The DOI matches its Crossref record; 160 of the 160 references it cites were found in a registry or an index.
Sirtuins as regulators of metabolism and healthspan
Open accessAbstract
Since the beginning of the century, the mammalian sirtuin protein family (comprising SIRT1-SIRT7) has received much attention for its regulatory role, mainly in metabolism and ageing. Sirtuins act in different cellular compartments: they deacetylate histones and several transcriptional regulators in the nucleus, but also specific proteins in other cellular compartments, such as in the cytoplasm and in mitochondria. As a consequence, sirtuins regulate fat and glucose metabolism in response to physiological changes in energy levels, thereby acting as crucial regulators of the network that controls energy homeostasis and as such determines healthspan.
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?
The cited source says what the claim attributes to it.
In the citing paper
“Regarding mammals, several studies have shown that several of the seven mammalian sirtuins can delay various parameters of aging in mice (Houtkooper et al., 2012; Sebastian et al., 2012).”
From The Hallmarks of Aging (2013) · cites this paper as Houtkooper et al., 2012
In the citing paper
“sirtuins can regulate gene expression by deacetylating histone and non-histone substrates, and this activity depends on a cofactor linked to the cellular energy status, NAD+ (nicotinamide adenine dinucleotide) (Houtkooper et al., 2012).”
From The Aging Epigenome (2016) · cites this paper as Houtkooper et al., 2012
In the citing paper
“The SIRT family of NAD+-dependent deacylases, comprising seven members that vary in tissue specificity, subcellular localization, enzymatic activity, and targets, mediates metabolic flexibility in animal models (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“Nicotinamide mononucleotide conversion to NAD+ activates SIRT1 and improves glucose homeostasis in mice (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“SIRT3, which is localized in the mitochondrial matrix, targets many proteins involved in metabolic homeostasis, including OXPHOS subunits (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“SIRT1 controls the activity of transcription factors and cofactors such as p53, MEF2, FOXO, and PGC1α, which govern mitochondrial biogenesis and activity and lipid and glucose metabolism (42).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [42]
In the citing paper
“This is due to changes in the balances between acetylation and deacetylation rates, for instance involving the mitochondrial NAD+-dependent deacetylase SIRT3 (Houtkooper et al, 2012).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Houtkooper et al, 2012
In the citing paper
“Indeed, different situations of energy restriction, including fasting and exercise, increase NAD+ levels and trigger SIRT1/PGC-1α-dependent mitochondrial adaptation (Lin et al, 2000; Houtkooper et al, 2012).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Houtkooper et al, 2012
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
1 retracted
RETRACTED: Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex
Zhang, Q., Wang, S.-Y., Fleuriel, C., Leprince, D., Rocheleau, J. V., Piston, D. W., & Goodman, R. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610590104 · Cited by 171
RetractedSREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15593 · Cited by 4,794
Resveratrol improves health and survival of mice on a high-calorie diet
Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290
SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver
Horton, J. D., Goldstein, J. L., & Brown, M. S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215593 · Cited by 4,092
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
Self-citationmTOR: from growth signal integration to cancer, diabetes and ageing
Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941
Kim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905
Small 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
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
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
Self-citationStress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
Extending Healthy Life Span—From Yeast to Humans
Fontana, L., Partridge, L., & Longo, V. D. (2010) · Science · doi:10.1126/science.1172539 · Cited by 3,023
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
AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
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
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
Poly(ADP-ribose): novel functions for an old molecule
Schreiber, V., Dantzer, F., Amé, J., & de MURCIA, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,975
