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Volumn 1171, Issue , 2009, Pages 59-76

Signal transducer and activator of transcription-3, inflammation, and cancer: How intimate is the relationship?

Author keywords

Cancer; Chemoresistance; Inflammation; STAT 3

Indexed keywords

2 CYANO 3,12 DIOXOOLEANA 1,9 DIEN 28 OIC ACID; 2,5 DIHYDROXYBENZENESULFONIC ACID; 7 HYDROXYSTAUROSPORINE; ATIPRIMOD; AURANOFIN; AUROTHIOMALATE; CHALCONE; CORE PROTEIN; CYCLIN D1; EMODIN; EPIGALLOCATECHIN GALLATE; FLAVOPIRIDOL; FLICE INHIBITORY PROTEIN; GELATINASE A; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 11; INTERLEUKIN 12P40; INTERLEUKIN 6; LONAFARNIB; MYC PROTEIN; NELFINAVIR; PROTEIN BCL XL; PROTEIN C FOS; PROTEIN MCL 1; RESVERATROL; RITUXIMAB; S 31 M 2001; SALICYLATE SODIUM; SD 1029; SILIBININ; STA 21; STAT3 PROTEIN; SURVIVIN; T 40214; TIPIFARNIB; TKS 050; UNCLASSIFIED DRUG; VASCULOTROPIN; WP 1034;

EID: 69149098253     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2009.04911.x     Document Type: Conference Paper
Times cited : (621)

References (243)
  • 1
    • 0028303977 scopus 로고
    • Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway
    • Akira, S. et al. 1994. Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway. Cell 77 : 63 71.
    • (1994) Cell , vol.77 , pp. 63-71
    • Akira, S.1
  • 2
    • 0028349735 scopus 로고
    • Stat3: A STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
    • Zhong, Z., Z. Wen J.E. Darnell, Jr. 1994. Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science 264 : 95 98.
    • (1994) Science , vol.264 , pp. 95-98
    • Zhong, Z.1    Wen, Z.2    Darnell Jr., J.E.3
  • 3
    • 0029916933 scopus 로고    scopus 로고
    • Activation and association of Stat3 with Src in v-Src-transformed cell lines
    • Cao, X. et al. 1996. Activation and association of Stat3 with Src in v-Src-transformed cell lines. Mol. Cell Biol. 16 : 1595 1603.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1595-1603
    • Cao, X.1
  • 4
    • 0029966664 scopus 로고    scopus 로고
    • Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins
    • Vignais, M.L. et al. 1996. Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins. Mol. Cell Biol. 16 : 1759 1769.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1759-1769
    • Vignais, M.L.1
  • 5
    • 0029069540 scopus 로고
    • Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein
    • Yu, C.L. et al. 1995. Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein. Science 269 : 81 83.
    • (1995) Science , vol.269 , pp. 81-83
    • Yu, C.L.1
  • 6
    • 0031137912 scopus 로고    scopus 로고
    • Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase
    • Giordano, V. et al. 1997. Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase. J. Immunol. 158 : 4097 4103.
    • (1997) J. Immunol. , vol.158 , pp. 4097-4103
    • Giordano, V.1
  • 7
    • 33750135226 scopus 로고    scopus 로고
    • Receptor-mediated tobacco toxicity: Cooperation of the Ras/Raf-1/MEK1/ERK and JAK-2/STAT-3 pathways downstream of alpha7 nicotinic receptor in oral keratinocytes
    • Arredondo, J. et al. 2006. Receptor-mediated tobacco toxicity: cooperation of the Ras/Raf-1/MEK1/ERK and JAK-2/STAT-3 pathways downstream of alpha7 nicotinic receptor in oral keratinocytes. FASEB J. 20 : 2093 2101.
    • (2006) FASEB J. , vol.20 , pp. 2093-2101
    • Arredondo, J.1
  • 8
    • 0037087577 scopus 로고    scopus 로고
    • Regulation of cell proliferation, apoptosis, and transcription factor activities during the promotion of liver carcinogenesis by polychlorinated biphenyls
    • Tharappel, J.C. et al. 2002. Regulation of cell proliferation, apoptosis, and transcription factor activities during the promotion of liver carcinogenesis by polychlorinated biphenyls. Toxicol. Appl. Pharmacol. 179 : 172 184.
    • (2002) Toxicol. Appl. Pharmacol. , vol.179 , pp. 172-184
    • Tharappel, J.C.1
  • 9
    • 4944239032 scopus 로고    scopus 로고
    • Disruption of Stat3 reveals a critical role in both the initiation and the promotion stages of epithelial carcinogenesis
    • Chan, K.S. et al. 2004. Disruption of Stat3 reveals a critical role in both the initiation and the promotion stages of epithelial carcinogenesis. J. Clin. Invest. 114 : 720 728.
    • (2004) J. Clin. Invest. , vol.114 , pp. 720-728
    • Chan, K.S.1
  • 10
    • 34547951341 scopus 로고    scopus 로고
    • Can the protective actions of JAK-STAT in the heart be exploited therapeutically? Parsing the regulation of interleukin-6-type cytokine signaling
    • Kurdi, M. G.W. Booz. 2007. Can the protective actions of JAK-STAT in the heart be exploited therapeutically? Parsing the regulation of interleukin-6-type cytokine signaling. J. Cardiovasc. Pharmacol. 50 : 126 141.
    • (2007) J. Cardiovasc. Pharmacol. , vol.50 , pp. 126-141
    • Kurdi, M.1    Booz, G.W.2
  • 11
    • 0842308889 scopus 로고    scopus 로고
    • CNTF promotes survival of retinal ganglion cells after induction of ocular hypertension in rats: The possible involvement of STAT3 pathway
    • Ji, J.Z. et al. 2004. CNTF promotes survival of retinal ganglion cells after induction of ocular hypertension in rats: the possible involvement of STAT3 pathway. Eur. J. Neurosci. 19 : 265 272.
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 265-272
    • Ji, J.Z.1
  • 12
    • 0028849704 scopus 로고
    • Activation of signal transducer and activator of transcription-3 (Stat3) expression by interferon-gamma and interleukin-6 in hepatoma cells
    • Kordula, T. et al. 1995. Activation of signal transducer and activator of transcription-3 (Stat3) expression by interferon-gamma and interleukin-6 in hepatoma cells. Biochem. Biophys. Res. Commun. 216 : 999 1005.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 999-1005
    • Kordula, T.1
  • 13
    • 8444247043 scopus 로고    scopus 로고
    • IL-5 and granulocyte-macrophage colony-stimulating factor activate STAT3 and STAT5 and promote Pim-1 and cyclin D3 protein expression in human eosinophils
    • Stout, B.A. et al. 2004. IL-5 and granulocyte-macrophage colony-stimulating factor activate STAT3 and STAT5 and promote Pim-1 and cyclin D3 protein expression in human eosinophils. J. Immunol. 173 : 6409 6417.
    • (2004) J. Immunol. , vol.173 , pp. 6409-6417
    • Stout, B.A.1
  • 14
    • 0029785080 scopus 로고    scopus 로고
    • A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9
    • Demoulin, J.B. et al. 1996. A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9. Mol. Cell Biol. 16 : 4710 4716.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 4710-4716
    • Demoulin, J.B.1
  • 15
    • 0346103717 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3 is the dominant mediator of the anti-inflammatory effects of IL-10 in human macrophages
    • Williams, L. et al. 2004. Signal transducer and activator of transcription 3 is the dominant mediator of the anti-inflammatory effects of IL-10 in human macrophages. J. Immunol. 172 : 567 576.
    • (2004) J. Immunol. , vol.172 , pp. 567-576
    • Williams, L.1
  • 16
    • 0034105254 scopus 로고    scopus 로고
    • Astrocyte differentiation of fetal neuroepithelial cells by interleukin-11 via activation of a common cytokine signal transducer, gp130, and a transcription factor, STAT3
    • Yanagisawa, M. et al. 2000. Astrocyte differentiation of fetal neuroepithelial cells by interleukin-11 via activation of a common cytokine signal transducer, gp130, and a transcription factor, STAT3. J. Neurochem. 74 : 1498 1504.
    • (2000) J. Neurochem. , vol.74 , pp. 1498-1504
    • Yanagisawa, M.1
  • 17
    • 0028943484 scopus 로고
    • Interleukin 12 signaling in T helper type 1 (Th1) cells involves tyrosine phosphorylation of signal transducer and activator of transcription (Stat)3 and Stat4
    • Jacobson, N.G. et al. 1995. Interleukin 12 signaling in T helper type 1 (Th1) cells involves tyrosine phosphorylation of signal transducer and activator of transcription (Stat)3 and Stat4. J. Exp. Med. 181 : 1755 1762.
    • (1995) J. Exp. Med. , vol.181 , pp. 1755-1762
    • Jacobson, N.G.1
  • 18
    • 36849036211 scopus 로고    scopus 로고
    • IL-21 is produced by Th17 cells and drives IL-17 production in a STAT3-dependent manner
    • Wei, L. et al. 2007. IL-21 is produced by Th17 cells and drives IL-17 production in a STAT3-dependent manner. J. Biol. Chem. 282 : 34605 34610.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34605-34610
    • Wei, L.1
  • 19
    • 2342462460 scopus 로고    scopus 로고
    • Interleukin 22 (IL-22) plays a protective role in T cell-mediated murine hepatitis: IL-22 is a survival factor for hepatocytes via STAT3 activation
    • Radaeva, S. et al. 2004. Interleukin 22 (IL-22) plays a protective role in T cell-mediated murine hepatitis: IL-22 is a survival factor for hepatocytes via STAT3 activation. Hepatology 39 : 1332 1342.
    • (2004) Hepatology , vol.39 , pp. 1332-1342
    • Radaeva, S.1
  • 20
    • 22644446255 scopus 로고    scopus 로고
    • Tuning of macrophage responses by Stat3-inducing cytokines: Molecular mechanisms and consequences in infection
    • Lang, R. 2005. Tuning of macrophage responses by Stat3-inducing cytokines: molecular mechanisms and consequences in infection. Immunobiology 210 : 63 76.
    • (2005) Immunobiology , vol.210 , pp. 63-76
    • Lang, R.1
  • 21
    • 34249931559 scopus 로고    scopus 로고
    • LIGHT, a member of the TNF superfamily, activates Stat3 mediated by NIK pathway
    • Nadiminty, N. et al. 2007. LIGHT, a member of the TNF superfamily, activates Stat3 mediated by NIK pathway. Biochem. Biophys. Res. Commun. 359 : 379 384.
    • (2007) Biochem. Biophys. Res. Commun. , vol.359 , pp. 379-384
    • Nadiminty, N.1
  • 22
    • 2642641315 scopus 로고    scopus 로고
    • The chemokine monocyte chemotactic protein 1 triggers Janus kinase 2 activation and tyrosine phosphorylation of the CCR2B receptor
    • Mellado, M. et al. 1998. The chemokine monocyte chemotactic protein 1 triggers Janus kinase 2 activation and tyrosine phosphorylation of the CCR2B receptor. J. Immunol. 161 : 805 813.
    • (1998) J. Immunol. , vol.161 , pp. 805-813
    • Mellado, M.1
  • 23
    • 0031594715 scopus 로고    scopus 로고
    • RANTES and MIP-1alpha activate stats in T cells
    • Wong, M. E.N. Fish. 1998. RANTES and MIP-1alpha activate stats in T cells. J. Biol. Chem. 273 : 309 314.
    • (1998) J. Biol. Chem. , vol.273 , pp. 309-314
    • Wong, M.1    Fish, E.N.2
  • 24
    • 50349102697 scopus 로고    scopus 로고
    • Box 2 region of the oncostatin m receptor determines specificity for recruitment of Janus kinases and STAT5 activation
    • Hintzen, C. et al. 2008. Box 2 region of the oncostatin m receptor determines specificity for recruitment of Janus kinases and STAT5 activation. J. Biol. Chem. 283 : 19465 19477.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19465-19477
    • Hintzen, C.1
  • 25
    • 0030006364 scopus 로고    scopus 로고
    • Steel factor induces serine phosphorylation of Stat3 in human growth factor-dependent myeloid cell lines
    • Gotoh, A. et al. 1996. Steel factor induces serine phosphorylation of Stat3 in human growth factor-dependent myeloid cell lines. Blood 88 : 138 145.
    • (1996) Blood , vol.88 , pp. 138-145
    • Gotoh, A.1
  • 26
    • 0036148801 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha (TNF-alpha) activates Jak1/Stat3-Stat5B signaling through TNFR-1 in human B cells
    • Miscia, S. et al. 2002. Tumor necrosis factor alpha (TNF-alpha) activates Jak1/Stat3-Stat5B signaling through TNFR-1 in human B cells. Cell Growth Differ. 13 : 13 18.
    • (2002) Cell Growth Differ. , vol.13 , pp. 13-18
    • Miscia, S.1
  • 27
    • 2442593744 scopus 로고    scopus 로고
    • Selective activation of STAT3 in human monocytes stimulated by G-CSF: Implication in inhibition of LPS-induced TNF-alpha production
    • Nishiki, S. et al. 2004. Selective activation of STAT3 in human monocytes stimulated by G-CSF: implication in inhibition of LPS-induced TNF-alpha production. Am. J. Physiol. Cell Physiol. 286 : C1302 1311.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Nishiki, S.1
  • 28
    • 0013689209 scopus 로고    scopus 로고
    • Requirement of Stat3 but not Stat1 activation for epidermal growth factor receptor- mediated cell growth in vitro
    • Grandis, J.R. et al. 1998. Requirement of Stat3 but not Stat1 activation for epidermal growth factor receptor- mediated cell growth in vitro. J. Clin. Invest. 102 : 1385 1392.
    • (1998) J. Clin. Invest. , vol.102 , pp. 1385-1392
    • Grandis, J.R.1
  • 29
    • 33847076848 scopus 로고    scopus 로고
    • Diesel exhaust particulate-induced activation of Stat3 requires activities of EGFR and Src in airway epithelial cells
    • Cao, D. et al. 2007. Diesel exhaust particulate-induced activation of Stat3 requires activities of EGFR and Src in airway epithelial cells. Am. J. Physiol. Lung Cell Mol. Physiol. 292 : L422 429.
