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Volumn 17, Issue 26, 2010, Pages 2921-2932

Sirtuin family: A link to metabolic signaling and senescence

Author keywords

Cellular senescence; Histone deacetylase; Lifespan; Metabolism; Nad; Oaadpr; P53; Resveratrol

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE ACETATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; RESVERATROL; SIRTUIN;

EID: 77955608578     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986710792065009     Document Type: Article
Times cited : (25)

References (125)
  • 1
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann, C.B.; Sherman, J.M.; Devine, S.E.; Cameron, E.E.; Pillus, L.; Boeke, J.D. The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev., 1995, 9, 2888-2902.
    • (1995) Genes Dev , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5    Boeke, J.D.6
  • 2
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nu-cleosome acetylation
    • Braunstein, M.; Rose, A.B.; Holmes, S.G.; Allis, C.D.; Broach, J.R. Transcriptional silencing in yeast is associated with reduced nu-cleosome acetylation. Genes Dev., 1993, 7, 592-604.
    • (1993) Genes Dev , vol.7 , pp. 592-604
    • Braunstein, M.1    Rose, A.B.2    Holmes, S.G.3    Allis, C.D.4    Broach, J.R.5
  • 3
    • 0024536650 scopus 로고
    • A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA
    • Gottlieb, S.; Esposito, R.E. A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA. Cell, 1989, 56, 771-776.
    • (1989) Cell , vol.56 , pp. 771-776
    • Gottlieb, S.1    Esposito, R.E.2
  • 4
    • 0033600176 scopus 로고    scopus 로고
    • 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. 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. Bio-chem. Biophys. Res. Commun., 1999, 260, 273-279.
    • (1999) Bio-chem. Biophys. Res. Commun , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 5
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukary-otic Sir2-like proteins
    • Frye, R.A. Phylogenetic classification of prokaryotic and eukary-otic Sir2-like proteins. Biochem. Biophys. Res. Commun., 2000, 273, 793-798.
    • (2000) Biochem. Biophys. Res. Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 7
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • Lin, S.J.; Guarente, L. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr. Opin. Cell Biol., 2003, 15, 241-246.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 8
    • 0041755793 scopus 로고
    • Is longevity compatible with optimum growth?
    • McCay, C.M. Is longevity compatible with optimum growth? Science, 1933, 77, 410-411.
    • (1933) Science , vol.77 , pp. 410-411
    • McCay, C.M.1
  • 9
    • 84882139840 scopus 로고
    • Effect of Restricted Feeding Upon Aging and Chronic Diseases in Rats and Dogs
    • McCay, C.M. Effect of Restricted Feeding Upon Aging and Chronic Diseases in Rats and Dogs. Am. J. Public Health Nations Health, 1947, 37, 521-528.
    • (1947) Am. J. Public Health Nations Health , vol.37 , pp. 521-528
    • McCay, C.M.1
  • 11
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M.; McVey, M.; Guarente, L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev., 1999, 13, 2570-2580.
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 12
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomy-ces cerevisiae
    • Lin, S.J.; Defossez, P.A.; Guarente, L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomy-ces cerevisiae. Science, 2000, 289, 2126-2128.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 13
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum, H.A.; Guarente, L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature, 2001, 410, 227-230.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 14
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina, B.; Helfand, S.L. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. U.S.A., 2004, 101, 15998-16003.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 15
    • 58849158388 scopus 로고    scopus 로고
    • How does SIRT1 affect metabolism, senescence and cancer?
    • Brooks, C.L.; Gu, W. How does SIRT1 affect metabolism, senescence and cancer? Nat. Rev. Cancer, 2009, 9, 123-128.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 123-128
    • Brooks, C.L.1    Gu, W.2
  • 16
    • 67749122294 scopus 로고    scopus 로고
    • Stress-induced premature senescence of endothelial cells: A perilous state between recovery and point of no return
    • Goligorsky, M.S.; Chen, J.; Patschan, S. Stress-induced premature senescence of endothelial cells: a perilous state between recovery and point of no return. Curr. Opin. Hematol., 2009, 16, 215-219.
    • (2009) Curr. Opin. Hematol , vol.16 , pp. 215-219
    • Goligorsky, M.S.1    Chen, J.2    Patschan, S.3
  • 17
    • 47149091117 scopus 로고    scopus 로고
    • Sirtuin 1, stem cells, aging, and stem cell aging
    • Mantel, C.; Broxmeyer, H.E. Sirtuin 1, stem cells, aging, and stem cell aging. Curr. Opin. Hematol., 2008, 15, 326-331.
