메뉴 건너뛰기




Volumn 1271, Issue 1, 2012, Pages 10-19

Janus-faced role of SIRT1 in tumorigenesis

Author keywords

Cancer; SIRT1; Subcellular localization

Indexed keywords

HYPOXIA INDUCIBLE FACTOR 1ALPHA; LIPOPOLYSACCHARIDE; MULTIDRUG RESISTANCE PROTEIN 1; SIRTUIN 1; STAT3 PROTEIN; TRANSCRIPTION FACTOR AP 1; TUMOR NECROSIS FACTOR ALPHA;

EID: 84867380741     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2012.06762.x     Document Type: Article
Times cited : (127)

References (97)
  • 1
    • 79958206937 scopus 로고    scopus 로고
    • Franklin H. Epstein Lecture: sirtuins, aging, and medicine
    • Guarente, L. 2011. Franklin H. Epstein Lecture: sirtuins, aging, and medicine. N. Engl. J. Med. 364: 2235-2244.
    • (2011) N. Engl. J. Med. , vol.364 , pp. 2235-2244
    • Guarente, L.1
  • 3
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen, H.Y. et al. 2004. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305: 390-392.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1
  • 4
    • 45549098657 scopus 로고    scopus 로고
    • SirT1 regulates energy metabolism and response to caloric restriction in mice
    • Boily, G. et al. 2008. SirT1 regulates energy metabolism and response to caloric restriction in mice. PLoS One 3: e1759.
    • (2008) PLoS One , vol.3
    • Boily, G.1
  • 5
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra, M.T., B.C. Smith & J.M. Denu. 2005. Mechanism of human SIRT1 activation by resveratrol. J. Biol. Chem. 280: 17187-17195.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 6
    • 33751072349 scopus 로고    scopus 로고
    • Resveratrol improves health and survival of mice on a high-calorie diet
    • Baur, J.A. et al. 2006. Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444: 337-342.
    • (2006) Nature , vol.444 , pp. 337-342
    • Baur, J.A.1
  • 7
    • 33846583673 scopus 로고    scopus 로고
    • SIR2: a potential target for calorie restriction mimetics
    • Chen, D. & L. Guarente. 2007. SIR2: a potential target for calorie restriction mimetics. Trends Mol. Med. 13: 64-71.
    • (2007) Trends Mol. Med. , vol.13 , pp. 64-71
    • Chen, D.1    Guarente, L.2
  • 8
    • 84860477354 scopus 로고    scopus 로고
    • SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function
    • Price, N.L. et al. 2012. SIRT1 is required for AMPK activation and the beneficial effects of resveratrol on mitochondrial function. Cell Metab. 15: 675-690.
    • (2012) Cell Metab. , vol.15 , pp. 675-690
    • Price, N.L.1
  • 9
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S. et al. 2000. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1
  • 10
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: biological insights and disease relevance
    • Haigis, M.C. & D.A. Sinclair. 2010. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 5: 253-295.
    • (2010) Annu. Rev. Pathol. , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 11
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri, H. et al. 2001. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107: 149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 12
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: codified crosstalk with other posttranslational modifications
    • Yang, X.J. & E. Seto. 2008. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 31: 449-461.
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 13
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • Kim, E.J. et al. 2007. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol. Cell. 28: 277-290.
    • (2007) Mol. Cell. , vol.28 , pp. 277-290
    • Kim, E.J.1
  • 14
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • Kim, J.E., J. Chen & Z. Lou. 2008. DBC1 is a negative regulator of SIRT1. Nature 451: 583-586.
    • (2008) Nature , vol.451 , pp. 583-586
    • Kim, J.E.1    Chen, J.2    Lou, Z.3
  • 15
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • Yang, Y. et al. 2007. SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat. Cell Biol. 9: 1253-1262.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1253-1262
    • Yang, Y.1
  • 16
    • 58149202185 scopus 로고    scopus 로고
    • Phosphorylation regulates SIRT1 function
    • Sasaki, T. et al. 2008. Phosphorylation regulates SIRT1 function. PLoS One 3: e4020.
    • (2008) PLoS One , vol.3
    • Sasaki, T.1
  • 17
    • 77949539030 scopus 로고    scopus 로고
    • JNK1 phosphorylates SIRT1 and promotes its enzymatic activity
    • Nasrin, N. et al. 2009. JNK1 phosphorylates SIRT1 and promotes its enzymatic activity. PLoS One 4: e8414.
