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Volumn 67, Issue 1, 2013, Pages 60-67

Negative regulation of inflammation by SIRT1

Author keywords

Acetylation; Histone deacetylase; Inflammation; Post translational modification; Sirtuin 1

Indexed keywords

HISTONE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SIRTUIN 1; TRANSCRIPTION FACTOR AP 1;

EID: 84870942679     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2012.10.010     Document Type: Review
Times cited : (207)

References (107)
  • 1
    • 0032750220 scopus 로고    scopus 로고
    • Diverse and dynamic functions of the sir silencing complex
    • L. Guarente Diverse and dynamic functions of the sir silencing complex Nature Genetics 23 1999 281 285
    • (1999) Nature Genetics , vol.23 , pp. 281-285
    • Guarente, L.1
  • 2
    • 0035861202 scopus 로고    scopus 로고
    • The molecular biology of the sir proteins
    • S.M. Gasser, and M.M. Cockell The molecular biology of the sir proteins Gene 279 2001 1 16
    • (2001) Gene , vol.279 , pp. 1-16
    • Gasser, S.M.1    Cockell, M.M.2
  • 3
  • 10
    • 77953480631 scopus 로고    scopus 로고
    • Biochemical effects of sirt1 activators
    • J.A. Baur Biochemical effects of sirt1 activators Biochimica et Biophysica Acta 1804 2010 1626 1634
    • (2010) Biochimica et Biophysica Acta , vol.1804 , pp. 1626-1634
    • Baur, J.A.1
  • 11
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • S. Michan, and D. Sinclair Sirtuins in mammals: insights into their biological function Biochemical Journal 404 2007 1 13
    • (2007) Biochemical Journal , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 14
    • 34547101692 scopus 로고    scopus 로고
    • The expression of sirt1 in nonalcoholic fatty liver disease induced by high-fat diet in rats
    • X.Q. Deng, L.L. Chen, and N.X. Li The expression of sirt1 in nonalcoholic fatty liver disease induced by high-fat diet in rats Liver International 27 2007 708 715
    • (2007) Liver International , vol.27 , pp. 708-715
    • Deng, X.Q.1    Chen, L.L.2    Li, N.X.3
  • 15
    • 22744444561 scopus 로고    scopus 로고
    • Calorie restriction and sir2 genes-towards a mechanism
    • L. Guarente Calorie restriction and sir2 genes-towards a mechanism Mechanisms of Ageing and Development 126 2005 923 928
    • (2005) Mechanisms of Ageing and Development , vol.126 , pp. 923-928
    • Guarente, L.1
  • 18
    • 77953290752 scopus 로고    scopus 로고
    • Sirt1-dependent regulation of chromatin and transcription: Linking NAD(+) metabolism and signaling to the control of cellular functions
    • T. Zhang, and W.L. Kraus Sirt1-dependent regulation of chromatin and transcription: linking NAD(+) metabolism and signaling to the control of cellular functions Biochimica et Biophysica Acta 1804 2010 1666 1675
    • (2010) Biochimica et Biophysica Acta , vol.1804 , pp. 1666-1675
    • Zhang, T.1    Kraus, W.L.2
  • 21
    • 0141557899 scopus 로고    scopus 로고
    • Role of lipopolysaccharide (lps) in asthma and other pulmonary conditions
    • O. Michel Role of lipopolysaccharide (lps) in asthma and other pulmonary conditions Journal of Endotoxin Research 9 2003 293 300
    • (2003) Journal of Endotoxin Research , vol.9 , pp. 293-300
    • Michel, O.1
  • 23
    • 33746294223 scopus 로고    scopus 로고
    • The global burden of asthma
    • S.S. Braman The global burden of asthma Chest 130 2006 4S 12S
    • (2006) Chest , vol.130
    • Braman, S.S.1
  • 24
    • 34548222188 scopus 로고    scopus 로고
    • Global burden of copd: Risk factors, prevalence, and future trends
    • D.M. Mannino, and A.S. Buist Global burden of copd: risk factors, prevalence, and future trends Lancet 370 2007 765 773
    • (2007) Lancet , vol.370 , pp. 765-773
    • Mannino, D.M.1    Buist, A.S.2
  • 25