    • (2008) Curr. Opin. Hematol , vol.15 , pp. 326-331
    • Mantel, C.1    Broxmeyer, H.E.2
  • 18
    • 64049094851 scopus 로고    scopus 로고
    • Epigenetic therapies in haematological malignancies: Searching for true targets
    • Altucci, L.; Minucci, S. Epigenetic therapies in haematological malignancies: searching for true targets. Eur. J. Cancer, 2009, 45, 1137-1145.
    • (2009) Eur. J. Cancer , vol.45 , pp. 1137-1145
    • Altucci, L.1    Minucci, S.2
  • 20
    • 0033598942 scopus 로고    scopus 로고
    • 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. An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell, 1999, 99, 735-745.
    • (1999) Cell , vol.99 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 21
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
    • Landry, J.; Slama, J.T.; Sternglanz, R. Role of NAD(+) in the deacetylase activity of the SIR2-like proteins. Biochem. Biophys. Res. Commun., 2000, 278, 685-690.
    • (2000) Biochem. Biophys. Res. Commun , vol.278 , pp. 685-690
    • Landry, J.1    Slama, J.T.2    Sternglanz, R.3
  • 23
    • 0034677535 scopus 로고    scopus 로고
    • Transcrip-tional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S.; Armstrong, C.M.; Kaeberlein, M.; Guarente, L. Transcrip-tional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature, 2000, 403, 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 24
    • 4544243684 scopus 로고    scopus 로고
    • Coenzyme specificity of Sir2 protein deacetylases: Implications for physiological regulation
    • Schmidt, M.T.; Smith, B.C.; Jackson, M.D.; Denu, J.M. Coenzyme specificity of Sir2 protein deacetylases: implications for physiological regulation. J. Biol. Chem., 2004, 279, 40122-40129.
    • (2004) J. Biol. Chem , vol.279 , pp. 40122-40129
    • Schmidt, M.T.1    Smith, B.C.2    Jackson, M.D.3    Denu, J.M.4
  • 25
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD+-dependent deacetylation reactions
    • Sauve, A.A.; Celic, I.; Avalos, J.; Deng, H.; Boeke, J.D.; Schramm, V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry, 2001, 40, 15456-15463.
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 26
    • 1842430616 scopus 로고    scopus 로고
    • SIR2: The biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediates
    • Sauve, A.A.; Schramm, V.L. SIR2: the biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediates. Curr. Med. Chem., 2004, 11, 807-826.
    • (2004) Curr. Med. Chem , vol.11 , pp. 807-826
    • Sauve, A.A.1    Schramm, V.L.2
  • 28
    • 77953291365 scopus 로고    scopus 로고
    • Sirtuin chemical mechanisms
    • Epub Feb 2, DOI 016/j.bbapap.2010.01.021
    • Sauve, A.A. Sirtuin chemical mechanisms. Biochim. Biophys. Acta, 2010, Epub Feb 2, DOI 016/j.bbapap.2010.01.021.
    • (2010) Biochim. Biophys. Acta
    • Sauve, A.A.1
  • 29
    • 22144494168 scopus 로고    scopus 로고
    • Getting a grip on O-acetyl-ADP-ribose
    • Hoff, K.G.; Wolberger, C. Getting a grip on O-acetyl-ADP-ribose. Nat. Struct. Mol. Biol., 2005, 12, 560-561.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 560-561
    • Hoff, K.G.1    Wolberger, C.2
  • 30
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction
    • Haigis, M.C.; Guarente, L.P. Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction. Genes Dev., 2006, 20, 2913-2921.
    • (2006) Genes Dev , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 31
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • Guarente, L. Sir2 links chromatin silencing, metabolism, and aging. Genes Dev., 2000, 14, 1021-1026.
    • (2000) Genes Dev , vol.14 , pp. 1021-1026
    • Guarente, L.1
  • 32
    • 34247502715 scopus 로고    scopus 로고
    • Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+
    • Belenky, P.; Racette, F.G.; Bogan, K.L.; McClure, J.M.; Smith, J.S.; Brenner, C. Nicotinamide riboside promotes Sir2 silencing and extends lifespan via Nrk and Urh1/Pnp1/Meu1 pathways to NAD+. Cell, 2007, 129, 473-484.
    • (2007) Cell , vol.129 , pp. 473-484
    • Belenky, P.1    Racette, F.G.2    Bogan, K.L.3    McClure, J.M.4    Smith, J.S.5    Brenner, C.6
  • 34
    • 0034687694 scopus 로고    scopus 로고
    • 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.; Sternglanz, R.; Denu, J.M. Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc. Natl. Acad. Sci. U.S.A., 2000, 97, 14178-14182.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 35
    • 0035895275 scopus 로고    scopus 로고
    • 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. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product. Proc. Natl. Acad. Sci. U.S.A., 2001, 98, 415-420.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 36
    • 4944245398 scopus 로고    scopus 로고
    • 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. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell, 2004, 16, 93-105.