    • (2009) PLoS One , vol.4
    • Nasrin, N.1
  • 18
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo, J. et al. 2001. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107: 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 19
    • 33847647624 scopus 로고    scopus 로고
    • SIRT1 promotes DNA repair activity and deacetylation of Ku70
    • Jeong, J. et al. 2007. SIRT1 promotes DNA repair activity and deacetylation of Ku70. Exp. Mol. Med. 39: 8-13.
    • (2007) Exp. Mol. Med. , vol.39 , pp. 8-13
    • Jeong, J.1
  • 20
    • 34948883324 scopus 로고    scopus 로고
    • SIRT1 deacetylates and positively regulates the nuclear receptor LXR
    • Li, X. et al. 2007. SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol. Cell 28: 91-106.
    • (2007) Mol. Cell , vol.28 , pp. 91-106
    • Li, X.1
  • 21
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers, J.T. et al. 2005. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434: 113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1
  • 22
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}
    • Nemoto, S., M.M. Fergusson & T. Finkel. 2005. SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}. J. Biol. Chem. 280: 16456-16460.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 23
    • 84859635458 scopus 로고    scopus 로고
    • Emerging avenues linking inflammation and cancer
    • Kundu, J.K. & Y.J. Surh. 2012. Emerging avenues linking inflammation and cancer. Free Radic. Biol. Med. 52: 2013-2037.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 2013-2037
    • Kundu, J.K.1    Surh, Y.J.2
  • 24
    • 80055113353 scopus 로고    scopus 로고
    • Activation of Sirt1 by resveratrol inhibits TNF-alpha induced inflammation in fibroblasts
    • Zhu, X. et al. 2011. Activation of Sirt1 by resveratrol inhibits TNF-alpha induced inflammation in fibroblasts. PLoS One 6: e27081.
    • (2011) PLoS One , vol.6
    • Zhu, X.1
  • 25
    • 78650648938 scopus 로고    scopus 로고
    • Roles of SIRT1 in the acute and restorative phases following induction of inflammation
    • Zhang, Z. et al. 2010. Roles of SIRT1 in the acute and restorative phases following induction of inflammation. J. Biol. Chem. 285: 41391-41401.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41391-41401
    • Zhang, Z.1
  • 26
    • 77349087078 scopus 로고    scopus 로고
    • SIRT1 inhibits inflammatory pathways in macrophages and modulates insulin sensitivity
    • Yoshizaki, T. et al. 2010. SIRT1 inhibits inflammatory pathways in macrophages and modulates insulin sensitivity. Am. J. Physiol. Endocrinol. Metab. 298: E419-E428.
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.298
    • Yoshizaki, T.1
  • 27
    • 63449112017 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation
    • Purushotham, A. et al. 2009. Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Cell Metab. 9: 327-338.
    • (2009) Cell Metab. , vol.9 , pp. 327-338
    • Purushotham, A.1
  • 28
    • 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
    • Xu, F. et al. 2010. Lack of SIRT1 (Mammalian Sirtuin 1) activity leads to liver steatosis in the SIRT1+/- mice: a role of lipid mobilization and inflammation. Endocrinology 151: 2504-2514.
    • (2010) Endocrinology , vol.151 , pp. 2504-2514
    • Xu, F.1
  • 29
    • 42649146208 scopus 로고    scopus 로고
    • SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease
    • Rajendrasozhan, S. et al. 2008. SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease. Am. J. Respir Crit. Care Med. 177: 861-870.
    • (2008) Am. J. Respir Crit. Care Med. , vol.177 , pp. 861-870
    • Rajendrasozhan, S.1
  • 30
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung, F. et al. 2004. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J. 23: 2369-2380.
    • (2004) EMBO J. , vol.23 , pp. 2369-2380
    • Yeung, F.1
  • 31
    • 77249089947 scopus 로고    scopus 로고
    • Resveratrol (trans-3,5,4'-trihydroxystilbene) induces silent mating type information regulation-1 and down-regulates nuclear transcription factor-kappaB activation to abrogate dextran sulfate sodium-induced colitis
    • Singh, U.P. et al. 2010. Resveratrol (trans-3, 5, 4'-trihydroxystilbene) induces silent mating type information regulation-1 and down-regulates nuclear transcription factor-kappaB activation to abrogate dextran sulfate sodium-induced colitis. J. Pharmacol. Exp. Ther. 332: 829-839.
