Sirtuin Functions in Health and Disease

Alzheimer's disease: the amyloid cascade hypothesis

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Alzheimer's Disease: Genes, Proteins, and Therapy

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Amyloid plaque core protein in Alzheimer disease and Down syndrome.

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Resveratrol improves health and survival of mice on a high-calorie diet

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Resveratrol Improves Mitochondrial Function and Protects against Metabolic Disease by Activating SIRT1 and PGC-1α

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Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

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Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

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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

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

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hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

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

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Suppression of Reactive Oxygen Species and Neurodegeneration by the PGC-1 Transcriptional Coactivators

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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

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RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease

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

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The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans

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Sirtuin activators mimic caloric restriction and delay ageing in metazoans

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

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

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

The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase

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daf-16 : An HNF-3/forkhead Family Member That Can Function to Double the Life-Span of Caenorhabditis elegans

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Extrachromosomal rDNA circles—a cause of aging in yeast

Sinclair, D. A., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80493-6 · Cited by 1,500

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 1,497

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

Amyotrophic lateral sclerosis is a distal axonopathy: evidence in mice and man

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

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Untitled work

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ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease

Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303

Axonopathy and Transport Deficits Early in the Pathogenesis of Alzheimer’s Disease

Stokin, G. B., Lillo, C., Falzone, T. L., Brusch, R. G., Rockenstein, E., Mount, S. L., Raman, R., Davies, P., Masliah, E., Williams, D. S., et al. (2005) · Science · doi:10.1126/science.1105681 · Cited by 1,214

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

Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression

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Post‐translational modifications and activation of p53 by genotoxic stresses

Appella, E., & Anderson, C. W. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02225.x · Cited by 1,095

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

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Protein Kinase B Kinases That Mediate Phosphatidylinositol 3,4,5-Trisphosphate-Dependent Activation of Protein Kinase B

Stephens, L., Anderson, K. E., Stokoe, D., Erdjument‐Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F. P., Tempst, P., et al. (1998) · Science · doi:10.1126/science.279.5351.710 · Cited by 1,061

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

Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration

Lin, S.-J., Kaeberlein, M., Andalis, A. A., Sturtz, L. A., Defossez, P.-A., Culotta, V. C., Fink, G. R., & Guarente, L. (2002) · Nature · doi:10.1038/nature00829 · Cited by 1,057

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

Calorie restriction, SIRT1 and metabolism: understanding longevity

Bordone, L., & Guarente, L. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1616 · Cited by 1,038

Transcriptional Repression of PGC-1α by Mutant Huntingtin Leads to Mitochondrial Dysfunction and Neurodegeneration

Cui, L., Jeong, H., Borovecki, F., Parkhurst, C. N., Tanese, N., & Krainc, D. (2006) · Cell · doi:10.1016/j.cell.2006.09.015 · Cited by 1,012

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

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

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Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin.

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PML regulates p53 acetylation and premature senescence induced by oncogenic Ras

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Human SIR2 deacetylates p53 and antagonizes PML/p53‐induced cellular senescence

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Requirement of mammalian DNA polymerase-β in base-excision repair

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Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity

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Amyloid β-Protein and the Genetics of Alzheimer's Disease

Selkoe, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18295 · Cited by 805

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

Discoveries of Nicotinamide Riboside as a Nutrient and Conserved NRK Genes Establish a Preiss-Handler Independent Route to NAD+ in Fungi and Humans

Bieganowski, P., & Brenner, C. (2004) · Cell · doi:10.1016/s0092-8674(04)00416-7 · Cited by 750

Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation

Brooks, C. L., & Gu, W. J. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00003-6 · Cited by 746

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

Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae

Anderson, R. M., Bitterman, K. J., Wood, J. G., Medvedik, O., & Sinclair, D. A. (2003) · Nature · doi:10.1038/nature01578 · Cited by 736

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

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

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

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

Axonal Self-Destruction and Neurodegeneration

Raff, M., Whitmore, A., & Finn, J. (2002) · Science · doi:10.1126/science.1068613 · Cited by 670

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

Absence of Wallerian Degeneration does not Hinder Regeneration in Peripheral Nerve

Lunn, E. R., Perry, V. H., Brown, M. C., Rosen, H., & Gordon, S. (1989) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1989.tb00771.x · Cited by 646

