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 · 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

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

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

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

Ogg, S., Paradis, S., Gottlieb, S., Patterson, G. I., Lee, L., Tissenbaum, H. A., & Ruvkun, G. (1997) · Nature · doi:10.1038/40194 · Cited by 1,935 · 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

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

Genomic Instability and Aging-like Phenotype in the Absence of Mammalian SIRT6

Mostoslavsky, R., Chua, K. F., Lombard, D. B., Pang, W. W., Fischer, M. R., Gellon, L., Liu, P., Mostoslavsky, G., Franco, S., Murphy, M. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.044 · Cited by 1,637 · see citing works

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

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Extrachromosomal rDNA circles—a cause of aging in yeast

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

Lin, K., Dorman, J. B., Rodan, A. R., & Kenyon, C. J. (1997) · Science · doi:10.1126/science.278.5341.1319 · Cited by 1,496 · see citing works

The Sir2 Family of Protein Deacetylases

Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,496 · see citing works

Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins

Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works

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

Untitled work

(2004) · doi:10.1016/s0092-8674(04)00452-0 · Cited by 1,356 · see citing works

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

Fischer, L. R., Culver, D. G., Tennant, P., Davis, A. A., Wang, M.-S., Castellano-Sanchez, A. A., Khan, J., Polak, M. A., & Glass, J. D. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2003.10.004 · Cited by 1,338 · see citing works

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 · see citing works

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 · 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

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

Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · 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

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 1,071 · see citing works

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 · 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

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 · 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

Calorie restriction, SIRT1 and metabolism: understanding longevity

Bordone, L., & Guarente, L. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1616 · Cited by 1,021 · see citing works

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 · see citing works

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

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

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

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

Vaquero, A., Scher, M., Lee, D., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.031 · Cited by 916 · see citing works

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

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PML regulates p53 acetylation and premature senescence induced by oncogenic Ras

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

Sobol, R. W., Horton, J. K., Kühn, R., Gu, H., Singhal, R. K., Prasad, R., Rajewsky, K., & Wilson, S. H. (1996) · Nature · doi:10.1038/379183a0 · Cited by 834 · see citing works

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

Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809 · see citing works

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 798 · 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

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 · see citing works

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 742 · 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

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 · 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

Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells

Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715 · see citing works

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

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

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

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

Axonal Self-Destruction and Neurodegeneration

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

SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosisPreprint

Vaquero, A., Scher, M. B., Lee, D. H., Sutton, A., Cheng, H.-L., Alt, F. W., Serrano, L., Sternglanz, R., & Reinberg, D. (2006) · Genes & Development · doi:10.1101/gad.1412706 · Cited by 670 · see citing works

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 · see citing works

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

Ho, L., Qin, W., Pompl, P., Xiang, Z.-M., Wang, J., Zhao, Z., Peng, Y., Cambareri, G., Rocher, A., Mobbs, C., et al. (2004) · The FASEB Journal · doi:10.1096/fj.03-0978fje · Cited by 646 · 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

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 630 · see citing works

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

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

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

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

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

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 · see citing works

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 602 · see citing works

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

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

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 590 · see citing works

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

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

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 · see citing works

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 · 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

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

Frescas, D., Valenti, L. N., & Accili, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412357200 · Cited by 554 · see citing works

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 550 · 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 545 · see citing works

A Conserved Regulatory System for Aging

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

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 500 · see citing works

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

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

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Structure of the histone deacetylase SIRT2.

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

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SirT1 Regulates Energy Metabolism and Response to Caloric Restriction in Mice

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SIRT1 induces EMT by cooperating with EMT transcription factors and enhances prostate cancer cell migration and metastasis

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Vascular Smooth Muscle Cell Sirtuin 1 Protects Against DNA Damage and Inhibits Atherosclerosis

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Stealing the Keys to the Kitchen: Viral Manipulation of the Host Cell Metabolic Network

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Resveratrol attenuates doxorubicin-induced cardiomyocyte apoptosis in mice through SIRT1-mediated deacetylation of p53

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High Glucose Induced Alteration of SIRTs in Endothelial Cells Causes Rapid Aging in a p300 and FOXO Regulated Pathway

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

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Development of vorinostat: Current applications and future perspectives for cancer therapy

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Nicotinamide mononucleotide adenylyltransferase expression in mitochondrial matrix delays Wallerian degeneration

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

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The Poly(ADP-ribose) Polymerase PARP-1 Is Required for Oxidative Stress-induced TRPM2 Activation in Lymphocytes

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Resveratrol Modulates Tumor Cell Proliferation and Protein Translation via SIRT1-Dependent AMPK Activation

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