Resveratrol Improves Mitochondrial Function and Protects against Metabolic Disease by Activating SIRT1 and PGC-1α
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Diminished mitochondrial oxidative phosphorylation and aerobic capacity are associated with reduced longevity. We tested whether resveratrol (RSV), which is known to extend lifespan, impacts mitochondrial function and metabolic homeostasis. Treatment of mice with RSV significantly increased their aerobic capacity, as evidenced by their increased running time and consumption of oxygen in muscle fibers. RSV's effects were associated with an induction of genes for oxidative phosphorylation and mitochondrial biogenesis and were largely explained by an RSV-mediated decrease in PGC-1alpha acetylation and an increase in PGC-1alpha activity. This mechanism is consistent with RSV being a known activator of the protein deacetylase, SIRT1, and by the lack of effect of RSV in SIRT1(-/-) MEFs. Importantly, RSV treatment protected mice against diet-induced-obesity and insulin resistance. These pharmacological effects of RSV combined with the association of three Sirt1 SNPs and energy homeostasis in Finnish subjects implicates SIRT1 as a key regulator of energy and metabolic homeostasis.
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Impaired mitochondrial function directs fatty acids toward storage rather than oxidation, contributing considerably to intramyocellular lipid accumulation and insulin resistance.
“Indeed, impaired mitochondrial function directs fatty acids toward storage, as opposed to oxidation, which contributes considerably to intramyocellular lipid accumulation and insulin resistance [16].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [16]
Molecular targets of resveratrol include PGC1α, SIRT1, NFκB, AMPK, FoxO3, and PPARγ, which are responsible for modulating mitochondrial activity.
“Studies have demonstrated the characterization of molecular targets of resveratrol, including PGC1α, SIRT1, NFκB, AMPK, FoxO3, and PPARγ [16, 61, 85, 89], that are responsible for modulating mitochondrial activity.”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [16]
Mammalian SIRT1 plays a context-dependent role in health span regulation, including mediating effects in metabolic stress such as high-fat diet-induced obesity.
“What is clear, however, is that mammalian SIRT1 plays a context-dependent role in health span regulation, for instance by mediating effects in metabolic stress situations, such as high-fat diet-induced obesity (Baur et al., 2006; Lagouge et al., 2006; Pearson et al., 2008).”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Lagouge et al., 2006
Resveratrol is a natural compound that influences energy metabolism and mitochondrial function and acts as a calorie restriction mimetic in animal obesity models.
“resveratrol treatment in mice fed a high calorie diet consistently improved various health parameters including glucose homeostasis, endurance and survival (Baur et al., 2006; Lagouge et al., 2006; Pearson et al., 2008; Sun et al., 2007), and has therefore been suggested to act as a calorie restriction mimetic.”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Lagouge et al., 2006
In rodents, resveratrol reduces heart rate.
“to reduce heart rate (Lagouge et al., 2006)”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Lagouge et al., 2006
The gene expression effects of resveratrol in humans are highly similar to those in mice treated with resveratrol, though more pronounced in mice.
“Importantly, these effects are highly similar to the effects observed in mice treated with resveratrol (figure 2C), even though the effects in the latter are more pronounced, probably due to longer treatment time and their identical genetic and environmental background.”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Lagouge et al., 2006
Resveratrol treatment in mice on a high-calorie diet consistently improved health parameters including glucose homeostasis, endurance, and survival.
“Regardless of the mode of activation, resveratrol treatment in mice fed a high calorie diet consistently improved various health parameters including glucose homeostasis, endurance and survival (Baur et al., 2006; Lagouge et al., 2006; Pearson et al., 2008; Sun et al., 2007)”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Lagouge et al., 2006
The human dose of 150 mg/day resveratrol is 133-266 fold lower than mouse doses of 200-400 mg/kg/day, but human plasma resveratrol levels averaged 231 ng/ml, higher than mouse levels of 10-120 ng/ml.
“although the dosage of 150 mg of resveratrol per day is around 133-266 fold lower compared to the high doses of 200 to 400 mg/kg/day used to supplement mice (Baur et al., 2006; Lagouge et al., 2006), plasma resveratrol levels in our human intervention (231 ng/ml on average during the 30 days) were even higher than those obtained in mice (10-120 ng/ml) (Lagouge et al., 2006).”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Lagouge et al., 2006
The beneficial metabolic effects of resveratrol are concordant with findings from animal resveratrol supplementation studies.
“These beneficial effects of resveratrol on metabolism are in concordance with several findings of resveratrol supplementation in animals (Baur et al., 2006; Canto et al., 2009; Lagouge et al., 2006; Pearson et al., 2008; Sun et al., 2007).”
From Calorie Restriction-like Effects of 30 Days of Resveratrol Supplementation on Energy Metabolism and Metabolic Profile in Obese Humans (2011) · cites this paper as Lagouge et al., 2006
Resveratrol is able to induce the expression of genes that promote oxidative phosphorylation and mitochondrial biogenesis as a result of SIRT-1.
“Resveratrol is in fact able to induce the expression of genes that promote oxidative phosphorylation and mitochondrial biogenesis as a result of SIRT-1 [23].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [23]
SIRT-1 can increase the activity of PGC-1α, which induces gluconeogenesis and glycolysis in the liver by increasing transcription of glycogenetic genes.
