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Volumn 54, Issue SUPPL., 2012, Pages

SIRT1 as a therapeutic target in inflammaging of the pulmonary disease

Author keywords

COPD; DNA damage response; FOXO3; Histone modifications; Inflammaging; NF B; Oxidative stress; Polyphenols; SIRT1; Tobacco smoke

Indexed keywords

ALDEHYDE; BETA CATENIN; CURCUMIN; DNA; ENDOTHELIAL NITRIC OXIDE SYNTHASE; ENVIRONMENTAL CHEMICAL; HISTONE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KLOTHO PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NOTCH RECEPTOR; OXIDIZING AGENT; POLYPHENOL DERIVATIVE; PROTEASOME INHIBITOR; PROTEIN; PROTEIN P53; QUERCETIN; RESVERATROL; SERINE; SIRTINOL; SIRTUIN 1; SRT 1720; TRANSCRIPTION FACTOR FKHRL1; TRANSCRIPTION FACTOR RELA; UNCLASSIFIED DRUG; UNINDEXED DRUG; WERNER SYNDROME PROTEIN; WNT PROTEIN;

EID: 84860880317     PISSN: 00917435     EISSN: 10960260     Source Type: Journal    
DOI: 10.1016/j.ypmed.2011.11.014     Document Type: Review
Times cited : (97)

References (152)
  • 1
    • 44649120132 scopus 로고    scopus 로고
    • Chemokine signaling via the CXCR2 receptor reinforces senescence
    • Acosta J.C., O'Loghlen A., Banito A., et al. Chemokine signaling via the CXCR2 receptor reinforces senescence. Cell 2008, 133:1006-1018.
    • (2008) Cell , vol.133 , pp. 1006-1018
    • Acosta, J.C.1    O'Loghlen, A.2    Banito, A.3
  • 2
    • 77957341040 scopus 로고    scopus 로고
    • Reactive oxygen species and age-related genes p66shc, Sirtuin, FOX03 and Klotho in senescence
    • Afanas'ev I. Reactive oxygen species and age-related genes p66shc, Sirtuin, FOX03 and Klotho in senescence. Oxid. Med. Cell. Longev. 2010, 3:77-85.
    • (2010) Oxid. Med. Cell. Longev. , vol.3 , pp. 77-85
    • Afanas'ev, I.1
  • 3
    • 34249669270 scopus 로고    scopus 로고
    • Sirt1 regulates aging and resistance to oxidative stress in the heart
    • Alcendor R.R., Gao S., Zhai P., et al. Sirt1 regulates aging and resistance to oxidative stress in the heart. Circ. Res. 2007, 100:1512-1521.
    • (2007) Circ. Res. , vol.100 , pp. 1512-1521
    • Alcendor, R.R.1    Gao, S.2    Zhai, P.3
  • 4
    • 73149091434 scopus 로고    scopus 로고
    • Senescence hypothesis for the pathogenetic mechanism of chronic obstructive pulmonary disease
    • Aoshiba K., Nagai A. Senescence hypothesis for the pathogenetic mechanism of chronic obstructive pulmonary disease. Proc. Am. Thorac. Soc. 2009, 6:596-601.
    • (2009) Proc. Am. Thorac. Soc. , vol.6 , pp. 596-601
    • Aoshiba, K.1    Nagai, A.2
  • 5
    • 77249158771 scopus 로고    scopus 로고
    • SIRT1 regulates oxidant- and cigarette smoke-induced eNOS acetylation in endothelial cells: role of resveratrol
    • Arunachalam G., Yao H., Sundar I.K., Caito S., Rahman I. SIRT1 regulates oxidant- and cigarette smoke-induced eNOS acetylation in endothelial cells: role of resveratrol. Biochem. Biophys. Res. Commun. 2010, 393:66-72.
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 66-72
    • Arunachalam, G.1    Yao, H.2    Sundar, I.K.3    Caito, S.4    Rahman, I.5
  • 6
    • 0036829085 scopus 로고    scopus 로고
    • Down-regulation of p300/CBP histone acetyltransferase activates a senescence checkpoint in human melanocytes
    • Bandyopadhyay D., Okan N.A., Bales E., Nascimento L., Cole P.A., Medrano E.E. Down-regulation of p300/CBP histone acetyltransferase activates a senescence checkpoint in human melanocytes. Cancer Res. 2002, 62:6231-6239.
    • (2002) Cancer Res. , vol.62 , pp. 6231-6239
    • Bandyopadhyay, D.1    Okan, N.A.2    Bales, E.3    Nascimento, L.4    Cole, P.A.5    Medrano, E.E.6
  • 7
    • 70350524083 scopus 로고    scopus 로고
    • Resveratrol is not a direct activator of SIRT1 enzyme activity
    • Beher D., Wu J., Cumine S., et al. Resveratrol is not a direct activator of SIRT1 enzyme activity. Chem. Biol. Drug Des. 2009, 74:619-624.
    • (2009) Chem. Biol. Drug Des. , vol.74 , pp. 619-624
    • Beher, D.1    Wu, J.2    Cumine, S.3
  • 8
    • 1642515805 scopus 로고    scopus 로고
    • Involvement of Rel/nuclear factor-kappaB transcription factors in keratinocyte senescence
    • Bernard D., Gosselin K., Monte D., et al. Involvement of Rel/nuclear factor-kappaB transcription factors in keratinocyte senescence. Cancer Res. 2004, 64:472-481.
    • (2004) Cancer Res. , vol.64 , pp. 472-481
    • Bernard, D.1    Gosselin, K.2    Monte, D.3
  • 9
    • 77955501977 scopus 로고    scopus 로고
    • Maternal smoking promotes chronic obstructive lung disease in the offspring as adults
    • Beyer D., Mitfessel H., Gillissen A. Maternal smoking promotes chronic obstructive lung disease in the offspring as adults. Eur. J. Med. Res. 2009, 14(Suppl. 4):27-31.
    • (2009) Eur. J. Med. Res. , vol.14 , Issue.SUPPL. 4 , pp. 27-31
    • Beyer, D.1    Mitfessel, H.2    Gillissen, A.3
  • 10
    • 78649649752 scopus 로고    scopus 로고
    • Genetic downregulation of AMPK-alpha isoforms uncovers the mechanism by which metformin decreases FA uptake and oxidation in skeletal muscle cells
    • Bogachus L.D., Turcotte L.P. Genetic downregulation of AMPK-alpha isoforms uncovers the mechanism by which metformin decreases FA uptake and oxidation in skeletal muscle cells. Am. J. Physiol. Cell Physiol. 2010, 299:C1549-C1561.
    • (2010) Am. J. Physiol. Cell Physiol. , vol.299
    • Bogachus, L.D.1    Turcotte, L.P.2
  • 11
    • 36248975293 scopus 로고    scopus 로고
    • SIRT1 transgenic mice show phenotypes resembling calorie restriction
    • Bordone L., Cohen D., Robinson A., et al. SIRT1 transgenic mice show phenotypes resembling calorie restriction. Aging Cell 2007, 6:759-767.
    • (2007) Aging Cell , vol.6 , pp. 759-767
    • Bordone, L.1    Cohen, D.2    Robinson, A.3
  • 12
    • 23244461708 scopus 로고    scopus 로고
    • Oncogene-induced senescence as an initial barrier in lymphoma development
    • Braig M., Lee S., Loddenkemper C., et al. Oncogene-induced senescence as an initial barrier in lymphoma development. Nature 2005, 436:660-665.
    • (2005) Nature , vol.436 , pp. 660-665
    • Braig, M.1    Lee, S.2    Loddenkemper, C.3
  • 13
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A., Sweeney L.B., Sturgill J.F., et al. Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 2004, 303:2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3
  • 15
    • 77956180402 scopus 로고    scopus 로고
    • SIRT1 is a redox-sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress
    • Caito S., Rajendrasozhan S., Cook S., et al. SIRT1 is a redox-sensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress. FASEB J. 2010, 24:3145-3159.
