The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Open accessAbstract
AMP-activated protein kinase (AMPK) is a metabolic fuel gauge conserved along the evolutionary scale in eukaryotes that senses changes in the intracellular AMP/ATP ratio. Recent evidence indicated an important role for AMPK in the therapeutic benefits of metformin, thiazolidinediones and exercise, which form the cornerstones of the clinical management of type 2 diabetes and associated metabolic disorders. In general, activation of AMPK acts to maintain cellular energy stores, switching on catabolic pathways that produce ATP, mostly by enhancing oxidative metabolism and mitochondrial biogenesis, while switching off anabolic pathways that consume ATP. This regulation can take place acutely, through the regulation of fast post-translational events, but also by transcriptionally reprogramming the cell to meet energetic needs. Here we demonstrate that AMPK controls the expression of genes involved in energy metabolism in mouse skeletal muscle by acting in coordination with another metabolic sensor, the NAD+-dependent type III deacetylase SIRT1. AMPK enhances SIRT1 activity by increasing cellular NAD+ levels, resulting in the deacetylation and modulation of the activity of downstream SIRT1 targets that include the peroxisome proliferator-activated receptor-gamma coactivator 1alpha and the forkhead box O1 (FOXO1) and O3 (FOXO3a) transcription factors. The AMPK-induced SIRT1-mediated deacetylation of these targets explains many of the convergent biological effects of AMPK and SIRT1 on energy metabolism.
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“The synthesis of mitochondria in myocytes is upregulated to meet the demands associated with an increase in capillary density, which in turn leads to increased oxygen extraction and metabolism122 through the induction of calcium and metabolic signalling pathways such as those involving 5’-AMP-activated serine/threonine-protein kinase (AMPK) and sirtuins123.”
From Sarcopenic obesity in older adults: aetiology, epidemiology and treatment strategies (2018) · cites this paper as [123]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“SIRT1 increases mitochondrial activity and biogenesis by deacetylating and activating PGC1α (peroxisome proliferator-activated receptor-γ co-activator 1α) [102].”
From NAD+ Precursors Nicotinamide Mononucleotide (NMN) and Nicotinamide Riboside (NR): Potential Dietary Contribution to Health (2023) · cites this paper as [102]
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“The adenosine monophosphate-activated protein kinase (AMPK) is a cellular energy regulator which senses changes in the intracellular AMP/ATP ratio. During energy limitation, low levels of ATP activate AMPK, which acts to maintain cellular energy stores.”
From NAD+ Precursors Nicotinamide Mononucleotide (NMN) and Nicotinamide Riboside (NR): Potential Dietary Contribution to Health (2023) · cites this paper as [102]
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“Thus, AMPK enhances the SIRT1 activity by increasing cellular NAD+ levels, resulting in the deacetylation and modulation of the activity of energy metabolism-related downstream SIRT1 targets, which include the PGC1α, the forkhead box O1 (FOXO1) and O3 (FOXO3a) transcription factors [102].”
From NAD+ Precursors Nicotinamide Mononucleotide (NMN) and Nicotinamide Riboside (NR): Potential Dietary Contribution to Health (2023) · cites this paper as [102]
In the citing paper
“In support of this hypothesis, it has now been demonstrated in mammalian systems that lifespan-extending metabolic manipulations, such as exercise75–77, caloric restriction78, time-restricted feeding and a ketogenic diet79, as well as healthy circadian rhythms1,11 (including regular sleep patterns80), work in part by increasing NAD+ levels, which leads to the activation of sirtuins.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [77]
In the citing paper
“SIRT1 is known to be activated in response to metabolic changes, such as low glucose or exercise, that increase cellular NAD+ (62, 354).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [62]
In the citing paper
“Drug-induced activation of AMPK produces gene expression patterns similar to those observed during exercise (104).”
From Diet and physical exercise as key players to tackle MASLD through improvement of insulin resistance and metabolic flexibility (2024) · cites this paper as [104]
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“Deacetylation of FOXO1 and FOXO3a by SIRT1 (19, 20) mediates autophagic signaling in muscle cells, and aging attenuates SIRT1, which reduces autophagy (134).”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [19]
In the citing paper
“Recent studies show that AMPK also enhances SIRT1 activity by increasing cellular NAD+ levels, resulting in the deacetylation and modulation of the activity of downstream SIRT1 targets 160.”
