The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α
Open accessAbstract
In lower organisms, increased expression of the NAD-dependent deacetylase Sir2 augments lifespan. The mechanism through which this life extension is mediated remains incompletely understood. Here we have examined the cellular effects of overexpression of SIRT1, the closest mammalian ortholog of Sir2. In PC12 cells, increased expression of the NAD-dependent deacetylase SIRT1 reduces cellular oxygen consumption by approximately 25%. We further demonstrate that SIRT1 expression can alter the transcriptional activity of the mitochondrial biogenesis coactivator PGC-1alpha. In addition, SIRT1 and PGC-1alpha directly interact and can be co-immunoprecipitated as a molecular complex. A single amino acid mutation in the putative ADP-ribosyltransferase domain of SIRT1 inhibits the interaction of SIRT1 with PGC-1alpha but does not effect the interaction of SIRT1 with either p53 or Foxo3a. We further show that PGC-1alpha is acetylated in vivo. This acetylation is augmented by treatment with the SIRT1 inhibitor nicotinamide or by expression of the transcriptional coactivator p300. Finally we demonstrate that SIRT1 catalyzes PGC-1alpha deacetylation both in vitro and in vivo. These results provide a direct link between the sirtuins, a family of proteins linked to lifespan determination and PGC-1alpha, a coactivator that regulates cellular metabolism.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“SIRT-1 is a key regulatory factor in muscle metabolism.”
From GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway (2023) · cites this paper as [51]
In the citing paper
“In apparent contrast with its role in promoting mitochondrial biogenesis through peroxisome proliferator-activated receptor-γ co-activator 1α deacetylation19–21, SIRT1 has also been implicated in turnover of defective mitochondria by mitophagy22,23.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [20]
In the citing paper
“The interaction between PGC-1α and SIRT1 also suggests a role for SIRT1 in exercise-induced mitochondrial biogenesis [89].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [89]
In the citing paper
“Activity of PGC-1α is regulated through inhibitory acetylation by GCN5 [59] and stimulatory deacetlyation by SIRT1 [60-62].”
From PGC-1α in aging and anti-aging interventions (2009) · cites this paper as [60]
In the citing paper
“AMPK and SIRT1, two major metabolic sensors in cells, modulate directly PGC1α activity through phosphorylation and deacetylation respectively”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Nemoto et al., 2005
In the citing paper
“AMPK and SIRT1, the two mainmajor metabolic sensors in cells, modulate directly are direct modulators of PGC1α activity through phosphorylation and deacetylation respectively (Jager et al., 2007; Nemoto et al., 2005).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Nemoto et al., 2005
Citations
Cites
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413
Self-citationWu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
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
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750
hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076
Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924
Research works printed but not linked: 3
- North, 2004, Genome Biology
- Tran, 2003, Science's STKE
- Bouras, 2005, J. Biol. Chem.
Cited by
Sorted by citations
Items 201–300 of 999
Acetyl-lysine Analog Peptides as Mechanistic Probes of Protein Deacetylases
Smith, B. C., & Denu, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707878200 · Cited by 141
Metabolic Signaling to ChromatinPreprint
Berger, S. L., & Sassone‐Corsi, P. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019463 · Cited by 145
Alcaín, F. J., & Villalba, J. M. (2009) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543770902762893 · Cited by 137
The NAD-dependent deacetylase SIRT2 is required for programmed necrosis
Narayan, N., Lee, I. H., Borenstein, R., Sun, J., Wong, R. P., Tong, G., Fergusson, M. M., Liu, J., Rovira, I. I., Cheng, H.-L., et al. (2012) · Nature · doi:10.1038/nature11700 · Cited by 136
Self-citationRetractedEffect of chronic alcohol consumption on Hepatic SIRT1 and PGC-1α in rats
Lieber, C. S., Leo, M. A., Wang, X., & DeCarli, L. M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.005 · Cited by 135
Cellular and molecular effects of sirtuins in health and disease
Horio, Y., Hayashi, T., Kuno, A., & Kunimoto, R. (2011) · Clinical Science · doi:10.1042/cs20100587 · Cited by 138
Cardiac fatty acid oxidation in heart failure associated with obesity and diabetes
Fukushima, A., & Lopaschuk, G. D. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.03.020 · Cited by 140
Silva, D. F., Selfridge, J. E., Lu, J., E, L., Roy, N., Hutfles, L., Burns, J. M., Michaelis, E. K., Yan, S., Cardoso, S. M., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt247 · Cited by 133
Zhu, H.-R., Wang, Z., Zhu, X., Wu, X., Li, E., & Xu, Y. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.03.017 · Cited by 133
Sirtuin 1 signaling and alcoholic fatty liver disease.
