메뉴 건너뛰기




Volumn 4, Issue 3-4, 2013, Pages 172-182

Stress Inducibility of SIRT1 and Its Role in Cytoprotection and Cancer

Author keywords

apoptosis; cancer; chaperones; cytoprotection; genotoxic stress; heat shock response; HSF1; metabolic stress; SIRT1; stress responses

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HEAT SHOCK TRANSCRIPTION FACTOR 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; PEPTIDASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; PROTEIN P53; REACTIVE OXYGEN METABOLITE; RECQ HELICASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SENTRIN SPECIFIC PEPTIDASE 1; SIRTUIN 1; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FKHRL1; UNCLASSIFIED DRUG;

EID: 84887412756     PISSN: 19476019     EISSN: 19476027     Source Type: Journal    
DOI: 10.1177/1947601913484497     Document Type: Article
Times cited : (54)

References (151)
  • 1
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann CB,Sherman JM,Devine SE,Cameron EE,Pillus L,Boeke JD.The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability.Genes Dev. 1995;9:2888-902.
    • (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
    • 0018564390 scopus 로고
    • A suppressor of mating-type locus mutations in Saccharomyces cerevisiae: evidence for and identification of cryptic mating-type loci
    • Rine J,Strathern JN,Hicks JB,Herskowitz I.A suppressor of mating-type locus mutations in Saccharomyces cerevisiae: evidence for and identification of cryptic mating-type loci.Genetics. 1979;93:877-901.
    • (1979) Genetics , vol.93 , pp. 877-901
    • Rine, J.1    Strathern, J.N.2    Hicks, J.B.3    Herskowitz, I.4
  • 3
    • 0030831573 scopus 로고    scopus 로고
    • Direct evidence for SIR2 modulation of chromatin structure in yeast rDNA
    • Fritze CE,Verschueren K,Strich R,Easton Esposito R.Direct evidence for SIR2 modulation of chromatin structure in yeast rDNA.EMBO J. 1997;16:6495-509.
    • (1997) EMBO J , vol.16 , pp. 6495-6509
    • Fritze, C.E.1    Verschueren, K.2    Strich, R.3    Easton Esposito, R.4
  • 4
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins: emerging roles in physiology, aging, and calorie restriction
    • Haigis MC,Guarente LP.Mammalian sirtuins: emerging roles in physiology, aging, and calorie restriction.Genes Dev. 2006;20:2913-21.
    • (2006) Genes Dev , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 5
    • 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
  • 6
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
    • Landry J,Slama JT,Sternglanz R.Role of NAD(+) in the deacetylase activity of the SIR2-like proteins.Biochem Biophys Res Commun. 2000;278:685-90.
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 685-690
    • Landry, J.1    Slama, J.T.2    Sternglanz, R.3
  • 8
    • 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
  • 9
    • 80053168829 scopus 로고    scopus 로고
    • Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila
    • Burnett C,Valentini S,Cabreiro F,et al.Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila.Nature. 2011;477:482-5.
    • (2011) Nature , vol.477 , pp. 482-485
    • Burnett, C.1    Valentini, S.2    Cabreiro, F.3
  • 10
    • 80053134340 scopus 로고    scopus 로고
    • Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes
    • Viswanathan M,Guarente L.Regulation of Caenorhabditis elegans lifespan by sir-2.1 transgenes.Nature. 2011;477:E1-2.
    • (2011) Nature , vol.477
    • Viswanathan, M.1    Guarente, L.2
  • 11
    • 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
  • 12
    • 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
    • 84855929223 scopus 로고    scopus 로고
    • SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones
    • Donmez G,Arun A,Chung CY,McLean PJ,Lindquist S,Guarente L.SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones.J Neurosci. 2012;32:124-32.
    • (2012) J Neurosci , vol.32 , pp. 124-132
    • Donmez, G.1    Arun, A.2    Chung, C.Y.3    McLean, P.J.4    Lindquist, S.5    Guarente, L.6
  • 16
    • 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
  • 17
    • 40949123149 scopus 로고    scopus 로고
    • Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging
    • Salminen A,Huuskonen J,Ojala J,Kauppinen A,Kaarniranta K,Suuronen T.Activation of innate immunity system during aging: NF-kB signaling is the molecular culprit of inflamm-aging.Ageing Res Rev. 2008;7:83-105.
    • (2008) Ageing Res Rev , vol.7 , pp. 83-105
    • Salminen, A.1    Huuskonen, J.2    Ojala, J.3    Kauppinen, A.4    Kaarniranta, K.5    Suuronen, T.6
  • 18
    • 85042594546 scopus 로고    scopus 로고
    • Effect of short term calorie restriction on pro-inflammatory NF-kB and AP-1 in aged rat kidney
    • Jung KJ,Lee EK,Kim JY,et al.Effect of short term calorie restriction on pro-inflammatory NF-kB and AP-1 in aged rat kidney.Inflamm Res. 2009;58:143-50.
    • (2009) Inflamm Res , vol.58 , pp. 143-150
    • Jung, K.J.1    Lee, E.K.2    Kim, J.Y.3
  • 20
  • 21
    • 27644585190 scopus 로고    scopus 로고
    • A role for SIR-2.1 regulation of ER stress response genes in determining C. elegans life span
    • Viswanathan M,Kim SK,Berdichevsky A,Guarente L.A role for SIR-2.1 regulation of ER stress response genes in determining C. elegans life span.Dev Cell. 2005;9:605-15.
    • (2005) Dev Cell , vol.9 , pp. 605-615
    • Viswanathan, M.1    Kim, S.K.2    Berdichevsky, A.3    Guarente, L.4
  • 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
  • 24
    • 0037221445 scopus 로고    scopus 로고
    • Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases
    • Denu JM.Linking chromatin function with metabolic networks: Sir2 family of NAD(+)-dependent deacetylases.Trends Biochem Sci. 2003;28:41-8.
