Protective effects and mechanisms of sirtuins in the nervous system

MicroRNAs: Target Recognition and Regulatory Functions

Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.01.002 · Cited by 20,068 · see citing works

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works

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 · see citing works

A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis

Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works

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 · see citing works

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 · 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

The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253 · see citing works

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 · see citing works

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · 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

Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans

Tissenbaum, H. A., & Guarente, L. (2001) · Nature · doi:10.1038/35065638 · Cited by 1,918 · see citing works

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868 · see citing works

Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1

Yoon, J. C., Puigserver, P., Chen, G., Donovan, J., Wu, Z., Rhee, J., Adelmant, G., Stafford, J., Kahn, C. R., Granner, D. K., et al. (2001) · Nature · doi:10.1038/35093050 · Cited by 1,821 · see citing works

The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress

Shaw, R. J., Kosmatka, M., Bardeesy, N., Hurley, R. L., Witters, L. A., DePinho, R. A., & Cantley, L. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308061100 · Cited by 1,797 · see citing works

CBP/p300 in cell growth, transformation, and development

Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778 · 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

Sirtuins in mammals: insights into their biological function

Michán, S., & Sinclair, D. A. (2007) · Biochemical Journal · doi:10.1042/bj20070140 · Cited by 1,719 · 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

A probability-based approach for high-throughput protein phosphorylation analysis and site localization

Beausoleil, S. A., Villén, J., Gerber, S. A., Rush, J., & Gygi, S. P. (2006) · Nature Biotechnology · doi:10.1038/nbt1240 · Cited by 1,577 · 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

Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction

Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487 · 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

Large-scale characterization of HeLa cell nuclear phosphoproteins

Beausoleil, S. A., Jedrychowski, M. P., Schwartz, D., Elias, J. E., Villén, J., Li, J., Cohn, M. A., Cantley, L. C., & Gygi, S. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404720101 · 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

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 · see citing works

Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease

Ittner, L. M., & Götz, J. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2967 · Cited by 1,357 · see citing works

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 1,351 · 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

Calorie 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 · 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

The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor α in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes

Vega, R. B., Huss, J. M., & Kelly, D. P. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1868-1876.2000 · Cited by 1,195 · 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

Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction

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 · 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

HuR and mRNA stability

Brennan, C. M., & Steitz*, J. A. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000854 · Cited by 1,095 · 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

‘Ischemic tolerance’ phenomenon found in the brain

Kitagawa, K., Matsumoto, M., Tagaya, M., Hata, R., Ueda, H., Niinobe, M., Handa, N., Fukunaga, R., Kimura, K., Mikoshiba, K., et al. (1990) · Brain Research · doi:10.1016/0006-8993(90)90189-i · Cited by 1,090 · see citing works

Nibrin, a Novel DNA Double-Strand Break Repair Protein, Is Mutated in Nijmegen Breakage Syndrome

Varon, R., Vissinga, C., Platzer, M., Cerosaletti, K. M., Chrzanowska, K. H., Saar, K., Beckmann, G., Seemanová, E., Cooper, P. R., Nowak, N. J., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81174-5 · Cited by 1,079 · 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

Increased Nuclear NAD Biosynthesis and SIRT1 Activation Prevent Axonal Degeneration

Araki, T., Sasaki, Y., & Milbrandt, J. (2004) · Science · doi:10.1126/science.1098014 · Cited by 1,060 · 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

HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention

Yang, X.-J., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210599 · Cited by 1,040 · 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

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

A novel pathway regulates memory and plasticity via SIRT1 and miR-134

Gao, J., Wang, W.-Y., Mao, Y.-W., Gräff, J., Guan, J.-S., Pan, L., Mak, G., Kim, D., Su, S. C., & Tsai, L.-H. (2010) · Nature · doi:10.1038/nature09271 · Cited by 975 · see citing works

The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases

Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970 · 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

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

In vivo evidence that erythropoietin protects neurons from ischemic damage

Sakanaka, M., Wen, T., Matsuda, S., Masuda, S., Morishita, E., Nagao, M., & Sasaki, R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.8.4635 · Cited by 948 · see citing works

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. (1993) · Nature · doi:10.1038/364362c0 · Cited by 922 · 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

Sirt3-mediated deacetylation of evolutionarily conserved lysine 122 regulates MnSOD activity in response to stress

Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.013 · Cited by 899 · 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

SIRT6 Promotes DNA Repair Under Stress by Activating PARP1

Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., Seluanov, A., & Gorbunova, V. (2011) · Science · doi:10.1126/science.1202723 · Cited by 867 · 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

Glucose Restriction Inhibits Skeletal Myoblast Differentiation by Activating SIRT1 through AMPK-Mediated Regulation of Nampt

Fulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 821 · see citing works

Axon degeneration mechanisms: Commonality amid diversity

Coleman, M. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1788 · Cited by 819 · 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

Transcriptional silencing in yeast is associated with reduced nucleosome acetylation.Preprint

Braunstein, M., Rose, A. B., Holmes, S. G., Allis, C. D., & Broach, J. R. (1993) · Genes & Development · doi:10.1101/gad.7.4.592 · 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

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 · see citing works

The biochemistry of sirtuins

Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763 · see citing works

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 · 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

Resveratrol stimulates AMP kinase activity in neurons

Dasgupta, B., & Milbrandt, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610068104 · Cited by 723 · see citing works

A phylogenetically conserved NAD ⁺ -dependent protein deacetylase activity in the Sir2 protein family

Smith, J. S., Brachmann, C. B., Celic, I., Kenna, M. A., Muhammad, S., Starai, V. J., Avalos, J. L., Escalante-Semerena, J. C., Grubmeyer, C., Wolberger, C., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6658 · Cited by 718 · see citing works

Enlarged Infarcts in Endothelial Nitric Oxide Synthase Knockout Mice are Attenuated by Nitro-L-Arginine

Huang, Z., Huang, P. L., Ma, J., Meng, W., Ayata, C., Fishman, M. C., & Moskowitz, M. A. (1996) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199609000-00023 · Cited by 715 · 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

Identification of the differential distribution patterns of mRNAs and consensus binding sequences for mouse DAF-16 homologues

Furuyama, T., Nakazawa, T., Nakano, I., & Mori, N. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3490629 · Cited by 672 · see citing works

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 · see citing works

Mitochondrial calcium and the permeability transition in cell death

Lemasters, J. J., Theruvath, T. P., Zhong, Z., & Nieminen, A. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.06.009 · Cited by 656 · 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

Regulation of SIRT1 in cellular functions: Role of polyphenols

Chung, S., Yao, H., Caito, S. W., Hwang, J., Arunachalam, G., & Rahman, I. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.05.003 · Cited by 651 · 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

FOXO transcription factors directly activate bim gene expression and promote apoptosis in sympathetic neurons

Gilley, J., Coffer, P. J., & Ham, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200303026 · Cited by 646 · see citing works

p300/CBP and cancer

Iyer, N. G., Özdağ, H., & Caldas, C. (2004) · Oncogene · doi:10.1038/sj.onc.1207118 · Cited by 645 · see citing works

Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney

Kume, S., Uzu, T., Horiike, K., Chin-Kanasaki, M., Isshiki, K., Araki, S.-I., Sugimoto, T., Haneda, M., Kashiwagi, A., & Koya, D. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41376 · Cited by 640 · see citing works

