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.
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
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?
Sirt3 is an established deacetylase whose targets include LCAD, succinate dehydrogenase, and SOD2.
“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
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 [85]
Loss of SIRT3 inhibits fatty acid oxidation.
“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
Loss of SIRT3 decreases gluconeogenic glucose production after cold challenge and decreases beta-hydroxybutyrate production during fasting.
“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
SIRT3 is upregulated during fasting.
“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
Mice lacking SIRT3 share characteristics of human fatty acid oxidation disorders, including cold intolerance and reduced basal ATP levels.
“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
SIRT3 promotes efficient lipid utilization during fasting by activating long-chain acyl-CoA dehydrogenase via deacetylation at K42.
“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
Mice lacking SIRT3 accumulate β-oxidation precursors and intermediates, including triglycerides and long-chain fatty acids.
“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 mice, SIRT3 is normally upregulated during fasting in liver and brown fat where it plays a role in fatty-acid oxidation by maintaining deacetylation of long-chain acyl coenzyme A dehydrogenase in mitochondria.
“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]
SIRT3-deficient mice show reduced utilization of lipid stores during fasting: decreased fatty acid oxidation, accumulation of triglycerides, and diminished production of hepatic ATP.
“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]
Upon fasting, SIRT3 expression is rapidly induced and deacetylates key residues on mitochondrial proteins.
“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
One week of HFD enhanced SIRT3 levels and prevented mitochondrial hyperacetylation despite higher levels of lipid substrates.
“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
Dietary excess of lipids dramatically changes mitochondrial protein acetylation.
“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
Prolonged HFD dramatically decreases SIRT3 expression, correlating with the appearance of mitochondrial hyperacetylation and mitochondrial dysfunction.
“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
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.
“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].”
SIRT3 regulates mitochondrial fatty acid β-oxidation via deacetylation of long-chain acyl-CoA dehydrogenase, and dysregulation of this process results in defective fatty acid oxidation.
“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
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., 2010
SIRT3 is present in mitochondria, where it regulates the acetylation and activity of a variety of metabolic enzymes.
“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.
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 278 · see citing works
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 · see citing works
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 · see citing works
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/y59-099 · Cited by 23,189 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationSrere, P. A. (1969) · Methods in Enzymology · doi:10.1016/0076-6879(69)13005-0 · Cited by 2,005 · 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
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 · see citing works
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 · 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-citationImmunoaffinity profiling of tyrosine phosphorylation in cancer cells
Rush, A. J., Moritz, A., Lee, K. A., Guo, A., Goss, V. L., Spek, E. J., Zhang, H., Zha, X., Polakiewicz, R. D., & Comb, M. J. (2004) · Nature Biotechnology · doi:10.1038/nbt1046 · Cited by 1,126 · see citing works
Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival
Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950 · see citing works
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works
Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works
Self-citationLipid oxidation is reduced in obese human skeletal muscle
