The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
SirT1 Regulates Energy Metabolism and Response to Caloric Restriction in Mice
Open accessAbstract
The yeast sir2 gene and its orthologues in Drosophila and C. elegans have well-established roles in lifespan determination and response to caloric restriction. We have studied mice carrying two null alleles for SirT1, the mammalian orthologue of sir2, and found that these animals inefficiently utilize ingested food. These mice are hypermetabolic, contain inefficient liver mitochondria, and have elevated rates of lipid oxidation. When challenged with a 40% reduction in caloric intake, normal mice maintained their metabolic rate and increased their physical activity while the metabolic rate of SirT1-null mice dropped and their activity did not increase. Moreover, CR did not extend lifespan of SirT1-null mice. Thus, SirT1 is an important regulator of energy metabolism and, like its orthologues from simpler eukaryotes, the SirT1 protein appears to be required for a normal response to caloric restriction.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Homologues of Sir2 (called sirtuins) have subsequently been shown to mediate some of the effects of caloric restriction in flies (82) and mammals (83,84).”
From Neural mechanisms of ageing and cognitive decline (2010) · cites this paper as [83]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · cited 1×
“In yeast, worms and flies, an extra copy of the sir2 gene or its orthologue increases lifespan by 18% to 50% [4–6] whereas a deletion of the gene, in yeast, reduces lifespan [4].”
BackgroundSirt1 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
Self-citationCalorie 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
Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775
Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,603
Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409
Sir2 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
Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α
Gerhart‐Hines, Z., Rodgers, J. T., Bare, O., Lerin, C., Kim, S., Mostoslavsky, R., Alt, F. W., Wu, Z., & Puigserver, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601633 · Cited by 1,294
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 444
Funk, J. A., Odejinmi, S. I., & Schnellmann, R. G. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.161992 · Cited by 156
Barclay, R. D., Burd, N. A., Tyler, C. J., Tillin, N. A., & Mackenzie, R. W. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00146 · Cited by 161
Janus‐faced role of SIRT1 in tumorigenesis
Song, N., & Surh, Y. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06762.x · Cited by 146
Fusco, S., Ripoli, C., Podda, M. V., Ranieri, S. C., Leone, L., Toietta, G., McBurney, M. W., Schütz, G., Riccio, A., Grassi, C., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109237109 · Cited by 148
Self-citationAnti-aging pharmacology: Promises and pitfalls
Vaiserman, A. M., Lushchak, O. V., & Koliada, A. K. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.08.004 · Cited by 148
Effect of feeding regimens on circadian rhythms: Implications for agingand longevity
Froy, O., & Miskin, R. (2010) · Aging · doi:10.18632/aging.100116 · Cited by 143
The Tale of Protein Lysine Acetylation in the Cytoplasm
Sadoul, K., Wang, J., Diagouraga, B., & Khochbin, S. (2010) · BioMed Research International · doi:10.1155/2011/970382 · Cited by 148
Alcaín, F. J., & Villalba, J. M. (2009) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543770902762893 · Cited by 137