    • (2003) Trends Biochem Sci , vol.28 , pp. 41-48
    • Denu, J.M.1
  • 26
    • 34249696938 scopus 로고    scopus 로고
    • Extension of human cell lifespan by nicotinamide phosphoribosyltransferase
    • van der Veer E,Ho C,O'Neil C,et al.Extension of human cell lifespan by nicotinamide phosphoribosyltransferase.J Biol Chem. 2007;282:10841-5.
    • (2007) J Biol Chem , vol.282 , pp. 10841-10845
    • van der Veer, E.1    Ho, C.2    O'Neil, C.3
  • 27
    • 0038329323 scopus 로고    scopus 로고
    • Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae
    • Anderson RM,Bitterman KJ,Wood JG,Medvedik O,Sinclair DA.Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae.Nature. 2003;423:181-5.
    • (2003) Nature , vol.423 , pp. 181-185
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Sinclair, D.A.5
  • 28
    • 1642580758 scopus 로고    scopus 로고
    • Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity
    • Gallo CM,Smith DL,Smith JS.Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity.Mol Cell Biol. 2004;24:1301-12.
    • (2004) Mol Cell Biol , vol.24 , pp. 1301-1312
    • Gallo, C.M.1    Smith, D.L.2    Smith, J.S.3
  • 29
    • 55549129616 scopus 로고    scopus 로고
    • Life span extension and neuronal cell protection by Drosophila nicotinamidase
    • Balan V,Miller GS,Kaplun L,et al.Life span extension and neuronal cell protection by Drosophila nicotinamidase.J Biol Chem. 2008;283:27810-9.
    • (2008) J Biol Chem , vol.283 , pp. 27810-27819
    • Balan, V.1    Miller, G.S.2    Kaplun, L.3
  • 30
    • 35348972430 scopus 로고    scopus 로고
    • Genetic links between diet and lifespan: shared mechanisms from yeast to humans
    • Bishop NA,Guarente L.Genetic links between diet and lifespan: shared mechanisms from yeast to humans.Nat Rev Genet. 2007;8:835-44.
    • (2007) Nat Rev Genet , vol.8 , pp. 835-844
    • Bishop, N.A.1    Guarente, L.2
  • 31
    • 0024656069 scopus 로고
    • The effect of retarded growth upon the length of life span and upon the ultimate body size: 1935
    • McCay CM,Crowell MF,Maynard LA.The effect of retarded growth upon the length of life span and upon the ultimate body size: 1935.Nutrition. 1989;5:155 72-71.
    • (1989) Nutrition , vol.5 , pp. 15571-15572
    • McCay, C.M.1    Crowell, M.F.2    Maynard, L.A.3
  • 32
    • 27744511769 scopus 로고    scopus 로고
    • Regulation of yeast replicative life span by TOR and Sch9 in response to nutrients
    • Kaeberlein M,Powers RW,Steffen KK,et al.Regulation of yeast replicative life span by TOR and Sch9 in response to nutrients.Science. 2005;310:1193-6.
    • (2005) Science , vol.310 , pp. 1193-1196
    • Kaeberlein, M.1    Powers, R.W.2    Steffen, K.K.3
  • 34
    • 36849087923 scopus 로고    scopus 로고
    • Caenorhabditis elegans 2007: the premier model for the study of aging
    • Johnson TE.Caenorhabditis elegans 2007: the premier model for the study of aging.Exp Gerontol. 2008;43:1-4.
    • (2008) Exp Gerontol , vol.43 , pp. 1-4
    • Johnson, T.E.1
  • 35
    • 63549108476 scopus 로고    scopus 로고
    • Different dietary restriction regimens extend lifespan by both independent and overlapping genetic pathways in C-elegans
    • Greer EL,Brunet A.Different dietary restriction regimens extend lifespan by both independent and overlapping genetic pathways in C-elegans.Aging Cell. 2009;8:113-27.
    • (2009) Aging Cell , vol.8 , pp. 113-127
    • Greer, E.L.1    Brunet, A.2
  • 36
    • 40549146580 scopus 로고    scopus 로고
    • Role of dFOXO in lifespan extension by dietary restriction in Drosophila melanogaster: not required, but its activity modulates the response
    • Giannakou ME,Goss M,Partridge L.Role of dFOXO in lifespan extension by dietary restriction in Drosophila melanogaster: not required, but its activity modulates the response.Aging Cell. 2008;7:187-98.
    • (2008) Aging Cell , vol.7 , pp. 187-198
    • Giannakou, M.E.1    Goss, M.2    Partridge, L.3
  • 37
    • 40549127471 scopus 로고    scopus 로고
    • Drosophila lifespan control by dietary restriction independent of insulin-like signaling
    • Min KJ,Yamamoto R,Buch S,Pankratz M,Tatar M.Drosophila lifespan control by dietary restriction independent of insulin-like signaling.Aging Cell. 2008;7:199-206.
    • (2008) Aging Cell , vol.7 , pp. 199-206
    • Min, K.J.1    Yamamoto, R.2    Buch, S.3    Pankratz, M.4    Tatar, M.5
  • 39
    • 77952288176 scopus 로고    scopus 로고
    • Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARalpha in mice
    • Hayashida S,Arimoto A,Kuramoto Y,et al.Fasting promotes the expression of SIRT1, an NAD+-dependent protein deacetylase, via activation of PPARalpha in mice.Mol Cell Biochem. 2010;339:285-92.