Kim, J.-Y., Hickner, R. C., Cortright, R. L., Dohm, G. L., & Houmard, J. A. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.279.5.e1039 · Cited by 634 · 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-citationTargher, G., Bertolini, L., Poli, F., Rodella, S., Scala, L., Tessari, R., Zenari, L., & Falezza, G. (2005) · Diabetes · doi:10.2337/diabetes.54.12.3541 · Cited by 577 · see citing works
Sirtuins as potential targets for metabolic syndrome
Guarente, L. (2006) · Nature · doi:10.1038/nature05486 · Cited by 468 · see citing works
Mammalian mitochondrial β -oxidation
Eaton, S. D., Bartlett, K., & Pourfarzam, M. (1996) · Biochemical Journal · doi:10.1042/bj3200345 · Cited by 425 · see citing works
Conserved Metabolic Regulatory Functions of Sirtuins
Schwer, B., & Verdin, E. M. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.006 · Cited by 415 · see citing works
Self-citationUeki, K., Kondo, T., Tseng, Y., & Kahn, C. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402511101 · Cited by 382 · see citing works
Self-citationZhang, 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
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 · see citing works
Self-citationKurtz, 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
Nonalcoholic Fatty Liver Disease Is a Risk Factor for Type 2 Diabetes in Middle-Aged Japanese Men
Shibata, M., Kihara, Y., Taguchi, M., Tashiro, M., & Otsuki, M. (2007) · Diabetes Care · doi:10.2337/dc07-0792 · Cited by 238 · see citing works
Saha, A. K., Avilucea, P. R., Ye, J.-M., Assifi, M. M., Kraegen, E. W., & Ruderman, N. B. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.120 · Cited by 218 · see citing works
Self-citationSignificant correlations between severe fatty liver and risk factors for metabolic syndrome
Hsiao, P., Kuo, K., Shin, S., Yang, Y., Lin, W., Yang, J., Chiu, C., Chuang, W., Tsai, T., & Yu, M. (2006) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2006.04698.x · Cited by 152 · see citing works
Compensatory Responses to Pyruvate Carboxylase Suppression in Islet β-Cells
Jensen, M. V., Joseph, J. W., Ilkayeva, O., Burgess, S. C., Lu, D., Ronnebaum, S. M., Odegaard, M. L., Becker, T. C., Sherry, A. D., & Newgard, C. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604350200 · Cited by 144 · see citing works
Self-citationStremmel, W., & Berk, P. D. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.10.3086 · Cited by 144 · see citing works
Database of mRNA gene expression profiles of multiple human organsPreprint
Son, C., Bilke, S., Davis, S. R., Greer, B. T., Wei, J. S., Whiteford, C. C., Chen, Q., Cenacchi, N., & Khan, J. I. (2005) · Genome Research · doi:10.1101/gr.3124505 · Cited by 130 · see citing works
Cox, K. B. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.19.2069 · Cited by 120 · see citing works
Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts
Frerman, F. E., & Goodman, S. I. (1985) · Biochemical Medicine · doi:10.1016/0006-2944(85)90124-3 · Cited by 114 · see citing works
Medium-Chain Acyl-CoA Dehydrogenase Deficiency in Gene-Targeted Mice
Tolwani, R. J., Hamm, D. A., Tian, L., Sharer, J. D., Vockley, J. E., Rinaldo, P., Matern, D., Schoeb, T. R., & Wood, P. A. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0010023 · Cited by 112 · see citing works
Yechoor, V. K., Patti, M., Ueki, K., Laustsen, P. G., Saccone, R., Rauniyar, R. K., & Kahn, C. R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407574101 · Cited by 106 · see citing works
Self-citationWu, J.-Y., Kao, H., Li, S., Stevens, R., Hillman, S. L., Millington, D. S., & Chen, Y.-T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19574 · Cited by 104 · see citing works
Self-citationIsolation 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
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
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-citationMouse Models for Disorders of Mitochondrial Fatty Acid -Oxidation
Schuier, A. M., & Wood, P. A. (2002) · ILAR Journal · doi:10.1093/ilar.43.2.57 · Cited by 54 · see citing works
Adipose tissue gene expression profiles in ob/ob mice treated with leptin
Zhang, W., Della‐Fera, M. A., Hartzell, D. L., Hausman, D. B., & Baile, C. A. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.04.021 · Cited by 53 · see citing works
Herrema, H., Derks, T. G. J., van Dijk, T. H., Bloks, V. W., Gerding, A., Havinga, R., Tietge, U. J. F., Müller, M. M., Smit, P. G. A., Kuipers, F., et al. (2008) · Hepatology · doi:10.1002/hep.22284 · Cited by 38 · see citing works
Evidence for Impaired Gluconeogenesis in Very Long-chain Acyl-CoA Dehydrogenase-deficient Mice
Spiekerkoetter, U., Ruiter, J. P. N., Tokunaga, C., Wendel, U., Mayatepek, E., Wijburg, F. A., Strauss, A. W., & Wanders, R. J. A. (2006) · Hormone and Metabolic Research · doi:10.1055/s-2006-954581 · Cited by 22 · see citing works