“SIRT-1 can also increase the activity of PGC-1α, which in turn induces gluconeogenesis and glycolysis in the liver by increasing the transcription of glycogenetic genes [23].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [23]
Resveratrol has been shown to promote the differentiation of white adipocytes into brown ones.
“Resveratrol has also been shown to promote the differentiation of white adipocytes into brown ones [23].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [23]
Resveratrol stimulates mitochondrial activity through SIRT-1-mediated activation of PGC-1α, contributing to fiber-type switching and adaptive thermogenesis in muscles and brown adipose tissue.
“Some evidence indicates that resveratrol stimulates mitochondrial activity through SIRT-1-mediated activation of PGC-1α, which contributes to fiber-type switching and adaptive thermogenesis in muscles and brown adipose tissue, respectively [23].”
From The Role of Resveratrol Administration in Human Obesity (2021) · cites this paper as [23]
SIRT1 activation with resveratrol in mice increased mitochondrial activity and protected against diet-induced obesity and insulin resistance.
“activation of SIRT1 with resveratrol in mice resulted in increased mitochondrial activity and protected the animals from diet-induced obesity and insulin resistance [134].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [134]
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 [87]
Resveratrol-treated mice show metabolic activation parameters including increased mitochondria number, AMPK activation, and PGC-1α deacetylation.
“Several parameters in resveratrol-treated mice are consistent with metabolic activation, including increased mitochondria number, activation of AMPK and PGC-1α deacetylation [145, 150].”
From PGC-1α in aging and anti-aging interventions (2009) · cites this paper as [145]
Resveratrol activates SIRT1, PGC-1α, and AMPK and inhibits AKT.
“Resveratrol treatment activates SIRT1, PGC-1α and AMPK [29, 145-148] and inhibits AKT [149] (Figure 4).”
From PGC-1α in aging and anti-aging interventions (2009) · cites this paper as [145]
PGC-1α activity is co-regulated by phosphorylation and NAD(+)-dependent deacetylation via AMPK, p38MAPK, and SIRT1.
“PGC-1α activity is co-regulated by phosphorylation and NAD(+)-dependent deacetylation via metabolic biosensors AMP-activated protein kinase (AMPK), mitogen-associated protein kinase (p38MAPK), and sirtuin 1 (SIRT1) (73, 74).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [74]
Animal studies demonstrated that resveratrol could stimulate energy expenditure and protect against a high-fat diet-induced weight gain via induction of FAO and reduced lipogenesis, mediated by activation of the AMPK-SIRT1 axis.
“Animal studies have also demonstrated that resveratrol could stimulate energy expenditure and protect against a high-fat diet-induced weight gain (250), via induction of FAO and reduced lipogenesis, mediated by activation of the AMPK-SIRT1 axis (251, 252).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [250]
Resveratrol enhances mitochondrial biogenesis and oxidative capacity in animal models of diet-induced obesity and ageing.
“Resveratrol enhances mitochondrial biogenesis and oxidative capacity in animal models of diet-induced obesity and ageing226,227.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [227]
Resveratrol can improve exercise endurance and protect mice against diet-induced obesity and insulin resistance.
“Resveratrol (3,5,4'-trihydroxystilbene), a polyphenol found in grape skins, red wine, peanuts, and mulberries, can improve exercise endurance and protect mice against diet-induced obesity and insulin resistance 155.”
From Cellular bioenergetics as a target for obesity therapy (2010) · cites this paper as [155]
Resveratrol promotes mitochondrial biogenesis by activating SIRT1, which deacetylates PGC1α, inducing its transcriptional activity and increasing mitochondria number in mice.
“resveratrol has been reported to promote mitochondria biogenesis by activating SIRT1, which in turn, by deacetylating PGC 1α, induces its transcriptional activity resulting in an increase in mitochondria number in mice (Lagouge et al., 2006).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Lagouge et al., 2006
Resveratrol in another study improved motor function in mice accompanied by a decrease in PGC1α acetylation leading to increased activity and mitochondrial biogenesis.
“Similarly, resveratrol in another study improved motor function in mice which was accompanied by a decrease in PGC1α acetylation leading to increased activity and mitochondrial biogenesis196.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [196]
Resveratrol offers protection in models of stress- or age-associated diseases, including chronic overfeeding, insulin resistance, type 2 diabetes, or cardiovascular dysfunction.
“Nevertheless, resveratrol offers protection in models of stress- or age-associated diseases, including chronic overfeeding, insulin resistance, type 2 diabetes, or cardiovascular dysfunction (Baur et al., 2006; Lagouge et al., 2006).”
From The Search for Antiaging Interventions: From Elixirs to Fasting Regimens (2014) · cites this paper as Lagouge et al., 2006
In mice, resveratrol improves insulin resistance, protects against diet-induced obesity, induces genes for oxidative phosphorylation, and activates PGC-1α.
“In mice, resveratrol improves insulin resistance, protects against diet-induced obesity, induces genes for oxidative phosphorylation, and activates PGC-1α (22, 184).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [184]
PGC-1 activity can also be modulated at the level of translation and by posttranscriptional changes, including inhibitory GCN5-mediated acetylation and stimulatory sirtuin 1 mediated deacetylation.