    • 84859424158 scopus 로고    scopus 로고
    • Chronic obstructive pulmonary disease
    • M. Decramer, W. Janssens, and M. Miravitlles Chronic obstructive pulmonary disease Lancet 379 2012 1341 1351
    • (2012) Lancet , vol.379 , pp. 1341-1351
    • Decramer, M.1    Janssens, W.2    Miravitlles, M.3
  • 28
    • 84855413331 scopus 로고    scopus 로고
    • Metalloproteases/anti-metalloproteases imbalance in chronic obstructive pulmonary disease: Genetic factors and treatment implications
    • E. Mocchegiani, R. Giacconi, and L. Costarelli Metalloproteases/anti- metalloproteases imbalance in chronic obstructive pulmonary disease: genetic factors and treatment implications Current Opinion in Pulmonary Medicine 17 Suppl. 1 2011 S11 S19
    • (2011) Current Opinion in Pulmonary Medicine , vol.17 , Issue.SUPPL. 1
    • Mocchegiani, E.1    Giacconi, R.2    Costarelli, L.3
  • 29
  • 32
    • 79955397959 scopus 로고    scopus 로고
    • Sirt1 acts in association with pparalpha to protect the heart from hypertrophy, metabolic dysregulation, and inflammation
    • A. Planavila, R. Iglesias, M. Giralt, and F. Villarroya Sirt1 acts in association with pparalpha to protect the heart from hypertrophy, metabolic dysregulation, and inflammation Cardiovascular Research 90 2011 276 284
    • (2011) Cardiovascular Research , vol.90 , pp. 276-284
    • Planavila, A.1    Iglesias, R.2    Giralt, M.3    Villarroya, F.4
  • 35
    • 33749627330 scopus 로고    scopus 로고
    • How to modulate inflammatory cytokines in liver diseases
    • H. Tilg, A. Kaser, and A.R. Moschen How to modulate inflammatory cytokines in liver diseases Liver International 26 2006 1029 1039
    • (2006) Liver International , vol.26 , pp. 1029-1039
    • Tilg, H.1    Kaser, A.2    Moschen, A.R.3
  • 36
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of sirt1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • A. Purushotham, T.T. Schug, Q. Xu, S. Surapureddi, X. Guo, and X. Li Hepatocyte-specific deletion of sirt1 alters fatty acid metabolism and results in hepatic steatosis and inflammation Cell Metabolism 9 2009 327 338
    • (2009) Cell Metabolism , vol.9 , pp. 327-338
    • Purushotham, A.1    Schug, T.T.2    Xu, Q.3    Surapureddi, S.4    Guo, X.5    Li, X.6
  • 37
    • 77954515012 scopus 로고    scopus 로고
    • Lack of sirt1 (mammalian sirtuin 1) activity leads to liver steatosis in the sirt1+/- mice: A role of lipid mobilization and inflammation
    • F. Xu, Z. Gao, J. Zhang, C.A. Rivera, J. Yin, and J. Weng Lack of sirt1 (mammalian sirtuin 1) activity leads to liver steatosis in the sirt1+/- mice: a role of lipid mobilization and inflammation Endocrinology 151 2010 2504 2514
    • (2010) Endocrinology , vol.151 , pp. 2504-2514
    • Xu, F.1    Gao, Z.2    Zhang, J.3    Rivera, C.A.4    Yin, J.5    Weng, J.6
  • 39
    • 28844474597 scopus 로고    scopus 로고
    • Sirt1 protects against microglia-dependent amyloid-beta toxicity through inhibiting nf-kappab signaling
    • J. Chen, Y. Zhou, S. Mueller-Steiner, L.F. Chen, H. Kwon, and S. Yi Sirt1 protects against microglia-dependent amyloid-beta toxicity through inhibiting nf-kappab signaling Journal of Biological Chemistry 280 2005 40364 40374
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.F.4    Kwon, H.5    Yi, S.6
  • 40
    • 54149103338 scopus 로고    scopus 로고
    • Endothelium-specific overexpression of class iii deacetylase sirt1 decreases atherosclerosis in apolipoprotein e-deficient mice
    • Q.-J. Zhang, Z. Wang, H.-Z. Chen, S. Zhou, W. Zheng, and G. Liu Endothelium-specific overexpression of class iii deacetylase sirt1 decreases atherosclerosis in apolipoprotein e-deficient mice Cardiovascular Research 80 2008 191 199
    • (2008) Cardiovascular Research , vol.80 , pp. 191-199