Calorie restriction extends yeast life span by lowering the level of NADH

Lin, S.-J., Ford, E., Haigis, M., Liszt, G., & Guarente, L. (2004) · Genes &amp; Development · doi:10.1101/gad.1164804 · Cited by 632 · 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

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

Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene

Mack, T. G. A., Reiner, M., Beirowski, B., Mi, W., Emanuelli, M., Wagner, D., Thomson, D., Gillingwater, T., Court, F., Conforti, L., et al. (2001) · Nature Neuroscience · doi:10.1038/nn770 · Cited by 611 · see citing works

Hexokinase-2 bound to mitochondria: Cancer's stygian link to the “Warburg effect” and a pivotal target for effective therapy

Mathupala, S. P., Ko, Y. H., & Pedersen, P. L. (2008) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2008.11.006 · Cited by 578 · 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

Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1- O- acetyl-ADP-ribose

Tanner, K. G., Landry, J. W., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 557 · 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

Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy

Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C., Palmeira, C. M., Rosenzweig, A., & Sinclair, D. A. (2010) · Aging · doi:10.18632/aging.100252 · Cited by 542 · 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

Identification of a Class of Small Molecule Inhibitors of the Sirtuin Family of NAD-dependent Deacetylases by Phenotypic Screening

Grozinger, C. M., Chao, E. D., Blackwell, H. E., Moazed, D., & Schreiber, S. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106779200 · Cited by 533 · 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

Discovery of Indoles as Potent and Selective Inhibitors of the Deacetylase SIRT1

Napper, A. D., Hixon, J., McDonagh, T., Keavey, K., Pons, J., Barker, J., Yau, W. T., Amouzegh, P., Flegg, A., Hamelin, E. M.-N., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050522v · Cited by 524 · see citing works

Resveratrol: from grapevines to mammalian biology

Pervaiz, S. (2003) · The FASEB Journal · doi:10.1096/fj.03-0168rev · Cited by 518 · see citing works

Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons

Parker, J. A., Arango-Lievano, M., Abderrahmane, S., Lambert, E., Tourette, C., Catoire, H., & Néri, C. (2005) · Nature Genetics · doi:10.1038/ng1534 · Cited by 509 · 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

Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease

Karuppagounder, S. S., Pinto, J. T., Xu, H., Chen, H., Beal, M. F., & Gibson, G. E. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.10.008 · Cited by 488 · see citing works

Nrf2: friend or foe for chemoprevention?

Kensler, T. W., & Wakabayashi, N. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp231 · Cited by 487 · see citing works

Quercetin increases brain and muscle mitochondrial biogenesis and exercise tolerance

Davis, J. M., Murphy, E. A., Carmichael, M. D., & Davis, B. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90925.2008 · Cited by 486 · see citing works

Inhibition of SIRT1 Catalytic Activity Increases p53 Acetylation but Does Not Alter Cell Survival following DNA Damage

Solomon, J. M., Pasupuleti, R., Xu, L., McDonagh, T., Curtis, R., DiStefano, P. S., & Huber, L. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.28-38.2006 · Cited by 481 · see citing works

Sirtuin Functions in Health and Disease

Yamamoto, H., Schoonjans, K., & Auwerx, J. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0079 · Cited by 480 · see citing works

MicroRNA 217 Modulates Endothelial Cell Senescence via Silent Information Regulator 1

Menghini, R., Casagrande, V., Cardellini, M., Martelli, E., Terrinoni, A., Amati, F., Vasa‐Nicotera, M., Ippoliti, A., Novelli, G., Melino, G., et al. (2009) · Circulation · doi:10.1161/circulationaha.109.864629 · Cited by 479 · 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

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

Modification with SUMO

Verger, A., Perdomo, J., & Crossley, M. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor738 · Cited by 442 · see citing works

Mechanisms of anti-inflammatory and neuroprotective actions of PPAR-gamma agonists

Kapadia, R. (2008) · Frontiers in Bioscience · doi:10.2741/2802 · Cited by 433 · see citing works

Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras–MAPK signaling in human cancer cells

Ota, H., Tokunaga, E., Chang, K., Hikasa, M., Iijima, K., Eto, M., Kozaki, K., Akishita, M., Ouchi, Y., & Kaneki, M. (2005) · Oncogene · doi:10.1038/sj.onc.1209049 · Cited by 431 · see citing works

Can autophagy promote longevity?

Madeo, F., Tavernarakis, N., & Kroemer, G. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-842 · Cited by 429 · see citing works

How does SIRT1 affect metabolism, senescence and cancer?

Brooks, C. L., & Gu, W. J. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2562 · Cited by 426 · 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

Increase in Activity During Calorie Restriction Requires Sirt1

Chen, D., Steele, A. D., Lindquist, S., & Guarente, L. (2005) · Science · doi:10.1126/science.1118357 · Cited by 419 · see citing works

Atomic structure and chemistry of human serum albumin

He, X. M., & Carter, D. C. (1993) · Nature · doi:10.1038/364362b0 · Cited by 415 · see citing works

Sirtuins: The ‘ <i>magnificent seven</i> ’, function, metabolism and longevity

Dali‐Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., & Auwerx, J. (2007) · Annals of Medicine · doi:10.1080/07853890701408194 · Cited by 402 · see citing works

Effect of ischaemic preconditioning on genomic response to cerebral ischaemia: similarity to neuroprotective strategies in hibernation and hypoxia-tolerant states

Stenzel‐Poore, M. P., Stevens, S. L., Xiong, Z., Lessov, N. S., Harrington, C. A., Mori, M., Meller, R., Rosenzweig, H. L., Tobar, E., Shaw, T., et al. (2003) · The Lancet · doi:10.1016/s0140-6736(03)14412-1 · Cited by 394 · see citing works

Composition and dynamics of human mitochondrial nucleoids.

Garrido, N., Griparić, L., Jokitalo, E., Wartiovaara, J., van der Bliek, A. M., & Spelbrink, J. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0399 · Cited by 390 · 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

Sirt3 promotes the urea cycle and fatty acid oxidation during dietary restriction

Hallows, W. C., Yu, W., Smith, B. C., Devires, M. K., Ellinger, J. J., Someya, S., Shortreed, M. R., Prolla, T., Markley, J. L., Smith, L. M., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.002 · Cited by 389 · see citing works

Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases

Imai, S., & Guarente, L. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.02.003 · Cited by 387 · see citing works

Mammalian Abasic Site Base Excision Repair

Srivastava, D., Berg, B. J. V., Prasad, R., Molina, J. T., Beard, W. A., Tomkinson, A. E., & Wilson, S. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.33.21203 · Cited by 381 · see citing works

Structure of the histone deacetylase SIRT2.

