SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome
Open accessAbstract
Acetylation is increasingly recognized as an important metabolic regulatory posttranslational protein modification, yet the metabolic consequence of mitochondrial protein hyperacetylation is unknown. We find that high-fat diet (HFD) feeding induces hepatic mitochondrial protein hyperacetylation in mice and downregulation of the major mitochondrial protein deacetylase SIRT3. Mice lacking SIRT3 (SIRT3KO) placed on a HFD show accelerated obesity, insulin resistance, hyperlipidemia, and steatohepatitis compared to wild-type (WT) mice. The lipogenic enzyme stearoyl-CoA desaturase 1 is highly induced in SIRT3KO mice, and its deletion rescues both WT and SIRT3KO mice from HFD-induced hepatic steatosis and insulin resistance. We further identify a single nucleotide polymorphism in the human SIRT3 gene that is suggestive of a genetic association with the metabolic syndrome. This polymorphism encodes a point mutation in the SIRT3 protein, which reduces its overall enzymatic efficiency. Our findings show that loss of SIRT3 and dysregulation of mitochondrial protein acetylation contribute to the metabolic syndrome.
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Sirt3 knockout mice develop multiple elements of the metabolic syndrome with aging.
“These animals also develop multiple elements of the metabolic syndrome with aging (Hirschey et al., 2011).”
From Lipid-Induced Mitochondrial Stress and Insulin Action in Muscle (2012) · cites this paper as Hirschey et al., 2011
Higher NAD+ levels promote the deacetylase and deacylase activity of nuclear SIRT1 and mitochondrial SIRT3, which regulate mitochondrial function and protect from high-fat diet-induced metabolic disease.
“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 [86]
The V208I mutation increases the KM of SIRT3 for NAD+ and reduces the Vmax toward peptide substrate, reducing catalytic efficiency and creating a ~1.4-fold increase in risk for metabolic syndrome.
“The V208I mutation caused by this polymorphism both increased the KM of SIRT3 for NAD+ and reduced the Vmax of the enzyme towards peptide substrate, reducing overall catalytic efficiency and mimicking the effects of reduced SIRT3 expression at the whole-body level and creating a ~1.4-fold increase in risk for metabolic syndrome ((Hirschey et al. 2011)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2011
SIRT3 knockout mice exhibit metabolic changes similar to those observed in human metabolic syndrome.
“SIRT3 knockout mice exhibit metabolic changes similar to those observed in the human metabolic syndrome ((Hirschey et al. 2011);(Jing et al. 2013)), and a human SIRT3 polymorphism associated with reduced SIRT3 deacetylase activity is associated with increased risk of metabolic syndrome in humans ((Hirschey et al. 2011).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2011
A SIRT3 polymorphism previously linked to metabolic syndrome was identified in a cohort of 162 patients and controls.
“via identification of a SIRT3 polymorphism previously associated with metabolic syndrome ((Hirschey et al. 2011) in a cohort of 162 patients and controls.”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2011
A human SIRT3 polymorphism associated with reduced SIRT3 deacetylase activity is associated with increased risk of metabolic syndrome.
“and a human SIRT3 polymorphism associated with reduced SIRT3 deacetylase activity is associated with increased risk of metabolic syndrome in humans ((Hirschey et al. 2011).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Hirschey et al. 2011
Mitochondrial accumulation of fatty acid oxidation intermediates triggers metabolic complications via protein modification.
“implies that mitochondrial accumulation of FAO intermediates triggers metabolic complications *via* protein modification ([71](#B71), [80](#B80)).”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [71]
SIRT3 knockout mice have high acylcarnitines and increased acylated mitochondrial proteins and develop metabolic syndrome.
“This along with the observation that SIRT3 knockout mice have high acylcarnitines and increased acylated mitochondrial proteins and develop metabolic syndrome, implies that mitochondrial accumulation of FAO intermediates triggers metabolic complications *via* protein modification ([71](#B71), [80](#B80)).”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [71]
SIRT3 deletion in mice exacerbates the deleterious effect of a high-fat diet on metabolic health, resulting in accelerated obesity, insulin resistance, hyperlipidaemia and steatohepatitis compared to wild-type littermates.
“SIRT3 plays a central role in the regulation of mitochondrial and energy metabolism with its deletion in mice exacerbating the deleterious effect of a high-fat diet on metabolic health resulting in accelerated obesity, insulin resistance, hyperlipidaemia and steatohepatitis compared to their wild-type littermates (Hirschey et al., 2011).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Hirschey et al., 2011
A high-fat diet also increases mitochondrial protein acetylation.
“Counterintuitively, a high-fat diet also increases mitochondrial protein acetylation (Hirschey et al., 2011).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Hirschey et al., 2011
SIRT3 is a pivotal regulator of mitochondrial protein acetylation and energy metabolism.
“A pivotal regulator of mitochondrial protein acetylation, and thereby energy metabolism, is the mitochondrial NAD-dependent protein deacetylase SIRT3.”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Hirschey et al., 2011
A single nucleotide polymorphism in the SIRT3 gene is associated with increased susceptibility to develop the metabolic syndrome in humans.
“The importance of SIRT3 in metabolic health has been also demonstrated in humans where a single nucleotide polymorphism in the SIRT3 gene has been associated with increased susceptibility to develop the metabolic syndrome (Hirschey et al., 2011).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Hirschey et al., 2011
SIRT3 is a key regulator of mitochondrial energy metabolism.
