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Volumn 4, Issue 3-4, 2013, Pages 97-104

The Roles of SIRT1 in Cancer

Author keywords

cancer; deacetylase; SIRT1

Indexed keywords

AUTOPHAGY PROTEIN 5; BETA CATENIN; BREAST CANCER ASSOCIATED PROTEIN 3; CAMBINOL; ENZYME ACTIVATOR; ENZYME INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; JGB 1741; ONCOPROTEIN; PROTEIN P53; RESVERATROL; SALERMIDE; SIRTINOL; SIRTUIN 1; SRT 1460; SRT 1720; SRT 2183; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR FKHRL1; TRANSCRIPTION FACTOR FOXO; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG; WNT PROTEIN;

EID: 84887428122     PISSN: 19476019     EISSN: 19476027     Source Type: Journal    
DOI: 10.1177/1947601912475079     Document Type: Review
Times cited : (192)

References (114)
  • 1
    • 70349440053 scopus 로고    scopus 로고
    • The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice
    • Zhang J,Lee SM,Shannon S,et al.The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice.J Clin Invest. 2009;119:3048-58.
    • (2009) J Clin Invest , vol.119 , pp. 3048-3058
    • Zhang, J.1    Lee, S.M.2    Shannon, S.3
  • 2
    • 84861461517 scopus 로고    scopus 로고
    • USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development
    • Lin Z,Yang H,Kong Q,et al.USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development.Mol Cell. 2012;46:484-94.
    • (2012) Mol Cell , vol.46 , pp. 484-494
    • Lin, Z.1    Yang, H.2    Kong, Q.3
  • 3
    • 80052359850 scopus 로고    scopus 로고
    • Resveratrol-activated AMPK/SIRT1/autophagy in cellular models of Parkinson's disease
    • Wu Y,Li X,Zhu JX,et al.Resveratrol-activated AMPK/SIRT1/autophagy in cellular models of Parkinson's disease.Neurosignals. 2011;19:163-74.
    • (2011) Neurosignals , vol.19 , pp. 163-174
    • Wu, Y.1    Li, X.2    Zhu, J.X.3
  • 4
    • 13944253348 scopus 로고    scopus 로고
    • Calorie restriction: the SIR2 connection
    • Guarente L,Picard F.Calorie restriction: the SIR2 connection.Cell. 2005;120:473-82.
    • (2005) Cell , vol.120 , pp. 473-482
    • Guarente, L.1    Picard, F.2
  • 5
    • 84864615516 scopus 로고    scopus 로고
    • Brown remodeling of white adipose tissue by SirT1-dependent deacetylation of Ppargamma
    • Qiang L,Wang L,Kon N,et al.Brown remodeling of white adipose tissue by SirT1-dependent deacetylation of Ppargamma.Cell. 2012;150:620-32.
    • (2012) Cell , vol.150 , pp. 620-632
    • Qiang, L.1    Wang, L.2    Kon, N.3
  • 6
    • 53149137486 scopus 로고    scopus 로고
    • Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice
    • Wang RH,Sengupta K,Li C,et al.Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice.Cancer Cell. 2008;14:312-23.
    • (2008) Cancer Cell , vol.14 , pp. 312-323
    • Wang, R.H.1    Sengupta, K.2    Li, C.3
  • 7
    • 84855860714 scopus 로고    scopus 로고
    • mIGF-1/JNK1/SirT1 signaling confers protection against oxidative stress in the heart
    • Vinciguerra M,Santini MP,Martinez C,et al.mIGF-1/JNK1/SirT1 signaling confers protection against oxidative stress in the heart.Aging Cell. 2012;11:139-49.
    • (2012) Aging Cell , vol.11 , pp. 139-149
    • Vinciguerra, M.1    Santini, M.P.2    Martinez, C.3
  • 8
    • 34248151365 scopus 로고    scopus 로고
    • The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation
    • Inoue T,Hiratsuka M,Osaki M,Oshimura M.The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation.Cell Cycle. 2007;6:1011-8.
    • (2007) Cell Cycle , vol.6 , pp. 1011-1018
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Oshimura, M.4
  • 9
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander G,Guarente L.The Sir2 family of protein deacetylases.Annu Rev Biochem. 2004;73:417-35.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 10
    • 53249121556 scopus 로고    scopus 로고
    • Sirtuins: novel therapeutic targets to treat age-associated diseases
    • Lavu S,Boss O,Elliott PJ,Lambert PD.Sirtuins: novel therapeutic targets to treat age-associated diseases.Nat Rev Drug Discov. 2008;7:841-53.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 841-853
    • Lavu, S.1    Boss, O.2    Elliott, P.J.3    Lambert, P.D.4
  • 11
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S,Armstrong CM,Kaeberlein M,Guarente L.Transcriptional 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
  • 12
    • 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
  • 13
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H,Dessain SK,Ng Eaton E,et al.hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase.Cell. 2001;107:149-59.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3
  • 14
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J,Nikolaev AY,Imai S,et al.Negative control of p53 by Sir2alpha promotes cell survival under stress.Cell. 2001;107:137-48.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3
  • 15
    • 33845396682 scopus 로고    scopus 로고
    • SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity
    • Dai JM,Wang ZY,Sun DC,Lin RX,Wang SQ.SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity.J Cell Physiol. 2007;210:161-6.