    • (2007) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.292
    • Cao, D.1
  • 30
    • 0036717295 scopus 로고    scopus 로고
    • Activation of STAT3 by the hepatitis C virus core protein leads to cellular transformation
    • Yoshida, T. et al. 2002. Activation of STAT3 by the hepatitis C virus core protein leads to cellular transformation. J. Exp. Med. 196 : 641 653.
    • (2002) J. Exp. Med. , vol.196 , pp. 641-653
    • Yoshida, T.1
  • 31
    • 4344568740 scopus 로고    scopus 로고
    • Role of endogenous IL-10 in LPS-induced STAT3 activation and IL-1 receptor antagonist gene expression
    • Carl, V.S. et al. 2004. Role of endogenous IL-10 in LPS-induced STAT3 activation and IL-1 receptor antagonist gene expression. J. Leukoc. Biol. 76 : 735 742.
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 735-742
    • Carl, V.S.1
  • 32
    • 0036569522 scopus 로고    scopus 로고
    • Activation of Stat-3 as one of the early events in tobacco chewing-mediated oral carcinogenesis
    • Nagpal, J.K., R. Mishra B.R. Das. 2002. Activation of Stat-3 as one of the early events in tobacco chewing-mediated oral carcinogenesis. Cancer 94 : 2393 2400.
    • (2002) Cancer , vol.94 , pp. 2393-2400
    • Nagpal, J.K.1    Mishra, R.2    Das, B.R.3
  • 33
    • 20444452000 scopus 로고    scopus 로고
    • Ultraviolet B exposure activates Stat3 signaling via phosphorylation at tyrosine705 in skin of SKH1 hairless mouse: A target for the management of skin cancer?
    • Ahsan, H., M.H. Aziz N. Ahmad. 2005. Ultraviolet B exposure activates Stat3 signaling via phosphorylation at tyrosine705 in skin of SKH1 hairless mouse: a target for the management of skin cancer? Biochem. Biophys. Res. Commun. 333 : 241 246.
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 241-246
    • Ahsan, H.1    Aziz, M.H.2    Ahmad, N.3
  • 34
    • 34848856813 scopus 로고    scopus 로고
    • Activation of the interleukin-6/STAT3 antiapoptotic pathway in esophageal cells by bile acids and low pH: Relevance to barrett's esophagus
    • Dvorak, K. et al. 2007. Activation of the interleukin-6/STAT3 antiapoptotic pathway in esophageal cells by bile acids and low pH: relevance to barrett's esophagus. Clin. Cancer Res. 13 : 5305 5313.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 5305-5313
    • Dvorak, K.1
  • 35
    • 47249161117 scopus 로고    scopus 로고
    • Novel black soy peptides with antiobesity effects: Activation of leptin-like signaling and AMP-activated protein kinase
    • Jang, E.H. et al. 2008. Novel black soy peptides with antiobesity effects: activation of leptin-like signaling and AMP-activated protein kinase. Int. J. Obes. (Lond.) 32 : 1161 1170.
    • (2008) Int. J. Obes. (Lond.) , vol.32 , pp. 1161-1170
    • Jang, E.H.1
  • 36
    • 45549108898 scopus 로고    scopus 로고
    • Activated Ca2+/calmodulin-dependent protein kinase IIgamma is a critical regulator of myeloid leukemia cell proliferation
    • Si, J. S.J. Collins. 2008. Activated Ca2+/calmodulin-dependent protein kinase IIgamma is a critical regulator of myeloid leukemia cell proliferation. Cancer Res. 68 : 3733 3742.
    • (2008) Cancer Res. , vol.68 , pp. 3733-3742
    • Si, J.1    Collins, S.J.2
  • 37
    • 34548675199 scopus 로고    scopus 로고
    • Cardioplegia and diazoxide modulate STAT3 activation and DNA binding
    • Hsieh, Y.J. et al. 2007. Cardioplegia and diazoxide modulate STAT3 activation and DNA binding. Ann. Thorac. Surg. 84 : 1272 1278.
    • (2007) Ann. Thorac. Surg. , vol.84 , pp. 1272-1278
    • Hsieh, Y.J.1
  • 38
    • 36148987265 scopus 로고    scopus 로고
    • Physiologically achievable concentrations of genistein enhance telomerase activity in prostate cancer cells via the activation of STAT3
    • Chau, M.N. et al. 2007. Physiologically achievable concentrations of genistein enhance telomerase activity in prostate cancer cells via the activation of STAT3. Carcinogenesis 28 : 2282 2290.
    • (2007) Carcinogenesis , vol.28 , pp. 2282-2290
    • Chau, M.N.1
  • 39
    • 33750293043 scopus 로고    scopus 로고
    • Metallothionein mediates cardioprotection of isoliquiritigenin against ischemia-reperfusion through JAK2/STAT3 activation
    • An, W., J. Yang Y. Ao. 2006. Metallothionein mediates cardioprotection of isoliquiritigenin against ischemia-reperfusion through JAK2/STAT3 activation. Acta Pharmacol. Sin. 27 : 1431 1437.
    • (2006) Acta Pharmacol. Sin. , vol.27 , pp. 1431-1437
    • An, W.1    Yang, J.2    Ao, Y.3
  • 40
    • 0029739826 scopus 로고    scopus 로고
    • Leptin activation of Stat3 in the hypothalamus of wild-type and ob/ob mice but not db/db mice
    • Vaisse, C. et al. 1996. Leptin activation of Stat3 in the hypothalamus of wild-type and ob/ob mice but not db/db mice. Nat. Genet. 14 : 95 97.
    • (1996) Nat. Genet. , vol.14 , pp. 95-97
    • Vaisse, C.1
  • 41
    • 48249147414 scopus 로고    scopus 로고
    • Morphine induces mesangial cell proliferation and glomerulopathy via kappa-opioid receptors
    • Weber, M.L. et al. 2008. Morphine induces mesangial cell proliferation and glomerulopathy via kappa-opioid receptors. Am. J. Physiol. Renal. Physiol. 294 : F1388 1397.
    • (2008) Am. J. Physiol. Renal. Physiol. , vol.294
    • Weber, M.L.1
  • 42
    • 34548031646 scopus 로고    scopus 로고
    • Chronic olanzapine activates the Stat3 signal transduction pathway and alters expression of components of the 5-HT2A receptor signaling system in rat frontal cortex
    • Muma, N.A. et al. 2007. Chronic olanzapine activates the Stat3 signal transduction pathway and alters expression of components of the 5-HT2A receptor signaling system in rat frontal cortex. Neuropharmacology 53 : 552 562.
    • (2007) Neuropharmacology , vol.53 , pp. 552-562
    • Muma, N.A.1
  • 43
    • 0032483533 scopus 로고    scopus 로고
    • Activation of the Janus kinase/signal transducer and activator of transcription pathway by osmotic shock
    • Gatsios, P. et al. 1998. Activation of the Janus kinase/signal transducer and activator of transcription pathway by osmotic shock. J. Biol. Chem. 273 : 22962 22968.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22962-22968
    • Gatsios, P.1
  • 44
    • 0030978808 scopus 로고    scopus 로고
    • Constitutive activation of a slowly migrating isoform of Stat3 in mycosis fungoides: Tyrphostin AG490 inhibits Stat3 activation and growth of mycosis fungoides tumor cell lines
    • Nielsen, M. et al. 1997. Constitutive activation of a slowly migrating isoform of Stat3 in mycosis fungoides: tyrphostin AG490 inhibits Stat3 activation and growth of mycosis fungoides tumor cell lines. Proc. Natl. Acad. Sci. USA 94 : 6764 6769.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6764-6769
    • Nielsen, M.1
  • 45
    • 23044478114 scopus 로고    scopus 로고
    • Atiprimod blocks STAT3 phosphorylation and induces apoptosis in multiple myeloma cells
    • Amit-Vazina, M. et al. 2005. Atiprimod blocks STAT3 phosphorylation and induces apoptosis in multiple myeloma cells. Br. J. Cancer 93 : 70 80.
    • (2005) Br. J. Cancer , vol.93 , pp. 70-80
    • Amit-Vazina, M.1
  • 46
    • 35948995412 scopus 로고    scopus 로고
    • Auranofin blocks interleukin-6 signalling by inhibiting phosphorylation of JAK1 and STAT3
    • Kim, N.H. et al. 2007. Auranofin blocks interleukin-6 signalling by inhibiting phosphorylation of JAK1 and STAT3. Immunology 122 : 607 614.
    • (2007) Immunology , vol.122 , pp. 607-614
    • Kim, N.H.1
  • 47
    • 34047260409 scopus 로고    scopus 로고
    • The anti-rheumatic gold salt aurothiomalate suppresses interleukin-1beta-induced hyaluronan accumulation by blocking HAS1 transcription and by acting as a COX-2 transcriptional repressor
    • Stuhlmeier, K.M. 2007. The anti-rheumatic gold salt aurothiomalate suppresses interleukin-1beta-induced hyaluronan accumulation by blocking HAS1 transcription and by acting as a COX-2 transcriptional repressor. J. Biol. Chem. 282 : 2250 2258.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2250-2258
    • Stuhlmeier, K.M.1
  • 48
    • 33645821453 scopus 로고    scopus 로고
    • Potent inhibition of platelet-derived growth factor-induced responses in vascular smooth muscle cells by BMS-354825 (dasatinib)
    • Chen, Z. et al. 2006. Potent inhibition of platelet-derived growth factor-induced responses in vascular smooth muscle cells by BMS-354825 (dasatinib). Mol. Pharmacol. 69 : 1527 1533.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1527-1533
    • Chen, Z.1
  • 49
    • 34548059697 scopus 로고    scopus 로고
    • Caffeic acid and its synthetic derivative CADPE suppress tumor angiogenesis by blocking STAT3-mediated VEGF expression in human renal carcinoma cells
    • Jung, J.E. et al. 2007. Caffeic acid and its synthetic derivative CADPE suppress tumor angiogenesis by blocking STAT3-mediated VEGF expression in human renal carcinoma cells. Carcinogenesis 28 : 1780 1787.
    • (2007) Carcinogenesis , vol.28 , pp. 1780-1787
    • Jung, J.E.1
  • 50
    • 33750982120 scopus 로고    scopus 로고
    • Stattic: A small-molecule inhibitor of STAT3 activation and dimerization
    • Schust, J. et al. 2006. Stattic: a small-molecule inhibitor of STAT3 activation and dimerization. Chem. Biol. 13 : 1235 1242.
    • (2006) Chem. Biol. , vol.13 , pp. 1235-1242
    • Schust, J.1
  • 51
    • 33645767865 scopus 로고    scopus 로고
    • Dobesilate inhibits the activation of signal transducer and activator of transcription 3, and the expression of cyclin D1 and bcl-XL in glioma cells
    • Cuevas, P. et al. 2006. Dobesilate inhibits the activation of signal transducer and activator of transcription 3, and the expression of cyclin D1 and bcl-XL in glioma cells. Neurol. Res. 28 : 127 130.
    • (2006) Neurol. Res. , vol.28 , pp. 127-130
    • Cuevas, P.1
  • 52
    • 0032792685 scopus 로고    scopus 로고
    • Ethanol rapidly inhibits IL-6-activated STAT3 and C/EBP mRNA expression in freshly isolated rat hepatocytes
    • Chen, J., G. Kunos B. Gao. 1999. Ethanol rapidly inhibits IL-6-activated STAT3 and C/EBP mRNA expression in freshly isolated rat hepatocytes. FEBS Lett. 457 : 162 168.
    • (1999) FEBS Lett. , vol.457 , pp. 162-168
    • Chen, J.1    Kunos, G.2    Gao, B.3
  • 53
    • 38349191618 scopus 로고    scopus 로고
    • NCX-4016, a nitro-derivative of aspirin, inhibits EGFR and STAT3 signaling and modulates Bcl-2 proteins in cisplatin-resistant human ovarian cancer cells and xenografts
    • Selvendiran, K. et al. 2008. NCX-4016, a nitro-derivative of aspirin, inhibits EGFR and STAT3 signaling and modulates Bcl-2 proteins in cisplatin-resistant human ovarian cancer cells and xenografts. Cell Cycle 7 : 81 88.
    • (2008) Cell Cycle , vol.7 , pp. 81-88
    • Selvendiran, K.1
  • 54
    • 23844434338 scopus 로고    scopus 로고
    • HIV-1 protease inhibitor induces growth arrest and apoptosis of human prostate cancer LNCaP cells in vitro and in vivo in conjunction with blockade of androgen receptor STAT3 and AKT signaling
    • Yang, Y. et al. 2005. HIV-1 protease inhibitor induces growth arrest and apoptosis of human prostate cancer LNCaP cells in vitro and in vivo in conjunction with blockade of androgen receptor STAT3 and AKT signaling. Cancer Sci. 96 : 425 433.
    • (2005) Cancer Sci. , vol.96 , pp. 425-433
    • Yang, Y.1
  • 55
    • 0043175471 scopus 로고    scopus 로고
    • Identification and characterization of signal transducer and activator of transcription 3 recruitment sites within the epidermal growth factor receptor
    • Shao, H. et al. 2003. Identification and characterization of signal transducer and activator of transcription 3 recruitment sites within the epidermal growth factor receptor. Cancer Res. 63 : 3923 3930.
    • (2003) Cancer Res. , vol.63 , pp. 3923-3930
    • Shao, H.1
  • 56
    • 42449129677 scopus 로고    scopus 로고
    • Synthesis, characterization and Stat3 inhibitory properties of the prototypical platinum(IV) anticancer drug, [PtCl3(NO2)(NH3)2] (CPA-7)
    • Littlefield, S.L. et al. 2008. Synthesis, characterization and Stat3 inhibitory properties of the prototypical platinum(IV) anticancer drug, [PtCl3(NO2)(NH3)2] (CPA-7). Inorg. Chem. 47 : 2798 2804.