Finnin, M. S., Donigian, J. R., & Pavletich, N. P. (2001) · Nature Structural Biology · doi:10.1038/89668 · Cited by 376 · see citing works

Resveratrol pretreatment protects rat brain from cerebral ischemic damage via a sirtuin 1–uncoupling protein 2 pathway

Della‐Morte, D., Dave, K. R., DeFazio, R. A., Bao, Y. C., Raval, A. P., & Pérez‐Pinzón, M. A. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.01.017 · Cited by 375 · see citing works

Mitochondrial and apoptotic neuronal death signaling pathways in cerebral ischemia

Niizuma, K., Yoshioka, H., Chen, H., Kim, G. S., Jung, J. E., Katsu, M., Okami, N., & Chan, P. H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.002 · Cited by 360 · see citing works

SIRT1 promotes DNA repair activity and deacetylation of Ku70

Jeong, J., Juhn, K., Lee, H., Kim, S. H., Min, B.-H., Lee, K., Cho, M., Park, G. H., & Lee, K.-H. (2007) · Experimental & Molecular Medicine · doi:10.1038/emm.2007.2 · Cited by 356 · see citing works

Repeat motifs of tau bind to the insides of microtubules in the absence of taxol

Kar, S., Fan, J., Smith, M. J., Goedert, M., & Amos, L. A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg001 · Cited by 355 · see citing works

Acetylation-Deacetylation of the Transcription Factor Nrf2 (Nuclear Factor Erythroid 2-related Factor 2) Regulates Its Transcriptional Activity and Nucleocytoplasmic Localization

Kawai, Y., Garduño, L., Theodore, M., Yang, J., & Arinze, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208173 · Cited by 355 · see citing works

SIRT1 Deacetylation and Repression of p300 Involves Lysine Residues 1020/1024 within the Cell Cycle Regulatory Domain 1

Bouras, T., Fu, M., Sauve, A. A., Wang, F., Quong, A. A., Perkins, N. D., Hay, R. T., Gu, W. J., & Pestell, R. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408748200 · Cited by 354 · see citing works

Molecular Mechanisms of Prion Pathogenesis

Aguzzi, A., Sigurdson, C. J., & Heikenwaelder, M. (2008) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.154326 · Cited by 354 · see citing works

A local mechanism mediates NAD-dependent protection of axon degeneration

Wang, J., Zhai, Q., Chen, Y., Lin, E., Gu, W., McBurney, M. W., & He, Z. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504028 · Cited by 352 · see citing works

Suppression of FOXO1 activity by FHL2 through SIRT1‐mediated deacetylation

Yang, Y., Hou, H., Haller, E. M., Nicosia, S. V., & Bai, W. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600570 · Cited by 348 · see citing works

Regulation of histone deacetylase activities

Sengupta, N., & Seto, E. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20179 · Cited by 347 · see citing works

Identification of a small molecule inhibitor of Sir2p

Bedalov, A., Gatbonton, T., Irvine, W. P., Gottschling, D. E., & Simon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261574398 · Cited by 344 · see citing works

SIRT1 and p53, effect on cancer, senescence and beyond

Yi, J., & Luo, J. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.05.002 · Cited by 340 · see citing works

SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis

Luthi‐Carter, R., Taylor, D. M., Pallos, J., Lambert, E., Amore, A. M., Parker, J. A., Moffitt, H., Smith, D. L., Runne, H., Gökçe, Ö., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002924107 · Cited by 338 · 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

Resveratrol as a Therapeutic Agent for Neurodegenerative Diseases

Sun, A. Y., Wang, Q., Simonyi, Á., & Sun, G. Y. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8111-y · Cited by 330 · see citing works

Caloric restriction attenuates Aβ-deposition in Alzheimer transgenic models

Patel, N. V., Gordon, M. N., Connor, K. E., Good, R. A., Engelman, R. W., Mason, J., Morgan, D. G., Morgan, T. E., & Finch, C. E. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.09.014 · Cited by 329 · see citing works

MicroRNA-34a induces endothelial progenitor cell senescence and impedes its angiogenesis via suppressing silent information regulator 1

Zhao, T., Li, J., & Chen, A. F. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00192.2010 · Cited by 325 · 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

Optimal Depth and Duration of Mild Hypothermia in a Focal Model of Transient Cerebral Ischemia

Maier, C. M., Ahern, K. V. B., Cheng, M., Lee, J. E., Yenari, M. A., & Steinberg, G. K. (1998) · Stroke · doi:10.1161/01.str.29.10.2171 · Cited by 321 · see citing works

Caloric restriction attenuates β‐amyloid neuropathology in a mouse model of Alzheimer's disease

Wang, J., Ho, L., Qin, W., Rocher, A. B., Seror, I., Humala, N., Maniar, K. P., Dolios, G., Wang, R., Hof, P. R., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-3182fje · Cited by 317 · see citing works

SIRT1 is critical regulator of FOXO-mediated transcription in response to oxidative stress

Kobayashi, Y., Furukawa‐Hibi, Y., Chen, C., Horio, Y., Isobe, K., Ikeda, K., & Motoyama, N. (2005) · International Journal of Molecular Medicine · doi:10.3892/ijmm.16.2.237 · Cited by 316 · see citing works

Brain SIRT1: Anatomical Distribution and Regulation by Energy Availability

Ramadori, G., Lee, C. E., Bookout, A. L., Lee, S., Williams, K. W., Anderson, J. G., Elmquist, J. K., & Coppari, R. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3257-08.2008 · Cited by 311 · see citing works

SIRT1-dependent regulation of chromatin and transcription: Linking NAD+ metabolism and signaling to the control of cellular functions

Zhang, T., & Kraus, W. L. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.10.022 · Cited by 306 · see citing works

SIRT1 Promotes Proliferation and Prevents Senescence Through Targeting LKB1 in Primary Porcine Aortic Endothelial Cells

Zu, Y., Liu, L., Lee, M. Y. K., Xu, C., Liang, Y., Man, R. Y., Vanhoutte, P. M., & Wang, Y. (2010) · Circulation Research · doi:10.1161/circresaha.109.215483 · Cited by 303 · see citing works

SIRT1 Promotes Cell Survival under Stress by Deacetylation-Dependent Deactivation of Poly(ADP-Ribose) Polymerase 1

Rajamohan, S. B., Pillai, V. B., Gupta, M., Sundaresan, N. R., Birukov, K. G., Samant, S. A., Hottiger, M. O., & Gupta, M. P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-09 · Cited by 303 · see citing works

Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant

Sydow, A., Van der Jeugd, A., Zheng, F., Ahmed, T., Balschun, D., Petrova, O., Drexler, D., Zhou, L., Rune, G., Mandelkow, E., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-10.2011 · Cited by 302 · see citing works

Chemistry of Gene Silencing: The Mechanism of NAD+-Dependent Deacetylation Reactions

Sauve, A. A., Celic, I., Avalos‬, J. L., Deng, H., Boeke, J. D., & Schramm, V. L. (2001) · Biochemistry · doi:10.1021/bi011858j · Cited by 301 · see citing works

DYRK2 Is Targeted to the Nucleus and Controls p53 via Ser46 Phosphorylation in the Apoptotic Response to DNA Damage

Taira, N., Nihira, K., Yamaguchi, T., Miki, Y., & Yoshida, K. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.007 · Cited by 299 · see citing works

SIRT1 is a redox‐sensitive deacetylase that is post‐translationally modified by oxidants and carbonyl stress

Caito, S. W., Rajendrasozhan, S., Cook, S., Chung, S., Yao, H., Friedman, A. E., Brookes, P. S., & Rahman, I. (2010) · The FASEB Journal · doi:10.1096/fj.09-151308 · Cited by 296 · see citing works

PGC-1α and PGC-1Β Regulate Mitochondrial Density in Neurons

Warȩski, P., Vaarmann, A., Choubey, V., Safiulina, D., Liiv, J., Kuum, M., & Kaasik, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.018911 · Cited by 294 · see citing works