    • (2010) J. Pharmacol. Exp. Ther. , vol.332 , pp. 829-839
    • Singh, U.P.1
  • 32
    • 70350500225 scopus 로고    scopus 로고
    • STATs in cancer inflammation and immunity: a leading role for STAT3
    • Yu, H., D. Pardoll & R. Jove. 2009. STATs in cancer inflammation and immunity: a leading role for STAT3. Nat. Rev. Cancer 9: 798-809.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 798-809
    • Yu, H.1    Pardoll, D.2    Jove, R.3
  • 33
    • 64049109876 scopus 로고    scopus 로고
    • STAT3 inhibition of gluconeogenesis is downregulated by SirT1
    • Nie, Y. et al. 2009. STAT3 inhibition of gluconeogenesis is downregulated by SirT1. Nat. Cell Biol. 11: 492-500.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 492-500
    • Nie, Y.1
  • 34
    • 79954569231 scopus 로고    scopus 로고
    • STAT3-dependent effects of IL-22 in human keratinocytes are counterregulated by sirtuin 1 through a direct inhibition of STAT3 acetylation
    • Sestito, R. et al. 2011. STAT3-dependent effects of IL-22 in human keratinocytes are counterregulated by sirtuin 1 through a direct inhibition of STAT3 acetylation. FASEB J. 25: 916-927.
    • (2011) FASEB J. , vol.25 , pp. 916-927
    • Sestito, R.1
  • 35
    • 53449090280 scopus 로고    scopus 로고
    • Inhibition of transcriptional activity of c-JUN by SIRT1
    • Gao, Z. & J. Ye. 2008. Inhibition of transcriptional activity of c-JUN by SIRT1. Biochem. Biophys. Res. Commun. 376: 793-796.
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 793-796
    • Gao, Z.1    Ye, J.2
  • 36
    • 67651210858 scopus 로고    scopus 로고
    • SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1
    • Rajamohan, S.B. et al. 2009. SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol. Cell Biol. 29: 4116-4129.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 4116-4129
    • Rajamohan, S.B.1
  • 37
    • 78651105018 scopus 로고    scopus 로고
    • Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C
    • Ming, M. et al. 2010. Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C. Proc. Natl. Acad. Sci. U. S. A. 107: 22623-22628.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 22623-22628
    • Ming, M.1
  • 38
    • 56749156405 scopus 로고    scopus 로고
    • SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging
    • Oberdoerffer, P. et al. 2008. SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging. Cell 135: 907-918.
    • (2008) Cell , vol.135 , pp. 907-918
    • Oberdoerffer, P.1
  • 39
    • 78650747994 scopus 로고    scopus 로고
    • SIRT1 contributes to telomere maintenance and augments global homologous recombination
    • Palacios, J.A. et al. 2010. SIRT1 contributes to telomere maintenance and augments global homologous recombination. J. Cell Biol. 191: 1299-1313.
    • (2010) J. Cell Biol. , vol.191 , pp. 1299-1313
    • Palacios, J.A.1
  • 40
    • 65349096174 scopus 로고    scopus 로고
    • A c-Myc-SIRT1 feedback loop regulates cell growth and transformation
    • Yuan, J., K. Minter-Dykhouse & Z. Lou. 2009. A c-Myc-SIRT1 feedback loop regulates cell growth and transformation. J. Cell Biol. 185: 203-211.
    • (2009) J. Cell Biol. , vol.185 , pp. 203-211
    • Yuan, J.1    Minter-Dykhouse, K.2    Lou, Z.3
  • 41
    • 67650563916 scopus 로고    scopus 로고
    • SirT1 is an inhibitor of proliferation and tumor formation in colon cancer
    • Kabra, N. et al. 2009. SirT1 is an inhibitor of proliferation and tumor formation in colon cancer. J. Biol. Chem. 284: 18210-18217.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18210-18217
    • Kabra, N.1
  • 42
    • 67650677845 scopus 로고    scopus 로고
    • Resveratrol induces senescence-like growth inhibition of U-2 OS cells associated with the instability of telomeric DNA and upregulation of BRCA1
    • Rusin, M., A. Zajkowicz & D. Butkiewicz. 2009. Resveratrol induces senescence-like growth inhibition of U-2 OS cells associated with the instability of telomeric DNA and upregulation of BRCA1. Mech. Ageing Dev. 130: 528-537.