    • (2007) J Cell Physiol , vol.210 , pp. 161-166
    • Dai, J.M.1    Wang, Z.Y.2    Sun, D.C.3    Lin, R.X.4    Wang, S.Q.5
  • 16
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • Chen WY,Wang DH,Yen RC,Luo J,Gu W,Baylin SB.Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses.Cell. 2005;123:437-48.
    • (2005) Cell , vol.123 , pp. 437-448
    • Chen, W.Y.1    Wang, D.H.2    Yen, R.C.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 17
    • 79955773522 scopus 로고    scopus 로고
    • The type III histone deacetylase Sirt1 protein suppresses p300-mediated histone H3 lysine 56 acetylation at Bclaf1 promoter to inhibit T cell activation
    • Kong S,Kim SJ,Sandal B,et al.The type III histone deacetylase Sirt1 protein suppresses p300-mediated histone H3 lysine 56 acetylation at Bclaf1 promoter to inhibit T cell activation.J Biol Chem. 2011;286:16967-75.
    • (2011) J Biol Chem , vol.286 , pp. 16967-16975
    • Kong, S.1    Kim, S.J.2    Sandal, B.3
  • 18
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F,Hoberg JE,Ramsey CS,et al.Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase.EMBO J. 2004;23:2369-80.
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3
  • 19
    • 77956677458 scopus 로고    scopus 로고
    • Myeloid deletion of SIRT1 induces inflammatory signaling in response to environmental stress
    • Schug TT,Xu Q,Gao H,et al.Myeloid deletion of SIRT1 induces inflammatory signaling in response to environmental stress.Mol Cell Biol. 2010;30:4712-21.
    • (2010) Mol Cell Biol , vol.30 , pp. 4712-4721
    • Schug, T.T.1    Xu, Q.2    Gao, H.3
  • 20
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • Chen LF,Mu Y,Greene WC.Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB.EMBO J. 2002;21:6539-48.
    • (2002) EMBO J , vol.21 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 21
    • 0037462725 scopus 로고    scopus 로고
    • Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65
    • Kiernan R,Bres V,Ng RW,et al.Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65.J Biol Chem. 2003;278:2758-66.
    • (2003) J Biol Chem , vol.278 , pp. 2758-2766
    • Kiernan, R.1    Bres, V.2    Ng, R.W.3
  • 22
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A,Sweeney LB,Sturgill JF,et al.Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase.Science. 2004;303:2011-5.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3
  • 23
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta MC,Divecha N,Lemieux M,et al.Mammalian SIRT1 represses forkhead transcription factors.Cell. 2004;116:551-63.
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1    Divecha, N.2    Lemieux, M.3
  • 25
    • 79953152333 scopus 로고    scopus 로고
    • FoxO1 mediates an autofeedback loop regulating SIRT1 expression
    • Xiong S,Salazar G,Patrushev N,Alexander RW.FoxO1 mediates an autofeedback loop regulating SIRT1 expression.J Biol Chem. 2011;286:5289-99.
    • (2011) J Biol Chem , vol.286 , pp. 5289-5299
    • Xiong, S.1    Salazar, G.2    Patrushev, N.3    Alexander, R.W.4
  • 27
    • 78649852533 scopus 로고    scopus 로고
    • SIRT1 is regulated by a PPAR{gamma}-SIRT1 negative feedback loop associated with senescence
    • Han L,Zhou R,Niu J,McNutt MA,Wang P,Tong T.SIRT1 is regulated by a PPAR{gamma}-SIRT1 negative feedback loop associated with senescence.Nucleic Acids Res. 2010;38:7458-71.
    • (2010) Nucleic Acids Res , vol.38 , pp. 7458-7471
    • Han, L.1    Zhou, R.2    Niu, J.3    McNutt, M.A.4    Wang, P.5    Tong, T.6
  • 28
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows WC,Lee S,Denu JM.Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases.Proc Natl Acad Sci U S A. 2006;103:10230-5.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 29
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum EM,Chen R,Alexander MS,et al.Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1.Science. 2009;324:1289-93.
    • (2009) Science , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3
  • 30
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha
    • Lim JH,Lee YM,Chun YS,Chen J,Kim JE,Park JW.Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha.Mol Cell. 2010;38:864-78.
    • (2010) Mol Cell , vol.38 , pp. 864-878
    • Lim, J.H.1    Lee, Y.M.2    Chun, Y.S.3    Chen, J.4    Kim, J.E.5    Park, J.W.6
  • 31
    • 79952590211 scopus 로고    scopus 로고
    • A role for SIRT1 in the hypoxic response
    • Leiser SF,Kaeberlein M.A role for SIRT1 in the hypoxic response.Mol Cell. 2010;38:779-80.
    • (2010) Mol Cell , vol.38 , pp. 779-780
    • Leiser, S.F.1    Kaeberlein, M.2
  • 32
    • 52049102233 scopus 로고    scopus 로고
    • PTEN acetylation modulates its interaction with PDZ domain
    • Ikenoue T,Inoki K,Zhao B,Guan KL.PTEN acetylation modulates its interaction with PDZ domain.Cancer Res. 2008;68:6908-12.