    • (2004) Mol. Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 37
    • 0037166269 scopus 로고    scopus 로고
    • Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases
    • Jackson, M.D.; Denu, J.M. Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases. J. Biol. Chem., 2002, 277, 18535-18544.
    • (2002) J. Biol. Chem , vol.277 , pp. 18535-18544
    • Jackson, M.D.1    Denu, J.M.2
  • 38
    • 0037066738 scopus 로고    scopus 로고
    • Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases
    • Borra, M.T.; O'Neill, F.J.; Jackson, M.D.; Marshall, B.; Verdin, E.; Foltz, K.R.; Denu, J.M. Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases. J. Biol. Chem., 2002, 277, 12632-12641.
    • (2002) J. Biol. Chem , vol.277 , pp. 12632-12641
    • Borra, M.T.1    O'Neill, F.J.2    Jackson, M.D.3    Marshall, B.4    Verdin, E.5    Foltz, K.R.6    Denu, J.M.7
  • 40
    • 0037033021 scopus 로고    scopus 로고
    • Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases
    • Rafty, L.A.; Schmidt, M.T.; Perraud, A.L.; Scharenberg, A.M.; Denu, J.M. Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolases. J. Biol. Chem., 2002, 277, 47114-47122.
    • (2002) J. Biol. Chem , vol.277 , pp. 47114-47122
    • Rafty, L.A.1    Schmidt, M.T.2    Perraud, A.L.3    Scharenberg, A.M.4    Denu, J.M.5
  • 41
    • 66449123334 scopus 로고    scopus 로고
    • Hydrolase regulates NAD+ metabolites and modulates cellular redox
    • Tong, L.; Lee, S.; Denu, J.M. Hydrolase regulates NAD+ metabolites and modulates cellular redox. J. Biol. Chem., 2009, 284, 11256-11266.
    • (2009) J. Biol. Chem , vol.284 , pp. 11256-11266
    • Tong, L.1    Lee, S.2    Denu, J.M.3
  • 42
    • 1842610541 scopus 로고    scopus 로고
    • A link between transcription and intermediary metabolism: A role for Sir2 in the control of acetyl-coenzyme A synthetase
    • Starai, V.J.; Takahashi, H.; Boeke, J.D.; Escalante-Semerena, J.C. A link between transcription and intermediary metabolism: a role for Sir2 in the control of acetyl-coenzyme A synthetase. Curr. Opin. Microbiol., 2004, 7, 115-119.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 115-119
    • Starai, V.J.1    Takahashi, H.2    Boeke, J.D.3    Escalante-Semerena, J.C.4
  • 43
    • 33750940806 scopus 로고    scopus 로고
    • The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
    • Ono, T.; Kasamatsu, A.; Oka, S.; Moss, J. The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases. Proc. Natl. Acad. Sci. U.S.A., 2006, 103, 16687-16691.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 16687-16691
    • Ono, T.1    Kasamatsu, A.2    Oka, S.3    Moss, J.4
  • 44
    • 19344377042 scopus 로고    scopus 로고
    • Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation
    • Liou, G.G.; Tanny, J.C.; Kruger, R.G.; Walz, T.; Moazed, D. Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell, 2005, 121, 515-527.
    • (2005) Cell , vol.121 , pp. 515-527
    • Liou, G.G.1    Tanny, J.C.2    Kruger, R.G.3    Walz, T.4    Moazed, D.5
  • 46
    • 50249084505 scopus 로고    scopus 로고
    • Bypassing Sir2 and O-acetyl-ADP-ribose in transcriptional silencing
    • Chou, C.C.; Li, Y.C.; Gartenberg, M.R. Bypassing Sir2 and O-acetyl-ADP-ribose in transcriptional silencing. Mol. Cell, 2008, 31, 650-659.
    • (2008) Mol. Cell , vol.31 , pp. 650-659
    • Chou, C.C.1    Li, Y.C.2    Gartenberg, M.R.3
  • 48
    • 54249140416 scopus 로고    scopus 로고
    • Quantification of endogenous sirtuin metabolite O-acetyl-ADP-ribose
    • Lee, S.; Tong, L.; Denu, J.M. Quantification of endogenous sirtuin metabolite O-acetyl-ADP-ribose. Anal. Biochem., 2008, 383, 174-179.
    • (2008) Anal. Biochem , vol.383 , pp. 174-179
    • Lee, S.1    Tong, L.2    Denu, J.M.3
  • 49
    • 67149108542 scopus 로고    scopus 로고
    • Mitochondria-Nucleus Energetic Communication: Role for Phosphotransfer Networks in Processing Cellular Information
    • Lajtha, A., Ed.; Springer US
    • Dzeja, P. P.; Terzic, A. Mitochondria-Nucleus Energetic Communication: Role for Phosphotransfer Networks in Processing Cellular Information. In Handbook of Neurochemistry and Molecular Neu-robiology; Lajtha, A., Ed.; Springer US: 2007; pp. 641-666.
