Protein deacetylation by sirtuins: delineating a post-translational regulatory program responsive to nutrient and redox stressors

AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity

Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239 · see citing works

Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1

Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160 · see citing works

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 · see citing works

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 2,653 · see citing works

Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ

Picard, F., Kurtev, M. V., Chung, N., Topark‐Ngarm, A., Senawong, T., de Oliveira, R. M., Leid, M. E., McBurney, M. W., & Guarente, L. (2004) · Nature · doi:10.1038/nature02583 · Cited by 1,943 · see citing works

Requirement of NAD and <i>SIR2</i> for Life-Span Extension by Calorie Restriction in <i>Saccharomyces cerevisiae</i>

Lin, S.-J., Defossez, P.-A., & Guarente, L. (2000) · Science · doi:10.1126/science.289.5487.2126 · Cited by 1,775 · see citing works

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487 · see citing works

The Sir2 Family of Protein Deacetylases

Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,480 · see citing works

The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control

Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427 · see citing works

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 · see citing works

SIRT1 regulates circadian clock gene expression through PER2 deacetylation

Asher, G., Gatfield, D., Stratmann, M., Reinke, H., Dibner, C., Kreppel, F., Mostoslavsky, R., Alt, F. W., & Schibler, U. (2008) · Cell · doi:10.1016/j.cell.2008.06.050 · Cited by 1,376 · see citing works

Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins

Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0033 · Cited by 1,364 · see citing works

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 1,344 · see citing works

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 · see citing works

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 · see citing works

Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation

Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works

Circadian Control of the NAD ⁺ Salvage Pathway by CLOCK-SIRT1

Nakahata, Y., Sahar, S., Astarita, G., Kaluzova, M., & Sassone-Corsi, P. (2009) · Science · doi:10.1126/science.1170803 · Cited by 1,198 · see citing works

SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

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 · see citing works

Sirt1 Regulates Aging and Resistance to Oxidative Stress in the Heart

Alcendor, R. R., Gao, S., Zhai, P., Zablocki, D., Holle, E., Yu, X., Tian, B., Wagner, T., Vatner, S. F., & Sadoshima, J. (2007) · Circulation Research · doi:10.1161/01.res.0000267723.65696.4a · Cited by 1,147 · see citing works

Circadian Clock Feedback Cycle Through NAMPT-Mediated NAD ⁺ Biosynthesis

Ramsey, K. M., Yoshino, J., Brace, C. S., Abrassart, D., Kobayashi, Y., Marcheva, B., Hong, H.-K., Chong, J. L., Buhr, E. D., Lee, C., et al. (2009) · Science · doi:10.1126/science.1171641 · Cited by 1,126 · see citing works

Hepatocyte-Specific Deletion of SIRT1 Alters Fatty Acid Metabolism and Results in Hepatic Steatosis and Inflammation

Purushotham, A., Schug, T. T., Xu, Q., Surapureddi, S., Guo, X., & Li, X. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.02.006 · Cited by 1,112 · see citing works

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 · see citing works

Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice

Cheng, H.-L., Mostoslavsky, R., Saito, S., Manis, J. P., Gu, Y., Patel, P., Bronson, R., Appella, E., Alt, F. W., & Chua, K. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934713100 · Cited by 1,095 · see citing works

SIRT6 Links Histone H3 Lysine 9 Deacetylation to NF-κB-Dependent Gene Expression and Organismal Life Span

Kawahara, T. L. A., Michishita, E., Adler, A. S., Damian, M., Berber, E., Lin, M., McCord, R. A., Ongaigui, K. C. L., Boxer, L. D., Chang, H. Y., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.052 · Cited by 1,090 · see citing works

SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis

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 · see citing works

Sirtuin 2 Inhibitors Rescue α-Synuclein-Mediated Toxicity in Models of Parkinson's Disease

Outeiro, T. F., Kontopoulos, E., Altmann, S. M., Kufareva, I., Strathearn, K. E., Amore, A. M., Volk, C. B., Maxwell, M. M., Rochet, J., McLean, P. J., et al. (2007) · Science · doi:10.1126/science.1143780 · Cited by 1,066 · see citing works

SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α

Nemoto, S., Fergusson, M. M., & Finkel, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501485200 · Cited by 1,047 · see citing works

The NAD Biosynthesis Pathway Mediated by Nicotinamide Phosphoribosyltransferase Regulates Sir2 Activity in Mammalian Cells

Revollo, J. R., Grimm, A. A., & Imai, S.-I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408388200 · Cited by 1,010 · see citing works

Inhibition of Silencing and Accelerated Aging by Nicotinamide, a Putative Negative Regulator of Yeast Sir2 and Human SIRT1

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 · see citing works

The Histone Deacetylase Sirt6 Regulates Glucose Homeostasis via Hif1α

Zhong, L., D'Urso, A., Toiber, D., Sebastian, C., Henry, R. E., Vadysirisack, D. D., Guimaraes, A., Marinelli, B., Wikstrom, J. D., Nir, T., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.041 · Cited by 1,001 · see citing works

Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice

Sundaresan, N. R., Gupta, M., Gene, K., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 996 · see citing works

Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival

Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950 · see citing works

Sirt1 protects against high-fat diet-induced metabolic damage

Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschöp, M. H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802917105 · Cited by 928 · see citing works

SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1

Pacholec, M., Bleasdale, J. E., Chrunyk, B., Cunningham, D., Flynn, D., Garofalo, R. S., Griffith, D., Griffor, M., Loulakis, P., Pabst, B., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088682 · Cited by 915 · see citing works

SIRT1 Promotes Endothelium-Dependent Vascular Relaxation by Activating Endothelial Nitric Oxide Synthase

Mattagajasingh, I., Kim, C.-S., Naqvi, A., Yamamori, T., Hoffman, T. A., Jung, S.-B., DeRicco, J., Kasuno, K., & Irani, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704329104 · Cited by 881 · see citing works

SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging

Oberdoerffer, P., Michan, S., McVay, M., Mostoslavsky, R., Vann, J., Park, S.-K., Hartlerode, A., Stegmuller, J., Hafner, A., Loerch, P., et al. (2008) · Cell · doi:10.1016/j.cell.2008.10.025 · Cited by 852 · see citing works

SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1

Lan, F., Cacicedo, J. M., Ruderman, N., & Ido, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805711200 · Cited by 825 · see citing works

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 · see citing works

SIRT5 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 · see citing works

SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress

Kim, H.-S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., van der Meer, R., Nguyen, P., Savage, J., Owens, K. M., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.023 · Cited by 785 · see citing works

SIRT1 Regulates Hepatocyte Lipid Metabolism through Activating AMP-activated Protein Kinase

Hou, X., Xu, S., Maitland-Toolan, K. A., Sato, K., Jiang, B., Ido, Y., Lan, F., Walsh, K., Wierzbicki, M., Verbeuren, T. J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802187200 · Cited by 778 · see citing works

Impaired DNA Damage Response, Genome Instability, and Tumorigenesis in SIRT1 Mutant Mice

Wang, R.-H., Sengupta, K., Li, C., Kim, H., Cao, L., Xiao, C., Kim, S., Xu, X., Yin, Z., Chilton, B. S., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.09.001 · Cited by 769 · see citing works