    • (2008) Inorg. Chem. , vol.47 , pp. 2798-2804
    • Littlefield, S.L.1
  • 57
    • 0346122900 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 abrogates IL-6 triggered signaling cascades via caspase-dependent downregulation of gp130 in multiple myeloma
    • Hideshima, T. et al. 2003. Proteasome inhibitor PS-341 abrogates IL-6 triggered signaling cascades via caspase-dependent downregulation of gp130 in multiple myeloma. Oncogene 22 : 8386 8393.
    • (2003) Oncogene , vol.22 , pp. 8386-8393
    • Hideshima, T.1
  • 58
    • 0037294154 scopus 로고    scopus 로고
    • Identification of a high-affinity phosphopeptide inhibitor of Stat3
    • Ren, Z. et al. 2003. Identification of a high-affinity phosphopeptide inhibitor of Stat3. Bioorg. Med. Chem. Lett. 13 : 633 636.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 633-636
    • Ren, Z.1
  • 59
    • 16844365486 scopus 로고    scopus 로고
    • Farnesyl transferase inhibitor (R115777)-induced inhibition of STAT3(Tyr705) phosphorylation in human pancreatic cancer cell lines require extracellular signal-regulated kinases
    • Venkatasubbarao, K., A. Choudary J.W. Freeman. 2005. Farnesyl transferase inhibitor (R115777)-induced inhibition of STAT3(Tyr705) phosphorylation in human pancreatic cancer cell lines require extracellular signal-regulated kinases. Cancer Res. 65 : 2861 2871.
    • (2005) Cancer Res. , vol.65 , pp. 2861-2871
    • Venkatasubbarao, K.1    Choudary, A.2    Freeman, J.W.3
  • 60
    • 38649129118 scopus 로고    scopus 로고
    • An oxazole-based small-molecule Stat3 inhibitor modulates Stat3 stability and processing and induces antitumor cell effects
    • Siddiquee, K.A. et al. 2007. An oxazole-based small-molecule Stat3 inhibitor modulates Stat3 stability and processing and induces antitumor cell effects. ACS Chem. Biol. 2 : 787 798.
    • (2007) ACS Chem. Biol. , vol.2 , pp. 787-798
    • Siddiquee, K.A.1
  • 61
    • 34250658084 scopus 로고    scopus 로고
    • Selective chemical probe inhibitor of Stat3, identified through structure-based virtual screening, induces antitumor activity
    • Siddiquee, K. et al. 2007. Selective chemical probe inhibitor of Stat3, identified through structure-based virtual screening, induces antitumor activity. Proc. Natl. Acad. Sci. USA 104 : 7391 7396.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7391-7396
    • Siddiquee, K.1
  • 62
    • 36549089617 scopus 로고    scopus 로고
    • SCH66336, inhibitor of protein farnesylation, blocks signal transducer and activators of transcription 3 signaling in lung cancer and interacts with a small molecule inhibitor of epidermal growth factor receptor/human epidermal growth factor receptor 2
    • Dowlati, A. et al. 2008. SCH66336, inhibitor of protein farnesylation, blocks signal transducer and activators of transcription 3 signaling in lung cancer and interacts with a small molecule inhibitor of epidermal growth factor receptor/human epidermal growth factor receptor 2. Anticancer Drugs 19 : 9 16.
    • (2008) Anticancer Drugs , vol.19 , pp. 9-16
    • Dowlati, A.1
  • 63
    • 33845310503 scopus 로고    scopus 로고
    • SD-1029 inhibits signal transducer and activator of transcription 3 nuclear translocation
    • Duan, Z. et al. 2006. SD-1029 inhibits signal transducer and activator of transcription 3 nuclear translocation. Clin. Cancer Res. 12 : 6844 6852.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 6844-6852
    • Duan, Z.1
  • 64
    • 0036535981 scopus 로고    scopus 로고
    • Selective inhibition of STAT3 phosphorylation by sodium salicylate in cardiac fibroblasts
    • Wang, Z., B. Jiang P. Brecher. 2002. Selective inhibition of STAT3 phosphorylation by sodium salicylate in cardiac fibroblasts. Biochem. Pharmacol. 63 : 1197 1207.
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 1197-1207
    • Wang, Z.1    Jiang, B.2    Brecher, P.3
  • 65
    • 20144379879 scopus 로고    scopus 로고
    • Statins reduce interleukin-6-induced C-reactive protein in human hepatocytes: New evidence for direct antiinflammatory effects of statins
    • Arnaud, C. et al. 2005. Statins reduce interleukin-6-induced C-reactive protein in human hepatocytes: new evidence for direct antiinflammatory effects of statins. Arterioscler Thromb. Vasc. Biol. 25 : 1231 1236.
    • (2005) Arterioscler Thromb. Vasc. Biol. , vol.25 , pp. 1231-1236
    • Arnaud, C.1
  • 66
    • 0344984245 scopus 로고    scopus 로고
    • Targeting Stat3 with G-quartet oligodeoxynucleotides in human cancer cells
    • Jing, N. et al. 2003. Targeting Stat3 with G-quartet oligodeoxynucleotides in human cancer cells. DNA Cell Biol. 22 : 685 696.
    • (2003) DNA Cell Biol. , vol.22 , pp. 685-696
    • Jing, N.1
  • 67
    • 19944432818 scopus 로고    scopus 로고
    • The broad-range cyclin-dependent kinase inhibitor UCN-01 induces apoptosis in colon carcinoma cells through transcriptional suppression of the Bcl-x(L) protein
    • Bhonde, M.R. et al. 2005. The broad-range cyclin-dependent kinase inhibitor UCN-01 induces apoptosis in colon carcinoma cells through transcriptional suppression of the Bcl-x(L) protein. Oncogene 24 : 148 156.
    • (2005) Oncogene , vol.24 , pp. 148-156
    • Bhonde, M.R.1
  • 68
    • 21344459787 scopus 로고    scopus 로고
    • WP-1034, a novel JAK-STAT inhibitor, with proapoptotic and antileukemic activity in acute myeloid leukemia (AML)
    • Faderl, S. et al. 2005. WP-1034, a novel JAK-STAT inhibitor, with proapoptotic and antileukemic activity in acute myeloid leukemia (AML). Anticancer Res. 25 : 1841 1850.
    • (2005) Anticancer Res. , vol.25 , pp. 1841-1850
    • Faderl, S.1
  • 69
    • 34249792353 scopus 로고    scopus 로고
    • Capsaicin is a novel blocker of constitutive and interleukin-6-inducible STAT3 activation
    • Bhutani, M. et al. 2007. Capsaicin is a novel blocker of constitutive and interleukin-6-inducible STAT3 activation. Clin. Cancer Res. 13 : 3024 3032.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 3024-3032
    • Bhutani, M.1
  • 70
    • 34249337388 scopus 로고    scopus 로고
    • The novel triterpenoid C-28 methyl ester of 2-cyano-3, 12-dioxoolen-1, 9-dien-28-oic acid inhibits metastatic murine breast tumor growth through inactivation of STAT3 signaling
    • Ling, X. et al. 2007. The novel triterpenoid C-28 methyl ester of 2-cyano-3, 12-dioxoolen-1, 9-dien-28-oic acid inhibits metastatic murine breast tumor growth through inactivation of STAT3 signaling. Cancer Res. 67 : 4210 4218.
    • (2007) Cancer Res. , vol.67 , pp. 4210-4218
    • Ling, X.1
  • 71
    • 33847633373 scopus 로고    scopus 로고
    • Chalcone inhibits the activation of NF-kappaB and STAT3 in endothelial cells via endogenous electrophile
    • Liu, Y.C. et al. 2007. Chalcone inhibits the activation of NF-kappaB and STAT3 in endothelial cells via endogenous electrophile. Life Sci. 80 : 1420 1430.
    • (2007) Life Sci. , vol.80 , pp. 1420-1430
    • Liu, Y.C.1
  • 72
    • 44949105638 scopus 로고    scopus 로고
    • Cucurbitacin I inhibits Stat3 and induces apoptosis in Sezary cells
    • van Kester, M.S. et al. 2008. Cucurbitacin I inhibits Stat3 and induces apoptosis in Sezary cells. J. Invest. Dermatol. 128 : 1691 1695.
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 1691-1695
    • Van Kester, M.S.1
  • 73
    • 0141955061 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) inhibits constitutive and IL-6-inducible STAT3 phosphorylation in human multiple myeloma cells
    • Bharti, A.C., N. Donato B.B. Aggarwal. 2003. Curcumin (diferuloylmethane) inhibits constitutive and IL-6-inducible STAT3 phosphorylation in human multiple myeloma cells. J. Immunol. 171 : 3863 3871.
    • (2003) J. Immunol. , vol.171 , pp. 3863-3871
    • Bharti, A.C.1    Donato, N.2    Aggarwal, B.B.3
  • 74
    • 33847396951 scopus 로고    scopus 로고
    • Small molecule inhibitors of Stat3 signaling pathway
    • Deng, J., F. Grande N. Neamati. 2007. Small molecule inhibitors of Stat3 signaling pathway. Curr. Cancer Drug Targets 7 : 91 107.
    • (2007) Curr. Cancer Drug Targets , vol.7 , pp. 91-107
    • Deng, J.1    Grande, F.2    Neamati, N.3
  • 75
    • 46749148503 scopus 로고    scopus 로고
    • EGCG inhibits activation of the insulin-like growth factor (IGF)/IGF-1 receptor axis in human hepatocellular carcinoma cells
    • Shimizu, M. et al. 2007. EGCG inhibits activation of the insulin-like growth factor (IGF)/IGF-1 receptor axis in human hepatocellular carcinoma cells. Cancer Lett. 206 : 10 18.
    • (2007) Cancer Lett. , vol.206 , pp. 10-18
    • Shimizu, M.1
  • 76
    • 34147152865 scopus 로고    scopus 로고
    • Emodin has a cytotoxic activity against human multiple myeloma as a Janus-activated kinase 2 inhibitor
    • Muto, A. et al. 2007. Emodin has a cytotoxic activity against human multiple myeloma as a Janus-activated kinase 2 inhibitor. Mol. Cancer Ther. 6 : 987 994.
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 987-994
    • Muto, A.1
  • 77
    • 37549068947 scopus 로고    scopus 로고
    • The functional role of an interleukin 6-inducible CDK9.STAT3 complex in human gamma-fibrinogen gene expression
    • Hou, T., S. Ray A.R. Brasier. 2007. The functional role of an interleukin 6-inducible CDK9.STAT3 complex in human gamma-fibrinogen gene expression. J. Biol. Chem. 282 : 37091 37102.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37091-37102
    • Hou, T.1    Ray, S.2    Brasier, A.R.3
  • 78
    • 0034721813 scopus 로고    scopus 로고
    • Inhibition of interleukin-6 signaling by galiellalactone
    • Weidler, M. et al. 2000. Inhibition of interleukin-6 signaling by galiellalactone. FEBS Lett. 484 : 1 6.
    • (2000) FEBS Lett. , vol.484 , pp. 1-6
    • Weidler, M.1
  • 79
    • 33845742037 scopus 로고    scopus 로고
    • Inhibition of leiomyoma cell proliferation in vitro by genistein and the protein tyrosine kinase inhibitor TKS050
    • Shushan, A. et al. 2007. Inhibition of leiomyoma cell proliferation in vitro by genistein and the protein tyrosine kinase inhibitor TKS050. Fertil. Steril. 87 : 127 135.
    • (2007) Fertil. Steril. , vol.87 , pp. 127-135
    • Shushan, A.1
  • 80
    • 49249128130 scopus 로고    scopus 로고
    • Guggulsterone, a farnesoid X receptor antagonist, inhibits constitutive and inducible STAT3 activation through induction of a protein tyrosine phosphatase SHP-1
    • Ahn, K.S. et al. 2008. Guggulsterone, a farnesoid X receptor antagonist, inhibits constitutive and inducible STAT3 activation through induction of a protein tyrosine phosphatase SHP-1. Cancer Res. 68 : 4406 4415.
    • (2008) Cancer Res. , vol.68 , pp. 4406-4415
    • Ahn, K.S.1
  • 81
    • 20944435625 scopus 로고    scopus 로고
    • Indirubin derivatives inhibit Stat3 signaling and induce apoptosis in human cancer cells
    • Nam, S. et al. 2005. Indirubin derivatives inhibit Stat3 signaling and induce apoptosis in human cancer cells. Proc. Natl. Acad. Sci. USA 102 : 5998 6003.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5998-6003
    • Nam, S.1
  • 82
    • 33745054187 scopus 로고    scopus 로고
    • Herbal remedy magnolol suppresses IL-6-induced STAT3 activation and gene expression in endothelial cells
    • Chen, S.C. et al. 2006. Herbal remedy magnolol suppresses IL-6-induced STAT3 activation and gene expression in endothelial cells. Br. J. Pharmacol. 148 : 226 232.
    • (2006) Br. J. Pharmacol. , vol.148 , pp. 226-232
    • Chen, S.C.1
  • 83
    • 0034614643 scopus 로고    scopus 로고
    • Parthenolide inhibits activation of signal transducers and activators of transcription (STATs) induced by cytokines of the IL-6 family
    • Sobota, R. et al. 2000. Parthenolide inhibits activation of signal transducers and activators of transcription (STATs) induced by cytokines of the IL-6 family. Biochem. Biophys. Res. Commun. 267 : 329 333.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 329-333
    • Sobota, R.1
  • 84
    • 0034725025 scopus 로고    scopus 로고
    • Distinct mechanisms of STAT phosphorylation via the interferon-alpha/beta receptor. Selective inhibition of STAT3 and STAT5 by piceatannol
    • Su, L. M. David. 2000. Distinct mechanisms of STAT phosphorylation via the interferon-alpha/beta receptor. Selective inhibition of STAT3 and STAT5 by piceatannol. J. Biol. Chem. 275 : 12661 12666.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12661-12666
    • Su, L.1    David, M.2
  • 85
    • 33947197883 scopus 로고    scopus 로고
    • Resveratrol inhibits proliferation, induces apoptosis, and overcomes chemoresistance through down-regulation of STAT3 and nuclear factor-kappaB-regulated antiapoptotic and cell survival gene products in human multiple myeloma cells
    • Bhardwaj, A. et al. 2007. Resveratrol inhibits proliferation, induces apoptosis, and overcomes chemoresistance through down-regulation of STAT3 and nuclear factor-kappaB-regulated antiapoptotic and cell survival gene products in human multiple myeloma cells. Blood 109 : 2293 2302.