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 528-537
    • Rusin, M.1    Zajkowicz, A.2    Butkiewicz, D.3
  • 43
    • 53149144656 scopus 로고    scopus 로고
    • Interplay among BRCA1, SIRT1, and Survivin during BRCA1-associated tumorigenesis
    • Wang, R.H. et al. 2008. Interplay among BRCA1, SIRT1, and Survivin during BRCA1-associated tumorigenesis. Mol. Cell 32: 11-20.
    • (2008) Mol. Cell , vol.32 , pp. 11-20
    • Wang, R.H.1
  • 44
    • 79551521179 scopus 로고    scopus 로고
    • Disruption of a Sirt1-dependent autophagy checkpoint in the prostate results in prostatic intraepithelial neoplasia lesion formation
    • Powell, M.J. et al. 2011. Disruption of a Sirt1-dependent autophagy checkpoint in the prostate results in prostatic intraepithelial neoplasia lesion formation. Cancer Res. 71: 964-975.
    • (2011) Cancer Res. , vol.71 , pp. 964-975
    • Powell, M.J.1
  • 45
    • 77955499804 scopus 로고    scopus 로고
    • Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha
    • Lim, J.H. et al. 2010. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Mol. Cell 38: 864-878.
    • (2010) Mol. Cell , vol.38 , pp. 864-878
    • Lim, J.H.1
  • 46
    • 70349324812 scopus 로고    scopus 로고
    • A protein deacetylase SIRT1 is a negative regulator of metalloproteinase-9
    • Nakamaru, Y. et al. 2009. A protein deacetylase SIRT1 is a negative regulator of metalloproteinase-9. FASEB J. 23: 2810-2819.
    • (2009) FASEB J. , vol.23 , pp. 2810-2819
    • Nakamaru, Y.1
  • 47
    • 59149085705 scopus 로고    scopus 로고
    • Hyaluronan-mediated CD44 interaction with p300 and SIRT1 regulates beta-catenin signaling and NFkappaB-specific transcription activity leading to MDR1 and Bcl-xL gene expression and chemoresistance in breast tumor cells
    • Bourguignon, L.Y., W. Xia & G. Wong. 2009. Hyaluronan-mediated CD44 interaction with p300 and SIRT1 regulates beta-catenin signaling and NFkappaB-specific transcription activity leading to MDR1 and Bcl-xL gene expression and chemoresistance in breast tumor cells. J. Biol. Chem. 284: 2657-2671.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2657-2671
    • Bourguignon, L.Y.1    Xia, W.2    Wong, G.3
  • 48
    • 53149137486 scopus 로고    scopus 로고
    • Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice
    • Wang, R.H. et al. 2008. Impaired DNA damage response, genome instability, and tumorigenesis in SIRT1 mutant mice. Cancer Cell. 14: 312-323.
    • (2008) Cancer Cell. , vol.14 , pp. 312-323
    • Wang, R.H.1
  • 49
    • 44849096876 scopus 로고    scopus 로고
    • The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth
    • Firestein, R. et al. 2008. The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS One 3: e2020.
    • (2008) PLoS One , vol.3
    • Firestein, R.1
  • 50
    • 34547100073 scopus 로고    scopus 로고
    • SIRT1 is significantly elevated in mouse and human prostate cancer
    • Huffman, D.M. et al. 2007. SIRT1 is significantly elevated in mouse and human prostate cancer. Cancer Res. 67: 6612-6618.
    • (2007) Cancer Res. , vol.67 , pp. 6612-6618
    • Huffman, D.M.1
  • 51
    • 59649126261 scopus 로고    scopus 로고
    • Deacetylation of cortactin by SIRT1 promotes cell migration
    • Zhang, Y. et al. 2009. Deacetylation of cortactin by SIRT1 promotes cell migration. Oncogene 28: 445-460.
    • (2009) Oncogene , vol.28 , pp. 445-460
    • Zhang, Y.1
  • 52
    • 84865143188 scopus 로고    scopus 로고
    • SIRT1 promotes tumorigenesis and resistance to chemotherapy in hepatocellular carcinoma and its expression predicts poor prognosis
    • Chen, H.C. et al. 2012. SIRT1 promotes tumorigenesis and resistance to chemotherapy in hepatocellular carcinoma and its expression predicts poor prognosis. Ann. Surg. Oncol. 19: 2011-2019.
    • (2012) Ann. Surg. Oncol. 19: 2011-2019.
    • Chen, H.C.1
  • 53
    • 77954647009 scopus 로고    scopus 로고
    • Balance between SIRT1 and DBC1 expression is lost in breast cancer
    • Sung, J.Y. et al. 2010. Balance between SIRT1 and DBC1 expression is lost in breast cancer. Cancer Sci. 101: 1738-1744.