    • (2010) FASEB J. , vol.24 , pp. 3145-3159
    • Caito, S.1    Rajendrasozhan, S.2    Cook, S.3
  • 16
    • 67349276169 scopus 로고    scopus 로고
    • AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
    • Canto C., Gerhart-Hines Z., Feige J.N., et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 2009, 458:1056-1060.
    • (2009) Nature , vol.458 , pp. 1056-1060
    • Canto, C.1    Gerhart-Hines, Z.2    Feige, J.N.3
  • 17
    • 0037383155 scopus 로고    scopus 로고
    • Nuclear localisation of p65 in sputum macrophages but not in sputum neutrophils during COPD exacerbations
    • Caramori G., Romagnoli M., Casolari P., et al. Nuclear localisation of p65 in sputum macrophages but not in sputum neutrophils during COPD exacerbations. Thorax 2003, 58:348-351.
    • (2003) Thorax , vol.58 , pp. 348-351
    • Caramori, G.1    Romagnoli, M.2    Casolari, P.3
  • 18
    • 79956366064 scopus 로고    scopus 로고
    • Unbalanced oxidant-induced DNA damage and repair in COPD: a link towards lung cancer
    • Caramori G., Adcock I.M., Casolari P., et al. Unbalanced oxidant-induced DNA damage and repair in COPD: a link towards lung cancer. Thorax 2011, 66:521-527.
    • (2011) Thorax , vol.66 , pp. 521-527
    • Caramori, G.1    Adcock, I.M.2    Casolari, P.3
  • 20
    • 78650413625 scopus 로고    scopus 로고
    • Evaluation of the protective effects of quercetin, rutin, naringenin, resveratrol and trolox against idarubicin-induced DNA damage
    • Celik H., Arinc E. Evaluation of the protective effects of quercetin, rutin, naringenin, resveratrol and trolox against idarubicin-induced DNA damage. J. Pharm. Pharm. Sci. 2010, 13:231-241.
    • (2010) J. Pharm. Pharm. Sci. , vol.13 , pp. 231-241
    • Celik, H.1    Arinc, E.2
  • 21
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • Chen L.F., Mu Y., Greene W.C. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J. 2002, 21:6539-6548.
    • (2002) EMBO J. , vol.21 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 22
    • 9744227998 scopus 로고    scopus 로고
    • N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1)
    • Chen X., Chi Y., Bloecher A., Aebersold R., Clurman B.E., Roberts J.M. N-acetylation and ubiquitin-independent proteasomal degradation of p21(Cip1). Mol. Cell 2004, 16:839-847.
    • (2004) Mol. Cell , vol.16 , pp. 839-847
    • Chen, X.1    Chi, Y.2    Bloecher, A.3    Aebersold, R.4    Clurman, B.E.5    Roberts, J.M.6
  • 23
    • 58349094740 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate, a histone acetyltransferase inhibitor, inhibits EBV-induced B lymphocyte transformation via suppression of RelA acetylation
    • Choi K.C., Jung M.G., Lee Y.H., et al. Epigallocatechin-3-gallate, a histone acetyltransferase inhibitor, inhibits EBV-induced B lymphocyte transformation via suppression of RelA acetylation. Cancer Res. 2009, 69:583-592.
    • (2009) Cancer Res. , vol.69 , pp. 583-592
    • Choi, K.C.1    Jung, M.G.2    Lee, Y.H.3
  • 25
    • 84891713034 scopus 로고    scopus 로고
    • Senescence-associated secretory phenotypes reveal cell-nonautonomous functions of oncogenic RAS and the p53 tumor suppressor
    • Coppe J.P., Patil C.K., Rodier F., et al. Senescence-associated secretory phenotypes reveal cell-nonautonomous functions of oncogenic RAS and the p53 tumor suppressor. PLoS Biol. 2008, 6:2853-2868.
    • (2008) PLoS Biol. , vol.6 , pp. 2853-2868
    • Coppe, J.P.1    Patil, C.K.2    Rodier, F.3
  • 26
    • 77958488312 scopus 로고    scopus 로고
    • SIRT1 activation by small molecules: kinetic and biophysical evidence for direct interaction of enzyme and activator
    • Dai H., Kustigian L., Carney D., et al. SIRT1 activation by small molecules: kinetic and biophysical evidence for direct interaction of enzyme and activator. J. Biol. Chem. 2010, 285:32695-32703.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32695-32703
    • Dai, H.1    Kustigian, L.2    Carney, D.3
  • 29
    • 23944452543 scopus 로고    scopus 로고
    • Vitamin B3 and sirtuin function
    • Denu J.M. Vitamin B3 and sirtuin function. Trends Biochem. Sci. 2005, 30:479-483.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 479-483
    • Denu, J.M.1
  • 30
    • 18544383099 scopus 로고    scopus 로고
    • Increased expression of nuclear factor-kappaB in bronchial biopsies from smokers and patients with COPD
    • Di Stefano A., Caramori G., Oates T., et al. Increased expression of nuclear factor-kappaB in bronchial biopsies from smokers and patients with COPD. Eur. Respir. J. 2002, 20:556-563.
    • (2002) Eur. Respir. J. , vol.20 , pp. 556-563
    • Di Stefano, A.1    Caramori, G.2    Oates, T.3
  • 31
    • 77953944814 scopus 로고    scopus 로고
    • Chromatin modifications: the driving force of senescence and aging?
    • Dimauro T., David G. Chromatin modifications: the driving force of senescence and aging?. Aging (Albany NY) 2009, 1:182-190.
    • (2009) Aging (Albany NY) , vol.1 , pp. 182-190
    • Dimauro, T.1    David, G.2
  • 32
    • 23944482310 scopus 로고    scopus 로고
    • Dissection of a DNA-damage-induced transcriptional network using a combination of microarrays, RNA interference and computational promoter analysis
    • Elkon R., Rashi-Elkeles S., Lerenthal Y., et al. Dissection of a DNA-damage-induced transcriptional network using a combination of microarrays, RNA interference and computational promoter analysis. Genome Biol. 2005, 6:R43.
    • (2005) Genome Biol. , vol.6
    • Elkon, R.1    Rashi-Elkeles, S.2    Lerenthal, Y.3
  • 33
    • 70349782222 scopus 로고    scopus 로고
    • A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide
    • Feng Y., Wu J., Chen L., et al. A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide. Anal. Biochem. 2009, 395:205-210.
    • (2009) Anal. Biochem. , vol.395 , pp. 205-210
    • Feng, Y.1    Wu, J.2    Chen, L.3
  • 34
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel T., Deng C.X., Mostoslavsky R. Recent progress in the biology and physiology of sirtuins. Nature 2009, 460:587-591.
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 35
    • 29744463503 scopus 로고    scopus 로고
    • Sirtuin 1 (SIRT1) sequence variation is not associated with exceptional human longevity
    • Flachsbart F., Croucher P.J., Nikolaus S., et al. Sirtuin 1 (SIRT1) sequence variation is not associated with exceptional human longevity. Exp. Gerontol. 2006, 41:98-102.
    • (2006) Exp. Gerontol. , vol.41 , pp. 98-102
    • Flachsbart, F.1    Croucher, P.J.2    Nikolaus, S.3
  • 36
    • 0033911488 scopus 로고    scopus 로고
    • Inflamm-aging. An evolutionary perspective on immunosenescence
    • Franceschi C., Bonafe M., Valensin S., et al. Inflamm-aging. An evolutionary perspective on immunosenescence. Ann. NY. Acad. Sci. 2000, 908:244-254.
    • (2000) Ann. NY. Acad. Sci. , vol.908 , pp. 244-254
    • Franceschi, C.1    Bonafe, M.2    Valensin, S.3
  • 37
    • 77952105389 scopus 로고    scopus 로고
    • Inflammatory networks during cellular senescence: causes and consequences
    • Freund A., Orjalo A.V., Desprez P.Y., Campisi J. Inflammatory networks during cellular senescence: causes and consequences. Trends Mol. Med. 2010, 16:238-246.