From Cellular bioenergetics as a target for obesity therapy (2010) · cites this paper as [160]
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Cites
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290
Self-citationLagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.11.013 · Cited by 4,057
Self-citationTranscriptional 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
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
Self-citationAMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491
AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
Hardie, D. G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2249 · Cited by 2,261
Bile acids induce energy expenditure by promoting intracellular thyroid hormone activation
Watanabe, M., Houten, S. M., Mataki, C., Christoffolete, M. A., Kim, B. W., Sato, H., Messaddeq, N., Harney, J. W., Ezaki, O., Kodama, T., et al. (2006) · Nature · doi:10.1038/nature04330 · Cited by 2,220
Self-citationThe Kinase LKB1 Mediates Glucose Homeostasis in Liver and Therapeutic Effects of Metformin
Shaw, R. J., Lamia, K. A., Vasquez, D., Koo, S.-H., Bardeesy, N., DePinho, R. A., Montminy, M., & Cantley, L. C. (2005) · Science · doi:10.1126/science.1120781 · Cited by 1,950
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Geng, T., Liu, Y., Xu, Y., Jiang, Y., Zhang, N., Wang, Z., Carmichael, G., Taylor, H. S., Li, D., & Huang, Y. (2018) · Diabetes · doi:10.2337/db18-0370 · Cited by 101
SIRT1 Antagonizes Oxidative Stress in Diabetic Vascular Complication
Meng, T., Qin, W., & Liu, B. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.568861 · Cited by 100
The aldolase inhibitor aldometanib mimics glucose starvation to activate lysosomal AMPK
Zhang, C., Li, M., Wang, Y., Li, X., Zong, Y., Long, S., Zhang, M., Feng, J.-W., Wei, X., Liu, Y., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00640-7 · Cited by 104
Packer, M. (2023) · European Heart Journal · doi:10.1093/eurheartj/ehad235 · Cited by 100
Transcriptional control of mitochondrial biogenesis and its interface with inflammatory processes
Piantadosi, C. A., & Suliman, H. B. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.01.003 · Cited by 101
Tong, J. F., Yan, X., Zhu, M. J., & Du, . (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22272 · Cited by 100
Chen, Z. B., Shentu, T., Wen, L., Johnson, D. A., & Shyy, J. Y.-J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4803 · Cited by 99
Xu, S., Bai, P., Little, P. J., & Liu, P. (2013) · Medicinal Research Reviews · doi:10.1002/med.21300 · Cited by 99
Mitochondria as pharmacological targets in Down syndrome
Valenti, D., Braidy, N., Rasmo, D. D., Signorile, A., Rossi, L., Atanasov, A. G., Volpicella, M., Henrion‐Caude, A., Nabavi, S. M., & Vacca, R. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.014 · Cited by 99
Mitochondrial stress management: a dynamic journey
Valera‐Alberni, M., & Cantó, C. (2018) · Cell Stress · doi:10.15698/cst2018.10.158 · Cited by 99
Self-citationLee, H. S., Lim, S.-M., Jung, J. I., Kim, S. M., Lee, J. K., Kim, Y. H., Cha, K. M., Oh, T. K., Moon, J. M., Kim, T. Y., et al. (2019) · Nutrients · doi:10.3390/nu11102475 · Cited by 99
The Role of microRNAs in Metabolic Syndrome-Related Oxidative Stress
Włodarski, A., Strycharz, J., Wróblewski, A. M., Kasznicki, J., Drzewoski, J., & Śliwińska, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186902 · Cited by 99
Cardiac SIRT1 ameliorates doxorubicin-induced cardiotoxicity by targeting sestrin 2
Wang, J., Tang, Y., Zhang, J., Wang, J., Xiao, M., Lu, G., Li, J., Liu, Q., Guo, Y., & Gu, J. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102310 · Cited by 99
Restoring the infected powerhouse: Mitochondrial quality control in sepsis
Chavez, F. L., Gartzke, L. P., van Beuningen, F. E., Wink, S. E., Henning, R. H., Krenning, G., & Bouma, H. R. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102968 · Cited by 99
Pasinetti, G. M., Wang, J., Marambaud, P., Ferruzzi, M. G., Gregor, P., Knable, L. A., & Ho, L. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.08.014 · Cited by 99
The Protein Level of PGC-1α, a Key Metabolic Regulator, Is Controlled by NADH-NQO1
