메뉴 건너뛰기




Volumn 21, Issue 1, 2011, Pages 65-83

Signal transducer and activator of transcription 3 inhibitors: A patent review

Author keywords

Anticancer drugs; Cancer therapeutics; JAK STAT pathway; Molecular therapeutics; Oncogene; Proteinprotein interactions; Stat3

Indexed keywords

CARBOPLATIN; CISPLATIN; CPA 7; CPD188; CPD3 2; CPD3 7; CPD30; CPD30 12; IS3 295; ISS610; OLIGONUCLEOTIDE; OXALIPLATIN; PROTEIN SH2; S31 2001; S31 M2001; S3I 2001; STA 21; STAT3 PROTEIN; STX 0119; UNCLASSIFIED DRUG;

EID: 78650499336     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.2011.539205     Document Type: Review
Times cited : (94)

References (84)
  • 1
    • 54349127051 scopus 로고    scopus 로고
    • Molecular approaches towards the inhibition of the signal transducer and activator of transcription 3 (Stat3) protein
    • Fletcher S, Turkson J, Gunning PT. Molecular approaches towards the inhibition of the signal transducer and activator of transcription 3 (Stat3) protein. ChemMedChem 2008;3(8):1159-68
    • (2008) ChemMedChem , vol.3 , Issue.8 , pp. 1159-68
    • Fletcher, S.1    Turkson, J.2    Gunning, P.T.3
  • 2
    • 74549185979 scopus 로고    scopus 로고
    • Molecular disruption of oncogenic signal transducer and activator of transcription 3 (STAT3) protein
    • Fletcher S, Drewry JA, Shahani VM, et al. Molecular disruption of oncogenic signal transducer and activator of transcription 3 (STAT3) protein. Biochem Cell Biol 2009;87(6):825-33
    • (2009) Biochem Cell Biol , vol.87 , Issue.6 , pp. 825-33
    • Fletcher, S.1    Drewry, J.A.2    Shahani, V.M.3
  • 3
    • 0034658698 scopus 로고    scopus 로고
    • STATs in oncogenesis
    • Bowman T, Garcia R, Turkson J, et al. STATs in oncogenesis. Oncogene 2000;19(21):2474-88
    • (2000) Oncogene , vol.19 , Issue.21 , pp. 2474-88
    • Bowman, T.1    Garcia, R.2    Turkson, J.3
  • 4
    • 0036251154 scopus 로고    scopus 로고
    • Stat proteins and oncogenesis
    • Bromberg J. Stat proteins and oncogenesis. J Clin Invest 2002;109(9):1139-42
    • (2002) J Clin Invest , vol.109 , Issue.9 , pp. 1139-42
    • Bromberg, J.1
  • 6
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell Jr JE. STATs and gene regulation. Science 1997;277(5332):1630-5
    • (1997) Science , vol.277 , Issue.5332 , pp. 1630-5
    • Darnell Jr., J.E.1
  • 7
    • 20844444135 scopus 로고    scopus 로고
    • Targeting Stat3 in cancer therapy
    • Jing N, Tweardy DJ. Targeting Stat3 in cancer therapy. Anticancer Drugs 2005;16(6):601-7
    • (2005) Anticancer Drugs , vol.16 , Issue.6 , pp. 601-7
    • Jing, N.1    Tweardy, D.J.2
  • 8
    • 34548549283 scopus 로고    scopus 로고
    • Stat3 is tyrosine-phosphorylated through the interleukin-6/glycoprotein 130/Janus kinase pathway in breast cancer
    • Berishaj M, Gao SP, Ahmed S, et al. Stat3 is tyrosine-phosphorylated through the interleukin-6/glycoprotein 130/Janus kinase pathway in breast cancer. Breast Cancer Res 2007;9:3:R32
    • (2007) Breast Cancer Res , vol.9 , Issue.3
    • Berishaj, M.1    Gao, S.P.2    Ahmed, S.3
  • 9
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell Jr JE, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 1994;264(5164):1415-21
    • (1994) Science , vol.264 , Issue.5164 , pp. 1415-21
    • Darnell Jr., J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 10
    • 0033520313 scopus 로고    scopus 로고
    • Cellular physiology of STAT3: Where's the cytoplasmic monomer?