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
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
SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Hirschey, M. D., Shimazu, T., Goetzman, E., Jing, E., Schwer, B., Lombard, D. B., Grueter, C. A., Harris, C., Biddinger, S., Ilkayeva, O. R., et al. (2010) · Nature · doi:10.1038/nature08778 · Cited by 1,687
Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6
Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637
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
Self-citationIncreased 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
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
Self-citationPhylogenetic 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
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 1,366
miR-34a repression of SIRT1 regulates apoptosis
Yamakuchi, M., Ferlito, M., & Lowenstein, C. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801613105 · Cited by 1,362
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
Yoshino, J., Mills, K. F., Yoon, M. J., & Imai, S.-I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.014 · Cited by 1,340
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
Self-citationCalorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
Qiu, X., Brown, K., Hirschey, M. D., Verdin, E., & Chen, D. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.015 · Cited by 1,310
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291
Regulation of pgc-1α, a nodal regulator of mitochondrial biogenesis
Fernandez-Marcos, P. J., & Auwerx, J. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.001917 · Cited by 1,237
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
Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes
Muoio, D. M., & Newgard, C. B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2327 · Cited by 1,177
Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162
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
Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111
Handschin, C., & Spiegelman, B. M. (2006) · Endocrine Reviews · doi:10.1210/er.2006-0037 · Cited by 1,090
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 1,003
Bitterman, K. J., Anderson, R. M., Cohen, H. Y., Latorre-Esteves, M., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205670200 · Cited by 1,002
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
Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921
Self-citationSRT1720, 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
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
Self-citationThe PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.017 · Cited by 877
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
Self-citationSirt1 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 818
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · cited 1×
“As a result, deletion of Sirt3 in mice impairs fat breakdown, exacerbating diet-induced obesity and rendering them sensitive to cold upon fastin”
BackgroundSIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
Nakagawa, T., Lomb, D. J., Haigis, M. C., & Guarente, L. (2009) · Cell · doi:10.1016/j.cell.2009.02.026 · Cited by 787
Nucleocytoplasmic Shuttling of the NAD+-dependent Histone Deacetylase SIRT1*
Tanno, M., Sakamoto, J., Miura, T., Shimamoto, K., & Horio, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609554200 · Cited by 784
SIRT3 Opposes Reprogramming of Cancer Cell Metabolism through HIF1α Destabilization
Finley, L. W. S., Carracedo, A., Lee, J., Souza, A., Egia, A., Zhang, J., Teruya-Feldstein, J., Moreira, P. I., Cardoso, S. M., Clish, C. B., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.02.014 · Cited by 782
Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation
Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., Towler, M. C., Brown, L. J., Ogunbayo, O. A., Evans, A. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.001 · Cited by 773
Sirtuin 1 Modulates Cellular Responses to Hypoxia by Deacetylating Hypoxia-Inducible Factor 1α
Lim, J.-H., Lee, Y.-M., Chun, Y.-S., Chen, J., Kim, J.-E., & Park, J.-W. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.023 · Cited by 758
The first identification of lysine malonylation substrates and its regulatory enzyme
Peng, C., Lu, Z., Xie, Z., Cheng, Z., Chen, Y., Tan, M., Luo, H., Zhang, Y., He, W., Yang, K., et al. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.012658 · Cited by 751
Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750
Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736
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
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