    • (2010) Trends Mol. Med. , vol.16 , pp. 238-246
    • Freund, A.1    Orjalo, A.V.2    Desprez, P.Y.3    Campisi, J.4
  • 38
    • 43049121395 scopus 로고    scopus 로고
    • Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt
    • Fulco M., Cen Y., Zhao P., et al. Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev. Cell 2008, 14:661-673.
    • (2008) Dev. Cell , vol.14 , pp. 661-673
    • Fulco, M.1    Cen, Y.2    Zhao, P.3
  • 40
    • 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, 376:793-796.
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 793-796
    • Gao, Z.1    Ye, J.2
  • 41
    • 58149341744 scopus 로고    scopus 로고
    • Coevolution of telomerase activity and body mass in mammals: From mice to beavers
    • Gorbunova V., Seluanov A. Coevolution of telomerase activity and body mass in mammals: From mice to beavers. Mech. Ageing Dev. 2009, 130:3-9.
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 3-9
    • Gorbunova, V.1    Seluanov, A.2
  • 42
    • 39149116326 scopus 로고    scopus 로고
    • AsSIRTing the DNA damage response
    • Gorospe M., de Cabo R. AsSIRTing the DNA damage response. Trends Cell Biol. 2008, 18:77-83.
    • (2008) Trends Cell Biol. , vol.18 , pp. 77-83
    • Gorospe, M.1    de Cabo, R.2
  • 43
    • 79955926985 scopus 로고    scopus 로고
    • Acetylation-dependent regulation of endothelial Notch signalling by the SIRT1 deacetylase
    • Guarani V., Deflorian G., Franco C.A., et al. Acetylation-dependent regulation of endothelial Notch signalling by the SIRT1 deacetylase. Nature 2011, 473:234-238.
    • (2011) Nature , vol.473 , pp. 234-238
    • Guarani, V.1    Deflorian, G.2    Franco, C.A.3
  • 44
    • 58149308524 scopus 로고    scopus 로고
    • Altered kinetics of nonhomologous end joining and class switch recombination in ligase IV-deficient B cells
    • Han L., Yu K. Altered kinetics of nonhomologous end joining and class switch recombination in ligase IV-deficient B cells. J. Exp. Med. 2008, 205:2745-2753.
    • (2008) J. Exp. Med. , vol.205 , pp. 2745-2753
    • Han, L.1    Yu, K.2
  • 45
    • 77952714326 scopus 로고    scopus 로고
    • SIRT1 regulates dishevelled proteins and promotes transient and constitutive Wnt signaling
    • Holloway K.R., Calhoun T.N., Saxena M., et al. SIRT1 regulates dishevelled proteins and promotes transient and constitutive Wnt signaling. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:9216-9221.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9216-9221
    • Holloway, K.R.1    Calhoun, T.N.2    Saxena, M.3
  • 46
    • 50649112638 scopus 로고    scopus 로고
    • SIRT1 regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase
    • Hou X., Xu S., Maitland-Toolan K.A., et al. SIRT1 regulates hepatocyte lipid metabolism through activating AMP-activated protein kinase. J. Biol. Chem. 2008, 283:20015-20026.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20015-20026
    • Hou, X.1    Xu, S.2    Maitland-Toolan, K.A.3
  • 47
    • 58249084014 scopus 로고    scopus 로고
    • Telomere shortening in chronic obstructive pulmonary disease
    • Houben J.M., Mercken E.M., Ketelslegers H.B., et al. Telomere shortening in chronic obstructive pulmonary disease. Respir. Med. 2009, 103:230-236.
    • (2009) Respir. Med. , vol.103 , pp. 230-236
    • Houben, J.M.1    Mercken, E.M.2    Ketelslegers, H.B.3
  • 48
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz K.T., Bitterman K.J., Cohen H.Y., et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 2003, 425:191-196.
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3
  • 49
    • 77954623119 scopus 로고    scopus 로고
    • Cigarette smoke-induced autophagy is regulated by SIRT1-PARP-1-dependent mechanism: implication in pathogenesis of COPD
    • Hwang J.W., Chung S., Sundar I.K., et al. Cigarette smoke-induced autophagy is regulated by SIRT1-PARP-1-dependent mechanism: implication in pathogenesis of COPD. Arch. Biochem. Biophys. 2010, 500:203-209.
    • (2010) Arch. Biochem. Biophys. , vol.500 , pp. 203-209
    • Hwang, J.W.1    Chung, S.2    Sundar, I.K.3
  • 50
    • 79960527353 scopus 로고    scopus 로고
    • FoxO3 deficiency leads to increased susceptibility to cigarette smoke-induced inflammation, airspace enlargement, and chronic obstructive pulmonary disease
    • Hwang J., Rajendrasozhan S., Yao H., et al. FoxO3 deficiency leads to increased susceptibility to cigarette smoke-induced inflammation, airspace enlargement, and chronic obstructive pulmonary disease. J. Immunol. 2011, 187:987-998.
    • (2011) J. Immunol. , vol.187 , pp. 987-998
    • Hwang, J.1    Rajendrasozhan, S.2    Yao, H.3
  • 51
    • 58249099942 scopus 로고    scopus 로고
    • COPD as a disease of accelerated lung aging
    • Ito K., Barnes P.J. COPD as a disease of accelerated lung aging. Chest 2009, 135:173-180.
    • (2009) Chest , vol.135 , pp. 173-180
    • Ito, K.1    Barnes, P.J.2
  • 52
    • 21044458874 scopus 로고    scopus 로고
    • Decreased histone deacetylase activity in chronic obstructive pulmonary disease
    • Ito K., Ito M., Elliott W.M., et al. Decreased histone deacetylase activity in chronic obstructive pulmonary disease. N. Engl. J. Med. 2005, 352:1967-1976.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1967-1976
    • Ito, K.1    Ito, M.2    Elliott, W.M.3
  • 53
    • 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
  • 54
    • 58149090925 scopus 로고    scopus 로고
    • SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span
    • Kawahara T.L., Michishita E., Adler A.S., et al. SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell 2009, 136:62-74.
    • (2009) Cell , vol.136 , pp. 62-74
    • Kawahara, T.L.1    Michishita, E.2    Adler, A.S.3
  • 55
    • 77952779760 scopus 로고    scopus 로고
    • Complete lack of vitamin C intake generates pulmonary emphysema in senescence marker protein-30 knockout mice
    • Koike K., Kondo Y., Sekiya M., et al. Complete lack of vitamin C intake generates pulmonary emphysema in senescence marker protein-30 knockout mice. Am. J. Physiol. Lung Cell. Mol. Physiol. 2010, 298:L784-L792.
    • (2010) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.298
    • Koike, K.1    Kondo, Y.2    Sekiya, M.3
  • 56
    • 0037136563 scopus 로고    scopus 로고
    • Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress
    • Kops G.J., Dansen T.B., Polderman P.E., et al. Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress. Nature 2002, 419:316-321.
    • (2002) Nature , vol.419 , pp. 316-321
    • Kops, G.J.1    Dansen, T.B.2    Polderman, P.E.3
  • 57
    • 44649101304 scopus 로고    scopus 로고
    • Oncogene-induced senescence relayed by an interleukin-dependent inflammatory network
    • Kuilman T., Michaloglou C., Vredeveld L.C., et al. Oncogene-induced senescence relayed by an interleukin-dependent inflammatory network. Cell 2008, 133:1019-1031.