Macronutrients and caloric intake in health and longevity
Solon‐Biet, S. M., Mitchell, S. J., de Cabo, R., Raubenheimer, D., Couteur, D. G. L., & Simpson, S. J. (2015) · Journal of Endocrinology · doi:10.1530/joe-15-0173 · Cited by 140
SirT1-null mice develop tumors at normal rates but are poorly protected by resveratrol
Boily, G., He, X. H., Pearce, B., Jardine, K. E., & McBurney, M. W. (2009) · Oncogene · doi:10.1038/onc.2009.147 · Cited by 137
Self-citationKelly, G. S. (2010) · PubMed · Cited by 135
Sirtuin‐dependent epigenetic regulation in the maintenance of genome integrity
Bosch‐Presegué, L., & Vaquero, A. (2015) · The FEBS Journal · doi:10.1111/febs.13053 · Cited by 132
Tauopathy: A common mechanism for neurodegeneration and brain aging
Saha, P., & Sen, N. (2019) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2019.01.007 · Cited by 134
Distinct Patterns of Sirtuin Expression During Progression of Alzheimer’s Disease
Lutz, M. I., Milenković, I., Regelsberger, G., & Kovács, G. G. (2014) · NeuroMolecular Medicine · doi:10.1007/s12017-014-8288-8 · Cited by 134
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
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
Sirtuins in stress response: guardians of the genome
Bosch‐Presegué, L., & Vaquero, A. (2013) · Oncogene · doi:10.1038/onc.2013.344 · Cited by 126
TAp63 Is a Master Transcriptional Regulator of Lipid and Glucose Metabolism
Su, X., Gi, Y. J., Chakravarti, D., Chan, I. L., Zhang, A., Xia, X., Tsai, K. Y., & Flores, E. R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.09.006 · Cited by 128
Shinmura, K., Tamaki, K., & Bolli, R. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00602.2008 · Cited by 122
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
SIRT1 metabolic actions: Integrating recent advances from mouse models
Boutant, M., & Cantó, C. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.10.006 · Cited by 122
Caloric restriction and its mimetics
Lee, S.-H., & Min, K.-J. (2013) · BMB Reports · doi:10.5483/bmbrep.2013.46.4.033 · Cited by 119
Sirtuins and Their Relevance to the Kidney
Hao, C., & Haase, V. H. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010010046 · Cited by 118
The conserved role of sirtuins in chromatin regulation
Vaquero, A. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082675av · Cited by 119
SIRT1 is a positive regulator of in vivo bone mass and a therapeutic target for osteoporosis
Zainabadi, K., Liu, C. J., Caldwell, A. L. M., & Guarente, L. (2017) · PLoS ONE · doi:10.1371/journal.pone.0185236 · Cited by 118
Rascón, B., Hubbard, B. P., Sinclair, D. A., & Amdam, G. V. (2012) · Aging · doi:10.18632/aging.100474 · Cited by 119
Law, I. K. M., Liu, L., Xu, A., Lam, K. S. L., Vanhoutte, P. M., Che, C., Leung, P. T. Y., & Wang, Y. (2009) · PROTEOMICS · doi:10.1002/pmic.200800738 · Cited by 114
Mercken, E. M., Hu, J. H., Krzysik-Walker, S. M., Wei, M., Li, Y., McBurney, M. W., de Cabo, R., & Longo, V. D. (2013) · Aging Cell · doi:10.1111/acel.12151 · Cited by 117
Self-citationInduction of Hypothalamic Sirt1 Leads to Cessation of Feeding via Agouti-Related Peptide
Sasaki, T., Kim, H.-J., Kobayashi, M., Kitamura, Y.-I., Yokota‐Hashimoto, H., Shiuchi, T., Minokoshi, Y., & Kitamura, T. (2010) · Endocrinology · doi:10.1210/en.2009-1319 · Cited by 109
Sirtuin-1 regulation of mammalian metabolism
Gillum, M. P., Erion, D. M., & Shulman, G. I. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.09.005 · Cited by 110