“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., 2011
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Cites
Role of Insulin Resistance in Human Disease
Reaven, G. M. (1988) · Diabetes · doi:10.2337/diab.37.12.1595 · Cited by 12,154 · see citing works
Adipose Expression of Tumor Necrosis Factor-α: Direct Role in Obesity-Linked Insulin Resistance
Hotamisligil, G. S., Shargill, N. S., & Spiegelman, B. M. (1993) · Science · doi:10.1126/science.7678183 · Cited by 7,518 · see citing works
Mechanisms linking obesity to insulin resistance and type 2 diabetes
Kahn, S. E., Hull, R. L., & Utzschneider, K. M. (2006) · Nature · doi:10.1038/nature05482 · Cited by 5,448 · see citing works
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works
Banting lecture 1988. Role of insulin resistance in human disease.
Reaven, G. (1988) · Diabetes · doi:10.2337/diabetes.37.12.1595 · Cited by 3,801 · see citing works
Biological, clinical and population relevance of 95 loci for blood lipids
Teslovich, T. M., Musunuru, K., Smith, A. V., Edmondson, A. C., Stylianou, I. M., Koseki, M., Pirruccello, J. P., Ripatti, S., Chasman, D. I., Willer, C. J., et al. (2010) · Nature · doi:10.1038/nature09270 · Cited by 3,527 · see citing works
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works
Association analyses of 249,796 individuals reveal 18 new loci associated with body mass index
MAGIC, Speliotes, E. K., on behalf of Procardis Consortium, Willer, C. J., Berndt, S. I., Monda, K. L., Thorleifsson, G., Jackson, A. U., Allen, H. L., Lindgren, C. M., et al. (2010) · Nature Genetics · doi:10.1038/ng.686 · Cited by 2,912 · see citing works
Dysfunction of Mitochondria in Human Skeletal Muscle in Type 2 Diabetes
Kelley, D. E., He, J., Menshikova, E. V., & Ritov, V. B. (2002) · Diabetes · doi:10.2337/diabetes.51.10.2944 · Cited by 2,321 · see citing works
Protection from obesity-induced insulin resistance in mice lacking TNF-α function
Uysal, K. T., Wiesbrock, S. M., Marino, M. W., & Hotamisligil, G. S. (1997) · Nature · doi:10.1038/39335 · Cited by 2,234 · see citing works
Impaired Mitochondrial Activity in the Insulin-Resistant Offspring of Patients with Type 2 Diabetes
Petersen, K. F., Dufour, S., Befroy, D., Garcia, R., & Shulman, G. I. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa031314 · Cited by 2,193 · see citing works
New genetic loci implicated in fasting glucose homeostasis and their impact on type 2 diabetes risk
DIAGRAM Consortium, Dupuis, J., GIANT Consortium, Global BPgen Consortium, Anders Hamsten on behalf of Procardis Consortium, the MAGIC investigators, Langenberg, C., Prokopenko, I., Saxena, R., Soranzo, N., et al. (2010) · Nature Genetics · doi:10.1038/ng.520 · Cited by 2,166 · see citing works
Koves, T. R., Ussher, J. R., Noland, R. C., Slentz, D., Mosedale, M., Ilkayeva, O., Bain, J., Stevens, R., Dyck, J. R. B., Newgard, C. B., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.013 · Cited by 1,990 · see citing works
Self-citationPatti, M. E., Butte, A. J., Crunkhorn, S., Cusi, K., Berria, R., Kashyap, S., Miyazaki, Y., Kohane, I., Costello, M., Saccone, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1032913100 · Cited by 1,952 · see citing works
Self-citationRegulation of cellular metabolism by protein lysine acetylation
Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910 · see citing works
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687 · see citing works
Self-citationMechanism of free fatty acid-induced insulin resistance in humans.
Roden, M., Price, T. B., Perseghin, G., Petersen, K. F., Rothman, D. L., Cline, G. W., & Shulman, G. I. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118742 · Cited by 1,539 · see citing works
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 · see citing works
Recent progress in the biology and physiology of sirtuins
Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,484 · see citing works
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works
Mechanism of hepatic insulin resistance in non-alcoholic fatty liver disease
Samuel, V. T., Liu, Z.-X., Qu, X., Elder, B. D., Bilz, S., Befroy, D., Romanelli, A. J., & Shulman, G. I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313478200 · Cited by 1,322 · see citing works
Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310 · see citing works
Self-citationA 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 · see citing works
Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works
Self-citationSomeya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works
Identification of a Lipokine, a Lipid Hormone Linking Adipose Tissue to Systemic Metabolism