    • (2010) Mol Cell Biochem , vol.339 , pp. 285-292
    • Hayashida, S.1    Arimoto, A.2    Kuramoto, Y.3
  • 40
    • 0345731468 scopus 로고    scopus 로고
    • Yeast life-span extension by calorie restriction is independent of NAD fluctuation
    • Anderson RM,Latorre-Esteves M,Neves AR,et al.Yeast life-span extension by calorie restriction is independent of NAD fluctuation.Science. 2003;302:2124-6.
    • (2003) Science , vol.302 , pp. 2124-2126
    • Anderson, R.M.1    Latorre-Esteves, M.2    Neves, A.R.3
  • 41
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin SJ,Ford E,Haigis M,Liszt G,Guarente L.Calorie restriction extends yeast life span by lowering the level of NADH.Genes Dev. 2004;18:12-6.
    • (2004) Genes Dev , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 42
    • 79951790057 scopus 로고    scopus 로고
    • Multiple pathways regulating the calorie restriction response in yeast
    • Rahat O,Maoz N,Cohen HY.Multiple pathways regulating the calorie restriction response in yeast.J Gerontol A Biol Sci Med Sci. 2011;66:163-9.
    • (2011) J Gerontol A Biol Sci Med Sci , vol.66 , pp. 163-169
    • Rahat, O.1    Maoz, N.2    Cohen, H.Y.3
  • 43
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • Lin SJ,Kaeberlein M,Andalis AA,et al.Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration.Nature. 2002;418:344-8.
    • (2002) Nature , vol.418 , pp. 344-348
    • Lin, S.J.1    Kaeberlein, M.2    Andalis, A.A.3
  • 44
    • 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;7:3669-79.
    • (2008) Cell Cycle , vol.7 , pp. 3669-3679
    • Fulco, M.1    Sartorelli, V.2
  • 45
    • 67349276169 scopus 로고    scopus 로고
    • AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
    • Canto C,Gerhart-Hines Z,Feige JN,et al.AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity.Nature. 2009;458:1056-60.
    • (2009) Nature , vol.458 , pp. 1056-1060
    • Canto, C.1    Gerhart-Hines, Z.2    Feige, J.N.3
  • 46
    • 77249156847 scopus 로고    scopus 로고
    • Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle
    • Canto C,Jiang LQ,Deshmukh AS,et al.Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle.Cell Metab. 2010;11:213-9.
    • (2010) Cell Metab , vol.11 , pp. 213-219
    • Canto, C.1    Jiang, L.Q.2    Deshmukh, A.S.3
  • 47
    • 10644282295 scopus 로고    scopus 로고
    • The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans
    • Apfeld J,O'Connor G,McDonagh T,DiStefano PS,Curtis R.The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans.Genes Dev. 2004;18:3004-9.
    • (2004) Genes Dev , vol.18 , pp. 3004-3009
    • Apfeld, J.1    O'Connor, G.2    McDonagh, T.3    DiStefano, P.S.4    Curtis, R.5
  • 48
    • 22344443522 scopus 로고    scopus 로고
    • A systematic RNAi screen for longevity genes in C. elegans
    • Hamilton B,Dong Y,Shindo M,et al.A systematic RNAi screen for longevity genes in C. elegans.Genes Dev. 2005;19:1544-55.
    • (2005) Genes Dev , vol.19 , pp. 1544-1555
    • Hamilton, B.1    Dong, Y.2    Shindo, M.3
  • 50
    • 28844469898 scopus 로고    scopus 로고
    • Increase in activity during calorie restriction requires Sirt1
    • Chen D,Steele AD,Lindquist S,Guarente L.Increase in activity during calorie restriction requires Sirt1.Science. 2005;310:1641.
    • (2005) Science , vol.310 , pp. 1641
    • Chen, D.1    Steele, A.D.2    Lindquist, S.3    Guarente, L.4
  • 51
    • 84865246956 scopus 로고    scopus 로고
    • Heat shock and caloric restriction have a synergistic effect on the heat shock response in a sir2.1-dependent manner in Caenorhabditis elegans
    • Raynes R,Leckey BD,Nguyen K,Westerheide SD.Heat shock and caloric restriction have a synergistic effect on the heat shock response in a sir2.1-dependent manner in Caenorhabditis elegans.J Biol Chem. 2012;287:29045-53.
    • (2012) J Biol Chem , vol.287 , pp. 29045-29053
    • Raynes, R.1    Leckey, B.D.2    Nguyen, K.3    Westerheide, S.D.4
  • 52
    • 18644364411 scopus 로고    scopus 로고
    • DBC2, a candidate for a tumor suppressor gene involved in breast cancer
    • Hamaguchi M,Meth JL,von Klitzing C,et al.DBC2, a candidate for a tumor suppressor gene involved in breast cancer.Proc Natl Acad Sci U S A. 2002;99:13647-52.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13647-13652
    • Hamaguchi, M.1    Meth, J.L.2    von Klitzing, C.3
  • 53
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • Kim JE,Chen J,Lou Z.DBC1 is a negative regulator of SIRT1.Nature. 2008;451:583-6.
    • (2008) Nature , vol.451 , pp. 583-586
    • Kim, J.E.1    Chen, J.2    Lou, Z.3
  • 54
  • 55
    • 78649852533 scopus 로고    scopus 로고
    • SIRT1 is regulated by a PPARg-SIRT1 negative feedback loop associated with senescence
    • Han L,Zhou R,Niu J,McNutt MA,Wang P,Tong T.SIRT1 is regulated by a PPARg-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
  • 56
    • 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
  • 57
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim EJ,Kho JH,Kang MR,Um SJ.Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity.Mol Cell. 2007;28:277-90.
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 58
    • 58149202185 scopus 로고    scopus 로고
    • Phosphorylation regulates SIRT1 function
    • Sasaki T,Maier B,Koclega KD,et al.Phosphorylation regulates SIRT1 function.PLoS One. 2008;3:e4020.