Self-citationSirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells
Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715
Nutrient Availability Regulates SIRT1 Through a Forkhead-Dependent Pathway
Nemoto, S., Fergusson, M. M., & Finkel, T. (2004) · Science · doi:10.1126/science.1101731 · Cited by 671
SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosisPreprint
Vaquero, A., Scher, M. B., Lee, D. H., Sutton, A., Cheng, H.-L., Alt, F. W., Serrano, L., Sternglanz, R., & Reinberg, D. (2006) · Genes & Development · doi:10.1101/gad.1412706 · Cited by 670
Tumor Suppressor HIC1 Directly Regulates SIRT1 to Modulate p53-Dependent DNA-Damage Responses
Chen, W., Wang, D. H., Yen, R.-W. C., Luo, J., Gu, W. J., & Baylin, S. B. (2005) · Cell · doi:10.1016/j.cell.2005.08.011 · Cited by 663
Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
Verdin, E., Hirschey, M. D., Finley, L. W. S., & Haigis, M. C. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.003 · Cited by 661
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
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
Vakhrusheva, O., Smolka, C., Gajawada, P., Sawa Kostin, D., Boettger, T., Kubin, T., Braun, T. W., & Bober, E. (2008) · Circulation Research · doi:10.1161/circresaha.107.164558 · Cited by 646
Moynihan, K. A., Grimm, A. A., Plueger, M. M., Bernal‐Mizrachi, E., Ford, E. L., CRAS-MÉNEUR, C. M. H., Permutt, M. A., & Imai, S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.07.001 · Cited by 638
Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription
Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L. (2006) · Genes & Development · doi:10.1101/gad.1399706 · Cited by 629
Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila
Burnett, C., Valentini, S., Cabreiro, F., Goss, M., Somogyvári, M., Piper, M. D., Hoddinott, M., Sutphin, G. L., Leko, V., McElwee, J. J., et al. (2011) · Nature · doi:10.1038/nature10296 · Cited by 624
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
Rane, S., He, M., Sayed, D. H., Vashistha, H., Malhotra, A., Sadoshima, J., Vatner, D. E., Vatner, S. F., & Abdellatif, M. (2009) · Circulation Research · doi:10.1161/circresaha.108.193102 · Cited by 588
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
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
FOXO4 Is Acetylated upon Peroxide Stress and Deacetylated by the Longevity Protein hSir2
van der Horst, A., Tertoolen, L. G. J., Smits, L. M. M., Frye, R. A., Medema, R. H., & Burgering, B. M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401138200 · Cited by 553
Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase
Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548
Frescas, D., Valenti, L. V. C., & Accili, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412357200 · Cited by 541
Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C. F. W., & Steegborn, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.048 · Cited by 531
DBC1 is a negative regulator of SIRT1
Kim, J., Chen, J., & Lou, Z. (2008) · Nature · doi:10.1038/nature06500 · Cited by 513
(2010) · doi:10.1016/j.cmet.2010.06.009 · Cited by 512
Guarente, L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1100831 · Cited by 510
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
Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle
Palacios, O. M., Carmona, J. J., Michan, S., Chen, K. Y., Manabe, Y., III, J. L. W., Goodyear, L. J., & Tong, Q. (2009) · Aging · doi:10.18632/aging.100075 · Cited by 487
A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange
Liu, Y., Dentin, R., Chen, D., Hedrick, S., Ravnskjaer, K., Schenk, S., Milne, J., Meyers, D. J., Cole, P., III, J. Y., et al. (2008) · Nature · doi:10.1038/nature07349 · Cited by 484
Shimazu, T., Hirschey, M. D., Hua, L., Dittenhafer-Reed, K. E., Schwer, B., Lombard, D. B., Li, Y., Bunkenborg, J., Alt, F. W., Denu, J. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.003 · Cited by 484
Negative regulation of the deacetylase SIRT1 by DBC1
Zhao, W., Kruse, J.-P., Tang, Y., Jung, S. Y., Qin, J., & Gu, W. J. (2008) · Nature · doi:10.1038/nature06515 · Cited by 475
Jing, E., Emanuelli, B., Hirschey, M. D., Boucher, J., Lee, K. Y., Lombard, D., Verdin, E. M., & Kahn, C. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111308108 · Cited by 469
Fasting-dependent glucose and lipid metabolic response through hepatic sirtuin 1
Rodgers, J. T., & Puigserver, P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702509104 · Cited by 466
Inhibition of mitochondrial proton F0F1‐ATPase/ATP synthase by polyphenolic phytochemicals
Zheng, J., & Ramirez, V. D. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703397 · Cited by 453
Effects of resveratrol on lifespan in Drosophila melanogaster and Caenorhabditis elegans