Adamovich, Y., Shlomai, A., Tsvetkov, P., Umansky, K. B., Reuven, N. B., Estall, J. L., Spiegelman, B. M., & Shaul, Y. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01672-12 · Cited by 99
Garaulet, M., Esteban Tardido, A., Lee, Y.-C., Smith, C. E., Parnell, L. D., & Ordovás, J. M. (2012) · International Journal of Obesity · doi:10.1038/ijo.2011.270 · Cited by 98
AMP-activated protein kinase as a key molecular link between metabolism and clockwork
Lee, Y., & Kim, E. K. (2013) · Experimental & Molecular Medicine · doi:10.1038/emm.2013.65 · Cited by 100
Liu, P., Zou, D., Yi, L., Chen, M., Gao, Y., Zhou, R., Zhang, Q., Zhou, Y. G., Zhu, J., Chen, K., et al. (2015) · Restorative Neurology and Neuroscience · doi:10.3233/rnn-140446 · Cited by 98
Regulation of Immune Cell Functions by Metabolic Reprogramming
Kim, J. (2018) · Journal of Immunology Research · doi:10.1155/2018/8605471 · Cited by 97
Xenohormesis: health benefits from an eon of plant stress response evolution
Hooper, P. L., Hooper, P. L., Tytell, M., & Vígh, L. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0206-x · Cited by 97
Zmrzljak, U. P., & Rozman, D. (2012) · Chemical Research in Toxicology · doi:10.1021/tx200538r · Cited by 97
Sikka, A., Kaur, M., Agarwal, C., Deep, G., & Agarwal, R. (2012) · Cell Cycle · doi:10.4161/cc.19798 · Cited by 96
Hypothalamic AMP-activated protein kinase as a mediator of whole body energy balance
de Morentin, P. B. M., González, C. R., Saha, A. K., Martins, L., Diéguez, C., Vidal‐Puig, A., Tena‐Sempere, M., & López, M. (2011) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-011-9165-5 · Cited by 96
Ježek, P., Plecitá‐Hlavatá, L., Smolková, K., & Rossignol, R. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.11.008 · Cited by 96
Barcena, M. L., Pozdniakova, S., Kühl, A. A., Baczkó, I., Ladilov, Y. V., & Regitz‐Zagrosek, V. (2019) · Aging · doi:10.18632/aging.101881 · Cited by 96
Khalafi, M., Mohebbi, H., Symonds, M. E., Karimi, P., Akbari, A. M., Tabari, E., Faridnia, M., & Moghaddami, K. (2020) · Nutrients · doi:10.3390/nu12040925 · Cited by 96
The Role of SIRT1 in Diabetic Kidney Disease
Yacoub, R., Lee, K., & He, C. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00166 · Cited by 96
Resveratrol and rapamycin: are they anti‐aging drugs?
Kaeberlein, M. R. (2010) · BioEssays · doi:10.1002/bies.200900171 · Cited by 96
Adiponectin/adiponectin receptor in disease and aging
Iwabu, M., Okada‐Iwabu, M., Yamauchi, T., & Kadowaki, T. (2015) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2015.13 · Cited by 96
Leal‐Díaz, A. M., Noriega, L. G., Torre-Villalvazo, I., Torres, N., Alemán, G., López‐Romero, P., Sánchez‐Tapia, M., Aguilar‐López, M., Furuzawa‐Carballeda, J., Velázquez‐Villegas, L. A., et al. (2016) · Scientific Reports · doi:10.1038/srep34242 · Cited by 96
Self-citationGaldieri, L. C., Gatla, H. R., Vancurova, I., & Vančura, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.742247 · Cited by 96
Chang, E., & Kim, Y. (2017) · Nutrients · doi:10.3390/nu9040338 · Cited by 95
High intensity interval training and molecular adaptive response of skeletal muscle
Torma, F., Gombos, Z., Jokai, M., Takeda, M., Mimura, T., & Radak, Z. (2019) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2019.08.003 · Cited by 95
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Zhang, H., Puleston, D. J., & Simon, A. K. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.06.001 · Cited by 95
Selenoprotein P as an in vivo redox regulator: disorders related to its deficiency and excess
Saito, Y. (2019) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.19-31 · Cited by 95
Bao, Y., Xiao, J., Weng, Z., Lü, X., Shen, X., & Wang, F. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.125948 · Cited by 95
Peng, W.-Q., Xiao, G., Li, B., Guo, Y., Guo, L., & Tang, Q.-Q. (2021) · Diabetes · doi:10.2337/db20-1210 · Cited by 95
Thompson, A. M., Martin, K. A., & Rzucidlo, E. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085495 · Cited by 95
The role of sirtuins in modulating redox stressors
Webster, B. R., Lu, Z., Sack, M. N., & Scott, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.484 · Cited by 95
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Hoeks, J., & Schrauwen, P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.05.007 · Cited by 94