SIRT1 Improves Insulin Sensitivity under Insulin-Resistant Conditions by Repressing PTP1B

Sun, C., Zhang, F., Ge, X., Yan, T., Chen, X., Shi, X., & Zhai, Q. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.014 · Cited by 766 · see citing works

Substrate-specific activation of sirtuins by resveratrol

Kaeberlein, M., McDonagh, T., Heltweg, B., Hixon, J., Westman, E. A., Caldwell, S. D., Napper, A., Curtis, R., DiStefano, P. S., Fields, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500655200 · Cited by 745 · see citing works

SIRT1 Protects against Microglia-dependent Amyloid-β Toxicity through Inhibiting NF-κB Signaling

Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L.-F., Kwon, H., Yi, S., Mucke, L., & Gan, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509329200 · Cited by 740 · see citing works

SIRT1 transgenic mice show phenotypes resembling calorie restriction

Bordone, L., Cohen, D., Robinson, A., Motta, M. C., Van Veen, E., Czopik, A., Steele, A. D., Crowe, H., Marmor, S., Luo, J., et al. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00335.x · Cited by 722 · see citing works

Specific SIRT1 Activation Mimics Low Energy Levels and Protects against Diet-Induced Metabolic Disorders by Enhancing Fat Oxidation

Feige, J. N., Lagouge, M., Canto, C., Strehle, A., Houten, S. M., Milne, J. C., Lambert, P. D., Mataki, C., Elliott, P. J., & Auwerx, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.017 · Cited by 719 · see citing works

Sirt1 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 · see citing works

SIRT3, a Mitochondrial Sirtuin Deacetylase, Regulates Mitochondrial Function and Thermogenesis in Brown Adipocytes

Shi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works

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 · see citing works

SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction

Wang, F., Nguyen, M., Qin, F. X.-F., & Tong, Q. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00304.x · Cited by 652 · see citing works

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 649 · see citing works

Sirt7 Increases Stress Resistance of Cardiomyocytes and Prevents Apoptosis and Inflammatory Cardiomyopathy in Mice

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 639 · see citing works

SirT1 Gain of Function Increases Energy Efficiency and Prevents Diabetes in Mice

Banks, A. S., Kon, N., Knight, C. M., Matsumoto, M., Juárez, R. G., Rossetti, L., Gu, W. J., & Accili, D. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.014 · Cited by 636 · see citing works

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 631 · see citing works

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 &amp; Development · doi:10.1101/gad.1399706 · Cited by 629 · see citing works

Neuronal SIRT1 Activation as a Novel Mechanism Underlying the Prevention of Alzheimer Disease Amyloid Neuropathology by Calorie Restriction

Qin, W., Yang, T., Ho, L., Zhao, Z., Wang, J., Chen, L., Zhao, W., Thiyagarajan, M., MacGrogan, D., Rodgers, J. T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602909200 · Cited by 626 · see citing works

SIRT1 Controls Endothelial Angiogenic Functions During Vascular Growth

Potente, M., Ghaeni, L., Baldessari, D., Mostoslavsky, R., Rossig, L., Dequiedt, F., Haendeler, J., Mione, M., Dejana, E., Alt, F. W., et al. (2007) · Genes &amp; Development · doi:10.1101/gad.435107 · Cited by 608 · see citing works

The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide–dependent deacetylase

Schwer, B., North, B. J., Frye, R. A., Ott, M., & Verdin, E. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205057 · Cited by 599 · see citing works

The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth.

Firestein, R., Blander, G., Michan, S., Oberdoerffer, P., Ogino, S., Campbell, J., Bhimavarapu, A., Luikenhuis, S., de Cabo, R., Fuchs, C., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002020 · Cited by 588 · see citing works

Endurance Exercise as a Countermeasure for Aging

Lanza, I. R., Short, D. K., Short, K. R., Raghavakaimal, S., Basu, R., Joyner, M. J., McConnell, J. P., & Nair, K. S. (2008) · Diabetes · doi:10.2337/db08-0349 · Cited by 582 · see citing works

Downregulation of MiR-199a Derepresses Hypoxia-Inducible Factor-1α and Sirtuin 1 and Recapitulates Hypoxia Preconditioning in Cardiac Myocytes

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 578 · see citing works

Acetylation of the C Terminus of Ku70 by CBP and PCAF Controls Bax-Mediated Apoptosis

Cohen, H. Y., Lavu, S., Bitterman, K. J., Hekking, B., Imahiyerobo, T. A., Miller, C. M., Frye, R. A., Ploegh, H. L., Kessler, B. M., & Sinclair, D. A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00094-2 · Cited by 574 · see citing works

SIRT3, a human SIR2 homologue, is an NAD- dependent deacetylase localized to mitochondria

Onyango, P. O., Celic, I., McCaffery, J. M., Boeke, J. D., & Feinberg, A. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222538099 · Cited by 573 · see citing works

Sirtuins: Sir2-related NAD-dependent protein deacetylases.

North, B. J., & Verdin, E. M. (2004) · Genome biology · doi:10.1186/gb-2004-5-5-224 · Cited by 568 · see citing works

A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange

Liu, Y., Dentin, R., Chen, D., Hedrick, S. A., Ravnskjær, K., Schenk, S., Milne, J. C., Meyers, D. J., Cole, P., Yates, J. R., et al. (2008) · Nature · doi:10.1038/nature07349 · Cited by 556 · see citing works

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 549 · see citing works

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 · see citing works

SIRT3 Is a Stress-Responsive Deacetylase in Cardiomyocytes That Protects Cells from Stress-Mediated Cell Death by Deacetylation of Ku70

Sundaresan, N. R., Samant, S. A., Pillai, V. B., Rajamohan, S. B., & Gupta, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00426-08 · Cited by 542 · see citing works

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 541 · see citing works

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 · see citing works

Phosphorylation of HuR by Chk2 Regulates SIRT1 Expression

Abdelmohsen, K., Pullmann, R., Lal, A., Kim, H. H., Galbán, S., Yang, X., Blethrow, J. D., Walker, M., Shubert, J., Gillespie, D. A., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.011 · Cited by 527 · see citing works

Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms

Berger, F., Lau, C., Dahlmann, M., & Ziegler, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508660200 · Cited by 508 · see citing works

DBC1 is a negative regulator of SIRT1

Kim, J., Chen, J., & Lou, Z. (2008) · Nature · doi:10.1038/nature06500 · Cited by 503 · see citing works

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 490 · see citing works

Disruption of the Ang II type 1 receptor promotes longevity in mice

Benigni, A., Corna, D., Zoja, C., Sonzogni, A., Latini, R., Salio, M., Conti, S., Rottoli, D., Longaretti, L., Cassis, P., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci36703 · Cited by 486 · see citing works

Regulation of Succinate Dehydrogenase Activity by SIRT3 in Mammalian Mitochondria

Çimen, H., Han, M., Yang, Y., Tong, Q., Koc, H., & Koc, E. C. (2009) · Biochemistry · doi:10.1021/bi901627u · Cited by 478 · see citing works

SirT3 is a nuclear NAD + -dependent histone deacetylase that translocates to the mitochondria upon cellular stressPreprint

Scher, M. B., Vaquero, A., & Reinberg, D. (2007) · Genes & Development · doi:10.1101/gad.1527307 · Cited by 476 · see citing works

