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
Lagouge, 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
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
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185
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
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
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
Recent progress in the biology and physiology of sirtuins
Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,506
Self-citationA 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 1,510
Self-citationNakahata, 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
Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction
Haigis, M. C., & Guarente, L. P. (2006) · Genes & Development · doi:10.1101/gad.1467506 · Cited by 1,295
Histone Deacetylase Inhibitors: Overview and Perspectives
Dokmanovic, M., Clarke, C., & Marks, P. A. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-0324 · Cited by 1,194
Kim, D., Nguyen, M. D., Dobbin, M. M., Fischer, A., Sananbenesi, F., Rodgers, J. T., Delalle, I., Baur, J. A., Sui, G., Armour, S. M., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601758 · Cited by 1,074
AMPK 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
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 843
The Role of Sirtuins in Antioxidant and Redox Signaling
Singh, C. K., Chhabra, G., Ndiaye, M. A., Garcia‐Peterson, L. M., Mack, N. J., & Ahmad, N. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7290 · Cited by 820
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 847
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792
Calorie Restriction Increases Muscle Mitochondrial Biogenesis in Healthy Humans
Civitarese, A. E., Carling, S., Heilbronn, L. K., Hulver, M. H., Ukropcova, B., Deutsch, W. A., Smith, S. R., & Ravussin, E. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040076 · Cited by 790
Stressing the role of FoxO proteins in lifespan and disease
van der Horst, A., & Burgering, B. M. T. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2190 · Cited by 759
Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740
Timmons, J. A., Wennmalm, K., Larsson, O., Walden, T. B., Lassmann, T., Petrovic, N., Hamilton, D. L., Gimeno, R. E., Wahlestedt, C., Baar, K., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610615104 · Cited by 732
Sirtuin 1 and Sirtuin 3: Physiological Modulators of Metabolism
Nogueiras, R., Habegger, K. M., Chaudhary, N., Finan, B., Banks, A. S., Dietrich, M. O., Horváth, T. L., Sinclair, D. A., Pfluger, P. T., & Tschöp, M. H. (2012) · Physiological Reviews · doi:10.1152/physrev.00022.2011 · Cited by 724
Targeting adipose tissue in the treatment of obesity-associated diabetes
Kusminski, C. M., Bickel, P. E., & Scherer, P. E. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.75 · Cited by 678
Calorie restriction induces mitochondrial biogenesis and bioenergetic efficiency
López-Lluch, G., Hunt, N., Jones, B., Zhu, M., Jamieson, H., Hilmer, S., Cascajo, M. V., Allard, J., Ingram, D. K., Navas, P., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510452103 · Cited by 699
SIRT1 Deacetylates and Positively Regulates the Nuclear Receptor LXR
Li, X., Zhang, S., Blander, G., Tse, J. G., Krieger, M., & Guarente, L. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.032 · Cited by 649
Schieke, S. M., Phillips, D., McCoy, J. P., Aponte, A. M., Shen, R.-F., Balaban, R. S., & Finkel, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603536200 · Cited by 623
Self-citationYun, J., & Finkel, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.011 · Cited by 626
Self-citationTranscriptional 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 626
Mitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641
Radak, Z. O., Zhao, Z., Koltai, E., Ohno, H., & Atalay, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4498 · Cited by 643
Metabolic adaptations through the PGC‐1α and SIRT1 pathways
Rodgers, J. T., Lerin, C., Gerhart-Hines, Z., & Puigserver, P. (2008) · FEBS Letters · doi:10.1016/j.febslet.2007.11.034 · Cited by 561
Wenz, 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
RetractedThe neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies
Maalouf, M., Rho, J. M., & Mattson, M. P. (2008) · Brain Research Reviews · doi:10.1016/j.brainresrev.2008.09.002 · Cited by 584
Silent Information Regulator 1 Protects the Heart From Ischemia/Reperfusion
Hsu, C., Zhai, P., Yamamoto, T., Maejima, Y., Matsushima, S., Hariharan, N., Shao, D., Takagi, H., Oka, S., & Sadoshima, J. (2010) · Circulation · doi:10.1161/circulationaha.110.958033 · Cited by 573
SIRT1 Deacetylates and Inhibits SREBP-1C Activity in Regulation of Hepatic Lipid Metabolism*
Ponugoti, B., Kim, D.-H., Xiao, Z., Smith, Z., Miao, J., Zang, M., Wu, S.-Y., Chiang, C., Veenstra, T. D., & Kemper, J. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.122978 · Cited by 553
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
SIRT2 Regulates Adipocyte Differentiation through FoxO1 Acetylation/Deacetylation
Jing, E., Gesta, S., & Kahn, C. R. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.07.003 · Cited by 500
Sirtuin Functions in Health and Disease
Yamamoto, H., Schoonjans, K., & Auwerx, J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0079 · Cited by 480
Mechanisms of neurodegeneration in Huntington’s disease
Gil‐Mohapel, J., & Rego, A. C. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06310.x · Cited by 497
Sirtuins as potential targets for metabolic syndrome
Guarente, L. (2006) · Nature · doi:10.1038/nature05486 · Cited by 468
Crosstalk between Oxidative Stress and SIRT1: Impact on the Aging Process
Salminen, A., Kaarniranta, K., & Kauppinen, A. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14023834 · Cited by 464
Resveratrol induces mitochondrial biogenesis in endothelial cells
Csiszár, A., Labinskyy, N., Pinto, J. T., Ballabh, P., Zhang, H., Losonczy, G., Pearson, K. J., de Cabo, R., Pacher, P., Zhang, C., et al. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00368.2009 · Cited by 459
SirT1 Regulates Energy Metabolism and Response to Caloric Restriction in Mice
Boily, G., Seifert, E. L., Bevilacqua, L., He, X. H., Sabourin, G., Estey, C., Moffat, C., Crawford, S., Saliba, S., Jardine, K., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001759 · Cited by 444
Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?
Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433
Akt-dependent transformation: there is more to growth than just surviving
Plas, D. R., & Thompson, C. B. (2005) · Oncogene · doi:10.1038/sj.onc.1209097 · Cited by 431
Sirtuins — novel therapeutic targets to treat age-associated diseases
Lavu, S., Boss, O., Elliott, P. J., & Lambert, P. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2665 · Cited by 427
Are sirtuins viable targets for improving healthspan and lifespan?
Baur, J. A., Ungvari, Z. I., Minor, R. K., Couteur, D. G. L., & de Cabo, R. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3738 · Cited by 393
Seven sirtuins for seven deadly diseases ofaging
Morris, B. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.525 · Cited by 386
The role of sirtuins in cardiac disease
Matsushima, S., & Sadoshima, J. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00053.2015 · Cited by 390
Coordination of metabolic plasticity in skeletal muscle
Hood, D. A., Irrcher, I., Ljubicic, V., & Joseph, A.-M. (2006) · Journal of Experimental Biology · doi:10.1242/jeb.02182 · Cited by 370
Mitochondrial function in hypoxic ischemic injury and influence of aging
Ham, P. B., & Raju, R. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.006 · Cited by 374
Liang, F.-X., Kume, S., & Koya, D. (2009) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2009.101 · Cited by 358
Walker, A. K., Yang, F., Jiang, K., Ji, J.-Y., Watts, J. L., Purushotham, A., Boss, O., Hirsch, M. L., Ribich, S., Smith, J. J., et al. (2010) · Genes & Development · doi:10.1101/gad.1901210 · Cited by 357
Sirtuin activators and inhibitors
Villalba, J. M., & Alcain, F. J. (2012) · BioFactors · doi:10.1002/biof.1032 · Cited by 361
Gong, B., Pan, Y., Vempati, P., Zhao, W., Knable, L., Ho, L., Wang, J., Sastre, M., Ono, K., Sauve, A. A., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.12.005 · Cited by 345
Aquilano, K., Vigilanza, P., Baldelli, S., Pagliei, B., Rotilio, G., & Ciriolo, M. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.070169 · Cited by 347
