi, J., Yadav, V., Samanta, S. K., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.687269 · Cited by 46
Are sirtuin deacylase enzymes important modulators of mitochondrial energy metabolism?
Osborne, B., Cooney, G. J., & Turner, N. A. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.08.016 · Cited by 47
Parodi‐Rullán, R. M., Barreto‐Torres, G., Ruiz, L., Casasnovas, J., & Javadov, S. A. (2012) · Cellular Physiology and Biochemistry · doi:10.1159/000178526 · Cited by 48
Nutrient sensing by the mitochondrial transcription machinery dictates oxidative phosphorylation
Liu, L., Nam, M., Fan, W., Akie, T. E., Hoaglin, D. C., Gao, G., Keaney, J. F., & Cooper, M. P. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69413 · Cited by 48
Fgf21 is required for cardiac remodeling in pregnancy
Redondo‐Angulo, I., Mas‐Stachurska, A., Sitges, M., Tinahones, F. J., Giralt, M., Villarroya, F., & Planavila, A. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx088 · Cited by 48
Li, A., Liu, Q., Li, Q., Liu, B., Yang, Y., & Zhang, N. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.07.039 · Cited by 49
Meyer, J. G., Softic, S., Basisty, N., Rardin, M. J., Verdin, E. M., Gibson, B. W., Ilkayeva, O., Newgard, C. B., Kahn, C. R., & Schilling, B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208973 · Cited by 52
Self-citationde Urturi, D. S., Buqué, X., Porteiro, B., Folgueira, C., Mora, A., Delgado, T. C., Prieto‐Fernández, E., Olaizola, P., Gómez‐Santos, B., Apodaka‐Biguri, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28749-z · Cited by 49
Tucci, S., Herebıan, D., Sturm, M., Seibt, A., & Spiekerkoetter, U. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045429 · Cited by 47
Targeting sirtuins for the treatment of diabetes
Huynh, F. K., Hershberger, K. A., & Hirschey, M. D. (2013) · Diabetes Management · doi:10.2217/dmt.13.6 · Cited by 48
Self-citationSIRT3 Overexpression Attenuates Palmitate-Induced Pancreatic β-Cell Dysfunction
Kim, M., Lee, J. S., Oh, J. E., Nan, J., Lee, H., Jung, H. S., Chung, S. S., & Park, K. S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124744 · Cited by 48
Preserved recovery of cardiac function following ischemia–reperfusion in mice lacking SIRT3
Koentges, C., Pfeil, K., Meyer-Steenbuck, M., Lother, A., Hoffmann, M. M., Odening, K. E., Hein, L., Bode, C., & Bugger, H. (2015) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2015-0152 · Cited by 47
Mitochondrial sirtuins in the heart
Bugger, H., Witt, C. N., & Bode, C. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9570-7 · Cited by 47
Li, Y., Meng, X., Wang, W., Liu, F., Hao, Z.-R., Yang, Y., Zhao, J., Yin, W., Xu, L., Zhao, R., et al. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00394 · Cited by 47
Self-citationSirtuin-3 Promotes Adipogenesis, Osteoclastogenesis, and Bone Loss in Aging Male Mice
Ho, L., Wang, L., Roth, T., Pan, Y., Verdin, E. M., Hsiao, E. C., & Nissenson, R. A. (2017) · Endocrinology · doi:10.1210/en.2016-1739 · Cited by 46
Self-citationRenu, K., Madhyastha, H., Madhyastha, R., Maruyama, M., Arunachlam, S., & Gopalakrishnan, A. V. (2017) · Toxicology Letters · doi:10.1016/j.toxlet.2017.11.032 · Cited by 47
Li, D., Tong, J., Zeng, F., Guo, M., Li, Y., Wang, H., & Wang, P. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14506 · Cited by 47
Self-citationDabke, P., & Das, A. M. (2020) · Nutrients · doi:10.3390/nu12082379 · Cited by 47
Hepatic levels of S-adenosylmethionine regulate the adaptive response to fasting
Capelo-Diz, A., Lachiondo‐Ortega, S., Fernández‐Ramos, D., Cañas-Martín, J., Goikoetxea‐Usandizaga, N., Serrano‐Maciá, M., Gonzalez-Rellan, M. J., Mosca, L., Vicens, J. B., Tinahones, A., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.07.002 · Cited by 46
Mitochondrial proteomics—a tool for the study of metabolic disorders
Gregersen, N., Hansen, J., & Palmfeldt, J. (2012) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-012-9480-3 · Cited by 48
Lxr-driven enterocyte lipid droplet formation delays transport of ingested lipids
Cruz-Garcia, L., & Schlegel, A. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m052845 · Cited by 50
Sun, Y., Teng, Z., Sun, X., Zhang, L., Chen, J., Wang, B., Lu, F., Liu, N., Yu, M., Peng, S., et al. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00326.2018 · Cited by 46
Tian, N., Liu, Q., Li, Y., Tong, L., Lu, Y., Zhu, Y., Zhang, P., Chen, H., Hu, L., Meng, J., et al. (2020) · Diabetes · doi:10.2337/db19-1087 · Cited by 48
Self-citationLoss of Mitochondrial Control Impacts Renal Health
Srivastava, S. P., Kanasaki, K., & Goodwin, J. E. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.543973 · Cited by 48
Evidence supporting a mechanistic role of sirtuins in mood and metabolic disorders