    • Ndubuisi MI, Guo GG, Fried VA, et al. Cellular physiology of STAT3: Where's the cytoplasmic monomer? J Biol Chem 1999;274(36):25499-509
    • (1999) J Biol Chem , vol.274 , Issue.36 , pp. 25499-509
    • Ndubuisi, M.I.1    Guo, G.G.2    Fried, V.A.3
  • 11
    • 1142287411 scopus 로고    scopus 로고
    • N-domain-dependent nonphosphorylated STAT4 dimers required for cytokine-driven activation
    • Ota N, Brett TJ, Murphy TL, et al. N-domain-dependent nonphosphorylated STAT4 dimers required for cytokine-driven activation. Nat Immunol 2004;5(5):208-15
    • (2004) Nat Immunol , vol.5 , Issue.5 , pp. 208-15
    • Ota, N.1    Brett, T.J.2    Murphy, T.L.3
  • 12
    • 0141483270 scopus 로고    scopus 로고
    • STATs dimerize in the absence of phosphorylation
    • Braunstein J, Brutsaert S, Olson R, et al. STATs dimerize in the absence of phosphorylation. J Biol Chem 2003;278(36):34133-40
    • (2003) J Biol Chem , vol.278 , Issue.36 , pp. 34133-40
    • Braunstein, J.1    Brutsaert, S.2    Olson, R.3
  • 13
    • 0036782706 scopus 로고    scopus 로고
    • Transcription factors as targets for cancer therapy
    • Darnell Jr JE. Transcription factors as targets for cancer therapy. Nat Rev Cancer 2002;2(2):740-9
    • (2002) Nat Rev Cancer , vol.2 , Issue.2 , pp. 740-9
    • Darnell Jr., J.E.1
  • 14
    • 0030792590 scopus 로고    scopus 로고
    • A family of cytokine-inducible inhibitors of signalling
    • Starr R, Willson TA, Viney EM, et al. A family of cytokine-inducible inhibitors of signalling. Nature 1997;387(6636):917-21
    • (1997) Nature , vol.387 , Issue.6636 , pp. 917-21
    • Starr, R.1    Willson, T.A.2    Viney, E.M.3
  • 15
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of Stat3 signal transduction by PIAS3
    • Chung CD, Liao J, Liu B, et al. Specific inhibition of Stat3 signal transduction by PIAS3. Science 1997;278(5344):1803-5
    • (1997) Science , vol.278 , Issue.5344 , pp. 1803-5
    • Chung, C.D.1    Liao, J.2    Liu, B.3
  • 16
    • 0028791664 scopus 로고
    • Roles of protein-tyrosine phosphatases in Stat1alpha-mediated cell signaling
    • Haque SJ, Flati V, Deb A, et al. Roles of protein-tyrosine phosphatases in Stat1alpha-mediated cell signaling. J Biol Chem 1995;270(43):25709-14
    • (1995) J Biol Chem , vol.270 , Issue.43 , pp. 25709-14
    • Haque, S.J.1    Flati, V.2    Deb, A.3
  • 17
    • 0029972194 scopus 로고    scopus 로고
    • The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase
    • Haspel RL, Salditt-Georgieff M, Darnell Jr JE. The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase. EMBO J 1996;15(22):6262-8
    • (1996) EMBO J , vol.15 , Issue.22 , pp. 6262-8
    • Haspel, R.L.1    Salditt-Georgieff, M.2    Darnell Jr., J.E.3
  • 18
    • 0029742102 scopus 로고    scopus 로고
    • Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of Stat1
    • Shuai K, Liao J, Song MM. Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of Stat1. Mol Cell Biol 1996;16(9):4932-41
    • (1996) Mol Cell Biol , vol.16 , Issue.9 , pp. 4932-41
    • Shuai, K.1    Liao, J.2    Song, M.M.3
  • 19
    • 0000413462 scopus 로고    scopus 로고
    • Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway
    • Kim TK, Maniatis T. Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 1996;273(5282):1717-19
    • (1996) Science , vol.273 , Issue.5282 , pp. 1717-19
    • Kim, T.K.1    Maniatis, T.2
  • 20
    • 0030983549 scopus 로고    scopus 로고
    • Involvement of proteasomes in regulating jak-STAT pathways upon interleukin-2 stimulation
    • Yu C-, Burakoff SJ. Involvement of proteasomes in regulating jak-STAT pathways upon interleukin-2 stimulation. J Biol Chem 1997;272(22):14017-20