Resveratrol attenuates mitochondrial oxidative stress in coronary arterial endothelial cells
Ungvari, Z. I., Labinskyy, N., Mukhopadhyay, P., Pinto, J. T., Bagi, Z. A., Ballabh, P., Zhang, C., Pacher, P., & Csiszár, A. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00375.2009 · Cited by 348
The Sir2 family of protein deacetylases
Denu, J. M. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2005.08.010 · Cited by 325
SIRT4 Regulates Fatty Acid Oxidation and Mitochondrial Gene Expression in Liver and Muscle Cells
Nasrin, N., Wu, X.-P., Fortier, E., Feng, Y., Bare, O., Chen, S., Ren, X., Wu, Z., Streeper, R. S., & Bordone, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.124164 · Cited by 327
SIRT3 regulation of mitochondrial oxidative stress
Bause, A. S., & Haigis, M. C. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.007 · Cited by 311
Kim, M. Y., Lim, J. H., Youn, H. H., Hong, Y. A., Yang, K. S., Park, H., Chung, S., Koh, S. H., Shin, S. J., Choi, B. S., et al. (2012) · Diabetologia · doi:10.1007/s00125-012-2747-2 · Cited by 315
Role of Sirtuin1-p53 regulatory axis in aging, cancer and cellular reprogramming
Ong, A. L. C., & Ramasamy, T. S. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.02.004 · Cited by 305
The Deacetylase Sirt6 Activates the Acetyltransferase GCN5 and Suppresses Hepatic Gluconeogenesis
Dominy, J. E., Lee, Y., Jedrychowski, M. P., Chim, H., Jurczak, M. J., Camporez, J. P., Ruan, H., Feldman, J., Pierce, K. A., Mostoslavsky, R., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.030 · Cited by 303
PGC-1α and PGC-1Β Regulate Mitochondrial Density in Neurons
Warȩski, P., Vaarmann, A., Choubey, V., Safiulina, D., Liiv, J., Kuum, M., & Kaasik, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.018911 · Cited by 295
Calorie restriction as an intervention in ageing
López‐Lluch, G., & Navas, P. (2015) · The Journal of Physiology · doi:10.1113/jp270543 · Cited by 301
Ippolito, L., Morandi, A., Taddei, M. L., Parri, M., Comito, G., Iscaro, A., Raspollini, M. R., Magherini, F., Rapizzi, E., Masquelier, J., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0805-7 · Cited by 290
Anderson, R. M., Barger, J. L., Edwards, M. G., Braun, K. H., O’Connor, C. E., Prolla, T. A., & Weindruch, R. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00357.x · Cited by 283
“Why the cellular response to oxidative stress alters mitochondrial function is a matter of speculation: the changes in membrane potential could reflect (i) a response to increased energy demand as cellular survival pathways are induced; (ii) a change in flux of endogenous mitochondrial-derived…”
BackgroundBraidy, N., Berg, J., Clement, J., Khorshidi, F., Poljak, A., Jayasena, T., Grant, R., & Sachdev, P. S. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7269 · Cited by 294
Endocrine Crosstalk Between Skeletal Muscle and the Brain
Delezie, J., & Handschin, C. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00698 · Cited by 277
Sirtuins in Epigenetic Regulation
Jing, H., & Lin, H. (2015) · Chemical Reviews · doi:10.1021/cr500457h · Cited by 276
SIRT1 Regulates the Function of the Nijmegen Breakage Syndrome Protein
Yuan, Z., Zhang, X. M., Sengupta, N., Lane, W. S., & Seto, E. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.029 · Cited by 277
Egan, B., & Sharples, A. P. (2023) · Physiological Reviews · doi:10.1152/physrev.00054.2021 · Cited by 278
Pallos, J., Bodai, L., Lukácsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., & Marsh, J. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn273 · Cited by 272
Nicotinamide N -Methyltransferase: More Than a Vitamin B3 Clearance Enzyme
Pissios, P. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.02.004 · Cited by 259
Hong, S., Moreno‐Navarrete, J. M., Wei, X., Kikukawa, Y., Tzameli, I., Prasad, D., Lee, Y., Asara, J. M., Fernández‐Real, J. M., Maratos–Flier, E., et al. (2015) · Nature Medicine · doi:10.1038/nm.3882 · Cited by 260
Regulation of catalase expression in healthy and cancerous cells
Glorieux, C., Zámocký, M., Sandoval, J. M., Verrax, J., & Calderón, P. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.017 · Cited by 268
Energy Balance, Host-Related Factors, and Cancer Progression
Hursting, S. D., & Berger, N. A. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2010.27.9935 · Cited by 257