You, M., Jogasuria, A. P., Taylor, C., & Wu, J. (2015) · PubMed Central · doi:10.3978/j.issn.2304-3881.2014.12.06 · Cited by 131
Guo, P., Pi, H., Xu, S., Zhang, L., Li, Y., Li, M., Cao, Z., Li, T. X., Xie, J., Li, R., et al. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu164 · Cited by 134
Aging and caloric restriction impact adipose tissue, adiponectin, and circulating lipids
Miller, K. N., Burhans, M. S., Clark, J. P., Howell, P. R., Polewski, M. A., DeMuth, T. M., Eliceiri, K. W., Lindstrom, M. J., Ntambi, J. M., & Anderson, R. M. (2017) · Aging Cell · doi:10.1111/acel.12575 · Cited by 133
Yang, S. J., Choi, J. M., Kim, L., Park, S. E., Rhee, E., Lee, W., Oh, K. W., Park, S. W., & Park, C.-Y. (2013) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2013.09.004 · Cited by 135
Mitochondrial biogenesis in cold-bodied fishes
O’Brien, K. M. (2010) · Journal of Experimental Biology · doi:10.1242/jeb.046854 · Cited by 138
GCN5-mediated Transcriptional Control of the Metabolic Coactivator PGC-1β through Lysine Acetylation
Kelly, T. J., Lerín, C., Haas, W., Gygi, S. P., & Puigserver, P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015164 · Cited by 137
Lei, Y., Wang, J., Wang, D., Li, C., Liu, B., Fang, X., You, J., Guo, M., & Lu, X.-Y. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0352-1 · Cited by 131
Morris, K. C., Lin, H. W., Thompson, J. W., & Pérez‐Pinzón, M. A. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2010.229 · Cited by 131
Bruckbauer, A., Zemel, M. B., Thorpe, T., Akula, M. R., Stuckey, A. C., Osborne, D., Martin, E. B., Kennel, S. J., & Wall, J. S. (2012) · Nutrition & Metabolism · doi:10.1186/1743-7075-9-77 · Cited by 130
Calorie restriction and cancer prevention: a mechanistic perspective
Hursting, S. D., Dunlap, S. M., Ford, N. A., Hursting, M. J., & Lashinger, L. M. (2013) · Cancer & Metabolism · doi:10.1186/2049-3002-1-10 · Cited by 137
The Role of Chronic Inflammation in Obesity-Associated Cancers
Ramos‐Niño, M. E. (2013) · ISRN Oncology · doi:10.1155/2013/697521 · Cited by 137
Air Pollution Stress and the Aging Phenotype: The Telomere Connection
Martens, D. S., & Nawrot, T. S. (2016) · Current Environmental Health Reports · doi:10.1007/s40572-016-0098-8 · Cited by 132
Hathorn, T., Snyder-Keller, A., & Messer, A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.08.017 · Cited by 123
Tian, G., Sawashita, J., Kubo, H., Nishio, S.-Y., Hashimoto, S., Suzuki, N., Yoshimura, H., Tsuruoka, M., Wang, Y., Liu, Y., et al. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5406 · Cited by 123
Regulation of Substrate Oxidation Preferences in Muscle by the Peptide Hormone Adropin
Gao, S., McMillan, R. P., Jacas, J., Zhu, Q., Li, X., Kumar, G., Casals, N., Hegardt, F. G., Robbins, P. D., Lopaschuk, G. D., et al. (2014) · Diabetes · doi:10.2337/db14-0388 · Cited by 126
Fröjdö, S., Durand, C., Molin, L., Carey, A. L., El‐Osta, A., Kingwell, B. A., Febbraio, M. A., Solari, F., Vidal, H., & Pirola, L. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.01.008 · Cited by 130
Pieters, N., Janssen, B. G., Dewitte, H., Cox, B., Cuypers, A., Lefebvre, W., Smeets, K., Vanpoucke, C., Plusquin, M., & Nawrot, T. S. (2015) · Environmental Health Perspectives · doi:10.1289/ehp.1509728 · Cited by 125
High-intensity interval training increases SIRT1 activity in human skeletal muscle
Gurd, B. J., Perry, C. G. R., Heigenhauser, G. J. F., Spriet, L. L., & Bonen, A. (2010) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h10-030 · Cited by 135
Review: Quantifying Mitochondrial Dysfunction in Complex Diseases of Aging
Horan, M. P., Pichaud, N., & Ballard, J. W. O. (2012) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr263 · Cited by 136