    • (2008) Cancer Res , vol.68 , pp. 6908-6912
    • Ikenoue, T.1    Inoki, K.2    Zhao, B.3    Guan, K.L.4
  • 33
    • 33846976509 scopus 로고    scopus 로고
    • SIRT1 inhibits transforming growth factor beta-induced apoptosis in glomerular mesangial cells via Smad7 deacetylation
    • Kume S,Haneda M,Kanasaki K,et al.SIRT1 inhibits transforming growth factor beta-induced apoptosis in glomerular mesangial cells via Smad7 deacetylation.J Biol Chem. 2007;282:151-8.
    • (2007) J Biol Chem , vol.282 , pp. 151-158
    • Kume, S.1    Haneda, M.2    Kanasaki, K.3
  • 34
    • 77956531086 scopus 로고    scopus 로고
    • Resveratrol inhibits renal fibrosis in the obstructed kidney: potential role in deacetylation of Smad3
    • Li J,Qu X,Ricardo SD,Bertram JF,Nikolic-Paterson DJ.Resveratrol inhibits renal fibrosis in the obstructed kidney: potential role in deacetylation of Smad3.Am J Pathol. 2010;177:1065-71.
    • (2010) Am J Pathol , vol.177 , pp. 1065-1071
    • Li, J.1    Qu, X.2    Ricardo, S.D.3    Bertram, J.F.4    Nikolic-Paterson, D.J.5
  • 35
    • 44849096876 scopus 로고    scopus 로고
    • The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth
    • Firestein R,Blander G,Michan S,et al.The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth.PloS One. 2008;3:e2020.
    • (2008) PloS One , vol.3
    • Firestein, R.1    Blander, G.2    Michan, S.3
  • 36
    • 77952714326 scopus 로고    scopus 로고
    • SIRT1 regulates Dishevelled proteins and promotes transient and constitutive Wnt signaling
    • Holloway KR,Calhoun TN,Saxena M,et al.SIRT1 regulates Dishevelled proteins and promotes transient and constitutive Wnt signaling.Proc Natl Acad Sci U S A. 2010;107:9216-21.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 9216-9221
    • Holloway, K.R.1    Calhoun, T.N.2    Saxena, M.3
  • 37
    • 33847647624 scopus 로고    scopus 로고
    • SIRT1 promotes DNA repair activity and deacetylation of Ku70
    • Jeong J,Juhn K,Lee H,et al.SIRT1 promotes DNA repair activity and deacetylation of Ku70.Exp Mol Med. 2007;39:8-13.
    • (2007) Exp Mol Med , vol.39 , pp. 8-13
    • Jeong, J.1    Juhn, K.2    Lee, H.3
  • 38
    • 77955501963 scopus 로고    scopus 로고
    • SIRT1 regulates UV-induced DNA repair through deacetylating XPA
    • Fan W,Luo J.SIRT1 regulates UV-induced DNA repair through deacetylating XPA.Mol Cell. 2010;39:247-58.
    • (2010) Mol Cell , vol.39 , pp. 247-258
    • Fan, W.1    Luo, J.2
  • 39
    • 78651105018 scopus 로고    scopus 로고
    • Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C
    • Ming M,Shea CR,Guo X,et al.Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C.Proc Natl Acad Sci U S A. 2010;107:22623-8.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 22623-22628
    • Ming, M.1    Shea, C.R.2    Guo, X.3
  • 40
    • 34250897968 scopus 로고    scopus 로고
    • SIRT1 regulates the function of the Nijmegen breakage syndrome protein
    • Yuan Z,Zhang X,Sengupta N,Lane WS,Seto E.SIRT1 regulates the function of the Nijmegen breakage syndrome protein.Mol Cell. 2007;27:149-62.
    • (2007) Mol Cell , vol.27 , pp. 149-162
    • Yuan, Z.1    Zhang, X.2    Sengupta, N.3    Lane, W.S.4    Seto, E.5
  • 41
    • 0027109075 scopus 로고
    • Cancer: p53, guardian of the genome
    • Lane DP.Cancer: p53, guardian of the genome.Nature. 1992;358:15-6.
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 42
    • 0037726822 scopus 로고    scopus 로고
    • Improving cancer therapy by non-genotoxic activation of p53
    • Lain S,Lane D.Improving cancer therapy by non-genotoxic activation of p53.Eur J Cancer. 2003;39:1053-60.
    • (2003) Eur J Cancer , vol.39 , pp. 1053-1060
    • Lain, S.1    Lane, D.2
  • 43
    • 15444377466 scopus 로고    scopus 로고
    • SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1
    • Bouras T,Fu M,Sauve AA,et al.SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1.J Biol Chem. 2005;280:10264-76.
    • (2005) J Biol Chem , vol.280 , pp. 10264-10276
    • Bouras, T.1    Fu, M.2    Sauve, A.A.3
  • 44
    • 33947217916 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation
    • Stiehl DP,Fath DM,Liang D,Jiang Y,Sang N.Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation.Cancer Res. 2007;67:2256-64.
    • (2007) Cancer Res , vol.67 , pp. 2256-2264
    • Stiehl, D.P.1    Fath, D.M.2    Liang, D.3    Jiang, Y.4    Sang, N.5
  • 45
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E,Pearson M,Faretta M,et al.Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.EMBO J. 2002;21:2383-96.