Cao, H.-M., Gerhold, K., Mayers, J. R., Wiest, M., Watkins, S., & Hotamışlıgil, G. S. (2008) · Cell · doi:10.1016/j.cell.2008.07.048 · Cited by 1,142 · see citing works
From noncoding variant to phenotype via SORT1 at the 1p13 cholesterol locus
Musunuru, K., Strong, A., Frank-Kamenetsky, M., Lee, N. E., Ahfeldt, T., Sachs, K. V., Li, X., Li, H., Kuperwasser, N., Ruda, V. M., et al. (2010) · Nature · doi:10.1038/nature09266 · Cited by 1,140 · see citing works
Loss of stearoyl–CoA desaturase-1 function protects mice against adiposity
Ntambi, J. M., Miyazaki, M., Stoehr, J. P., Hong, L., Kendziorski, C. M., Yandell, B. S., Song, Y., Cohen, P., Friedman, J. M., & Attie, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132384699 · Cited by 1,096 · see citing works
Acetylation of Metabolic Enzymes Coordinates Carbon Source Utilization and Metabolic Flux
Wang, Q., Zhang, Y., Yang, C., Xiong, H., Lin, Y., Yao, J., Li, H., Xie, L., Zhao, W., Yao, Y., et al. (2010) · Science · doi:10.1126/science.1179687 · Cited by 1,008 · see citing works
MAGIC, Heid, I. M., Jackson, A. U., Randall, J. C., Winkler, T. W., Qi, L., Steinthorsdottir, V., Thorleifsson, G., Zillikens, M. C., Speliotes, E. K., et al. (2010) · Nature Genetics · doi:10.1038/ng.685 · Cited by 931 · see citing works
Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899 · see citing works
Role for Stearoyl-CoA Desaturase-1 in Leptin-Mediated Weight Loss
Cohen, P., Miyazaki, M., Socci, N. D., Hagge-Greenberg, A., Liedtke, W., Soukas, A. A., Sharma, R., Hudgins, L. C., Ntambi, J. M., & Friedman, J. M. (2002) · Science · doi:10.1126/science.1071527 · Cited by 818 · see citing works
SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
Nakagawa, T., Lomb, D. J., Haigis, M. C., & Guarente, L. (2009) · Cell · doi:10.1016/j.cell.2009.02.026 · Cited by 787 · see citing works
Kim, H.-S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., van der Meer, R., Nguyen, P., Savage, J., Owens, K. M., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.023 · Cited by 785 · see citing works
Association analyses of 249,796 individuals reveal 18 new loci associated with body mass index
Speliotes, E. K., Willer, C. J., Berndt, S. I., Monda, K. L., Þorleifsson, G., Jackson, A., Allen, H. L., Lindgren, C. M., Luan, J., Mägi, R., et al. (2010) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/d3bn-7g86 · Cited by 767 · see citing works
Variants in MTNR1B influence fasting glucose levels
Prokopenko, I., Langenberg, C., Florez, J. C., Saxena, R., Soranzo, N., Þorleifsson, G., Loos, R. J. F., Manning, A. K., Jackson, A., Aulchenko, Y. S., et al. (2008) · Nature Genetics · doi:10.1038/ng.290 · Cited by 743 · see citing works
Self-citationBiochemical and physiological function of stearoyl-CoA desaturase
Paton, C. M., & Ntambi, J. M. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90897.2008 · Cited by 742 · see citing works
Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., & Chang, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011707 · Cited by 718 · see citing works
Lindgren, C. M., Heid, I. M., Randall, J. C., Lamina, C., Steinthórsdóttir, V., Qi, L., Speliotes, E. K., Þorleifsson, G., Willer, C. J., Herrera, B. M., et al. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000508 · Cited by 701 · see citing works
Self-citationFROM MICE TO MEN: Insights into the Insulin Resistance Syndromes
Biddinger, S. B., & Kahn, C. R. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.68.040104.124723 · Cited by 700 · see citing works
Self-citationShimano, H., Yahagi, N., Amemiya-Kudo, M., Hasty, A. H., Osuga, J.-I., Tamura, Y., Shionoiri, F., Iizuka, Y., Ohashi, K., Harada, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35832 · Cited by 691 · see citing works
Hunter, D. J., Peltonen, L., Guiducci, C., Crawford, G., Hirschhorn, J. N., Lyon, H. N., & Speliotes, E. K. (2009) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 687 · see citing works
Surwit, R. S., Feinglos, M. N., Rodin, J., Sutherland, A., Petro, A. E., Opara, E. C., Kuhn, C. M., & Rebuffe-Scrive, M. (1995) · Metabolism · doi:10.1016/0026-0495(95)90123-x · Cited by 618 · see citing works
Schwer, B., North, B. J., Frye, R. A., Ott, M., & Verdin, E. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205057 · Cited by 599 · see citing works
Self-citationSIRT3, a human SIR2 homologue, is an NAD- dependent deacetylase localized to mitochondria
Onyango, P. O., Celic, I., McCaffery, J. M., Boeke, J. D., & Feinberg, A. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222538099 · Cited by 573 · see citing works
The metabolic syndrome: is this diagnosis necessary?