Post-ischemic inflammation: molecular mechanisms and therapeutic implications

Zheng, Z., & Yenari, M. A. (2004) · Neurological Research · doi:10.1179/016164104x2357 · Cited by 290 · see citing works

Nicotinamide phosphoribosyltransferase protects against ischemic stroke through SIRT1‐dependent adenosine monophosphate–activated kinase pathway

Wang, P., Xu, T., Guan, Y., Tian, W., Viollet, B., Rui, Y., Zhai, Q., Su, D., & Miao, C. (2011) · Annals of Neurology · doi:10.1002/ana.22236 · Cited by 288 · 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

Neuroprotection by Hypoxic Preconditioning Requires Sequential Activation of Vascular Endothelial Growth Factor Receptor and Akt

Wick, A., Wick, W., Waltenberger, J. L., Weller, M., DICHGANS, J., & Schulz, J. B. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06401.2002 · Cited by 283 · see citing works

Histone deacetylase SIRT1 modulates neuronal differentiation by its nuclear translocation

Hisahara, S., Chiba, S., Matsumoto, H., Tanno, M., Yagi, H., Shimohama, S., Sato, M., & Horio, Y. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800612105 · Cited by 281 · see citing works

PPAR: a new pharmacological target for neuroprotection in stroke and neurodegenerative diseases

Bordet, R., Ouk, T., Pétrault, O., Gelé, P., Gautier, S., Laprais, M., Deplanque, D., Duriez, P., Staels, B., Fruchart, J., et al. (2006) · Biochemical Society Transactions · doi:10.1042/bst0341341 · Cited by 273 · see citing works

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 · 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

NAD + as a metabolic link between DNA damage and cell death

Ying, W., Alano, C. C., Garnier, P. E., & Swanson, R. A. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20289 · Cited by 269 · see citing works

Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington’s disease

Pallos, J., Bodai, L., Lukácsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., & Marsh, J. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn273 · Cited by 265 · 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

The SIRT1 activator resveratrol protects SK‐N‐BE cells from oxidative stress and against toxicity caused by α‐synuclein or amyloid‐β (1‐42) peptide

Albani, D., Polito, L., Batelli, S., Mauro, S. D., Fracasso, C., Martelli, G., Colombo, L., Manzoni, C., Salmona, M., Caccia, S., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06228.x · Cited by 260 · see citing works

A <i>Ufd2/D4Cole1e</i> chimeric protein and overexpression of <i>Rbp7</i> in the slow Wallerian degeneration ( <i>Wld</i> ^S ) mouse

Conforti, L., Tarlton, A., Mack, T. G. A., Mi, W., Buckmaster, E. A., Wagner, D., Perry, V. H., & Coleman, M. P. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.21.11377 · Cited by 251 · see citing works

Suppressing Cancer: The Importance of Being Senescent

Campisi, J. (2005) · Science · doi:10.1126/science.1116801 · Cited by 250 · see citing works

Nicotinamide Prevents NAD+ Depletion and Protects Neurons Against Excitotoxicity and Cerebral Ischemia: NAD+ Consumption by SIRT1 may Endanger Energetically Compromised Neurons

Liu, D., Gharavi, R. B., PITTA, M. G. R., Gleichmann, M., & Mattson, M. P. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8058-1 · Cited by 248 · see citing works

Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product

Tanny, J. C., & Moazed, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.415 · Cited by 242 · see citing works

Resveratrol Mimics Ischemic Preconditioning in the Brain

Raval, A. P., Dave, K. R., & Pérez‐Pinzón, M. A. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600262 · Cited by 239 · see citing works

Mechanism of Nicotinamide Inhibition and Transglycosidation by Sir2 Histone/Protein Deacetylases

Jackson, M. D., Schmidt, M. T., Oppenheimer, N. J., & Denu, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306552200 · Cited by 238 · see citing works

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 237 · see citing works

SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus

Satoh, A., Brace, C. S., Ben-Josef, G., West, T., Wozniak, D. F., Holtzman, D. M., Herzog, E. D., & Imai, S.-I. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1385-10.2010 · Cited by 237 · see citing works

miRNAs regulate SIRT1 expression during mouse embryonic stem cell differentiation and in adult mouse tissues

Saunders, L. R., Sharma, A., Tawney, J., Nakagawa, M., Okita, K., Yamanaka, S., Willenbring, H., & Verdin, E. M. (2010) · Aging · doi:10.18632/aging.100176 · Cited by 237 · see citing works

Enzymes in the NAD+ Salvage Pathway Regulate SIRT1 Activity at Target Gene Promoters

Zhang, T., Berrocal, J. G., Frizzell, K. M., Gamble, M. J., DuMond, M. E., Krishnakumar, R., Yang, T., Sauve, A. A., & Kraus, W. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016469 · Cited by 230 · 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

A tale of two mitochondrial channels, MAC and PTP, in apoptosis

Kinnally, K. W., & Antonsson, B. E. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0722-z · Cited by 224 · see citing works

Agrp Neurons Mediate Sirt1's Action on the Melanocortin System and Energy Balance: Roles for Sirt1 in Neuronal Firing and Synaptic Plasticity

Dietrich, M. O., Antunes, C., Geliang, G., Liu, Z.-W., Borók, E., Nie, Y., Xu, A. W., Souza, D. O., Gao, Q., Diano, S., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2234-10.2010 · Cited by 224 · see citing works

SIRT1 Regulates UV-Induced DNA Repair through Deacetylating XPA

Fan, W., & Luo, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.006 · Cited by 223 · see citing works

PCAF Modulates PTEN Activity

Okumura, K., Mendoza, M. C., Bachoo, R. M., DePinho, R. A., Cavenee, W. K., & Furnari, F. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605391200 · Cited by 222 · see citing works

Peroxisome Proliferator-Activated Receptor-α Activation as a Mechanism of Preventive Neuroprotection Induced by Chronic Fenofibrate Treatment

Deplanque, D., Gelé, P., Pétrault, O., Six, I., Furman, C., Bouly, M., Nion, S., Dupuis, B., Leys, D., Fruchart, J., et al. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-15-06264.2003 · Cited by 219 · see citing works

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 · see citing works

FoxO1 Mediates an Autofeedback Loop Regulating SIRT1 Expression

Xiong, S., Salazar, G., Patrushev, N. A., & Alexander, R. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163667 · Cited by 216 · see citing works

Sir2 Regulation by Nicotinamide Results from Switching between Base Exchange and Deacetylation Chemistry

Sauve, A. A., & Schramm, V. L. (2003) · Biochemistry · doi:10.1021/bi034959l · Cited by 216 · see citing works

Neuroprotective Effects of Adenosine Monophosphate- Activated Protein Kinase Inhibition and Gene Deletion in Stroke

Li, J., Zeng, Z., Viollet, B., Ronnett, G. V., & McCullough, L. D. (2007) · Stroke · doi:10.1161/strokeaha.107.490904 · Cited by 216 · see citing works

MNB/DYRK1A as a multiple regulator of neuronal development

Tejedor, F. J., & Hämmerle, B. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07954.x · Cited by 214 · see citing works

SIRT1 Activation by Small Molecules

Dai, H., Kustigian, L. M., Carney, D. P., Case, A. W., Considine, T., Hubbard, B. P., Perni, R. B., Riera, T. V., Szczepankiewicz, B. G., Vlasuk, G. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133892 · Cited by 211 · see citing works