    • Zhang, Q.-J.1    Wang, Z.2    Chen, H.-Z.3    Zhou, S.4    Zheng, W.5    Liu, G.6
  • 41
    • 63249112836 scopus 로고    scopus 로고
    • Overexpression of sirt1 protects pancreatic β-cells against cytokine toxicity by suppressing the nuclear factor-κb signaling pathway
    • J-H. Lee, M-Y. Song, E-K. Song, E-K. Kim, W.S. Moon, and M-K. Han Overexpression of sirt1 protects pancreatic β-cells against cytokine toxicity by suppressing the nuclear factor-κb signaling pathway Diabetes 58 2009 344 351
    • (2009) Diabetes , vol.58 , pp. 344-351
    • Lee, J.-H.1    Song, M.-Y.2    Song, E.-K.3    Kim, E.-K.4    Moon, W.S.5    Han, M.-K.6
  • 42
  • 44
    • 41449083867 scopus 로고    scopus 로고
    • Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice
    • O. Vakhrusheva, C. Smolka, P. Gajawada, S. Kostin, T. Boettger, and T. Kubin Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice Circulation Research 102 2008 703 710
    • (2008) Circulation Research , vol.102 , pp. 703-710
    • Vakhrusheva, O.1    Smolka, C.2    Gajawada, P.3    Kostin, S.4    Boettger, T.5    Kubin, T.6
  • 45
    • 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
    • S.R. Yang, J. Wright, M. Bauter, K. Seweryniak, A. Kode, and I. Rahman 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 American Journal of Physiology-Lung Cellular and Molecular Physiology 292 2007 L567 L576
    • (2007) American Journal of Physiology-Lung Cellular and Molecular Physiology , vol.292
    • Yang, S.R.1    Wright, J.2    Bauter, M.3    Seweryniak, K.4    Kode, A.5    Rahman, I.6
  • 48
    • 84863230325 scopus 로고    scopus 로고
    • Interferon gamma (ifn-gamma) disrupts energy expenditure and metabolic homeostasis by suppressing sirt1 transcription
    • P. Li, Y. Zhao, X. Wu, M. Xia, M. Fang, and Y. Iwasaki Interferon gamma (ifn-gamma) disrupts energy expenditure and metabolic homeostasis by suppressing sirt1 transcription Nucleic Acids Research 40 2012 1609 1620
    • (2012) Nucleic Acids Research , vol.40 , pp. 1609-1620
    • Li, P.1    Zhao, Y.2    Wu, X.3    Xia, M.4    Fang, M.5    Iwasaki, Y.6
  • 50
    • 33748200050 scopus 로고    scopus 로고
    • Interactions between e2f1 and sirt1 regulate apoptotic response to DNA damage
    • C. Wang, L. Chen, X. Hou, Z. Li, N. Kabra, and Y. Ma Interactions between e2f1 and sirt1 regulate apoptotic response to DNA damage Nature Cell Biology 8 2006 1025 1031
    • (2006) Nature Cell Biology , vol.8 , pp. 1025-1031
    • Wang, C.1    Chen, L.2    Hou, X.3    Li, Z.4    Kabra, N.5    Ma, Y.6
  • 51
    • 77954218572 scopus 로고    scopus 로고
    • Involvement of the p65/rela subunit of nf-kappab in tnf-alpha-induced sirt1 expression in vascular smooth muscle cells
    • H.N. Zhang, L. Li, P. Gao, H.Z. Chen, R. Zhang, and Y.S. Wei Involvement of the p65/rela subunit of nf-kappab in tnf-alpha-induced sirt1 expression in vascular smooth muscle cells Biochemical and Biophysical Research Communications 397 2010 569 575
    • (2010) Biochemical and Biophysical Research Communications , vol.397 , pp. 569-575
    • Zhang, H.N.1    Li, L.2    Gao, P.3    Chen, H.Z.4    Zhang, R.5    Wei, Y.S.6
  • 52
    • 79954609893 scopus 로고    scopus 로고
    • Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner
    • R. Chen, E.M. Dioum, R.T. Hogg, R.D. Gerard, and J.A. Garcia Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner Journal of Biological Chemistry 286 2011 13869 13878
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 13869-13878
    • Chen, R.1    Dioum, E.M.2    Hogg, R.T.3    Gerard, R.D.4    Garcia, J.A.5
  • 54
    • 70350436694 scopus 로고    scopus 로고
    • Microrna 132 regulates nutritional stress-induced chemokine production through repression of sirt1