Assays of Fatty Acid β‐Oxidation Activity
Bennett, M. J. (2007) · Methods in cell biology · doi:10.1016/s0091-679x(06)80009-9 · Cited by 19 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Exercise Metabolism and the Molecular Regulation of Skeletal Muscle Adaptation
Egan, B., & Zierath, J. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.012 · Cited by 2,084 · see citing works
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
Energy Metabolism in the Liver
Rui, L. (2014) · Comprehensive physiology · doi:10.1002/cphy.c130024 · Cited by 2,258 · 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-citationFunctions and mechanisms of non-histone protein acetylation
Narita, T., Weinert, B. T., & Choudhary, C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0081-3 · Cited by 1,232 · see citing works
Someya, 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
SIRT1 and other sirtuins in metabolism
Chang, H.-C., & Guarente, L. (2014) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.12.001 · Cited by 1,138 · see citing works
den Besten, G., Bleeker, A., Gerding, A., van Eunen, K., Havinga, R., van Dijk, T. H., Oosterveer, M. H., Jonker, J. W., Groen, A. K., Reijngoud, D.-J., et al. (2015) · Diabetes · doi:10.2337/db14-1213 · Cited by 1,125 · see citing works
NAD(H) and NADP(H) Redox Couples and Cellular Energy Metabolism
Xiao, W., Wang, R., Handy, D. E., & Loscalzo, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7216 · Cited by 1,074 · 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
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
Mitochondrial dysfunction in pathophysiology of heart failure
Zhou, B., & Tian, R. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120849 · Cited by 934 · see citing works
The Biochemistry and Physiology of Mitochondrial Fatty Acid β-Oxidation and Its Genetic Disorders
Houten, S. M., Violante, S. N., Ventura, F. V., & Wanders, R. J. A. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105045 · Cited by 938 · see citing works
Acetyl-CoA and the regulation of metabolism: mechanisms and consequences
Shi, L., & Tu, B. P. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.02.003 · Cited by 903 · see citing works
Camacho-Pereira, J., Tarragó, M. G., Chini, C. C. S., Nin, V., Escande, C., Warner, G. M., Puranik, A. S., Schoon, R. A., Reid, J. M., Galina, A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.006 · Cited by 901 · see citing works
β-Hydroxybutyrate: A Signaling Metabolite
Newman, J. C., & Verdin, E. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064916 · Cited by 872 · see citing works
Self-citationTherapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence
Rajman, L., Chwalek, K., & Sinclair, D. A. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.011 · Cited by 865 · see citing works
The 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
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
Self-citationMetabolic reprogramming and epigenetic modifications on the path to cancer
Sun, L., Zhang, H., & Gao, P. (2021) · Protein & Cell · doi:10.1007/s13238-021-00846-7 · Cited by 796 · see citing works
SIRT3 Opposes Reprogramming of Cancer Cell Metabolism through HIF1α Destabilization
Finley, L. W. S., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya-Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.02.014 · Cited by 782 · see citing works
Liu, P., Wang, Y., Yang, G., Zhang, Q., Meng, L., Xin, Y., & Jiang, X. M. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105420 · Cited by 787 · see citing works
Flipping the Metabolic Switch: Understanding and Applying the Health Benefits of Fasting
Anton, S. D., Moehl, K., Donahoo, W. T., Marosi, K., Lee, S. A., Mainous, A. G., Leeuwenburgh, C., & Mattson, M. P. (2017) · Obesity · doi:10.1002/oby.22065 · Cited by 782 · see citing works
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 757 · see citing works
Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism
Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horváth, T. L., Sinclair, D. A., Pfluger, P. T., & Tschöp, M. H. (2012) · Physiological Reviews · doi:10.1152/physrev.00022.2011 · Cited by 712 · see citing works
Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
Verdin, E., Hirschey, M. D., Finley, L. W. S., & Haigis, M. C. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.003 · Cited by 661 · see citing works
Self-citationCircadian Clock NAD + Cycle Drives Mitochondrial Oxidative Metabolism in Mice