    • (2008) Cell , vol.133 , pp. 1019-1031
    • Kuilman, T.1    Michaloglou, C.2    Vredeveld, L.C.3
  • 58
    • 14644409780 scopus 로고    scopus 로고
    • Down-regulation of a forkhead transcription factor, FOXO3a, accelerates cellular senescence in human dermal fibroblasts
    • Kyoung Kim H., Kyoung Kim Y., Song I.H., et al. Down-regulation of a forkhead transcription factor, FOXO3a, accelerates cellular senescence in human dermal fibroblasts. J. Gerontol. A Biol. Sci. Med. Sci. 2005, 60:4-9.
    • (2005) J. Gerontol. A Biol. Sci. Med. Sci. , vol.60 , pp. 4-9
    • Kyoung Kim, H.1    Kyoung Kim, Y.2    Song, I.H.3
  • 59
    • 79953739647 scopus 로고    scopus 로고
    • COPD in never smokers: results from the population-based burden of obstructive lung disease study
    • Lamprecht B., McBurnie M.A., Vollmer W.M., et al. COPD in never smokers: results from the population-based burden of obstructive lung disease study. Chest 2011, 139:752-763.
    • (2011) Chest , vol.139 , pp. 752-763
    • Lamprecht, B.1    McBurnie, M.A.2    Vollmer, W.M.3
  • 60
    • 53249121556 scopus 로고    scopus 로고
    • Sirtuins-novel therapeutic targets to treat age-associated diseases
    • Lavu S., Boss O., Elliott P.J., Lambert P.D. Sirtuins-novel therapeutic targets to treat age-associated diseases. Nat. Rev. Drug Discov. 2008, 7:841-853.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 841-853
    • Lavu, S.1    Boss, O.2    Elliott, P.J.3    Lambert, P.D.4
  • 61
    • 58149498955 scopus 로고    scopus 로고
    • Lung alveolar integrity is compromised by telomere shortening in telomerase-null mice
    • Lee J., Reddy R., Barsky L., et al. Lung alveolar integrity is compromised by telomere shortening in telomerase-null mice. Am. J. Physiol. Lung Cell. Mol. Physiol. 2009, 296:L57-L70.
    • (2009) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.296
    • Lee, J.1    Reddy, R.2    Barsky, L.3
  • 62
    • 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, 283:7590-7598.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7590-7598
    • Li, K.1    Casta, A.2    Wang, R.3
  • 64
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo V.D., Kennedy B.K. Sirtuins in aging and age-related disease. Cell 2006, 126:257-268.
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 66
    • 77949446867 scopus 로고    scopus 로고
    • Elevation of sputum matrix metalloproteinase-9 persists up to 6months after smoking cessation: a research study
    • Louhelainen N., Stark H., Mazur W., Rytila P., Djukanovic R., Kinnula V.L. Elevation of sputum matrix metalloproteinase-9 persists up to 6months after smoking cessation: a research study. BMC Pulm. Med. 2010, 10:13.
    • (2010) BMC Pulm. Med. , vol.10 , pp. 13
    • Louhelainen, N.1    Stark, H.2    Mazur, W.3    Rytila, P.4    Djukanovic, R.5    Kinnula, V.L.6
  • 67
    • 70349129549 scopus 로고    scopus 로고
    • Accelerated lung aging: a novel pathogenic mechanism of chronic obstructive pulmonary disease (COPD)
    • MacNee W. Accelerated lung aging: a novel pathogenic mechanism of chronic obstructive pulmonary disease (COPD). Biochem. Soc. Trans. 2009, 37:819-823.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 819-823
    • MacNee, W.1
  • 68
    • 70349118100 scopus 로고    scopus 로고
    • New paradigms in the pathogenesis of chronic obstructive pulmonary disease I
    • MacNee W., Tuder R.M. New paradigms in the pathogenesis of chronic obstructive pulmonary disease I. Proc. Am. Thorac. Soc. 2009, 6:527-531.
    • (2009) Proc. Am. Thorac. Soc. , vol.6 , pp. 527-531
    • MacNee, W.1    Tuder, R.M.2
  • 69
    • 47149091117 scopus 로고    scopus 로고
    • Sirtuin 1, stem cells, aging, and stem cell aging
    • Mantel C., Broxmeyer H.E. Sirtuin 1, stem cells, aging, and stem cell aging. Curr. Opin. Hematol. 2008, 15:326-331.
    • (2008) Curr. Opin. Hematol. , vol.15 , pp. 326-331
    • Mantel, C.1    Broxmeyer, H.E.2
  • 70
    • 52049098230 scopus 로고    scopus 로고
    • Comparison of nonhomologous end joining and homologous recombination in human cells
    • Mao Z., Bozzella M., Seluanov A., Gorbunova V. Comparison of nonhomologous end joining and homologous recombination in human cells. DNA Repair (Amst) 2008, 7:1765-1771.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1765-1771
    • Mao, Z.1    Bozzella, M.2    Seluanov, A.3    Gorbunova, V.4
  • 71
    • 51849121635 scopus 로고    scopus 로고
    • DNA repair by nonhomologous end joining and homologous recombination during cell cycle in human cells
    • Mao Z., Bozzella M., Seluanov A., Gorbunova V. DNA repair by nonhomologous end joining and homologous recombination during cell cycle in human cells. Cell Cycle 2008, 7:2902-2906.
    • (2008) Cell Cycle , vol.7 , pp. 2902-2906
    • Mao, Z.1    Bozzella, M.2    Seluanov, A.3    Gorbunova, V.4
  • 72
    • 79959363092 scopus 로고    scopus 로고
    • SIRT6 promotes DNA repair under stress by activating PARP1
    • Mao Z., Hine C., Tian X., et al. SIRT6 promotes DNA repair under stress by activating PARP1. Science 2011, 332:1443-1446.
    • (2011) Science , vol.332 , pp. 1443-1446
    • Mao, Z.1    Hine, C.2    Tian, X.3
  • 73
    • 0037207475 scopus 로고    scopus 로고
    • The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis
    • McBurney M.W., Yang X., Jardine K., et al. The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis. Mol. Cell. Biol. 2003, 23:38-54.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 38-54
    • McBurney, M.W.1    Yang, X.2    Jardine, K.3
  • 74
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • Michan S., Sinclair D. Sirtuins in mammals: insights into their biological function. Biochem. J. 2007, 404:1-13.
    • (2007) Biochem. J. , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 75
    • 41349090663 scopus 로고    scopus 로고
    • SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
    • Michishita E., McCord R.A., Berber E., et al. SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature 2008, 452:492-496.
    • (2008) Nature , vol.452 , pp. 492-496
    • Michishita, E.1    McCord, R.A.2    Berber, E.3
  • 76
    • 77956341931 scopus 로고    scopus 로고
    • Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
    • Miller K.M., Tjeertes J.V., Coates J., et al. Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining. Nat. Struct. Mol. Biol. 2010, 17:1144-1151.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1144-1151
    • Miller, K.M.1    Tjeertes, J.V.2    Coates, J.3
  • 77
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne J.C., Lambert P.D., Schenk S., et al. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 2007, 450:712-716.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3
  • 80
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky R., Chua K.F., Lombard D.B., et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 2006, 124:315-329.
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.F.2    Lombard, D.B.3
  • 81
    • 71549166705 scopus 로고    scopus 로고
    • Telomere length and chronic obstructive pulmonary disease: evidence of accelerated aging
    • Mui T.S., Man J.M., McElhaney J.E., et al. Telomere length and chronic obstructive pulmonary disease: evidence of accelerated aging. J. Am. Geriatr. Soc. 2009, 57:2372-2374.