    • (2007) Handbook of Neurochemistry and Molecular Neu-robiology , pp. 641-666
    • Dzeja, P.P.1    Terzic, A.2
  • 50
    • 34748850786 scopus 로고    scopus 로고
    • Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress
    • Schulz, T.J.; Zarse, K.; Voigt, A.; Urban, N.; Birringer, M.; Ristow, M. Glucose restriction extends Caenorhabditis elegans life span by inducing mitochondrial respiration and increasing oxidative stress. Cell Metab., 2007, 6, 280-293.
    • (2007) Cell Metab , vol.6 , pp. 280-293
    • Schulz, T.J.1    Zarse, K.2    Voigt, A.3    Urban, N.4    Birringer, M.5    Ristow, M.6
  • 51
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min, J.; Landry, J.; Sternglanz, R.; Xu, R.M. Crystal structure of a SIR2 homolog-NAD complex. Cell, 2001, 105, 269-279.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 53
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: The in vivo evidence
    • Baur, J.A.; Sinclair, D.A. Therapeutic potential of resveratrol: the in vivo evidence. Nat. Rev. Drug Discov., 2006, 5, 493-506.
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 493-506
    • Baur, J.A.1    Sinclair, D.A.2
  • 54
    • 70450123699 scopus 로고    scopus 로고
    • Resveratrol: A natural poly-phenol with multiple chemopreventive properties
    • Brisdelli, F.; D'Andrea, G.; Bozzi, A. Resveratrol: a natural poly-phenol with multiple chemopreventive properties. Curr. Drug Metab., 2009, 10, 530-546.
    • (2009) Curr. Drug Metab , vol.10 , pp. 530-546
    • Brisdelli, F.1    D'Andrea, G.2    Bozzi, A.3
  • 55
    • 65349091486 scopus 로고    scopus 로고
    • Resveratrol: Biologic and therapeutic implications
    • Sadruddin, S.; Arora, R. Resveratrol: biologic and therapeutic implications. J. Cardiometab. Syndr., 2009, 4, 102-106.
    • (2009) J. Cardiometab. Syndr , vol.4 , pp. 102-106
    • Sadruddin, S.1    Arora, R.2
  • 57
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra, M.T.; Smith, B.C.; Denu, J.M. Mechanism of human SIRT1 activation by resveratrol. J. Biol. Chem., 2005, 280, 17187-17195.
    • (2005) J. Biol. Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 58
    • 34250860632 scopus 로고    scopus 로고
    • Comparative analysis of the effects of resveratrol in two apoptotic models: Inhibition of complex I and potassium deprivation in cerebellar neurons
    • Alvira, D.; Yeste-Velasco, M.; Folch, J.; Verdaguer, E.; Canudas, A.M.; Pallas, M.; Camins, A. Comparative analysis of the effects of resveratrol in two apoptotic models: inhibition of complex I and potassium deprivation in cerebellar neurons. Neuroscience, 2007, 147, 746-756.
    • (2007) Neuroscience , vol.147 , pp. 746-756
    • Alvira, D.1    Yeste-Velasco, M.2    Folch, J.3    Verdaguer, E.4    Canudas, A.M.5    Pallas, M.6    Camins, A.7
  • 60
    • 34548730196 scopus 로고    scopus 로고
    • Resveratrol is a class IA phosphoinositide 3-kinase inhibitor
    • Frojdo, S.; Cozzone, D.; Vidal, H.; Pirola, L. Resveratrol is a class IA phosphoinositide 3-kinase inhibitor. Biochem. J., 2007, 406, 511-518.
    • (2007) Biochem. J , vol.406 , pp. 511-518
    • Frojdo, S.1    Cozzone, D.2    Vidal, H.3    Pirola, L.4
  • 61
    • 4444267291 scopus 로고    scopus 로고
    • Crystal structure of quinone reductase 2 in complex with resveratrol
    • Buryanovskyy, L.; Fu, Y.; Boyd, M.; Ma, Y.; Hsieh, T.C.; Wu, J.M.; Zhang, Z. Crystal structure of quinone reductase 2 in complex with resveratrol. Biochemistry, 2004, 43, 11417-11426.