Peek, C. B., Affinati, A. H., Ramsey, K. M., Kuo, H.-Y., Yu, W., Sena, L. A., Ilkayeva, O., Marcheva, B., Kobayashi, Y., Omura, C., et al. (2013) · Science · doi:10.1126/science.1243417 · Cited by 658 · see citing works
Self-citationPGC-1 α , Inflammation, and Oxidative Stress: An Integrative View in Metabolism
Rius‐Pérez, S., Torres-Cuevas, I., Millán, I., Ortega, Á., & Pérez, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1452696 · Cited by 648 · see citing works
Mitochondrial dysfunction in diabetic kidney disease
Forbes, J. M., & Thorburn, D. R. (2018) · Nature Reviews Nephrology · doi:10.1038/nrneph.2018.9 · Cited by 641 · see citing works
Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636 · see citing works
Radak, Z. O., Zhao, Z., Koltai, E., Ohno, H., & Atalay, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4498 · Cited by 616 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Cytosolic lipolysis and lipophagy: two sides of the same coin
Zechner, R., Madeo, F., & Kratky, D. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.76 · Cited by 550 · see citing works
Lundby, A., Lage, K., Weinert, B. T., Bekker‐Jensen, D. B., Secher, A., Skovgaard, T., Kelstrup, C. D., Dmytriyev, A., Choudhary, C., Lundby, C., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.07.006 · Cited by 544 · see citing works
Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C., Palmeira, C. M., Rosenzweig, A., & Sinclair, D. A. (2010) · Aging · doi:10.18632/aging.100252 · Cited by 547 · see citing works
The dynamic regulation of NAD metabolism in mitochondria
Stein, L. R., & Imai, S. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.06.005 · Cited by 529 · 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
Mitochondrial dysfunction and the inflammatory response
López-Armada, M. J., Riveiro-Naveira, R. R., Vaamonde‐García, C., & Valcarcel‐Ares, M. N. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.01.003 · Cited by 528 · see citing works
Metabolism and the Circadian Clock Converge
Eckel‐Mahan, K. L., & Sassone‐Corsi, P. (2013) · Physiological Reviews · doi:10.1152/physrev.00016.2012 · Cited by 530 · see citing works
Acylcarnitines: Nomenclature, Biomarkers, Therapeutic Potential, Drug Targets, and Clinical Trials
Dambrova, M., Makrecka‐Kuka, M., Kuka, J., Vilšķe̅rsts, R., Nordberg, D. O. T., Attwood, M. M., Smesny, S., Şen, Z. D., Guo, A. C., Oler, E., et al. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000408 · Cited by 528 · see citing works
Guarente, L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1100831 · Cited by 510 · see citing works
The multifaceted functions of sirtuins in cancer
Chalkiadaki, A., & Guarente, L. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3985 · Cited by 501 · see citing works
Wagner, G. R., & Payne, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.486753 · Cited by 490 · see citing works
SIRT1 in Neurodevelopment and Brain Senescence
Herskovits, A. Z., & Guarente, L. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.028 · Cited by 493 · 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
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-citationThe sirtuin SIRT6 blocks IGF-Akt signaling and development of cardiac hypertrophy by targeting c-Jun
Sundaresan, N. R., Vasudevan, P., Zhong, L., Kim, G. H., Samant, S. A., Parekh, V., Pillai, V. B., Veeranna, R. P., Gupta, M., Jeevanandam, V., et al. (2012) · Nature Medicine · doi:10.1038/nm.2961 · Cited by 477 · see citing works
Self-citationSirtuins, a promising target in slowing down the ageing process
Grabowska, W., Sikora, E., & Bielak-Zmijewska, A. (2017) · Biogerontology · doi:10.1007/s10522-017-9685-9 · Cited by 470 · see citing works
Jing, E., Emanuelli, B., Hirschey, M. D., Boucher, J., Lee, K. Y., Lombard, D., Verdin, E. M., & Kahn, C. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111308108 · Cited by 469 · see citing works
Self-citationCalorie restriction and sirtuins revisited
Guarente, L. (2013) · Genes & Development · doi:10.1101/gad.227439.113 · Cited by 464 · see citing works
Mitochondrial Function, Biology, and Role in Disease
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
Mitochondria and Reactive Oxygen Species in Aging and Age-Related Diseases
Giorgi, C., Marchi, S., Simões, I. C. M., Ren, Z., Morciano, G., Perrone, M., Patalas‐Krawczyk, P., Borchard, S., Jędrak, P., Pierzynowska, K., et al. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.006 · Cited by 467 · see citing works
SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage.