    • (2007) Blood , vol.109 , pp. 2293-2302
    • Bhardwaj, A.1
  • 86
    • 34547829030 scopus 로고    scopus 로고
    • Silibinin inhibits constitutive activation of Stat3, and causes caspase activation and apoptotic death of human prostate carcinoma DU145 cells
    • Agarwal, C. et al. 2007. Silibinin inhibits constitutive activation of Stat3, and causes caspase activation and apoptotic death of human prostate carcinoma DU145 cells. Carcinogenesis 28 : 1463 1470.
    • (2007) Carcinogenesis , vol.28 , pp. 1463-1470
    • Agarwal, C.1
  • 87
    • 34548693457 scopus 로고    scopus 로고
    • Ursolic acid inhibits STAT3 activation pathway leading to suppression of proliferation and chemosensitization of human multiple myeloma cells
    • Pathak, A.K. et al. 2007. Ursolic acid inhibits STAT3 activation pathway leading to suppression of proliferation and chemosensitization of human multiple myeloma cells. Mol Cancer Res. 5 : 943 955.
    • (2007) Mol Cancer Res. , vol.5 , pp. 943-955
    • Pathak, A.K.1
  • 88
    • 4444223238 scopus 로고    scopus 로고
    • Phosphorylation of extracellular signal-regulated kinase 1 and 2, protein kinase B, and signal transducer and activator of transcription 3 are differently inhibited by an epidermal growth factor receptor inhibitor, EKB-569, in tumor cells and normal human keratinocytes
    • Nunes, M., C. Shi L.M. Greenberger. 2004. Phosphorylation of extracellular signal-regulated kinase 1 and 2, protein kinase B, and signal transducer and activator of transcription 3 are differently inhibited by an epidermal growth factor receptor inhibitor, EKB-569, in tumor cells and normal human keratinocytes. Mol. Cancer Ther. 3 : 21 27.
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 21-27
    • Nunes, M.1    Shi, C.2    Greenberger, L.M.3
  • 89
    • 1642539961 scopus 로고    scopus 로고
    • Retinoic acid inhibits leukemia inhibitory factor signaling pathways in mouse embryonic stem cells
    • Tighe, A.P. L.J. Gudas. 2004. Retinoic acid inhibits leukemia inhibitory factor signaling pathways in mouse embryonic stem cells. J. Cell Physiol. 198 : 223 229.
    • (2004) J. Cell Physiol. , vol.198 , pp. 223-229
    • Tighe, A.P.1    Gudas, L.J.2
  • 90
    • 0035393595 scopus 로고    scopus 로고
    • Rituximab inactivates signal transducer and activation of transcription 3 (STAT3) activity in B-non-Hodgkin's lymphoma through inhibition of the interleukin 10 autocrine/paracrine loop and results in down-regulation of Bcl-2 and sensitization to cytotoxic drugs
    • Alas, S. B. Bonavida. 2001. Rituximab inactivates signal transducer and activation of transcription 3 (STAT3) activity in B-non-Hodgkin's lymphoma through inhibition of the interleukin 10 autocrine/paracrine loop and results in down-regulation of Bcl-2 and sensitization to cytotoxic drugs. Cancer Res. 61 : 5137 5144.
    • (2001) Cancer Res. , vol.61 , pp. 5137-5144
    • Alas, S.1    Bonavida, B.2
  • 91
    • 16344380754 scopus 로고    scopus 로고
    • A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells
    • Song, H. et al. 2005. A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells. Proc. Natl. Acad. Sci. USA 102 : 4700 4705.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4700-4705
    • Song, H.1
  • 92
    • 0031443156 scopus 로고    scopus 로고
    • Constitutive activation of Stat3 in fibroblasts transformed by diverse oncoproteins and in breast carcinoma cells
    • Garcia, R. et al. 1997. Constitutive activation of Stat3 in fibroblasts transformed by diverse oncoproteins and in breast carcinoma cells. Cell Growth Differ. 8 : 1267 1276.
    • (1997) Cell Growth Differ. , vol.8 , pp. 1267-1276
    • Garcia, R.1
  • 93
    • 0028296179 scopus 로고
    • Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130
    • Lutticken, C. et al. 1994. Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130. Science 263 : 89 92.
    • (1994) Science , vol.263 , pp. 89-92
    • Lutticken, C.1
  • 94
    • 0029856943 scopus 로고    scopus 로고
    • Multiple signaling pathways induced by granulocyte colony-stimulating factor involving activation of JAKs, STAT5, and/or STAT3 are required for regulation of three distinct classes of immediate early genes
    • Tian, S.S. et al. 1996. Multiple signaling pathways induced by granulocyte colony-stimulating factor involving activation of JAKs, STAT5, and/or STAT3 are required for regulation of three distinct classes of immediate early genes. Blood 88 : 4435 4444.
    • (1996) Blood , vol.88 , pp. 4435-4444
    • Tian, S.S.1
  • 95
    • 0029005549 scopus 로고
    • Constitutively activated Jak-STAT pathway in T cells transformed with HTLV-I
    • Migone, T.S. et al. 1995. Constitutively activated Jak-STAT pathway in T cells transformed with HTLV-I. Science 269 : 79 81.
    • (1995) Science , vol.269 , pp. 79-81
    • Migone, T.S.1
  • 96
    • 0029804456 scopus 로고    scopus 로고
    • BFGF and LIF signaling activates STAT3 in proliferating myoblasts
    • Megeney, L.A. et al. 1996. bFGF and LIF signaling activates STAT3 in proliferating myoblasts. Dev. Genet. 19 : 139 145.
    • (1996) Dev. Genet. , vol.19 , pp. 139-145
    • Megeney, L.A.1
  • 97
    • 0033588229 scopus 로고    scopus 로고
    • Protein kinase C delta associates with and phosphorylates Stat3 in an interleukin-6-dependent manner
    • Jain, N. et al. 1999. Protein kinase C delta associates with and phosphorylates Stat3 in an interleukin-6-dependent manner. J. Biol. Chem. 274 : 24392 24400.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24392-24400
    • Jain, N.1
  • 98
    • 2342483179 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 phosphorylates signal transducer and activator of transcription 3 and regulates its transcriptional activity
    • Fu, A.K. et al. 2004. Cyclin-dependent kinase 5 phosphorylates signal transducer and activator of transcription 3 and regulates its transcriptional activity. Proc. Natl. Acad. Sci. USA 101 : 6728 6733.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6728-6733
    • Fu, A.K.1
  • 99
    • 34548787911 scopus 로고    scopus 로고
    • Protein kinase Cepsilon interacts with signal transducers and activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and regulates its constitutive activation in prostate cancer
    • Aziz, M.H. et al. 2007. Protein kinase Cepsilon interacts with signal transducers and activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and regulates its constitutive activation in prostate cancer. Cancer Res. 67 : 8828 8838.
    • (2007) Cancer Res. , vol.67 , pp. 8828-8838
    • Aziz, M.H.1
  • 100
    • 0030744123 scopus 로고    scopus 로고
    • Mapping of Stat3 serine phosphorylation to a single residue (727) and evidence that serine phosphorylation has no influence on DNA binding of Stat1 and Stat3
    • Wen, Z. J.E. Darnell, Jr. 1997. Mapping of Stat3 serine phosphorylation to a single residue (727) and evidence that serine phosphorylation has no influence on DNA binding of Stat1 and Stat3. Nucleic Acids Res. 25 : 2062 2067.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2062-2067
    • Wen, Z.1    Darnell Jr., J.E.2
  • 101
    • 0033968596 scopus 로고    scopus 로고
    • Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR
    • Yokogami, K. et al. 2000. Serine phosphorylation and maximal activation of STAT3 during CNTF signaling is mediated by the rapamycin target mTOR. Curr. Biol. 10 : 47 50.
    • (2000) Curr. Biol. , vol.10 , pp. 47-50
    • Yokogami, K.1
  • 102
    • 0037160057 scopus 로고    scopus 로고
    • Activation of STAT3 by the Src family kinase Hck requires a functional SH3 domain
    • Schreiner, S.J., A.P. Schiavone T.E. Smithgall. 2002. Activation of STAT3 by the Src family kinase Hck requires a functional SH3 domain. J. Biol. Chem. 277 : 45680 45687.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45680-45687
    • Schreiner, S.J.1    Schiavone, A.P.2    Smithgall, T.E.3
  • 103
    • 0000506439 scopus 로고    scopus 로고
    • P210 and P190(BCR/ABL) induce the tyrosine phosphorylation and DNA binding activity of multiple specific STAT family members
    • Ilaria, R.L., Jr. & R.A. Van Etten. 1996. P210 and P190(BCR/ABL) induce the tyrosine phosphorylation and DNA binding activity of multiple specific STAT family members. J. Biol. Chem. 271 : 31704 31710.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31704-31710
    • Ilaria Jr., R.L.1    Van Etten, R.A.2
  • 104
    • 0030917141 scopus 로고    scopus 로고
    • Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells
    • Hanissian, S.H. R.S. Geha. 1997. Jak3 is associated with CD40 and is critical for CD40 induction of gene expression in B cells. Immunity 6 : 379 387.
    • (1997) Immunity , vol.6 , pp. 379-387
    • Hanissian, S.H.1    Geha, R.S.2
  • 105
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung, C.D. et al. 1997. Specific inhibition of Stat3 signal transduction by PIAS3. Science 278 : 1803 1805.
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1
  • 106
    • 0032549676 scopus 로고    scopus 로고
    • Activation of STAT3 by the c-Fes protein-tyrosine kinase
    • Nelson, K.L. et al. 1998. Activation of STAT3 by the c-Fes protein-tyrosine kinase. J. Biol. Chem. 273 : 7072 7077.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7072-7077
    • Nelson, K.L.1
  • 107
    • 0032479519 scopus 로고    scopus 로고
    • C-Fes tyrosine kinase binds to and activates STAT3 after granulocyte-macrophage colony-stimulating factor stimulation
    • Park, W.Y. et al. 1998. c-Fes tyrosine kinase binds to and activates STAT3 after granulocyte-macrophage colony-stimulating factor stimulation. Cancer Lett. 129 : 29 37.
    • (1998) Cancer Lett. , vol.129 , pp. 29-37
    • Park, W.Y.1
  • 108
    • 33748484690 scopus 로고    scopus 로고
    • Monocyte 15-lipoxygenase expression is regulated by a novel cytosolic signaling complex with protein kinase C delta and tyrosine-phosphorylated Stat3
    • Bhattacharjee, A. et al. 2006. Monocyte 15-lipoxygenase expression is regulated by a novel cytosolic signaling complex with protein kinase C delta and tyrosine-phosphorylated Stat3. J. Immunol. 177 : 3771 3781.
    • (2006) J. Immunol. , vol.177 , pp. 3771-3781
    • Bhattacharjee, A.1
  • 109
    • 0037147299 scopus 로고    scopus 로고
    • Protein kinase C delta associates with the interleukin-6 receptor subunit glycoprotein (gp) 130 via Stat3 and enhances Stat3-gp130 interaction
    • Novotny-Diermayr, V. et al. 2002. Protein kinase C delta associates with the interleukin-6 receptor subunit glycoprotein (gp) 130 via Stat3 and enhances Stat3-gp130 interaction. J. Biol. Chem. 277 : 49134 49142.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49134-49142
    • Novotny-Diermayr, V.1
  • 110
    • 0034666009 scopus 로고    scopus 로고
    • FER kinase activation of Stat3 is determined by the N-terminal sequence
    • Priel-Halachmi, S. et al. 2000. FER kinase activation of Stat3 is determined by the N-terminal sequence. J. Biol. Chem. 275 : 28902 28910.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28902-28910
    • Priel-Halachmi, S.1
  • 111
    • 10944228420 scopus 로고    scopus 로고
    • IRAK1 serves as a novel regulator essential for lipopolysaccharide- induced interleukin-10 gene expression
    • Huang, Y. et al. 2004. IRAK1 serves as a novel regulator essential for lipopolysaccharide-induced interleukin-10 gene expression. J. Biol. Chem. 279 : 51697 51703.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51697-51703
    • Huang, Y.1
  • 112
    • 6044254767 scopus 로고    scopus 로고
    • Implication of BRG1 and cdk9 in the STAT3-mediated activation of the p21waf1 gene
    • Giraud, S. et al. 2004. Implication of BRG1 and cdk9 in the STAT3-mediated activation of the p21waf1 gene. Oncogene 23 : 7391 7398.
    • (2004) Oncogene , vol.23 , pp. 7391-7398
    • Giraud, S.1
  • 113
    • 28744459372 scopus 로고    scopus 로고
    • Physical and functional interactions between STAT3 and ZIP kinase
    • Sato, N. et al. 2005. Physical and functional interactions between STAT3 and ZIP kinase. Int. Immunol. 17 : 1543 1552.
    • (2005) Int. Immunol. , vol.17 , pp. 1543-1552
    • Sato, N.1
  • 114
    • 20144376594 scopus 로고    scopus 로고
    • STAT3 regulates Nemo-like kinase by mediating its interaction with IL-6-stimulated TGFbeta-activated kinase 1 for STAT3 Ser-727 phosphorylation
    • Kojima, H. et al. 2005. STAT3 regulates Nemo-like kinase by mediating its interaction with IL-6-stimulated TGFbeta-activated kinase 1 for STAT3 Ser-727 phosphorylation. Proc. Natl. Acad. Sci. USA 102 : 4524 4529.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4524-4529
    • Kojima, H.1
  • 115
    • 33846425303 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase prevents activation of the anti-apoptotic transcription factor STAT3 and promotes apoptosis in neoplastic B-cells and B-cell precursors exposed to oxidative stress
    • Uckun, F., Z. Ozer A. Vassilev. 2007. Bruton's tyrosine kinase prevents activation of the anti-apoptotic transcription factor STAT3 and promotes apoptosis in neoplastic B-cells and B-cell precursors exposed to oxidative stress. Br. J. Haematol. 136 : 574 589.