    • (1997) J Biol Chem , vol.272 , Issue.22 , pp. 14017-20
    • Yu, C.1    Burakoff, S.J.2
  • 21
    • 0035977055 scopus 로고    scopus 로고
    • Phosphotyrosyl peptides block Stat3-mediated DNA binding activity, gene regulation, and cell transformation
    • Turkson J, Ryan D, Kim JS, et al. Phosphotyrosyl peptides block Stat3-mediated DNA binding activity, gene regulation, and cell transformation. J Biol Chem 2001;276(48):45443-55
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 45443-55
    • Turkson, J.1    Ryan, D.2    Kim, J.S.3
  • 22
    • 3543055012 scopus 로고    scopus 로고
    • Novel peptidomimetic inhibitors of signal transducer and activator of transcription 3 dimerization and biological activity
    • Turkson J, Kim JS, Zhang S, et al. Novel peptidomimetic inhibitors of signal transducer and activator of transcription 3 dimerization and biological activity. Mol Cancer Ther 2004;3(3):261-9
    • (2004) Mol Cancer Ther , vol.3 , Issue.3 , pp. 261-9
    • Turkson, J.1    Kim, J.S.2    Zhang, S.3
  • 23
    • 50249186849 scopus 로고    scopus 로고
    • Inhibition of transcription factors with small organic molecules
    • Berg T. Inhibition of transcription factors with small organic molecules. Curr Opin Chem Biol 2008;12(4):464-71
    • (2008) Curr Opin Chem Biol , vol.12 , Issue.4 , pp. 464-71
    • Berg, T.1
  • 24
    • 0035977055 scopus 로고    scopus 로고
    • Phosphotyrosyl peptides block Stat3-mediated DNA binding activity, gene regulation, and cell transformation
    • Turkson J, Ryan D, Kim JS, et al. Phosphotyrosyl peptides block Stat3-mediated DNA binding activity, gene regulation, and cell transformation. J Biol Chem 2001;276(48):45443-55
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 45443-55
    • Turkson, J.1    Ryan, D.2    Kim, J.S.3
  • 25
    • 64849111865 scopus 로고    scopus 로고
    • Targeting STAT3 in cancer: How successful are we?
    • Yue P, Turkson J. Targeting STAT3 in cancer: how successful are we? Expert Opin Investig Drugs 2009;18(1):45-56
    • (2009) Expert Opin Investig Drugs , vol.18 , Issue.1 , pp. 45-56
    • Yue, P.1    Turkson, J.2
  • 26
    • 75649128334 scopus 로고    scopus 로고
    • Coordination complex SH2 domain proteomimetics: An alternative approach to disrupting oncogenic protein-protein interactions
    • Drewry JA, Fletcher S, Yue P, et al. Coordination complex SH2 domain proteomimetics: an alternative approach to disrupting oncogenic protein-protein interactions. Chem Commun 2010;46(6):892-4
    • (2010) Chem Commun , vol.46 , Issue.6 , pp. 892-4
    • Drewry, J.A.1    Fletcher, S.2    Yue, P.3
  • 27
    • 70349558529 scopus 로고    scopus 로고
    • Disruption of transcriptionally active stat3 dimers with non-phosphorylated, salicylic acid-based small molecules: Potent in vitro and tumor cell activities
    • Fletcher S, Singh J, Zhang X, et al. Disruption of transcriptionally active stat3 dimers with non-phosphorylated, salicylic acid-based small molecules: potent in vitro and tumor cell activities. ChemBioChem 2009;10(12):1959-64
    • (2009) ChemBioChem , vol.10 , Issue.12 , pp. 1959-64
    • Fletcher, S.1    Singh, J.2    Zhang, X.3
  • 28
    • 77955633773 scopus 로고    scopus 로고
    • Fluacrypyrim, a novel STAT3 activation inhibitor, induces cell cycle arrest and apoptosis in cancer cells harboring constitutively-active STAT3
    • Yu Z-, Huang R, Xiao H, et al. Fluacrypyrim, a novel STAT3 activation inhibitor, induces cell cycle arrest and apoptosis in cancer cells harboring constitutively-active STAT3. Int J Cancer 2010;127(6):1259-70