    • (2004) Biochemistry , vol.43 , pp. 11417-11426
    • Buryanovskyy, L.1    Fu, Y.2    Boyd, M.3    Ma, Y.4    Hsieh, T.C.5    Wu, J.M.6    Zhang, Z.7
  • 64
    • 74449093522 scopus 로고    scopus 로고
    • Resveratrol is neuroprotective because it is not a direct activator of Sirt1-A hypothesis
    • Tang, B.L. Resveratrol is neuroprotective because it is not a direct activator of Sirt1-A hypothesis. Brain Res. Bull., 2010, 81, 359-361.
    • (2010) Brain Res. Bull , vol.81 , pp. 359-361
    • Tang, B.L.1
  • 65
    • 36249016246 scopus 로고    scopus 로고
    • A therapeutic role for sirtuins in diseases of aging?
    • Westphal, C.H.; Dipp, M.A.; Guarente, L. A therapeutic role for sirtuins in diseases of aging? Trends Biochem. Sci., 2007, 32, 555-560.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 555-560
    • Westphal, C.H.1    Dipp, M.A.2    Guarente, L.3
  • 66
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition
    • Sauve, A.A.; Moir, R.D.; Schramm, V.L.; Willis, I.M. Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol. Cell, 2005, 17, 595-601.
    • (2005) Mol. Cell , vol.17 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 67
    • 0041571570 scopus 로고    scopus 로고
    • Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
    • Sauve, A.A.; Schramm, V.L. Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry. Biochemistry, 2003, 42, 9249-9256.
    • (2003) Biochemistry , vol.42 , pp. 9249-9256
    • Sauve, A.A.1    Schramm, V.L.2
  • 69
    • 62149085241 scopus 로고    scopus 로고
    • Pharmaceutical strategies for activating sirtuins
    • Sauve, A.A. Pharmaceutical strategies for activating sirtuins. Curr. Pharm. Des., 2009, 15, 45-56.
    • (2009) Curr. Pharm. Des , vol.15 , pp. 45-56
    • Sauve, A.A.1
  • 70
    • 70349515574 scopus 로고    scopus 로고
    • Is there more to aging than mitochondrial DNA and reactive oxygen species?
    • Alexeyev, M.F. Is there more to aging than mitochondrial DNA and reactive oxygen species? FEBS J., 2009, 276, 5768-5787.
    • (2009) FEBS J , vol.276 , pp. 5768-5787
    • Alexeyev, M.F.1
  • 72
    • 0034033586 scopus 로고    scopus 로고
    • Caloric restriction and aging: An update
    • Masoro, E.J. Caloric restriction and aging: an update. Exp. Gerontol., 2000, 35, 299-305.
    • (2000) Exp. Gerontol , vol.35 , pp. 299-305
    • Masoro, E.J.1
  • 73
    • 50649099122 scopus 로고    scopus 로고
    • Aging and survival: The genetics of life span extension by dietary restriction
    • Mair, W.; Dillin, A. Aging and survival: the genetics of life span extension by dietary restriction. Annu. Rev. Biochem., 2008, 77, 727-754.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 727-754
    • Mair, W.1    Dillin, A.2
  • 76
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated het-erochromatin formation and silencing of E2F target genes during cellular senescence
    • Narita, M.; Nunez, S.; Heard, E.; Narita, M.; Lin, A.W.; Hearn, S.A.; Spector, D.L.; Hannon, G.J.; Lowe, S.W. Rb-mediated het-erochromatin formation and silencing of E2F target genes during cellular senescence. Cell, 2003, 113, 703-716.
    • (2003) Cell , vol.113 , pp. 703-716
    • Narita, M.1    Nunez, S.2    Heard, E.3    Narita, M.4    Lin, A.W.5    Hearn, S.A.6    Spector, D.L.7    Hannon, G.J.8    Lowe, S.W.9
  • 77
    • 33748331132 scopus 로고    scopus 로고
    • Progressive loss of SIRT1 with cell cycle withdrawal
    • Sasaki, T.; Maier, B.; Bartke, A.; Scrable, H. Progressive loss of SIRT1 with cell cycle withdrawal. Aging Cell, 2006, 5, 413-422.
    • (2006) Aging Cell , vol.5 , pp. 413-422
    • Sasaki, T.1    Maier, B.2    Bartke, A.3    Scrable, H.4
  • 78
    • 67349173185 scopus 로고    scopus 로고
    • Relation between replicative senescence of human fibroblasts and life history characteristics
    • Maier, A.B.; Westendorp, R.G. Relation between replicative senescence of human fibroblasts and life history characteristics. Ageing Res. Rev., 2009, 8, 237-243.
    • (2009) Ageing Res. Rev , vol.8 , pp. 237-243
    • Maier, A.B.1    Westendorp, R.G.2
  • 79
    • 67650828068 scopus 로고    scopus 로고
    • A comparative analysis of the cell biology of senescence and aging
    • Hwang, E.S.; Yoon, G.; Kang, H.T. A comparative analysis of the cell biology of senescence and aging. Cell Mol. Life Sci., 2009, 66, 2503-2524.