Sirt1 and the Mitochondria

Luen Tang, B. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2318 · Cited by 740 · see citing works

SIRT1 and SIRT2: emerging targets in neurodegeneration

Dönmez, G., & Outeiro, T. F. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302451 · Cited by 414 · see citing works

Role of NAD+ in regulating cellular and metabolic signaling pathways

Amjad, S., Nisar, S., Bhat, A. A., Shah, A. R., Frenneaux, M. P., Fakhro, K. A., Haris, M., Reddy, R. D., Patay, Z. J., Baur, J. A., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101195 · Cited by 394 · see citing works

Mitochondrial function in hypoxic ischemic injury and influence of aging

Ham, P. B., & Raju, R. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.006 · Cited by 367 · see citing works

SIRT1 Deficiency in Microglia Contributes to Cognitive Decline in Aging and Neurodegeneration via Epigenetic Regulation of IL-1β

Cho, S.-H., Chen, J. A., Sayed, F., Ward, M. E., Gao, F., Nguyen, T. A., Krabbe, G., Sohn, P. D., Lo, I., Minami, S., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2939-14.2015 · Cited by 275 · see citing works

Nutrition Facts in Multiple Sclerosis

Riccio, P., & Rossano, R. (2015) · ASN NEURO · doi:10.1177/1759091414568185 · Cited by 232 · see citing works

Parkinson’s disease as a result of aging

Rodriguez, M., Rodriguez‐Sabate, C., Morales, I., Sanchez, A., & Sabate, M. (2015) · Aging Cell · doi:10.1111/acel.12312 · Cited by 214 · see citing works

Understanding the role of histone deacetylase and their inhibitors in neurodegenerative disorders: current targets and future perspective

Kumar, V., Kundu, S., Singh, A., & Singh, S. (2022) · Current Neuropharmacology · doi:10.2174/1570159x19666210609160017 · Cited by 210 · see citing works

Sirtuins' modulation of autophagy

Ng, F., & Tang, B. L. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24399 · Cited by 194 · see citing works

Mechanisms of white matter damage in multiple sclerosis

Lassmann, H. (2014) · Glia · doi:10.1002/glia.22597 · Cited by 191 · see citing works

SIRT1 in the brain—connections with aging-associated disorders and lifespan

Ng, F. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00064 · Cited by 185 · see citing works

Energy metabolism and energy-sensing pathways in mammalian embryonic and adult stem cell fate

Rafalski, V. A., Mancini, E., & Brunet, A. (2012) · Journal of Cell Science · doi:10.1242/jcs.114827 · Cited by 179 · see citing works

An exploratory double‐blind, randomized clinical trial with selisistat, a SirT1 inhibitor, in patients with H untington's disease

Süßmuth, S. D., Salman, H., Landwehrmeyer, G. B., Farmer, R. E., Frost, C. D., Tripepi, G., Andersen, C. A. F., Bacco, M. D., Lamanna, C., Diodato, E., et al. (2014) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12512 · Cited by 177 · see citing works

Epileptic brain fluorescent imaging reveals apigenin can relieve the myeloperoxidase-mediated oxidative stress and inhibit ferroptosis

Shao, C., Yuan, J., Liu, Y., Qin, Y., Wang, X., Gu, J., Chen, G., Zhang, B., Liu, H., Zhao, J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917946117 · Cited by 178 · see citing works

Role of mitochondrial homeostasis and dynamics in Alzheimer's disease

Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175 · see citing works

Antiageing strategy for neurodegenerative diseases: from mechanisms to clinical advances

Jiang, Q., Liu, J., Huang, S., Wang, X.-Y., Chen, X., Liu, G.-H., Ye, K., Song, W., Masters, C. L., Wang, J., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02145-7 · Cited by 165 · see citing works

Brain SIRT1 Mediates Metabolic Homeostasis and Neuroprotection

Xu, J., Jackson, C. W., Khoury, N., Escobar, I., & Pérez‐Pinzón, M. A. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00702 · Cited by 158 · see citing works

Dietary and Metabolic Control of Stem Cell Function in Physiology and Cancer

Mihaylova, M. M., Sabatini, D. M., & Yilmaz, Ö. H. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.02.008 · Cited by 153 · see citing works

Epigenetics Control Microglia Plasticity

Cheray, M., & Joseph, B. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00243 · Cited by 151 · see citing works

The Diversity of Histone Versus Nonhistone Sirtuin Substrates

Martínez‐Redondo, P., & Vaquero, A. (2013) · Genes & Cancer · doi:10.1177/1947601913483767 · Cited by 142 · see citing works

Effects of Resveratrol and other Polyphenols on Sirt1: Relevance to Brain Function During Aging

Sarubbo, F., Esteban, S., Miralles, A., & Moranta, D. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170703113212 · Cited by 144 · see citing works

Multiple Sclerosis: Molecular Mechanisms and Therapeutic Opportunities

Miljković, D. M., & Spasojević, I. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5068 · Cited by 136 · see citing works

Methamphetamine Downregulates Striatal Glutamate Receptors via Diverse Epigenetic Mechanisms

Jayanthi, S., McCoy, M. T., Chen, B., Britt, J. P., Kourrich, S., Yau, H., Ladenheim, B., Krasnova, I. N., Bonci, A., & Cadet, J. L. (2013) · Biological Psychiatry · doi:10.1016/j.biopsych.2013.09.034 · Cited by 133 · see citing works

Swimming exercise stimulates IGF1/ PI3K/Akt and AMPK/SIRT1/PGC1α survival signaling to suppress apoptosis and inflammation in aging hippocampus

Lin, J., Kuo, W., Baskaran, R., Kuo, C., Chen, Y., Chen, W. S., Ho, T., Day, C. H., Mahalakshmi, B., & Huang, C. (2020) · Aging · doi:10.18632/aging.103046 · Cited by 133 · see citing works

Sirtuin 1 activation protects against early brain injury after experimental subarachnoid hemorrhage in rats

Zhang, X., Wu, L., Wu, L.-Y., Ye, Z.-N., Jiang, T., Li, W., Zhuang, Z., Zhou, M., Hang, C., & Hang, C. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.292 · Cited by 132 · see citing works

Physical exercise improves synaptic dysfunction and recovers the loss of survival factors in 3xTg-AD mouse brain.

Revilla, S., Suñol, C., Garcia-Mesa, Y., Giménez-Llort, L., Sanfeliu, C., & Cristòfol, R. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.01.037 · Cited by 127 · see citing works

The DNA Damage Response in Neurons: Die by Apoptosis or Survive in a Senescence-Like State?