    • J.C. Strum, J.H. Johnson, J. Ward, H. Xie, J. Feild, and A. Hester Microrna 132 regulates nutritional stress-induced chemokine production through repression of sirt1 Molecular Endocrinology 23 2009 1876 1884
    • (2009) Molecular Endocrinology , vol.23 , pp. 1876-1884
    • Strum, J.C.1    Johnson, J.H.2    Ward, J.3    Xie, H.4    Feild, J.5    Hester, A.6
  • 56
    • 65249185780 scopus 로고    scopus 로고
    • Downregulation of mir-199a derepresses hypoxia-inducible factor-1alpha and sirtuin 1 and recapitulates hypoxia preconditioning in cardiac myocytes
    • S. Rane, M. He, D. Sayed, H. Vashistha, A. Malhotra, and J. Sadoshima Downregulation of mir-199a derepresses hypoxia-inducible factor-1alpha and sirtuin 1 and recapitulates hypoxia preconditioning in cardiac myocytes Circulation Research 104 2009 879 886
    • (2009) Circulation Research , vol.104 , pp. 879-886
    • Rane, S.1    He, M.2    Sayed, D.3    Vashistha, H.4    Malhotra, A.5    Sadoshima, J.6
  • 57
    • 78650843340 scopus 로고    scopus 로고
    • Mirnas regulate sirt1 expression during mouse embryonic stem cell differentiation and in adult mouse tissues
    • L.R. Saunders, A.D. Sharma, J. Tawney, M. Nakagawa, K. Okita, and S. Yamanaka Mirnas regulate sirt1 expression during mouse embryonic stem cell differentiation and in adult mouse tissues Aging (Albany NY) 2 2010 415 431
    • (2010) Aging (Albany NY) , vol.2 , pp. 415-431
    • Saunders, L.R.1    Sharma, A.D.2    Tawney, J.3    Nakagawa, M.4    Okita, K.5    Yamanaka, S.6
  • 58
    • 79952742806 scopus 로고    scopus 로고
    • Increased expression of mir-34a and mir-93 in rat liver during aging, and their impact on the expression of mgst1 and sirt1
    • N. Li, S. Muthusamy, R. Liang, H. Sarojini, and E. Wang Increased expression of mir-34a and mir-93 in rat liver during aging, and their impact on the expression of mgst1 and sirt1 Mechanisms of Ageing and Development 132 2011 75 85
    • (2011) Mechanisms of Ageing and Development , vol.132 , pp. 75-85
    • Li, N.1    Muthusamy, S.2    Liang, R.3    Sarojini, H.4    Wang, E.5
  • 59
    • 79960391940 scopus 로고    scopus 로고
    • Mir-200a regulates sirt1 expression and epithelial to mesenchymal transition (emt)-like transformation in mammary epithelial cells
    • G. Eades, Y. Yao, M. Yang, Y. Zhang, S. Chumsri, and Q. Zhou Mir-200a regulates sirt1 expression and epithelial to mesenchymal transition (emt)-like transformation in mammary epithelial cells Journal of Biological Chemistry 286 2011 25992 26002
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 25992-26002
    • Eades, G.1    Yao, Y.2    Yang, M.3    Zhang, Y.4    Chumsri, S.5    Zhou, Q.6
  • 60
    • 80052908737 scopus 로고    scopus 로고
    • Microrna-195 promotes palmitate-induced apoptosis in cardiomyocytes by down-regulating sirt1
    • H. Zhu, Y. Yang, Y. Wang, J. Li, P.W. Schiller, and T. Peng Microrna-195 promotes palmitate-induced apoptosis in cardiomyocytes by down-regulating sirt1 Cardiovascular Research 92 2011 75 84
    • (2011) Cardiovascular Research , vol.92 , pp. 75-84
    • Zhu, H.1    Yang, Y.2    Wang, Y.3    Li, J.4    Schiller, P.W.5    Peng, T.6
  • 61
    • 82155163830 scopus 로고    scopus 로고
    • Mir-520c and mir-373 upregulate mmp9 expression by targeting mtor and sirt1, and activate the ras/raf/mek/erk signaling pathway and nf-kappab factor in human fibrosarcoma cells
    • P. Liu, and M.J. Wilson Mir-520c and mir-373 upregulate mmp9 expression by targeting mtor and sirt1, and activate the ras/raf/mek/erk signaling pathway and nf-kappab factor in human fibrosarcoma cells Journal of Cellular Physiology 227 2012 867 876
    • (2012) Journal of Cellular Physiology , vol.227 , pp. 867-876
    • Liu, P.1    Wilson, M.J.2
  • 63
    • 53649100104 scopus 로고    scopus 로고
    • Jnk2-dependent regulation of sirt1 protein stability