    • (2010) Int J Cancer , vol.127 , Issue.6 , pp. 1259-70
    • Yu, Z.1    Huang, R.2    Xiao, H.3
  • 29
    • 77954364837 scopus 로고    scopus 로고
    • TRIM8 modulates STAT3 activity through negative regulation of PIAS3
    • Okumura F, Matsunaga Y, Katayama Y, et al. TRIM8 modulates STAT3 activity through negative regulation of PIAS3. J Cell Sci 2010;123(13):2238-45
    • (2010) J Cell Sci , vol.123 , Issue.13 , pp. 2238-45
    • Okumura, F.1    Matsunaga, Y.2    Katayama, Y.3
  • 30
    • 77955505020 scopus 로고    scopus 로고
    • Targeted inhibition of src kinase signaling attenuates pancreatic tumorigenesis
    • Nagaraj NS, Smith JJ, Revetta F, et al. Targeted inhibition of src kinase signaling attenuates pancreatic tumorigenesis. Mol Cancer Ther 2010;9(8):2322-32
    • (2010) Mol Cancer Ther , vol.9 , Issue.8 , pp. 2322-32
    • Nagaraj, N.S.1    Smith, J.J.2    Revetta, F.3
  • 31
    • 75649128334 scopus 로고    scopus 로고
    • Coordination complex SH2 domain proteomimetics: An alternative approach to disrupting oncogenic protein-protein interactions
    • Drewry JA, Fletcher S, Yue P, et al. Coordination complex SH2 domain proteomimetics: an alternative approach to disrupting oncogenic protein-protein interactions. Chem Commun 2010;46(6):892-4
    • (2010) Chem Commun , vol.46 , Issue.6 , pp. 892-4
    • Drewry, J.A.1    Fletcher, S.2    Yue, P.3
  • 32
    • 62849104063 scopus 로고    scopus 로고
    • Chemical probes that competitively and selectively inhibit Stat3 activation
    • Xu X, Kasembeli MM, Jiang X, et al. Chemical probes that competitively and selectively inhibit Stat3 activation. PLoS ONE 2009;4(3):e4783
    • (2009) PLoS ONE , vol.4 , Issue.3
    • Xu, X.1    Kasembeli, M.M.2    Jiang, X.3
  • 33
    • 0037294154 scopus 로고    scopus 로고
    • Identification of a high-affinity phosphopeptide inhibitor of Stat3
    • Ren Z, Cabell LA, Schaefer TS, et al. Identification of a high-affinity phosphopeptide inhibitor of Stat3. Bioorg Med Chem Lett 2003;13(4):633-6
    • (2003) Bioorg Med Chem Lett , vol.13 , Issue.4 , pp. 633-6
    • Ren, Z.1    Cabell, L.A.2    Schaefer, T.S.3
  • 34
    • 37549062631 scopus 로고    scopus 로고
    • Design syn thesis and studies of small molecule STAT3 inhibitors
    • Bhasin D, Cisek K, Pandharkar T, et al. Design, synthesis, and studies of small molecule STAT3 inhibitors. Bioorg Med Chem Lett 2008;18(1):391-5
    • (2008) Bioorg Med Chem Lett , vol.18 , Issue.1 , pp. 391-5
    • Bhasin, D.1    Cisek, K.2    Pandharkar, T.3
  • 35
    • 16344380754 scopus 로고    scopus 로고
    • A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells
    • Song H, Wang R, Wang S, et al. A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells. Proc Natl Acad Sci USA 2005;102(13):4700-5
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.13 , pp. 4700-5
    • Song, H.1    Wang, R.2    Wang, S.3
  • 36
    • 78649286584 scopus 로고    scopus 로고
    • Identification of a new series of STAT3 inhibitors by virtual screening
    • Matsuno K, Masuda Y, Sato H, et al. Identification of a new series of STAT3 inhibitors by virtual screening. ACS Med Chem Lett 2010;1(8):371-5
    • (2010) ACS Med Chem Lett , vol.1 , Issue.8 , pp. 371-5
    • Matsuno, K.1    Masuda, Y.2    Sato, H.3
  • 37
    • 77956627676 scopus 로고    scopus 로고
    • Structure-based design of conformationally constrained, cell-permeable Stat3 inhibitors
    • Chen J, Bai L, Bernard D, et al. Structure-based design of conformationally constrained, cell-permeable Stat3 inhibitors. ACS Med Chem Lett 2010;1:85-9