Fielder, E., von Zglinicki, T., & Jurk, D. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161221 · Cited by 126 · see citing works

A dietary regimen of caloric restriction or pharmacological activation of SIRT1 to delay the onset of neurodegeneration

Gräff, J., Kahn, M., Samiei, A., Gao, J., Ota, K. T., Rei, D., & Tsai, L.-H. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.5657-12.2013 · Cited by 124 · see citing works

The promise and perils of HDAC inhibitors in neurodegeneration

Didonna, A., & Opal, P. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.147 · Cited by 120 · see citing works

Cycloastragenol upregulates SIRT1 expression, attenuates apoptosis and suppresses neuroinflammation after brain ischemia

Li, M., Li, S., Dou, B., Zou, Y., Han, H., Liu, D.-X., Ke, Z., & Wang, Z. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0386-6 · Cited by 121 · see citing works

Mitochondria, the NLRP3 Inflammasome, and Sirtuins in Type 2 Diabetes: New Therapeutic TargetsReviewing Editors: Markus Bachschmid, Dylan Burger, Vittorio Calabrese, Amadou Camara, Lukas Kubala, Giuseppe Poli, and Chandan K. Sen

Rovira‐Llopis, S., Apostolova, N., Bañuls, C., Muntané, J., Rocha, M., & Víctor, V. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7313 · Cited by 120 · see citing works

Cerebroprotection by salvianolic acid B after experimental subarachnoid hemorrhage occurs via Nrf2- and SIRT1-dependent pathways

Zhang, X., Wu, Q., Lu, Y., Wan, J., Dai, H., Zhou, X., Lv, S., Chen, X., Zhang, X., Hang, C., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.035 · Cited by 118 · see citing works

Inflammation and immune cell abnormalities in intracranial aneurysm subarachnoid hemorrhage (SAH): Relevant signaling pathways and therapeutic strategies

Jin, J., Duan, J., Du, L., Xing, W., Peng, X., & Zhao, Q. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1027756 · Cited by 115 · see citing works

The role of citicoline in cognitive impairment: pharmacological characteristics, possible advantages, and doubts for an old drug with new perspectives

Gareri, P., Castagna, A., Cotroneo, A. M., Putignano, S., Sarro, G. D., & Bruni, A. C. (2015) · Clinical Interventions in Aging · doi:10.2147/cia.s87886 · Cited by 113 · see citing works

The role of SIRT1 in ocular aging

Mimura, T., Kaji, Y., Noma, H., Funatsu, H., & Okamoto, S. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.07.017 · Cited by 109 · see citing works

The Dynamics of the Mitochondrial Organelle as a Potential Therapeutic Target

Stetler, R. A., Leak, R. K., Gao, Y., & Chen, J. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.158 · Cited by 106 · see citing works

17β-Estradiol Modulates SIRT1 and Halts Oxidative Stress-Mediated Cognitive Impairment in a Male Aging Mouse Model

Khan, M., Ullah, R., Rehman, S. U., Shah, S. A., Saeed, K. M., Muhammad, T., Park, H. Y., Jo, M. H., Choe, K., Rutten, B. P. F., et al. (2019) · Cells · doi:10.3390/cells8080928 · Cited by 102 · see citing works

Longevity Pathways (mTOR, SIRT, Insulin/IGF-1) as Key Modulatory Targets on Aging and Neurodegeneration

Mazucanti, C. H., Cabral‐Costa, J. V., Vasconcelos, A. R., Andreotti, D. Z., Scavone, C., & Kawamoto, E. M. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150610125715 · Cited by 102 · see citing works

Interactions between Sirt1 and MAPKs regulate astrocyte activation induced by brain injury in vitro and in vivo

Li, D., Liu, N., Zhao, H., Zhang, X., Kawano, H., Liu, L., Zhao, L., & Li, H.-P. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0841-6 · Cited by 100 · see citing works

AMPK and SIRT1 activation contribute to inhibition of neuroinflammation by thymoquinone in BV2 microglia

Velagapudi, R., El‐Bakoush, A., Lepiarz‐Raba, I., Ogunrinade, F., & Olajide, O. A. (2017) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-017-3064-3 · Cited by 99 · see citing works

Unveiling the interplay of AMPK/SIRT1/PGC-1α axis in brain health: Promising targets against aging and NDDs

Rakshe, P. S., Dutta, B. J., Chib, S., Maurya, N., & Singh, S. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102255 · Cited by 103 · see citing works

Sirt1 regulates glial progenitor proliferation and regeneration in white matter after neonatal brain injury

Jablonska, B., Gierdalski, M., Chew, L., Hawley, T. S., Catron, M. A., Lichauco, A. M., Cabrera‐Luque, J., Yuen, T. J., Rowitch, D. H., & Gallo, V. (2016) · Nature Communications · doi:10.1038/ncomms13866 · Cited by 94 · see citing works

Brain Activation of SIRT1: Role in Neuropathology

Paraíso, A. F., Mendes, K. L., & Santos, S. H. S. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8459-x · Cited by 91 · see citing works

Lipidome analysis in multiple sclerosis reveals protein lipoxidative damage as a potential pathogenic mechanism

Gonzalo, H., Brieva, L., Tatzber, F., Jové, M., Cacabelos, D., Cassanyé, A., Lanau-Angulo, L., Boada, J., Serrano, J. C. E., González, C., et al. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07934.x · Cited by 87 · see citing works

SIRT1 attenuates blood-spinal cord barrier disruption after spinal cord injury by deacetylating p66Shc

Jiang, T., Qin, T., Gao, P., Tao, Z., Wang, X., Wu, M., Gu, J., Chu, B., Zheng, Z., Jiang, Y., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102615 · Cited by 89 · see citing works

Activation of SIRT1 by curcumin blocks the neurotoxicity of amyloid-β25–35 in rat cortical neurons

Sun, Q., Jia, N., Wang, W., Jin, H. M., Xu, J., & Hu, H. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.066 · Cited by 85 · see citing works

Resveratrol Promotes Mitochondrial Biogenesis and Protects against Seizure-Induced Neuronal Cell Damage in the Hippocampus Following Status Epilepticus by Activation of the PGC-1α Signaling Pathway

Chuang, Y., Chen, S., Hsu, C., Chen, S.-F., Chen, N.-C., & Jou, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040998 · Cited by 81 · see citing works

The role of sirtuin 1 in ageing and neurodegenerative disease: A molecular perspective

Thapa, R., Moglad, E. H. O., Afzal, M., Gupta, G., Bhat, A. A., Almalki, W. H., Kazmi, I. A., Alzarea, S. I., Pant, K., Singh, T. G., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102545 · Cited by 84 · see citing works

Ischemic Preconditioning Alters the Epigenetic Profile of the Brain from Ischemic Intolerance to Ischemic Tolerance

Thompson, J. W., Dave, K. R., Young, J. I., & Pérez‐Pinzón, M. A. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0202-9 · Cited by 79 · see citing works

SIRT3 a Major Player in Attenuation of Hepatic Ischemia‐Reperfusion Injury by Reducing ROS via Its Downstream Mediators: SOD2, CYP‐D, and HIF‐1α

Katwal, G., Baral, D., Fan, X., He, W., Zhang, X., Li, L., Xiong, Y., Ye, Q., & Wang, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2976957 · Cited by 78 · see citing works

Dietary polyphenols and neurogenesis: Molecular interactions and implication for brain ageing and cognition

Sarubbo, F., Moranta, D., & Pani, G. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.05.011 · Cited by 77 · see citing works

Cognitive Dysfunction in Huntington's Disease: Humans, Mouse Models and Molecular Mechanisms

Giralt, A., Saavedra, A., Alberch, J., & Pérez‐Navarro, E. (2012) · Journal of Huntington s Disease · doi:10.3233/jhd-120023 · Cited by 76 · see citing works

Hydrogen Sulfide Inhibits Formaldehyde-Induced Endoplasmic Reticulum Stress in PC12 Cells by Upregulation of SIRT-1

Li, X., Zhang, K., Zhang, P., Chen, L., Wang, L., Xie, M., Wang, C., & Tang, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089856 · Cited by 73 · see citing works

