메뉴 건너뛰기




Volumn 206, Issue , 2011, Pages 241-255

Sirtuin modulators

Author keywords

NAD; Sirtuin inhibitors; Sirtuins

Indexed keywords

2 [1 (3 AMIDINOTHIOPROPYL) 1H INDOL 3 YL] 3 (1 METHYL 1H INDOL 3 YL)MALEIMIDE; AC 93253; BETA PHENYLSPLITOMICIN; CAMBINOL; CHALCONE DERIVATIVE; DIHYDROPYRIDINE DERIVATIVE; EX 527; HYDROLASE INHIBITOR; ISONICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; RESVERATROL; SALERMIDE; SIRTINOL; SIRTUIN; SIRTUIN 1; SIRTUIN 2; SIRTUIN INHIBITOR; SPLITOMICIN; SRT 1720; STAT PROTEIN; SURAMIN; TENOVIN; TENOVIN 6; UNCLASSIFIED DRUG;

EID: 80054767989     PISSN: 01712004     EISSN: 18650325     Source Type: Book Series    
DOI: 10.1007/978-3-642-21631-2_11     Document Type: Article
Times cited : (30)

References (60)
  • 2
    • 0038329323 scopus 로고    scopus 로고
    • Nicatinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • DOI 10.1038/nature01578
    • Anderson RM et al (2003) Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae. Nature 423(6936):181-185 (Pubitemid 36569542)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 3
    • 70149123204 scopus 로고    scopus 로고
    • Inhibition of human sirtuins by in situ generation of an acetylated lysine- ADP-ribose conjugate
    • Asaba T et al (2009) Inhibition of human sirtuins by in situ generation of an acetylated lysine- ADP-ribose conjugate. J Am Chem Soc 131(20):6989-6996
    • (2009) J Am Chem Soc , vol.131 , Issue.20 , pp. 6989-6996
    • Asaba, T.1
  • 7
    • 50949120914 scopus 로고    scopus 로고
    • Nicotinic acid, nicotinamide, and nicotinamide riboside: A molecular evaluation of NAD+ precursor vitamins in human nutrition
    • Bogan KL, Brenner C (2008) Nicotinic acid, nicotinamide, and nicotinamide riboside: a molecular evaluation of NAD+ precursor vitamins in human nutrition. Annu Rev Nutr 28:115-130
    • (2008) Annu Rev Nutr , vol.28 , pp. 115-130
    • Bogan, K.L.1    Brenner, C.2
  • 8
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • DOI 10.1038/nrm1616
    • Bordone L, Guarente L (2005) Calorie restriction, SIRT1 and metabolism: understanding longevity. Nat Rev Mol Cell Biol 6(4):298-305 (Pubitemid 40516896)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.4 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 9
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • DOI 10.1074/jbc.M501250200
    • Borra MT, Smith BC, Denu JM (2005) Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 280(17):17187-17195 (Pubitemid 41389185)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 10
    • 54849425547 scopus 로고    scopus 로고
    • Specific SIRT1 activation mimics low energy levels and protects against diet-induced metabolic disorders by enhancing fat oxidation
    • Feige JN et al (2008) Specific SIRT1 activation mimics low energy levels and protects against diet-induced metabolic disorders by enhancing fat oxidation. Cell Metab 8(5):347-358
    • (2008) Cell Metab , vol.8 , Issue.5 , pp. 347-358
    • Feige, J.N.1
  • 11
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • FulcoMet al (2003) Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell 12(1):51-62
    • (2003) Mol Cell , vol.12 , Issue.1 , pp. 51-62
  • 12
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • Grozinger CM et al (2001) Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J Biol Chem 276(42): 38837-38843
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 38837-38843
    • Grozinger, C.M.1
  • 13
    • 0034193776 scopus 로고    scopus 로고
    • Sir2 links chromatin silencing, metabolism, and aging
    • Guarente L (2000) Sir2 links chromatin silencing, metabolism, and aging. Genes Dev 14(9): 1021-1026 (Pubitemid 30324417)
    • (2000) Genes and Development , vol.14 , Issue.9 , pp. 1021-1026
    • Guarente, L.1
  • 14
    • 68049096181 scopus 로고    scopus 로고
    • Structural and synthetic investigations of tanikolide dimer, a SIRT2 selective inhibitor, and tanikolide seco-acid from the Madagascar marine cyanobacterium Lyngbya majuscula
    • Gutierrez M et al (2009) Structural and synthetic investigations of tanikolide dimer, a SIRT2 selective inhibitor, and tanikolide seco-acid from the Madagascar marine cyanobacterium Lyngbya majuscula. J Org Chem 74(15):5267-5275
    • (2009) J Org Chem , vol.74 , Issue.15 , pp. 5267-5275
    • Gutierrez, M.1
  • 15
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha HC, Snyder SH (1999) Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc Natl Acad Sci USA 96(24):13978-13982