    • (2007) Br. J. Haematol. , vol.136 , pp. 574-589
    • Uckun, F.1    Ozer, Z.2    Vassilev, A.3
  • 116
    • 36849062265 scopus 로고    scopus 로고
    • Pin1 is required for the Ser727 phosphorylation-dependent Stat3 activity
    • Lufei, C. et al. 2007. Pin1 is required for the Ser727 phosphorylation-dependent Stat3 activity. Oncogene 26 : 7656 7664.
    • (2007) Oncogene , vol.26 , pp. 7656-7664
    • Lufei, C.1
  • 117
    • 0031888837 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 2 (SHP-2) moderates signaling by gp130 but is not required for the induction of acute-phase plasma protein genes in hepatic cells
    • Kim, H. et al. 1998. Protein tyrosine phosphatase 2 (SHP-2) moderates signaling by gp130 but is not required for the induction of acute-phase plasma protein genes in hepatic cells. Mol. Cell Biol. 18 : 1525 1533.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 1525-1533
    • Kim, H.1
  • 118
    • 0032549520 scopus 로고    scopus 로고
    • The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling
    • Chiarugi, P. et al. 1998. The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling. J. Biol. Chem. 273 : 6776 6785.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6776-6785
    • Chiarugi, P.1
  • 119
    • 0033538452 scopus 로고    scopus 로고
    • Regulation of angiotensin II-induced phosphorylation of STAT3 in vascular smooth muscle cells
    • Liang, H. et al. 1999. Regulation of angiotensin II-induced phosphorylation of STAT3 in vascular smooth muscle cells. J. Biol. Chem. 274 : 19846 19851.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19846-19851
    • Liang, H.1
  • 120
    • 13044259628 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase 2A induces serine/threonine phosphorylation, subcellular redistribution, and functional inhibition of STAT3
    • Woetmann, A. et al. 1999. Inhibition of protein phosphatase 2A induces serine/threonine phosphorylation, subcellular redistribution, and functional inhibition of STAT3. Proc. Natl. Acad. Sci. USA 96 : 10620 10625.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10620-10625
    • Woetmann, A.1
  • 121
    • 0034731509 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase D1, a potential regulator and effector for Tec family kinases
    • Jui, H.Y. et al. 2000. Protein-tyrosine phosphatase D1, a potential regulator and effector for Tec family kinases. J. Biol. Chem. 275 : 41124 41132.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41124-41132
    • Jui, H.Y.1
  • 122
    • 0035892127 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase epsilonC selectively inhibits interleukin-6- and interleukin- 10-induced JAK-STAT signaling
    • Tanuma, N. et al. 2001. Protein tyrosine phosphatase epsilonC selectively inhibits interleukin-6- and interleukin- 10-induced JAK-STAT signaling. Blood 98 : 3030 3034.
    • (2001) Blood , vol.98 , pp. 3030-3034
    • Tanuma, N.1
  • 123
    • 0035905767 scopus 로고    scopus 로고
    • CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling
    • Irie-Sasaki, J. et al. 2001. CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling. Nature 409 : 349 354.
    • (2001) Nature , vol.409 , pp. 349-354
    • Irie-Sasaki, J.1
  • 124
    • 0036298183 scopus 로고    scopus 로고
    • PTEN is a negative regulator of STAT3 activation in human papillomavirus-infected cells
    • Sun, S. B.M. Steinberg. 2002. PTEN is a negative regulator of STAT3 activation in human papillomavirus-infected cells. J. Gen. Virol. 83 : 1651 1658.
    • (2002) J. Gen. Virol. , vol.83 , pp. 1651-1658
    • Sun, S.1    Steinberg, B.M.2
  • 125
    • 36048963331 scopus 로고    scopus 로고
    • Activation of the PTEN/mTOR/STAT3 pathway in breast cancer stem-like cells is required for viability and maintenance
    • Zhou, J. et al. 2007. Activation of the PTEN/mTOR/STAT3 pathway in breast cancer stem-like cells is required for viability and maintenance. Proc. Natl. Acad. Sci. USA 104 : 16158 16163.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16158-16163
    • Zhou, J.1
  • 126
    • 0036228770 scopus 로고    scopus 로고
    • Attenuation of leptin action and regulation of obesity by protein tyrosine phosphatase 1B
    • Cheng, A. et al. 2002. Attenuation of leptin action and regulation of obesity by protein tyrosine phosphatase 1B. Dev. Cell. 2 : 497 503.
    • (2002) Dev. Cell. , vol.2 , pp. 497-503
    • Cheng, A.1
  • 127
    • 0036033161 scopus 로고    scopus 로고
    • The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation
    • Yamamoto, T. et al. 2002. The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation. Biochem. Biophys. Res. Commun. 297 : 811 817.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 811-817
    • Yamamoto, T.1
  • 128
    • 29644441336 scopus 로고    scopus 로고
    • Modulation of TLR4 signaling by a novel adaptor protein signal-transducing adaptor protein-2 in macrophages
    • Sekine, Y. et al. 2006. Modulation of TLR4 signaling by a novel adaptor protein signal-transducing adaptor protein-2 in macrophages. J. Immunol. 176 : 380 389.
    • (2006) J. Immunol. , vol.176 , pp. 380-389
    • Sekine, Y.1
  • 129
    • 34247189533 scopus 로고    scopus 로고
    • Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T
    • Zhang, X. et al. 2007. Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T. Proc. Natl. Acad. Sci. USA 104 : 4060 4064.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4060-4064
    • Zhang, X.1
  • 130
    • 0037112933 scopus 로고    scopus 로고
    • A novel nuclear zinc finger protein EZI enhances nuclear retention and transactivation of STAT3
    • Nakayama, K., K.W. Kim A. Miyajima. 2002. A novel nuclear zinc finger protein EZI enhances nuclear retention and transactivation of STAT3. EMBO J. 21 : 6174 6184.
    • (2002) EMBO J. , vol.21 , pp. 6174-6184
    • Nakayama, K.1    Kim, K.W.2    Miyajima, A.3
  • 131
    • 0037589016 scopus 로고    scopus 로고
    • Kaposi sarcoma-associated viral cyclin K overrides cell growth inhibition mediated by oncostatin M through STAT3 inhibition
    • Lundquist, A. et al. 2003. Kaposi sarcoma-associated viral cyclin K overrides cell growth inhibition mediated by oncostatin M through STAT3 inhibition. Blood 101 : 4070 4077.
    • (2003) Blood , vol.101 , pp. 4070-4077
    • Lundquist, A.1
  • 132
    • 2642581525 scopus 로고    scopus 로고
    • Activation of Stat3 transcription factor by Herpesvirus saimiri STP-A oncoprotein
    • Chung, Y.H. et al. 2004. Activation of Stat3 transcription factor by Herpesvirus saimiri STP-A oncoprotein. J. Virol. 78 : 6489 6497.
    • (2004) J. Virol. , vol.78 , pp. 6489-6497
    • Chung, Y.H.1
  • 133
    • 33645530423 scopus 로고    scopus 로고
    • Physical and functional interactions between Daxx and STAT3
    • Muromoto, R. et al. 2006. Physical and functional interactions between Daxx and STAT3. Oncogene 25 : 2131 21316.
    • (2006) Oncogene , vol.25 , pp. 2131-21316
    • Muromoto, R.1
  • 134
    • 0029075875 scopus 로고
    • Cooperative transcriptional activity of Jun and Stat3 beta, a short form of Stat3
    • Schaefer, T.S., L.K. Sanders D. Nathans. 1995. Cooperative transcriptional activity of Jun and Stat3 beta, a short form of Stat3. Proc. Natl. Acad. Sci. USA 92 : 9097 9101.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9097-9101
    • Schaefer, T.S.1    Sanders, L.K.2    Nathans, D.3
  • 135
    • 0029872610 scopus 로고    scopus 로고
    • Direct association of STAT3 with the IFNAR-1 chain of the human type I interferon receptor
    • Yang, C.H. et al. 1996. Direct association of STAT3 with the IFNAR-1 chain of the human type I interferon receptor. J. Biol. Chem. 271 : 8057 8061.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8057-8061
    • Yang, C.H.1
  • 136
    • 0030792590 scopus 로고    scopus 로고
    • A family of cytokine-inducible inhibitors of signalling
    • Starr, R. et al. 1997. A family of cytokine-inducible inhibitors of signalling. Nature 387 : 917 921.
    • (1997) Nature , vol.387 , pp. 917-921
    • Starr, R.1
  • 137
    • 0030667790 scopus 로고    scopus 로고
    • STAT3 acts as a co-activator of glucocorticoid receptor signaling
    • Zhang, Z. et al. 1997. STAT3 acts as a co-activator of glucocorticoid receptor signaling. J. Biol. Chem. 272 : 30607 30610.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30607-30610
    • Zhang, Z.1
  • 138
    • 0030755934 scopus 로고    scopus 로고
    • Structure and function of a new STAT-induced STAT inhibitor
    • Naka, T. et al. 1997. Structure and function of a new STAT-induced STAT inhibitor. Nature 387 : 924 929.
    • (1997) Nature , vol.387 , pp. 924-929
    • Naka, T.1
  • 139
    • 0031559593 scopus 로고    scopus 로고
    • The competitive binding of STAT3 and NF-kappaB on an overlapping DNA binding site
    • Zhang, Z. G.M. Fuller. 1997. The competitive binding of STAT3 and NF-kappaB on an overlapping DNA binding site. Biochem. Biophys. Res. Commun. 237 : 90 94.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 90-94
    • Zhang, Z.1    Fuller, G.M.2
  • 140
    • 0036797750 scopus 로고    scopus 로고
    • Signal transducers and activators of transcription 3 (STAT3) inhibits transcription of the inducible nitric oxide synthase gene by interacting with nuclear factor kappaB
    • Yu, Z., W. Zhang B.C. Kone. 2002. Signal transducers and activators of transcription 3 (STAT3) inhibits transcription of the inducible nitric oxide synthase gene by interacting with nuclear factor kappaB. Biochem. J. 367 : 97 105.
    • (2002) Biochem. J. , vol.367 , pp. 97-105
    • Yu, Z.1    Zhang, W.2    Kone, B.C.3
  • 141
    • 0345826123 scopus 로고    scopus 로고
    • Interleukin 1 activates STAT3/nuclear factor-kappaB cross-talk via a unique TRAF6- and p65-dependent mechanism
    • Yoshida, Y. et al. 2004. Interleukin 1 activates STAT3/nuclear factor-kappaB cross-talk via a unique TRAF6- and p65-dependent mechanism. J. Biol. Chem. 279 : 1768 1776.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1768-1776
    • Yoshida, Y.1
  • 142
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan, Z.L. et al. 2005. Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 307 : 269 273.
    • (2005) Science , vol.307 , pp. 269-273
    • Yuan, Z.L.1
  • 143
    • 0033574767 scopus 로고    scopus 로고
    • Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300
    • Nakashima, K. et al. 1999. Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300. Science 284 : 479 482.
    • (1999) Science , vol.284 , pp. 479-482
    • Nakashima, K.1
  • 144
    • 0033520422 scopus 로고    scopus 로고
    • Stat protein transactivation domains recruit p300/CBP through widely divergent sequences
    • Paulson, M. et al. 1999. Stat protein transactivation domains recruit p300/CBP through widely divergent sequences. J. Biol. Chem. 274 : 25343 25349.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25343-25349
    • Paulson, M.1
  • 145
    • 15744385061 scopus 로고    scopus 로고
    • Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation
    • Wang, R., P. Cherukuri J. Luo. 2005. Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation. J. Biol. Chem. 280 : 11528 11534.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11528-11534
    • Wang, R.1    Cherukuri, P.2    Luo, J.3
  • 146
    • 0034730176 scopus 로고    scopus 로고
    • A Stat3-interacting protein (StIP1) regulates cytokine signal transduction
    • Collum, R.G. et al. 2000. A Stat3-interacting protein (StIP1) regulates cytokine signal transduction. Proc. Natl. Acad. Sci. USA 97 : 10120 10125.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10120-10125
    • Collum, R.G.1
  • 147
    • 20444423286 scopus 로고    scopus 로고
    • Nuclear interaction of EGFR and STAT3 in the activation of the iNOS/NO pathway
    • Lo, H.W. et al. 2005. Nuclear interaction of EGFR and STAT3 in the activation of the iNOS/NO pathway. Cancer Cell. 7 : 575 589.
    • (2005) Cancer Cell. , vol.7 , pp. 575-589
    • Lo, H.W.1
  • 148
    • 0033988288 scopus 로고    scopus 로고
    • Association of STAT1, STAT3 and STAT5 proteins with the IL-2 receptor involves different subdomains of the IL-2 receptor beta chain
    • Delespine-Carmagnat, M., G. Bouvier J. Bertoglio. 2000. Association of STAT1, STAT3 and STAT5 proteins with the IL-2 receptor involves different subdomains of the IL-2 receptor beta chain. Eur. J. Immunol. 30 : 59 68.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 59-68
    • Delespine-Carmagnat, M.1    Bouvier, G.2    Bertoglio, J.3
  • 149
    • 0034705540 scopus 로고    scopus 로고
    • Functional interaction of STAT3 transcription factor with the cell cycle inhibitor p21WAF1/CIP1/SDI1
    • Coqueret, O. H. Gascan. 2000. Functional interaction of STAT3 transcription factor with the cell cycle inhibitor p21WAF1/CIP1/SDI1. J. Biol. Chem. 275 : 18794 18800.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18794-18800
    • Coqueret, O.1    Gascan, H.2
  • 150
    • 0035907245 scopus 로고    scopus 로고
    • Cyclin D1 represses STAT3 activation through a Cdk4-independent mechanism
    • Bienvenu, F., H. Gascan O. Coqueret. 2001. Cyclin D1 represses STAT3 activation through a Cdk4-independent mechanism. J. Biol. Chem. 276 : 16840 16847.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16840-16847
    • Bienvenu, F.1    Gascan, H.2    Coqueret, O.3
  • 151
    • 0037040924 scopus 로고    scopus 로고
    • Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a
    • Giraud, S. et al. 2002. Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a. J. Biol. Chem. 277 : 8004 8011.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8004-8011
    • Giraud, S.1
  • 152
    • 7644236907 scopus 로고    scopus 로고
    • Region 752-761 of STAT3 is critical for SRC-1 recruitment and Ser727 phosphorylation
    • Zhao, H. et al. 2004. Region 752-761 of STAT3 is critical for SRC-1 recruitment and Ser727 phosphorylation. Biochem. Biophys. Res. Commun. 325 : 541 548.