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
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
He, X., Gao, J., Hou, H., Qi, Z., Chen, H., & Zhang, X. (2019) · Environmental Science & Technology · doi:10.1021/acs.est.9b05131 · Cited by 106
Self-citationChen, J., Martin‐Gronert, M. S., Tarry‐Adkins, J. L., & Ozanne, S. E. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004950 · Cited by 109
Finley, L. W. S., Lee, J., Souza, A., Desquiret-Dumas, V., Bullock, K., Rowe, G. C., Procaccio, V., Clish, C. B., Arany, Z., & Haigis, M. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1115813109 · Cited by 102
Nutrient Sensing and the Oxidative Stress Response
Luo, H., Chiang, H.-H., Louw, M., Susanto, A., & Chen, D. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.02.008 · Cited by 107
Autophagy as a Potential Target for Sarcopenia: AUTOPHAGY REGULATION IN SARCOPENIA
Fan, J., Kou, X., Jia, S., Yang, X., Yang, Y., & Chen, N. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25260 · Cited by 101
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
Biala, A., Tauriainen, E., Siltanen, A., Shi, J., Merasto, S., Louhelainen, M., Martonen, E., Finckenberg, P., Muller, D. N., & Mervaala, E. (2010) · Blood Pressure · doi:10.3109/08037051.2010.481808 · Cited by 97
PPAR.BETA./.DELTA. regulates the human SIRT1 gene transcription via Sp1
Okazaki, M., Iwasaki, Y., Nishiyama, M., Taguchi, T., Tsugita, M., Nakayama, S., Kambayashi, M., Hashimoto, K., & Terada, Y. (2010) · Endocrine Journal · doi:10.1507/endocrj.k10e-004 · Cited by 102
Association of SIRT1 gene variation with visceral obesity
Peeters, A. V., Beckers, S., Verrijken, A., Mertens, I. L., Roevens, P. W. M., Peeters, P. J., Hul, W. V., & Gaal, L. F. V. (2008) · Human Genetics · doi:10.1007/s00439-008-0567-8 · Cited by 98
Patel, S. A., Chaudhari, A., Gupta, R., Velingkaar, N., & Kondratov, R. V. (2016) · The FASEB Journal · doi:10.1096/fj.15-282475 · Cited by 94
Planavila, A., Domínguez, E., Navarro, M., Vinciguerra, M., Iglesias, R., Giralt, M., Lope‐Piedrafita, S., Ruberte, J., & Villarroya, F. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.07.019 · Cited by 92
SIRT1 regulates metabolism and leukemogenic potential in CML stem cells
Abraham, A., Qiu, S., Chacko, B. K., Li, H., Paterson, A., He, J., Agarwal, P., Shah, M., Welner, R. S., Darley-Usmar, V. M., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci127080 · Cited by 92
SIRT1 suppresses self-renewal of adult hippocampal neural stem cells
Ma, C., Yao, M., Zhai, Q., Jiao, J., Yuan, X., & Poo, M. (2014) · Development · doi:10.1242/dev.117937 · Cited by 87
The SIRT1 deacetylase protects mice against the symptoms of metabolic syndrome
Caron, A. Z., He, X., Mottawea, W., Seifert, E. L., Jardine, K. E., Dewar‐Darch, D., Cron, G. O., Harper, M., Stintzi, A. P., & McBurney, M. W. (2013) · The FASEB Journal · doi:10.1096/fj.13-243568 · Cited by 88
Self-citationThe emerging role of metabolism in fibrosis
Henderson, J., & O’Reilly, S. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.05.003 · Cited by 87
DNA damage and repair in the female germline: contributions to ART
Martin, J. H., Aitken, R. J., Bromfield, E. G., & Nixon, B. (2018) · Human Reproduction Update · doi:10.1093/humupd/dmy040 · Cited by 87
Aging and Inflammation: Etiological Culprits of Cancer
Ahmad, A., Banerjee, S., Wang, Z. P., Kong, D., Majumdar, A. P. N., & Sarkar, F. H. (2009) · Current Aging Science · doi:10.2174/1874609810902030174 · Cited by 83
Kidney aging—inevitable or preventable?