    • (2009) J. Am. Geriatr. Soc. , vol.57 , pp. 2372-2374
    • Mui, T.S.1    Man, J.M.2    McElhaney, J.E.3
  • 82
    • 59249084680 scopus 로고    scopus 로고
    • Expression of the longevity proteins by both red and white wines and their cardioprotective components, resveratrol, tyrosol, and hydroxytyrosol
    • Mukherjee S., Lekli I., Gurusamy N., Bertelli A.A., Das D.K. Expression of the longevity proteins by both red and white wines and their cardioprotective components, resveratrol, tyrosol, and hydroxytyrosol. Free Radic. Biol. Med. 2009, 46:573-578.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 573-578
    • Mukherjee, S.1    Lekli, I.2    Gurusamy, N.3    Bertelli, A.A.4    Das, D.K.5
  • 83
    • 33645781050 scopus 로고    scopus 로고
    • Lung fibroblasts from patients with emphysema show markers of senescence in vitro
    • Muller K.C., Welker L., Paasch K., et al. Lung fibroblasts from patients with emphysema show markers of senescence in vitro. Respir. Res. 2006, 7:32.
    • (2006) Respir. Res. , vol.7 , pp. 32
    • Muller, K.C.1    Welker, L.2    Paasch, K.3
  • 84
    • 79551470041 scopus 로고    scopus 로고
    • Lysine deacetylation in ischaemic preconditioning: the role of SIRT1
    • Nadtochiy S.M., Redman E., Rahman I., Brookes P.S. Lysine deacetylation in ischaemic preconditioning: the role of SIRT1. Cardiovasc. Res. 2011, 89:643-649.
    • (2011) Cardiovasc. Res. , vol.89 , pp. 643-649
    • Nadtochiy, S.M.1    Redman, E.2    Rahman, I.3    Brookes, P.S.4
  • 85
    • 33745150422 scopus 로고    scopus 로고
    • Long term smoking with age builds up excessive oxidative stress in bronchoalveolar lavage fluid
    • Nagai K., Betsuyaku T., Kondo T., Nasuhara Y., Nishimura M. Long term smoking with age builds up excessive oxidative stress in bronchoalveolar lavage fluid. Thorax 2006, 61:496-502.
    • (2006) Thorax , vol.61 , pp. 496-502
    • Nagai, K.1    Betsuyaku, T.2    Kondo, T.3    Nasuhara, Y.4    Nishimura, M.5
  • 86
    • 70349324812 scopus 로고    scopus 로고
    • A protein deacetylase SIRT1 is a negative regulator of metalloproteinase-9
    • Nakamaru Y., Vuppusetty C., Wada H., et al. A protein deacetylase SIRT1 is a negative regulator of metalloproteinase-9. FASEB J. 2009, 23:2810-2819.
    • (2009) FASEB J. , vol.23 , pp. 2810-2819
    • Nakamaru, Y.1    Vuppusetty, C.2    Wada, H.3
  • 87
    • 79956220705 scopus 로고    scopus 로고
    • Choosing the right path: does DNA-PK help make the decision?
    • Neal J.A., Meek K. Choosing the right path: does DNA-PK help make the decision?. Mutat. Res. 2011, 711:73-86.
    • (2011) Mutat. Res. , vol.711 , pp. 73-86
    • Neal, J.A.1    Meek, K.2
  • 89
    • 60749102389 scopus 로고    scopus 로고
    • Cigarette smoke induces cellular senescence via Werner's syndrome protein down-regulation
    • Nyunoya T., Monick M.M., Klingelhutz A.L., et al. Cigarette smoke induces cellular senescence via Werner's syndrome protein down-regulation. Am. J. Respir. Crit. Care Med. 2009, 179:279-287.
    • (2009) Am. J. Respir. Crit. Care Med. , vol.179 , pp. 279-287
    • Nyunoya, T.1    Monick, M.M.2    Klingelhutz, A.L.3
  • 91
  • 92
    • 77953355431 scopus 로고    scopus 로고
    • SIRT1/eNOS axis as a potential target against vascular senescence, dysfunction and atherosclerosis
    • Ota H., Eto M., Ogawa S., Iijima K., Akishita M., Ouchi Y. SIRT1/eNOS axis as a potential target against vascular senescence, dysfunction and atherosclerosis. J. Atheroscler. Thromb. 2010, 17:431-435.
    • (2010) J. Atheroscler. Thromb. , vol.17 , pp. 431-435
    • Ota, H.1    Eto, M.2    Ogawa, S.3    Iijima, K.4    Akishita, M.5    Ouchi, Y.6
  • 93
    • 78751506082 scopus 로고    scopus 로고
    • SIRT1 deficiency compromises mouse embryonic stem cell hematopoietic differentiation, and embryonic and adult hematopoiesis in the mouse
    • Ou X., Chae H.D., Wang R.H., et al. SIRT1 deficiency compromises mouse embryonic stem cell hematopoietic differentiation, and embryonic and adult hematopoiesis in the mouse. Blood 2011, 117:440-450.
    • (2011) Blood , vol.117 , pp. 440-450
    • Ou, X.1    Chae, H.D.2    Wang, R.H.3
  • 94
    • 77950246109 scopus 로고    scopus 로고
    • SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
    • Pacholec M., Bleasdale J.E., Chrunyk B., et al. SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. J. Biol. Chem. 2010, 285:8340-8351.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8340-8351
    • Pacholec, M.1    Bleasdale, J.E.2    Chrunyk, B.3
  • 95
    • 78751627156 scopus 로고    scopus 로고
    • Resveratrol inhibits proliferation and promotes apoptosis of neuroblastoma cells: role of sirtuin 1
    • Pizarro J.G., Verdaguer E., Ancrenaz V., et al. Resveratrol inhibits proliferation and promotes apoptosis of neuroblastoma cells: role of sirtuin 1. Neurochem. Res. 2011, 36:187-194.
    • (2011) Neurochem. Res. , vol.36 , pp. 187-194
    • Pizarro, J.G.1    Verdaguer, E.2    Ancrenaz, V.3
  • 96
    • 42649146208 scopus 로고    scopus 로고
    • SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease
    • Rajendrasozhan S., Yang S.R., Kinnula V.L., Rahman I. SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med. 2008, 177:861-870.
    • (2008) Am. J. Respir. Crit. Care Med. , vol.177 , pp. 861-870
    • Rajendrasozhan, S.1    Yang, S.R.2    Kinnula, V.L.3    Rahman, I.4
  • 97
    • 68249096784 scopus 로고    scopus 로고
    • Persistent DNA damage signalling triggers senescence-associated inflammatory cytokine secretion
    • Rodier F., Coppe J.P., Patil C.K., et al. Persistent DNA damage signalling triggers senescence-associated inflammatory cytokine secretion. Nat. Cell Biol. 2009, 11:973-979.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 973-979
    • Rodier, F.1    Coppe, J.P.2    Patil, C.K.3
  • 98
    • 69149102202 scopus 로고    scopus 로고
    • Chronic obstructive pulmonary disease in non-smokers
    • Salvi S.S., Barnes P.J. Chronic obstructive pulmonary disease in non-smokers. Lancet 2009, 374:733-743.
    • (2009) Lancet , vol.374 , pp. 733-743
    • Salvi, S.S.1    Barnes, P.J.2
  • 99
    • 0037131426 scopus 로고    scopus 로고
    • Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging
    • Sarg B., Koutzamani E., Helliger W., Rundquist I., Lindner H.H. Postsynthetic trimethylation of histone H4 at lysine 20 in mammalian tissues is associated with aging. J. Biol. Chem. 2002, 277:39195-39201.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39195-39201
    • Sarg, B.1    Koutzamani, E.2    Helliger, W.3    Rundquist, I.4    Lindner, H.H.5
  • 100
    • 33748331132 scopus 로고    scopus 로고
    • Progressive loss of SIRT1 with cell cycle withdrawal
    • Sasaki T., Maier B., Bartke A., Scrable H. Progressive loss of SIRT1 with cell cycle withdrawal. Aging Cell 2006, 5:413-422.
    • (2006) Aging Cell , vol.5 , pp. 413-422
    • Sasaki, T.1    Maier, B.2    Bartke, A.3    Scrable, H.4
  • 101
    • 33748297499 scopus 로고    scopus 로고
    • Senescence marker protein-30 protects mice lungs from oxidative stress, aging, and smoking
    • Sato T., Seyama K., Sato Y., et al. Senescence marker protein-30 protects mice lungs from oxidative stress, aging, and smoking. Am. J. Respir. Crit. Care Med. 2006, 174:530-537.