The many roles of PGC-1α in muscle — recent developments
Chan, M. C., & Arany, Z. P. (2014) · Metabolism · doi:10.1016/j.metabol.2014.01.006 · Cited by 127
Endurance Exercise and the Regulation of Skeletal Muscle Metabolism
Booth, F. W., Ruegsegger, G. N., Toedebusch, R. G., & Yan, Z. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.07.016 · Cited by 128
Nadtochiy, S. M., & Redman, E. (2011) · Nutrition · doi:10.1016/j.nut.2010.12.006 · Cited by 125
Epigenetics in ovarian cancer: premise, properties, and perspectives
Yang, Q., Yang, Y., Zhou, N., Tang, K., Lau, W. B., Lau, B., Wang, W., Xu, L., Yang, Z., Huang, S., et al. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0855-4 · Cited by 123
Albani, D., Polito, L., & Forloni, G. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1215 · Cited by 122
The Current State of NAD+‐Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets
Schiedel, M., Robaa, D., Rumpf, T., Sippl, W., & Jung, M. (2017) · Medicinal Research Reviews · doi:10.1002/med.21436 · Cited by 125
Sirtuins regulate key aspects of lipid metabolism
Lomb, D. J., Laurent, G., & Haigis, M. C. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.11.021 · Cited by 129
Chromatin remodeling, metabolism and circadian clocks: The interplay of CLOCK and SIRT1
Grimaldi, B., Nakahata, Y., Kaluzová, M., Masubuchi, S., & Sassone‐Corsi, P. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.035 · Cited by 121
Neurophysiological and epigenetic effects of physical exercise on the aging process
Kaliman, P., Párrizas, M., Lalanza, J. F., Camins, A., Escorihuela, R. M., & Pallàs, M. (2011) · Ageing Research Reviews · doi:10.1016/j.arr.2011.05.002 · Cited by 125
Therapeutic role of sirtuins in neurodegenerative disease
Outeiro, T. F., Marques, O., & Kazantsev, A. G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.02.010 · Cited by 122
Wilkins, H., Harris, J. L., Carl, S. M., Lezi, E., Lu, J., Selfridge, J. E., Roy, N., Hutfles, L. J., Koppel, S. J., Morris, J. K., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu371 · Cited by 119
Rizki, G., Iwata, T., Li, J., Riedel, C. G., Picard, C. L., Jan, M., Murphy, C. T., & Lee, S. S. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002235 · Cited by 116
Joseph, A.-M., Joanisse, D. R., Baillot, R. G., & Hood, D. A. (2011) · Experimental Diabetes Research · doi:10.1155/2012/642038 · Cited by 119
The Role of Sirtuin1 in Regulating Endothelial Function, Arterial Remodeling and Vascular Aging
Man, A. W. C., Li, H., & Xia, N. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01173 · Cited by 123
Liang, X., Finkel, T., Shen, D., Yin, J., Aszalós, A., & Gottesman, M. M. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-2130 · Cited by 116
Self-citationYuan, Y., Chen, Y., Zhang, P., Huang, S., Zhu, C., Ding, G., Liu, B., Yang, T., & Zhang, A. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.03.015 · Cited by 116
Mäkelä, J., Tselykh, T. V., Maiorana, F., Eriksson, O., Thi, H., Mudò, G., Korhonen, L., Belluardo, N., & Lindholm, D. (2014) · SpringerPlus · doi:10.1186/2193-1801-3-2 · Cited by 119
Sirt1: a metabolic master switch that modulates lifespan
Leibiger, I. B., & Berggren, P. (2006) · Nature Medicine · doi:10.1038/nm0106-34 · Cited by 115
Muñoz-Nájar, U., & Sedivy, J. M. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3250 · Cited by 114
Baskaran, P., Krishnan, V., Fettel, K. D., Gao, P., Zhu, Z., Ren, J. T., & Thyagarajan, B. (2017) · International Journal of Obesity · doi:10.1038/ijo.2017.16 · Cited by 119
Redox-regulating sirtuins in aging, caloric restriction, and exercise