    • (2002) EMBO J , vol.21 , pp. 2383-2396
    • Langley, E.1    Pearson, M.2    Faretta, M.3
  • 47
    • 0029014425 scopus 로고
    • p53 activates expression of HIC-1, a new candidate tumour suppressor gene on 17p13.3
    • Wales MM,Biel MA,el Deiry W,et al.p53 activates expression of HIC-1, a new candidate tumour suppressor gene on 17p13.3.Nat Med. 1995;1:570-7.
    • (1995) Nat Med , vol.1 , pp. 570-577
    • Wales, M.M.1    Biel, M.A.2    el Deiry, W.3
  • 48
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum HA,Guarente L.Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans.Nature. 2001;410:227-30.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 49
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}
    • Nemoto S,Fergusson MM,Finkel T.SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}.J Biol Chem. 2005;280:16456-60.
    • (2005) J Biol Chem , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 50
    • 16344384026 scopus 로고    scopus 로고
    • Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation
    • Yang Y,Hou H,Haller EM,Nicosia SV,Bai W.Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation.EMBO J. 2005;24:1021-32.
    • (2005) EMBO J , vol.24 , pp. 1021-1032
    • Yang, Y.1    Hou, H.2    Haller, E.M.3    Nicosia, S.V.4    Bai, W.5
  • 51
    • 84858795617 scopus 로고    scopus 로고
    • Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation
    • Wang F,Chan CH,Chen K,Guan X,Lin HK,Tong Q.Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation.Oncogene. 2012;31:1546-57.
    • (2012) Oncogene , vol.31 , pp. 1546-1557
    • Wang, F.1    Chan, C.H.2    Chen, K.3    Guan, X.4    Lin, H.K.5    Tong, Q.6
  • 52
    • 10844236451 scopus 로고    scopus 로고
    • Nutrient availability regulates SIRT1 through a forkhead-dependent pathway
    • Nemoto S,Fergusson MM,Finkel T.Nutrient availability regulates SIRT1 through a forkhead-dependent pathway.Science. 2004;306:2105-8.
    • (2004) Science , vol.306 , pp. 2105-2108
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 53
    • 84863011200 scopus 로고    scopus 로고
    • Analysis of sirtuin 1 expression reveals a molecular explanation of IL-2-mediated reversal of T-cell tolerance
    • Gao B,Kong Q,Kemp K,Zhao YS,Fang D.Analysis of sirtuin 1 expression reveals a molecular explanation of IL-2-mediated reversal of T-cell tolerance.Proc Natl Acad Sci U S A. 2012;109:899-904.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 899-904
    • Gao, B.1    Kong, Q.2    Kemp, K.3    Zhao, Y.S.4    Fang, D.5
  • 54
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: same molecule, different degradation pathways
    • Clague MJ,Urbe S.Ubiquitin: same molecule, different degradation pathways.Cell. 2010;143:682-5.
    • (2010) Cell , vol.143 , pp. 682-685
    • Clague, M.J.1    Urbe, S.2
  • 55
    • 65549139675 scopus 로고    scopus 로고
    • Regulation of the aging process by autophagy
    • Salminen A,Kaarniranta K.Regulation of the aging process by autophagy.Trends Mol Med. 2009;15:217-24.
    • (2009) Trends Mol Med , vol.15 , pp. 217-224
    • Salminen, A.1    Kaarniranta, K.2
  • 56
    • 67349273985 scopus 로고    scopus 로고
    • SIRT1: regulation of longevity via autophagy
    • Salminen A,Kaarniranta K.SIRT1: regulation of longevity via autophagy.Cell Signal. 2009;21:1356-60.
    • (2009) Cell Signal , vol.21 , pp. 1356-1360
    • Salminen, A.1    Kaarniranta, K.2
  • 57
    • 79551521179 scopus 로고    scopus 로고
    • Disruption of a Sirt1-dependent autophagy checkpoint in the prostate results in prostatic intraepithelial neoplasia lesion formation
    • Powell MJ,Casimiro MC,Cordon-Cardo C,et al.Disruption of a Sirt1-dependent autophagy checkpoint in the prostate results in prostatic intraepithelial neoplasia lesion formation.Cancer Res. 2011;71:964-75.
    • (2011) Cancer Res , vol.71 , pp. 964-975
    • Powell, M.J.1    Casimiro, M.C.2    Cordon-Cardo, C.3
  • 58
    • 41549138483 scopus 로고    scopus 로고
    • A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
    • Lee IH,Cao L,Mostoslavsky R,et al.A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy.Proc Natl Acad Sci U S A. 2008;105:3374-9.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3374-3379
    • Lee, I.H.1    Cao, L.2    Mostoslavsky, R.3
  • 59
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. 'Protein modifications: beyond the usual suspects' review series
    • Geng J,Klionsky DJ.The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. 'Protein modifications: beyond the usual suspects' review series.EMBO Rep. 2008;9:859-64.
    • (2008) EMBO Rep , vol.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 60
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague J.TGF-beta signal transduction.Annu Rev Biochem. 1998;67:753-91.
    • (1998) Annu Rev Biochem , vol.67 , pp. 753-791
    • Massague, J.1
  • 61
    • 0034644472 scopus 로고    scopus 로고
    • TGFbeta signaling in growth control, cancer, and heritable disorders
    • Massague J,Blain SW,Lo RS.TGFbeta signaling in growth control, cancer, and heritable disorders.Cell. 2000;103:295-309.