Regulation of Hypoxia-Inducible Factor 2α Signaling by the Stress-Responsive Deacetylase Sirtuin 1

Dioum, E. M., Chen, R., Alexander, M. S., Zhang, Q., Hogg, R. T., Gerard, R. D., & Garcia, J. A. (2009) · Science · doi:10.1126/science.1169956 · Cited by 470 · see citing works

Sirtuin 1 Reduction Parallels the Accumulation of Tau in Alzheimer Disease

Julien, C., Tremblay, C., Émond, V., Lebbadi, M., Salem, N., Bennett, D. A., & Calon, F. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181922348 · Cited by 467 · see citing works

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 464 · see citing works

Sirt1 contributes critically to the redox-dependent fate of neural progenitors

Prozorovski, T., Schulze-Topphoff, U., Glumm, R., Baumgart, J., Schröter, F., Ninnemann, O., Siegert, E., Bendix, I., Brüstle, O., Nitsch, R., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1700 · Cited by 451 · see citing works

Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage

Wang, C., Chen, L., Hou, X., Li, Z., Kabra, N., Ma, Y., Nemoto, S., Finkel, T., Gu, W. J., Cress, W. D., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1468 · Cited by 447 · see citing works

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 · see citing works

Genetics and the Specificity of the Aging Process

Hekimi, S., & Guarente, L. (2003) · Science · doi:10.1126/science.1082358 · Cited by 434 · see citing works

SIRT1 Is Significantly Elevated in Mouse and Human Prostate Cancer

Huffman, D. M., Grizzle, W. E., Bamman, M. M., Kim, J.-S., Eltoum, I. A., Elgavish, A., & Nagy, T. R. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0085 · Cited by 428 · see citing works

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 &amp; Drug Design · doi:10.1111/j.1747-0285.2009.00901.x · Cited by 426 · see citing works

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 · see citing works

SIRT1 inhibits inflammatory pathways in macrophages and modulates insulin sensitivity

Yoshizaki, T., Schenk, S., Imamura, T., Babendure, J. L., Sonoda, N., Bae, E. J., Oh, D. Y., Lu, M. M., Milne, J. C., Westphal, C. H., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00417.2009 · Cited by 420 · see citing works

Conserved Metabolic Regulatory Functions of Sirtuins

Schwer, B., & Verdin, E. M. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.006 · Cited by 416 · see citing works

SIRT1 Exerts Anti-Inflammatory Effects and Improves Insulin Sensitivity in Adipocytes

Yoshizaki, T., Milne, J. C., Imamura, T., Schenk, S., Sonoda, N., Babendure, J. L., Lu, J.-C., Smith, J. J., Jirousek, M. R., & Olefsky, J. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00705-08 · Cited by 416 · see citing works

Epigenetic control of rDNA loci in response to intracellular energy status

Murayama, A., Ohmori, K., Fujimura, A., Minami, H., Yasuzawa-Tanaka, K., Kuroda, T., Oie, S., Daitoku, H., Okuwaki, M., Nagata, K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.03.030 · Cited by 394 · see citing works

Active 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 389 · see citing works

Endothelium-specific overexpression of class III deacetylase SIRT1 decreases atherosclerosis in apolipoprotein E-deficient mice

Zhang, Q., Wang, Z., Chen, H., Zhou, S., Zheng, W., Liu, G., Wei, Y.-S., Cai, H. “., Liu, D., & Liang, C. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn224 · Cited by 388 · see citing works

A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages

Bellizzi, D., Rose, G., Cavalcante, P., Covello, G., Dato, S., De Rango, F., Greco, V., Maggiolini, M., Feraco, E., Mari, V., et al. (2005) · Genomics · doi:10.1016/j.ygeno.2004.11.003 · Cited by 367 · see citing works

Interplay among BRCA1, SIRT1, and Survivin during BRCA1-Associated Tumorigenesis

Wang, R.-H., Yin, Z., Kim, H., Xu, X., Cao, L., Lahusen, T. J., Lee, M., Xiao, C., Vassilopoulos, A., Chen, W., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.09.011 · Cited by 361 · see citing works

The interaction between FOXO and SIRT1: tipping the balance towards survival

Giannakou, M. E., & Partridge, L. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.07.006 · Cited by 354 · see citing works

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 343 · see citing works

Abnormal Angiogenesis in Foxo1 (Fkhr)-deficient Mice

Furuyama, T., Kitayama, K., Shimoda, Y., Ogawa, M., Sone, K., Yoshida-Araki, K., Hisatsune, H., Nishikawa, S.-I., Nakayama, K., Nakayama, K., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314214200 · Cited by 336 · see citing works

FXR Acetylation Is Normally Dynamically Regulated by p300 and SIRT1 but Constitutively Elevated in Metabolic Disease States

Kemper, J. K., Xiao, Z., Ponugoti, B., Miao, J., Fang, S., Kanamaluru, D., Tsang, S., Wu, S.-Y., Chiang, C.-M., & Veenstra, T. D. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.09.009 · Cited by 332 · see citing works

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 · see citing works

STAT3 inhibition of gluconeogenesis is downregulated by SirT1

Nie, Y., Erion, D. M., Yuan, Z., Dietrich, M. O., Shulman, G. I., Horváth, T. L., & Gao, Q. (2009) · Nature Cell Biology · doi:10.1038/ncb1857 · Cited by 331 · see citing works

Angiopoietin-1 modulates endothelial cell function and gene expression via the transcription factor FKHR (FOXO1)Preprint

Daly, C., Wong, V., Burova, E., Wei, Y., Zabski, S. M., Griffiths, J., Lai, K. V., Lin, H. C., Ioffe, E., Yancopoulos, G. D., et al. (2004) · Genes & Development · doi:10.1101/gad.1189704 · Cited by 326 · see citing works

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 324 · see citing works

SIRT6 protects against pathological damage caused by diet‐induced obesity

Kanfi, Y., Peshti, V., Gil, R., Naiman, S., Nahum, L., Levin, E., Kronfeld‐Schor, N., & Cohen, H. Y. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2009.00544.x · Cited by 311 · see citing works

The regulation of nicotinamide adenine dinucleotide biosynthesis by Nampt/PBEF/visfatin in mammals

Revollo, J. R., Grimm, A. A., & Imai, S. (2007) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32801b3c8f · Cited by 310 · see citing works

Silent Information Regulator 2α, a Longevity Factor and Class III Histone Deacetylase, Is an Essential Endogenous Apoptosis Inhibitor in Cardiac Myocytes

Alcendor, R. R., Kirshenbaum, L. A., Imai, S., Vatner, S. F., & Sadoshima, J. (2004) · Circulation Research · doi:10.1161/01.res.0000147557.75257.ff · Cited by 302 · see citing works

Acetylation of MEK2 and IκB kinase (IKK) activation loop residues by YopJ inhibits signaling

Mittal, R., Peak‐Chew, S., & McMahon, H. T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608995103 · Cited by 299 · see citing works

Manipulation of a Nuclear NAD+ Salvage Pathway Delays Aging without Altering Steady-state NAD+ Levels

Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., Cohen, H. Y., Lin, S., Manchester, J. K., Gordon, J. I., & Sinclair, D. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111773200 · Cited by 295 · see citing works