    • (2010) Cancer Sci. , vol.101 , pp. 1738-1744
    • Sung, J.Y.1
  • 54
    • 84860253067 scopus 로고    scopus 로고
    • Expression of SIRT1 in gastric cardiac cancer and its clinicopathologic significance
    • Feng, A.N. et al. 2011. Expression of SIRT1 in gastric cardiac cancer and its clinicopathologic significance. Int. J. Surg. Pathol 19: 743-750.
    • (2011) Int. J. Surg. Pathol , vol.19 , pp. 743-750
    • Feng, A.N.1
  • 55
    • 80052600926 scopus 로고    scopus 로고
    • SIRT1 RNAi knockdown induces apoptosis and senescence, inhibits invasion and enhances chemosensitivity in pancreatic cancer cells
    • Zhao, G. et al. 2011. SIRT1 RNAi knockdown induces apoptosis and senescence, inhibits invasion and enhances chemosensitivity in pancreatic cancer cells. Gene Ther. 18: 920-928.
    • (2011) Gene Ther. , vol.18 , pp. 920-928
    • Zhao, G.1
  • 56
    • 36549044009 scopus 로고    scopus 로고
    • Function of the SIRT1 protein deacetylase in cancer
    • Stunkel, W. et al. 2007. Function of the SIRT1 protein deacetylase in cancer. Biotechnol. J. 2: 1360-1368.
    • (2007) Biotechnol. J. , vol.2 , pp. 1360-1368
    • Stunkel, W.1
  • 57
    • 84864549056 scopus 로고    scopus 로고
    • Loss of SIRT1 histone deacetylase expression associates with tumour progression in colorectal adenocarcinoma
    • Jang, S.H. et al. 2012. Loss of SIRT1 histone deacetylase expression associates with tumour progression in colorectal adenocarcinoma. J. Clin. Pathol. 65: 735-739.
    • (2012) J. Clin. Pathol. , vol.65 , pp. 735-739
    • Jang, S.H.1
  • 58
    • 53449083751 scopus 로고    scopus 로고
    • SIRT1 expression is associated with poor prognosis of diffuse large B-cell lymphoma
    • Jang, K.Y. et al. 2008. SIRT1 expression is associated with poor prognosis of diffuse large B-cell lymphoma. Am. J. Surg. Pathol. 32: 1523-1531.
    • (2008) Am. J. Surg. Pathol. , vol.32 , pp. 1523-1531
    • Jang, K.Y.1
  • 59
    • 68849097673 scopus 로고    scopus 로고
    • Expression and prognostic significance of SIRT1 in ovarian epithelial tumours
    • Jang, K.Y. et al. 2009. Expression and prognostic significance of SIRT1 in ovarian epithelial tumours. Pathology. 41: 366-371.
    • (2009) Pathology. , vol.41 , pp. 366-371
    • Jang, K.Y.1
  • 60
    • 67650348173 scopus 로고    scopus 로고
    • Expression of DBC1 and SIRT1 is associated with poor prognosis of gastric carcinoma
    • Cha, E.J. et al. 2009. Expression of DBC1 and SIRT1 is associated with poor prognosis of gastric carcinoma. Clin. Cancer Res. 15: 4453-4459.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 4453-4459
    • Cha, E.J.1
  • 61
    • 34249817549 scopus 로고    scopus 로고
    • Transactivation of miR-34a by p53 broadly influences gene expression and promotes apoptosis
    • Chang, T.C. et al. 2007. Transactivation of miR-34a by p53 broadly influences gene expression and promotes apoptosis. Mol. Cell 26: 745-752.
    • (2007) Mol. Cell , vol.26 , pp. 745-752
    • Chang, T.C.1
  • 62
    • 77953292238 scopus 로고    scopus 로고
    • SIRT1 and p53, effect on cancer, senescence and beyond
    • Yi, J. & J. Luo. 2010. SIRT1 and p53, effect on cancer, senescence and beyond. Biochim. Biophys. Acta. 1804: 1684-1689.
    • (2010) Biochim. Biophys. Acta. , vol.1804 , pp. 1684-1689
    • Yi, J.1    Luo, J.2
  • 63
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • Chen, W.Y. et al. 2005. Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell 123: 437-448.
    • (2005) Cell , vol.123 , pp. 437-448
    • Chen, W.Y.1
  • 64
    • 35748949600 scopus 로고    scopus 로고
    • Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1
    • Wong, S. & J.D. Weber. 2007. Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1. Biochem J. 407: 451-460.