    • (2006) Am. J. Respir. Crit. Care Med. , vol.174 , pp. 530-537
    • Sato, T.1    Seyama, K.2    Sato, Y.3
  • 102
    • 78650843340 scopus 로고    scopus 로고
    • MiRNAs regulate SIRT1 expression during mouse embryonic stem cell differentiation and in adult mouse tissues
    • Saunders L.R., Sharma A.D., Tawney J., et al. miRNAs regulate SIRT1 expression during mouse embryonic stem cell differentiation and in adult mouse tissues. Aging (Albany NY) 2010, 2:415-431.
    • (2010) Aging (Albany NY) , vol.2 , pp. 415-431
    • Saunders, L.R.1    Sharma, A.D.2    Tawney, J.3
  • 103
    • 65249172518 scopus 로고    scopus 로고
    • Shortened telomeres in circulating leukocytes of patients with chronic obstructive pulmonary disease
    • Savale L., Chaouat A., Bastuji-Garin S., et al. Shortened telomeres in circulating leukocytes of patients with chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med. 2009, 179:566-571.
    • (2009) Am. J. Respir. Crit. Care Med. , vol.179 , pp. 566-571
    • Savale, L.1    Chaouat, A.2    Bastuji-Garin, S.3
  • 104
    • 0034126440 scopus 로고    scopus 로고
    • Smoking and chronic obstructive pulmonary disease
    • viii
    • Sethi J.M., Rochester C.L. Smoking and chronic obstructive pulmonary disease. Clin. Chest Med. 2000, 21:67-86. viii.
    • (2000) Clin. Chest Med. , vol.21 , pp. 67-86
    • Sethi, J.M.1    Rochester, C.L.2
  • 105
    • 78650636700 scopus 로고    scopus 로고
    • Antidiabetic activity of resveratrol, a known SIRT1 activator in a genetic model for type-2 diabetes
    • Sharma S., Misra C.S., Arumugam S., et al. Antidiabetic activity of resveratrol, a known SIRT1 activator in a genetic model for type-2 diabetes. Phytother. Res. 2011, 25:67-73.
    • (2011) Phytother. Res. , vol.25 , pp. 67-73
    • Sharma, S.1    Misra, C.S.2    Arumugam, S.3
  • 106
    • 80051995791 scopus 로고    scopus 로고
    • Cellular senescence increases expression of bacterial ligands in the lungs and is positively correlated with increased susceptibility to pneumococcal pneumonia
    • Shivshankar P., Boyd A.R., Le Saux C.J., Yeh I.T., Orihuela C.J. Cellular senescence increases expression of bacterial ligands in the lungs and is positively correlated with increased susceptibility to pneumococcal pneumonia. Aging Cell 2011, 10:798-806.
    • (2011) Aging Cell , vol.10 , pp. 798-806
    • Shivshankar, P.1    Boyd, A.R.2    Le Saux, C.J.3    Yeh, I.T.4    Orihuela, C.J.5
  • 107
    • 63549094179 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 replicate signaling pathways triggered by calorie restriction in vivo
    • Smith J.J., Kenney R.D., Gagne D.J., et al. Small molecule activators of SIRT1 replicate signaling pathways triggered by calorie restriction in vivo. BMC Syst. Biol. 2009, 3:31.
    • (2009) BMC Syst. Biol. , vol.3 , pp. 31
    • Smith, J.J.1    Kenney, R.D.2    Gagne, D.J.3
  • 108
    • 0141814999 scopus 로고    scopus 로고
    • Oxidative stress induces nuclear loss of DNA repair proteins Ku70 and Ku80 and apoptosis in pancreatic acinar AR42J cells
    • Song J.Y., Lim J.W., Kim H., Morio T., Kim K.H. Oxidative stress induces nuclear loss of DNA repair proteins Ku70 and Ku80 and apoptosis in pancreatic acinar AR42J cells. J. Biol. Chem. 2003, 278:36676-36687.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36676-36687
    • Song, J.Y.1    Lim, J.W.2    Kim, H.3    Morio, T.4    Kim, K.H.5
  • 110
    • 57849131142 scopus 로고    scopus 로고
    • Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells
    • Suchankova G., Nelson L.E., Gerhart-Hines Z., et al. Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells. Biochem. Biophys. Res. Commun. 2009, 378:836-841.
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 836-841
    • Suchankova, G.1    Nelson, L.E.2    Gerhart-Hines, Z.3
  • 111
    • 0034093125 scopus 로고    scopus 로고
    • Disruption of the klotho gene causes pulmonary emphysema in mice. Defect in maintenance of pulmonary integrity during postnatal life
    • Suga T., Kurabayashi M., Sando Y., et al. Disruption of the klotho gene causes pulmonary emphysema in mice. Defect in maintenance of pulmonary integrity during postnatal life. Am. J. Respir. Cell Mol. Biol. 2000, 22:26-33.
    • (2000) Am. J. Respir. Cell Mol. Biol. , vol.22 , pp. 26-33
    • Suga, T.1    Kurabayashi, M.2    Sando, Y.3
  • 112
    • 79958820786 scopus 로고    scopus 로고
    • Lung cancer and its association with chronic obstructive pulmonary disease: update on nexus of epigenetics
    • Sundar I.K., Mullapudi N., Yao H., Spivack S.D., Rahman I. Lung cancer and its association with chronic obstructive pulmonary disease: update on nexus of epigenetics. Curr. Opin. Pulm. Med. 2011, 17:279-285.
    • (2011) Curr. Opin. Pulm. Med. , vol.17 , pp. 279-285
    • Sundar, I.K.1    Mullapudi, N.2    Yao, H.3    Spivack, S.D.4    Rahman, I.5
  • 113
    • 79951805107 scopus 로고    scopus 로고
    • Short-term adenosine monophosphate-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside treatment increases the sirtuin 1 protein expression in skeletal muscle
    • Suwa M., Nakano H., Radak Z., Kumagai S. Short-term adenosine monophosphate-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside treatment increases the sirtuin 1 protein expression in skeletal muscle. Metabolism 2011, 60:394-403.
    • (2011) Metabolism , vol.60 , pp. 394-403
    • Suwa, M.1    Nakano, H.2    Radak, Z.3    Kumagai, S.4
  • 114
    • 79955594658 scopus 로고    scopus 로고
    • Novel role of AMP-activated protein kinase signaling in cigarette smoke induction of IL-8 in human lung epithelial cells and lung inflammation in mice
    • Tang G.J., Wang H.Y., Wang J.Y., et al. Novel role of AMP-activated protein kinase signaling in cigarette smoke induction of IL-8 in human lung epithelial cells and lung inflammation in mice. Free Radic. Biol. Med. 2011, 50:1492-1502.
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 1492-1502
    • Tang, G.J.1    Wang, H.Y.2    Wang, J.Y.3
  • 115
    • 77950901103 scopus 로고    scopus 로고
    • Induction of manganese superoxide dismutase by nuclear translocation and activation of SIRT1 promotes cell survival in chronic heart failure
    • Tanno M., Kuno A., Yano T., et al. Induction of manganese superoxide dismutase by nuclear translocation and activation of SIRT1 promotes cell survival in chronic heart failure. J. Biol. Chem. 2010, 285:8375-8382.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8375-8382
    • Tanno, M.1    Kuno, A.2    Yano, T.3
  • 116
    • 9744272376 scopus 로고    scopus 로고
    • Cigarette smoke induces senescence in alveolar epithelial cells
    • Tsuji T., Aoshiba K., Nagai A. Cigarette smoke induces senescence in alveolar epithelial cells. Am. J. Respir. Cell Mol. Biol. 2004, 31:643-649.