    • (2000) Cell , vol.103 , pp. 295-309
    • Massague, J.1    Blain, S.W.2    Lo, R.S.3
  • 62
    • 71049139747 scopus 로고    scopus 로고
    • Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-beta signaling
    • Yan X,Lin Z,Chen F,et al.Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-beta signaling.J Biol Chem. 2009;284:30097-104.
    • (2009) J Biol Chem , vol.284 , pp. 30097-30104
    • Yan, X.1    Lin, Z.2    Chen, F.3
  • 63
    • 0030611757 scopus 로고    scopus 로고
    • Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling
    • Nakao A,Afrakhte M,Moren A,et al.Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling.Nature. 1997;389:631-5.
    • (1997) Nature , vol.389 , pp. 631-635
    • Nakao, A.1    Afrakhte, M.2    Moren, A.3
  • 64
    • 84863898701 scopus 로고    scopus 로고
    • Molecular mechanisms of MMP9 overexpression and its role in emphysema pathogenesis of Smad3-deficient mice
    • Xu B,Chen H,Xu W,et al.Molecular mechanisms of MMP9 overexpression and its role in emphysema pathogenesis of Smad3-deficient mice.Am J Physiol Lung Cell Mol Physiol. 2012;303:L89-96.
    • (2012) Am J Physiol Lung Cell Mol Physiol , vol.303
    • Xu, B.1    Chen, H.2    Xu, W.3
  • 65
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, beta-catenin, and cadherin pathways
    • Nelson WJ,Nusse R.Convergence of Wnt, beta-catenin, and cadherin pathways.Science. 2004;303:1483-7.
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 66
    • 57749112098 scopus 로고    scopus 로고
    • The pseudoreceptor BMP and activin membrane-bound inhibitor positively modulates Wnt/beta-catenin signaling
    • Lin Z,Gao C,Ning Y,He X,Wu W,Chen YG.The pseudoreceptor BMP and activin membrane-bound inhibitor positively modulates Wnt/beta-catenin signaling.J Biol Chem. 2008;283:33053-8.
    • (2008) J Biol Chem , vol.283 , pp. 33053-33058
    • Lin, Z.1    Gao, C.2    Ning, Y.3    He, X.4    Wu, W.5    Chen, Y.G.6
  • 67
    • 0030949463 scopus 로고    scopus 로고
    • Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC
    • Morin PJ,Sparks AB,Korinek V,et al.Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC.Science. 1997;275:1787-90.
    • (1997) Science , vol.275 , pp. 1787-1790
    • Morin, P.J.1    Sparks, A.B.2    Korinek, V.3
  • 68
    • 0030975671 scopus 로고    scopus 로고
    • Constitutive transcriptional activation by a beta-catenin-Tcf complex in APC-/- colon carcinoma
    • Korinek V,Barker N,Morin PJ,et al.Constitutive transcriptional activation by a beta-catenin-Tcf complex in APC-/- colon carcinoma.Science. 1997;275:1784-7.
    • (1997) Science , vol.275 , pp. 1784-1787
    • Korinek, V.1    Barker, N.2    Morin, P.J.3
  • 70
    • 11144353713 scopus 로고    scopus 로고
    • Acetylation of beta-catenin by p300 regulates beta-catenin-Tcf4 interaction
    • Levy L,Wei Y,Labalette C,et al.Acetylation of beta-catenin by p300 regulates beta-catenin-Tcf4 interaction.Mol Cell Biol. 2004;24:3404-14.
    • (2004) Mol Cell Biol , vol.24 , pp. 3404-3414
    • Levy, L.1    Wei, Y.2    Labalette, C.3
  • 71
    • 56249131423 scopus 로고    scopus 로고
    • Radiobiologic response of medulloblastoma cell lines: involvement of beta-catenin?
    • Salaroli R,Di Tomaso T,Ronchi A,et al.Radiobiologic response of medulloblastoma cell lines: involvement of beta-catenin?.J Neurooncol. 2008;90:243-51.
    • (2008) J Neurooncol , vol.90 , pp. 243-251
    • Salaroli, R.1    Di Tomaso, T.2    Ronchi, A.3
  • 72
    • 84862852344 scopus 로고    scopus 로고
    • SIRT1 inhibits proliferation of pancreatic cancer cells expressing pancreatic adenocarcinoma up-regulated factor (PAUF), a novel oncogene, by suppression of beta-catenin
    • Cho IR,Koh SS,Malilas W,et al.SIRT1 inhibits proliferation of pancreatic cancer cells expressing pancreatic adenocarcinoma up-regulated factor (PAUF), a novel oncogene, by suppression of beta-catenin.Biochem Biophys Res Commun. 2012;423:270-5.
    • (2012) Biochem Biophys Res Commun , vol.423 , pp. 270-275
    • Cho, I.R.1    Koh, S.S.2    Malilas, W.3
  • 73
    • 84859219442 scopus 로고    scopus 로고
    • Multi-level interactions between the nuclear receptor TRalpha1 and the WNT effectors beta-catenin/Tcf4 in the intestinal epithelium
    • Sirakov M,Skah S,Lone IN,Nadjar J,Angelov D,Plateroti M.Multi-level interactions between the nuclear receptor TRalpha1 and the WNT effectors beta-catenin/Tcf4 in the intestinal epithelium.PloS One. 2012;7:e34162.