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 541-548
    • Zhao, H.1
  • 153
    • 0348147580 scopus 로고    scopus 로고
    • Grb2 regulates Stat3 activation negatively in epidermal growth factor signalling
    • Zhang, T., J. Ma X. Cao. 2003. Grb2 regulates Stat3 activation negatively in epidermal growth factor signalling. Biochem. J. 376 : 457 464.
    • (2003) Biochem. J. , vol.376 , pp. 457-464
    • Zhang, T.1    Ma, J.2    Cao, X.3
  • 154
    • 0034613161 scopus 로고    scopus 로고
    • Regulation of STAT3 by direct binding to the Rac1 GTPase
    • Simon, A.R. et al. 2000. Regulation of STAT3 by direct binding to the Rac1 GTPase. Science 290 : 144 147.
    • (2000) Science , vol.290 , pp. 144-147
    • Simon, A.R.1
  • 155
    • 0242582469 scopus 로고    scopus 로고
    • Reciprocal inhibition between MyoD and STAT3 in the regulation of growth and differentiation of myoblasts
    • Kataoka, Y. et al. 2003. Reciprocal inhibition between MyoD and STAT3 in the regulation of growth and differentiation of myoblasts. J. Biol. Chem. 278 : 44178 44187.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44178-44187
    • Kataoka, Y.1
  • 156
    • 0037866479 scopus 로고    scopus 로고
    • Opposing effects of PML and PML/RAR alpha on STAT3 activity
    • Kawasaki, A. et al. 2003. Opposing effects of PML and PML/RAR alpha on STAT3 activity. Blood 101 : 3668 3673.
    • (2003) Blood , vol.101 , pp. 3668-3673
    • Kawasaki, A.1
  • 157
    • 0037451235 scopus 로고    scopus 로고
    • GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction
    • Lufei, C. et al. 2003. GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 22 : 1325 1335.
    • (2003) EMBO J. , vol.22 , pp. 1325-1335
    • Lufei, C.1
  • 158
    • 3042823705 scopus 로고    scopus 로고
    • Interferon induces the interaction of prothymosin-alpha with STAT3 and results in the nuclear translocation of the complex
    • Yang, C.H. et al. 2004. Interferon induces the interaction of prothymosin-alpha with STAT3 and results in the nuclear translocation of the complex. Exp. Cell Res. 298 : 197 206.
    • (2004) Exp. Cell Res. , vol.298 , pp. 197-206
    • Yang, C.H.1
  • 159
    • 10744226417 scopus 로고    scopus 로고
    • Transcriptional inactivation of STAT3 by PPARgamma suppresses IL-6-responsive multiple myeloma cells
    • Wang, L.H. et al. 2004. Transcriptional inactivation of STAT3 by PPARgamma suppresses IL-6-responsive multiple myeloma cells. Immunity 20 : 205 218.
    • (2004) Immunity , vol.20 , pp. 205-218
    • Wang, L.H.1
  • 160
    • 16244393552 scopus 로고    scopus 로고
    • Growth hormone attenuates the transcriptional activity of Runx2 by facilitating its physical association with Stat3beta
    • Ziros, P.G. et al. 2004. Growth hormone attenuates the transcriptional activity of Runx2 by facilitating its physical association with Stat3beta. J. Bone Miner. Res. 19 : 1892 1904.
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 1892-1904
    • Ziros, P.G.1
  • 161
    • 21344444583 scopus 로고    scopus 로고
    • Proline-, glutamic acid-, and leucine-rich protein-1 is essential in growth factor regulation of signal transducers and activators of transcription 3 activation
    • Manavathi, B. et al. 2005. Proline-, glutamic acid-, and leucine-rich protein-1 is essential in growth factor regulation of signal transducers and activators of transcription 3 activation. Cancer Res. 65 : 5571 5577.
    • (2005) Cancer Res. , vol.65 , pp. 5571-5577
    • Manavathi, B.1
  • 162
    • 27944479710 scopus 로고    scopus 로고
    • Coordinated oncogenic transformation and inhibition of host immune responses by the PAX3-FKHR fusion oncoprotein
    • Nabarro, S. et al. 2005. Coordinated oncogenic transformation and inhibition of host immune responses by the PAX3-FKHR fusion oncoprotein. J. Exp. Med. 202 : 1399 1410.
    • (2005) J. Exp. Med. , vol.202 , pp. 1399-1410
    • Nabarro, S.1
  • 163
    • 23044503446 scopus 로고    scopus 로고
    • A Ras homologue member I directly inhibits signal transducers and activators of transcription 3 translocation and activity in human breast and ovarian cancer cells
    • Nishimoto, A. et al. 2005. A Ras homologue member I directly inhibits signal transducers and activators of transcription 3 translocation and activity in human breast and ovarian cancer cells. Cancer Res. 65 : 6701 6710.
    • (2005) Cancer Res. , vol.65 , pp. 6701-6710
    • Nishimoto, A.1
  • 164
    • 17844396959 scopus 로고    scopus 로고
    • Interleukin-6 induces transcriptional activation of vascular endothelial growth factor (VEGF) in astrocytes in vivo and regulates VEGF promoter activity in glioblastoma cells via direct interaction between STAT3 and Sp1
    • Loeffler, S. et al. 2005. Interleukin-6 induces transcriptional activation of vascular endothelial growth factor (VEGF) in astrocytes in vivo and regulates VEGF promoter activity in glioblastoma cells via direct interaction between STAT3 and Sp1. Int. J. Cancer 115 : 202 213.
    • (2005) Int. J. Cancer , vol.115 , pp. 202-213
    • Loeffler, S.1
  • 165
    • 23444449093 scopus 로고    scopus 로고
    • STAT3 is a potential modulator of HIF-1-mediated VEGF expression in human renal carcinoma cells
    • Jung, J.E. et al. 2005. STAT3 is a potential modulator of HIF-1-mediated VEGF expression in human renal carcinoma cells. FASEB J. 19 : 1296 1298.
    • (2005) FASEB J. , vol.19 , pp. 1296-1298
    • Jung, J.E.1
  • 166
    • 33646365075 scopus 로고    scopus 로고
    • Regulation of Stat3 nuclear import by importin alpha5 and importin alpha7 via two different functional sequence elements
    • Ma, J. X. Cao. 2006. Regulation of Stat3 nuclear import by importin alpha5 and importin alpha7 via two different functional sequence elements. Cell Signal. 18 : 1117 1126.
    • (2006) Cell Signal. , vol.18 , pp. 1117-1126
    • Ma, J.1    Cao, X.2
  • 167
    • 33644550632 scopus 로고    scopus 로고
    • Unique structural determinants for Stat3 recruitment and activation by the granulocyte colony-stimulating factor receptor at phosphotyrosine ligands 704 and 744
    • Shao, H. et al. 2006. Unique structural determinants for Stat3 recruitment and activation by the granulocyte colony-stimulating factor receptor at phosphotyrosine ligands 704 and 744. J. Immunol. 176 : 2933 2941.
    • (2006) J. Immunol. , vol.176 , pp. 2933-2941
    • Shao, H.1
  • 168
    • 33645296303 scopus 로고    scopus 로고
    • Suppression of STAT3 activity by Duplin, which is a negative regulator of the Wnt signal
    • Yamashina, K. et al. 2006. Suppression of STAT3 activity by Duplin, which is a negative regulator of the Wnt signal. J. Biochem. 139 : 305 314.
    • (2006) J. Biochem. , vol.139 , pp. 305-314
    • Yamashina, K.1
  • 169
    • 34249868449 scopus 로고    scopus 로고
    • Unphosphorylated STAT3 accumulates in response to IL-6 and activates transcription by binding to NFkappaB
    • Yang, J. et al. 2007. Unphosphorylated STAT3 accumulates in response to IL-6 and activates transcription by binding to NFkappaB. Genes Dev. 21 : 1396 1408.
    • (2007) Genes Dev. , vol.21 , pp. 1396-1408
    • Yang, J.1
  • 170
    • 44649197895 scopus 로고    scopus 로고
    • Nescient helix-loop-helix 2 interacts with signal transducer and activator of transcription 3 to regulate transcription of prohormone convertase 1/3
    • Fox, D.L. D.J. Good. 2008. Nescient helix-loop-helix 2 interacts with signal transducer and activator of transcription 3 to regulate transcription of prohormone convertase 1/3. Mol. Endocrinol. 22 : 1438 1448.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1438-1448
    • Fox, D.L.1    Good, D.J.2
  • 171
    • 43449110430 scopus 로고    scopus 로고
    • Physical and functional interactions between STAT3 and KAP1
    • Tsuruma, R. et al. 2008. Physical and functional interactions between STAT3 and KAP1. Oncogene 27 : 3054 3059.
    • (2008) Oncogene , vol.27 , pp. 3054-3059
    • Tsuruma, R.1
  • 172
    • 40049103757 scopus 로고    scopus 로고
    • BART is essential for nuclear retention of STAT3
    • Muromoto, R. et al. 2008. BART is essential for nuclear retention of STAT3. Int. Immunol. 20 : 395 403.
    • (2008) Int. Immunol. , vol.20 , pp. 395-403
    • Muromoto, R.1
  • 173
    • 0028931604 scopus 로고
    • Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors
    • Stahl, N. et al. 1995. Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors. Science 267 : 1349 1353.
    • (1995) Science , vol.267 , pp. 1349-1353
    • Stahl, N.1
  • 174
    • 0034655577 scopus 로고    scopus 로고
    • Induction of apoptosis by extracellular ubiquitin in human hematopoietic cells: Possible involvement of STAT3 degradation by proteasome pathway in interleukin 6-dependent hematopoietic cells
    • Daino, H. et al. 2000. Induction of apoptosis by extracellular ubiquitin in human hematopoietic cells: possible involvement of STAT3 degradation by proteasome pathway in interleukin 6-dependent hematopoietic cells. Blood 95 : 2577 2585.
    • (2000) Blood , vol.95 , pp. 2577-2585
    • Daino, H.1
  • 175
    • 13044263097 scopus 로고    scopus 로고
    • The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation
    • Zhang, J.G. et al. 1999. The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation. Proc. Natl. Acad. Sci. USA 96 : 2071 2076.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2071-2076
    • Zhang, J.G.1
  • 176
    • 34249660614 scopus 로고    scopus 로고
    • SOCS proteins, cytokine signalling and immune regulation
    • Yoshimura, A., T. Naka M. Kubo. 2007. SOCS proteins, cytokine signalling and immune regulation. Nat. Rev. Immunol. 7 : 454 465.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 454-465
    • Yoshimura, A.1    Naka, T.2    Kubo, M.3
  • 177
    • 45349102930 scopus 로고    scopus 로고
    • SOCS3 negatively regulates the gp130-STAT3 pathway in mouse skin wound healing
    • Zhu, B.M. et al. 2008. SOCS3 negatively regulates the gp130-STAT3 pathway in mouse skin wound healing. J. Invest. Dermatol. 128 : 1821 1829.
    • (2008) J. Invest. Dermatol. , vol.128 , pp. 1821-1829
    • Zhu, B.M.1
  • 178
    • 34547199420 scopus 로고    scopus 로고
    • Methylation of SOCS-3 and SOCS-1 in the carcinogenesis of Barrett's adenocarcinoma
    • Tischoff, I. et al. 2007. Methylation of SOCS-3 and SOCS-1 in the carcinogenesis of Barrett's adenocarcinoma. Gut 56 : 1047 1053.
    • (2007) Gut , vol.56 , pp. 1047-1053
    • Tischoff, I.1
  • 179
    • 27144433826 scopus 로고    scopus 로고
    • Methylation silencing of SOCS-3 promotes cell growth and migration by enhancing JAK/STAT and FAK signalings in human hepatocellular carcinoma
    • Niwa, Y. et al. 2005. Methylation silencing of SOCS-3 promotes cell growth and migration by enhancing JAK/STAT and FAK signalings in human hepatocellular carcinoma. Oncogene 24 : 6406 6417.
    • (2005) Oncogene , vol.24 , pp. 6406-6417
    • Niwa, Y.1
  • 180
    • 27144540201 scopus 로고    scopus 로고
    • SOCS-3 is frequently methylated in head and neck squamous cell carcinoma and its precursor lesions and causes growth inhibition
    • Weber, A. et al. 2005. SOCS-3 is frequently methylated in head and neck squamous cell carcinoma and its precursor lesions and causes growth inhibition.
    • (2005) Oncogene , vol.24 , pp. 6699-6708
    • Weber, A.1
  • 181
    • 0345492424 scopus 로고    scopus 로고
    • SOCS-3 is frequently silenced by hypermethylation and suppresses cell growth in human lung cancer
    • He, B. et al. 2003. SOCS-3 is frequently silenced by hypermethylation and suppresses cell growth in human lung cancer. Proc. Natl. Acad. Sci. USA 100 : 14133 14138.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14133-14138
    • He, B.1
  • 182
    • 49249095430 scopus 로고    scopus 로고
    • Inhibition of STAT3 Tyr705 phosphorylation by Smad4 suppresses transforming growth factor beta-mediated invasion and metastasis in pancreatic cancer cells
    • Zhao, S. et al. 2008. Inhibition of STAT3 Tyr705 phosphorylation by Smad4 suppresses transforming growth factor beta-mediated invasion and metastasis in pancreatic cancer cells. Cancer Res. 68 : 4221 4228.