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.31 , pp. 643-649
    • Tsuji, T.1    Aoshiba, K.2    Nagai, A.3
  • 117
    • 33749841717 scopus 로고    scopus 로고
    • Alveolar cell senescence in patients with pulmonary emphysema
    • Tsuji T., Aoshiba K., Nagai A. Alveolar cell senescence in patients with pulmonary emphysema. Am. J. Respir. Crit. Care Med. 2006, 174:886-893.
    • (2006) Am. J. Respir. Crit. Care Med. , vol.174 , pp. 886-893
    • Tsuji, T.1    Aoshiba, K.2    Nagai, A.3
  • 118
    • 77953812712 scopus 로고    scopus 로고
    • Alveolar cell senescence exacerbates pulmonary inflammation in patients with chronic obstructive pulmonary disease
    • Tsuji T., Aoshiba K., Nagai A. Alveolar cell senescence exacerbates pulmonary inflammation in patients with chronic obstructive pulmonary disease. Respiration 2010, 80:59-70.
    • (2010) Respiration , vol.80 , pp. 59-70
    • Tsuji, T.1    Aoshiba, K.2    Nagai, A.3
  • 119
    • 45849131959 scopus 로고    scopus 로고
    • Cigarette smoke triggers code red: p21CIP1/WAF1/SDI1 switches on danger responses in the lung
    • Tuder R.M., Yun J.H., Graham B.B. Cigarette smoke triggers code red: p21CIP1/WAF1/SDI1 switches on danger responses in the lung. Am. J. Respir. Cell Mol. Biol. 2008, 39:1-6.
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.39 , pp. 1-6
    • Tuder, R.M.1    Yun, J.H.2    Graham, B.B.3
  • 120
    • 80051694933 scopus 로고    scopus 로고
    • Resveratrol selectively induces DNA damage, independent of Smad4 expression, in its efficacy against human head and neck squamous cell carcinoma
    • Tyagi A., Gu M., Takahata T., et al. Resveratrol selectively induces DNA damage, independent of Smad4 expression, in its efficacy against human head and neck squamous cell carcinoma. Clin. Cancer Res. 2011, 17:5402-5411.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 5402-5411
    • Tyagi, A.1    Gu, M.2    Takahata, T.3
  • 122
    • 77950348878 scopus 로고    scopus 로고
    • AMP-activated protein kinase-deficient mice are resistant to the metabolic effects of resveratrol
    • Um J.H., Park S.J., Kang H., et al. AMP-activated protein kinase-deficient mice are resistant to the metabolic effects of resveratrol. Diabetes 2010, 59:554-563.
    • (2010) Diabetes , vol.59 , pp. 554-563
    • Um, J.H.1    Park, S.J.2    Kang, H.3
  • 123
    • 70350464512 scopus 로고    scopus 로고
    • Resveratrol attenuates mitochondrial oxidative stress in coronary arterial endothelial cells
    • Ungvari Z.I., Labinskyy N., Mukhopadhyay P., et al. Resveratrol attenuates mitochondrial oxidative stress in coronary arterial endothelial cells. Am. J. Physiol. Heart Circ. Physiol. 2009, 297:H1876-H1881.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Ungvari, Z.I.1    Labinskyy, N.2    Mukhopadhyay, P.3
  • 124
    • 37349090772 scopus 로고    scopus 로고
    • Expression and localization of Werner syndrome protein is modulated by SIRT1 and PML
    • Vaitiekunaite R., Butkiewicz D., Krzesniak M., et al. Expression and localization of Werner syndrome protein is modulated by SIRT1 and PML. Mech. Ageing Dev. 2007, 128:650-661.
    • (2007) Mech. Ageing Dev. , vol.128 , pp. 650-661
    • Vaitiekunaite, R.1    Butkiewicz, D.2    Krzesniak, M.3
  • 125
    • 36248954501 scopus 로고    scopus 로고
    • SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation
    • Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L., Reinberg D. SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature 2007, 450:440-444.
    • (2007) Nature , vol.450 , pp. 440-444
    • Vaquero, A.1    Scher, M.2    Erdjument-Bromage, H.3    Tempst, P.4    Serrano, L.5    Reinberg, D.6
  • 126
    • 77956553913 scopus 로고    scopus 로고
    • P300-mediated acetylation of histone H3 lysine 56 functions in DNA damage response in mammals
    • Vempati R.K., Jayani R.S., Notani D., Sengupta A., Galande S., Haldar D. p300-mediated acetylation of histone H3 lysine 56 functions in DNA damage response in mammals. J. Biol. Chem. 2010, 285:28553-28564.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28553-28564
    • Vempati, R.K.1    Jayani, R.S.2    Notani, D.3    Sengupta, A.4    Galande, S.5    Haldar, D.6
  • 127
    • 43449121547 scopus 로고    scopus 로고
    • Senescence, apoptosis or autophagy? When a damaged cell must decide its path-a mini-review
    • Vicencio J.M., Galluzzi L., Tajeddine N., et al. Senescence, apoptosis or autophagy? When a damaged cell must decide its path-a mini-review. Gerontology 2008, 54:92-99.
    • (2008) Gerontology , vol.54 , pp. 92-99
    • Vicencio, J.M.1    Galluzzi, L.2    Tajeddine, N.3
  • 128
    • 70449094653 scopus 로고    scopus 로고
    • RelA/p65 functions to maintain cellular senescence by regulating genomic stability and DNA repair
    • Wang J., Jacob N.K., Ladner K.J., et al. RelA/p65 functions to maintain cellular senescence by regulating genomic stability and DNA repair. EMBO Rep. 2009, 10:1272-1278.
    • (2009) EMBO Rep. , vol.10 , pp. 1272-1278
    • Wang, J.1    Jacob, N.K.2    Ladner, K.J.3
  • 129
    • 79953239122 scopus 로고    scopus 로고
    • SIRT1 and AMPK in regulating mammalian senescence: a critical review and a working model
    • Wang Y., Liang Y., Vanhoutte P.M. SIRT1 and AMPK in regulating mammalian senescence: a critical review and a working model. FEBS Lett. 2011, 585:986-994.
    • (2011) FEBS Lett. , vol.585 , pp. 986-994
    • Wang, Y.1    Liang, Y.2    Vanhoutte, P.M.3
  • 130
    • 52949122885 scopus 로고    scopus 로고
    • FOXO3A genotype is strongly associated with human longevity
    • Willcox B.J., Donlon T.A., He Q., et al. FOXO3A genotype is strongly associated with human longevity. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:13987-13992.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13987-13992
    • Willcox, B.J.1    Donlon, T.A.2    He, Q.3
  • 131
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • Wood J.G., Rogina B., Lavu S., et al. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 2004, 430:686-689.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3
  • 132
    • 33644538632 scopus 로고    scopus 로고
    • Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli
    • Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S. Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli. Science 2006, 311:1141-1146.
    • (2006) Science , vol.311 , pp. 1141-1146
    • Wu, Z.H.1    Shi, Y.2    Tibbetts, R.S.3    Miyamoto, S.4
  • 133
    • 33750445309 scopus 로고    scopus 로고
    • NAD metabolism and sirtuins: metabolic regulation of protein deacetylation in stress and toxicity
    • Yang T., Sauve A.A. NAD metabolism and sirtuins: metabolic regulation of protein deacetylation in stress and toxicity. AAPS J. 2006, 8:E632-E643.
    • (2006) AAPS J. , vol.8
    • Yang, T.1    Sauve, A.A.2
  • 134
    • 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 S.R., 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-L576.
    • (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
  • 135
    • 45249105749 scopus 로고    scopus 로고
    • IKK alpha causes chromatin modification on pro-inflammatory genes by cigarette smoke in mouse lung
    • Yang S.R., Valvo S., Yao H., et al. IKK alpha causes chromatin modification on pro-inflammatory genes by cigarette smoke in mouse lung. Am. J. Respir. Cell Mol. Biol. 2008, 38:689-698.