Diet‐induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease

Ho, L., Qin, W., Pompl, P. N., Xiang, Z., Wang, J., Zhao, Z., Peng, Y., Cambareri, G. M., Rocher, A. B., Mobbs, C. V., et al. (2004) · The FASEB Journal · doi:10.1096/fj.03-0978fje · Cited by 640

Increased dosage of mammalian Sir2 in pancreatic β cells enhances glucose-stimulated insulin secretion in mice

Moynihan, K. A., Grimm, A. A., Plueger, M. M., Bernal‐Mizrachi, E., Ford, E. L., CRAS-MÉNEUR, C. M. H., Permutt, M. A., & Imai, S. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.07.001 · Cited by 638

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 & Development · doi:10.1101/gad.1164804 · Cited by 632

Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription

Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L. (2006) · Genes & Development · doi:10.1101/gad.1399706 · Cited by 629

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

Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity

Daitoku, H., Hatta, M., Matsuzaki, H., Aratani, S., Ohshima, T., Miyagishi, M., Nakajima, T., & Fukamizu, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400593101 · Cited by 616

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

The Mammalian SIR2α Protein Has a Role in Embryogenesis and Gametogenesis

McBurney, M. W., Yang, X., Jardine, K., Hixon, M., Boekelheide, K., Webb, J. R., Lansdorp, P. M., & Lemieux, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.38-54.2003 · Cited by 611

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

Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State

Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 591

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

Thermoregulatory and metabolic defects in Huntington's disease transgenic mice implicate PGC-1α in Huntington's disease neurodegeneration

Weydt, P., Pineda, V. V., Torrence, A. E., Libby, R. T., Satterfield, T. F., Lazarowski, E. R., Gilbert, M. L., Morton, G. J., Bammler, T. K., Strand, A. D., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.10.004 · Cited by 562

14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport

Brunet, A., Kanai, F., Stehn, J. R., Xu, J., Sarbassova, D. A., Frangioni, J. V., Dalal, S. N., DeCaprio, J. A., Greenberg, M. E., & Yaffe, M. B. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200112059 · Cited by 562

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

FOXO4 Is Acetylated upon Peroxide Stress and Deacetylated by the Longevity Protein hSir2

van der Horst, A., Tertoolen, L. G. J., Smits, L. M. M., Frye, R. A., Medema, R. H., & Burgering, B. M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401138200 · Cited by 553

Take five—BACE and the γ‐secretase quartet conduct Alzheimer's amyloid β‐peptide generation

Haass, C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600061 · Cited by 547

Nuclear Trapping of the Forkhead Transcription Factor FoxO1 via Sirt-dependent Deacetylation Promotes Expression of Glucogenetic Genes

Frescas, D., Valenti, L. V. C., & Accili, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412357200 · Cited by 541

A Conserved Regulatory System for Aging

Kenyon, C. J. (2001) · Cell · doi:10.1016/s0092-8674(01)00306-3 · Cited by 529

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 518

Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle

Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S., & Tainsky, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.9.3173-3185.2003 · Cited by 506

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 489

Caloric Intake and the Risk of Alzheimer Disease

Luchsinger, J. A., Tang, M., Shea, S. A., & Mayeux, R. P. (2002) · Archives of Neurology · doi:10.1001/archneur.59.8.1258 · Cited by 470

PPARγ AND G LUCOSE H OMEOSTASIS

Picard, F., & Auwerx, J. H. (2002) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.22.010402.102808 · Cited by 412

An Enzymatic Activity in the Yeast Sir2 Protein that Is Essential for Gene Silencing

Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H., & Moazed, D. (1999) · Cell · doi:10.1016/s0092-8674(00)81671-2 · Cited by 391

Caloric restriction increases neurotrophic factor levels and attenuates neurochemical and behavioral deficits in a primate model of Parkinson's disease

Maswood, N., Young, J., Tilmont, E. M., Zhang, Z., Gash, D. M., Gerhardt, G. A., Grondin, R., Roth, G. S., Mattison, J. A., Lane, M. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405831102 · Cited by 383

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

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

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Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B

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The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity

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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

Copper-Dependent Inhibition of Human Cytochrome c Oxidase by a Dimeric Conformer of Amyloid-β1-42

Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327

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 324

Splicing regulates NAD metabolite binding to histone macroH2A

Kustatscher, G., Hothorn, M., Pugieux, C., Scheffzek, K., & Ladurner, A. G. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb956 · Cited by 300

14-3-3 proteins; bringing new definitions to scaffolding

Tzivion, G., Shen, Y. H., & Zhu, J. (2001) · Oncogene · doi:10.1038/sj.onc.1204777 · Cited by 300