    • (2010) ACS Med Chem Lett , vol.1 , pp. 85-9
    • Chen, J.1    Bai, L.2    Bernard, D.3
  • 38
    • 22944434871 scopus 로고    scopus 로고
    • Targeting transcription factors for cancer therapy
    • Redell MS, Tweardy DJ. Targeting transcription factors for cancer therapy. Curr Pharm Des 2005;11(22):2873-87
    • (2005) Curr Pharm des , vol.11 , Issue.22 , pp. 2873-87
    • Redell, M.S.1    Tweardy, D.J.2
  • 42
    • 0028931604 scopus 로고
    • Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors
    • Stahl N, Farruggella TJ, Boulton TG, et al. Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors. Science 1995;267(5202):1349-53
    • (1995) Science , vol.267 , Issue.5202 , pp. 1349-53
    • Stahl, N.1    Farruggella, T.J.2    Boulton, T.G.3
  • 43
    • 0029981103 scopus 로고    scopus 로고
    • Stat3 recruitment by two distinct ligand-induced, tyrosine-phosphorylated docking sites in the interleukin-10 receptor intracellular domain
    • Weber-Nordtt RM, Riley JK, Greenlund AC, et al. Stat3 recruitment by two distinct ligand-induced, tyrosine-phosphorylated docking sites in the interleukin-10 receptor intracellular domain. J Biol Chem 1996;271:27954-61
    • (1996) J Biol Chem , vol.271 , pp. 27954-61
    • Weber-Nordtt, R.M.1    Riley, J.K.2    Greenlund, A.C.3
  • 44
    • 27144475507 scopus 로고    scopus 로고
    • Investigation of the binding determinants of phosphopeptides targeted to the src homology 2 domain of the signal transducer and activator of transcription 3. development of a high-affinity peptide inhibitor
    • Coleman IV DR, Ren Z, Mandal PK, et al. Investigation of the binding determinants of phosphopeptides targeted to the src homology 2 domain of the signal transducer and activator of transcription 3. development of a high-affinity peptide inhibitor. J Med Chem 2005;48(21):6661-70
    • (2005) J Med Chem , vol.48 , Issue.21 , pp. 6661-70
    • Coleman, I.V.D.R.1    Ren, Z.2    Mandal, P.K.3
  • 45
    • 2942579547 scopus 로고    scopus 로고
    • A high-throughput fluorescence polarization assay for signal transducer and activator of transcription 3
    • Schust J, Berg T. A high-throughput fluorescence polarization assay for signal transducer and activator of transcription 3. Anal Biochem 2004;330(1):114-18
    • (2004) Anal Biochem , vol.330 , Issue.1 , pp. 114-18
    • Schust, J.1    Berg, T.2
  • 48
    • 33847682326 scopus 로고    scopus 로고
    • Isoform selective inhibition of STAT1 or STAT3 homo-dimerization via peptidomimetic probes: Structural recognition of STAT SH2 domains
    • Gunning PT, Katt WP, Glenn M, et al. Isoform selective inhibition of STAT1 or STAT3 homo-dimerization via peptidomimetic probes: Structural recognition of STAT SH2 domains. Bioorg Med Chem Lett 2007;17(7):1875-8
    • (2007) Bioorg Med Chem Lett , vol.17 , Issue.7 , pp. 1875-8
    • Gunning, P.T.1    Katt, W.P.2    Glenn, M.3
  • 49
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, et al. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997;267(3):727-48
    • (1997) J Mol Biol , vol.267 , Issue.3 , pp. 727-48
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 50
    • 0033834679 scopus 로고    scopus 로고
    • The coiled-coil domain of Stat3 is essential for its SH2 domain-mediated receptor binding and subsequent activation induced by epidermal growth factor and interleukin-6
    • Zhang T, Kee WH, Seow KT, et al. The coiled-coil domain of Stat3 is essential for its SH2 domain-mediated receptor binding and subsequent activation induced by epidermal growth factor and interleukin-6. Mol Cell Biol 2000;20(19):7132-9