Positive effects of intermittent fasting in ischemic stroke

Fann, D., Ng, G., Poh, L., & Arumugam, T. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.01.014 · Cited by 66 · see citing works

Neurohormetic phytochemicals: An evolutionary–bioenergetic perspective

Murugaiyah, V., & Mattson, M. P. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.03.009 · Cited by 71 · see citing works

Up-regulation of microRNA-142 in simian immunodeficiency virus encephalitis leads to repression of sirtuin1

Chaudhuri, A. D., Yelamanchili, S. V., Marcondes, M. C. G., & Fox, H. S. (2013) · The FASEB Journal · doi:10.1096/fj.13-232678 · Cited by 67 · see citing works

Resveratrol Preconditioning Induces a Novel Extended Window of Ischemic Tolerance in the Mouse Brain

Koronowski, K. B., Dave, K. R., Saul, I., Camarena, V., Thompson, J. W., Neumann, J. T., Young, J. I., & Pérez‐Pinzón, M. A. (2015) · Stroke · doi:10.1161/strokeaha.115.009876 · Cited by 71 · see citing works

The multi‐faceted role of mitochondria in the pathology of Parkinson’s disease

Trinh, D., Israwi, A. R., Arathoon, L. R., Gleave, J. A., & Nash, J. E. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15154 · Cited by 72 · see citing works

Intrinsically disordered proteins and proteins with intrinsically disordered regions in neurodegenerative diseases

Coskuner‐Weber, O., Mirzanli, O., & Uversky, V. N. (2022) · Biophysical Reviews · doi:10.1007/s12551-022-00968-0 · Cited by 69 · see citing works

Sirt1 in cerebral ischemia

Pérez‐Pinzón, M. A., & Koronowski, K. B. (2015) · Brain Circulation · doi:10.4103/2394-8108.162532 · Cited by 69 · see citing works

Paeonol Ameliorates Diabetic Renal Fibrosis Through Promoting the Activation of the Nrf2/ARE Pathway via Up-Regulating Sirt1

Zhang, L., Chen, Z., Gong, W., Zou, Y., Xu, F., Chen, L., & Huang, H. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00512 · Cited by 69 · see citing works

Sirtuin 1 Regulates Mitochondrial Biogenesis and Provides an Endogenous Neuroprotective Mechanism Against Seizure-Induced Neuronal Cell Death in the Hippocampus Following Status Epilepticus

Chuang, Y., Chen, S., Jou, S., Lin, T., Chen, S.-F., Chen, N.-C., & Hsu, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143588 · Cited by 68 · see citing works

Exercise-Induced Benefits for Alzheimer’s Disease by Stimulating Mitophagy and Improving Mitochondrial Function

Liang, J., Wang, C., Zhang, H., Huang, J., Xie, J., & Chen, N. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.755665 · Cited by 66 · see citing works

Role of SIRT1 in autoimmune demyelination and neurodegeneration

Martin, A., Tegla, C., Cudrici, C. D., Kruszewski, A. M., Azimzadeh, P. N., Boodhoo, D., Mekala, A. P., Rus, V., & Rus, H. (2014) · Immunologic Research · doi:10.1007/s12026-014-8557-5 · Cited by 66 · see citing works

Minutes of PPAR-γ agonism and neuroprotection

Kumar, B. R. P., Kumar, A. P., Jose, J. A., Prabhakaran, P., Yuvaraj, S., Chipurupalli, S., Jeyarani, V., Manisha, C., Banerjee, S., Jeyabalan, J. B., et al. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104814 · Cited by 65 · see citing works

SIRT1 Promotes Neuronal Fortification in Neurodegenerative Diseases through Attenuation of Pathological Hallmarks and Enhancement of Cellular Lifespan

Mishra, P., Mittal, A. K., Kalonia, H., Madan, S., Ghosh, S., Sinha, J. K., & Rajput, S. K. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200729111744 · Cited by 68 · see citing works

Silent Information Regulator 2 Homolog 1 Counters Cerebral Hypoperfusion Injury by Deacetylating Endothelial Nitric Oxide Synthase

Hattori, Y., Okamoto, Y., Maki, T., Yamamoto, Y., Oishi, N., Yamahara, K., Nagatsuka, K., Takahashi, R., Kalaria, R. N., Fukuyama, H., et al. (2014) · Stroke · doi:10.1161/strokeaha.114.006265 · Cited by 63 · see citing works

New role of silent information regulator 1 in cerebral ischemia

Yang, Y., Duan, W., Li, Y., Yan, J., Yi, W., Liang, Z., Wang, N., Yi, D., & Jin, Z. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.06.008 · Cited by 61 · see citing works

Brain response to calorie restriction

Fusco, S., & Pani, G. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1223-y · Cited by 63 · see citing works

Role of Sirt1 During the Ageing Process: Relevance to Protection of Synapses in the Brain

Godoy, J. A., Zolezzi, J. M., Braidy, N., & Inestrosa, N. C. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8645-5 · Cited by 60 · see citing works

The Citicholinage Study: Citicoline Plus Cholinesterase Inhibitors in Aged Patients Affected with Alzheimer’s Disease Study

Gareri, P., Castagna, A., Cotroneo, A. M., Putignano, D., Conforti, R., Santamaria, F., Marino, S., & Putignano, S. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160808 · Cited by 62 · see citing works

Hydrogen Sulfide Inhibits Chronic Unpredictable Mild Stress-Induced Depressive-Like Behavior by Upregulation of Sirt-1: Involvement in Suppression of Hippocampal Endoplasmic Reticulum Stress

Liu, S., Li, D., Zeng, H.-Y., Kan, L.-Y., Zou, W., Zhang, P., Gu, H., & Tang, X. (2017) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyx030 · Cited by 58 · see citing works

Targeting Sirtuin-1 in Huntington’s Disease: Rationale and Current Status

Duan, W. (2013) · CNS Drugs · doi:10.1007/s40263-013-0055-0 · Cited by 54 · see citing works

Salidroside reduces neuropathology in Alzheimer’s disease models by targeting NRF2/SIRT3 pathway

Yao, Y., Ren, Z., Yang, R., Mei, Y., Dai, Y., Cheng, Q., Xu, C., Xu, X., Wang, S., Kim, K. M., et al. (2022) · Cell & Bioscience · doi:10.1186/s13578-022-00918-z · Cited by 52 · see citing works

Decreased expression of sirtuin 6 is associated with release of high mobility group box-1 after cerebral ischemia

Lee, O.-H., Kim, J., Kim, J.-M., Lee, H., Kim, E. H., Bae, S., Choi, Y., Nam, H. S., & Heo, J. H. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.07.085 · Cited by 52 · see citing works

Tissue-specific deregulation of selected HDACs characterizes ALS progression in mouse models: pharmacological characterization of SIRT1 and SIRT2 pathways

Valle, C., Salvatori, I., Gerbino, V., Rossi, S., Palamiuc, L., René, F., & Carrı̀, M. T. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.247 · Cited by 52 · see citing works

Targeting Sirtuins: Substrate Specificity and Inhibitor Design

Rajabi, N., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.11.003 · Cited by 52 · see citing works

Cadmium, an Environmental Contaminant, Exacerbates Alzheimer’s Pathology in the Aged Mice’s Brain