Bass, T. M., Weinkove, D., Houthoofd, K., Gems, D., & Partridge, L. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.07.007 · Cited by 447
Lerin, C., Rodgers, J. T., Kalume, D. E., Kim, S.-H., Pandey, A., & Puigserver, P. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.013 · Cited by 443
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
Self-citationGenetic control of de novo lipogenesis: role in diet-induced obesity
Strable, M. S., & Ntambi, J. M. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003667500 · Cited by 428
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
Resveratrol is not a direct activator of SIRT1 enzyme activity
Beher, D., Wu, J., Cumine, S., Kim, K. W., Lu, S., Atangan, L., & Wang, M. (2009) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2009.00901.x · Cited by 426
Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K., & Zhao, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.028 · Cited by 424
Regulation of Insulin Secretion by SIRT4, a Mitochondrial ADP-ribosyltransferase
Ahuja, N., Schwer, B., Carobbio, S., Waltregny, D., North, B. J., Castronovo, V., Maechler, P., & Verdin, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705488200 · Cited by 422
AMP-activated protein kinase and its downstream transcriptional pathways
Cantó, C., & Auwerx, J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0454-z · Cited by 421
Self-citationActive Regulator of SIRT1 Cooperates with SIRT1 and Facilitates Suppression of p53 Activity
Kim, E.-J., Kho, J.-H., Kang, M., & Um, S. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.030 · Cited by 400
Metabolomic Analysis of Livers and Serum from High-Fat Diet Induced Obese Mice
Kim, H.-J., Kim, J. H., Noh, S., Hur, H. J., Sung, M. J., Hwang, J.-T., Park, J. H., Yang, H. J., Kim, M.-S., Kwon, D. Y., et al. (2011) · Journal of Proteome Research · doi:10.1021/pr100892r · Cited by 376
Braunstein, M., Sobel, R. E., Allis, C. D., Turner, B. M., & Broach, J. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4349 · Cited by 373
Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity
Finley, L. W. S., Haas, W., Desquiret‐Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., & Haigis, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023295 · Cited by 364
The Cellular Fate of Glucose and Its Relevance in Type 2 Diabetes
Bouché, C., Serdy, S., Kahn, C. R., & Goldfine, A. B. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0026 · Cited by 361
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
SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
Yang, Y., Fu, W., Chen, J., Olashaw, N., Zhang, X. M., Nicosia, S. V., Bhalla, K. N., & Bai, W. (2007) · Nature Cell Biology · doi:10.1038/ncb1645 · Cited by 339
SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neurons
Li, Y., Xu, W., McBurney, M. W., & Longo, V. D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.05.004 · Cited by 331
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
The secretory function of adipocytes in the physiology of white adipose tissue
Wang, P., Mariman, E., Renes, J., & Keijer, J. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21386 · Cited by 318
Wang, R.-H., Kim, H., Xiao, C., Xu, X., Gavrilova, O., & Deng, C. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46243 · Cited by 315
Resveratrol alleviates alcoholic fatty liver in mice
Ajmo, J. M., Liang, X., Rogers, C. Q., Pennock, B., & You, M. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90358.2008 · Cited by 314
SRT1720 improves survival and healthspan of obese mice
Minor, R. K., Baur, J. A., Gomes, A. P., Ward, T. M., Csiszár, A., Mercken, E. M., Abdelmohsen, K., Shin, Y., Cantó, C., Scheibye‐Knudsen, M., et al. (2011) · Scientific Reports · doi:10.1038/srep00070 · Cited by 306
Self-citationLi, Y., Xu, S., Giles, A. J., Nakamura, K., Lee, J. W., Hou, X., Dönmez, G., Li, J., Luo, Z., Walsh, K. X., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-173492 · Cited by 305
Regulatory enzymes of mitochondrial β‐oxidation as targets for treatment of the metabolic syndrome
Schreurs, M., Kuipers, F., & van der Leij, F. R. (2009) · Obesity Reviews · doi:10.1111/j.1467-789x.2009.00642.x · Cited by 304
Splicing regulates NAD metabolite binding to histone macroH2A
Kustatscher, G., Hothorn, M., Pugieux, C., Scheffzek, K., & Ladurner, A. G. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb956 · Cited by 300
Sirtuin 1 in lipid metabolism and obesity
Schug, T. T., & Li, X. (2011) · Annals of Medicine · doi:10.3109/07853890.2010.547211 · Cited by 295
Wang, F., & Tong, Q. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-06-0647 · Cited by 289
Phosphorylation Regulates SIRT1 Function