    • (2000) Mol Cell Biol , vol.20 , Issue.19 , pp. 7132-9
    • Zhang, T.1    Kee, W.H.2    Seow, K.T.3
  • 51
    • 0035823547 scopus 로고    scopus 로고
    • Functional importance of Stat3 tetramerization in activation of the alpha2-macroglobulin gene
    • Zhang X, Darnell Jr JE. Functional importance of Stat3 tetramerization in activation of the alpha2-macroglobulin gene. J Biol Chem 2001;276(36):33576-81
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 33576-81
    • Zhang, X.1    Darnell Jr., J.E.2
  • 52
    • 0029739627 scopus 로고    scopus 로고
    • Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain
    • Xu X, Sun Y-, Hoey T. Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain. Science 1996;273(5276):794-7
    • (1996) Science , vol.273 , Issue.5276 , pp. 794-7
    • Xu, X.1    Sun, Y.2    Hoey, T.3
  • 53
    • 38649086742 scopus 로고    scopus 로고
    • Rationally designed inhibitors identify STAT3 N-domain as a promising anticancer drug target
    • Timofeeva OA, Gaponenko V, Lockett SJ, et al. Rationally designed inhibitors identify STAT3 N-domain as a promising anticancer drug target. ACS Chem Biol 2007;2(12):799-809
    • (2007) ACS Chem Biol , vol.2 , Issue.12 , pp. 799-809
    • Timofeeva, O.A.1    Gaponenko, V.2    Lockett, S.J.3
  • 55
    • 0029739627 scopus 로고    scopus 로고
    • Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain
    • Xu X, Sun Y-, Hoey T. Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain. Science 1996;273(5276):794-7
    • (1996) Science , vol.273 , Issue.5276 , pp. 794-7
    • Xu, X.1    Sun, Y.2    Hoey, T.3
  • 56
    • 0035823547 scopus 로고    scopus 로고
    • Functional importance of Stat3 tetramerization in activation of the alpha2-macroglobulin gene
    • Zhang X, Darnell Jr JE. Functional importance of Stat3 tetramerization in activation of the alpha2-macroglobulin gene. J Biol Chem 2001;276(36):33576-81
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 33576-81
    • Zhang, X.1    Darnell Jr., J.E.2
  • 57
    • 0042206459 scopus 로고    scopus 로고
    • A novel sequence in the coiled-coil domain of Stat3 essential for its nuclear translocation
    • Ma J, Zhang T, Novotny-Diermayr V, et al. A novel sequence in the coiled-coil domain of Stat3 essential for its nuclear translocation. J Biol Chem 2003;278(31):29252-60
    • (2003) J Biol Chem , vol.278 , Issue.31 , pp. 29252-60
    • Ma, J.1    Zhang, T.2    Novotny-Diermayr, V.3
  • 58
    • 15244359491 scopus 로고    scopus 로고
    • New insights into dimerization of STAT proteins: A vehicle to modulate signaling for therapeutic purposes? (meeting abstract)
    • Byrd RA, Gaponenko V, Sarma SP, et al. New insights into dimerization of STAT proteins: a vehicle to modulate signaling for therapeutic purposes? (meeting abstract). Proc Amer Assoc Cancer Res 2002;43:139
    • (2002) Proc Amer Assoc Cancer Res , vol.43 , pp. 139
    • Byrd, R.A.1    Gaponenko, V.2    Sarma, S.P.3
  • 59
    • 33748433244 scopus 로고    scopus 로고
    • Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery
    • Mae M, Langel U. Cell-penetrating peptides as vectors for peptide, protein and oligonucleotide delivery. Curr Opin Pharmacol 2006;6(5):509-14
    • (2006) Curr Opin Pharmacol , vol.6 , Issue.5 , pp. 509-14
    • Mae, M.1    Langel, U.2
  • 61
    • 16344380754 scopus 로고    scopus 로고
    • A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells
    • Song H, Wang R, Wang S, et al. A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells. Proc Natl Acad Sci USA 2005;102(13):4700-5
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.13 , pp. 4700-5