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Self-citationTherapeutic role of sirtuins in neurodegenerative disease and their modulation by polyphenols
Ajami, M., Pazoki–Toroudi, H., Amani, H., Nabavi, S. F., Braidy, N., Vacca, R. A., Atanasov, A. G., MOCAN, A., & Nabavi, S. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.11.022 · Cited by 94
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Radak, Z. O., Suzuki, K., Pósa, A., Petrovszki, Z., Koltai, E., & Boldogh, I. R. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101467 · Cited by 94
de Kreutzenberg, S. V., Ceolotto, G., Cattelan, A. M., Pagnin, E., Mazzucato, M., Garagnani, P., Borelli, V., Bacalini, M. G., Franceschi, C., Fadini, G. P., et al. (2015) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2015.03.007 · Cited by 94
Lombard, D. B., & Zwaans, B. M. M. (2013) · Gerontology · doi:10.1159/000354382 · Cited by 94
Ljubicic, V., Burt, M., Lunde, J. A., & Jasmin, B. J. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00357.2013 · Cited by 94
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Kong, S., McBurney, M. W., & Fang, D. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.102 · Cited by 94
SUGIYAMA, M., Kawahara‐Miki, R., KAWANA, H., Shirasuna, K., Kuwayama, T., & Iwata, H. (2015) · Journal of Reproduction and Development · doi:10.1262/jrd.2015-001 · Cited by 94
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Elhassan, Y., Philp, A., & Lavery, G. G. (2017) · Journal of the Endocrine Society · doi:10.1210/js.2017-00092 · Cited by 93
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Diallo, I., Seve, M., Cunin, V., Minassian, F., Poisson, J., Michelland, S., & Bourgoin‐Voillard, S. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1559061 · Cited by 93
Gu, T., Zhang, Z., Liu, J., Chen, L., Tian, Y., Xu, W., Zeng, T., Wu, W., & Lu, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713516 · Cited by 93
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Yin, F., Sancheti, H., Liu, Z., & Cadenas, E. (2015) · The Journal of Physiology · doi:10.1113/jp270541 · Cited by 93
Jin, X., Chen, M., Yi, L., Chang, H., Zhang, T., Wang, L., Ma, W., Peng, X., Zhou, Y. G., & Mi, M. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400161 · Cited by 93
Adrenergic signaling and oxidative stress: a role for sirtuins?
Corbi, G., Conti, V., Russomanno, G., Longobardi, G., Furgi, G., Filippelli, A., & Ferrara, N. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00324 · Cited by 92
Charytoniuk, T., Drygalski, K., Konstantynowicz-Nowicka, K., Berk, K., & Chabowski, A. (2016) · Nutrition · doi:10.1016/j.nut.2016.09.001 · Cited by 92
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Hart, N., Sarga, L., Csende, Z., Koltai, E., Koch, L. G., Britton, S. L., Davies, K. J. A., Kouretas, D., Wessner, B., & Radak, Z. O. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.01.051 · Cited by 93
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Cai, Y., Yu, S., Chen, S., Pi, R., Gao, S., Li, H., Ye, J., & Liu, P. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.02.014 · Cited by 92
Frederick, D. W., Davis, J. G., Dávila, A., Agarwal, B., Michán, S., Puchowicz, M. A., Nakamaru‐Ogiso, E., & Baur, J. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.579565 · Cited by 91
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Wang, L., Di, L., & Noguchi, C. T. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.9518 · Cited by 91
Jung, Y., Park, J., Kim, H., Sim, J., Youn, D., Kang, J., Lim, S., Jeong, M., Yang, W. M., Lee, S., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700231rr · Cited by 91
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Zeng, Y., Nie, C., Min, J., Chen, H., Liu, X., Ye, R., Chen, Z., Bai, C., Xie, E., Yin, Z., et al. (2018) · JAMA Network Open · doi:10.1001/jamanetworkopen.2018.1670 · Cited by 91
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Ryall, J. G. (2013) · FEBS Journal · doi:10.1111/febs.12189 · Cited by 91
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Cui, X., Yao, L., Yang, X., Gao, Y., Fang, F., Zhang, J., Wang, Q., & Chang, Y. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00122.2017 · Cited by 91