    • (2008) PLoS One , vol.3
    • Sasaki, T.1    Maier, B.2    Koclega, K.D.3
  • 59
    • 77949539030 scopus 로고    scopus 로고
    • JNK1 phosphorylates SIRT1 and promotes its enzymatic activity
    • Nasrin N,Kaushik VK,Fortier E,et al.JNK1 phosphorylates SIRT1 and promotes its enzymatic activity.PLoS One. 2009;4:e8414.
    • (2009) PLoS One , vol.4
    • Nasrin, N.1    Kaushik, V.K.2    Fortier, E.3
  • 61
    • 79956331962 scopus 로고    scopus 로고
    • Cancer cell survival following DNA damage-mediated premature senescence is regulated by mammalian target of rapamycin (mTOR)-dependent inhibition of sirtuin 1
    • Back JH,Rezvani HR,Zhu Y,et al.Cancer cell survival following DNA damage-mediated premature senescence is regulated by mammalian target of rapamycin (mTOR)-dependent inhibition of sirtuin 1.J Biol Chem. 2011;286:19100-8.
    • (2011) J Biol Chem , vol.286 , pp. 19100-19108
    • Back, J.H.1    Rezvani, H.R.2    Zhu, Y.3
  • 63
    • 69949138641 scopus 로고    scopus 로고
    • CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage
    • Kang H,Jung JW,Kim MK,Chung JH.CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage.PLoS One. 2009;4:e6611.
    • (2009) PLoS One , vol.4
    • Kang, H.1    Jung, J.W.2    Kim, M.K.3    Chung, J.H.4
  • 64
    • 62049084424 scopus 로고    scopus 로고
    • Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2
    • Zschoernig B,Mahlknecht U.Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2.Biochem Biophys Res Commun. 2009;381:372-7.
    • (2009) Biochem Biophys Res Commun , vol.381 , pp. 372-377
    • Zschoernig, B.1    Mahlknecht, U.2
  • 66
    • 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
  • 67
    • 79952124926 scopus 로고    scopus 로고
    • Methyltransferase Set7/9 regulates p53 activity by interacting with sirtuin 1 (SIRT1)
    • Liu X,Wang D,Zhao Y,et al.Methyltransferase Set7/9 regulates p53 activity by interacting with sirtuin 1 (SIRT1).Proc Natl Acad Sci U S A. 2011;108:1925-30.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 1925-1930
    • Liu, X.1    Wang, D.2    Zhao, Y.3
  • 68
    • 78149284226 scopus 로고    scopus 로고
    • GAPDH mediates nitrosylation of nuclear proteins
    • Kornberg MD,Sen N,Hara MR,et al.GAPDH mediates nitrosylation of nuclear proteins.Nat Cell Biol. 2010;12:1094-100.
    • (2010) Nat Cell Biol , vol.12 , pp. 1094-1100
    • Kornberg, M.D.1    Sen, N.2    Hara, M.R.3
  • 69
    • 77953292238 scopus 로고    scopus 로고
    • SIRT1 and p53, effect on cancer, senescence and beyond
    • Yi J,Luo J.SIRT1 and p53, effect on cancer, senescence and beyond.Biochim Biophys Acta. 2010;1804:1684-9.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1684-1689
    • Yi, J.1    Luo, J.2
  • 70
    • 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
  • 71
    • 65349096174 scopus 로고    scopus 로고
    • A c-Myc-SIRT1 feedback loop regulates cell growth and transformation
    • Yuan J,Minter-Dykhouse K,Lou Z.A c-Myc-SIRT1 feedback loop regulates cell growth and transformation.J Cell Biol. 2009;185:203-11.
    • (2009) J Cell Biol , vol.185 , pp. 203-211
    • Yuan, J.1    Minter-Dykhouse, K.2    Lou, Z.3
  • 72
    • 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
  • 73
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • Purushotham A,Schug TT,Xu Q,Surapureddi S,Guo X,Li X.Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation.Cell Metab. 2009;9:327-38.
    • (2009) Cell Metab , vol.9 , pp. 327-338
    • Purushotham, A.1    Schug, T.T.2    Xu, Q.3    Surapureddi, S.4    Guo, X.5    Li, X.6
  • 74
    • 77953633702 scopus 로고    scopus 로고
    • PPARbeta/delta regulates the human SIRT1 gene transcription via Sp1
    • Okazaki M,Iwasaki Y,Nishiyama M,et al.PPARbeta/delta regulates the human SIRT1 gene transcription via Sp1.Endocr J. 2010;57:403-13.
    • (2010) Endocr J , vol.57 , pp. 403-413
    • Okazaki, M.1    Iwasaki, Y.2    Nishiyama, M.3
  • 75
    • 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
  • 76
    • 33846505019 scopus 로고    scopus 로고
    • Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex
    • Zhang Q,Wang SY,Fleuriel C,et al.Metabolic regulation of SIRT1 transcription via a HIC1:CtBP corepressor complex.Proc Natl Acad Sci U S A. 2007;104:829-33.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 829-833
    • Zhang, Q.1    Wang, S.Y.2    Fleuriel, C.3
  • 78
    • 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
  • 79
    • 62449117918 scopus 로고    scopus 로고
    • MiR-34, SIRT1 and p53: the feedback loop
    • Yamakuchi M,Lowenstein CJ.MiR-34, SIRT1 and p53: the feedback loop.Cell Cycle. 2009;8:712-5.
    • (2009) Cell Cycle , vol.8 , pp. 712-715
    • Yamakuchi, M.1    Lowenstein, C.J.2
  • 80
    • 34249812122 scopus 로고    scopus 로고
    • MicroRNA-34a functions as a potential tumor suppressor by inducing apoptosis in neuroblastoma cells
    • Welch C,Chen Y,Stallings RL.MicroRNA-34a functions as a potential tumor suppressor by inducing apoptosis in neuroblastoma cells.Oncogene. 2007;26:5017-22.