    • Song, H.1    Wang, R.2    Wang, S.3
  • 62
    • 0032499801 scopus 로고    scopus 로고
    • Three-dimensional structure of the Stat3beta homodimer bound to DNA
    • Becker S, Groner B, Muller CW. Three-dimensional structure of the Stat3beta homodimer bound to DNA. Nature 1998;394(6689):145-51
    • (1998) Nature , vol.394 , Issue.6689 , pp. 145-51
    • Becker, S.1    Groner, B.2    Muller, C.W.3
  • 63
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
    • Ewing TJA, Makino S, Skillman AG, et al. DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases. J Comput Aided Mol Des 2001;15(5):411-28
    • (2001) J Comput Aided Mol des , vol.15 , Issue.5 , pp. 411-28
    • Tja, E.1    Makino, S.2    Skillman, A.G.3
  • 65
    • 34250658084 scopus 로고    scopus 로고
    • Selective chemical probe inhibitor of Stat3, identified through structure-based virtual screening, induces antitumor activity
    • Siddiquee K, Zhang S, Guida WC, et al. Selective chemical probe inhibitor of Stat3, identified through structure-based virtual screening, induces antitumor activity. Proc Natl Acad Sci USA 2007;104(18):7391-6
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.18 , pp. 7391-6
    • Siddiquee, K.1    Zhang, S.2    Guida, W.C.3
  • 66
    • 77649178678 scopus 로고    scopus 로고
    • A novel small-molecule disrupts Stat3 SH2 domain-phosphotyrosine interactions and Stat3-dependent tumor processes
    • Zhang X, Yue P, Fletcher S, et al. A novel small-molecule disrupts Stat3 SH2 domain-phosphotyrosine interactions and Stat3-dependent tumor processes. Biochem Pharmacol 2010;79(10):1398-409
    • (2010) Biochem Pharmacol , vol.79 , Issue.10 , pp. 1398-409
    • Zhang, X.1    Yue, P.2    Fletcher, S.3
  • 68
    • 0031302358 scopus 로고    scopus 로고
    • Flexible protein-ligand docking by global energy optimization in internal coordinates
    • Totrov M, Abagyan R. Flexible protein-ligand docking by global energy optimization in internal coordinates. Proteins: structure, function and genetics 1997;29(Suppl. 1):215-20
    • (1997) Proteins: Structure, Function and Genetics , vol.29 , Issue.SUPPL. 1 , pp. 215-20
    • Totrov, M.1    Abagyan, R.2
  • 70
    • 58149392583 scopus 로고    scopus 로고
    • Targeting protein-protein interactions: Suppression of Stat3 dimerization with rationally designed small-molecule, nonpeptidic SH2 domain binders
    • Gunning PT, Glenn MP, Siddiquee KA, et al. Targeting protein-protein interactions: Suppression of Stat3 dimerization with rationally designed small-molecule, nonpeptidic SH2 domain binders. ChemBioChem 2008;9(17):2800-3
    • (2008) ChemBioChem , vol.9 , Issue.17 , pp. 2800-3
    • Gunning, P.T.1    Glenn, M.P.2    Siddiquee, K.A.3
  • 71
    • 38649129118 scopus 로고    scopus 로고
    • An oxazole-based small-molecule stat3 inhibitor modulates stat3 stability and processing and induces antitumor cell effects
    • Siddiquee KAZ, Gunning PT, Glen M, et al. An oxazole-based small-molecule stat3 inhibitor modulates stat3 stability and processing and induces antitumor cell effects. ACS Chem Biol 2007;2(12):787-98
    • (2007) ACS Chem Biol , vol.2 , Issue.12 , pp. 787-98
    • Kaz, S.1    Gunning, P.T.2    Glen, M.3
  • 74
    • 0037386568 scopus 로고    scopus 로고
    • Targeted inhibition of Stat3 with a decoy oligonucleotide abrogates head and neck cancer cell growth
    • Leong PL, Andrews GA, Johnson DE, et al. Targeted inhibition of Stat3 with a decoy oligonucleotide abrogates head and neck cancer cell growth. Proc Natl Acad Sci USA 2003;100(7):4138-43