Acetyl-CoA Synthetase 2, a Mitochondrial Matrix Enzyme Involved in the Oxidation of Acetate

Fujino, T., Kondo, J., Ishikawa, M., Morikawa, K., & Yamamoto, T. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008782200 · Cited by 298

Regulation of MEF2 by Histone Deacetylase 4- and SIRT1 Deacetylase-Mediated Lysine Modifications

Zhao, X., Sternsdorf, T., Bolger, T. A., Evans, R. M., & Yao, T.-P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8456-8464.2005 · Cited by 264

The molecular biology of the SIR proteins

Gasser, S. M., & Cockell, M. M. (2001) · Gene · doi:10.1016/s0378-1119(01)00741-7 · Cited by 263

Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation sites in regulating 14-3-3 binding, transactivation and nuclear targetting

Rena, G., Prescott, A. R., Guo, S., Cohen, P., & Unterman, T. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3540605 · Cited by 263

Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene

Hiratsuka, M., Inoue, T., Toda, T., Kimura, N., Shirayoshi, Y., Kamitani, H., Watanabe, T., Ohama, E., Tahimic, C. G. T., Kurimasa, A., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.029 · Cited by 261

Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation

Liou, G., Tanny, J. C., Kruger, R. G., Walz, T., & Moazed, D. (2005) · Cell · doi:10.1016/j.cell.2005.03.035 · Cited by 260

Mammalian SIRT1 limits replicative life span in response to chronic genotoxic stress

Chua, K. F., Mostoslavsky, R., Lombard, D. B., Pang, W. W., Saito, S., Franco, S., Kaushal, D., Cheng, H.-L., Fischer, M. R., Stokes, N., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.06.007 · Cited by 258

A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the slow Wallerian degeneration ( Wld 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

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 249

The Energetics of Huntington's Disease

Browne, S. E., & Beal, M. F. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000014824.04728.dd · Cited by 240

Hormonal Control of Androgen Receptor Function through SIRT1

Fu, M., Liu, M., Sauve, A. A., Jiao, X., Zhang, X., Wu, X., Powell, M. J., Yang, T., Gu, W. J., Avantaggiati, M. L., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00289-06 · Cited by 234

HST2 Mediates SIR2 -Independent Life-Span Extension by Calorie Restriction

Lamming, D. W., Latorre‐Esteves, M., Medvedik, O., Wong, S. N., Tsang, F. A., Wang, C., Lin, S.-J., & Sinclair, D. A. (2005) · Science · doi:10.1126/science.1113611 · Cited by 227

The role of the tumor suppressor p53 in spermatogenesis

Beumer, T. L., Roepers‐Gajadien, H. L., Gademan, I. S., van Buul, P. P. W., Gil‐Gómez, G., Rutgers, D. H., & de Rooij, D. G. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400396 · Cited by 221

Phosphatidylinositol 3-Kinase Signaling Inhibits DAF-16 DNA Binding and Function via 14-3-3-dependent and 14-3-3-independent Pathways

Cahill, C. M., Tzivion, G., Nasrin, N., Ogg, S., Dore, J., Ruvkun, G., & Alexander-Bridges, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010042200 · Cited by 219

Substrate Specificity and Kinetic Mechanism of the Sir2 Family of NAD+-Dependent Histone/Protein Deacetylases

Borra, M. T., Langer, M. R., Slama, J. T., & Denu, J. M. (2004) · Biochemistry · doi:10.1021/bi049592e · Cited by 217

Linking chromatin function with metabolic networks: Sir2 family of NAD+-dependent deacetylases

Denu, J. M. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00005-1 · Cited by 210

Tumor Necrosis Factor Death Receptor Signaling Cascade Is Required for Amyloid-β Protein-Induced Neuron Death

Li, R., Yang, L., Lindholm, K., Konishi, Y., Yue, X., Hampel, H., Zhang, D., & Shen, Y. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4580-03.2004 · Cited by 177

In Vivo Imaging of Reactive Oxygen Species Specifically Associated with Thioflavine S-Positive Amyloid Plaques by Multiphoton Microscopy

McLellan, M. E., Kajdasz, S. T., Hyman, B. T., & Bacskai, B. J. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-06-02212.2003 · Cited by 174

The retardation of aging by caloric restriction: its significance in the transgenic era