    • (2012) PloS One , vol.7
    • Sirakov, M.1    Skah, S.2    Lone, I.N.3    Nadjar, J.4    Angelov, D.5    Plateroti, M.6
  • 74
    • 65949116604 scopus 로고    scopus 로고
    • Tobacco smoke induces polycomb-mediated repression of Dickkopf-1 in lung cancer cells
    • Hussain M,Rao M,Humphries AE,et al.Tobacco smoke induces polycomb-mediated repression of Dickkopf-1 in lung cancer cells.Cancer Res. 2009;69:3570-8.
    • (2009) Cancer Res , vol.69 , pp. 3570-3578
    • Hussain, M.1    Rao, M.2    Humphries, A.E.3
  • 75
    • 84868685287 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase ITCH negatively regulates canonical Wnt signaling by targeting dishevelled protein
    • Wei W,Li M,Wang J,Nie F,Li L.The E3 ubiquitin ligase ITCH negatively regulates canonical Wnt signaling by targeting dishevelled protein.Mol Cell Biol. 2012;32:3903-12.
    • (2012) Mol Cell Biol , vol.32 , pp. 3903-3912
    • Wei, W.1    Li, M.2    Wang, J.3    Nie, F.4    Li, L.5
  • 76
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappaB action regulated by reversible acetylation
    • Chen L,Fischle W,Verdin E,Greene WC.Duration of nuclear NF-kappaB action regulated by reversible acetylation.Science. 2001;293:1653-7.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 77
    • 84867440428 scopus 로고    scopus 로고
    • SIRT1 regulates CD40 expression induced by TNF-alpha via NF-kB pathway in endothelial cells
    • Yang L,Zhang J,Yan C,et al.SIRT1 regulates CD40 expression induced by TNF-alpha via NF-kB pathway in endothelial cells.Cell Physiol Biochem. 2012;30:1287-98.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 1287-1298
    • Yang, L.1    Zhang, J.2    Yan, C.3
  • 78
    • 77950642805 scopus 로고    scopus 로고
    • Functional interplay between acetylation and methylation of the RelA subunit of NF-kappaB
    • Yang XD,Tajkhorshid E,Chen LF.Functional interplay between acetylation and methylation of the RelA subunit of NF-kappaB.Mol Cell Biol. 2010;30:2170-80.
    • (2010) Mol Cell Biol , vol.30 , pp. 2170-2180
    • Yang, X.D.1    Tajkhorshid, E.2    Chen, L.F.3
  • 79
    • 33847060910 scopus 로고    scopus 로고
    • Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: implications for chronic inflammation and aging
    • Yang SR,Wright J,Bauter M,Seweryniak K,Kode A,Rahman I.Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: implications for chronic inflammation and aging.Am J Physiol Lung Cell Mol Physiol. 2007;292:L567-76.
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.292
    • Yang, S.R.1    Wright, J.2    Bauter, M.3    Seweryniak, K.4    Kode, A.5    Rahman, I.6
  • 80
    • 80055113353 scopus 로고    scopus 로고
    • Activation of Sirt1 by resveratrol inhibits TNF-alpha induced inflammation in fibroblasts
    • Zhu X,Liu Q,Wang M,et al.Activation of Sirt1 by resveratrol inhibits TNF-alpha induced inflammation in fibroblasts.PloS One. 2011;6:e27081.
    • (2011) PloS One , vol.6
    • Zhu, X.1    Liu, Q.2    Wang, M.3
  • 81
    • 84868382788 scopus 로고    scopus 로고
    • Cigarette smoke promotes drug resistance and expansion of cancer stem cell-like side population
    • An Y,Kiang A,Lopez JP,et al.Cigarette smoke promotes drug resistance and expansion of cancer stem cell-like side population.PloS One. 2012;7:e47919.
    • (2012) PloS One , vol.7
    • An, Y.1    Kiang, A.2    Lopez, J.P.3
  • 82
    • 33749173298 scopus 로고    scopus 로고
    • Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFkappaB-dependent transcription
    • Gao F,Cheng J,Shi T,Yeh ET.Neddylation of a breast cancer-associated protein recruits a class III histone deacetylase that represses NFkappaB-dependent transcription.Nat Cell Biol. 2006;8:1171-7.
    • (2006) Nat Cell Biol , vol.8 , pp. 1171-1177
    • Gao, F.1    Cheng, J.2    Shi, T.3    Yeh, E.T.4
  • 83
    • 36248935670 scopus 로고    scopus 로고
    • Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor kappaB-mediated transcription
    • Ghosh HS,Spencer JV,Ng B,McBurney MW,Robbins PD.Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor kappaB-mediated transcription.Biochem J. 2007;408:105-11.
    • (2007) Biochem J , vol.408 , pp. 105-111
    • Ghosh, H.S.1    Spencer, J.V.2    Ng, B.3    McBurney, M.W.4    Robbins, P.D.5
  • 84
    • 53449090280 scopus 로고    scopus 로고
    • Inhibition of transcriptional activity of c-JUN by SIRT1
    • Gao Z,Ye J.Inhibition of transcriptional activity of c-JUN by SIRT1.Biochem Biophys Res Commun. 2008;376:793-6.