    • (2007) Oncogene , vol.26 , pp. 5017-5022
    • Welch, C.1    Chen, Y.2    Stallings, R.L.3
  • 81
    • 77951210885 scopus 로고    scopus 로고
    • A pathway involving farnesoid X receptor and small heterodimer partner positively regulates hepatic sirtuin 1 levels via microRNA-34a inhibition
    • Lee J,Padhye A,Sharma A,et al.A pathway involving farnesoid X receptor and small heterodimer partner positively regulates hepatic sirtuin 1 levels via microRNA-34a inhibition.J Biol Chem. 2010;285:12604-11.
    • (2010) J Biol Chem , vol.285 , pp. 12604-12611
    • Lee, J.1    Padhye, A.2    Sharma, A.3
  • 82
    • 80052908737 scopus 로고    scopus 로고
    • MicroRNA-195 promotes palmitate-induced apoptosis in cardiomyocytes by down-regulating Sirt1
    • Zhu H,Yang Y,Wang Y,Li J,Schiller PW,Peng T.MicroRNA-195 promotes palmitate-induced apoptosis in cardiomyocytes by down-regulating Sirt1.Cardiovasc Res. 2011;92:75-84.
    • (2011) Cardiovasc Res , vol.92 , pp. 75-84
    • Zhu, H.1    Yang, Y.2    Wang, Y.3    Li, J.4    Schiller, P.W.5    Peng, T.6
  • 83
    • 65249185780 scopus 로고    scopus 로고
    • Downregulation of miR-199a derepresses hypoxia-inducible factor-1alpha and sirtuin 1 and recapitulates hypoxia preconditioning in cardiac myocytes
    • Rane S,He M,Sayed D,et al.Downregulation of miR-199a derepresses hypoxia-inducible factor-1alpha and sirtuin 1 and recapitulates hypoxia preconditioning in cardiac myocytes.Circ Res. 2009;104:879-86.
    • (2009) Circ Res , vol.104 , pp. 879-886
    • Rane, S.1    He, M.2    Sayed, D.3
  • 84
    • 79953225194 scopus 로고    scopus 로고
    • Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization
    • Kawai Y,Garduno L,Theodore M,Yang J,Arinze IJ.Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization.J Biol Chem. 2011;286:7629-40.
    • (2011) J Biol Chem , vol.286 , pp. 7629-7640
    • Kawai, Y.1    Garduno, L.2    Theodore, M.3    Yang, J.4    Arinze, I.J.5
  • 85
    • 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
  • 86
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY,Miller C,Bitterman KJ,et al.Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase.Science. 2004;305:390-2.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3
  • 87
    • 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
  • 88
    • 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
  • 89
    • 43149118368 scopus 로고    scopus 로고
    • Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation
    • Li K,Casta A,Wang R,et al.Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation.J Biol Chem. 2008;283:7590-8.
    • (2008) J Biol Chem , vol.283 , pp. 7590-7598
    • Li, K.1    Casta, A.2    Wang, R.3
  • 90
    • 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
  • 91
    • 37549016377 scopus 로고    scopus 로고
    • A functional link between SIRT1 deacetylase and NBS1 in DNA damage response
    • Yuan Z,Seto E.A functional link between SIRT1 deacetylase and NBS1 in DNA damage response.Cell Cycle. 2007;6:2869-71.
    • (2007) Cell Cycle , vol.6 , pp. 2869-2871
    • Yuan, Z.1    Seto, E.2
  • 92
    • 84860340226 scopus 로고    scopus 로고
    • Activation of p53/ATM-dependent DNA damage signaling pathway by shiga toxin in mammalian cells
    • Talukder KA,Azmi IJ,Ahmed KA,et al.Activation of p53/ATM-dependent DNA damage signaling pathway by shiga toxin in mammalian cells.Microb Pathog. 2012;52:311-7.
    • (2012) Microb Pathog , vol.52 , pp. 311-317
    • Talukder, K.A.1    Azmi, I.J.2    Ahmed, K.A.3
  • 93
    • 0033555260 scopus 로고    scopus 로고
    • A role for ATR in the DNA damage-induced phosphorylation of p53
    • Tibbetts RS,Brumbaugh KM,Williams JM,et al.A role for ATR in the DNA damage-induced phosphorylation of p53.Genes Dev. 1999;13:152-7.
    • (1999) Genes Dev , vol.13 , pp. 152-157
    • Tibbetts, R.S.1    Brumbaugh, K.M.2    Williams, J.M.3
  • 94
    • 33645222458 scopus 로고    scopus 로고
    • The involvement of MAPK signaling pathways in determining the cellular response to p53 activation: cell cycle arrest or apoptosis
    • Brown L,Benchimol S.The involvement of MAPK signaling pathways in determining the cellular response to p53 activation: cell cycle arrest or apoptosis.J Biol Chem. 2006;281:3832-40.
    • (2006) J Biol Chem , vol.281 , pp. 3832-3840
    • Brown, L.1    Benchimol, S.2
  • 95
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim EJ,Kho JH,Kang MR,Um SJ.Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity.Mol Cell. 2007;28:277-90.
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 96
    • 79953193084 scopus 로고    scopus 로고
    • MST1 promotes apoptosis through regulating Sirt1-dependent p53 deacetylation
    • Yuan F,Xie Q,Wu J,et al.MST1 promotes apoptosis through regulating Sirt1-dependent p53 deacetylation.J Biol Chem. 2011;286:6940-5.