Reaven, G. (2006) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.6.1237 · Cited by 546 · see citing works
Akt/PKB regulates hepatic metabolism by directly inhibiting PGC-1α transcription coactivator
Li, X., Monks, B., Ge, Q., & Birnbaum, M. J. (2007) · Nature · doi:10.1038/nature05861 · Cited by 487 · see citing works
Collins, S., Martin, T. L., Surwit, R. S., & Robidoux, J. (2004) · Physiology & Behavior · doi:10.1016/j.physbeh.2004.02.006 · Cited by 486 · see citing works
Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.003 · Cited by 484 · see citing works
Self-citationBefroy, D. E., Petersen, K. F., Dufour, S., Mason, G. F., de Graaf, R. A., Rothman, D. L., & Shulman, G. I. (2007) · Diabetes · doi:10.2337/db06-0783 · Cited by 453 · see citing works
Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction
Hallows, W. C., Yu, W., Smith, B. C., Devires, M. K., Ellinger, J. J., Someya, S., Shortreed, M. R., Prolla, T., Markley, J. L., Smith, L. M., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.002 · Cited by 389 · see citing works
Hulver, M. W., Berggren, J. R., Carper, M. J., Miyazaki, M., Ntambi, J. M., Hoffman, E. P., Thyfault, J. P., Stevens, R., Dohm, G. L., Houmard, J. A., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.09.002 · Cited by 384 · see citing works
Self-citationStančáková, A., Javorský, M., Kuulasmaa, T., Haffner, S. M., Kuusisto, J., & Laakso, M. (2009) · Diabetes · doi:10.2337/db08-1607 · Cited by 348 · see citing works
Self-citationAttie, A., Krauss, R. M., Gray-Keller, M. P., Brownlie, A., Miyazaki, M., Kastelein, J. J. P., Lusis, A. J., Stalenhoef, A. F. H., Stoehr, J. P., Hayden, M. R., et al. (2002) · Journal of Lipid Research · doi:10.1194/jlr.m200189-jlr200 · Cited by 347 · see citing works
Metabolic syndrome: from epidemiology to systems biology
Lusis, A. J., Attie, A., & Reue, K. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2468 · Cited by 340 · see citing works
Petersen, K. F., Dufour, S., & Shulman, G. I. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020233 · Cited by 308 · see citing works
Zhang, D., Liu, Z.-X., Choi, C. S., Tian, L., Kibbey, R., Dong, J., Cline, G. W., Wood, P. A., & Shulman, G. I. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707060104 · Cited by 291 · see citing works
Variation in Type 2 Diabetes-Related Traits in Mouse Strains Susceptible to Diet-Induced Obesity
Rossmeisl, M., Rim, J. S., Koza, R. A., & Kozak, L. P. (2003) · Diabetes · doi:10.2337/diabetes.52.8.1958 · Cited by 283 · see citing works
Miyazaki, M., Kim, Y., & Ntambi, J. M. (2001) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31589-3 · Cited by 265 · see citing works
Calorie restriction alters mitochondrial protein acetylation
Schwer, B., Eckersdorff, M., Li, Y., Silva, J. C., Fermin, D., Kurtev, M. V., Giallourakis, C., Comb, M. J., Alt, F. W., & Lombard, D. B. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00503.x · Cited by 259 · cited 2× · see citing works
“, 2006), calorie restriction (Schwer et al., 2009), and ethanol metabolism (Picklo, 2008).”
Self-citationHepatic gene expression profiles in a long-term high-fat diet-induced obesity mouse model
Kim, S., Sohn, I., Ahn, J., Lee, K.-H., Lee, Y. S., & Lee, Y. S. (2004) · Gene · doi:10.1016/j.gene.2004.06.015 · Cited by 248 · see citing works
Kurtz, D. M., Rinaldo, P., Rhead, W. J., Tian, L., Millington, D. S., Vockley, J. E., Hamm, D. A., Brix, A. E., Lindsey, J. R., Pinkert, C. A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15592 · Cited by 248 · see citing works
Peroxisome Proliferator Activator Receptor γ Coactivator-1 Expression Is Reduced in Obesity
Crunkhorn, S., Dearie, F., Mantzoros, C., Gami, H., da Silva, W. S., Espinoza, D., Faucette, R., Barry, K., Bianco, A. C., & Patti, M. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611214200 · Cited by 236 · cited 11× · see citing works
“Furthermore, we found a 1.7-fold increase in SIRT3 expression in mice overexpressing adenoviral PGC-1a fed aHFD, compared tomice overexpressing adenoviral GFP (Figure 1F).”
InfluentialRole of adiponectin in human skeletal muscle bioenergetics
Civitarese, A. E., Ukropcova, B., Carling, S., Hulver, M., DeFronzo, R. A., Mandarino, L., Ravussin, E., & Smith, S. R. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.002 · Cited by 234 · see citing works
Ford, E. S., Li, C., Zhao, G., Pearson, W. S., & Mokdad, A. H. (2008) · Diabetes Care · doi:10.2337/dc07-1030 · Cited by 227 · see citing works
Fat, carbohydrate, and calories in the development of diabetes and obesity in the C57BL/6J mouse
Petro, A. E., Cotter, J., Cooper, D. A., Peters, J. C., Surwit, S. J., & Surwit, R. S. (2004) · Metabolism · doi:10.1016/j.metabol.2003.11.018 · Cited by 207 · see citing works
Nutritional strategies in the prevention and treatment of metabolic syndrome
Feldeisen, S. E., & Tucker, K. L. (2007) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h06-101 · Cited by 206 · see citing works
Ukropcova, B., Sereda, O., de Jonge, L., Bogacka, I., Nguyen, T., Xie, H., Bray, G. A., & Smith, S. R. (2007) · Diabetes · doi:10.2337/db06-0521 · Cited by 165 · see citing works
SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity
Bao, J., Scott, I., Lu, Z., Pang, L., Dimond, C. C., Gius, D., & Sack, M. N. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.009 · Cited by 157 · see citing works
Regulation of stearoyl‐CoA desaturase expression
Ntambi, J. M., Miyazaki, M., & Dobrzyń, A. (2004) · Lipids · doi:10.1007/s11745-004-1331-2 · Cited by 136 · see citing works