Ma, J., Guillot, A., Yang, Z., Mackowiak, B., Hwang, S., Park, O., Peiffer, B. J., Ahmadi, A. R., Melo, L., Kusumanchi, P., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci157780 · Cited by 90
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Cordani, M., Butera, G., Pacchiana, R., & Donadelli, M. (2016) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2016.11.003 · Cited by 90
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Yang, D., Xiao, C., Long, F., Su, Z., Jia, W., Qin, M., Huang, M., Wu, W., Suguro, R., Liu, X., et al. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy051 · Cited by 90
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Vazquez, M. J., Velasco, I., & Tena‐Sempere, M. (2019) · Journal of Endocrinology · doi:10.1530/joe-19-0223 · Cited by 90
Bottani, E., Lamperti, C., Prigione, A., Tiranti, V., Persico, N., & Brunetti, D. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12111083 · Cited by 89
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Chen, W.-K., Tsai, Y., Shibu, M. A., Shen, C.-Y., Chang-Lee, S. N., Chen, R., Yao, C., Ban, B., Kuo, W., & Huang, C. (2018) · Aging · doi:10.18632/aging.101714 · Cited by 89
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Raffaello, A., & Rizzuto, R. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.007 · Cited by 72
Wang, X., Zhu, L., Hong, X., Wang, Y., Wang, F., Bao, J.-P., Xie, X.-H., Liu, L., & Wu, X. (2016) · Experimental Biology and Medicine · doi:10.1177/1535370216637940 · Cited by 89
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Woller, A., Duez, H., Staels, B., & Lefranc, M. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.060 · Cited by 89
Wu, B., Feng, J., Yu, L., Wang, Y., Chen, Y., Wei, Y., Han, J., Xiao, F., Zhang, Y., Di, S., et al. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14457 · Cited by 88
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Shaito, A. A., Al‐Mansoob, M., Ahmad, S. M. S., Haider, M. Z., Eid, A. H., Posadino, A. M., Pintus, G., & Giordo, R. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666221012122855 · Cited by 88
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Wen, L., Chen, Z. B., Zhang, F., Cui, X., Sun, W., Geary, G. G., Wang, Y., Johnson, D. A., Zhu, Y., Chien, S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309354110 · Cited by 88
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Huang, Y., Lu, J., Li, Z., Wang, M., Shi, R., Yuan, X. N., Gao, X., Liu, X., Zang, J., Liu, W., et al. (2020) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100929 · Cited by 87
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Synergism between resveratrol and other phytochemicals: Implications for obesity and osteoporosis
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Metadata
- Authors
- Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Harvard University (US)
- Corresponding author
- Auwerx, Johan
- Venue
- Nature
- Published
- 2009-03-04
- Volume
- 458
- Issue
- 7241
- Pages
- 1056-1060
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3616311
- OpenAlex
- W2022267544
- Cited by
- 3,300
- References
- 33
- Citations by year
- 2026: 197 · 2025: 185 · 2024: 185 · 2023: 191 · 2022: 221 · 2021: 221 · 2020: 231 · 2019: 191 · 2018: 195 · 2017: 187 · 2016: 206 · 2015: 175 · 2014: 179 · 2013: 200 · 2012: 183
- FWCI
- 71.47
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-59820, DK069966, R01DK069966, P01DK059820)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- AMPK, SIRT1, NAD+ metabolism, energy expenditure, skeletal muscle, PGC-1α, FOXO1, FOXO3, deacetylation, mitochondrial biogenesis, oxidative metabolism, type 2 diabetes, transcriptional regulation
- MeSH terms
- Forkhead Box Protein O1, Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Forkhead Box Protein O3, Acetylation, Aminoimidazole Carboxamide, Animals, Cell Line, Energy Metabolism, Enzyme Activation, Gene Expression Regulation, Male, Mutation, NAD, Oxygen Consumption, Phosphorylation, Ribonucleotides, Transcription Factors, Transcription, Genetic, Trans-Activators, Muscle, Skeletal, Sirtuins, Genes, Mitochondrial, Mice, Forkhead Transcription Factors, AMP-Activated Protein Kinases, Sirtuin 1
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