Tseng, A. H., Shieh, S., & Wang, D. (2013) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2013.05.002 · Cited by 445 · see citing works
Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3
Pillai, V. B., Samant, S. A., Sundaresan, N. R., Raghuraman, H., Kim, G. H., Bonner, M. Y., Arbiser, J. L., Walker, D. I., Jones, D. P., Gius, D. R., et al. (2015) · Nature Communications · doi:10.1038/ncomms7656 · Cited by 453 · 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
Self-citationYu, W., Dittenhafer‐Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355206 · Cited by 445 · see citing works
Jeong, S. M., Xiao, C., Finley, L. W. S., Lahusen, T., Souza, A. L., Pierce, K., Li, Y.-H., Wang, X., Laurent, G., German, N. J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.024 · Cited by 445 · see citing works
Self-citationProtective effects of sirtuins in cardiovascular diseases: from bench to bedside
Winnik, S. H., Auwerx, J. H., Sinclair, D. A., & Matter, C. M. (2015) · European Heart Journal · doi:10.1093/eurheartj/ehv290 · Cited by 443 · see citing works
Metabolic Inflexibility: When Mitochondrial Indecision Leads to Metabolic Gridlock
Muoio, D. M. (2014) · Cell · doi:10.1016/j.cell.2014.11.034 · Cited by 438 · see citing works
SIRT3 Reverses Aging-Associated Degeneration
Brown, K., Xie, S., Qiu, X., Mohrin, M., Shin, J., Liu, Y., Zhang, D., Scadden, D. T., & Chen, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.005 · Cited by 436 · see citing works
Metabolic control of epigenetics in cancer
Kinnaird, A. S., Zhao, S., Wellen, K. E., & Michelakis, E. D. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.82 · Cited by 419 · see citing works
The nexus of chromatin regulation and intermediary metabolism
Gut, P., & Verdin, E. M. (2013) · Nature · doi:10.1038/nature12752 · Cited by 419 · see citing works
Self-citationJiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K., & Zhao, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.028 · Cited by 415 · see citing works
Tumor metastasis to lymph nodes requires YAP-dependent metabolic adaptation
Lee, C., Jeong, S., Jang, C., Bae, H., Kim, Y. H., Park, I., Kim, S. K., & Koh, G. Y. (2019) · Science · doi:10.1126/science.aav0173 · Cited by 405 · see citing works
NAFLD: Mechanisms, Treatments, and Biomarkers
Nassir, F. (2022) · Biomolecules · doi:10.3390/biom12060824 · Cited by 422 · 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
Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases
Imai, S., & Guarente, L. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.02.003 · Cited by 387 · see citing works
Nuclear DNA damage signalling to mitochondria in ageing
Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387 · see citing works
Are sirtuins viable targets for improving healthspan and lifespan?
Baur, J. A., Ungvari, Z. I., Minor, R. K., Couteur, D. G. L., & de Cabo, R. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3738 · Cited by 389 · see citing works
Fatty liver is associated with reduced SIRT3 activity and mitochondrial protein hyperacetylation
Kendrick, A. A., Choudhury, M., Rahman, S. M., McCurdy, C. E., Friederich, M., Van Hove, J. L. K., Watson, P. A., Birdsey, N., Bao, J., Gius, D., et al. (2011) · Biochemical Journal · doi:10.1042/bj20100791 · Cited by 382 · see citing works
Self-citationEnergy Metabolism in the Liver
Rui, L. (2014) · Comprehensive physiology · doi:10.1002/j.2040-4603.2014.tb00548.x · Cited by 382 · see citing works
Seven sirtuins for seven deadly diseases ofaging
Morris, B. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.525 · Cited by 380 · see citing works
The role of sirtuins in cardiac disease
Matsushima, S., & Sadoshima, J. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00053.2015 · Cited by 378 · see citing works
Dikalova, A., Pandey, A. K., Xiao, L., Arslanbaeva, L. R., Sidorova, T. N., Lopez, M. G., Billings, F. T., Verdin, E. M., Auwerx, J. H., Harrison, D. G., et al. (2019) · Circulation Research · doi:10.1161/circresaha.119.315767 · Cited by 374 · see citing works
Self-citationLysine 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-citationMitochondrial function in hypoxic ischemic injury and influence of aging
Ham, P. B., & Raju, R. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.006 · Cited by 367 · see citing works
AMPK regulation of fatty acid metabolism and mitochondrial biogenesis: implications for obesity.