    • J. Ford, S. Ahmed, S. Allison, M. Jiang, and J. Milner Jnk2-dependent regulation of sirt1 protein stability Cell Cycle 7 2008 3091 3097
    • (2008) Cell Cycle , vol.7 , pp. 3091-3097
    • Ford, J.1    Ahmed, S.2    Allison, S.3    Jiang, M.4    Milner, J.5
  • 64
    • 69949138641 scopus 로고    scopus 로고
    • Ck2 is the regulator of sirt1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage
    • H. Kang, J.W. Jung, M.K. Kim, and J.H. Chung Ck2 is the regulator of sirt1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage PLoS One 4 2009 e6611
    • (2009) PLoS One , vol.4 , pp. 6611
    • Kang, H.1    Jung, J.W.2    Kim, M.K.3    Chung, J.H.4
  • 65
    • 77951225449 scopus 로고    scopus 로고
    • Dyrk1a and dyrk3 promote cell survival through phosphorylation and activation of sirt1
    • X. Guo, J.G. Williams, T.T. Schug, and X. Li Dyrk1a and dyrk3 promote cell survival through phosphorylation and activation of sirt1 Journal of Biological Chemistry 285 2010 13223 13232
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 13223-13232
    • Guo, X.1    Williams, J.G.2    Schug, T.T.3    Li, X.4
  • 66
    • 35748962613 scopus 로고    scopus 로고
    • Sirt1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • Y. Yang, W. Fu, J. Chen, N. Olashaw, X. Zhang, and S.V. Nicosia Sirt1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress Nature Cell Biology 9 2007 1253 1262
    • (2007) Nature Cell Biology , vol.9 , pp. 1253-1262
    • Yang, Y.1    Fu, W.2    Chen, J.3    Olashaw, N.4    Zhang, X.5    Nicosia, S.V.6
  • 69
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • K.K. Lee, and J.L. Workman Histone acetyltransferase complexes: one size doesn't fit all Nature Reviews Molecular Cell Biology 8 2007 284 295
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 70
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T. Jenuwein, and C.D. Allis Translating the histone code Science 293 2001 1074 1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 71
    • 64549139803 scopus 로고    scopus 로고
    • Reversible acetylation of chromatin: Implication in regulation of gene expression, disease and therapeutics
    • R.B. Selvi, and T.K. Kundu Reversible acetylation of chromatin: implication in regulation of gene expression, disease and therapeutics Biotechnology Journal 4 2009 375 390
    • (2009) Biotechnology Journal , vol.4 , pp. 375-390
    • Selvi, R.B.1    Kundu, T.K.2
  • 73
    • 4944245398 scopus 로고    scopus 로고
    • Human sirt1 interacts with histone h1 and promotes formation of facultative heterochromatin
    • A. Vaquero, M. Scher, D. Lee, H. Erdjument-Bromage, P. Tempst, and D. Reinberg Human sirt1 interacts with histone h1 and promotes formation of facultative heterochromatin Molecular Cell 16 2004 93 105
    • (2004) Molecular Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 74
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein sir2 is an NAD-dependent histone deacetylase
    • C.M. Imai S-i Armstrong, M. Kaeberlein, and L. Guarente Transcriptional silencing and longevity protein sir2 is an NAD-dependent histone deacetylase Nature 403 2000 795 800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, C.M.1    Armstrong, S.-I.2    Kaeberlein, M.3    Guarente, L.4
  • 75
    • 33847188791 scopus 로고    scopus 로고
    • Nf-kappab inhibitors for the treatment of inflammatory diseases and cancer
    • M.A. Calzado, S. Bacher, and M.L. Schmitz Nf-kappab inhibitors for the treatment of inflammatory diseases and cancer Current Medicinal Chemistry 14 2007 367 376
    • (2007) Current Medicinal Chemistry , vol.14 , pp. 367-376
    • Calzado, M.A.1    Bacher, S.2    Schmitz, M.L.3
  • 76
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the nf-kappab pathway