    • (2011) J Biol Chem , vol.286 , pp. 6940-6945
    • Yuan, F.1    Xie, Q.2    Wu, J.3
  • 97
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • Cheng HL,Mostoslavsky R,Saito S,et al.Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice.Proc Natl Acad Sci U S A. 2003;100:10794-9.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10794-10799
    • Cheng, H.L.1    Mostoslavsky, R.2    Saito, S.3
  • 98
    • 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
  • 99
    • 0034643331 scopus 로고    scopus 로고
    • AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1
    • Medema RH,Kops GJ,Bos JL,Burgering BM.AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1.Nature. 2000;404:782-7.
    • (2000) Nature , vol.404 , pp. 782-787
    • Medema, R.H.1    Kops, G.J.2    Bos, J.L.3    Burgering, B.M.4
  • 100
    • 0037136563 scopus 로고    scopus 로고
    • Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress
    • Kops GJ,Dansen TB,Polderman PE,et al.Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress.Nature. 2002;419:316-21.
    • (2002) Nature , vol.419 , pp. 316-321
    • Kops, G.J.1    Dansen, T.B.2    Polderman, P.E.3
  • 101
    • 27844497945 scopus 로고    scopus 로고
    • FOXO transcription factors at the interface between longevity and tumor suppression
    • Greer EL,Brunet A.FOXO transcription factors at the interface between longevity and tumor suppression.Oncogene. 2005;24:7410-25.
    • (2005) Oncogene , vol.24 , pp. 7410-7425
    • Greer, E.L.1    Brunet, A.2
  • 103
    • 20144365700 scopus 로고    scopus 로고
    • Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes
    • Frescas D,Valenti L,Accili D.Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes.J Biol Chem. 2005;280:20589-95.
    • (2005) J Biol Chem , vol.280 , pp. 20589-20595
    • Frescas, D.1    Valenti, L.2    Accili, D.3
  • 104
    • 3042750643 scopus 로고    scopus 로고
    • Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity
    • Daitoku H,Hatta M,Matsuzaki H,et al.Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity.Proc Natl Acad Sci U S A. 2004;101:10042-7.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10042-10047
    • Daitoku, H.1    Hatta, M.2    Matsuzaki, H.3
  • 106
    • 1842431822 scopus 로고    scopus 로고
    • Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1 complex
    • Lee JH,Paull TT.Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1 complex.Science. 2004;304:93-6.
    • (2004) Science , vol.304 , pp. 93-96
    • Lee, J.H.1    Paull, T.T.2
  • 107
    • 3242892589 scopus 로고    scopus 로고
    • Nijmegen breakage syndrome: clinical manifestation of defective response to DNA double-strand breaks
    • Digweed M,Sperling K.Nijmegen breakage syndrome: clinical manifestation of defective response to DNA double-strand breaks.DNA Repair (Amst). 2004;3:1207-17.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1207-1217
    • Digweed, M.1    Sperling, K.2
  • 108
    • 24044521924 scopus 로고    scopus 로고
    • Current advances in unraveling the function of the Werner syndrome protein
    • Ozgenc A,Loeb LA.Current advances in unraveling the function of the Werner syndrome protein.Mutat Res. 2005;577:237-51.
    • (2005) Mutat Res , vol.577 , pp. 237-251
    • Ozgenc, A.1    Loeb, L.A.2
  • 110
    • 42449160125 scopus 로고    scopus 로고
    • Regulation of the proapoptotic factor Bax by Ku70-dependent deubiquitylation
    • Amsel AD,Rathaus M,Kronman N,Cohen HY.Regulation of the proapoptotic factor Bax by Ku70-dependent deubiquitylation.Proc Natl Acad Sci U S A. 2008;105:5117-22.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5117-5122
    • Amsel, A.D.1    Rathaus, M.2    Kronman, N.3    Cohen, H.Y.4
  • 112
    • 33749638442 scopus 로고    scopus 로고
    • Modulation of oxidative stress-induced changes in hypertension and atherosclerosis by antioxidants
    • Vasdev S,Gill VD,Singal PK.Modulation of oxidative stress-induced changes in hypertension and atherosclerosis by antioxidants.Exp Clin Cardiol. 2006;11:206-16.
    • (2006) Exp Clin Cardiol , vol.11 , pp. 206-216
    • Vasdev, S.1    Gill, V.D.2    Singal, P.K.3
  • 113
    • 67649402187 scopus 로고    scopus 로고
    • The Nrf2- antioxidant response element signaling pathway and its activation by oxidative stress
    • Nguyen T,Nioi P,Pickett CB.The Nrf2- antioxidant response element signaling pathway and its activation by oxidative stress.J Biol Chem. 2009;284:13291-5.
    • (2009) J Biol Chem , vol.284 , pp. 13291-13295
    • Nguyen, T.1    Nioi, P.2    Pickett, C.B.3
  • 114
    • 79953225194 scopus 로고    scopus 로고
    • Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization
    • Kawai Y,Garduno L,Theodore M,Yang J,Arinze IJ.Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization.J Biol Chem. 2011;286:7629-40.
    • (2011) J Biol Chem , vol.286 , pp. 7629-7640
    • Kawai, Y.1    Garduno, L.2    Theodore, M.3    Yang, J.4    Arinze, I.J.5
  • 115
    • 4544342570 scopus 로고    scopus 로고
    • Nuclear factor-kappaB: the enemy within
    • Aggarwal BB.Nuclear factor-kappaB: the enemy within.Cancer Cell. 2004;6:203-8.
    • (2004) Cancer Cell , vol.6 , pp. 203-208
    • Aggarwal, B.B.1
  • 116
    • 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
  • 117
    • 39749087530 scopus 로고    scopus 로고
    • SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization
    • Han MK,Song EK,Guo Y,Ou X,Mantel C,Broxmeyer HE.SIRT1 regulates apoptosis and Nanog expression in mouse embryonic stem cells by controlling p53 subcellular localization.Cell Stem Cell. 2008;2:241-51.