SIRT2 Suppresses Adipocyte Differentiation by Deacetylating FOXO1 and Enhancing FOXO1's Repressive Interaction with PPARγ

Wang, F., & Tong, Q. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-06-0647 · Cited by 289 · see citing works

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 · see citing works

Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly

Rose, G., Dato, S., Altomare, K., Bellizzi, D., Garasto, S., Greco, V, Passarino, G., Feraco, E., Mari, V, Barbi, C., et al. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(03)00209-2 · Cited by 282 · see citing works

SIRT3 interacts with the daf-16 homolog FOXO3a in the Mitochondria, as well as increases FOXO3a Dependent Gene expression

Jacobs, K. M., Pennington, J. D., Bisht, K. S., Aykin‐Burns, N., Kim, H., Mishra, M. V., Sun, L., Nguyen, P., Ahn, B., Leclerc, J., et al. (2008) · International Journal of Biological Sciences · doi:10.7150/ijbs.4.291 · Cited by 281 · see citing works

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 271 · see citing works

Sirtuin 2, a Mammalian Homolog of Yeast Silent Information Regulator-2 Longevity Regulator, Is an Oligodendroglial Protein That Decelerates Cell Differentiation through Deacetylating α-Tubulin

Li, W., Zhang, B., Tang, J., Cao, Q., Wu, Y., Wu, C. A., Guo, J., Ling, E., & Liang, F. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4181-06.2007 · Cited by 265 · see citing works

Calorie restriction alters mitochondrial protein acetylation

Schwer, B., Eckersdorff, M., Li, Y., Silva, J. C., Fermin, D., Kurtev, M. V., Giallourakis, C., Comb, M. J., Alt, F. W., & Lombard, D. B. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00503.x · Cited by 259 · cited 1× · see citing works

SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress

Inoue, T., Hiratsuka, M., Osaki, M., Yamada, H. Y., Kishimoto, I., Yamaguchi, S., Nakano, S., Katoh, M., Ito, H., & Oshimura, M. (2006) · Oncogene · doi:10.1038/sj.onc.1209857 · Cited by 258 · see citing works

The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability

Yang, B., Zwaans, B. M. M., Eckersdorff, M., & Lombard, D. B. (2009) · Cell Cycle · doi:10.4161/cc.8.16.9329 · Cited by 254 · see citing works

Anti-oxidative and anti-inflammatory vasoprotective effects of caloric restriction in aging: Role of circulating factors and SIRT1

Csiszár, A., Labinskyy, N., Jiménez, R., Pinto, J. T., Ballabh, P., Losonczy, G., Pearson, K. J., de Cabo, R., & Ungvari, Z. I. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.06.004 · Cited by 248 · see citing works

Altered sirtuin expression is associated with node-positive breast cancer

Ashraf, N., Zino, S., MacIntyre, A., Kingsmore, D. B., Payne, P., George, W. D., & Shiels, P. G. (2006) · British Journal of Cancer · doi:10.1038/sj.bjc.6603384 · Cited by 247 · see citing works

An accelerated assay for the identification of lifespan-extending interventions in <i>Drosophila</i> melanogaster

Bauer, J. H., Goupil, S., Garber, G. B., & Helfand, S. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403493101 · Cited by 234 · see citing works

A c-Myc–SIRT1 feedback loop regulates cell growth and transformation

Yuan, J., Minter‐Dykhouse, K., & Lou, Z. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200809167 · Cited by 232 · see citing works

SIRT1 Inhibits Transforming Growth Factor β-Induced Apoptosis in Glomerular Mesangial Cells via Smad7 Deacetylation

Kume, S., Haneda, M., Kanasaki, K., Sugimoto, T., Araki, S., Isshiki, K., Isono, M., Uzu, T., Guarente, L., Kashiwagi, A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605904200 · Cited by 231 · see citing works

MicroRNA 132 Regulates Nutritional Stress-Induced Chemokine Production through Repression of SirT1

Strum, J. C., Johnson, J. H., Ward, J. M., Xie, H., Feild, J. A., Hester, A. G., Alford, A., & Waters, K. M. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0117 · Cited by 226 · see citing works

The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility

Pandithage, R., Lilischkis, R., Harting, K., Wolf, A., Jedamzik, B., Lüscher‐Firzlaff, J., Vervoorts, J., Lasonder, E., Kremmer, E., Knöll, B., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707126 · Cited by 213 · see citing works

SIRT1, a Longevity Gene, Downregulates Angiotensin II Type 1 Receptor Expression in Vascular Smooth Muscle Cells

Miyazaki, R., Ichiki, T., Hashimoto, T., Inanaga, K., Imayama, I., Sadoshima, J., & Sunagawa, K. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.166991 · Cited by 213 · see citing works

Deacetylation of cortactin by SIRT1 promotes cell migration

Zhang, Y., Zhang, M., Dong, H., Yong, S., Li, X., Olashaw, N., Kruk, P. A., Cheng, J., Bai, W., Chen, J., et al. (2008) · Oncogene · doi:10.1038/onc.2008.388 · Cited by 205 · see citing works

Expression of DBC1 and SIRT1 Is Associated with Poor Prognosis of Gastric Carcinoma

Cha, E. J., Noh, S. J., Kwon, K. S., Kim, C. Y., Park, B., Park, H. S., Lee, H., Chung, M. J., Kang, M. J., Lee, D. G., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-3329 · Cited by 186 · see citing works

SirT1 knockdown in liver decreases basal hepatic glucose production and increases hepatic insulin responsiveness in diabetic rats

Erion, D. M., Yonemitsu, S., Nie, Y., Nagai, Y., Gillum, M. P., Hsiao, J. J., Iwasaki, T., Stark, R., Weismann, D., Yu, X. X., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812931106 · Cited by 181 · see citing works

SIRT1 deacetylates APE1 and regulates cellular base excision repair

Yamamori, T., DeRicco, J. S., Naqvi, A., Hoffman, T. A., Mattagajasingh, I., Kasuno, K., Jung, S.-B., Kim, C., & Irani, K. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1039 · Cited by 176 · see citing works

EXPRESSION OF CONCERN: Kaempferol induces apoptosis in two different cell lines via Akt inactivation, Bax and SIRT3 activation, and mitochondrial dysfunction

Marfè, G., Tafani, M., Indelicato, M., Sinibaldi‐Salimei, P., Reali, V., Pucci, B., Fini, M., & Russo, M. A. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22044 · Cited by 174 · see citing works

SIRT1 Activation Confers Neuroprotection in Experimental Optic Neuritis

Shindler, K. S., Ventura, E. S., Rex, T. S., Elliott, P. J., & Rostami, A. M. (2007) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-0131 · Cited by 173 · see citing works

Hyaluronan-mediated CD44 Interaction with p300 and SIRT1 Regulates β-Catenin Signaling and NFκB-specific Transcription Activity Leading to MDR1 and Bcl-xL Gene Expression and Chemoresistance in Breast Tumor Cells

Bourguignon, L., Xia, W., & Wong, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806708200 · Cited by 173 · see citing works

Investigating the ADP-ribosyltransferase Activity of Sirtuins with NAD Analogues and 32 P-NAD