“PGC-1 activity can also be modulated at the level of translation and by posttranscriptional changes, including inhibitory GCN5-mediated acetylation (147) and stimulatory sirtuin 1 mediated deacetylation (148).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [148]
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Cites
Part of this paper’s reference list could not be split into single entries.
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625 · see citing works
Mootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197 · see citing works
Self-citationResveratrol 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 · see citing works
Self-citationTherapeutic potential of resveratrol: the in vivo evidence
Baur, J. A., & Sinclair, D. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2060 · Cited by 3,958 · see citing works
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works
Self-citationSmall molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796 · see citing works
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 · see citing works
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185 · see citing works
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 · see citing works
Self-citationTranscriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works
Self-citationImpaired 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
Metabolic control through the PGC-1 family of transcription coactivators
Lin, J., Handschin, C., & Spiegelman, B. M. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.004 · Cited by 2,130 · cited 3× · see citing works
“Values represent means ± SEM. factors, an array of additional downstream targets of PGC-1a (Lin et al., 2005), including genes involved in fatty-acid oxidation (medium chain acyl-CoA dehydrogenase, MCAD), uncoupling, and protection against ROS (uncoupling protein 3, UCP-3), and fiber-type markers…”
BackgroundMitochondrial dysfunction in the elderly: possible role in insulin resistance
Petersen, K. F., Befroy, D., Dufour, S., Dziura, J., Ariyan, C., Rothman, D. L., DiPietro, L., Cline, G. W., & Shulman, G. I. (2003) · Science · doi:10.1126/science.1082889 · Cited by 2,107 · see citing works
Mitochondria: Dynamic Organelles in Disease, Aging, and Development
Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987 · see citing works
Patti, 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
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943 · see citing works
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works
p53 Regulates Mitochondrial Respiration
Matoba, S., Kang, J.-G., Patino, W. D., Wragg, A., Boehm, M., Gavrilova, O., Hurley, P. J., Bunz, F., & Hwang, P. M. (2006) · Science · doi:10.1126/science.1126863 · Cited by 1,650 · see citing works
Towards a molecular understanding of adaptive thermogenesis
Lowell, B. B., & Spiegelman, B. M. (2000) · Nature · doi:10.1038/35007527 · Cited by 1,630 · see citing works
Mitochondrial transcription factor A is necessary for mtDNA maintance and embryogenesis in mice
Larsson, N.-G., Wang, J., Wilhelmsson, H., Oldfors, A., Rustin, P., Lewandoski, M., Barsh, G. S., & Clayton, D. A. (1998) · Nature Genetics · doi:10.1038/ng0398-231 · Cited by 1,594 · see citing works
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,496 · see citing works
Bile acids lower triglyceride levels via a pathway involving FXR, SHP, and SREBP-1c
渡辺, 光., Houten, S. M., Wang, L., Moschetta, A., Mangelsdorf, D. J., Heyman, R. A., Moore, D. D., & Auwerx, J. H. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21025 · Cited by 1,398 · see citing works
Self-citationSir2 mediates longevity in the fly through a pathway related to calorie restriction
Rogina, B., & Helfand, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404184101 · Cited by 1,361 · see citing works
Mammalian SIRT1 Represses Forkhead Transcription Factors
Motta, M. C., Divecha, N., Lemieux, M. E., Kamel, C., Chen, D., Gu, W. J., Bultsma, Y., McBurney, M. W., & Guarente, L. (2004) · Cell · doi:10.1016/s0092-8674(04)00126-6 · Cited by 1,351 · see citing works
Peroxisome proliferator–activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis
Lehman, J. J., Barger, P. M., Kovacs, A., Saffitz, J. E., Medeiros, D. M., & Kelly, D. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10268 · Cited by 1,285 · see citing works
Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
Kelly, D. P., & Scarpulla, R. C. (2004) · Genes & Development · doi:10.1101/gad.1177604 · Cited by 1,243 · see citing works
Defects in Adaptive Energy Metabolism with CNS-Linked Hyperactivity in PGC-1α Null Mice
Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., Zhang, C.-Y., Mootha, V. K., Jäger, S., Vianna, C. R., Reznick, R. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.013 · Cited by 1,162 · see citing works
Regulation of Muscle Fiber Type and Running Endurance by PPARδ
Wang, Y.-X., Zhang, C.-L., Yu, R. T., Cho, H. K., Nelson, M. C., Bayuga-Ocampo, C. R., Ham, J., Kang, H., & Evans, R. M. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020294 · Cited by 1,089 · see citing works
Mechanism of Human SIRT1 Activation by Resveratrol
Borra, M. T., Smith, B. C., & Denu, J. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501250200 · Cited by 1,065 · see citing works
Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration
Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060 · see citing works
Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
Lin, S.-J., Kaeberlein, M., Andalis, A. A., Sturtz, L. A., Defossez, P.-A., Culotta, V. C., Fink, G. R., & Guarente, L. (2002) · Nature · doi:10.1038/nature00829 · Cited by 1,057 · see citing works
SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α
Nemoto, S., Fergusson, M. M., & Finkel, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501485200 · Cited by 1,047 · see citing works
Leone, T. C., Lehman, J. J., Finck, B. N., Schaeffer, P. J., Wende, A. R., Boudina, S., Courtois, M., Wozniak, D. F., Sambandam, N., Bernal-Mizrachi, C., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030101 · Cited by 951 · see citing works
Valenzano, D. R., Tozzini, E. T., Genade, T., Cattaneo, A., Domenici, L., & Cellerino, A. (2006) · Current Biology · doi:10.1016/j.cub.2005.12.038 · Cited by 786 · see citing works
Mootha, V. K., Handschin, C., Arlow, D., Xie, X., St. Pierre, J., Sihag, S., Yang, W., Altshuler, D., Puigserver, P., Patterson, N., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401401101 · Cited by 688 · see citing works
Self-citationRegulation of mitochondrial biogenesis in skeletal muscle by CaMK
Wu, H., Kanatous, S. B., Thurmond, F. A., Gallardo, T., Isotani, E., Bassel-Duby, R., & Williams, R. S. (2002) · Science · doi:10.1126/science.1071163 · Cited by 684 · see citing works
Schreiber, S., Emter, R., Hock, M. B., Knutti, D., Cardenas, J., Podvinec, M., Oakeley, E. J., & Kralli, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308686101 · Cited by 657 · see citing works
Cardiovascular risk factors emerge after artificial selection for low aerobic capacity.