    • (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
  • 119
    • 84867380741 scopus 로고    scopus 로고
    • Janus-faced role of SIRT1 in tumorigenesis
    • Song NY,Surh YJ.Janus-faced role of SIRT1 in tumorigenesis.Ann N Y Acad Sci. 2012;1271:10-9.
    • (2012) Ann N Y Acad Sci , vol.1271 , pp. 10-19
    • Song, N.Y.1    Surh, Y.J.2
  • 120
    • 80054782483 scopus 로고    scopus 로고
    • The dual role of sirtuins in cancer
    • Bosch-Presegue L,Vaquero A.The dual role of sirtuins in cancer.Genes Cancer. 2011;2:648-62.
    • (2011) Genes Cancer , vol.2 , pp. 648-662
    • Bosch-Presegue, L.1    Vaquero, A.2
  • 121
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide SD,Morimoto RI.Heat shock response modulators as therapeutic tools for diseases of protein conformation.J Biol Chem. 2005;280:33097-100.
    • (2005) J Biol Chem , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 122
    • 84934443868 scopus 로고    scopus 로고
    • Heat shock factor 1 as a coordinator of stress and developmental pathways
    • Anckar J,Sistonen L.Heat shock factor 1 as a coordinator of stress and developmental pathways.Adv Exp Med Biol. 2007;594:78-88.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 78-88
    • Anckar, J.1    Sistonen, L.2
  • 123
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • Kline MP,Morimoto RI.Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation.Mol Cell Biol. 1997;17:2107-15.
    • (1997) Mol Cell Biol , vol.17 , pp. 2107-2115
    • Kline, M.P.1    Morimoto, R.I.2
  • 124
    • 15944373162 scopus 로고    scopus 로고
    • Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo
    • Tang D,Khaleque MA,Jones EL,et al.Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo.Cell Stress Chaperones. 2005;10:46-58.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 46-58
    • Tang, D.1    Khaleque, M.A.2    Jones, E.L.3
  • 125
    • 84860377679 scopus 로고    scopus 로고
    • Discrimination of clinical stages in non-small cell lung cancer patients by serum HSP27 and HSP70: a multi-institutional case-control study
    • Zimmermann M,Nickl S,Lambers C,et al.Discrimination of clinical stages in non-small cell lung cancer patients by serum HSP27 and HSP70: a multi-institutional case-control study.Clin Chim Acta. 2012;413:1115-20.
    • (2012) Clin Chim Acta , vol.413 , pp. 1115-1120
    • Zimmermann, M.1    Nickl, S.2    Lambers, C.3
  • 126
    • 0028044818 scopus 로고
    • Differential expression of heat shock proteins in pancreatic carcinoma
    • Gress TM,Muller-Pillasch F,Weber C,et al.Differential expression of heat shock proteins in pancreatic carcinoma.Cancer Res. 1994;54:547-51.
    • (1994) Cancer Res , vol.54 , pp. 547-551
    • Gress, T.M.1    Muller-Pillasch, F.2    Weber, C.3
  • 127
    • 0037334496 scopus 로고    scopus 로고
    • Clinical significance of heat shock protein-70 expression in bladder cancer
    • Syrigos KN,Harrington KJ,Karayiannakis AJ,et al.Clinical significance of heat shock protein-70 expression in bladder cancer.Urology. 2003;61:677-80.
    • (2003) Urology , vol.61 , pp. 677-680
    • Syrigos, K.N.1    Harrington, K.J.2    Karayiannakis, A.J.3
  • 128
    • 84859771372 scopus 로고    scopus 로고
    • Amplification and high-level expression of heat shock protein 90 marks aggressive phenotypes of human epidermal growth factor receptor 2 negative breast cancer
    • Cheng Q,Chang JT,Geradts J,et al.Amplification and high-level expression of heat shock protein 90 marks aggressive phenotypes of human epidermal growth factor receptor 2 negative breast cancer.Breast Cancer Res. 2012;14:R62.
    • (2012) Breast Cancer Res , vol.14
    • Cheng, Q.1    Chang, J.T.2    Geradts, J.3
  • 129
    • 84887426617 scopus 로고    scopus 로고
    • Amsterdam: Harwood Academic Publishers
    • Bukau BAmsterdam: Harwood Academic Publishers; 1999:.
    • (1999)
    • Bukau, B.1
  • 130
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU.Molecular chaperones in cellular protein folding.Nature. 1996;381:571-9.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 131
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB,Toft DO.Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.Exp Biol Med (Maywood). 2003;228:111-33.
    • (2003) Exp Biol Med (Maywood) , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 132
    • 0038377853 scopus 로고    scopus 로고
    • Expression of heat-shock proteins hsp27, hsp70 and hsp90 in malignant epithelial tumour of the ovaries
    • Elpek GO,Karaveli S,Simsek T,Keles N,Aksoy NH.Expression of heat-shock proteins hsp27, hsp70 and hsp90 in malignant epithelial tumour of the ovaries.Apmis. 2003;111:523-30.
    • (2003) Apmis , vol.111 , pp. 523-530
    • Elpek, G.O.1    Karaveli, S.2    Simsek, T.3    Keles, N.4    Aksoy, N.H.5
  • 133
    • 69049099972 scopus 로고    scopus 로고
    • Expression and clinical role of antiapoptotic proteins of the bag, heat shock, and Bcl-2 families in effusions, primary tumors, and solid metastases in ovarian carcinoma
    • Elstrand MB,Kleinberg L,Kohn EC,Trope CG,Davidson B.Expression and clinical role of antiapoptotic proteins of the bag, heat shock, and Bcl-2 families in effusions, primary tumors, and solid metastases in ovarian carcinoma.Int J Gynecol Pathol. 2009;28:211-21.