Du, J., Jiang, H. X., & Lin, H. (2009) · Biochemistry · doi:10.1021/bi802093g · Cited by 166 · see citing works

The SIRT2 Deacetylase Regulates Autoacetylation of p300

Black, J. C., Mosley, A. L., Kitada, T., Washburn, M. P., & Carey, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.09.018 · Cited by 166 · see citing works

NAD+-dependent Deacetylase SIRT3 Regulates Mitochondrial Protein Synthesis by Deacetylation of the Ribosomal Protein MRPL10

Yang, Y., Çimen, H., Han, M.-J., Shi, T., Deng, J., Koç, H., Palacios, O. M., Montier, L., Bai, Y., Tong, Q., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.053421 · Cited by 164 · see citing works

Treatment with SRT1720, a SIRT1 activator, ameliorates fatty liver with reduced expression of lipogenic enzymes in MSG mice

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 164 · see citing works

Role of Sirtuin Histone Deacetylase SIRT1 in Prostate Cancer

Jung-Hynes, B. D., Nihal, M., Zhong, W., & Ahmad, N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807869200 · Cited by 163 · see citing works

Mitotic Regulation of SIRT2 by Cyclin-dependent Kinase 1-dependent Phosphorylation

North, B. J., & Verdin, E. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702990200 · Cited by 159 · see citing works

Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3

Jin, L., Galonek, H. L., Israelian, K., Choy, W., Morrison, M. C., Xia, Y. X., Wang, X., Xu, Y., Yang, Y., Smith, J. J., et al. (2009) · Protein Science · doi:10.1002/pro.50 · Cited by 153 · see citing works

Involvement of SIRT7 in resumption of rDNA transcription at the exit from mitosis

Grob, A., Roussel, P., Wright, J. E., McStay, B., Hernandez‐Verdun, D., & Sirri, V. (2009) · Journal of Cell Science · doi:10.1242/jcs.042382 · Cited by 153 · see citing works

SIRT3 is Pro-Apoptotic and Participates in Distinct Basal Apoptotic Pathways

Allison, S. J., & Milner, J. (2007) · Cell Cycle · doi:10.4161/cc.6.21.4866 · Cited by 147 · see citing works

The human SIRT3 protein deacetylase is exclusively mitochondrial

Cooper, H. M., & Spelbrink, J. N. (2008) · Biochemical Journal · doi:10.1042/bj20071624 · Cited by 133 · see citing works

Localization of mouse mitochondrial SIRT proteins: Shift of SIRT3 to nucleus by co-expression with SIRT5

Nakamura, Y., Ogura, M., Tanaka, D., & Inagaki, N. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.11.122 · Cited by 129 · see citing works

Regulation of SIRT1 protein levels by nutrient availability

Kanfi, Y., Peshti, V., Gozlan, Y. M., RATHAUS, M., Gil, R., & Cohen, H. Y. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.005 · Cited by 128 · see citing works

PGC-1α Integrates Insulin Signaling, Mitochondrial Regulation, and Bioenergetic Function in Skeletal Muscle

Pagel-Langenickel, I., Bao, J., Joseph, J. J., Schwartz, D. R., Mantell, B. S., Xu, X., Raghavachari, N., & Sack, M. N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800842200 · Cited by 124 · see citing works

SIRT1 Expression is Associated With Poor Prognosis of Diffuse Large B-Cell Lymphoma

Jang, K. Y., Hwang, S. H., Kwon, K. S., Kim, K. R., Choi, H. N., Lee, N., Kwak, J., Park, B., Park, H. S., Chung, M. J., et al. (2008) · The American Journal of Surgical Pathology · doi:10.1097/pas.0b013e31816b6478 · Cited by 122 · see citing works

Mammalian Sir2-related protein (SIRT) 2–mediated modulation of resistance to axonal degeneration in slow Wallerian degeneration mice: A crucial role of tubulin deacetylation

Suzuki, K., & Koike, T. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.04.059 · Cited by 119 · see citing works

Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti‐aging and metabolic effects of sirtuins

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 115 · see citing works

Characterization of the murine SIRT3 mitochondrial localization sequence and comparison of mitochondrial enrichment and deacetylase activity of long and short SIRT3 isoforms

Bao, J., Lu, Z., Joseph, J. J., Carabenciov, D., Dimond, C. C., Pang, L., Samsel, L., McCoy, J. P., Leclerc, J., Nguyen, P., et al. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22531 · Cited by 115 · see citing works

Modulation of SIRT1 expression in different neurodegenerative models and human pathologies

Pallàs, M., Pizarro, J. G., Cuesta, J., Crespo‐Biel, N., Alvira, D., Tajes, M., Yeste‐Velasco, M., Folch, J., Canudas, A. M., Sureda, F. X., et al. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.04.065 · Cited by 112 · see citing works

Where in the cell is SIRT3? – functional localization of an NAD+-dependent protein deacetylase

Hallows, W. C., Albaugh, B. N., & Denu, J. M. (2008) · Biochemical Journal · doi:10.1042/bj20080336 · Cited by 109 · see citing works

SIRT1 Acts as a Nutrient-sensitive Growth Suppressor and Its Loss Is Associated with Increased AMPK and Telomerase Activity

Narala, S. R., Allsopp, R. C., Wells, T. B., Zhang, G., Prasad, P., Coussens, M. J., Rossi, D. J., Weissman, I. L., & Vaziri, H. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0965 · Cited by 106 · see citing works

Sirt2 interacts with 14-3-3 β/γ and down-regulates the activity of p53

Jin, Y.-H., Kim, Y.-J., Kim, D., Baek, K., Kang, B. Y., Yeo, C., & Lee, K.-Y. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.114 · Cited by 101 · see citing works

Acetylation of Sirt2 by p300 attenuates its deacetylase activity

Han, Y., Jin, Y.-H., Kim, Y.-J., Kang, B. Y., Choi, H.-J., Kim, D., Yeo, C., & Lee, K.-Y. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.042 · Cited by 101 · see citing works

Histone H2A.z Is Essential for Cardiac Myocyte Hypertrophy but Opposed by Silent Information Regulator 2α

Chen, I.-Y., Lypowy, J., Pain, J., Sayed, D. H., Grinberg, S., Alcendor, R. R., Sadoshima, J., & Abdellatif, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601443200 · Cited by 98 · see citing works

SIRT2 is a negative regulator of anoxia–reoxygenation tolerance via regulation of 14‐3‐3 ζ and BAD in H9c2 cells

Lynn, E. G., McLeod, C. J., Gordon, J. P., Bao, J., & Sack, M. N. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.07.016 · Cited by 87 · see citing works

Sirt7-dependent inhibition of cell growth and proliferation might be instrumental to mediate tissue integrity during aging.