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.7 , pp. 4138-43
    • Leong, P.L.1    Andrews, G.A.2    Johnson, D.E.3
  • 75
    • 13944250650 scopus 로고    scopus 로고
    • In vivo antitumor efficacy of STAT3 blockade using a transcription factor decoy approach: Implications for cancer therapy
    • Xi S, Gooding WE, Grandis JR. In vivo antitumor efficacy of STAT3 blockade using a transcription factor decoy approach: implications for cancer therapy. Oncogene 2005;24(6):970-9
    • (2005) Oncogene , vol.24 , Issue.6 , pp. 970-9
    • Xi, S.1    Gooding, W.E.2    Grandis, J.R.3
  • 76
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y, Sherman Y, Ben-Sasson SA. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 1992;119(3):493-501
    • (1992) J Cell Biol , vol.119 , Issue.3 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 77
    • 0028543658 scopus 로고
    • In situ end labeling of fragmented DNA in induced ovarian atresia
    • D'Herde K, De Pestel G, Roels F. In situ end labeling of fragmented DNA in induced ovarian atresia. Biochem Cell Biol 1994;72(11-12):573-9
    • (1994) Biochem Cell Biol , vol.72 , Issue.11-12 , pp. 573-9
    • D'Herde, K.1    De Pestel, G.2    Roels, F.3
  • 78
    • 63949085226 scopus 로고    scopus 로고
    • Lack of toxicity of a STAT3 decoy oligonucleotide
    • Sen M, Tosca PJ, Zwayer C, et al. Lack of toxicity of a STAT3 decoy oligonucleotide. Cancer Chemother Pharmacol 2009;63(6):983-95
    • (2009) Cancer Chemother Pharmacol , vol.63 , Issue.6 , pp. 983-95
    • Sen, M.1    Tosca, P.J.2    Zwayer, C.3
  • 79
    • 12344328541 scopus 로고    scopus 로고
    • Inhibition of constitutive signal transducer and activator of transcription 3 activation by novel platinum complexes with potent antitumor activity
    • Turkson J, Zhang S, Palmer J, et al. Inhibition of constitutive signal transducer and activator of transcription 3 activation by novel platinum complexes with potent antitumor activity. Mol Cancer Ther 2004;3(12):1533-42
    • (2004) Mol Cancer Ther , vol.3 , Issue.12 , pp. 1533-42
    • Turkson, J.1    Zhang, S.2    Palmer, J.3
  • 81
    • 25444513779 scopus 로고    scopus 로고
    • A novel platinum compound inhibits constitutive Stat3 signaling and induces cell cycle arrest and apoptosis of malignant cells
    • Turkson J, Zhang S, Mora LB, et al. A novel platinum compound inhibits constitutive Stat3 signaling and induces cell cycle arrest and apoptosis of malignant cells. J Biol Chem 2005;280(38):32979-88
    • (2005) J Biol Chem , vol.280 , Issue.38 , pp. 32979-88
    • Turkson, J.1    Zhang, S.2    Mora, L.B.3
  • 83
    • 70350212976 scopus 로고    scopus 로고
    • STAT3 is required for proliferation and maintenance of multipotency in glioblastoma stem cells
    • Sherry MM, Reeves A, Wu JK, et al. STAT3 is required for proliferation and maintenance of multipotency in glioblastoma stem cells. Stem Cells 2009;27(10):2383-92
    • (2009) Stem Cells , vol.27 , Issue.10 , pp. 2383-92
    • Sherry, M.M.1    Reeves, A.2    Wu, J.K.3
  • 84
    • 73949096430 scopus 로고    scopus 로고
    • Glioblastoma cancer-initiating cells inhibit T-cell proliferation and effector responses by the signal transducers and activators of transcription 3 pathway
    • Wei J, Barr J, Kong L, et al. Glioblastoma cancer-initiating cells inhibit T-cell proliferation and effector responses by the signal transducers and activators of transcription 3 pathway. Mol Cancer Ther 2010;9(1):67-78
    • (2010) Mol Cancer Ther , vol.9 , Issue.1 , pp. 67-78
    • Wei, J.1    Barr, J.2    Kong, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.