    • (2007) Biochem J. , vol.407 , pp. 451-460
    • Wong, S.1    Weber, J.D.2
  • 65
    • 52049102233 scopus 로고    scopus 로고
    • PTEN acetylation modulates its interaction with PDZ domain
    • Ikenoue, T. et al. 2008. PTEN acetylation modulates its interaction with PDZ domain. Cancer Res. 68: 6908-6912.
    • (2008) Cancer Res. , vol.68 , pp. 6908-6912
    • Ikenoue, T.1
  • 67
    • 84856384698 scopus 로고    scopus 로고
    • The c-MYC oncoprotein, the NAMPT enzyme, the SIRT1-inhibitor DBC1, and the SIRT1 deacetylase form a positive feedback loop
    • Menssen, A. et al. 2012. The c-MYC oncoprotein, the NAMPT enzyme, the SIRT1-inhibitor DBC1, and the SIRT1 deacetylase form a positive feedback loop. Proc. Natl. Acad. Sci. USA 109: E187-196.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Menssen, A.1
  • 68
    • 80053377582 scopus 로고    scopus 로고
    • Sirt1 deacetylates c-Myc and promotes c-Myc/Max association
    • Mao, B. et al. 2011. Sirt1 deacetylates c-Myc and promotes c-Myc/Max association. Int. J. Biochem. Cell Biol. 43: 1573-1581.
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1573-1581
    • Mao, B.1
  • 69
    • 79959837062 scopus 로고    scopus 로고
    • SIRT1 promotes N-Myc oncogenesis through a positive feedback loop involving the effects of MKP3 and ERK on N-Myc protein stability
    • Marshall, G.M. et al. 2011. SIRT1 promotes N-Myc oncogenesis through a positive feedback loop involving the effects of MKP3 and ERK on N-Myc protein stability. PLoS Genet. 7: e1002135.
    • (2011) PLoS Genet. , vol.7
    • Marshall, G.M.1
  • 70
    • 84863116364 scopus 로고    scopus 로고
    • Activation of stress response gene SIRT1 by BCR-ABL promotes leukemogenesis
    • Yuan, H. et al. 2012. Activation of stress response gene SIRT1 by BCR-ABL promotes leukemogenesis. Blood 119: 1904-1914.
    • (2012) Blood , vol.119 , pp. 1904-1914
    • Yuan, H.1
  • 71
    • 79960620082 scopus 로고    scopus 로고
    • The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy
    • Sundaresan, N.R. et al. 2011. The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy. Sci. Signal. 4: ra46.
    • (2011) Sci. Signal. , vol.4
    • Sundaresan, N.R.1
  • 72
    • 30544445468 scopus 로고    scopus 로고
    • Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells
    • Ota, H. et al. 2006. Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells. Oncogene. 25: 176-185.
    • (2006) Oncogene. , vol.25 , pp. 176-185
    • Ota, H.1
  • 73
    • 84863011183 scopus 로고    scopus 로고
    • Activation of p53 by SIRT1 inhibition enhances elimination of CML leukemia stem cells in combination with imatinib
    • Li, L. et al. 2012. Activation of p53 by SIRT1 inhibition enhances elimination of CML leukemia stem cells in combination with imatinib. Cancer Cell 21: 266-281.
    • (2012) Cancer Cell , vol.21 , pp. 266-281
    • Li, L.1
  • 74
    • 47249154705 scopus 로고    scopus 로고
    • A role for SIRT1 in cell growth and chemoresistance in prostate cancer PC3 and DU145 cells
    • Kojima, K. et al. 2008. A role for SIRT1 in cell growth and chemoresistance in prostate cancer PC3 and DU145 cells. Biochem. Biophys. Res. Commun. 373: 423-428.
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 423-428
    • Kojima, K.1
  • 75
    • 60149091562 scopus 로고    scopus 로고
    • Salermide, a Sirtuin inhibitor with a strong cancer-specific proapoptotic effect
    • Lara, E. et al. 2009. Salermide, a Sirtuin inhibitor with a strong cancer-specific proapoptotic effect. Oncogene. 28: 781-791.
    • (2009) Oncogene. , vol.28 , pp. 781-791
    • Lara, E.1
  • 76
    • 77950835404 scopus 로고    scopus 로고
    • SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2
    • Peck, B. et al. 2010. SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2. Mol. Cancer Ther. 9: 844-855.