Vakhrusheva, O., Braeuer, D., Liu, Z., Braun, T. W., & Bober, E. (2008) · PubMed · Cited by 85 · see citing works

Human Histone Deacetylase SIRT2 Interacts with the Homeobox Transcription Factor HOXA10

Bae, N. S. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh084 · Cited by 84 · see citing works

Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin

Nahhas, F. A., Dryden, S. C., Abrams, J., & Tainsky, M. A. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9478-6 · Cited by 81 · see citing works

A Functional Link Between SIRT1 Deacetylase and NBS1 in DNA Damage Response

Yuan, Z., & Seto, E. (2007) · Cell Cycle · doi:10.4161/cc.6.23.5026 · Cited by 77 · see citing works

Sirtuin 1 overexpression mice show a reference memory deficit, but not neuroprotection

Kakefuda, K., Fujita, Y., Oyagi, A., Hyakkoku, K., Kojima, T., Umemura, K., Tsuruma, K., Shimazawa, M., Ito, M., Nozawa, Y., et al. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.07.119 · Cited by 74 · see citing works

SIRT2 downregulation confers resistance to microtubule inhibitors by prolonging chronic mitotic arrest

Inoue, T., Nakayama, Y., Yamada, H., Li, Y. C., Yamaguchi, S., Osaki, M., Kurimasa, A., Hiratsuka, M., Katoh, M., & Oshimura, M. (2009) · Cell Cycle · doi:10.4161/cc.8.8.8245 · Cited by 58 · see citing works

A New Splice Variant of the Mouse SIRT3 Gene Encodes the Mitochondrial Precursor Protein

Cooper, H. M., Huang, J.-Y., Verdin, E. M., & Spelbrink, J. N. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004986 · Cited by 55 · see citing works

Transcriptional activation of NAD+-dependent protein deacetylase SIRT1 by nuclear receptor TLX

Iwahara, N., Hisahara, S., Hayashi, T., & Horio, Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.103 · Cited by 51 · see citing works

Activation of SIRT1, a class III histone deacetylase, contributes to fructose feeding-mediated induction of the α-myosin heavy chain expression

Pillai, J. B., Chen, M., Rajamohan, S. B., Samant, S. A., Pillai, V. B., Gupta, M., & Gupta, M. P. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01339.2007 · Cited by 43 · see citing works

Tryptophan Metabolism was Accelerated by Exercise in Rat

Ito, Y., Yonekura, R., Nakagami, Y., Maruta, K., Koike, T., Nagamura, Y., Shibata, K., & Saito, K. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0135-0_61 · Cited by 30 · see citing works

Nad Levels In The Rat Primary Cultured Hepatocytes Affected By Peroxisome- Proliferators

Shin, M., Ohnishi, M., Sano, K., & Umezawa, C. Y. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0135-0_76 · Cited by 6 · see citing works

Aging: The Sins of the Parents

Haber, J. E. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.018 · Cited by 3 · see citing works

The return of the nucleus: transcriptional and epigenetic control of autophagy

Füllgrabe, J., Klionsky, D. J., & Joseph, B. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3716 · Cited by 463 · see citing works

Transcriptional Regulation of Autophagy: Mechanisms and Diseases

Di Malta, C., Cinque, L., & Settembre, C. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00114 · Cited by 255 · see citing works

Epigenetic regulation in major depression and other stress-related disorders: molecular mechanisms, clinical relevance and therapeutic potential

Yuan, M., Yang, B., Rothschild, G., Mann, J. J., Sanford, L. D., Tang, X., Huang, C., Wang, C., & Zhang, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01519-z · Cited by 246 · see citing works

Impaired adenosine monophosphate-activated protein kinase signalling in dorsal root ganglia neurons is linked to mitochondrial dysfunction and peripheral neuropathy in diabetes

Chowdhury, S. R., Smith, D. R., Saleh, A. J., Schapansky, J., Marquez, A. M., Gomes, S., Akude, E., Morrow, D., Calcutt, N. A., & Fernyhough, P. (2012) · Brain · doi:10.1093/brain/aws097 · Cited by 215 · see citing works

Peroxisome Proliferator-activated Receptor-γ Coactivator-1α Controls Transcription of the Sirt3 Gene, an Essential Component of the Thermogenic Brown Adipocyte Phenotype

Giralt, 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 · see citing works

Metabolic reprogramming orchestrates cancer stem cell properties in nasopharyngeal carcinoma

Shen, Y., Wang, C.-Y., Hsieh, Y.-T., Chen, Y.-J., & Wei, Y. (2014) · Cell Cycle · doi:10.4161/15384101.2014.974419 · Cited by 209 · see citing works

Multiple roles of class I HDACs in proliferation, differentiation, and development

Reichert, N., Choukrallah, M.-A., & Matthias, P. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0921-9 · Cited by 194 · see citing works

Epigenetic mechanisms of major depression: Targeting neuronal plasticity

Uchida, S., Yamagata, H., Seki, T., & Watanabe, Y. (2018) · Psychiatry and Clinical Neurosciences · doi:10.1111/pcn.12621 · Cited by 181 · see citing works

Mitochondrial Dysfunction in Diabetic Neuropathy: a Series of Unfortunate Metabolic Events

Fernyhough, P. (2015) · Current Diabetes Reports · doi:10.1007/s11892-015-0671-9 · Cited by 163 · see citing works

Resveratrol Induces a Mitochondrial Complex I-dependent Increase in NADH Oxidation Responsible for Sirtuin Activation in Liver Cells

Desquiret‐Dumas, V., Guéguen, N., Leman, G., Baron, S., Nivet‐Antoine, V., Chupin, S., Chevrollier, A., Vessières, E., Ayer, A., Ferré, M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.466490 · Cited by 142 · see citing works

Altered sirtuin deacetylase gene expression in patients with a mood disorder

Abe, N., Uchida, S., Otsuki, K., Hobara, T., Yamagata, H., Higuchi, F., Shibata, T., & Watanabe, Y. (2011) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2011.01.016 · Cited by 131 · see citing works

Phytochemical Antioxidants Modulate Mammalian Cellular Epigenome: Implications in Health and Disease

Malireddy, S., Kotha, S. R., Secor, J. D., Gurney, T. O., Abbott, J. L., Maulik, G., Maddipati, K. R., & Parinandi, N. L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4600 · Cited by 129 · see citing works

SIRT1-mediated acute cardioprotection

Nadtochiy, S. M., Yao, H., McBurney, M. W., Gu, W. J., Guarente, L., Rahman, I., & Brookes, P. S. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00587.2011 · Cited by 105 · see citing works

Dietary plant polyphenols as the potential drugs in neurodegenerative diseases: current evidence, advances, and opportunities

Yan, L., Guo, M.-S., Zhang, Y., Yu, L., Wu, J.-M., Tang, Y., Ai, W., Zhu, F.-D., Law, B. Y.-K., Chen, Q., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/5288698 · Cited by 97 · see citing works

The role of sirtuins in modulating redox stressors

Webster, B. R., Lu, Z., Sack, M. N., & Scott, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.484 · Cited by 95 · see citing works

Multiple Site Acetylation of Rictor Stimulates Mammalian Target of Rapamycin Complex 2 (mTORC2)-dependent Phosphorylation of Akt Protein

Glidden, E. J., Gray, L. G., Vemuru, S., Li, D., Harris, T. E., & Mayo, M. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.304337 · Cited by 88 · see citing works

Caloric Restriction Primes Mitochondria for Ischemic Stress by Deacetylating Specific Mitochondrial Proteins of the Electron Transport Chain

Shinmura, K., Tamaki, K., Sano, M., Nakashima-Kamimura, N., Wolf, A. M., Amo, T., Ohta, S., Katsumata, Y., Fukuda, K., Ishiwata, K., et al. (2011) · Circulation Research · doi:10.1161/circresaha.111.243097 · Cited by 88 · see citing works