Choudhury, D., & Levi, M. (2011) · Nature Reviews Nephrology · doi:10.1038/nrneph.2011.104 · Cited by 84
Hoffmann, J., Romey, R., Fink, C., Yong, L., & Roeder, T. (2013) · Aging · doi:10.18632/aging.100553 · Cited by 82
Emerging Roles of SIRT1 in Cancer Drug Resistance
Wang, Z., & Chen, W. (2013) · Genes & Cancer · doi:10.1177/1947601912473826 · Cited by 87
The role of mitochondria in rheumatic diseases
Becker, Y. L. C., Duvvuri, B., Fortin, P. R., Lood, C., & Boilard, E. (2022) · Nature Reviews Rheumatology · doi:10.1038/s41584-022-00834-z · Cited by 81
Duszka, K., Gregor, A., Guillou, H., König, J. S., & Wahli, W. (2020) · Cells · doi:10.3390/cells9071708 · Cited by 86
The controversial links among calorie restriction, SIRT1, and resveratrol
Hu, Y., Liu, J., Wang, J., & Liu, Q. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.034 · Cited by 82
Tannous, C., Booz, G. W., Altara, R., Muhieddine, D. H., Mericskay, M., Refaat, M. M., & Zouein, F. A. (2020) · Acta Physiologica · doi:10.1111/apha.13551 · Cited by 80
Dietary restriction: standing up for sirtuins
Baur, J. A., Chen, D., Chini, E. N., Chua, K., Cohen, H. Y., Cabo, R. D., Deng, C., Dimmeler, S., Gius, D., Guarente, L. P., et al. (2010) · Science · doi:10.1126/science.329.5995.1012 · Cited by 76
Self-citationBayliss, J. A., Lemus, M. B., dos Santos, V. V., Deo, M., Davies, J. S., Kemp, B. E., Elsworth, J. D., & Andrews, Z. B. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159381 · Cited by 78
Commonly adopted caloric restriction protocols often involve malnutrition
Cerqueira, F. M., & Kowaltowski, A. J. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.05.002 · Cited by 76
Khader, A., Yang, W.-L., Kuncewitch, M., Jacob, A., Prince, J. M., Asirvatham, J. R., Nicastro, J. M., Coppa, G. F., & Wang, P. (2014) · Transplantation · doi:10.1097/tp.0000000000000194 · Cited by 75
Maeda, S., Koya, D., Araki, S., Babazono, T., Umezono, T., Toyoda, M., Kawai, K., Imanishi, M., Uzu, T., Suzuki, D., et al. (2011) · Clinical and Experimental Nephrology · doi:10.1007/s10157-011-0418-0 · Cited by 76
The Importance of NAD in Multiple Sclerosis
Penberthy, W. T., & Tsunoda, I. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787185751 · Cited by 77
Caloric restriction and chronic inflammatory diseases
González, O. A., Tobia, C. M., Ebersole, J. L., & Novak, M. J. (2011) · Oral Diseases · doi:10.1111/j.1601-0825.2011.01830.x · Cited by 81
Calorie restriction protects against experimental abdominal aortic aneurysms in mice
Liu, Y., Wang, T., Zhang, R., Fu, W.-Y., Wang, X., Wang, F., Gao, P., Ding, Y.-N., Xie, Y., Hao, D., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151794 · Cited by 75
Cerqueira, F. M., da Cunha, F. M., da Silva, C. C. C., Chausse, B., Romano, R. L., Garcia, C. C. M., Colepicolo, P., de Medeiros, M. H. G., & Kowaltowski, A. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.07.006 · Cited by 73
Mouchiroud, L., Molin, L., Dallière, N., & Solari, F. (2010) · BioFactors · doi:10.1002/biof.127 · Cited by 74
Ambient temperature influences aging in an annual fish (Nothobranchius rachovii)
Hsu, C., & Chiu, Y. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00525.x · Cited by 72
The role of sirtuins in Alzheimer's disease