Civitarese, A. E., MacLean, P. S., Carling, S., Kerr-Bayles, L., McMillan, R. P., Pierce, A., Becker, T. C., Moro, C., Finlayson, J., Lefort, N., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.004 · Cited by 95 · see citing works
Self-citationTaubes, G. (2009) · Science · doi:10.1126/science.325_256 · Cited by 91 · see citing works
Isolation of Mitochondria from Tissues and Cells by Differential Centrifugation
Graham, J. M. (1999) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0303s04 · Cited by 88 · see citing works
Long-Chain Acyl-CoA–Dependent Regulation of Gene Expression in Bacteria, Yeast and Mammals
Black, P. N., Færgeman, N. J., & Dirusso, C. (2000) · Journal of Nutrition · doi:10.1093/jn/130.2.305s · Cited by 88 · see citing works
Purification of a Crude Mitochondrial Fraction by Density‐Gradient Centrifugation
Graham, J. M. (1999) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0304s04 · Cited by 83 · see citing works
Graham, J. M. (2001) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0309s10 · Cited by 68 · see citing works
Ji, H. L., & Friedman, M. I. (2007) · Metabolism · doi:10.1016/j.metabol.2007.04.006 · Cited by 61 · see citing works
Ethanol intoxication increases hepatic N-lysyl protein acetylation
Picklo, M. J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.09.039 · Cited by 60 · see citing works
Chapter 8 Acetylation of Mitochondrial Proteins
Hirschey, M. D., Shimazu, T., Huang, J., & Verdin, E. (2009) · Methods in Enzymology · doi:10.1016/s0076-6879(09)05008-3 · Cited by 55 · see citing works
Self-citationJi, H. L., & Friedman, M. I. (2008) · International Journal of Obesity · doi:10.1038/ijo.2008.71 · Cited by 35 · see citing works
Race and Sex Similarities in Exercise-Induced Changes in Blood Lipids and Fatness
Ardern, C. I., Katzmarzyk, P. T., Janssen, I., Leon, A. S., Wilmore, J. H., Skinner, J. S., Rao, D. C., Després, J., Rankinen, T., & Bouchard, C. (2004) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000139798.54405.af · Cited by 30 · see citing works
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Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008 · see citing works
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works
NAD+ metabolism and its roles in cellular processes during ageing
Covarrubias, A. J., Perrone, R., Grozio, A., & Verdin, E. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00313-x · Cited by 1,617 · see citing works
Self-citationNAD <sup>+</sup> in aging, metabolism, and neurodegeneration
Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319 · see citing works
Self-citationCantó, C., Houtkooper, R. H., Pirinen, E., Youn, D. Y., Oosterveer, M. H., Cen, Y., Fernandez-Marcos, P. J., Yamamoto, H., Andreux, P. A., Cettour-Rose, P., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.022 · Cited by 1,238 · see citing works
NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Xie, N., Zhang, L., Gao, W. Q., Huang, C., Huber, P., Zhou, X., Li, C. L., Shen, G., & Zou, B. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00311-7 · Cited by 1,076 · see citing works
Ketone bodies as signaling metabolites
Newman, J. C., & Verdin, E. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.09.002 · Cited by 966 · see citing works
Self-citationThe world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 798 · see citing works
Metabolites as regulators of insulin sensitivity and metabolism
Yang, Q., Vijayakumar, A., & Kahn, B. B. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0044-8 · Cited by 680 · see citing works
NAD+ homeostasis in health and disease
Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627 · see citing works
Mammalian Mitochondria and Aging: An Update
Kauppila, T. E. S., Kauppila, J. H. K., & Larsson, N.-G. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.017 · Cited by 578 · see citing works
Oxidative Stress in Type 2 Diabetes: Impacts from Pathogenesis to Lifestyle Modifications
Caturano, A., D’Angelo, M., Mormone, A., Russo, V., Mollica, M. P., Salvatore, T., Galiero, R., Rinaldi, L., Vetrano, E., Marfella, R., et al. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45080420 · Cited by 579 · see citing works
Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)
Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534 · see citing works
Nishida, Y., Rardin, M. J., Carrico, C., He, W., Sahu, A. K., Gut, P., Najjar, R., Fitch, M., Hellerstein, M., Gibson, B. W., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.022 · Cited by 481 · see citing works
Self-citationWagner, G. R., & Payne, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.486753 · Cited by 490 · see citing works
Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target
Zhang, J., Xiang, H., Liu, J., Chen, Y., He, R.-R., & Liu, B. (2020) · Theranostics · doi:10.7150/thno.45922 · Cited by 503 · see citing works
Sirtuins and NAD + in the Development and Treatment of Metabolic and Cardiovascular Diseases
Kane, A. E., & Sinclair, D. A. (2018) · Circulation Research · doi:10.1161/circresaha.118.312498 · Cited by 490 · see citing works
Sirtuin activators and inhibitors: Promises, achievements, and challenges
Dai, H., Sinclair, D. A., Ellis, J. L., & Steegborn, C. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.03.004 · Cited by 463 · see citing works
“, 2010), as well as reducing reactive oxygen species and inflammation (Chalkiadaki and Guarente, 2012; Hirschey et al., 2011; Pfluger et al., 2008; Yoshizaki et al., 2009).”