Nutrient excess and altered mitochondrial proteome and function contribute to neurodegeneration in diabetes

Chowdhury, S. K. R., Dobrowsky, R. T., & Fernyhough, P. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.06.007 · Cited by 82 · see citing works

SIRT1 is a regulator of autophagy: Implications in gastric cancer progression and treatment

Qiu, G., Li, X., Che, X., Wei, C., He, S., Lü, J., Jia, Z., Pang, K., & Fan, L. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.05.042 · Cited by 82 · see citing works

Regulation of oxidative phosphorylation complex activity: effects of tissue-specific metabolic stress within an allometric series and acute changes in workload

Phillips, D. J., Covián, R., Aponte, A. M., Glancy, B. C., Taylor, J. F., Chess, D. J., & Balaban, R. S. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00596.2011 · Cited by 77 · see citing works

Protein Targets of Thioacetamide Metabolites in Rat Hepatocytes

Koen, Y. M., Sarma, D., Hajovsky, H., Galeva, N. A., Williams, T. D., Staudinger, J. L., & Hanzlik, R. P. (2013) · Chemical Research in Toxicology · doi:10.1021/tx400001x · Cited by 69 · see citing works

Epigenetic Regulation of Bone Marrow Stem Cell Aging: Revealing Epigenetic Signatures associated with Hematopoietic and Mesenchymal Stem Cell Aging

Cakouros, D., & Gronthos, S. (2018) · Aging and Disease · doi:10.14336/ad.2017.1213 · Cited by 68 · see citing works

The role of SIRT3 in mitochondrial homeostasis and cardiac adaptation to hypertrophy and aging

Sack, M. N. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.11.004 · Cited by 65 · see citing works

Adversity in childhood and depression: linked through SIRT1

Iacono, L. L., Visco‐Comandini, F., Valzania, A., Viscomi, M. T., Coviello, M., Giampà, A., Roscini, L., Bisicchia, E., Siracusano, A., Troisi, A., et al. (2015) · Translational Psychiatry · doi:10.1038/tp.2015.125 · Cited by 62 · see citing works

Bromodomain coactivators in cancer, obesity, type 2 diabetes, and inflammation.

Denis, G. V. (2010) · PubMed · Cited by 57 · see citing works

Role of sirtuins in chronic obstructive pulmonary disease

Chun, P. (2014) · Archives of Pharmacal Research · doi:10.1007/s12272-014-0494-2 · Cited by 55 · see citing works

Nicotinamide Phosphoribosyl Transferase (Nampt) Is Required for De Novo Lipogenesis in Tumor Cells

Bowlby, S. C., Thomas, M. J., D’Agostino, R. B., & Kridel, S. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040195 · Cited by 54 · see citing works

Functional Effects of Cigarette Smoke‐Induced Changes in Airway Smooth Muscle Mitochondrial Morphology

Aravamudan, B., Thompson, M., Sieck, G. C., Vassallo, R., Pabelick, C. M., & Prakash, Y. S. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25508 · Cited by 54 · see citing works

Sirtuins and inflammation: Friends or foes?

Gallí, M., Gool, F. V., & Léo, O. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.12.010 · Cited by 53 · see citing works

Identification of Inhibitor Binding Site in Human Sirtuin 2 Using Molecular Docking and Dynamics Simulations

Sakkiah, S., Arooj, M., Kumar, M. R., Eom, S. H., & Lee, K. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051429 · Cited by 40 · see citing works

Global Gene Expression Profiling Reveals Functional Importance of Sirt2 in Endothelial Cells under Oxidative Stress

Liu, J., Wu, X. B., Wang, X., Zhang, Y., Bu, P., Zhang, Q., & Jiang, F. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14035633 · Cited by 40 · see citing works

Recreational scuba diving: negative or positive effects of oxidative and cardiovascular stress?

Perović, A., Unić, A., & Dumić, J. (2014) · Biochemia Medica · doi:10.11613/bm.2014.026 · Cited by 39 · see citing works

Estrogen-related receptor alpha and mitochondria: tale of the titans

Ranhotra, H. S. (2014) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2014.959592 · Cited by 39 · see citing works

Sirtuins and Accelerated Aging in Scleroderma

Wyman, A. E., & Atamas, S. P. (2018) · Current Rheumatology Reports · doi:10.1007/s11926-018-0724-6 · Cited by 32 · see citing works

Sustained Activation of AMPK Enhances Differentiation of Human iPSC-Derived Cardiomyocytes via Sirtuin Activation

Sarikhani, M., Garbern, J. C., Ma, S., Sereda, R., Conde, J., Krähenbühl, G., Escalante, G. O., Ahmed, A., Buenrostro, J. D., & Lee, R. T. (2020) · Stem Cell Reports · doi:10.1016/j.stemcr.2020.06.012 · Cited by 30 · see citing works

Dysregulated cellular redox status during hyperammonemia causes mitochondrial dysfunction and senescence by inhibiting sirtuin‐mediated deacetylation

Mishra, S., Welch, N., Karthikeyan, M., Bellar, A., Musich, R. J., Singh, S. S., Zhang, D., Sekar, J., Attaway, A. H., Chelluboyina, A. K., et al. (2023) · Aging Cell · doi:10.1111/acel.13852 · Cited by 26 · see citing works

The orphan estrogen-related receptor alpha and metabolic regulation: new frontiers

Ranhotra, H. S. (2015) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2015.1024853 · Cited by 24 · see citing works

Genetic variants in NAMPT predict bladder cancer risk and prognosis in individuals from southwest Chinese Han group

Zhang, K., Zhou, B., Zhang, P., Zhang, Z., Chen, P., Pu, Y., Song, Y., & Zhang, L. (2013) · Tumor Biology · doi:10.1007/s13277-013-1527-z · Cited by 23 · see citing works

The Potential Role of Sirtuins Regarding the Effects of Exercise on Aging- Related Diseases

Suwa, M., & Sakuma, K. (2013) · Current Aging Science · doi:10.2174/18746098112059990035 · Cited by 23 · see citing works

miR-125-chinmo pathway regulates dietary restriction-dependent enhancement of lifespan in Drosophila

Pandey, M., Bansal, S., Bar, S., Yadav, A. K., Sokol, N. S., Tennessen, J. M., Kapahi, P., & Chawla, G. (2021) · eLife · doi:10.7554/elife.62621 · Cited by 21 · see citing works

Mitochondrial cytochrome c shot towards histone chaperone condensates in the nucleus

González‐Arzola, K., Guerra‐Castellano, A., Rivero‐Rodríguez, F., Casado‐Combreras, M. Á., Pérez‐Mejías, G., Dı́az-Quintana, A., Díaz‐Moreno, I., & la Rosa, M. Á. D. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13176 · Cited by 19 · see citing works

Neurobiological Opportunities in Diabetic Polyneuropathy

Poitras, T. M., Munchrath, E., & Zochodne, D. W. (2021) · Neurotherapeutics · doi:10.1007/s13311-021-01138-y · Cited by 18 · see citing works

Skin keratinocyte-derived SIRT1 and BDNF modulate mechanical allodynia in mouse models of diabetic neuropathy