    • (2009) Cell Mol. Life Sci , vol.66 , pp. 2503-2524
    • Hwang, E.S.1    Yoon, G.2    Kang, H.T.3
  • 80
    • 65349126392 scopus 로고    scopus 로고
    • Cellular senescence: Its role in tumor suppression and aging
    • Ohtani, N.; Mann, D.J.; Hara, E. Cellular senescence: its role in tumor suppression and aging. Cancer Sci., 2009, 100, 792-797.
    • (2009) Cancer Sci , vol.100 , pp. 792-797
    • Ohtani, N.1    Mann, D.J.2    Hara, E.3
  • 81
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel, T.; Deng, C.X.; Mostoslavsky, R. Recent progress in the biology and physiology of sirtuins. Nature, 2009, 460, 587-591.
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 83
    • 34250758020 scopus 로고    scopus 로고
    • H2O2 accelerates cellular senescence by accumulation of acetylated p53 via decrease in the function of SIRT1 by NAD+ depletion
    • Furukawa, A.; Tada-Oikawa, S.; Kawanishi, S.; Oikawa, S. H2O2 accelerates cellular senescence by accumulation of acetylated p53 via decrease in the function of SIRT1 by NAD+ depletion. Cell Physiol. Biochem., 2007, 20, 45-54.
    • (2007) Cell Physiol. Biochem , vol.20 , pp. 45-54
    • Furukawa, A.1    Tada-Oikawa, S.2    Kawanishi, S.3    Oikawa, S.4
  • 84
    • 0037163038 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by a new topoisomerase inhibitor through the generation of hydrogen peroxide
    • Mizutani, H.; Tada-Oikawa, S.; Hiraku, Y.; Oikawa, S.; Kojima, M.; Kawanishi, S. Mechanism of apoptosis induced by a new topoisomerase inhibitor through the generation of hydrogen peroxide. J. Biol. Chem., 2002, 277, 30684-30689.
    • (2002) J. Biol. Chem , vol.277 , pp. 30684-30689
    • Mizutani, H.1    Tada-Oikawa, S.2    Hiraku, Y.3    Oikawa, S.4    Kojima, M.5    Kawanishi, S.6
  • 85
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo, J.; Nikolaev, A.Y.; Imai, S.; Chen, D.; Su, F.; Shiloh, A.; Guarente, L.; Gu, W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell, 2001, 107, 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 86
    • 0034655373 scopus 로고    scopus 로고
    • Apoptosis or senescence-like growth arrest: Influence of cell-cycle position, p53, p21 and bax in 2932 Current Medicinal Chemistry, 2010 Vol. 17, No. 26 H2O2 response of normal human fibroblasts
    • Chen, Q.M.; Liu, J.; Merrett, J.B. Apoptosis or senescence-like growth arrest: influence of cell-cycle position, p53, p21 and bax in 2932 Current Medicinal Chemistry, 2010 Vol. 17, No. 26 H2O2 response of normal human fibroblasts. Biochem. J., 2000, 347, 543-551.
    • (2000) Biochem. J , vol.347 , pp. 543-551
    • Chen, Q.M.1    Liu, J.2    Merrett, J.B.3
  • 89
    • 35349011597 scopus 로고    scopus 로고
    • Sirt1 modulates premature senescence-like phenotype in human endothelial cells
    • Ota, H.; Akishita, M.; Eto, M.; Iijima, K.; Kaneki, M.; Ouchi, Y. Sirt1 modulates premature senescence-like phenotype in human endothelial cells. J. Mol. Cell Cardiol., 2007, 43, 571-579.
    • (2007) J. Mol. Cell Cardiol , vol.43 , pp. 571-579
    • Ota, H.1    Akishita, M.2    Eto, M.3    Iijima, K.4    Kaneki, M.5    Ouchi, Y.6
  • 90
    • 30544445468 scopus 로고    scopus 로고
    • 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. Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells. Oncogene, 2006, 25, 176-185.
    • (2006) Oncogene , vol.25 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3    Hikasa, M.4    Iijima, K.5    Eto, M.6    Kozaki, K.7    Akishita, M.8    Ouchi, Y.9    Kaneki, M.10
  • 91
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates F0X03a in response to oxidative stress and caloric restriction
    • Wang, F.; Nguyen, M.; Qin, F.X.; Tong, Q. SIRT2 deacetylates F0X03a in response to oxidative stress and caloric restriction. Aging Cell, 2007, 6, 505-514.
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 93
    • 38649124004 scopus 로고    scopus 로고
    • NEM0 shuttle: A link between DNA damage and NF-kappaB activation in progeroid syndromes?