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Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464 · see citing works
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Murphy, E., Ardehali, H., Balaban, R. S., DiLisa, F., Dorn, G. W., Kitsis, R. N., Otsu, K., Ping, P., Rizzuto, R., Sack, M. N., et al. (2016) · Circulation Research · doi:10.1161/res.0000000000000104 · Cited by 459 · see citing works
Rardin, M. J., Newman, J. C., Held, J. M., Cusack, M. P., Sorensen, D. J., Li, B., Schilling, B., Mooney, S. D., Kahn, C. R., Verdin, E. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302961110 · Cited by 446 · see citing works
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Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446 · see citing works
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Winnik, S. H., Auwerx, J. H., Sinclair, D. A., & Matter, C. M. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv290 · Cited by 444 · see citing works
Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation
Hirschey, M. D., & Zhao, Y. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r114.046664 · Cited by 423 · see citing works
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Nassir, F. (2022) · Biomolecules · doi:10.3390/biom12060824 · Cited by 422 · see citing works
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Morris, B. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.525 · Cited by 380 · see citing works
Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 366 · see citing works
Self-citationRole of Mitochondria in Nonalcoholic Fatty Liver Disease
Nassir, F., & Ibdah, J. A. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15058713 · Cited by 359 · see citing works
Sergi, D., Naumovski, N., Heilbronn, L. K., Abeywardena, M., O’Callaghan, N., Lionetti, L., & Luscombe-Marsh, N. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00532 · Cited by 347 · see citing works
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Muoio, D. M., & Neufer, P. D. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.010 · Cited by 343 · see citing works
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Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works
Carrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331 · see citing works
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Newman, J. C., & Verdin, E. M. (2014) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2014.08.009 · Cited by 334 · see citing works
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Yan, L. (2018) · Animal Models and Experimental Medicine · doi:10.1002/ame2.12001 · Cited by 327 · see citing works
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Wagner, G. R., & Hirschey, M. D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.027 · Cited by 319 · see citing works
Self-citationMichelakis, E. D., Gurtu, V., Webster, L., Barnes, G. D., Watson, G., Howard, L., Cupitt, J., Paterson, D. I., Thompson, R. B., Chow, K., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aao4583 · Cited by 318 · see citing works
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Wang, C., Wu, S., Wu, Y., & Wei, Y. (2013) · Experimental Biology and Medicine · doi:10.1177/1535370213493069 · Cited by 315 · see citing works
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van de Ven, R. A. H., Santos, D., & Haigis, M. C. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.02.005 · Cited by 309 · see citing works
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Hirschey, M. D., DeBerardinis, R. J., Diehl, A. M., Drew, J. E., Frezza, C., Green, M. F., Jones, L. W., Ko, Y. H., Le, A., Lea, M. A., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.10.002 · Cited by 305 · see citing works
Self-citationAnsari, A., Rahman, M. S., Saha, S. K., Saikot, F. K., Deep, A., & Kim, K. (2016) · Aging Cell · doi:10.1111/acel.12538 · Cited by 307 · see citing works
Brown, K. D., Maqsood, S., Huang, J.-Y., Pan, Y., Harkcom, W., Li, W., Sauve, A., Verdin, E., & Jaffrey, S. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.003 · Cited by 277 · see citing works
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Jing, E., O’Neill, B. T., Rardin, M. J., Kleinridders, A., Ilkeyeva, O. R., Ussar, S., Bain, J. R., Lee, K. Y., Verdin, E. M., Newgard, C. B., et al. (2013) · Diabetes · doi:10.2337/db12-1650 · Cited by 283 · see citing works
Self-citationSirtuins: guardians of mammalian healthspan
Giblin, W., Skinner, M. E., & Lombard, D. B. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.04.007 · Cited by 280 · see citing works
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Merksamer, P. I., Liu, Y., He, W., Hirschey, M. D., Chen, D., & Verdin, E. (2013) · Aging · doi:10.18632/aging.100544 · Cited by 275 · see citing works
Self-citationLai, Y.-C., Tabima, D. M., Dube, J. J., Hughan, K. S., Vanderpool, R. R., Goncharov, D. A., St. Croix, C. M., Garcia-Ocaña, A., Goncharova, E. A., Tofovic, S. P., et al. (2016) · Circulation · doi:10.1161/circulationaha.115.018935 · Cited by 270 · see citing works
Mitochondria, Energetics, Epigenetics, and Cellular Responses to Stress
Shaughnessy, D. T., McAllister, K. A., Worth, L., Haugen, A. C., Meyer, J. N., Domann, F. E., Houten, B. V., Mostoslavsky, R., Bultman, S. J., Baccarelli, A., et al. (2014) · Environmental Health Perspectives · doi:10.1289/ehp.1408418 · Cited by 267 · see citing works
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He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262 · see citing works
Self-citationMitochondrial Biogenesis through Activation of Nuclear Signaling ProteinsPreprint
Dominy, J. E., & Puigserver, P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a015008 · Cited by 255 · see citing works
SIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging
Giralt, A., & Villarroya, F. (2012) · Biochemical Journal · doi:10.1042/bj20120030 · Cited by 253 · see citing works
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Wang, T., Cao, Y., Zheng, Q., Tu, J., Zhou, W., He, J., Zhong, J., Chen, Y., Wang, J., Cai, R., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.008 · Cited by 250 · see citing works
Mitochondrial protein acetylation regulates metabolism