Radak, Z. O., Koltai, E., Taylor, A. W., Higuchi, M., Kumagai, S., Ohno, H., Goto, S., & Boldogh, I. R. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.004 · Cited by 115
Spermidine alleviates cardiac aging by improving mitochondrial biogenesis and function
Wang, J., Li, S., Wang, J., Wu, F., Chen, Y., Zhang, H., Guo, Y., Yan, L., Li, L., Yu, X., et al. (2020) · Aging · doi:10.18632/aging.102647 · Cited by 117
Sanders, O. D., & Rajagopal, L. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200191 · Cited by 117
Tang, B. L., & Chua, C. E. L. (2007) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2007.02.001 · Cited by 114
Singh, S. P., Schragenheim, J., Cao, J. J., Falck, J. R., Abraham, N. G., & Bellner, L. (2016) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2016.07.004 · Cited by 113
Guo, A., Li, K., Tian, H., Fan, Z., Chen, Q., Yang, Y., Yu, J., Wu, Y., & Xiao, Q. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16448 · Cited by 118
Biel, T. G., Lee, S., Flores‐Toro, J., Dean, J. W., Go, K. L., Lee, M.-H., Law, B. K., Law, M. E., Dunn, W. A., Zendejas, I. R., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.96 · Cited by 110
Zhang, X., Du, L.-D., Zhang, W., Yang, Y., Zhou, Q., & Du, G. (2017) · Scientific Reports · doi:10.1038/s41598-017-07442-y · Cited by 110
Ketogenic diets, physical activity and body composition: a review
Ashtary‐Larky, D., Bagheri, R., Bavi, H., Baker, J. S., Moro, T., Mancin, L., & Paoli, A. (2021) · British Journal Of Nutrition · doi:10.1017/s0007114521002609 · Cited by 120
Distribution Analysis of Deacetylase SIRT1 in Rodent and Human Nervous Systems
Zakhary, S. M., Ayubcha, D., Dileo, J. N., Jose, R., Leheste, J. R., Horowitz, J. M., & Torres, G. (2010) · The Anatomical Record · doi:10.1002/ar.21116 · Cited by 109
Metabolic effects of resveratrol: Addressing the controversies
Bitterman, J. L., & Chung, J. H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1808-8 · Cited by 109
Roles of SIRT1 in the acute and restorative phases following induction of inflammation
Zhang, Z., Lowry, S. F., Guarente, L., & Haimovich, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.174482 · Cited by 92
SUMOylation Attenuates the Function of PGC-1α
Rytinki, M. M., & Palvimo, J. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.038943 · Cited by 114
The role of SIRT1 in ocular aging
Mimura, T., Kaji, Y., Noma, H., Funatsu, H., & Okamoto, S. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.07.017 · Cited by 114
Borengasser, S. J., Lau, F., Kang, P., Blackburn, M. L., Ronis, M. J. J., Badger, T. M., & Shankar, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024068 · Cited by 111
Corton, J. C., & Brown-Borg, H. M. (2005) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/60.12.1494 · Cited by 106
Mitochondrial signaling, TOR, and life span
Schieke, S. M., & Finkel, T. (2006) · Biological Chemistry · doi:10.1515/bc.2006.170 · Cited by 106
Self-citationThe Dynamics of the Mitochondrial Organelle as a Potential Therapeutic Target
Stetler, R. A., Leak, R. K., Gao, Y., & Chen, J. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.158 · Cited by 106
Oxidative stress induced lung cancer and COPD: opportunities for epigenetic therapy
Lawless, M. W., O'Byrne, K. J., & Gray, S. G. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00845.x · Cited by 106
Carloni, S., Albertini, M. C., Galluzzi, L., Buonocore, G., Proietti, F., & Balduini, W. (2014) · Journal of Pineal Research · doi:10.1111/jpi.12156 · Cited by 106
The protein acetylome and the regulation of metabolism
Xing, S., & Poirier, Y. (2012) · Trends in Plant Science · doi:10.1016/j.tplants.2012.03.008 · Cited by 104