Ali, T., Khan, A., Alam, S. I., Ahmad, S., Ikram, M. A., Park, J. S., Lee, H. J., & Kim, M. O. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.650930 · Cited by 51 · see citing works

Yoga improves mitochondrial health and reduces severity of autoimmune inflammatory arthritis: A randomized controlled trial

Gautam, S., Kumar, U., Kumar, M., Rana, D., & Dada, R. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.03.004 · Cited by 53 · see citing works

The epigenetic regulation of HIF-1α by SIRT1 in MPP + treated SH-SY5Y cells

Dong, S., Guo, Y., Feng, Y., Cui, X., Kuo, S., Liu, T., & Wu, Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.01.013 · Cited by 49 · see citing works

SIRT1 mediates Sphk1/S1P-induced proliferation and migration of endothelial cells

Gao, Z., Wang, H., Xiao, F., Shi, X., Zhang, Y., Xu, Q. Q., Zhang, X.-Y., Ha, X., & Wang, L. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.02.018 · Cited by 47 · see citing works

Towards a ‘systems’-level understanding of the nervous system and its disorders

Qureshi, I., & Mehler, M. F. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.07.003 · Cited by 46 · see citing works

Sirtuins and their interactions with transcription factors and poly(ADP-ribose) polymerases

Jęśko, H. M., & Strosznajder, R. P. (2016) · Folia Neuropathologica · doi:10.5114/fn.2016.62531 · Cited by 44 · see citing works

Neuroprotective effect of salidroside against central nervous system inflammation‐induced cognitive deficits: A pivotal role of sirtuin 1‐dependent N rf‐2/ HO ‐1/ NF ‐κ B pathway

Xu, N., Huang, F., Jian, C., Qin, L., Lu, F. Y., Wang, Y., Zhang, Z., & Zhang, Q. (2019) · Phytotherapy Research · doi:10.1002/ptr.6335 · Cited by 44 · see citing works

Effects of Resveratrol Supplementation on the Cognitive Function of Patients with Alzheimer's Disease: A Systematic Review of Randomized Controlled Trials

Tosatti, J. A. G., Fontes, A. F. D. S., Caramelli, P., & Gomes, K. B. (2022) · Drugs & Aging · doi:10.1007/s40266-022-00923-4 · Cited by 43 · see citing works

SIRT1 inhibition by sirtinol aggravates brain edema after experimental subarachnoid hemorrhage

Zhou, X., Zhang, X., Zhang, X., Zhuang, Z., Li, W., Sun, Q., Li, T., Wang, C., Zhu, L., Shi, J., et al. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23359 · Cited by 42 · see citing works

SIRT1 mediates salidroside‐elicited protective effects against MPP + ‐induced apoptosis and oxidative stress in SH‐SY5Y cells: involvement in suppressing MAPK pathways

Wang, C., Sun, Z., Wang, M., & Zhang, C. (2017) · Cell Biology International · doi:10.1002/cbin.10864 · Cited by 42 · see citing works

The CITIRIVAD Study: CITIcoline plus RIVAstigmine in Elderly Patients Affected with Dementia Study

Castagna, A., Cotroneo, A. M., Ruotolo, G., & Gareri, P. (2016) · Clinical Drug Investigation · doi:10.1007/s40261-016-0454-3 · Cited by 41 · see citing works

Fucoxanthin Mitigates Subarachnoid Hemorrhage-Induced Oxidative Damage via Sirtuin 1-Dependent Pathway

Zhang, X., Lu, Y., Tao, T., Wang, H., Liu, G., Liu, X.-Z., Liu, C., Xia, D., Hang, C., & Li, W. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02095-x · Cited by 41 · see citing works

Why Is Longevity Still a Scientific Mystery? Sirtuins—Past, Present and Future

Ziętara, P., Dziewięcka, M., & Augustyniak, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010728 · Cited by 40 · see citing works

Neuromuscular and Systemic Presentations in Adults: diagnoses beyond MERRF and MELAS

Cohen, B. H. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0188-3 · Cited by 41 · see citing works

Sirtuins as modifiers of Parkinson's disease pathology

Tang, B. L. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23806 · Cited by 40 · see citing works

Targeting Sirtuin 1 signaling pathway by ginsenosides

Lou, T., Huang, Q., Su, H., Zhao, D., & Li, X. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113657 · Cited by 40 · see citing works

Blocking SIRT1 inhibits cell proliferation and promotes aging through the PI3K/AKT pathway

Li, H., & Wang, R. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.09.037 · Cited by 39 · see citing works

Multiple beneficial effects of melanocortin MC4 receptor agonists in experimental neurodegenerative disorders: Therapeutic perspectives

Giuliani, D., Ottani, A., Neri, L., Zaffe, D., Grieco, P., Jochem, J., Cavallini, G. M., Catania, A., & Guarini, S. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.11.004 · Cited by 38 · see citing works

SIRT1 Mediates Melatonin’s Effects on Microglial Activation in Hypoxia: In Vitro and In Vivo Evidence

Merlo, S., Luaces, J. P., Spampinato, S. F., Toro-Urrego, N., Caruso, G. I., D’Amico, F., Capani, F., & Sortino, M. A. (2020) · Biomolecules · doi:10.3390/biom10030364 · Cited by 38 · see citing works

Rhapontin ameliorates colonic epithelial dysfunction in experimental colitis through SIRT1 signaling

Wei, W., Wang, L., Zhou, K., Xie, H., Zhang, M., & Zhang, C. (2016) · International Immunopharmacology · doi:10.1016/j.intimp.2016.11.024 · Cited by 35 · see citing works

Activating Sirt1 by resveratrol suppresses Nav1.7 expression in DRG through miR-182 and alleviates neuropathic pain in rats

Jia, Q., Dong, W., Zhang, L., & Yang, X. (2020) · Channels · doi:10.1080/19336950.2020.1732003 · Cited by 35 · see citing works

SIRT1 Decreases Emotional Pain Vulnerability with Associated CaMKIIα Deacetylation in Central Amygdala

Zhou, C., Wu, Y., Ding, X., Shi, N., Cai, Y., & Pan, Z. Z. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1259-19.2020 · Cited by 35 · see citing works

SIRT1-Dependent Upregulation of BDNF in Human Microglia Challenged with Aβ: An Early but Transient Response Rescued by Melatonin

Caruso, G. I., Spampinato, S. F., Costantino, G., Merlo, S., & Sortino, M. A. (2021) · Biomedicines · doi:10.3390/biomedicines9050466 · Cited by 34 · see citing works

Sirtuins in neurodegenerative diseases

Sachan, N., Ali, Z., Fatma, N., & Chandra, P. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-45380-9.00002-x

Neuronal protection by sirtuins in Alzheimer's disease

Anekonda, T. S., & Reddy, P. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03492.x · Cited by 150 · see citing works

Targeting sirtuins in neurological disorders: A comprehensive review

Zhang, S.-Y., Yang, N., Hao, P.-H., Wen, R., & Zhang, T. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.139258 · Cited by 19 · see citing works

Sirtuins in Neuroendocrine Regulation and Neurological Diseases

Fujita, Y., & Yamashita, T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00778 · Cited by 109 · see citing works

Sirtuins in neurodegenerative diseases: an update on potential mechanisms

Min, S., Sohn, P., Cho, S.-H., Swanson, R. A., & Gan, L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00053 · Cited by 123 · see citing works