Anderson, K. A., & Hirschey, M. D. (2012) · Essays in Biochemistry · doi:10.1042/bse0520023 · Cited by 249 · see citing works
Self-citationCrosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes
Cantó, C., Sauve, A. A., & Bai, P. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.004 · Cited by 246 · see citing works
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Serra, D., Mera, P., Malandrino, M. I., Mir, J. F., & Herrero, L. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4875 · Cited by 246 · see citing works
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Ji, Z., Liu, G., & Qu, J. T. (2021) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2021.11.005 · Cited by 245 · see citing works
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Hesselink, M. K. C., Schrauwen-Hinderling, V., & Schrauwen, P. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.104 · Cited by 242 · see citing works
Softic, S., Meyer, J. G., Wang, G.-X., Gupta, M. K., Batista, T. M., Lauritzen, H. P. M. M., Fujisaka, S., Serra, D., Herrero, L., Willoughby, J., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.09.003 · Cited by 227 · see citing works
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Johnson, M. L., Robinson, M. M., & Nair, K. S. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.12.003 · Cited by 233 · see citing works
Metabolic aspects in NAFLD, NASH and hepatocellular carcinoma: the role of PGC1 coactivators
Piccinin, E., Villani, G., & Moschetta, A. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-018-0089-3 · Cited by 230 · see citing works
Mitochondrial Metabolism, Sirtuins, and AgingPreprint
Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 237 · see citing works
The sirtuin family’s role in aging and age-associated pathologies
Hall, J. A., Dominy, J. E., Lee, Y., & Puigserver, P. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64094 · Cited by 235 · see citing works
The importance of NAMPT / NAD / SIRT1 in the systemic regulation of metabolism and ageing
Imai, S., & Yoshino, J. (2013) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12171 · Cited by 232 · see citing works
From Sirtuin Biology to Human Diseases: An Update
Sebastián, C., Satterstrom, F. K., Haigis, M. C., & Mostoslavsky, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.402768 · Cited by 228 · see citing works
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McDonnell, E., Peterson, B. S., Bomze, H. M., & Hirschey, M. D. (2015) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.06.001 · Cited by 217 · see citing works
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Sinclair, D. A., & Guarente, L. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134657 · Cited by 223 · see citing works
Alrob, O. A., Sankaralingam, S., Ma, C., Wagg, C. S., Fillmore, N., Jaswal, J. S., Sack, M. N., Lehner, R. S., Gupta, M. P., Michelakis, E. D., et al. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu156 · Cited by 221 · see citing works
Molecular mechanism of endothelial and vascular aging: implications for cardiovascular disease
Camici, G. G., Savarese, G., Akhmedov, A., & Lüscher, T. F. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv587 · Cited by 223 · see citing works
PGC-1α, mitochondrial dysfunction, and Huntington's disease
Johri, A., Chandra, A., & Beal, M. F. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.016 · Cited by 223 · see citing works
Paulin, R., Dromparis, P., Sutendra, G., Gurtu, V., Zervopoulos, S., Bowers, L., Haromy, A., Webster, L., Provencher, S., Bonnet, S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.08.011 · Cited by 214 · see citing works
Song, W., Song, Y., Kincaid, B., Bossy, B., & Bossy‐Wetzel, E. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.07.004 · Cited by 215 · see citing works
Mitochondrial protein hyperacetylation in the failing heart
Horton, J. L., Martin, O. J., Lai, L., Riley, N. M., Richards, A., Vega, R. B., Leone, T. C., Pagliarini, D. J., Muoio, D. M., Bedi, K. C., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.84897 · Cited by 208 · see citing works
Molecular Pathogenesis of NASH
Caligiuri, A., Gentilini, A., & Marra, F. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091575 · Cited by 212 · see citing works
Newman, J. C., He, W., & Verdin, E. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.404863 · Cited by 207 · see citing works
Self-citationZhou, X., Chen, M., Zeng, X., Yang, J., Deng, H., Yi, L., & Mt, M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.530 · Cited by 208 · see citing works
Sundaresan, N. R., Bindu, S., Pillai, V. B., Samant, S. A., Pan, Y., Huang, J.-Y., Gupta, M., Nagalingam, R. S., Wolfgeher, D. J., Verdin, E. M., et al. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00586-15 · Cited by 206 · see citing works
Self-citationSources and implications of NADH/NAD+ redox imbalance in diabetes and its complications
Yan, L.-J., Wu, J., Jin, Z., & Zheng, H. (2016) · Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy · doi:10.2147/dmso.s106087 · Cited by 198 · see citing works
The Metabolic Syndrome in Men study: a resource for studies of metabolic and cardiovascular diseases
Laakso, M., Kuusisto, J., Stančáková, A., Kuulasmaa, T., Pajukanta, P., Lusis, A. J., Collins, F. S., Mohlke, K. L., & Boehnke, M. (2017) · Journal of Lipid Research · doi:10.1194/jlr.o072629 · Cited by 204 · see citing works
Self-citationTao, R., Vassilopoulos, A., Parisiadou, L., Yan, Y., & Gius, D. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194 · see citing works
Palomer, X., Azcona, M. S. R., Pizarro‐Delgado, J., Planavila, A., Villarroya, F., Valenzuela‐Alcaráz, B., Crispi, F., Sepúlveda-Martínez, Á., Miguel-Escalada, I., Ferrer, J. P., et al. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0114-1 · Cited by 201 · see citing works
Overmyer, K. A., Evans, C. R., Qi, N., Minogue, C. E., Carson, J. J., Chermside‐Scabbo, C. J., Koch, L. G., Britton, S. L., Pagliarini, D. J., Coon, J. J., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.007 · Cited by 196 · see citing works
Hsu, Y., Wu, Y., Yu, T.-H., & Wei, Y. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.02.011 · Cited by 190 · see citing works