Alageel, A., Tomasi, J., Tersigni, C., Brietzke, E., Zuckerman, H., Subramaniapillai, M., Lee, Y., Iacobucci, M., Rosenblat, J. D., Mansur, R. B., et al. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2018.05.017 · Cited by 45
Barroso, E., Rodríguez‐Rodríguez, R., Zarei, M., Pizarro‐Delgado, J., Planavila, A., Palomer, X., Villarroya, F., & Vázquez‐Carrera, M. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00640-8 · Cited by 49
Regulation and protection of mitochondrial physiology by sirtuins
Pereira, C. V., Lebiedzińska, M., Wieckowski, M. R., & Oliveira, P. J. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.07.003 · Cited by 46
Takei, M., Ando, Y., Saitoh, W., Tanimoto, T., Kiyosawa, N., Manabe, S., Sanbuissho, A., Okazaki, O., Iwabuchi, H., Yamoto, T., et al. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq211 · Cited by 44
Mitochondrial Dysfunction in Metabolic Syndrome and Asthma
Mabalirajan, U., & Ghosh, B. (2013) · Journal of Allergy · doi:10.1155/2013/340476 · Cited by 44
Rumpf, T., Gerhardt, S., Einsle, O., & Jung, M. (2015) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x15019986 · Cited by 44
Sirtuin 3, Endothelial Metabolic Reprogramming, and Heart Failure With Preserved Ejection Fraction
Zeng, H., & Chen, J. (2019) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000719 · Cited by 46
Epigenetic Remodeling in Obesity-Related Vascular Disease
Masi, S., Ambrosini, S., Mohammed, S. A., Sciarretta, S., Lüscher, T. F., Paneni, F., & Costantino, S. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8040 · Cited by 49
Sirtuins: The NAD + -Dependent Multifaceted Modulators of Inflammation
Santos, L., Benítez-Rosendo, A., Bresque, M., Camacho-Pereira, J., Calliari, A. J., & Escande, C. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0295 · Cited by 49
Mitochondrion as a Target for Heart Failure Therapy – Role of Protein Lysine Acetylation –
Lee, C. F., & Tian, R. (2015) · Circulation Journal · doi:10.1253/circj.cj-15-0742 · Cited by 46
Zhang, S., Li, Y.-F., Wang, G.-E., Tan, R., Tsoi, B., Mao, G., Zhai, Y.-J., Cao, L., Chen, M., Kurihara, H., et al. (2015) · Food & Function · doi:10.1039/c5fo00247h · Cited by 44
Self-citationPost-Translational Modification of Proteins in Toxicological Research: Focus on Lysine Acylation
Lee, S. (2013) · Toxicological Research · doi:10.5487/tr.2013.29.2.081 · Cited by 44
Maintaining good hearing: Calorie restriction, Sirt3, and glutathione
Han, C. J., & Someya, S. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.02.014 · Cited by 45
Zou, X., Santa-Maria, C. A., O’Brien, J., Gius, D. R., & Zhu, Y. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6641 · Cited by 44
Defining the Orphan Functions of Lysine Acetyltransferases
Montgomery, D. C., Sorum, A. W., & Meier, J. L. (2015) · ACS Chemical Biology · doi:10.1021/cb500853p · Cited by 44
Metadata
- Authors
- Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., Stevens, R. D., Li, Y., Saha, A. K., Ruderman, N. B., Bain, J. R., Newgard, C. B., Farese Jr, R. V., Alt, F. W., Kahn, C. R., & Verdin, E.
- Affiliations
- Gladstone Institutes (US)
- University of Pittsburgh (US)
- Joslin Diabetes Center (US)
- Howard Hughes Medical Institute (US)
- University of California, San Francisco (US)
- Duke University (US)
- Cell Signaling Technology (United States) (US)
- Boston University (US)
- Corresponding author
- Verdin, Eric
- ORCID
- Venue
- Nature
- Published
- 2010-03
- Volume
- 464
- Issue
- 7285
- Pages
- 121-125
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2841477
- OpenAlex
- W2052751736
- Cited by
- 1,687
- References
- 44
- Citations by year
- 2026: 77 · 2025: 86 · 2024: 108 · 2023: 95 · 2022: 125 · 2021: 107 · 2020: 110 · 2019: 112 · 2018: 110 · 2017: 102 · 2016: 127 · 2015: 113 · 2014: 95 · 2013: 110 · 2012: 97
- FWCI
- 40.96
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (5r01dk019514-35)
- National Institute on Aging (K08AG022325)
- National Heart, Lung, and Blood Institute (P01HL068758)
- National Institute of Diabetes and Digestive and Kidney Diseases (L40 DK065607, R01DK067509, DK59637, U24DK059637, K01DK076573, P30DK026743, R01-DK-019514)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- SIRT3, sirtuins, mitochondrial fatty acid oxidation, protein deacetylation, long-chain acyl-CoA dehydrogenase, acetylation, fasting, liver, brown adipose tissue, cold sensitivity, ATP levels, triglycerides, NAD+-dependent deacetylase, metabolic stress, caloric restriction
- MeSH terms
- Acetylation, Adenosine Triphosphate, Animals, Body Temperature Regulation, Adipose Tissue, Brown, Carnitine, Cell Line, Cold Temperature, Fasting, Fatty Acids, Humans, Hypoglycemia, Liver, Male, Mitochondria, Oxidation-Reduction, Mass Spectrometry, Triglycerides, Up-Regulation, Caloric Restriction, Acyl-CoA Dehydrogenase, Long-Chain, Mice, Sirtuin 3
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