Reconsidering the Role of Mitochondria in Aging
Gonzalez-Freire, M., de Cabo, R., Bernier, M., Sollott, S. J., Fabbri, E., Navas, P., & Ferrucci, L. (2015) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glv070 · Cited by 244
Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3
Brenmoehl, J., & Hoeflich, A. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.04.002 · Cited by 248
Radical medicine: treating ageing to cure disease
Finkel, T. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1763 · Cited by 234
Self-citationUittenbogaard, M. N., & Chiaramello, A. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140305224906 · Cited by 246
Mechanisms Underlying Caloric Restriction and Lifespan Regulation
Ungvari, Z. I., Parrado‐Fernández, C., Csiszár, A., & de Cabo, R. (2008) · Circulation Research · doi:10.1161/circresaha.107.168369 · Cited by 243
Lin, Z., & Fang, D. (2013) · Genes & Cancer · doi:10.1177/1947601912475079 · Cited by 250
Sirtuin regulation in aging and injury
Poulose, N., & Raju, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.08.017 · Cited by 236
Oxidative Stress and Huntington’s Disease: The Good, the Bad, and the Ugly
Kumar, A., & Ratan, R. R. (2016) · Journal of Huntington s Disease · doi:10.3233/jhd-160205 · Cited by 236
Metabolic aspects in NAFLD, NASH and hepatocellular carcinoma: the role of PGC1 coactivators
Piccinin, E., Villani, G., & Moschetta, A. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-018-0089-3 · Cited by 232
Mitochondrial Metabolism, Sirtuins, and AgingPreprint
Sack, M. N., & Finkel, T. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013102 · Cited by 242
Self-citationThe SirT3 Divining Rod Points to Oxidative Stress
Bell, E. L., & Guarente, L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.008 · Cited by 235
Metabolic Reprogramming Is Required for Myofibroblast Contractility and Differentiation
Bernard, K. F., Logsdon, N. J., Ravi, S., Xie, N., Persons, B. P., Rangarajan, S., Zmijewski, J. W., Mitra, K., Liu, G., Darley-Usmar, V. M., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.646984 · Cited by 231
Effects of Resveratrol and SIRT1 on PGC-1α Activity and Mitochondrial Biogenesis: A Reevaluation
Higashida, K., Kim, S. H., Jung, S. R., Asaka, M., Holloszy, J. O., & Han, D.-H. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001603 · Cited by 237
Role of Age-Related Mitochondrial Dysfunction in Sarcopenia
Ferri, E., Marzetti, E., Calvani, R., Picca, A., Cesari, M., & Arosio, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155236 · Cited by 224
Therapeutic potential of resveratrol in Alzheimer's disease
Vingtdeux, V., Dreses‐Werringloer, U., Zhao, H., Davies, P. J., & Marambaud, P. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-s2-s6 · Cited by 230
Mutual Dependence of Foxo3a and PGC-1α in the Induction of Oxidative Stress Genes
Olmos, Y., Valle, I., Borniquel, S., Tiérrez, A., Soria, E., Lamas, S., & Monsalve, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807397200 · Cited by 229
Amat, R., Planavila, A., Chen, S. L., Iglesias, R., Giralt, M., & Villarroya, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022749 · Cited by 224
SIRT1 is regulated by a PPARγ–SIRT1 negative feedback loop associated with senescence
Han, L., Zhou, R., Niu, J., McNutt, M. A., Wang, P., & Tong, T. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq609 · Cited by 218
Resveratrol and Brain Mitochondria: a Review
Jardim, F. R., de Rossi, F. T., Nascimento, M. X., Barros, R. G. D. S., Borges, P. A., Prescilio, I. C., & de Oliveira, M. R. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0448-z · Cited by 225
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · Stresses · doi:10.3390/stresses2030019 · Cited by 218
Ota, H., Eto, M., Kano, M. R., Kahyo, T., Setou, M., Ogawa, S., Iijima, K., Akishita, M., & Ouchi, Y. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.210500 · Cited by 218
Hadanny, A., & Efrati, S. (2020) · Biomolecules · doi:10.3390/biom10060958 · Cited by 228
FoxO1 Mediates an Autofeedback Loop Regulating SIRT1 Expression
Xiong, S., Salazar, G., Patrushev, N. A., & Alexander, R. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163667 · Cited by 221
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