    • (2008) Biochem Biophys Res Commun , vol.376 , pp. 793-796
    • Gao, Z.1    Ye, J.2
  • 85
    • 53349173254 scopus 로고    scopus 로고
    • Interactions between SIRT1 and AP-1 reveal a mechanistic insight into the growth promoting properties of alumina (Al2O3) nanoparticles in mouse skin epithelial cells
    • Dey S,Bakthavatchalu V,Tseng MT,et al.Interactions between SIRT1 and AP-1 reveal a mechanistic insight into the growth promoting properties of alumina (Al2O3) nanoparticles in mouse skin epithelial cells.Carcinogenesis. 2008;29:1920-9.
    • (2008) Carcinogenesis , vol.29 , pp. 1920-1929
    • Dey, S.1    Bakthavatchalu, V.2    Tseng, M.T.3
  • 86
    • 0035503278 scopus 로고    scopus 로고
    • A specific lysine in c-Jun is required for transcriptional repression by E1A and is acetylated by p300
    • Vries RG,Prudenziati M,Zwartjes C,Verlaan M,Kalkhoven E,Zantema A.A specific lysine in c-Jun is required for transcriptional repression by E1A and is acetylated by p300.EMBO J. 2001;20:6095-103.
    • (2001) EMBO J , vol.20 , pp. 6095-6103
    • Vries, R.G.1    Prudenziati, M.2    Zwartjes, C.3    Verlaan, M.4    Kalkhoven, E.5    Zantema, A.6
  • 87
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers JH.Genome maintenance mechanisms for preventing cancer.Nature. 2001;411:366-74.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 88
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky R,Chua KF,Lombard DB,et al.Genomic instability and aging-like phenotype in the absence of mammalian SIRT6.Cell. 2006;124:315-29.
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.F.2    Lombard, D.B.3
  • 89
    • 56749156405 scopus 로고    scopus 로고
    • SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging
    • Oberdoerffer P,Michan S,McVay M,et al.SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging.Cell. 2008;135:907-18.
    • (2008) Cell , vol.135 , pp. 907-918
    • Oberdoerffer, P.1    Michan, S.2    McVay, M.3
  • 90
    • 33645221885 scopus 로고    scopus 로고
    • Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage
    • Solomon JM,Pasupuleti R,Xu L,et al.Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage.Mol Cell Biol. 2006;26:28-38.
    • (2006) Mol Cell Biol , vol.26 , pp. 28-38
    • Solomon, J.M.1    Pasupuleti, R.2    Xu, L.3
  • 91
    • 0037472924 scopus 로고    scopus 로고
    • DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
    • Bakkenist CJ,Kastan MB.DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation.Nature. 2003;421:499-506.
    • (2003) Nature , vol.421 , pp. 499-506
    • Bakkenist, C.J.1    Kastan, M.B.2
  • 92
    • 0034611728 scopus 로고    scopus 로고
    • ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway
    • Lim DS,Kim ST,Xu B,et al.ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway.Nature. 2000;404:613-7.
    • (2000) Nature , vol.404 , pp. 613-617
    • Lim, D.S.1    Kim, S.T.2    Xu, B.3
  • 93
    • 0034713466 scopus 로고    scopus 로고
    • ATM phosphorylation of Nijmegen breakage syndrome protein is required in a DNA damage response
    • Wu X,Ranganathan V,Weisman DS,et al.ATM phosphorylation of Nijmegen breakage syndrome protein is required in a DNA damage response.Nature. 2000;405:477-82.
    • (2000) Nature , vol.405 , pp. 477-482
    • Wu, X.1    Ranganathan, V.2    Weisman, D.S.3
  • 94
    • 84859871053 scopus 로고    scopus 로고
    • Regulation of SIRT1 activity by genotoxic stress
    • Yuan J,Luo K,Liu T,Lou Z.Regulation of SIRT1 activity by genotoxic stress.Genes Dev. 2012;26:791-6.
    • (2012) Genes Dev , vol.26 , pp. 791-796
    • Yuan, J.1    Luo, K.2    Liu, T.3    Lou, Z.4
  • 95
    • 33847035824 scopus 로고    scopus 로고
    • Phosphorylation of HuR by Chk2 regulates SIRT1 expression
    • Abdelmohsen K,Pullmann R,Lal A,et al.Phosphorylation of HuR by Chk2 regulates SIRT1 expression.Mol Cell. 2007;25:543-57.
    • (2007) Mol Cell , vol.25 , pp. 543-557
    • Abdelmohsen, K.1    Pullmann, R.2    Lal, A.3
  • 96
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • Yang Y,Fu W,Chen J,et al.SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress.Nat Cell Biol. 2007;9:1253-62.
    • (2007) Nat Cell Biol , vol.9 , pp. 1253-1262
    • Yang, Y.1    Fu, W.2    Chen, J.3
  • 97
    • 78650758398 scopus 로고    scopus 로고
    • Sirt1 improves healthy ageing and protects from metabolic syndrome-associated cancer
    • Herranz D,Munoz-Martin M,Canamero M,et al.Sirt1 improves healthy ageing and protects from metabolic syndrome-associated cancer.Nat Commun. 2010;1:3.