    • (2008) Cancer Res. , vol.68 , pp. 4221-4228
    • Zhao, S.1
  • 183
    • 0032584235 scopus 로고    scopus 로고
    • Recruitment of SH2-containing protein tyrosine phosphatase SHP-1 to the interleukin 2 receptor; Loss of SHP-1 expression in human T-lymphotropic virus type I-transformed T cells
    • Migone, T.S. et al. 1998. Recruitment of SH2-containing protein tyrosine phosphatase SHP-1 to the interleukin 2 receptor; loss of SHP-1 expression in human T-lymphotropic virus type I-transformed T cells. Proc. Natl. Acad. Sci. USA 95 : 3845 3850.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3845-3850
    • Migone, T.S.1
  • 184
    • 0032212797 scopus 로고    scopus 로고
    • Activation of the protein tyrosine phosphatase SHP2 via the interleukin-6 signal transducing receptor protein gp130 requires tyrosine kinase Jak1 and limits acute-phase protein expression
    • Schaper, F. et al. 1998. Activation of the protein tyrosine phosphatase SHP2 via the interleukin-6 signal transducing receptor protein gp130 requires tyrosine kinase Jak1 and limits acute-phase protein expression. Biochem. J. 335 (Pt 3 557 565.
    • (1998) Biochem. J. , vol.335 , Issue.3 , pp. 557-565
    • Schaper, F.1
  • 185
    • 10644271682 scopus 로고    scopus 로고
    • TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3
    • Perry, E. et al. 2004. TMF/ARA160 is a BC-box-containing protein that mediates the degradation of Stat3. Oncogene 23 : 8908 8919.
    • (2004) Oncogene , vol.23 , pp. 8908-8919
    • Perry, E.1
  • 186
    • 23244438013 scopus 로고    scopus 로고
    • Composition and assembly of STAT-targeting ubiquitin ligase complexes: Paramyxovirus V protein carboxyl terminus is an oligomerization domain
    • Ulane, C.M. et al. 2005. Composition and assembly of STAT-targeting ubiquitin ligase complexes: paramyxovirus V protein carboxyl terminus is an oligomerization domain. J. Virol. 79 : 10180 10189.
    • (2005) J. Virol. , vol.79 , pp. 10180-10189
    • Ulane, C.M.1
  • 187
    • 33745868294 scopus 로고    scopus 로고
    • Stat3 cleavage by caspases: Impact on full-length Stat3 expression, fragment formation, and transcriptional activity
    • Darnowski, J.W. et al. 2006. Stat3 cleavage by caspases: impact on full-length Stat3 expression, fragment formation, and transcriptional activity. J. Biol. Chem. 281 : 17707 17717.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17707-17717
    • Darnowski, J.W.1
  • 188
    • 0030935260 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality
    • Takeda, K. et al. 1997. Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality. Proc. Natl. Acad. Sci. USA 94 : 3801 3804.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3801-3804
    • Takeda, K.1
  • 189
    • 0037047360 scopus 로고    scopus 로고
    • STAT3 contributes to the mitogenic response of hepatocytes during liver regeneration
    • Li, W. et al. 2002. STAT3 contributes to the mitogenic response of hepatocytes during liver regeneration. J. Biol. Chem. 277 : 28411 28417.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28411-28417
    • Li, W.1
  • 190
    • 0033034365 scopus 로고    scopus 로고
    • Enhanced Th1 activity and development of chronic enterocolitis in mice devoid of Stat3 in macrophages and neutrophils
    • Takeda, K. et al. 1999. Enhanced Th1 activity and development of chronic enterocolitis in mice devoid of Stat3 in macrophages and neutrophils. Immunity 10 : 39 49.
    • (1999) Immunity , vol.10 , pp. 39-49
    • Takeda, K.1
  • 191
    • 0033198793 scopus 로고    scopus 로고
    • Keratinocyte-specific ablation of Stat3 exhibits impaired skin remodeling, but does not affect skin morphogenesis
    • Sano, S. et al. 1999. Keratinocyte-specific ablation of Stat3 exhibits impaired skin remodeling, but does not affect skin morphogenesis. EMBO J. 18 : 4657 4668.
    • (1999) EMBO J. , vol.18 , pp. 4657-4668
    • Sano, S.1
  • 192
    • 0033214903 scopus 로고    scopus 로고
    • Suppression of epithelial apoptosis and delayed mammary gland involution in mice with a conditional knockout of Stat3
    • Chapman, R.S. et al. 1999. Suppression of epithelial apoptosis and delayed mammary gland involution in mice with a conditional knockout of Stat3. Genes Dev. 13 : 2604 2616.
    • (1999) Genes Dev. , vol.13 , pp. 2604-2616
    • Chapman, R.S.1
  • 193
    • 33748158716 scopus 로고    scopus 로고
    • The biological functions of the versatile transcription factors STAT3 and STAT5 and new strategies for their targeted inhibition
    • Desrivieres, S. et al. 2006. The biological functions of the versatile transcription factors STAT3 and STAT5 and new strategies for their targeted inhibition. J. Mamm. Gland Biol. Neoplasia 11 : 75 87.
    • (2006) J. Mamm. Gland Biol. Neoplasia , vol.11 , pp. 75-87
    • Desrivieres, S.1
  • 194
    • 33746764457 scopus 로고    scopus 로고
    • Beta 4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis
    • Guo, W. et al. 2006. Beta 4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis. Cell 126 : 489 502.
    • (2006) Cell , vol.126 , pp. 489-502
    • Guo, W.1
  • 195
    • 4444281108 scopus 로고    scopus 로고
    • The role of STATs in inflammation and inflammatory diseases
    • Pfitzner, E. et al. 2004. The role of STATs in inflammation and inflammatory diseases. Curr. Pharm. Des. 10 : 2839 2850.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2839-2850
    • Pfitzner, E.1
  • 196
    • 0033967026 scopus 로고    scopus 로고
    • Systemic lipopolysaccharide and interleukin-1beta activate the interleukin 6: STAT intracellular signaling pathway in neurons of mouse trigeminal ganglion
    • Kobierski, L.A., S. Srivastava D. Borsook. 2000. Systemic lipopolysaccharide and interleukin-1beta activate the interleukin 6: STAT intracellular signaling pathway in neurons of mouse trigeminal ganglion. Neurosci. Lett. 281 : 61 64.
    • (2000) Neurosci. Lett. , vol.281 , pp. 61-64
    • Kobierski, L.A.1    Srivastava, S.2    Borsook, D.3
  • 197
    • 11244348125 scopus 로고    scopus 로고
    • STAT3 regulates NF-kappaB recruitment to the IL-12p40 promoter in dendritic cells
    • Hoentjen, F. et al. 2005. STAT3 regulates NF-kappaB recruitment to the IL-12p40 promoter in dendritic cells. Blood 105 : 689 696.
    • (2005) Blood , vol.105 , pp. 689-696
    • Hoentjen, F.1
  • 198
    • 43049096401 scopus 로고    scopus 로고
    • STAT3 and STAT1 mediate IL-11-dependent and inflammation-associated gastric tumorigenesis in gp130 receptor mutant mice
    • Ernst, M. et al. 2008. STAT3 and STAT1 mediate IL-11-dependent and inflammation-associated gastric tumorigenesis in gp130 receptor mutant mice. J. Clin. Invest. 118 : 1727 1738.
    • (2008) J. Clin. Invest. , vol.118 , pp. 1727-1738
    • Ernst, M.1
  • 199
    • 27744468499 scopus 로고    scopus 로고
    • Cyclooxygenase-2-dependent activation of signal transducer and activator of transcription 3 by interleukin-6 in non-small cell lung cancer
    • Dalwadi, H. et al. 2005. Cyclooxygenase-2-dependent activation of signal transducer and activator of transcription 3 by interleukin-6 in non-small cell lung cancer. Clin. Cancer Res. 11 : 7674 7682.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 7674-7682
    • Dalwadi, H.1
  • 200
    • 34247600538 scopus 로고    scopus 로고
    • STAT3 as a central mediator of neoplastic cellular transformation
    • Frank, D.A. 2007. STAT3 as a central mediator of neoplastic cellular transformation. Cancer Lett. 251 : 199 210.
    • (2007) Cancer Lett. , vol.251 , pp. 199-210
    • Frank, D.A.1
  • 201
    • 0031893214 scopus 로고    scopus 로고
    • Stat3 activation is required for cellular transformation by v-src
    • Bromberg, J.F. et al. 1998. Stat3 activation is required for cellular transformation by v-src. Mol. Cell Biol. 18 : 2553 2558.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2553-2558
    • Bromberg, J.F.1
  • 202
    • 0037050212 scopus 로고    scopus 로고
    • Requirement of Stat3 signaling for HGF/SF-Met mediated tumorigenesis
    • Zhang, Y.W. et al. 2002. Requirement of Stat3 signaling for HGF/SF-Met mediated tumorigenesis. Oncogene 21 : 217 226.
    • (2002) Oncogene , vol.21 , pp. 217-226
    • Zhang, Y.W.1
  • 203
    • 0033529704 scopus 로고    scopus 로고
    • Stat3 as an oncogene
    • Bromberg, J.F. et al. 1999. Stat3 as an oncogene. Cell 98 : 295 303.
    • (1999) Cell , vol.98 , pp. 295-303
    • Bromberg, J.F.1
  • 204
    • 0032984589 scopus 로고    scopus 로고
    • Constitutive activation of Stat3 signaling confers resistance to apoptosis in human U266 myeloma cells
    • Catlett-Falcone, R. et al. 1999. Constitutive activation of Stat3 signaling confers resistance to apoptosis in human U266 myeloma cells. Immunity 10 : 105 115.
    • (1999) Immunity , vol.10 , pp. 105-115
    • Catlett-Falcone, R.1
  • 205
    • 0033584297 scopus 로고    scopus 로고
    • Inhibition of pp60c-Src reduces Bcl-XL expression and reverses the transformed phenotype of cells overexpressing EGF and HER-2 receptors
    • Karni, R., R. Jove A. Levitzki. 1999. Inhibition of pp60c-Src reduces Bcl-XL expression and reverses the transformed phenotype of cells overexpressing EGF and HER-2 receptors. Oncogene 18 : 4654 4662.
    • (1999) Oncogene , vol.18 , pp. 4654-4662
    • Karni, R.1    Jove, R.2    Levitzki, A.3
  • 206
    • 0032578721 scopus 로고    scopus 로고
    • STAT3 mediates the survival signal in oncogenic ras-transfected intestinal epithelial cells
    • Zushi, S. et al. 1998. STAT3 mediates the survival signal in oncogenic ras-transfected intestinal epithelial cells. Int. J. Cancer. 78 : 326 330.
    • (1998) Int. J. Cancer , vol.78 , pp. 326-330
    • Zushi, S.1
  • 207
    • 0035076453 scopus 로고    scopus 로고
    • Interleukin-11 up-regulates survivin expression in endothelial cells through a signal transducer and activator of transcription-3 pathway
    • Mahboubi, K. et al. 2001. Interleukin-11 up-regulates survivin expression in endothelial cells through a signal transducer and activator of transcription-3 pathway. Lab Invest. 81 : 327 334.
    • (2001) Lab Invest. , vol.81 , pp. 327-334
    • Mahboubi, K.1
  • 208
    • 0037902100 scopus 로고    scopus 로고
    • Serine phosphorylation of STAT3 is essential for Mcl-1 expression and macrophage survival
    • Liu, H. et al. 2003. Serine phosphorylation of STAT3 is essential for Mcl-1 expression and macrophage survival. Blood 102 : 344 352.
    • (2003) Blood , vol.102 , pp. 344-352
    • Liu, H.1
  • 209
  • 210
    • 0037441888 scopus 로고    scopus 로고
    • Inhibition of STAT3 signaling induces apoptosis and decreases survivin expression in primary effusion lymphoma
    • Aoki, Y., G.M. Feldman G. Tosato. 2003. Inhibition of STAT3 signaling induces apoptosis and decreases survivin expression in primary effusion lymphoma. Blood 101 : 1535 1542.
    • (2003) Blood , vol.101 , pp. 1535-1542
    • Aoki, Y.1    Feldman, G.M.2    Tosato, G.3
  • 211
    • 3042726888 scopus 로고    scopus 로고
    • STAT3 is constitutively activated and supports cell survival in association with survivin expression in gastric cancer cells
    • Kanda, N. et al. 2004. STAT3 is constitutively activated and supports cell survival in association with survivin expression in gastric cancer cells. Oncogene 23 : 4921 4929.
    • (2004) Oncogene , vol.23 , pp. 4921-4929
    • Kanda, N.1
  • 212
    • 3042748279 scopus 로고    scopus 로고
    • Knockdown of STAT3 expression by RNAi induces apoptosis in astrocytoma cells
    • Konnikova, L. et al. 2003. Knockdown of STAT3 expression by RNAi induces apoptosis in astrocytoma cells. BMC Cancer 3 : 23.
    • (2003) BMC Cancer , vol.3 , pp. 23
    • Konnikova, L.1
  • 213
    • 0035265830 scopus 로고    scopus 로고
    • Cooperation between STAT3 and c-jun suppresses Fas transcription
    • Ivanov, V.N. et al. 2001. Cooperation between STAT3 and c-jun suppresses Fas transcription. Mol. Cell. 7 : 517 528.
    • (2001) Mol. Cell. , vol.7 , pp. 517-528
    • Ivanov, V.N.1
  • 214
    • 0037096876 scopus 로고    scopus 로고
    • Constitutive activation of signal transducers and activators of transcription 3 correlates with cyclin D1 overexpression and may provide a novel prognostic marker in head and neck squamous cell carcinoma
    • Masuda, M. et al. 2002. Constitutive activation of signal transducers and activators of transcription 3 correlates with cyclin D1 overexpression and may provide a novel prognostic marker in head and neck squamous cell carcinoma. Cancer Res. 62 : 3351 3355.
    • (2002) Cancer Res. , vol.62 , pp. 3351-3355
    • Masuda, M.1
  • 215
    • 0033521595 scopus 로고    scopus 로고
    • STAT3 is required for the gp130-mediated full activation of the c-myc gene
    • Kiuchi, N. et al. 1999. STAT3 is required for the gp130-mediated full activation of the c-myc gene. J. Exp. Med. 189 : 63 73.