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 844-855
    • Peck, B.1
  • 77
    • 79958787784 scopus 로고    scopus 로고
    • Sirtuin 1 is upregulated in a subset of hepatocellular carcinomas where it is essential for telomere maintenance and tumor cell growth
    • Chen, J. et al. 2011. Sirtuin 1 is upregulated in a subset of hepatocellular carcinomas where it is essential for telomere maintenance and tumor cell growth. Cancer Res. 71: 4138-4149.
    • (2011) Cancer Res. , vol.71 , pp. 4138-4149
    • Chen, J.1
  • 78
    • 28544444366 scopus 로고    scopus 로고
    • Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival
    • Ford, J., M. Jiang & J. Milner. 2005. Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival. Cancer Res. 65: 10457-10463.
    • (2005) Cancer Res. , vol.65 , pp. 10457-10463
    • Ford, J.1    Jiang, M.2    Milner, J.3
  • 80
    • 79960391940 scopus 로고    scopus 로고
    • miR-200a regulates SIRT1 expression and epithelial to mesenchymal transition (EMT)-like transformation in mammary epithelial cells
    • Eades, G. et al. 2011. miR-200a regulates SIRT1 expression and epithelial to mesenchymal transition (EMT)-like transformation in mammary epithelial cells. J. Biol. Chem. 286: 25992-26002.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25992-26002
    • Eades, G.1
  • 81
    • 84867901275 scopus 로고    scopus 로고
    • SIRT1 induces EMT by cooperating with EMT transcription factors and enhances prostate cancer cell migration and metastasis
    • Jan 16. doi:10.1038/onc.2011.612. [Epub ahead of print].
    • Byles, V. et al. 2012. SIRT1 induces EMT by cooperating with EMT transcription factors and enhances prostate cancer cell migration and metastasis. Oncogene. Jan 16. doi:10.1038/onc.2011.612. [Epub ahead of print].
    • (2012) Oncogene.
    • Byles, V.1
  • 82
    • 77952714326 scopus 로고    scopus 로고
    • SIRT1 regulates Dishevelled proteins and promotes transient and constitutive Wnt signaling
    • Holloway, K.R. et al. 2010. SIRT1 regulates Dishevelled proteins and promotes transient and constitutive Wnt signaling. Proc. Natl. Acad. Sci. U. S. A. 107: 9216-9221.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9216-9221
    • Holloway, K.R.1
  • 83
    • 28544451205 scopus 로고    scopus 로고
    • Control of multidrug resistance gene mdr1 and cancer resistance to chemotherapy by the longevity gene sirt1
    • Chu, F. et al. 2005. Control of multidrug resistance gene mdr1 and cancer resistance to chemotherapy by the longevity gene sirt1. Cancer Res. 65: 10183-10187.
    • (2005) Cancer Res. , vol.65 , pp. 10183-10187
    • Chu, F.1
  • 84
    • 53349091778 scopus 로고    scopus 로고
    • SIRT1 contributes in part to cisplatin resistance in cancer cells by altering mitochondrial metabolism
    • Liang, X.J. et al. 2008. SIRT1 contributes in part to cisplatin resistance in cancer cells by altering mitochondrial metabolism. Mol. Cancer Res. 6: 1499-1506.
    • (2008) Mol. Cancer Res. , vol.6 , pp. 1499-1506
    • Liang, X.J.1
  • 85
    • 77958126835 scopus 로고    scopus 로고
    • Amurensin G, a potent natural SIRT1 inhibitor, rescues doxorubicin responsiveness via down-regulation of multidrug resistance 1
    • Oh, W.K. et al. 2010. Amurensin G, a potent natural SIRT1 inhibitor, rescues doxorubicin responsiveness via down-regulation of multidrug resistance 1. Mol. Pharmacol. 78: 855-864.
    • (2010) Mol. Pharmacol. , vol.78 , pp. 855-864
    • Oh, W.K.1
  • 86
    • 84873408603 scopus 로고    scopus 로고
    • SIRT1 deacetylase promotes acquisition of genetic mutations for drug resistance in CML cells
    • Mar 12. doi:10.1038/onc.2012.83. [Epub ahead of print].
    • Wang, Z. et al. 2012. SIRT1 deacetylase promotes acquisition of genetic mutations for drug resistance in CML cells. Oncogene. Mar 12. doi:10.1038/onc.2012.83. [Epub ahead of print].
    • (2012) Oncogene.