O’Neill, H. M., Holloway, G. P., & Steinberg, G. R. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.06.019 · Cited by 364 · see citing works
Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity
Finley, L. W. S., Haas, W., Desquiret‐Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., & Haigis, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023295 · Cited by 364 · see citing works
Role 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
Circadian Reprogramming in the Liver Identifies Metabolic Pathways of Aging
Sato, S., Solanas, G., Peixoto, F. O., Bee, L., Symeonidi, A., Schmidt, M. S., Brenner, C., Masri, S., Benitah, S. A., & Sassone‐Corsi, P. (2017) · Cell · doi:10.1016/j.cell.2017.07.042 · Cited by 359 · see citing works
The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy
Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 358 · see citing works
Histone Acetylation Enzymes Coordinate Metabolism and Gene Expression
Shen, Y., Wei, W., & Zhou, D. (2015) · Trends in Plant Science · doi:10.1016/j.tplants.2015.07.005 · Cited by 355 · see citing works
Sirtuins in Renal Health and Disease
Morigi, M., Perico, L., & Benigni, A. (2018) · Journal of the American Society of Nephrology · doi:10.1681/asn.2017111218 · Cited by 359 · see citing works
Regulation of intermediary metabolism by protein acetylation
Guan, K., & Xiong, Y. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.003 · Cited by 353 · 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
Sirtuins mediate mammalian metabolic responses to nutrient availability
Chalkiadaki, A., & Guarente, L. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.225 · Cited by 342 · see citing works
The Search for Antiaging Interventions: From Elixirs to Fasting Regimens
de Cabo, R., Carmona-Gutierrez, D., Bernier, M., Hall, M. N., & Madeo, F. (2014) · Cell · doi:10.1016/j.cell.2014.05.031 · Cited by 345 · see citing works
Lipid-Induced Mitochondrial Stress and Insulin Action in Muscle
Muoio, D. M., & Neufer, P. D. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.010 · Cited by 343 · see citing works
Yang, W., Nagasawa, K., Münch, C., Xu, Y., Satterstrom, F. K., Jeong, S., Hayes, S., Jedrychowski, M. P., Vyas, F. S., Zaganjor, E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.10.016 · Cited by 341 · see citing works
Normalization of NAD + Redox Balance as a Therapy for Heart Failure
Lee, C. F., Chavez, J. D., Garcia‐Menendez, L., Choi, Y. S., Roe, N. D., Chiao, Y. A., Edgar, J. S., Goo, Y. A., Goodlett, D. R., Bruce, J. E., et al. (2016) · Circulation · doi:10.1161/circulationaha.116.022495 · Cited by 337 · see citing works
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
Corbet, C., Pinto, A., Martherus, R., de Jesus, J. T. C. L., Polet, F., & Féron, O. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.003 · Cited by 335 · see citing works
Effects of Oxidative Stress on Mesenchymal Stem Cell Biology
Denu, R. A., & Hematti, P. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2989076 · Cited by 331 · see citing works
Protein acetylation in metabolism – metabolites and cofactors
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
Self-citationβ-hydroxybutyrate: Much more than a metabolite
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
Self-citationThe metabolic regulation of aging
Finkel, T. (2015) · Nature Medicine · doi:10.1038/nm.3998 · Cited by 325 · see citing works
SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells
Nasrin, N., Wu, X.-P., Fortier, E., Feng, Y., Bare, O., Chen, S., Ren, X., Wu, Z., Streeper, R. S., & Bordone, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.124164 · Cited by 323 · see citing works
Nonenzymatic Protein Acylation as a Carbon Stress Regulated by Sirtuin Deacylases
Wagner, G. R., & Hirschey, M. D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.027 · Cited by 319 · see citing works
Self-citation
- 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 › 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