Wisløff, U., Najjar, S. M., Ellingsen, Ø., Haram, P. M., Swoap, S., Al-Share, Q., Fernström, M., Rezaei, K., Lee, S. J., Koch, L. G., et al. (2005) · Science · doi:10.1126/science.1108177 · Cited by 657 · see citing works
Sparks, L. M., Xie, H., Koza, R. A., Mynatt, R., Hulver, M. W., Bray, G. A., & Smith, S. R. (2005) · Diabetes · doi:10.2337/diabetes.54.7.1926 · Cited by 629 · cited 4× · see citing works
“RSV’s effects were associated with an induction of genes for oxidative phosphorylation and mitochondrial biogenesis and were largely explained by an RSV-mediated decrease in PGC1a acetylation and an increase in PGC-1a activity.”
BackgroundInfluentialSir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 590 · see citing works
Toward a unified theory of caloric restriction and longevity regulation
Sinclair, D. A. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.03.019 · Cited by 561 · see citing works
Lin, J., Puigserver, P., Donovan, J., Tarr, P., & Spiegelman, B. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100631200 · Cited by 552 · see citing works
Self-citationResveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
Parker, J. A., Arango-Lievano, M., Abderrahmane, S., Lambert, E., Tourette, C., Catoire, H., & Néri, C. (2005) · Nature Genetics · doi:10.1038/ng1534 · Cited by 509 · see citing works
Peroxisome proliterator-activated receptors, orphans with ligands and functions
Schoonjans, K., Martin, G. V., Staels, B., & Auwerx, J. H. (1997) · Current Opinion in Lipidology · doi:10.1097/00041433-199706000-00006 · Cited by 488 · see citing works
Self-citationHuss, J. M., Kopp, R. P., & Kelly, D. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206324200 · Cited by 480 · see citing works
Schreiber, S., Knutti, D., Brogli, K., Uhlmann, T., & Kralli, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212923200 · Cited by 458 · see citing works
Increase in Activity During Calorie Restriction Requires Sirt1
Chen, D., Steele, A. D., Lindquist, S., & Guarente, L. (2005) · Science · doi:10.1126/science.1118357 · Cited by 419 · see citing works
PGC-1, a versatile coactivator
Knutti, D., & Kralli, A. (2001) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(01)00457-x · Cited by 294 · see citing works
Exercise and gene expression: physiological regulation of the human genome through physical activity
Booth, F. W., Chakravarthy, M. V., & Spangenburg, E. E. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.019265 · Cited by 277 · see citing works
Virkamäki, A., Korsheninnikova, E., Seppälä‐Lindroos, A., Vehkavaara, S., Goto, T., Halavaara, J. T., Häkkinen, A., & Yki‐Järvinen, H. (2001) · Diabetes · doi:10.2337/diabetes.50.10.2337 · Cited by 261 · see citing works
Salmenniemi, U., Ruotsalainen, E., Pihlajamäki, J., Vauhkonen, I., Kainulainen, S., Punnonen, K. R. A., Vanninen, E. J., & Laakso, M. (2004) · Circulation · doi:10.1161/01.cir.0000150391.38660.9b · Cited by 260 · see citing works
Self-citationMammalian SIRT1 limits replicative life span in response to chronic genotoxic stress
Chua, K. F., Mostoslavsky, R., Lombard, D. B., Pang, W. W., Saito, S., Franco, S., Kaushal, D., Cheng, H.-L., Fischer, M. R., Stokes, N., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.007 · Cited by 257 · see citing works
Modulation of Estrogen Receptor-α Transcriptional Activity by the Coactivator PGC-1
Tcherepanova, I. Y., Puigserver, P., Norris, J. D., Spiegelman, B. M., & McDonnell, D. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001364200 · Cited by 218 · see citing works
Self-citationRespiration uncoupling and metabolism in the control of energy expenditure
Ricquier, D. (2005) · Proceedings of The Nutrition Society · doi:10.1079/pns2004408 · Cited by 175 · see citing works
Kim, Y. I., Lee, F. N., Choi, W. S., Lee, S., & Youn, J. H. (2006) · Diabetes · doi:10.2337/db05-1606 · Cited by 119 · see citing works
Ceddia, R. B., William, W. N., Lima, F. B., Flandin, P., Curi, R., & Giacobino, J. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01664.x · Cited by 83 · see citing works
Interaction of carnitine with insulin-stimulated glucose metabolism in humans
Ferrannini, E., Buzzigoli, G., Bevilacqua, S., Boni, C. D., Chiaro, D. D., Oleggini, M., Brandi, L., & Maccari, F. (1988) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1988.255.6.e946 · Cited by 71 · see citing works
N’guessan, B. B., Zoll, J., Ribera, F., Ponsot, E., Lampert, E., Ventura‐Clapier, R., Veksler, V., & Mettauer, B. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000009874.14649.ca · Cited by 33 · see citing works
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- [46]46. Schreiber, S.N. ∙ Emter, R. ∙ Hock, M.B. ... The estrogen-related receptor alpha (ERRalpha) functions in PPARgamma coactivator 1alpha (PGC-1alpha)-induced mitochondrial biogenesis Proc. Natl. Acad. Sci. USA. 2004; 101:6472-6477 Crossref Scopus (544) PubMed Google Scholar
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Sorted by citations
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works
Dose translation from animal to human studies revisited.