Zhang, X., Ji, R., Liao, X., Castillero, E., Kennel, P. J., Brunjes, D. L., Franz, M., Möbius‐Winkler, S., Drosatos, K., George, I., et al. (2018) · Circulation · doi:10.1161/circulationaha.117.030486 · Cited by 186 · see citing works
NAMPT-Mediated NAD+ Biosynthesis Is Essential for Vision In Mice
Lin, J. B., Kubota, S., Ban, N., Yoshida, M., Santeford, A. C., Sène, A., Nakamura, R. E. I., Zapata, N., Kubota, M., Tsubota, K., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.073 · Cited by 185 · see citing works
Zheng, Y., Wang, S., Wu, J., & Wang, Y. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04367-1 · Cited by 192 · see citing works
SIRT3 regulates mitochondrial protein acetylation and intermediary metabolism
Hirschey, M. D., Shimazu, T., Huang, J. Y., Schwer, B., & Verdin, E. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010850 · Cited by 180 · see citing works
Self-citationSIRT3 promotes lipophagy and chaperon-mediated autophagy to protect hepatocytes against lipotoxicity
Zhang, T., Liu, J., Shen, S., Tong, Q., Ma, X., & Lin, L. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0356-z · Cited by 186 · see citing works
Whole-organism screening for gluconeogenesis identifies activators of fasting metabolism
Gut, P., Baeza-Raja, B., Andersson, O., Hasenkamp, L., Hsiao, J., Hesselson, D., Akassoglou, K., Verdin, E. M., Hirschey, M. D., & Stainier, D. Y. R. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1136 · Cited by 181 · see citing works
Self-citationThe role of mitochondrial sirtuins in health and disease
Osborne, B., Bentley, N. L., Montgomery, M. K., & Turner, N. A. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.197 · Cited by 179 · see citing works
Mitochondrial metabolism in pulmonary hypertension: beyond mountains there are mountains
Culley, M. K., & Chan, S. Y. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120847 · Cited by 178 · see citing works
Bharathi, S. S., Zhang, Y., Mohsen, A.-W. A., Uppala, R., Balasubramani, M., Schreiber, E. M., Uechi, G. T., Beck, M. E., Rardin, M. J., Vockley, J. E., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510354 · Cited by 179 · see citing works
Self-citationVassilopoulos, A., Pennington, J. D., Andresson, T., Rees, D. M., Bosley, A. D., Fearnley, I. M., Ham, A., Flynn, C. R., Hill, S., Rose, K. L., et al. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5420 · Cited by 173 · see citing works
Long-term reprogramming of the innate immune system
Domínguez‐Andrés, J., & Netea, M. G. (2018) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0318-104r · Cited by 176 · see citing works
Suter, M., Chen, A., Burdine, M., Choudhury, M., Harris, R. A., Lane, R. H., Friedman, J. E., Grove, K. L., Tackett, A. J., & Aagaard, K. M. (2012) · The FASEB Journal · doi:10.1096/fj.12-212878 · Cited by 171 · see citing works
SIRT3: A New Regulator of Cardiovascular Diseases
Sun, W., Liu, C., Chen, Q., Liu, N., Yan, Y., & Liu, B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7293861 · Cited by 170 · see citing works
Site-Specific Reactivity of Nonenzymatic Lysine Acetylation
Baeza, J., Smallegan, M. J., & Denu, J. M. (2015) · ACS Chemical Biology · doi:10.1021/cb500848p · Cited by 169 · see citing works
Mitochondrial NAD + /NADH Redox State and Diabetic Cardiomyopathy
Berthiaume, J. M., Kurdys, J., Muntean, D. M., & Rosca, M. G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7415 · Cited by 168 · see citing works
Acetylation of Mitochondrial Proteins in the Heart: The Role of SIRT3
Parodi‐Rullán, R. M., Chapa‐Dubocq, X. R., & Javadov, S. A. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01094 · Cited by 168 · see citing works
Perico, L., Morigi, M., Rota, C., Breno, M., Mele, C., Noris, M., Introna, M., Capelli, C., Longaretti, L., Rottoli, D., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00937-2 · Cited by 165 · see citing works
Mitochondrial protein acetylation is driven by acetyl-CoA from fatty acid oxidation
Pougovkina, O., Brinke, H. T., Ofman, R., van Cruchten, A. G., Kulik, W., Wanders, R. J. A., Houten, S. M., & de Boer, V. C. J. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu059 · Cited by 161 · see citing works
Zeng, X., Yang, J., Hu, O., Huang, J., Li, R., Chen, M., Zhang, Y., Zhou, X., Zhu, J., Zhang, Q., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7172 · Cited by 163 · see citing works
- Authors
- Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., Stevens, R. D., Muehlbauer, M. J., Kakar, S., Bass, N. M., Kuusisto, J., Laakso, M., Alt, F. W., Newgard, C. B., Farese, R. V., Kahn, C. R., & Verdin, E.
- Affiliations
- Gladstone Institutes (US)
- Joslin Diabetes Center (US)
- University of California, San Francisco (US)
- University of Eastern Finland (FI)
- University of Pittsburgh (US)
- San Francisco VA Medical Center (US)
- Duke University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Verdin, Eric
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 44
- Issue
- 2
- Pages
- 177-190
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3563434
- OpenAlex
- W2040625305
- Cited by
- 787
- References
- 81
- Citations by year
- 2026: 26 · 2025: 29 · 2024: 35 · 2023: 38 · 2022: 53 · 2021: 74 · 2020: 59 · 2019: 65 · 2018: 75 · 2017: 52 · 2016: 77 · 2015: 52 · 2014: 49 · 2013: 63 · 2012: 34
- FWCI
- 23.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of Diabetes and Digestive and Kidney Diseases (U01DK061730, R24DK085610, U24DK059637, R03DK088870, K01DK076573, P30DK026743, U01DK061731, U01DK061713, U01DK061728, U01DK061737, U01DK061732, U01DK061734, U01DK061718, U01DK061738)
- National Center for Research Resources (UL1RR024989, M01RR000750, KL2RR024130, M01RR020359, M01RR000065, M01RR000188, UL1RR025741, M01RR000827)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- SIRT3, mitochondrial protein acetylation, metabolic syndrome, high-fat diet, hepatic steatosis, insulin resistance, hyperlipidemia, obesity, stearoyl-CoA desaturase 1, SIRT3 knockout mice, single nucleotide polymorphisms, post-translational modification
- MeSH terms
- Acetylation, Animals, Humans, Models, Biological, Mice, Knockout, Mitochondrial Proteins, Metabolic Syndrome, Mice, Sirtuin 3, Diet, High-Fat
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