    • Z.J. Chen Ubiquitin signalling in the nf-kappab pathway Nature Cell Biology 7 2005 758 765
    • (2005) Nature Cell Biology , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 77
    • 0029874138 scopus 로고    scopus 로고
    • The nf-kappa b and i kappa b proteins: New discoveries and insights
    • A.S. Baldwin Jr. The nf-kappa b and i kappa b proteins: new discoveries and insights Annual Review of Immunology 14 1996 649 683
    • (1996) Annual Review of Immunology , vol.14 , pp. 649-683
    • Baldwin, Jr.A.S.1
  • 78
    • 33750448661 scopus 로고    scopus 로고
    • Transcriptional regulation via the nf-kappab signaling module
    • A. Hoffmann, G. Natoli, and G. Ghosh Transcriptional regulation via the nf-kappab signaling module Oncogene 25 2006 6706 6716
    • (2006) Oncogene , vol.25 , pp. 6706-6716
    • Hoffmann, A.1    Natoli, G.2    Ghosh, G.3
  • 79
    • 34548856201 scopus 로고    scopus 로고
    • Impact of protein acetylation in inflammatory lung diseases
    • K. Ito, C.E. Charron, and I.M. Adcock Impact of protein acetylation in inflammatory lung diseases Pharmacology and Therapeutics 116 2007 249 265
    • (2007) Pharmacology and Therapeutics , vol.116 , pp. 249-265
    • Ito, K.1    Charron, C.E.2    Adcock, I.M.3
  • 80
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear nf-kappab action regulated by reversible acetylation
    • L. Chen, W. Fischle, E. Verdin, and W.C. Greene Duration of nuclear nf-kappab action regulated by reversible acetylation Science 293 2001 1653 1657
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 81
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of rela at discrete sites regulates distinct nuclear functions of nf-[kappa]b
    • Y. Chen L-f Mu, and W.C. Greene Acetylation of rela at discrete sites regulates distinct nuclear functions of nf-[kappa]b EMBO Journal 21 2002 6539 6548
    • (2002) EMBO Journal , vol.21 , pp. 6539-6548
    • Chen, Y.1    Mu, L.-F.2    Greene, W.C.3
  • 82
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of nf-kappab-dependent transcription and cell survival by the sirt1 deacetylase
    • F. Yeung, J.E. Hoberg, C.S. Ramsey, M.D. Keller, D.R. Jones, and R.A. Frye Modulation of nf-kappab-dependent transcription and cell survival by the sirt1 deacetylase EMBO Journal 23 2004 2369 2380
    • (2004) EMBO Journal , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6
  • 83
    • 79951881254 scopus 로고    scopus 로고
    • Protective roles of sirt1 in atherosclerosis
    • S. Stein, and C.M. Matter Protective roles of sirt1 in atherosclerosis Cell Cycle 10 2011 640 647
    • (2011) Cell Cycle , vol.10 , pp. 640-647
    • Stein, S.1    Matter, C.M.2
  • 84
    • 0025946885 scopus 로고
    • Tumor necrosis factor-alpha mrna accumulation in human myelomonocytic cell lines. Role of transcriptional regulation by DNA sequence motifs and mrna stabilization
    • S.J. Sung, J.A. Walters, J. Hudson, and J.M. Gimble Tumor necrosis factor-alpha mrna accumulation in human myelomonocytic cell lines. Role of transcriptional regulation by DNA sequence motifs and mrna stabilization Journal of Immunology 147 1991 2047 2054
    • (1991) Journal of Immunology , vol.147 , pp. 2047-2054
    • Sung, S.J.1    Walters, J.A.2    Hudson, J.3    Gimble, J.M.4
  • 85
    • 0025720571 scopus 로고
    • Lipopolysaccharide-mediated transcriptional activation of the human tissue factor gene in thp-1 monocytic cells requires both activator protein 1 and nuclear factor kappa b binding sites
    • N. Mackman, K. Brand, and T.S. Edgington Lipopolysaccharide-mediated transcriptional activation of the human tissue factor gene in thp-1 monocytic cells requires both activator protein 1 and nuclear factor kappa b binding sites The Journal of Experimental Medicine 174 1991 1517 1526