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.24 , pp. 13978-13982
    • Ha, H.C.1    Snyder, S.H.2
  • 16
    • 43549088782 scopus 로고    scopus 로고
    • Resveratrol: A multitargeted agent for age-associated chronic diseases
    • Harikumar KB, Aggarwal BB (2008) Resveratrol: a multitargeted agent for age-associated chronic diseases. Cell Cycle 7(8):1020-1035
    • (2008) Cell Cycle , vol.7 , Issue.8 , pp. 1020-1035
    • Harikumar, K.B.1    Aggarwal, B.B.2
  • 17
    • 33646254136 scopus 로고    scopus 로고
    • Antitumor activity of a small molecule inhibitor of human Sir2 enzymes
    • Heltweg B et al (2006) Antitumor activity of a small molecule inhibitor of human Sir2 enzymes. Cancer Res 66(8):4368-4377
    • (2006) Cancer Res , vol.66 , Issue.8 , pp. 4368-4377
    • Heltweg, B.1
  • 21
    • 77249130268 scopus 로고    scopus 로고
    • Novel 3-arylideneindolin-2-ones as inhibitors of NAD+ -dependent histone deacetylases (sirtuins)
    • Huber K et al (2010) Novel 3-arylideneindolin-2-ones as inhibitors of NAD+ -dependent histone deacetylases (sirtuins). J Med Chem 53(3):1383-1386
    • (2010) J Med Chem , vol.53 , Issue.3 , pp. 1383-1386
    • Huber, K.1
  • 22
    • 77952547233 scopus 로고    scopus 로고
    • Ten years of NAD-dependent SIR2 family deacetylases: Implications for metabolic diseases
    • Imai S, Guarente L (2010) Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases. Trends Pharmacol Sci 31(5):212-220
    • (2010) Trends Pharmacol Sci , vol.31 , Issue.5 , pp. 212-220
    • Imai, S.1    Guarente, L.2
  • 23
    • 19344374925 scopus 로고    scopus 로고
    • Sir2-independent life span extension by calorie restriction in yeast
    • Kaeberlein M et al (2004) Sir2-independent life span extension by calorie restriction in yeast. PLoS Biol 2(9):E296
    • (2004) PLoS Biol , vol.2 , Issue.9
    • Kaeberlein, M.1
  • 25
    • 56649106665 scopus 로고    scopus 로고
    • A novel chalcone polyphenol inhibits the deacetylase activity of SIRT1 and cell growth in HEK293T cells
    • Kahyo T et al (2008) A novel chalcone polyphenol inhibits the deacetylase activity of SIRT1 and cell growth in HEK293T cells. J Pharmacol Sci 108(3):364-371
    • (2008) J Pharmacol Sci , vol.108 , Issue.3 , pp. 364-371
    • Kahyo, T.1
  • 26
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim EJ et al (2007) Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol Cell 28(2):277-290
    • (2007) Mol Cell , vol.28 , Issue.2 , pp. 277-290
    • Kim, E.J.1
  • 29
    • 60149091562 scopus 로고    scopus 로고
    • Salermide, a Sirtuin inhibitor with a strong cancer-specific proapoptotic effect
    • Lara E et al (2009) Salermide, a Sirtuin inhibitor with a strong cancer-specific proapoptotic effect. Oncogene 28(6):781-791
    • (2009) Oncogene , vol.28 , Issue.6 , pp. 781-791
    • Lara, E.1
  • 30
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin SJ et al (2004) Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev 18(1):12-16
    • (2004) Genes Dev , vol.18 , Issue.1 , pp. 12-16
    • Lin, S.J.1
  • 31
    • 69949096844 scopus 로고    scopus 로고
    • Study of 1,4-dihydropyridine structural scaffold: Discovery of novel sirtuin activators and inhibitors
    • Mai A et al (2009) Study of 1,4-dihydropyridine structural scaffold: discovery of novel sirtuin activators and inhibitors. J Med Chem 52(17):5496-5504
    • (2009) J Med Chem , vol.52 , Issue.17 , pp. 5496-5504
    • Mai, A.1
  • 32
    • 65649111534 scopus 로고    scopus 로고
    • Novel cambinol analogs as sirtuin inhibitors: Synthesis, biological evaluation, and rationalization of activity
    • Medda F et al (2009) Novel cambinol analogs as sirtuin inhibitors: synthesis, biological evaluation, and rationalization of activity. J Med Chem 52(9):2673-2682
    • (2009) J Med Chem , vol.52 , Issue.9 , pp. 2673-2682
    • Medda, F.1
  • 34
    • 0004760134 scopus 로고
    • Life span of individual yeast cells
    • Mortimer RK, Johnston JR (1959) Life span of individual yeast cells. Nature 183(4677): 1751-1752
    • (1959) Nature , vol.183 , Issue.4677 , pp. 1751-1752
    • Mortimer, R.K.1    Johnston, J.R.2
  • 35
    • 65549118773 scopus 로고    scopus 로고
    • Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1
    • Nakahata Y et al (2009) Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1. Science 324(5927):654-657
    • (2009) Science , vol.324 , Issue.5927 , pp. 654-657
    • Nakahata, Y.1
  • 39
    • 77950246109 scopus 로고    scopus 로고
    • SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