Reagan‐Shaw, S., Nihal, M., & Ahmad, N. (2008) · The FASEB Journal · doi:10.1096/fj.07-9574lsf · Cited by 6,524 · see citing works
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works
Self-citationThe AMPK signalling pathway coordinates cell growth, autophagy and metabolism
Mihaylova, M. M., & Shaw, R. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2329 · Cited by 2,923 · see citing works
Butyrate improves insulin sensitivity and increases energy expenditure in mice
Gao, Z., Yin, J., Zhang, J., Ward, R. E., Martin, R. J., Lefevre, M., Cefalu, W. T., & Ye, J. (2009) · Diabetes · doi:10.2337/db08-1637 · Cited by 2,204 · see citing works
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
Mammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085 · 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
Self-citationSarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
Sirtuins in mammals: insights into their biological function
Michán, S., & Sinclair, D. A. (2007) · Biochemical Journal · doi:10.1042/bj20070140 · Cited by 1,719 · see citing works
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works
Self-citationBhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655 · see citing works
Targeting mitochondria for cancer therapy
Fulda, S., Galluzzi, L., & Kroemer, G. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3137 · Cited by 1,638 · 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
PGC-1α, SIRT1 and AMPK, an energy sensing network that controls energy expenditure
Cantó, C., & Auwerx, J. (2009) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e328328d0a4 · Cited by 1,624 · see citing works
Self-citationThe intersection between aging and cardiovascular disease
North, B. J., & Sinclair, D. A. (2012) · Circulation Research · doi:10.1161/circresaha.111.246876 · Cited by 1,585 · see citing works
Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602 · see citing works
Mechanisms of mitophagy in cellular homeostasis, physiology and pathology
Palikaras, K., Lionaki, E., & Tavernarakis, N. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0176-2 · Cited by 1,505 · 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
A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
Lee, I. H., Cao, L., Mostoslavsky, R., Lombard, D. B., Liu, J., Bruns, N. E., Tsokos, M., Alt, F. W., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712145105 · Cited by 1,473 · see citing works
Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427 · see citing works
Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases
Park, S. J., Ahmad, F., Philp, A., Baar, K., Williams, T., Luo, H., Ke, H., Rehmann, H., Taussig, R., Brown, A. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.017 · Cited by 1,352 · see citing works
NAD <sup>+</sup> in aging, metabolism, and neurodegeneration
Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319 · see citing works
Timmers, S., Konings, E., Bilet, L., Houtkooper, R. H., van de Weijer, T., Goossens, G. H., Hoeks, J., van der Krieken, S., Ryu, D., Kersten, S., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.10.002 · Cited by 1,320 · see citing works
Self-citationMitochondrial Dynamics and Metabolic Regulation
Wai, T., & Langer, T. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.12.001 · Cited by 1,304 · see citing works
Cantó, 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
Self-citationMouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works
Self-citationMammalian 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
AMPK and PPARδ Agonists Are Exercise Mimetics
Narkar, V. A., Downes, M., Yu, R. T., Embler, E., Wang, Y.-X., Banayo, E., Mihaylova, M. M., Nelson, M. C., Zou, Y., Juguilon, H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.051 · Cited by 1,222 · see citing works
Liver Fibrosis: Mechanistic Concepts and Therapeutic Perspectives
Roehlen, N., Crouchet, E., & Baumert, T. F. (2020) · Cells · doi:10.3390/cells9040875 · Cited by 1,237 · see citing works
Adipose tissue browning and metabolic health
Bartelt, A., & Heeren, J. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2013.204 · Cited by 1,177 · see citing works
Pearson, K. J., Baur, J. A., Lewis, K. N., Peshkin, L., Price, N. L., Labinskyy, N., Swindell, W. R., Kamara, D., Minor, R. K., Perez, E., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.011 · Cited by 1,162 · see citing works
Self-citationImpact of Dietary Polyphenols on Carbohydrate Metabolism
Hanhineva, K., Törrönen, R., Bondia‐Pons, I., Pekkinen, J., Kolehmainen, M., Mykkänen, H. M., & Poutanen, K. S. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11041365 · Cited by 1,167 · 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
Purushotham, A., Schug, T. T., Xu, Q., Surapureddi, S., Guo, X., & Li, X. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.02.006 · Cited by 1,112 · see citing works
Regulation of mitochondrial biogenesis
Jornayvaz, F. R., & Shulman, G. I. (2010) · Essays in Biochemistry · doi:10.1042/bse0470069 · Cited by 1,119 · see citing works