OʼBrien, J., Niehaus, P., Chang, K., Remark, J., Barrett, J., Dasgupta, A., Adenegan, M., Salimian, M., Kevas, Y., Chandrasekaran, K., et al. (2024) · Brain · doi:10.1093/brain/awae100 · Cited by 17 · see citing works

Delactylation of H3K9 by Sirtuin6 inhibits MGMT transcription and reverses temozolomide resistance in glioblastoma

Zou, L., Liu, Z., Peng, L., Wu, B., Huang, Y., Wen, X., Han, D., Tan, W., & Zhou, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147332 · Cited by 16 · see citing works

SIRT1 increases cardiomyocyte binucleation in the heart development

Shin, A. N., Han, L., Dasgupta, C., Huang, L., Yang, S., & Zhang, L. (2018) · Oncotarget · doi:10.18632/oncotarget.23847 · Cited by 16 · see citing works

NAD+ metabolism in peripheral neuropathic pain

Dai, Y., Lin, J., Ren, J., Zhu, B., Wu, C., & Yu, L. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105435 · Cited by 15 · see citing works

Rhythms in Remodeling: Posttranslational Regulation of Bone by the Circadian Clock

Yuan, G. (2025) · Biomedicines · doi:10.3390/biomedicines13030705 · Cited by 13 · see citing works

DNA methyltransferase 1(DNMT1) induced the expression of suppressors of cytokine signaling3 (Socs3) in a mouse model of asthma

Verma, M., Chattopadhyay, B., Kumar, S., Kumar, K., & Verma, D. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3312-5 · Cited by 13 · see citing works

Histone acetyltransferase inhibition rescues differentiation of emerin‐deficient myogenic progenitors

Bossone, K. A., Ellis, J. A., & Holaska, J. M. (2020) · Muscle & Nerve · doi:10.1002/mus.26892 · Cited by 13 · see citing works

The Role of Epigenetic Regulator SIRT1 in Balancing the Homeostasis and Preventing the Formation of Specific “Soil” of Metabolic Disorders and Related Cancers

Németh, Z., Kiss, É., & Takács, I. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2709253 · Cited by 12 · see citing works

Epigenetic aging in major depressive disorder: Clocks, mechanisms and therapeutic perspectives

Shaikh, M., & Doshi, G. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176757 · Cited by 12 · see citing works

Molecular docking and mechanisms of fusaric acid induced mitochondrial sirtuin aberrations in glycolytically and oxidatively poised human hepatocellular carcinoma (HepG2) cells

Abdul, N. S., Nagiah, S., Anand, K., & Chuturgoon, A. A. (2019) · Toxicon · doi:10.1016/j.toxicon.2019.11.009 · Cited by 9 · see citing works

Newcastle disease virus regulates its replication by instigating oxidative stress-driven Sirtuin 7 production

Shokeen, K., & Kumar, S. (2024) · Journal of General Virology · doi:10.1099/jgv.0.001961 · Cited by 7 · see citing works

A Nutrigenomic View on the Premature-Aging Disease Fanconi Anemia

Velleuer, E., & Carlberg, C. (2024) · Nutrients · doi:10.3390/nu16142271 · Cited by 5 · see citing works

Sirtuin‐2 Is Involved in the Regulation of Claudin‐4 Expression and Paracellular Barrier Function in Keratinocytes

Matsuda, S., Miwa, M., Tanabe, M., Kobayashi, M., Shu, S., Yoshino, Y., Tada, N., Itoh, A., & Ikari, A. (2025) · Journal of Cellular Biochemistry · doi:10.1002/jcb.70027 · Cited by 4 · see citing works

Bambusa vulgaris leaves reverse mitochondria dysfunction in diabetic rats through modulation of mitochondria biogenic genes

Elekofehinti, O. O., Aladenika, Y. V., Iwaloye, O., Okon, E. I.-A., & Adanlawo, I. G. (2023) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci-2022-0053 · Cited by 4 · see citing works

Calorie Restriction Mimetics From Functional Foods

Sun, W. Y., & Wang, Y. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805376-8.00022-8 · Cited by 3 · see citing works

Effect of SIRT1 on white matter neural network in adolescent patients with depression

Ji, L., Jiang, W., Liu, D., & Hou, K. (2022) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2022.966315 · Cited by 2 · see citing works

Vitamin K and muscle health: mechanisms and clinical perspectives in sarcopenia and beyond: narrative review

Ran, X., Jiang, Y., Mao, L., Chen, X., Jing, D., Tang, X., & Tan, J. (2026) · Frontiers in Nutrition · doi:10.3389/fnut.2026.1726483 · Cited by 1 · see citing works

Exercising the brain: Molecular pathways linking exercise, neuronal mitochondria, and synaptic plasticity

Mao, X., Rygalski, E., & Yan, Z. (2026) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2026.07.001 · Cited by 1 · see citing works

Histone acetyltransferase inhibition rescues differentiation of emerin-deficient myogenic progenitorsPreprint

Bossone, K. A., Ellis, J. A., & Holaska, J. M. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/437343 · Cited by 1 · see citing works

Newcastle disease virus elevates its replication by instigating oxidative stress-driven Sirtuin 7 productionPreprint

Shokeen, K., & Kumar, S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.10.511685 · Cited by 1 · see citing works

Targeted Proteomics Using Immunoaffinity Purification

Jonscher, K. R., Jin, L., Cambier, J. C., Rahman, S. M., & Friedman, J. E. (2012) · doi:10.1002/9781118180730.ch1

Rictor Acetylation Promotes mTORC2-Medicated Akt Phosophorylation

Glidden, E. J. (2011) · doi:10.18130/v3rc4f

Evolutionary, structural and functional features of cellular signalling networks

Lang, B. (2012) · Apollo (University of Cambridge) · doi:10.17863/cam.39120

Rescue of sirtuin inhibitor-dependent decrease in claudin-4 expression and paracellular barrier property in keratinocytes by epigallocatechin gallate

Miwa, M., Tanabe, M., Matsuda, S., Yamakawa, K., Yoshino, Y., Tada, N., Itoh, A., & Ikari, A. (2025) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2025.184440

The Role of Sirtuin Inhibitors on the Proteomic Responses of the Mussels Mytilus galloprovincialis and Mytilus trossulus to Menadione Induced Oxidative Stress

Chilton, H. C. (2014) · doi:10.15368/theses.2014.129

Protein deacetylation by SIRT1: An emerging key post-translational modification in metabolic regulation

Yu, J., & Auwerx, J. H. (2009) · Pharmacological Research · doi:10.1016/j.phrs.2009.12.006 · Cited by 153 · see citing works

Sirtuins regulate metabolic adaptation to energy status

Denu, J. M., Hallows, W. C., & Smith, B. C. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.198.1

A Molecular Perspective on Sirtuin Activity

Teixeira, C. S. S., Cerqueira, N. M. F. S. A., Gomes, P., & Sousa, S. F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228609 · Cited by 56 · see citing works

Understanding the Function of Mammalian Sirtuins and Protein Lysine Acylation

Wang, M., & Lin, H. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-082520-125411 · Cited by 171 · see citing works

Lipoic acid activation of the α-ketobutyrate oxidation system in cell-free extracts of Streptococcus faecalis

Leach, F. R., Yasunobu, K. T., & Reed, L. J. (1955) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(55)90077-9 · Cited by 18 · see citing works