Histone methyltransferase Smyd1 regulates mitochondrial energetics in the heart
Warren, J. S., Tracy, C. M., Miller, M. R., Makaju, A., Szulik, M. W., Oka, S., Yuzyuk, T. N., Cox, J. E., Kumar, A., Lozier, B. K., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800680115 · Cited by 108
Progress in Nonalcoholic Fatty Liver Disease: SIRT Family Regulates Mitochondrial Biogenesis
Zeng, C., & Chen, M. (2022) · Biomolecules · doi:10.3390/biom12081079 · Cited by 108
Sirt1 protects the heart from aging and stress
Hsu, C., Odewale, I., Alcendor, R. R., & Sadoshima, J. (2008) · Biological Chemistry · doi:10.1515/bc.2008.032 · Cited by 108
Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity
López-Lluch, G. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.005 · Cited by 103
“Importantly, AMPK and SIRT1, the two mainmajor metabolic sensors in cells, modulate directly are direct modulators of PGC1α activity through phosphorylation and deacetylation respectively (Jager et al., 2007; Nemoto et al., 2005).”
BackgroundBrandauer, J., Vienberg, S. G., Agerholm, M., Ringholm, S., Risis, S., Larsen, P. S., Kristensen, J. M., Frøsig, C., Leick, L., Fentz, J., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.259515 · Cited by 107
Resveratrol Attenuates Diabetic Nephropathy via Modulating Angiogenesis
Wen, D., Huang, X., Zhang, M., Zhang, L., Chen, J., Gu, Y., & Hao, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082336 · Cited by 104
Mitochondrial Stress Signaling Promotes Cellular Adaptations
Barbour, J. A., & Turner, N. A. (2014) · International Journal of Cell Biology · doi:10.1155/2014/156020 · Cited by 108
Oocyte Aging: The Role of Cellular and Environmental Factors and Impact on Female Fertility
Ahmed, T. A., Ahmed, S. M., El-Gammal, Z., Shouman, S., Ahmed, A., Mansour, R., & El‐Badri, N. (2019) · Advances in experimental medicine and biology · doi:10.1007/5584_2019_456 · Cited by 105
Autophagy induced by the class III histone deacetylase Sirt1 prevents prion peptide neurotoxicity
Jeong, J., Moon, M., Lee, Y.-J., Seol, J., & Park, S. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.04.002 · Cited by 105
Resveratrol Improves the Mitochondrial Function and Fertilization Outcome of Bovine Oocytes
Takeo, S., Sato, D., Kimura, K., Monji, Y., Kuwayama, T., Kawahara‐Miki, R., & Iwata, H. (2013) · Journal of Reproduction and Development · doi:10.1262/jrd.2013-102 · Cited by 99
Mazucanti, C. H., Cabral‐Costa, J. V., Vasconcelos, A. R., Andreotti, D. Z., Scavone, C., & Kawamoto, E. M. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150610125715 · Cited by 103
Smith, B. C., & Denu, J. M. (2005) · Biochemistry · doi:10.1021/bi052014t · Cited by 102
GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway
Xiang, J., Qin, L., Zhong, J., Xia, N., & Liang, Y. (2023) · Diabetes, Metabolic Syndrome and Obesity · doi:10.2147/dmso.s425642 · Cited by 100
Cunningham, K. E., Vincent, G., Sodhi, C. P., Novak, E. A., Ranganathan, S., Egan, C. E., Stolz, D. B., Rogers, M. B., Firek, B., Morowitz, M. J., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.688812 · Cited by 100
Emerging roles of SIRT1 activator, SRT2104, in disease treatment
Chang, N., Li, J., Lin, S., Zhang, J., Zeng, W.-Q., Ma, G., & Wang, Y. (2024) · Scientific Reports · doi:10.1038/s41598-024-55923-8 · Cited by 107
Peripheral Circadian Oscillators
Cuninkova, L., & Brown, S. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1417.005 · Cited by 103
Metabolic benefits from Sirt1 and Sirt1 activators
Chaudhary, N., & Pfluger, P. T. (2009) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32832cdaae · Cited by 100