Sasaki, T., Maier, B., Koclega, K. D., Chruszcz, M., Gluba, W., Stukenberg, P. T., Minor, W., & Scrable, H. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0004020 · Cited by 285
JNK1 Phosphorylates SIRT1 and Promotes Its Enzymatic Activity
Nasrin, N., Kaushik, V. K., Fortier, E., Wall, D., Pearson, K. J., de Cabo, R., & Bordone, L. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008414 · Cited by 271
Lee, J., Padhye, A., Sharma, A., Song, G., Miao, J., Mo, Y.-Y., Wang, L., & Kemper, J. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.094524 · Cited by 269
NCoR1 Is a Conserved Physiological Modulator of Muscle Mass and Oxidative Function
Yamamoto, H., Williams, E. G., Mouchiroud, L., Cantó, C., Fan, W., Downes, M., Héligon, C., Barish, G. D., Desvergne, B., Evans, R. M., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.017 · Cited by 269
Self-citationSIRT1: recent lessons from mouse models
Herranz, D., & Serrano, M. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2962 · Cited by 261
PARP-2 Regulates SIRT1 Expression and Whole-Body Energy Expenditure
Bai, P., Cantó, C., Brunyánszki, A., Huber, A., Szántó, M., Cen, Y., Yamamoto, H., Houten, S. M., Kiss, B., Oudart, H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.013 · Cited by 260
Self-citationLiou, G., Tanny, J. C., Kruger, R. G., Walz, T., & Moazed, D. (2005) · Cell · doi:10.1016/j.cell.2005.03.035 · Cited by 260
Barbosa, M. T., Soares, S. M., Novak, C. M., Sinclair, D. A., Levine, J. A., Aksoy, P., & Chini, E. N. (2007) · The FASEB Journal · doi:10.1096/fj.07-8290com · Cited by 252
DYRK1A and DYRK3 Promote Cell Survival through Phosphorylation and Activation of SIRT1
Guo, X., Williams, J. G., Schug, T. T., & Li, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102574 · Cited by 251
Huang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231
PPARγ in human and mouse physiology
Heikkinen, S., Auwerx, J. H., & Argmann, C. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.03.006 · Cited by 224
Self-citationXu, F. L., Gao, Z., Zhang, J., Rivera, C. A., Yin, J., Weng, J., & Ye, J. (2010) · Endocrinology · doi:10.1210/en.2009-1013 · Cited by 221
A SIRT1-LSD1 Corepressor Complex Regulates Notch Target Gene Expression and Development
Mulligan, P., Yang, F., Stefano, L. D., Ji, J., Ouyang, J., Nishikawa, J. L., Toiber, D., Kulkarni, M., Wang, Q., Najafi-Shoushtari, S. H., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.04.020 · Cited by 221
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
Metabolic networks of longevity
Houtkooper, R. H., Williams, R. W., & Auwerx, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.029 · Cited by 217
Self-citationGiralt, A., Hondares, E., Villena, J. A., Ribas, F., Díaz-Delfín, J., Giralt, M., Iglesias, R., & Villarroya, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202390 · Cited by 210
Transcriptional targets of sirtuins in the coordination of mammalian physiology
Feige, J. N., & Auwerx, J. H. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.012 · Cited by 209
Self-citationCoste, A., Louet, J.-F., Lagouge, M., Lerin, C., Antal, M. C., Meziane, H., Schoonjans, K., Puigserver, P., O'Malley, B. W., & Auwerx, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808207105 · Cited by 205
Self-citationSirt1 enhances skeletal muscle insulin sensitivity in mice during caloric restriction
Schenk, S., McCurdy, C. E., Philp, A., Chen, M. Z., Holliday, M. J., Bandyopadhyay, G. K., Osborn, O., Baar, K., & Olefsky, J. M. (2011) · Journal of Clinical Investigation · doi:10.1172/jci58554 · Cited by 197
Escande, C., Chini, C. C. S., Nin, V., Dykhouse, K. M., Novak, C. M., Levine, J. A., van Deursen, J., Gores, G. J., Chen, J., Lou, Z., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci39319 · Cited by 190
Philp, A., Chen, A., Lan, D., Meyer, G. A., Murphy, A. N., Knapp, A. E., Olfert, I. M., McCurdy, C. E., Marcotte, G. R., Hogan, M. C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.261685 · Cited by 184
Neural sirtuin 6 (Sirt6) ablation attenuates somatic growth and causes obesity
Schwer, B., Schumacher, B., Lombard, D. B., Xiao, C., Kurtev, M. V., Gao, J., Schneider, J. I., Chai, H., Bronson, R. T., Tsai, L., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016306107 · Cited by 179
Beirowski, B., Gustin, J. A., Armour, S. M., Yamamoto, H., Viader, A., North, B. J., Michán, S., Baloh, R. H., Golden, J. P., Schmidt, R. E., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104969108 · Cited by 175
Self-citationCREB and ChREBP oppositely regulate SIRT1 expression in response to energy availability
Noriega, L. G., Feige, J. N., Cantó, C., Yamamoto, H., Yu, J., Herman, M. A., Mataki, C., Kahn, B. B., & Auwerx, J. H. (2011) · EMBO Reports · doi:10.1038/embor.2011.151 · Cited by 172