    • (2010) Nat Commun , vol.1 , pp. 3
    • Herranz, D.1    Munoz-Martin, M.2    Canamero, M.3
  • 98
    • 73449100838 scopus 로고    scopus 로고
    • Resveratrol: its biologic targets and functional activity
    • Pervaiz S,Holme AL.Resveratrol: its biologic targets and functional activity.Antioxid Redox Signal. 2009;11:2851-97.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2851-2897
    • Pervaiz, S.1    Holme, A.L.2
  • 99
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: the in vivo evidence
    • Baur JA,Sinclair DA.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
  • 100
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne JC,Lambert PD,Schenk S,et al.Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes.Nature. 2007;450:712-6.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3
  • 101
    • 77950246109 scopus 로고    scopus 로고
    • SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
    • Pacholec M,Bleasdale JE,Chrunyk B,et al.SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1.J Biol Chem. 2010;285:8340-51.
    • (2010) J Biol Chem , vol.285 , pp. 8340-8351
    • Pacholec, M.1    Bleasdale, J.E.2    Chrunyk, B.3
  • 102
    • 78650184332 scopus 로고    scopus 로고
    • SIRT1-independent mechanisms of the putative sirtuin enzyme activators SRT1720 and SRT2183
    • Huber JL,McBurney MW,Distefano PS,McDonagh T.SIRT1-independent mechanisms of the putative sirtuin enzyme activators SRT1720 and SRT2183.Future Med Chem. 2010;2:1751-9.
    • (2010) Future Med Chem , vol.2 , pp. 1751-1759
    • Huber, J.L.1    McBurney, M.W.2    Distefano, P.S.3    McDonagh, T.4
  • 103
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis
    • Cohen HY,Lavu S,Bitterman KJ,et al.Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis.Mol Cell. 2004;13:627-38.
    • (2004) Mol Cell , vol.13 , pp. 627-638
    • Cohen, H.Y.1    Lavu, S.2    Bitterman, K.J.3
  • 104
  • 105
    • 28544444366 scopus 로고    scopus 로고
    • Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival
    • Ford J,Jiang M,Milner J.Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival.Cancer Res. 2005;65:10457-63.
    • (2005) Cancer Res , vol.65 , pp. 10457-10463
    • Ford, J.1    Jiang, M.2    Milner, J.3
  • 106
    • 42949156843 scopus 로고    scopus 로고
    • p53 activation: a case against Sir
    • Brooks CL,Gu W.p53 activation: a case against Sir.Cancer Cell. 2008;13:377-8.
    • (2008) Cancer Cell , vol.13 , pp. 377-378
    • Brooks, C.L.1    Gu, W.2
  • 107
    • 60149091562 scopus 로고    scopus 로고
    • Salermide, a sirtuin inhibitor with a strong cancer-specific proapoptotic effect
    • Lara E,Mai A,Calvanese V,et al.Salermide, a sirtuin inhibitor with a strong cancer-specific proapoptotic effect.Oncogene. 2009;28:781-91.
    • (2009) Oncogene , vol.28 , pp. 781-791
    • Lara, E.1    Mai, A.2    Calvanese, V.3
  • 108
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: biological insights and disease relevance
    • Haigis MC,Sinclair DA.Mammalian sirtuins: biological insights and disease relevance.Annu Rev Pathol. 2010;5:253-95.
    • (2010) Annu Rev Pathol , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 109
    • 33646254136 scopus 로고    scopus 로고
    • Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes
    • Heltweg B,Gatbonton T,Schuler AD,et al.Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes.Cancer Res. 2006;66:4368-77.
    • (2006) Cancer Res , vol.66 , pp. 4368-4377
    • Heltweg, B.1    Gatbonton, T.2    Schuler, A.D.3
  • 110
    • 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,et al.Sirt1 inhibitor, sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells.Oncogene. 2006;25:176-85.
    • (2006) Oncogene , vol.25 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3
  • 112
    • 35548936745 scopus 로고    scopus 로고
    • Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins)
    • Trapp J,Meier R,Hongwiset D,Kassack MU,Sippl W,Jung M.Structure-activity studies on suramin analogues as inhibitors of NAD+-dependent histone deacetylases (sirtuins).Chem Med Chem. 2007;2:1419-31.
    • (2007) Chem Med Chem , vol.2 , pp. 1419-1431
    • Trapp, J.1    Meier, R.2    Hongwiset, D.3    Kassack, M.U.4    Sippl, W.5    Jung, M.6
  • 113
    • 42949114938 scopus 로고    scopus 로고
    • Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator
    • Lain S,Hollick JJ,Campbell J,et al.Discovery, in vivo activity, and mechanism of action of a small-molecule p53 activator.Cancer Cell. 2008;13:454-63.
    • (2008) Cancer Cell , vol.13 , pp. 454-463
    • Lain, S.1    Hollick, J.J.2    Campbell, J.3
  • 114
    • 77950835404 scopus 로고    scopus 로고
    • SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2
    • Peck B,Chen CY,Ho KK,et al.SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2.Mol Cancer Ther. 2010;9:844-55.
    • (2010) Mol Cancer Ther , vol.9 , pp. 844-855
    • Peck, B.1    Chen, C.Y.2    Ho, K.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.