    • Salminen, A.; Suuronen, T.; Huuskonen, J.; Kaarniranta, K. NEM0 shuttle: a link between DNA damage and NF-kappaB activation in progeroid syndromes? Biochem. Biophys. Res. Commun., 2008, 367, 715-718.
    • (2008) Biochem. Biophys. Res. Commun , vol.367 , pp. 715-718
    • Salminen, A.1    Suuronen, T.2    Huuskonen, J.3    Kaarniranta, K.4
  • 95
    • 70249098847 scopus 로고    scopus 로고
    • SIRT1 markedly extends replicative lifespan if the NAD+ salvage pathway is enhanced
    • Ho, C.; van der Veer, E.; Akawi, O Pickering, J.G. SIRT1 markedly extends replicative lifespan if the NAD+ salvage pathway is enhanced. FEBS Lett., 2009, 583, 3081-3085.
    • (2009) FEBS Lett , vol.583 , pp. 3081-3085
    • Ho, C.1    van der Veer, E.2    Akawi, O.3    Pickering, J.G.4
  • 96
    • 69949114091 scopus 로고    scopus 로고
    • Anti-aging properties of melatonin in an in vitro murine senescence model: Involvement of the sirtuin 1 pathway
    • Tajes, M.; Gutierrez-Cuesta, J.; Ortuno-Sahagun, D.; Camins, A.; Pallas, M. Anti-aging properties of melatonin in an in vitro murine senescence model: involvement of the sirtuin 1 pathway. J. Pineal Res., 2009, 47, 228-237.
    • (2009) J. Pineal Res , vol.47 , pp. 228-237
    • Tajes, M.1    Gutierrez-Cuesta, J.2    Ortuno-Sahagun, D.3    Camins, A.4    Pallas, M.5
  • 97
    • 63849252078 scopus 로고    scopus 로고
    • Therapeutic potential of SIRT1 and NAMPT-mediated NAD biosynthesis in type 2 diabetes
    • Imai, S.; Kiess, W. Therapeutic potential of SIRT1 and NAMPT-mediated NAD biosynthesis in type 2 diabetes. Front. Biosci., 2009, 14, 2983-2995.
    • (2009) Front. Biosci , vol.14 , pp. 2983-2995
    • Imai, S.1    Kiess, W.2
  • 98
    • 33746667829 scopus 로고    scopus 로고
    • Hyperglycemia accelerated endothelial progenitor cell senescence via the activation of p38 mitogen-activated protein kinase
    • Kuki, S.; Imanishi, T.; Kobayashi, K.; Matsuo, Y.; Obana, M.; Akasaka, T. Hyperglycemia accelerated endothelial progenitor cell senescence via the activation of p38 mitogen-activated protein kinase. Circ. J., 2006, 70, 1076-1081.
    • (2006) Circ. J , vol.70 , pp. 1076-1081
    • Kuki, S.1    Imanishi, T.2    Kobayashi, K.3    Matsuo, Y.4    Obana, M.5    Akasaka, T.6
  • 100
    • 35248869149 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma (PPARgamma) and colorectal carcinogenesis
    • Voutsadakis, I.A. Peroxisome proliferator-activated receptor gamma (PPARgamma) and colorectal carcinogenesis. J. Cancer Res. Clin. Oncol., 2007, 133, 917-928.
    • (2007) J. Cancer Res. Clin. Oncol , vol.133 , pp. 917-928
    • Voutsadakis, I.A.1
  • 101
    • 35748949600 scopus 로고    scopus 로고
    • Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1
    • Wong, S.; Weber, J.D. Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1. Biochem. J., 2007, 407, 451-460.
    • (2007) Biochem. J , vol.407 , pp. 451-460
    • Wong, S.1    Weber, J.D.2
  • 102
    • 45849137875 scopus 로고    scopus 로고
    • SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts
    • Huang, J.; Gan, Q.; Han, L.; Li, J.; Zhang, H.; Sun, Y.; Zhang, Z.; Tong, T. SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts. PLoS ONE, 2008, 3, e1710.
    • (2008) PLoS ONE , vol.3
    • Huang, J.1    Gan, Q.2    Han, L.3    Li, J.4    Zhang, H.5    Sun, Y.6    Zhang, Z.7    Tong, T.8
  • 103
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim, E.J.; Kho, J.H.; Kang, M.R.; Um, S.J. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol. Cell, 2007, 28, 277-290.
    • (2007) Mol. Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 104
    • 45749094496 scopus 로고    scopus 로고
    • Analysis of DBC1 and its ho-mologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites
    • Anantharaman, V.; Aravind, L. Analysis of DBC1 and its ho-mologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites. Cell Cycle, 2008, 7, 1467-1472.