    • (2009) Int J Gynecol Pathol , vol.28 , pp. 211-221
    • Elstrand, M.B.1    Kleinberg, L.2    Kohn, E.C.3    Trope, C.G.4    Davidson, B.5
  • 134
    • 0029586916 scopus 로고
    • Expression of the heat shock protein HSP27 in human ovarian cancer
    • Langdon SP,Rabiasz GJ,Hirst GL,et al.Expression of the heat shock protein HSP27 in human ovarian cancer.Clin Cancer Res. 1995;1:1603-9.
    • (1995) Clin Cancer Res , vol.1 , pp. 1603-1609
    • Langdon, S.P.1    Rabiasz, G.J.2    Hirst, G.L.3
  • 135
    • 0036832081 scopus 로고    scopus 로고
    • Heat shock proteins and malignancies of the female genital tract
    • 1009
    • Piura B,Rabinovich A,Yavelsky V,Wolfson M.[Heat shock proteins and malignancies of the female genital tract].Harefuah. 2002;141 1009:969 10-72.
    • (2002) Harefuah , vol.141 , pp. 96910-96972
    • Piura, B.1    Rabinovich, A.2    Yavelsky, V.3    Wolfson, M.4
  • 136
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
    • Ciocca DR,Calderwood SK.Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications.Cell Stress Chaperones. 2005;10:86-103.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 137
    • 34547560174 scopus 로고    scopus 로고
    • Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis
    • Ramp U,Mahotka C,Heikaus S,et al.Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis.Histol Histopathol. 2007;22:1099-107.
    • (2007) Histol Histopathol , vol.22 , pp. 1099-1107
    • Ramp, U.1    Mahotka, C.2    Heikaus, S.3
  • 139
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • Mosser DD,Morimoto RI.Molecular chaperones and the stress of oncogenesis.Oncogene. 2004;23:2907-18.
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 140
    • 0032404094 scopus 로고    scopus 로고
    • Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones
    • Garrido C,Fromentin A,Bonnotte B,et al.Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones.Cancer Res. 1998;58:5495-9.
    • (1998) Cancer Res , vol.58 , pp. 5495-5499
    • Garrido, C.1    Fromentin, A.2    Bonnotte, B.3
  • 141
    • 0033578065 scopus 로고    scopus 로고
    • Oncogenic potential of Hsp72
    • Volloch VZ,Sherman MY.Oncogenic potential of Hsp72.Oncogene. 1999;18:3648-51.
    • (1999) Oncogene , vol.18 , pp. 3648-3651
    • Volloch, V.Z.1    Sherman, M.Y.2
  • 142
    • 0028919063 scopus 로고
    • Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells
    • Wei YQ,Zhao X,Kariya Y,Teshigawara K,Uchida A.Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells.Cancer Immunol Immunother. 1995;40:73-8.
    • (1995) Cancer Immunol Immunother , vol.40 , pp. 73-78
    • Wei, Y.Q.1    Zhao, X.2    Kariya, Y.3    Teshigawara, K.4    Uchida, A.5
  • 143
  • 145
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM,Wolf BB,Cain K,et al.Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome.Nat Cell Biol. 2000;2:469-75.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.B.2    Cain, K.3
  • 146
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
    • Kamal A,Thao L,Sensintaffar J,et al.A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors.Nature. 2003;425:407-10.
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 147
    • 34548658230 scopus 로고    scopus 로고
    • Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis
    • Dai C,Whitesell L,Rogers AB,Lindquist S.Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis.Cell. 2007;130:1005-18.
    • (2007) Cell , vol.130 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 148
    • 77956929098 scopus 로고    scopus 로고
    • Heat-shock transcription factor HSF1 has a critical role in human epidermal growth factor receptor-2-induced cellular transformation and tumorigenesis
    • Meng L,Gabai VL,Sherman MY.Heat-shock transcription factor HSF1 has a critical role in human epidermal growth factor receptor-2-induced cellular transformation and tumorigenesis.Oncogene. 2010;29:5204-13.
    • (2010) Oncogene , vol.29 , pp. 5204-5213
    • Meng, L.1    Gabai, V.L.2    Sherman, M.Y.3
  • 149
    • 84867408640 scopus 로고    scopus 로고
    • Heat shock factor Hsf1 cooperates with ErbB2 (Her2/Neu) protein to promote mammary tumorigenesis and metastasis
    • Xi C,Hu Y,Buckhaults P,Moskophidis D,Mivechi NF.Heat shock factor Hsf1 cooperates with ErbB2 (Her2/Neu) protein to promote mammary tumorigenesis and metastasis.J Biol Chem. 2012;287:35646-57.
    • (2012) J Biol Chem , vol.287 , pp. 35646-35657
    • Xi, C.1    Hu, Y.2    Buckhaults, P.3    Moskophidis, D.4    Mivechi, N.F.5
  • 150
    • 34547616810 scopus 로고    scopus 로고
    • Selective suppression of lymphomas by functional loss of Hsf1 in a p53-deficient mouse model for spontaneous tumors
    • Min JN,Huang L,Zimonjic DB,Moskophidis D,Mivechi NF.Selective suppression of lymphomas by functional loss of Hsf1 in a p53-deficient mouse model for spontaneous tumors.Oncogene. 2007;26:5086-97.
    • (2007) Oncogene , vol.26 , pp. 5086-5097
    • Min, J.N.1    Huang, L.2    Zimonjic, D.B.3    Moskophidis, D.4    Mivechi, N.F.5
  • 151
    • 84864585171 scopus 로고    scopus 로고
    • HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers
    • Mendillo ML,Santagata S,Koeva M,et al.HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers.Cell. 2012;150:549-62.
    • (2012) Cell , vol.150 , pp. 549-562
    • Mendillo, M.L.1    Santagata, S.2    Koeva, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.