Lalla, R., & Dönmez, G. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00016 · Cited by 71
Resveratrol vs. calorie restriction: Data from rodents to humans
Lam, Y. Y., Peterson, C. M., & Ravussin, É. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.04.005 · Cited by 75
Modeling transcriptomic age using knowledge-primed artificial neural networks
Holzscheck, N., Falckenhayn, C., Söhle, J., Kristof, B., Siegner, R., Werner, A., Schössow, J., Jürgens, C., Völzke, H., Wenck, H., et al. (2021) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-021-00068-5 · Cited by 71
Kim, M. Y., Kang, E. S., Ham, S. A., Hwang, J. S., Yoo, T. S., Lee, H., Paek, K. S., Park, C., Lee, H. T., Kim, J., et al. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.09.008 · Cited by 71
A CREB-Sirt1-Hes1 Circuitry Mediates Neural Stem Cell Response to Glucose Availability
Fusco, S., Leone, L., Barbati, S. A., Samengo, D., Piacentini, R., Maulucci, G., Toietta, G., Spinelli, M., McBurney, M. W., Pani, G., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.092 · Cited by 71
Self-citationSrivastava, S., & Haigis, M. C. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072526 · Cited by 70
SIRT1 Regulation of Wakefulness and Senescence-Like Phenotype in Wake Neurons
Panossian, L. A., Fenik, P., Zhu, Y., Zhan, G., McBurney, M. W., & Veasey, S. C. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5166-10.2011 · Cited by 70
Self-citationQuintens, R., Singh, S., Lemaire, K., Bock, K. D., Granvik, M., Schraenen, A., Vroegrijk, I. O. C. M., Costa, V., Noten, P. V., Lambrechts, D., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056719 · Cited by 70
Dietary patterns and cardiometabolic health: Clinical evidence and mechanism
Wang, W., Liu, Y., Li, Y., Luo, B., Lin, Z., Chen, K., & Liu, Y. (2023) · MedComm · doi:10.1002/mco2.212 · Cited by 89
Saunders, L. R., & Verdin, E. M. (2009) · Science · doi:10.1126/science.1170007 · Cited by 70
Bao, J., & Sack, M. N. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0402-y · Cited by 67
Molecular Links between Caloric Restriction and Sir2/SIRT1 Activation
Wang, Y. (2014) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2014.38.5.321 · Cited by 68
Costa‐Machado, L. F., & Fernández-Marcos, P. J. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1634953 · Cited by 66
Histone variant macroH2A1 deletion in mice causes female-specific steatosis
Boulard, M., Storck, S., Cong, R., Pinto, R. O., Delage, H., & Bouvet, P. (2010) · Epigenetics & Chromatin · doi:10.1186/1756-8935-3-8 · Cited by 67
SirT1 in muscle physiology and disease: lessons from mouse models
Vinciguerra, M., Fulco, M., Ladurner, A. G., Sartorelli, V., & Rosenthal, N. A. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.004655 · Cited by 66
SIRT1 is a Highly Networked Protein That Mediates the Adaptation to Chronic Physiological Stress
McBurney, M. W., Clark-Knowles, K. V., Caron, A. Z., & Gray, D. A. (2013) · Genes & Cancer · doi:10.1177/1947601912474893 · Cited by 69
Self-citationBenayoun, B. A., Batista, F., Auer, J., Dipietromaria, A., L’Hôte, D., Baere, E. B. W. D., & Veitia, R. A. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn389 · Cited by 70
Distinctive Roles of Sirtuins on Diabetes, Protective or Detrimental?