Self-citationRegulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes
Viswanathan, M., & Guarente, L. (2011) · Nature · doi:10.1038/nature10440 · Cited by 166
Hayashida, S., Arimoto, A., Kuramoto, Y., Kozako, T., Honda, S., Shimeno, H., & Soeda, S. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0391-z · Cited by 139
Yamazaki, Y., Usui, I., Kanatani, Y., Matsuya, Y., Tsuneyama, K., Fujisaka, S., Bukhari, A., Suzuki, H., Senda, S., Imanishi, S., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90997.2008 · Cited by 137
Wang, R., Li, C., & Deng, C. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.682 · Cited by 123
Function and metabolism of sirtuin metabolite O-acetyl-ADP-ribose
Tong, L., & Denu, J. M. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.02.007 · Cited by 122
Sir2 and calorie restriction in yeast: A skeptical perspective
Kaeberlein, M. R., & Powers, R. W. (2007) · Ageing Research Reviews · doi:10.1016/j.arr.2007.04.001 · Cited by 109
SIRT1 mRNA expression may be associated with energy expenditure and insulin sensitivity
Rutanen, J., Yaluri, N., Modi, S., Pihlajamäki, J., Vänttinen, M., Itkonen, P., Kainulainen, S., Yamamoto, H., Lagouge, M., Sinclair, D. A., et al. (2010) · Diabetes · doi:10.2337/db09-1191 · Cited by 104
Self-citationThe Management of Nicotinamide and Nicotinic Acid in the Mouse
Collins, P. B., & Chaykin, S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45675-5 · Cited by 102
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
Fine Tuning Our Cellular Factories: Sirtuins in Mitochondrial Biology
Zhong, L., & Mostoslavsky, R. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.05.004 · Cited by 90
Sirtuin 1 (SIRT1) sequence variation is not associated with exceptional human longevity
Flachsbart, F., CROUCHER, P., Nikolaus, S., Hampe, J., CORDES, C., SCHREIBER, S., & Nebel, A. (2005) · Experimental Gerontology · doi:10.1016/j.exger.2005.09.008 · Cited by 80
Bastin, J., Costa, A. L., & Djouadi, F. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr089 · Cited by 76
Herzog, B., Hall, R. K., Wang, X. L., Waltner-Law, M. E., & Granner, D. K. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0384 · Cited by 46
Gonzalez, A. A., Kumar, R., Mulligan, J. D., Davis, A. J., & Saupe, K. W. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00409.2004 · Cited by 43
Design, synthesis and biological characterization of novel inhibitors of CD38
Dong, M., Si, Y.-Q., Sun, S.-Y., Pu, X., Yang, Z.-J., Zhang, L., Zhang, L., Leung, F. P., Lam, C. M. C., Kwong, A. K., et al. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c0ob00768d · Cited by 37
James, A. N. (2011) · Nature · doi:10.1038/nj7364-1 · Cited by 9
Flagged first, then by citations
Cited by
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
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648
Self-citationMitochondrial Dynamics Controls T Cell Fate through Metabolic Programming
Buck, M. D., O’Sullivan, D., Geltink, R. I. K., Curtis, J. D., Chang, C., Sanin, D. E., Qiu, J., Kretz, O., Braas, D., van der Windt, G. J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.035 · Cited by 1,491
Acetyl coenzyme A: a central metabolite and second messenger
Pietrocola, F., Galluzzi, L., Bravo-San Pedro, J. M., Madeo, F., & Kroemer, G. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.014 · Cited by 1,378
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324
Metadata
- Authors
- Houtkooper, R. H., Pirinen, E., & Auwerx, J.
- Affiliations
- École Polytechnique Fédérale de Lausanne (CH)
- University of Eastern Finland (FI)
- Corresponding author
- Auwerx, Johan
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2012-03-07
- Volume
- 13
- Issue
- 4
- Pages
- 225-238
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC4872805
- OpenAlex
- W2028178274
- Cited by
- 2,008
- References
- 160
- Citations by year
- 2026: 109 · 2025: 114 · 2024: 137 · 2023: 147 · 2022: 132 · 2021: 159 · 2020: 169 · 2019: 140 · 2018: 175 · 2017: 145 · 2016: 122 · 2015: 144 · 2014: 126 · 2013: 131 · 2012: 57
- FWCI
- 12.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion)
- PubMed Central (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (125487, 124713)
- 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
- sirtuins, histone deacetylation, energy homeostasis, glucose metabolism, lipid metabolism, healthspan, aging, transcriptional regulation
- MeSH terms
- Resveratrol, Insulin Secretion, Aging, Animals, Energy Metabolism, Multigene Family, Glucose, Histones, Homeostasis, Humans, Insulin, Longevity, NAD, Phylogeny, Protein Processing, Post-Translational, Stilbenes, Sirtuins, Lipid Metabolism
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