    • (1999) J. Exp. Med. , vol.189 , pp. 63-73
    • Kiuchi, N.1
  • 216
    • 0033451992 scopus 로고    scopus 로고
    • Synergistic roles for Pim-1 and c-Myc in STAT3-mediated cell cycle progression and antiapoptosis
    • Shirogane, T. et al. 1999. Synergistic roles for Pim-1 and c-Myc in STAT3-mediated cell cycle progression and antiapoptosis. Immunity 11 : 709 719.
    • (1999) Immunity , vol.11 , pp. 709-719
    • Shirogane, T.1
  • 217
    • 0032516898 scopus 로고    scopus 로고
    • Transcriptional activation of the p21(WAF1,CIP1,SDI1) gene by interleukin-6 type cytokines. A prerequisite for their pro-differentiating and anti-apoptotic effects on human osteoblastic cells
    • Bellido, T. et al. 1998. Transcriptional activation of the p21(WAF1,CIP1,SDI1) gene by interleukin-6 type cytokines. A prerequisite for their pro-differentiating and anti-apoptotic effects on human osteoblastic cells. J. Biol. Chem. 273 : 21137 21144.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21137-21144
    • Bellido, T.1
  • 218
    • 0037474270 scopus 로고    scopus 로고
    • Opposite regulation of myc and p21waf1 transcription by STAT3 proteins
    • Barre, B., S. Avril O. Coqueret. 2003. Opposite regulation of myc and p21waf1 transcription by STAT3 proteins. J. Biol. Chem. 278 : 2990 2996.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2990-2996
    • Barre, B.1    Avril, S.2    Coqueret, O.3
  • 219
    • 40149094813 scopus 로고    scopus 로고
    • Inhibition of JAK1, 2/STAT3 signaling induces apoptosis, cell cycle arrest, and reduces tumor cell invasion in colorectal cancer cells
    • Xiong, H. et al. 2008. Inhibition of JAK1, 2/STAT3 signaling induces apoptosis, cell cycle arrest, and reduces tumor cell invasion in colorectal cancer cells. Neoplasia 10 : 287 297.
    • (2008) Neoplasia , vol.10 , pp. 287-297
    • Xiong, H.1
  • 220
    • 34547558390 scopus 로고    scopus 로고
    • Downstream signalling and specific inhibition of c-MET/HGF pathway in small cell lung cancer: Implications for tumour invasion
    • Ma, P.C. et al. 2007. Downstream signalling and specific inhibition of c-MET/HGF pathway in small cell lung cancer: implications for tumour invasion. Br. J. Cancer 97 : 368 377.
    • (2007) Br. J. Cancer , vol.97 , pp. 368-377
    • Ma, P.C.1
  • 221
    • 34047259844 scopus 로고    scopus 로고
    • Expression of p-STAT3 in human gastric carcinoma: Significant correlation in tumour invasion and prognosis
    • Yakata, Y. et al. 2007. Expression of p-STAT3 in human gastric carcinoma: significant correlation in tumour invasion and prognosis. Int. J. Oncol. 30 : 437 442.
    • (2007) Int. J. Oncol. , vol.30 , pp. 437-442
    • Yakata, Y.1
  • 222
    • 2442685645 scopus 로고    scopus 로고
    • Stat3 activation regulates the expression of matrix metalloproteinase-2 and tumor invasion and metastasis
    • Xie, T.X. et al. 2004. Stat3 activation regulates the expression of matrix metalloproteinase-2 and tumor invasion and metastasis. Oncogene 23 : 3550 3560.
    • (2004) Oncogene , vol.23 , pp. 3550-3560
    • Xie, T.X.1
  • 223
    • 33644526633 scopus 로고    scopus 로고
    • Requirement of STAT3 activation for maximal collagenase-1 (MMP-1) induction by epidermal growth factor and malignant characteristics in T24 bladder cancer cells
    • Itoh, M. et al. 2006. Requirement of STAT3 activation for maximal collagenase-1 (MMP-1) induction by epidermal growth factor and malignant characteristics in T24 bladder cancer cells. Oncogene 25 : 1195 1204.
    • (2006) Oncogene , vol.25 , pp. 1195-1204
    • Itoh, M.1
  • 224
    • 21044447810 scopus 로고    scopus 로고
    • Overexpression of phosphorylated-STAT3 correlated with the invasion and metastasis of cutaneous squamous cell carcinoma
    • Suiqing, C., Z. Min C. Lirong. 2005. Overexpression of phosphorylated-STAT3 correlated with the invasion and metastasis of cutaneous squamous cell carcinoma. J. Dermatol. 32 : 354 360.
    • (2005) J. Dermatol. , vol.32 , pp. 354-360
    • Suiqing, C.1    Min, Z.2    Lirong, C.3
  • 225
    • 33746603930 scopus 로고    scopus 로고
    • Signal transducers and activators of transcription-3 up-regulates tissue inhibitor of metalloproteinase-1 expression and decreases invasiveness of breast cancer
    • Dien, J. et al. 2006. Signal transducers and activators of transcription-3 up-regulates tissue inhibitor of metalloproteinase-1 expression and decreases invasiveness of breast cancer. Am. J. Pathol. 169 : 633 642.
    • (2006) Am. J. Pathol. , vol.169 , pp. 633-642
    • Dien, J.1
  • 226
    • 0035794196 scopus 로고    scopus 로고
    • A stat-responsive element in the promoter of the episialin/MUC1 gene is involved in its overexpression in carcinoma cells
    • Gaemers, I.C. et al. 2001. A stat-responsive element in the promoter of the episialin/MUC1 gene is involved in its overexpression in carcinoma cells. J. Biol. Chem. 276 : 6191 6199.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6191-6199
    • Gaemers, I.C.1
  • 227
    • 0036484836 scopus 로고    scopus 로고
    • In vivo activation of JAK2/STAT-3 pathway during angiogenesis induced by GM-CSF
    • Valdembri, D. et al. 2002. In vivo activation of JAK2/STAT-3 pathway during angiogenesis induced by GM-CSF. FASEB J. 16 : 225 227.
    • (2002) FASEB J. , vol.16 , pp. 225-227
    • Valdembri, D.1
  • 228
    • 85047695527 scopus 로고    scopus 로고
    • Constitutive Stat3 activity up-regulates VEGF expression and tumor angiogenesis
    • Niu, G. et al. 2002. Constitutive Stat3 activity up-regulates VEGF expression and tumor angiogenesis. Oncogene 21 : 2000 2008.
    • (2002) Oncogene , vol.21 , pp. 2000-2008
    • Niu, G.1
  • 229
    • 0037461934 scopus 로고    scopus 로고
    • Stat3 activation regulates the expression of vascular endothelial growth factor and human pancreatic cancer angiogenesis and metastasis
    • Wei, D. et al. 2003. Stat3 activation regulates the expression of vascular endothelial growth factor and human pancreatic cancer angiogenesis and metastasis. Oncogene 22 : 319 329.
    • (2003) Oncogene , vol.22 , pp. 319-329
    • Wei, D.1
  • 230
    • 0037435011 scopus 로고    scopus 로고
    • Interleukin-6 promotes cervical tumor growth by VEGF-dependent angiogenesis via a STAT3 pathway
    • Wei, L.H. et al. 2003. Interleukin-6 promotes cervical tumor growth by VEGF-dependent angiogenesis via a STAT3 pathway. Oncogene 22 : 1517 1527.
    • (2003) Oncogene , vol.22 , pp. 1517-1527
    • Wei, L.H.1
  • 231
    • 33845771270 scopus 로고    scopus 로고
    • Inhibition of growth and metastasis of human hepatocellular carcinoma by antisense oligonucleotide targeting signal transducer and activator of transcription 3
    • Li, W.C. et al. 2006. Inhibition of growth and metastasis of human hepatocellular carcinoma by antisense oligonucleotide targeting signal transducer and activator of transcription 3. Clin. Cancer Res. 12 : 7140 7148.
    • (2006) Clin. Cancer Res. , vol.12 , pp. 7140-7148
    • Li, W.C.1
  • 232
    • 33645532055 scopus 로고    scopus 로고
    • Activation of stat3 in human melanoma promotes brain metastasis
    • Xie, T.X. et al. 2006. Activation of stat3 in human melanoma promotes brain metastasis. Cancer Res. 66 : 3188 3196.
    • (2006) Cancer Res. , vol.66 , pp. 3188-3196
    • Xie, T.X.1
  • 233
    • 47249161129 scopus 로고    scopus 로고
    • Twist is transcriptionally induced by activation of STAT3 and mediates STAT3 oncogenic function
    • Cheng, G.Z. et al. 2008. Twist is transcriptionally induced by activation of STAT3 and mediates STAT3 oncogenic function. J. Biol. Chem. 283 : 14665 14673.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14665-14673
    • Cheng, G.Z.1
  • 234
    • 39149129602 scopus 로고    scopus 로고
    • Forced expression of a constitutively active form of Stat3 in mouse epidermis enhances malignant progression of skin tumors induced by two-stage carcinogenesis
    • Chan, K.S. et al. 2008. Forced expression of a constitutively active form of Stat3 in mouse epidermis enhances malignant progression of skin tumors induced by two-stage carcinogenesis. Oncogene 27 : 1087 1094.
    • (2008) Oncogene , vol.27 , pp. 1087-1094
    • Chan, K.S.1
  • 235
    • 46949083070 scopus 로고    scopus 로고
    • Stage-specific disruption of Stat3 demonstrates a direct requirement during both the initiation and promotion stages of mouse skin tumorigenesis
    • Kataoka, K. et al. 2008. Stage-specific disruption of Stat3 demonstrates a direct requirement during both the initiation and promotion stages of mouse skin tumorigenesis. Carcinogenesis 29 : 1108 1114.
    • (2008) Carcinogenesis , vol.29 , pp. 1108-1114
    • Kataoka, K.1
  • 236
    • 38749084203 scopus 로고    scopus 로고
    • Regulation of liver regeneration and hepatocarcinogenesis by suppressor of cytokine signaling 3
    • Riehle, K.J. et al. 2008. Regulation of liver regeneration and hepatocarcinogenesis by suppressor of cytokine signaling 3. J. Exp. Med. 205 : 91 103.
    • (2008) J. Exp. Med. , vol.205 , pp. 91-103
    • Riehle, K.J.1
  • 237
    • 44249117111 scopus 로고    scopus 로고
    • Combined targeting of epidermal growth factor receptor, signal transducer and activator of transcription-3, and Bcl-X(L) enhances antitumor effects in squamous cell carcinoma of the head and neck
    • Boehm, A.L. et al. 2008. Combined targeting of epidermal growth factor receptor, signal transducer and activator of transcription-3, and Bcl-X(L) enhances antitumor effects in squamous cell carcinoma of the head and neck. Mol. Pharmacol. 73 : 1632 1642.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1632-1642
    • Boehm, A.L.1
  • 238
    • 1842579486 scopus 로고    scopus 로고
    • Nuclear factor-kappaB and STAT3 are constitutively active in CD138+ cells derived from multiple myeloma patients, and suppression of these transcription factors leads to apoptosis
    • Bharti, A.C. et al. 2004. Nuclear factor-kappaB and STAT3 are constitutively active in CD138+ cells derived from multiple myeloma patients, and suppression of these transcription factors leads to apoptosis. Blood 103 : 3175 3184.
    • (2004) Blood , vol.103 , pp. 3175-3184
    • Bharti, A.C.1
  • 239
    • 0037206950 scopus 로고    scopus 로고
    • Resistance to chemotherapy via Stat3-dependent overexpression of Bcl-2 in metastatic breast cancer cells
    • Real, P.J. et al. 2002. Resistance to chemotherapy via Stat3-dependent overexpression of Bcl-2 in metastatic breast cancer cells. Oncogene 21 : 7611 7618.
    • (2002) Oncogene , vol.21 , pp. 7611-7618
    • Real, P.J.1
  • 240
    • 33750827521 scopus 로고    scopus 로고
    • Cutting edge: Inherent and acquired resistance to radiation-induced apoptosis in B cells: A pivotal role for STAT3
    • Otero, D.C. et al. 2006. Cutting edge: inherent and acquired resistance to radiation-induced apoptosis in B cells: a pivotal role for STAT3. J. Immunol. 177 : 6593 6597.
    • (2006) J. Immunol. , vol.177 , pp. 6593-6597
    • Otero, D.C.1
  • 241
    • 33845228341 scopus 로고    scopus 로고
    • Inhibition of signal transducer and activator of transcription 3 activity results in down-regulation of Survivin following irradiation
    • Kim, K.W. et al. 2006. Inhibition of signal transducer and activator of transcription 3 activity results in down-regulation of Survivin following irradiation. Mol. Cancer Ther. 5 : 2659 2665.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 2659-2665
    • Kim, K.W.1
  • 242
    • 33747470228 scopus 로고    scopus 로고
    • Targeting constitutive and interleukin-6-inducible signal transducers and activators of transcription 3 pathway in head and neck squamous cell carcinoma cells by curcumin (diferuloylmethane)
    • Chakravarti, N., J.N. Myers B.B. Aggarwal. 2006. Targeting constitutive and interleukin-6-inducible signal transducers and activators of transcription 3 pathway in head and neck squamous cell carcinoma cells by curcumin (diferuloylmethane). Int. J. Cancer 119 : 1268 1275.
    • (2006) Int. J. Cancer , vol.119 , pp. 1268-1275
    • Chakravarti, N.1    Myers, J.N.2    Aggarwal, B.B.3
  • 243
    • 33646411225 scopus 로고    scopus 로고
    • Luteolin promotes degradation in signal transducer and activator of transcription 3 in human hepatoma cells: An implication for the antitumor potential of flavonoids
    • Selvendiran, K. et al. 2006. Luteolin promotes degradation in signal transducer and activator of transcription 3 in human hepatoma cells: an implication for the antitumor potential of flavonoids. Cancer Res. 66 : 4826 4834.
    • (2006) Cancer Res. , vol.66 , pp. 4826-4834
    • Selvendiran, K.1


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