Song, J., Yang, B., Jia, X., Li, M., Tan, W. F., Ma, S., Shi, X., & Feng, L. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00724 · Cited by 67
NAD: A master regulator of transcription
Ghosh, S., George, S., Roy, U., Ramachandran, D., & Kolthur‐Seetharam, U. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.08.002 · Cited by 64
Huang, J. H., & Hood, D. A. (2009) · IUBMB Life · doi:10.1002/iub.164 · Cited by 71
Fok, W. C., Zhang, Y., Salmon, A. B., Bhattacharya, A., Gunda, R., Jones, D. P., Ward, W. F., Fisher, K., Richardson, A. G., & Pérez, V. (2012) · The Journals of Gerontology Series A · doi:10.1093/gerona/gls127 · Cited by 66
Zhang, Y., Connelly, K. A., Thai, K., Wu, X., Kapùs, A., Kepecs, D. M., & Gilbert, R. E. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.09.016 · Cited by 64
Sirtuin 1, stem cells, aging, and stem cell aging
Mantel, C., & Broxmeyer, H. E. (2008) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3283043819 · Cited by 65
Systemic regulation of mammalian ageing and longevity by brain sirtuins
Satoh, A., & Imai, S. (2014) · Nature Communications · doi:10.1038/ncomms5211 · Cited by 63
Yu, W., Wan, Z., Qiu, X., Chen, Y., & Dai, Y. (2013) · Asian Journal of Andrology · doi:10.1038/aja.2013.60 · Cited by 63
Diversification of NAD biological role : the importance of location
Stefano, M. D., & Conforti, L. (2013) · FEBS Journal · doi:10.1111/febs.12433 · Cited by 62
SirT1 catalytic activity is required for male fertility and metabolic homeostasis in mice
Seifert, E. L., Caron, A. Z., Morin, K., Coulombe, J., He, X. H., Jardine, K. E., Dewar‐Darch, D., Boekelheide, K., Harper, M., & McBurney, M. W. (2011) · The FASEB Journal · doi:10.1096/fj.11-193979 · Cited by 63
Self-citationLiu, W.-J., Zhang, X., Wang, N., Zhou, X., Fu, Y., & Luo, L. (2015) · European journal of medical research · doi:10.1186/s40001-015-0114-8 · Cited by 61
Lidell, M. E., Seifert, E. L., Westergren, R., Heglind, M., Gowing, A., Sukonina, V., Arani, Z., Itkonen, P., Wallin, S., Westberg, F., et al. (2011) · Diabetes · doi:10.2337/db10-0409 · Cited by 64
Self-citationKitada, M., Kume, S., Takeda-Watanabe, A., Tsuda, S.-I., Kanasaki, K., & Koya, D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.06.014 · Cited by 60
Clinicopathological significance of SIRT1 expression in colorectal adenocarcinoma
Lv, L., Shen, Z., Zhang, J., Zhang, H., Dong, J., Yan, Y., Liu, F., Jiang, K., Ye, Y., & Wang, S. (2014) · Medical Oncology · doi:10.1007/s12032-014-0965-9 · Cited by 60
SIRT1 in the Development and Treatment of Hepatocellular Carcinoma
Farcas, M. F., Andrei-Alexandru, G., Gulei, D., Ionescu, C., Irimie, A., Cătană, C.-S., & Berindan‐Neagoe, I. (2019) · Frontiers in Nutrition · doi:10.3389/fnut.2019.00148 · Cited by 61
SIRT1 as a therapeutic target for Alzheimer’s disease
Wong, S. Y., & Tang, B. L. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0023 · Cited by 59
Metadata
- Authors
- Boily, G., Seifert, E. L., Bevilacqua, L., He, X. H., Sabourin, G., Estey, C., Moffat, C., Crawford, S., Saliba, S., Jardine, K., Xuan, J., Evans, M., Harper, M.-E., & McBurney, M. W.
- Affiliations
- University of Ottawa (CA)
- Corresponding author
- McBurney, Michael W.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2008-03-12
- Volume
- 3
- Issue
- 3
- Pages
- e1759
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC2258149
- OpenAlex
- W2035543709
- Cited by
- 444
- References
- 40
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 7 · 2023: 8 · 2022: 12 · 2021: 16 · 2020: 17 · 2019: 22 · 2018: 20 · 2017: 23 · 2016: 27 · 2015: 25 · 2014: 34 · 2013: 41 · 2012: 29
- FWCI
- 20.45
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Canadian Diabetes Association
- University of Guelph
- Canadian Institutes of Health Research
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- SIRT1, sirtuins, caloric restriction, energy metabolism, hypermetabolism, mitochondrial efficiency, liver mitochondria, lipid oxidation, metabolic rate, physical activity, lifespan
- MeSH terms
- Animals, Energy Intake, Calorimetry, Energy Metabolism, Hormones, Mitochondria, Liver, Reactive Oxygen Species, Mice, Knockout, Sirtuins, Mice, 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