    • (1991) The Journal of Experimental Medicine , vol.174 , pp. 1517-1526
    • MacKman, N.1    Brand, K.2    Edgington, T.S.3
  • 86
    • 0024414281 scopus 로고
    • Interleukin-1 costimulatory activity on the interleukin-2 promoter via ap-1
    • K. Muegge, T.M. Williams, J. Kant, M. Karin, R. Chiu, and A. Schmidt Interleukin-1 costimulatory activity on the interleukin-2 promoter via ap-1 Science 246 1989 249 251
    • (1989) Science , vol.246 , pp. 249-251
    • Muegge, K.1    Williams, T.M.2    Kant, J.3    Karin, M.4    Chiu, R.5    Schmidt, A.6
  • 87
    • 0028978703 scopus 로고
    • H2o2 and tumor necrosis factor-alpha activate intercellular adhesion molecule 1 (icam-1) gene transcription through distinct cis-regulatory elements within the icam-1 promoter
    • K.A. Roebuck, A. Rahman, V. Lakshminarayanan, K. Janakidevi, and A.B. Malik H2o2 and tumor necrosis factor-alpha activate intercellular adhesion molecule 1 (icam-1) gene transcription through distinct cis-regulatory elements within the icam-1 promoter Journal of Biological Chemistry 270 1995 18966 18974
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 18966-18974
    • Roebuck, K.A.1    Rahman, A.2    Lakshminarayanan, V.3    Janakidevi, K.4    Malik, A.B.5
  • 88
    • 0030962525 scopus 로고    scopus 로고
    • Cytokine induction of monocyte chemoattractant protein-1 gene expression in human endothelial cells depends on the cooperative action of nf-kappa b and ap-1
    • T. Martin, P.M. Cardarelli, G.C. Parry, K.A. Felts, and R.R. Cobb Cytokine induction of monocyte chemoattractant protein-1 gene expression in human endothelial cells depends on the cooperative action of nf-kappa b and ap-1 European Journal of Immunology 27 1997 1091 1097
    • (1997) European Journal of Immunology , vol.27 , pp. 1091-1097
    • Martin, T.1    Cardarelli, P.M.2    Parry, G.C.3    Felts, K.A.4    Cobb, R.R.5
  • 89
    • 0242691046 scopus 로고    scopus 로고
    • Ap-1. A double-edged sword in tumorigenesis
    • R. Eferl, and Wagner E.F. Ap-1. A double-edged sword in tumorigenesis Nature Reviews Cancer 3 2003 859 868
    • (2003) Nature Reviews Cancer , vol.3 , pp. 859-868
    • Eferl, R.1    Wagner, E.F.2
  • 90
    • 0035503278 scopus 로고    scopus 로고
    • A specific lysine in c-jun is required for transcriptional repression by e1a and is acetylated by p300
    • R.G.J. Vries, M. Prudenziati, C. Zwartjes, M. Verlaan, E. Kalkhoven, and A. Zantema A specific lysine in c-jun is required for transcriptional repression by e1a and is acetylated by p300 EMBO Journal 20 2001 6095 6103
    • (2001) EMBO Journal , vol.20 , pp. 6095-6103
    • Vries, R.G.J.1    Prudenziati, M.2    Zwartjes, C.3    Verlaan, M.4    Kalkhoven, E.5    Zantema, A.6
  • 92
    • 77951211562 scopus 로고    scopus 로고
    • Sirt1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophages
    • R. Zhang, H.Z. Chen, J.J. Liu, Y.Y. Jia, Z.Q. Zhang, and R.F. Yang Sirt1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophages Journal of Biological Chemistry 285 2010 7097 7110
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 7097-7110
    • Zhang, R.1    Chen, H.Z.2    Liu, J.J.3    Jia, Y.Y.4    Zhang, Z.Q.5    Yang, R.F.6
  • 93
    • 84855453214 scopus 로고    scopus 로고
    • P53-induced adipose tissue inflammation is critically involved in the development of insulin resistance in heart failure
    • I. Shimizu, Y. Yoshida, T. Katsuno, K. Tateno, S. Okada, and J. Moriya P53-induced adipose tissue inflammation is critically involved in the development of insulin resistance in heart failure Cell Metabolism 15 2012 51 64
    • (2012) Cell Metabolism , vol.15 , pp. 51-64
    • Shimizu, I.1    Yoshida, Y.2    Katsuno, T.3    Tateno, K.4    Okada, S.5    Moriya, J.6
  • 94
  • 95
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by sir2alpha promotes cell survival under stress