Mitonuclear protein imbalance as a conserved longevity mechanism
Houtkooper, R. H., Mouchiroud, L., Ryu, D., Moullan, N., Katsyuba, E., Knott, G., Williams, R. W., & Auwerx, J. (2013) · Nature · doi:10.1038/nature12188 · Cited by 1,035 · see citing works
Self-citationMitophagy: mechanisms, pathophysiological roles, and analysis
Ding, W.-X., & Yin, X.-M. (2012) · bchm · doi:10.1515/hsz-2012-0119 · Cited by 1,032 · see citing works
The Histone Deacetylase Sirt6 Regulates Glucose Homeostasis via Hif1α
Zhong, L., D'Urso, A., Toiber, D., Sebastian, C., Henry, R. E., Vadysirisack, D. D., Guimaraes, A., Marinelli, B., Wikstrom, J. D., Nir, T., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.041 · Cited by 1,001 · see citing works
Adipose tissue expandability, lipotoxicity and the Metabolic Syndrome — An allostatic perspective
Virtue, S., & Vidal-Puig, A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.12.006 · Cited by 1,013 · see citing works
NAD+ metabolism in health and disease
Belenky, P. A., Bogan, K. L., & Brenner, C. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.006 · Cited by 983 · see citing works
Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990 · see citing works
Autophagy—a key player in cellular and body metabolism
Kim, K. H., & Lee, M. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2014.35 · Cited by 962 · see citing works
Transcriptional control of mitochondrial biogenesis: the central role of PGC-1
Ventura-Clapier, R., Garnier, A., & Veksler, V. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn098 · Cited by 932 · see citing works
Sirt1 protects against high-fat diet-induced metabolic damage
Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 932 · see citing works
SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works
The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways
Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899 · see citing works
Self-citationAMPK and SIRT1: a long-standing partnership?
Ruderman, N. B., Julia Xu, X., Nelson, L., Cacicedo, J. M., Saha, A. K., Lan, F., & Ido, Y. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00745.2009 · Cited by 903 · see citing works
Novel insights of dietary polyphenols and obesity
Wang, S. F., Moustaïd‐Moussa, N., Chen, L., Mo, H., Shastri, A. A., Su, R., Bapat, P., Kwun, I., & Shen, C. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2013.09.001 · Cited by 903 · see citing works
Metabolic control of autophagy
Galluzzi, L., Pietrocola, F., Levine, B., & Kroemer, G. (2014) · Cell · doi:10.1016/j.cell.2014.11.006 · Cited by 855 · see citing works
PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation
Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., Yamamoto, H., Huber, A., Kiss, B., Houtkooper, R. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.004 · Cited by 837 · see citing works
Self-citationSlowing ageing by design: the rise of NAD+ and sirtuin-activating compounds
Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834 · see citing works
Boocock, D. J., Faust, G. E. S., Patel, K. R., Schinas, A. M., Brown, V. A., Ducharme, M. P., Booth, T. D., Crowell, J. A., Perloff, M., Gescher, A. J., et al. (2007) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-07-0022 · Cited by 823 · see citing works
Fulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 821 · see citing works
Bonnard, C., Durand, A., Peyrol, S., Chanseaume, E., Chauvin, M.-A., Morio, B., Vidal, H., & Rieusset, J. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32601 · Cited by 819 · see citing works
Brown Remodeling of White Adipose Tissue by SirT1-Dependent Deacetylation of Pparγ
Qiang, L., Wang, L., Kon, N., Zhao, W., Lee, S., Zhang, Y., ROSENBAUM, M. S., Zhao, Y., Gu, W. J., Farmer, S. R., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.027 · Cited by 802 · see citing works
Calabrese, V., Cornelius, C., Dinkova‐Kostova, A. T., Calabrese, E. J., & Mattson, M. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3074 · Cited by 803 · see citing works
SIRT1 Regulates Hepatocyte Lipid Metabolism through Activating AMP-activated Protein Kinase
Hou, X., Xu, S., Maitland-Toolan, K. A., Sato, K., Jiang, B., Ido, Y., Lan, F., Walsh, K., Wierzbicki, M., Verbeuren, T. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802187200 · Cited by 778 · see citing works
Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis
Henchcliffe, C., & Beal, M. F. (2008) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0924 · Cited by 786 · see citing works
Sustained proliferation in cancer: Mechanisms and novel therapeutic targets
Feitelson, M. A., Arzumanyan, A. L., Kulathinal, R. J., Blain, S. W., Holcombe, R. F., Mahajna, J. A., Marino, M., Martínez‐Chantar, M. L., Nawroth, R., Sánchez-Garcı́a, I., et al. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.02.006 · Cited by 783 · see citing works
Mechanisms of obesity-associated insulin resistance: many choices on the menuPreprint
Qatanani, M., & Lazar, M. A. (2007) · Genes & Development · doi:10.1101/gad.1550907 · Cited by 780 · see citing works
Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease
Smith, R. L., Soeters, M. R., Wüst, R. C. I., & Houtkooper, R. H. (2018) · Endocrine Reviews · doi:10.1210/er.2017-00211 · Cited by 787 · see citing works
Human iPSC-based modeling of late-onset disease via progerin-induced aging
Miller, J. D., Ganat, Y. M., Kishinevsky, S., Bowman, R. L., Liu, B., Tu, E. Y., Mandal, P. K., Vera, E., Shim, J.-W., Kriks, S., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.11.006 · Cited by 777 · see citing works
Impaired DNA Damage Response, Genome Instability, and Tumorigenesis in SIRT1 Mutant Mice
Wang, R.-H., Sengupta, K., Li, C., Kim, H., Cao, L., Xiao, C., Kim, S., Xu, X., Yin, Z., Chilton, B. S., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.09.001 · Cited by 769 · see citing works
SIRT1 Improves Insulin Sensitivity under Insulin-Resistant Conditions by Repressing PTP1B
Sun, C., Zhang, F., Ge, X., Yan, T., Chen, X., Shi, X., & Zhai, Q. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.014 · Cited by 766 · see citing works
Sivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742 · see citing works
Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740 · see citing works
Mitochondrial Energetics and Therapeutics
Wallace, D. C., Fan, W., & Procaccio, V. (2010) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092314 · Cited by 727 · see citing works
SIRT1 transgenic mice show phenotypes resembling calorie restriction
Bordone, L., Cohen, D., Robinson, A., Motta, M. C., Van Veen, E., Czopik, A., Steele, A. D., Crowe, H., Marmor, S., Luo, J., et al. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00335.x · Cited by 722 · see citing works
Overexpression of Atg5 in mice activates autophagy and extends lifespan
Pyo, J.-O., Yoo, S.-M., Ahn, H.-H., Nah, J., Hong, S.-H., Kam, T.-I., Jung, S., & Jung, Y.-K. (2013) · Nature Communications · doi:10.1038/ncomms3300 · Cited by 721 · see citing works
Feige, J. N., Lagouge, M., Canto, C., Strehle, A., Houten, S. M., Milne, J. C., Lambert, P. D., Mataki, C., Elliott, P. J., & Auwerx, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.017 · Cited by 719 · see citing works
Self-citationSirtuin 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
Defective Mitophagy in XPA via PARP-1 Hyperactivation and NAD+/SIRT1 Reduction
Fang, E. F., Scheibye-Knudsen, M., Brace, L. E., Kassahun, H., SenGupta, T., Nilsen, H., Mitchell, J. R., Croteau, D. L., & Bohr, V. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.026 · Cited by 711 · see citing works
Oxidant Mechanisms in Renal Injury and Disease
Ratliff, B. B., Abdulmahdi, W., Pawar, R. D., & Wolin, M. S. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6665 · Cited by 699 · see citing works
Yankner, B. A., Lu, T., & Loerch, P. (2008) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.2.010506.092044 · Cited by 677 · see citing works
Pathogenesis of insulin resistance in skeletal muscle
Abdul-Ghani, M. A., & DeFronzo, R. A. (2010) · Journal of Biomedicine and Biotechnology · doi:10.1155/2010/476279 · Cited by 670 · see citing works
Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease
Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654 · see citing works
Regulation of SIRT1 in cellular functions: Role of polyphenols
Chung, S., Yao, H., Caito, S. W., Hwang, J., Arunachalam, G., & Rahman, I. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.05.003 · Cited by 651 · see citing works
AMP-activated protein kinase-deficient mice are resistant to the metabolic effects of resveratrol
Um, J.-H., Park, S.-J., Kang, H., Yang, S., Foretz, M., McBurney, M. W., Kim, M. K., Viollet, B., & Chung, J. H. (2010) · Diabetes · doi:10.2337/db09-0482 · Cited by 647 · see citing works
Vingtdeux, V., Giliberto, L., Zhao, H., Chandakkar, P., Wu, Q., Simon, J. E., Janle, E. M., Lobo, J., Ferruzzi, M. G., Davies, P. J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.060061 · Cited by 648 · see citing works
Madeo, F., Carmona-Gutierrez, D., Hofer, S. J., & Kroemer, G. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.018 · Cited by 630 · see citing works
SirT1 Gain of Function Increases Energy Efficiency and Prevents Diabetes in Mice
Banks, A. S., Kon, N., Knight, C. M., Matsumoto, M., Juárez, R. G., Rossetti, L., Gu, W. J., & Accili, D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.014 · Cited by 636 · 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
A Mitochondrial Superoxide Signal Triggers Increased Longevity in Caenorhabditis elegans
Yang, W., & Hekimi, S. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000556 · Cited by 630 · see citing works
Transcriptional Control of Mitochondrial Biogenesis and Function
Hock, M. B., & Kralli, A. (2009) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163119 · Cited by 616 · see citing works
Sirt1 improves healthy ageing and protects from metabolic syndrome-associated cancer
Herranz, D., Muñoz-Martin, M., Cañamero, M., Mulero, F., Martinez-Pastor, B., Fernandez-Capetillo, O., & Serrano, M. (2010) · Nature Communications · doi:10.1038/ncomms1001 · Cited by 612 · see citing works