Barger, J. L., Walford, R. L., & Weindruch, R. (2003) · Experimental Gerontology · doi:10.1016/j.exger.2003.10.017 · Cited by 160

Small molecule regulation of Sir2 protein deacetylases

Grubisha, O., Smith, B. C., & Denu, J. M. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04862.x · Cited by 131

PPAR∞ AND GLUCOSE HOMEOSTASIS

Auwerx, J. H. (2002) · Cited by 127

Insulin Resistance, Affective Disorders, and Alzheimer's Disease: Review and Hypothesis

Rasgon, N., & Jarvik, L. F. (2004) · The Journals of Gerontology Series A · doi:10.1093/gerona/59.2.m178 · Cited by 123

Sir2 Protein Deacetylases: Evidence for Chemical Intermediates and Functions of a Conserved Histidine

Smith, B. C., & Denu, J. M. (2005) · Biochemistry · doi:10.1021/bi052014t · Cited by 102

Disorders of glutamate metabolism

Kelly, A. T., & Stanley, C. A. (2001) · Mental Retardation and Developmental Disabilities Research Reviews · doi:10.1002/mrdd.1040 · Cited by 100

Severe ultrastructural mitochondrial changes in lymphoblasts homozygous for Huntington disease mutation

Squitieri, F., Cannella, M., Sgarbi, G., Maglione, V., Falleni, A., Lenzi, P., Baracca, A., Cislaghi, G., Carsten Saft, C., Ragona, G., et al. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.09.010 · Cited by 96

Erratum: Isolation of a SIR-like gene, SIR-T8, that is overexpressed in thyroid carcinoma cell lines and tissues

de Nigris, F., Cerutti, J. M., Morelli, C., Califano, D., Chiariotti, L., Viglietto, G., Santelli, G., & Fusco, A. (2002) · British Journal of Cancer · doi:10.1038/sj.bjc.6600636 · Cited by 78

Transcriptional regulation of the Saccharomyces cerevisiae DAL5 gene family and identification of the high affinity nicotinic acid permease TNA1 (YGR260w)

Llorente, B., & Dujon, B. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01698-7 · Cited by 77

Isolation of a SIR-like gene, SIR-T8, that is overexpressed in thyroid carcinoma cell lines and tissues

de Nigris, F., Cerutti, J. M., Morelli, C., Califano, D., Chiariotti, L., Viglietto, G., Santelli, G., & Fusco, A. (2002) · British Journal of Cancer · doi:10.1038/sj.bjc.6600156 · Cited by 45

Reactive oxygen species, cellular redox systems, and apoptosis

Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340

Dietary factors and low-grade inflammation in relation to overweight and obesity

Calder, P. C., Ahluwalia, N., Brouns, F., Buetler, T., Clement, K., Cunningham, K., Esposito, K., Jönsson, L. S., Kolb, H., Lansink, M., et al. (2011) · British Journal of Nutrition · doi:10.1017/s0007114511005460 · Cited by 1,098

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 818

Salidroside Attenuates Ventilation Induced Lung Injury via SIRT1-Dependent Inhibition of NLRP3 Inflammasome

Wang, Y., Xu, C.-F., Liu, Y.-J., Mao, Y.-F., Lv, Z., Li, S.-Y., Zhu, X.-Y., & Jiang, L. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000477112 · Cited by 838

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

The Role of Sirtuins in Cell Life and their Potential Therapeutic Uses.

Méndez, L. C. C., García, A., & Franco‐Montoya, L. N. (2023) · PubMed

Sirtuin Modulators: Mechanisms and Potential Clinical Implications

Sánchez‐Fidalgo, S., Villegas, I., Sánchéz‐Hidalgo, M., & de la Lastra, C. A. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712800269272 · Cited by 47

Function of SIRT1 in physiology

Kong, X., Wang, R., Liu, X., Zhu, L., Shao, D., Chang, Y., & Fang, F. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909070013 · Cited by 28

Biological and Potential Therapeutic Roles of Sirtuin Deacetylases

Taylor, D. M., Maxwell, M. M., Luthi‐Carter, R., & Kazantsev, A. G. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8357-y · Cited by 146

SIRT Family: Biological Functions and Therapeutic Targets

Wang, J., Jiang, F., ZHANG, F.-Y., Huang, D., Li, X. G., Gao, S., You, H., Wu, Q., Chen, H., & Gong, T. Q. (2026) · MedComm · doi:10.1002/mco2.70866 · Cited by 2