    • J. Luo, A.Y. Nikolaev, S. Imai, D. Chen, F. Su, and A. Shiloh Negative control of p53 by sir2alpha promotes cell survival under stress Cell 107 2001 137 148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6
  • 98
    • 79957532361 scopus 로고    scopus 로고
    • Resveratrol attenuates doxorubicin-induced cardiomyocyte apoptosis in mice through sirt1-mediated deacetylation of p53
    • C. Zhang, Y. Feng, S. Qu, X. Wei, H. Zhu, and Q. Luo Resveratrol attenuates doxorubicin-induced cardiomyocyte apoptosis in mice through sirt1-mediated deacetylation of p53 Cardiovascular Research 90 2011 538 545
    • (2011) Cardiovascular Research , vol.90 , pp. 538-545
    • Zhang, C.1    Feng, Y.2    Qu, S.3    Wei, X.4    Zhu, H.5    Luo, Q.6
  • 100
    • 33745166337 scopus 로고    scopus 로고
    • Silent information regulator 2 (sirt1) attenuates oxidative stress-induced mesangial cell apoptosis via p53 deacetylation
    • S. Kume, M. Haneda, K. Kanasaki, T. Sugimoto, S. Araki, and M. Isono Silent information regulator 2 (sirt1) attenuates oxidative stress-induced mesangial cell apoptosis via p53 deacetylation Free Radical Biology and Medicine 40 2006 2175 2182
    • (2006) Free Radical Biology and Medicine , vol.40 , pp. 2175-2182
    • Kume, S.1    Haneda, M.2    Kanasaki, K.3    Sugimoto, T.4    Araki, S.5    Isono, M.6
  • 101
    • 78649852533 scopus 로고    scopus 로고
    • Sirt1 is regulated by a ppar{gamma}-sirt1 negative feedback loop associated with senescence
    • L. Han, R. Zhou, J. Niu, M.A. McNutt, P. Wang, and T. Tong Sirt1 is regulated by a ppar{gamma}-sirt1 negative feedback loop associated with senescence Nucleic Acids Research 38 2010 7458 7471
    • (2010) Nucleic Acids Research , vol.38 , pp. 7458-7471
    • Han, L.1    Zhou, R.2    Niu, J.3    McNutt, M.A.4    Wang, P.5    Tong, T.6
  • 102
    • 80054029513 scopus 로고    scopus 로고
    • Deacetylation of pgc-1alpha by sirt1: Importance for skeletal muscle function and exercise-induced mitochondrial biogenesis
    • B.J. Gurd Deacetylation of pgc-1alpha by sirt1: importance for skeletal muscle function and exercise-induced mitochondrial biogenesis Applied Physiology, Nutrition, and Metabolism 36 2011 589 597
    • (2011) Applied Physiology, Nutrition, and Metabolism , vol.36 , pp. 589-597
    • Gurd, B.J.1
  • 104
    • 85027946003 scopus 로고    scopus 로고
    • Modulations of hmof autoacetylation by sirt1 regulate hmof recruitment and activities on the chromatin
    • L. Lu, L. Li, X. Lv, X.S. Wu, D.P. Liu, and C.C. Liang Modulations of hmof autoacetylation by sirt1 regulate hmof recruitment and activities on the chromatin Cell Research 21 2011 1182 1195
    • (2011) Cell Research , vol.21 , pp. 1182-1195
    • Lu, L.1    Li, L.2    Lv, X.3    Wu, X.S.4    Liu, D.P.5    Liang, C.C.6
  • 105
    • 77951217683 scopus 로고    scopus 로고
    • Sirt1 regulates autoacetylation and histone acetyltransferase activity of tip60
    • J. Wang, and J. Chen Sirt1 regulates autoacetylation and histone acetyltransferase activity of tip60 Journal of Biological Chemistry 285 2010 11458 11464
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 11458-11464
    • Wang, J.1    Chen, J.2
  • 107
    • 45149132474 scopus 로고    scopus 로고
    • Acetylation of mitogen-activated protein kinase phosphatase-1 inhibits toll-like receptor signaling
    • W. Cao, C. Bao, E. Padalko, and C.J. Lowenstein Acetylation of mitogen-activated protein kinase phosphatase-1 inhibits toll-like receptor signaling Journal of Experimental Medicine 205 2008 1491 1503
    • (2008) Journal of Experimental Medicine , vol.205 , pp. 1491-1503
    • Cao, W.1    Bao, C.2    Padalko, E.3    Lowenstein, C.J.4


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