The role of mitochondria in insulin resistance and type 2 diabetes mellitus
Szendroedi, J., Phielix, E., & Roden, M. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.138 · Cited by 600 · see citing works
Aging and Survival: The Genetics of Life Span Extension by Dietary Restriction
Mair, W. B., & Dillin, A. G. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061206.171059 · Cited by 600 · see citing works
Metabolic adaptations through the PGC‐1α and SIRT1 pathways
Rodgers, J. T., Lerín, C., Gerhart‐Hines, Z., & Puigserver, P. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.11.034 · Cited by 599 · see citing works
Self-citationWenz, T., Rossi, S. G., Rotundo, R. L., Spiegelman, B. M., & Moraes, C. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911570106 · Cited by 600 · see citing works
RetractedResveratrol and health—A comprehensive review of human clinical trials
Smoliga, J. M., Baur, J. A., & Hausenblas, H. A. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100143 · Cited by 594 · see citing works
Liver fibrosis and hepatic stellate cells: Etiology, pathological hallmarks and therapeutic targets
Zhang, C.-Y., Yuan, W.-G., He, P., Lei, J.-H., & Wang, C.-X. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i48.10512 · Cited by 594 · see citing works
Fang, E. F., Kassahun, H., Croteau, D. L., Scheibye-Knudsen, M., Marosi, K., Lu, H., Shamanna, R. A., Kalyanasundaram, S., Bollineni, R. C., Wilson, M. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.004 · Cited by 575 · see citing works
Cellular bioenergetics as a target for obesity therapy
Tseng, Y.-H., Cypess, A. M., & Kahn, C. R. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3138 · Cited by 591 · see citing works
Transcriptional Control of Energy Homeostasis by the Estrogen-Related Receptors
Giguère, V. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0017 · Cited by 584 · see citing works
Barger, J. L., Kayo, T., Vann, J. M., Arias, E. B., Wang, J., Hacker, T. A., Wang, Y., Raederstorff, D., Morrow, J. D., Leeuwenburgh, C., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002264 · Cited by 580 · see citing works
Ungvari, Z. I., Bagi, Z. A., Fehér, A., Recchia, F. A., Sonntag, W. E., Pearson, K. J., de Cabo, R., & Csiszár, A. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00260.2010 · Cited by 571 · see citing works
D'Antona, G., Ragni, M., Cardile, A., Tedesco, L., Dossena, M., Bruttini, F., Caliaro, F., Corsetti, G., Bottinelli, R., Carruba, M. O., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.016 · Cited by 568 · see citing works
Tissue-specific regulation of SIRT1 by calorie restriction
Chen, D., Bruno, J., Easlon, E., Lin, S.-J., Cheng, H.-L., Alt, F. W., & Guarente, L. (2008) · Genes & Development · doi:10.1101/gad.1650608 · Cited by 567 · see citing works
The role of mitochondria in the pathogenesis of type 2 diabetes
Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551 · see citing works
- Authors
- Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., Messadeq, N., Milne, J., Lambert, P., Elliott, P., Geny, B., Laakso, M., Puigserver, P., & Auwerx, J.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Phénotypage et ingénierie précliniques des systèmes d’organismes modèles (FR)
- University of Eastern Finland (FI)
- Johns Hopkins University (US)
- Corresponding author
- Auwerx, Johan
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-12
- Volume
- 127
- Issue
- 6
- Pages
- 1109-1122
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2144600435
- Cited by
- 4,057
- References
- 58
- Citations by year
- 2026: 120 · 2025: 161 · 2024: 130 · 2023: 132 · 2022: 154 · 2021: 211 · 2020: 218 · 2019: 211 · 2018: 212 · 2017: 219 · 2016: 243 · 2015: 260 · 2014: 291 · 2013: 275 · 2012: 265
- FWCI
- 70.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2420 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, other-oa)
- HAL (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Danone
- Centre National de la Recherche Scientifique
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-59820, DK069966, R01DK069966, P01DK059820)
- 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 › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- resveratrol, SIRT1, PGC-1α, mitochondrial function, mitochondrial biogenesis, oxidative phosphorylation, cardiorespiratory fitness, diet-induced obesity, insulin resistance, metabolic disorders, longevity, energy homeostasis
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Resveratrol, Acetylation, Adult, Animals, Dietary Fats, Energy Metabolism, Gene Expression Regulation, Humans, Insulin Resistance, Male, Metabolic Diseases, Mice, Inbred C57BL, Mice, Inbred Strains, Mitochondria, Muscle, Motor Activity, Obesity, Oxidative Phosphorylation, Oxygen Consumption, Specific Pathogen-Free Organisms, Stilbenes, Transcription Factors, Trans-Activators, Muscle Fibers, Skeletal, Polymorphism, Single Nucleotide, Sirtuins, Mice, Sirtuin 1
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