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.38 , pp. 689-698
    • Yang, S.R.1    Valvo, S.2    Yao, H.3
  • 136
    • 69249229772 scopus 로고    scopus 로고
    • The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability
    • Yang B., Zwaans B.M., Eckersdorff M., Lombard D.B. The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic stability. Cell Cycle 2009, 8:2662-2663.
    • (2009) Cell Cycle , vol.8 , pp. 2662-2663
    • Yang, B.1    Zwaans, B.M.2    Eckersdorff, M.3    Lombard, D.B.4
  • 137
    • 68849111316 scopus 로고    scopus 로고
    • Current concepts on the role of inflammation in COPD and lung cancer
    • Yao H., Rahman I. Current concepts on the role of inflammation in COPD and lung cancer. Curr. Opin. Pharmacol. 2009, 9:375-383.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 375-383
    • Yao, H.1    Rahman, I.2
  • 138
    • 79957900741 scopus 로고    scopus 로고
    • Current concepts on oxidative/carbonyl stress, inflammation and epigenetics in pathogenesis of chronic obstructive pulmonary disease
    • Yao H., Rahman I. Current concepts on oxidative/carbonyl stress, inflammation and epigenetics in pathogenesis of chronic obstructive pulmonary disease. Toxicol. Appl. Pharmacol. 2011, 254:72-85.
    • (2011) Toxicol. Appl. Pharmacol. , vol.254 , pp. 72-85
    • Yao, H.1    Rahman, I.2
  • 139
    • 45849091423 scopus 로고    scopus 로고
    • Disruption of p21 attenuates lung inflammation induced by cigarette smoke, LPS, and fMLP in mice
    • Yao H., Yang S.R., Edirisinghe I., et al. Disruption of p21 attenuates lung inflammation induced by cigarette smoke, LPS, and fMLP in mice. Am. J. Respir. Cell Mol. Biol. 2008, 39:7-18.
    • (2008) Am. J. Respir. Cell Mol. Biol. , vol.39 , pp. 7-18
    • Yao, H.1    Yang, S.R.2    Edirisinghe, I.3
  • 140
    • 77949321456 scopus 로고    scopus 로고
    • Protein kinase C zeta mediates cigarette smoke/aldehyde- and lipopolysaccharide-induced lung inflammation and histone modifications
    • Yao H., Hwang J.W., Moscat J., et al. Protein kinase C zeta mediates cigarette smoke/aldehyde- and lipopolysaccharide-induced lung inflammation and histone modifications. J. Biol. Chem. 2010, 285:5405-5416.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5405-5416
    • Yao, H.1    Hwang, J.W.2    Moscat, J.3
  • 141
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F., Hoberg J.E., Ramsey C.S., et al. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 2004, 23:2369-2380.
    • (2004) EMBO J. , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3
  • 142
    • 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, 6:2869-2871.
    • (2007) Cell Cycle , vol.6 , pp. 2869-2871
    • Yuan, Z.1    Seto, E.2
  • 143
    • 34250897968 scopus 로고    scopus 로고
    • SIRT1 regulates the function of the Nijmegen breakage syndrome protein
    • Yuan Z., Zhang X., Sengupta N., Lane W.S., Seto E. SIRT1 regulates the function of the Nijmegen breakage syndrome protein. Mol. Cell 2007, 27:149-162.
    • (2007) Mol. Cell , vol.27 , pp. 149-162
    • Yuan, Z.1    Zhang, X.2    Sengupta, N.3    Lane, W.S.4    Seto, E.5
  • 144
    • 66749102871 scopus 로고    scopus 로고
    • Histone H3-K56 acetylation is important for genomic stability in mammals
    • Yuan J., Pu M., Zhang Z., Lou Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 2009, 8:1747-1753.
    • (2009) Cell Cycle , vol.8 , pp. 1747-1753
    • Yuan, J.1    Pu, M.2    Zhang, Z.3    Lou, Z.4
  • 145
    • 70149104225 scopus 로고    scopus 로고
    • Resveratrol and quercetin cooperate to induce senescence-like growth arrest in C6 rat glioma cells
    • Zamin L.L., Filippi-Chiela E.C., Dillenburg-Pilla P., Horn F., Salbego C., Lenz G. Resveratrol and quercetin cooperate to induce senescence-like growth arrest in C6 rat glioma cells. Cancer Sci. 2009, 100:1655-1662.
    • (2009) Cancer Sci. , vol.100 , pp. 1655-1662
    • Zamin, L.L.1    Filippi-Chiela, E.C.2    Dillenburg-Pilla, P.3    Horn, F.4    Salbego, C.5    Lenz, G.6
  • 146
    • 77955862787 scopus 로고    scopus 로고
    • Redox regulation of sirtuin-1 by S-glutathiolation
    • Zee R.S., Yoo C.B., Pimentel D.R., et al. Redox regulation of sirtuin-1 by S-glutathiolation. Antioxid. Redox Signal. 2010, 13:1023-1032.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1023-1032
    • Zee, R.S.1    Yoo, C.B.2    Pimentel, D.R.3
  • 147
    • 70349440053 scopus 로고    scopus 로고
    • The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice
    • Zhang J., Lee S.M., Shannon S., et al. The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice. J. Clin. Invest. 2009, 119:3048-3058.
    • (2009) J. Clin. Invest. , vol.119 , pp. 3048-3058
    • Zhang, J.1    Lee, S.M.2    Shannon, S.3
  • 148
    • 77951211562 scopus 로고    scopus 로고
    • SIRT1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophages
    • Zhang R., Chen H.Z., Liu J.J., et al. SIRT1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophages. J. Biol. Chem. 2010, 285:7097-7110.
    • (2010) J. Biol. Chem. , vol.285 , pp. 7097-7110
    • Zhang, R.1    Chen, H.Z.2    Liu, J.J.3
  • 149
    • 78650648938 scopus 로고    scopus 로고
    • Roles of SIRT1 in the acute and restorative phases following induction of inflammation
    • Zhang Z., Lowry S.F., Guarente L., Haimovich B. Roles of SIRT1 in the acute and restorative phases following induction of inflammation. J. Biol. Chem. 2010, 285:41391-41401.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41391-41401
    • Zhang, Z.1    Lowry, S.F.2    Guarente, L.3    Haimovich, B.4
  • 150
    • 52649141738 scopus 로고    scopus 로고
    • Activation of AMPK attenuates neutrophil proinflammatory activity and decreases the severity of acute lung injury
    • Zhao X., Zmijewski J.W., Lorne E., et al. Activation of AMPK attenuates neutrophil proinflammatory activity and decreases the severity of acute lung injury. Am. J. Physiol. Lung Cell. Mol. Physiol. 2008, 295:L497-L504.
    • (2008) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.295
    • Zhao, X.1    Zmijewski, J.W.2    Lorne, E.3
  • 151
    • 79958120387 scopus 로고    scopus 로고
    • Epithelial cell senescence impairs repair process and exacerbates inflammation after airway injury
    • Zhou F., Onizawa S., Nagai A., Aoshiba K. Epithelial cell senescence impairs repair process and exacerbates inflammation after airway injury. Respir. Res. 2011, 12:78.
    • (2011) Respir. Res. , vol.12 , pp. 78
    • Zhou, F.1    Onizawa, S.2    Nagai, A.3    Aoshiba, K.4
  • 152
    • 60449118870 scopus 로고    scopus 로고
    • SIRT1 genetic variation and mortality in type 2 diabetes: interaction with smoking and dietary niacin
    • Zillikens M.C., van Meurs J.B., Sijbrands E.J., et al. SIRT1 genetic variation and mortality in type 2 diabetes: interaction with smoking and dietary niacin. Free Radic. Biol. Med. 2009, 46:836-841.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 836-841
    • Zillikens, M.C.1    van Meurs, J.B.2    Sijbrands, E.J.3


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