Mitochondrial regulator PGC-1a—Modulating the modulator
Miller, K. N., Clark, J. P., & Anderson, R. M. (2019) · Current Opinion in Endocrine and Metabolic Research · doi:10.1016/j.coemr.2019.02.002 · Cited by 101
The physiological roles of Sirt1 in skeletal muscle
Pardo, P. S., & Boriek, A. M. (2011) · Aging · doi:10.18632/aging.100312 · Cited by 105
Koka, S., Aluri, H. S., Xi, L., Lesnefsky, E. J., & Kukreja, R. C. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00865.2013 · Cited by 97
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
Circadian Clocks, Food Intake, and Metabolism
Challet, É. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396971-2.00005-1 · Cited by 103
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
Mechanisms of mitochondrial dysfunction in ovarian aging and potential interventions
Ju, W., Zhao, Y., Yu, Y., Zhao, S., Xiang, S., & Lian, F. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1361289 · Cited by 106
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
MKK3 regulates mitochondrial biogenesis and mitophagy in sepsis-induced lung injury
Mannam, P., Shinn, A. S., Srivastava, A., Neamu, R., Walker, W. E., Bohanon, M. J., Merkel, J., Kang, M., Cruz, C. S. D., Ahasic, A. M., et al. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00272.2013 · Cited by 97
Civitarese, A. E., MacLean, P. S., Carling, S., Kerr-Bayles, L., McMillan, R. P., Pierce, A., Becker, T. C., Moro, C., Finlayson, J., Lefort, N., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.004 · Cited by 95
Fukushima, A., & Lopaschuk, G. D. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.020 · Cited by 94
SIRT1 enhances glucose tolerance by potentiating brown adipose tissue function
Boutant, M., Joffraud, M., Kulkarni, S. S., García-Casarrubios, E., García-Rovés, P. M., Ratajczak, J., Fernández-Marcos, P. J., Valverde, Á. M., Serrano, M., & Cantó, C. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.12.008 · Cited by 94
Moreno‐Ulloa, A., Nogueira, L., Rodríguez, A., Barboza, J., Hogan, M. C., Ceballos, G. M., Villarreal, F. J., & Ramírez‐Sánchez, I. (2014) · The Journals of Gerontology Series A · doi:10.1093/gerona/glu131 · Cited by 94
Gurd, B. J., Yoshida, Y., McFarlan, J. T., Holloway, G. P., Moyes, C. D., Heigenhauser, G. J. F., Spriet, L. L., & Bonen, A. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00417.2010 · Cited by 101
Metadata
- Authors
- Nemoto, S., Fergusson, M. M., & Finkel, T.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Finkel, Toren
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-04
- Volume
- 280
- Issue
- 16
- Pages
- 16456-16460
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2058768220
- Cited by
- 1,047
- References
- 35
- Citations by year
- 2026: 29 · 2025: 28 · 2024: 41 · 2023: 35 · 2022: 48 · 2021: 54 · 2020: 62 · 2019: 55 · 2018: 49 · 2017: 61 · 2016: 59 · 2015: 62 · 2014: 67 · 2013: 73 · 2012: 59
- FWCI
- 17.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- SIRT1, PGC-1α, Sir2, NAD+-dependent deacetylase, ADP-ribosyltransferase, protein-protein interaction, mitochondrial biogenesis, oxygen consumption, cellular metabolism, lifespan extension, nicotinamide, P300, p53, FOXO3, sirtuins
- MeSH terms
- Forkhead Box Protein O1, Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Acetylation, Animals, DNA-Binding Proteins, HeLa Cells, Humans, NAD, Nerve Tissue Proteins, Niacinamide, Nuclear Proteins, Oxygen Consumption, Transcription Factors, Trans-Activators, Tumor Suppressor Protein p53, RNA-Binding Proteins, PC12 Cells, Sirtuins, E1A-Associated p300 Protein, Rats, Forkhead Transcription Factors, Sirtuin 1
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