    • Wang, Z.1
  • 87
    • 34548598664 scopus 로고    scopus 로고
    • Downregulation of Sirt1 by antisense oligonucleotides induces apoptosis and enhances radiation sensitization in A549 lung cancer cells
    • Sun, Y. et al. 2007. Downregulation of Sirt1 by antisense oligonucleotides induces apoptosis and enhances radiation sensitization in A549 lung cancer cells. Lung Cancer 58: 21-29.
    • (2007) Lung Cancer , vol.58 , pp. 21-29
    • Sun, Y.1
  • 88
    • 34250365395 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1
    • Tanno, M. et al. 2007. Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J. Biol. Chem. 282: 6823-6832.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6823-6832
    • Tanno, M.1
  • 89
    • 25144454432 scopus 로고    scopus 로고
    • Increased dosage of mammalian Sir2 in pancreatic beta cells enhances glucose-stimulated insulin secretion in mice
    • Moynihan, K.A. et al. 2005. Increased dosage of mammalian Sir2 in pancreatic beta cells enhances glucose-stimulated insulin secretion in mice. Cell Metab. 2: 105-117.
    • (2005) Cell Metab. , vol.2 , pp. 105-117
    • Moynihan, K.A.1
  • 90
    • 36348974168 scopus 로고    scopus 로고
    • The direct involvement of SirT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation
    • Zhang, J. 2007. The direct involvement of SirT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation. J. Biol. Chem. 282: 34356-34364.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34356-34364
    • Zhang, J.1
  • 91
    • 78650048197 scopus 로고    scopus 로고
    • Aberrant cytoplasm localization and protein stability of SIRT1 is regulated by PI3K/IGF-1R signaling in human cancer cells
    • Byles, V. et al. 2010. Aberrant cytoplasm localization and protein stability of SIRT1 is regulated by PI3K/IGF-1R signaling in human cancer cells. Int. J. Biol. Sci. 6: 599-612.
    • (2010) Int. J. Biol. Sci. , vol.6 , pp. 599-612
    • Byles, V.1
  • 92
    • 69249161792 scopus 로고    scopus 로고
    • MYC insertions in diffuse-type gastric adenocarcinoma
    • Calcagno, D.Q. et al. 2009. MYC insertions in diffuse-type gastric adenocarcinoma. Anticancer Res. 29: 2479-2483.
    • (2009) Anticancer Res. , vol.29 , pp. 2479-2483
    • Calcagno, D.Q.1
  • 93
    • 0842269247 scopus 로고    scopus 로고
    • The importance of p53 location: nuclear or cytoplasmic zip code
    • O'Brate, A. & P. Giannakakou. 2003. The importance of p53 location: nuclear or cytoplasmic zip code Drug Resist. Updat. 6: 313-322.
    • (2003) Drug Resist. Updat. , vol.6 , pp. 313-322
    • O'Brate, A.1    Giannakakou, P.2
  • 94
    • 65949083750 scopus 로고    scopus 로고
    • Cytoplasmic functions of the tumour suppressor p53
    • Green, D.R. & G. Kroemer. 2009. Cytoplasmic functions of the tumour suppressor p53. Nature 458: 1127-1130.
    • (2009) Nature , vol.458 , pp. 1127-1130
    • Green, D.R.1    Kroemer, G.2
  • 95
    • 79953898189 scopus 로고    scopus 로고
    • Sirtuin 1 in lipid metabolism and obesity
    • Schug, T.T. & X. Li. 2011. Sirtuin 1 in lipid metabolism and obesity. Ann. Med. 43: 198-211.
    • (2011) Ann. Med. , vol.43 , pp. 198-211
    • Schug, T.T.1    Li, X.2
  • 96
    • 80052638751 scopus 로고    scopus 로고
    • Sirtinol treatment reduces inflammation in human dermal microvascular endothelial cells
    • Orecchia, A. et al. 2011. Sirtinol treatment reduces inflammation in human dermal microvascular endothelial cells. PLoS One 6: e24307.
    • (2011) PLoS One , vol.6
    • Orecchia, A.1
  • 97
    • 77953724950 scopus 로고    scopus 로고
    • Protein deacetylase SIRT1 in the cytoplasm promotes nerve growth factor-induced neurite outgrowth in PC12 cells
    • Sugino, T. et al. 2010. Protein deacetylase SIRT1 in the cytoplasm promotes nerve growth factor-induced neurite outgrowth in PC12 cells. FEBS Lett. 584: 2821-2826.
    • (2010) FEBS Lett. , vol.584 , pp. 2821-2826
    • Sugino, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.