    • Pacholec M et al (2010) SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. J Biol Chem 285(11):8340-8351
    • (2010) J Biol Chem , vol.285 , Issue.11 , pp. 8340-8351
    • Pacholec, M.1
  • 41
    • 42349085704 scopus 로고    scopus 로고
    • Sirt1 contributes critically to the redox-dependent fate of neural progenitors
    • Prozorovski T et al (2008) Sirt1 contributes critically to the redox-dependent fate of neural progenitors. Nat Cell Biol 10(4):385-394
    • (2008) Nat Cell Biol , vol.10 , Issue.4 , pp. 385-394
    • Prozorovski, T.1
  • 42
    • 65549103855 scopus 로고    scopus 로고
    • Circadian clock feedback cycle through NAMPT-mediated NAD+ biosynthesis
    • Ramsey KM et al (2009) Circadian clock feedback cycle through NAMPT-mediated NAD+ biosynthesis. Science 324(5927):651-654
    • (2009) Science , vol.324 , Issue.5927 , pp. 651-654
    • Ramsey, K.M.1
  • 43
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells
    • DOI 10.1074/jbc.M408388200
    • Revollo JR, Grimm AA, Imai S (2004) The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J Biol Chem 279(49): 50754-50763 (Pubitemid 40017813)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 50754-50763
    • Revollo, J.R.1    Grimm, A.A.2    Imai, S.-I.3
  • 44
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
    • DOI 10.1038/nature03354
    • Rodgers JT et al (2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434(7029):113-118 (Pubitemid 40349395)
    • (2005) Nature , vol.434 , Issue.7029 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 46
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition
    • DOI 10.1016/j.molcel.2004.12.032
    • Sauve AA et al (2005) Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol Cell 17(4):595-601 (Pubitemid 40269123)
    • (2005) Molecular Cell , vol.17 , Issue.4 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 47
    • 4544243684 scopus 로고    scopus 로고
    • Coenzyme specificity of Sir2 protein deacetylases. Implications for physiological regulation
    • DOI 10.1074/jbc.M407484200
    • Schmidt MT et al (2004) Coenzyme specificity of Sir2 protein deacetylases: implications for physiological regulation. J Biol Chem 279(38):40122-40129 (Pubitemid 39258287)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 40122-40129
    • Schmidt, M.T.1    Smith, B.C.2    Jackson, M.D.3    Denu, J.M.4
  • 49
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles - A cause of aging in yeast
    • DOI 10.1016/S0092-8674(00)80493-6
    • Sinclair DA, Guarente L (1997) Extrachromosomal rDNA circles - a cause of aging in yeast. Cell 91(7):1033-1042 (Pubitemid 28027835)
    • (1997) Cell , vol.91 , Issue.7 , pp. 1033-1042
    • Sinclair, D.A.1    Guarente, L.2
  • 51
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • DOI 10.1038/35065638
    • Tissenbaum HA, Guarente L (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410(6825):227-230 (Pubitemid 32216597)
    • (2001) Nature , vol.410 , Issue.6825 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 53
    • 35548936745 scopus 로고    scopus 로고
    • Structure-activity studies on suramin analogues as inhibitors of NAD+ dependent histone deacetylases (sirtuins)
    • Trapp J et al (2007) Structure-activity studies on suramin analogues as inhibitors of NAD+ dependent histone deacetylases (sirtuins). ChemMedChem 2(10):1419-1431
    • (2007) ChemMedChem , vol.2 , Issue.10 , pp. 1419-1431
    • Trapp, J.1
  • 54
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
    • DOI 10.1016/j.molcel.2004.08.031, PII S1097276504005180
    • Vaquero A et al (2004) Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol Cell 16(1):93-105 (Pubitemid 39330155)
    • (2004) Molecular Cell , vol.16 , Issue.1 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 59
    • 67650444786 scopus 로고    scopus 로고
    • Identification of a small molecule SIRT2 inhibitor with selective tumor cytotoxicity
    • Zhang Y et al (2009) Identification of a small molecule SIRT2 inhibitor with selective tumor cytotoxicity. Biochem Biophys Res Commun 386(4):729-733
    • (2009) Biochem Biophys Res Commun , vol.386 , Issue.4 , pp. 729-733
    • Zhang, Y.1
  • 60
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • DOI 10.1038/nature06515, PII NATURE06515
    • Zhao W et al (2008) Negative regulation of the deacetylase SIRT1 by DBC1. Nature 451(7178): 587-590 (Pubitemid 351186268)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 587-590
    • Zhao, W.1    Kruse, J.-P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.