    • (2008) Cell Cycle , vol.7 , pp. 1467-1472
    • Anantharaman, V.1    Aravind, L.2
  • 105
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • Zhao, W.; Kruse, J.P.; Tang, Y.; Jung, S.Y.; Qin, J.; Gu, W. Negative regulation of the deacetylase SIRT1 by DBC1. Nature, 2008, 451, 587-590.
    • (2008) Nature , vol.451 , pp. 587-590
    • Zhao, W.1    Kruse, J.P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6
  • 106
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT
    • Kim, J.E.; Chen, J.; Lou, Z. DBC1 is a negative regulator of SIRT1. Nature, 2008, 451, 583-586.
    • (2008) Nature , vol.451 , pp. 583-586
    • Kim, J.E.1    Chen, J.2    Lou, Z.3
  • 107
    • 70449748196 scopus 로고    scopus 로고
    • Interactions between DBC1 and SIRT 1 are deregulated in breast cancer cells
    • Kim, J.E.; Lou, Z.; Chen, J. Interactions between DBC1 and SIRT 1 are deregulated in breast cancer cells. Cell Cycle, 2009, 8, 3784-3785.
    • (2009) Cell Cycle , vol.8 , pp. 3784-3785
    • Kim, J.E.1    Lou, Z.2    Chen, J.3
  • 108
    • 30044440497 scopus 로고    scopus 로고
    • Sirt1: A metabolic master switch that modulates lifespan
    • discussion 36
    • Leibiger, I.B.; Berggren, P.O. Sirt1: a metabolic master switch that modulates lifespan. Nat. Med., 2006, 12, 34-6; discussion 36.
    • (2006) Nat. Med , vol.12 , pp. 34-36
    • Leibiger, I.B.1    Berggren, P.O.2
  • 109
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers, J.T.; Lerin, C.; Haas, W.; Gygi, S.P.; Spiegelman, B.M.; Puigserver, P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature, 2005, 434, 113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 110
    • 57349169258 scopus 로고    scopus 로고
    • Comparing and contrasting the roles of AMPK and SIRT1 in metabolic tissues
    • Fulco, M.; Sartorelli, V. Comparing and contrasting the roles of AMPK and SIRT1 in metabolic tissues. Cell Cycle, 2008, 7, 3669-3679.
    • (2008) Cell Cycle , vol.7 , pp. 3669-3679
    • Fulco, M.1    Sartorelli, V.2
  • 111
    • 43049134148 scopus 로고    scopus 로고
    • Glucose restriction: Longevity SIRTainly, but without building muscle?
    • Canto, C.; Auwerx, J. Glucose restriction: longevity SIRTainly, but without building muscle? Dev. Cell, 2008, 14, 642-644.
    • (2008) Dev. Cell , vol.14 , pp. 642-644
    • Canto, C.1    Auwerx, J.2
  • 112
    • 56649085322 scopus 로고    scopus 로고
    • SIRT1: Roles in aging and cancer
    • Kim, E.J.; Um, S.J. SIRT1: roles in aging and cancer. BMB Rep., 2008, 41, 751-756.
    • (2008) BMB Rep , vol.41 , pp. 751-756
    • Kim, E.J.1    Um, S.J.2
  • 113
    • 69849107217 scopus 로고    scopus 로고
    • Caloric restriction, SIRT1 and longevity
    • Canto, C.; Auwerx, J. Caloric restriction, SIRT1 and longevity. Trends Endocrinol. Metab., 2009, 20, 325-331.
    • (2009) Trends Endocrinol. Metab , vol.20 , pp. 325-331
    • Canto, C.1    Auwerx, J.2
  • 119
    • 39749087530 scopus 로고    scopus 로고
    • SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization
    • Han, M.K.; Song, E.K.; Guo, Y.; Ou, X.; Mantel, C.; Broxmeyer, H.E. SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization. Cell Stem Cell, 2008, 2, 241-251.
    • (2008) Cell Stem Cell , vol.2 , pp. 241-251
    • Han, M.K.1    Song, E.K.2    Guo, Y.3    Ou, X.4    Mantel, C.5    Broxmeyer, H.E.6
  • 120
    • 26244436281 scopus 로고    scopus 로고
    • 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. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell, 2005, 16, 4623-4635.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 125
    • 46749085503 scopus 로고    scopus 로고
    • Angiotensin II induces endothelial cell senescence via the activation of mitogen-activated protein kinases
    • Shan, H.; Bai, X.; Chen, X. Angiotensin II induces endothelial cell senescence via the activation of mitogen-activated protein kinases. Cell Biochem. Funct., 2008, 26, 459-466.
    • (2008) Cell Biochem. Funct , vol.26 , pp. 459-466
    • Shan, H.1    Bai, X.2    Chen, X.3


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