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Volumn 124, Issue 6, 2009, Pages 1429-1439

Synergistic anti-tumor effect of paclitaxel with CRM197, an inhibitor of HB-EGF, in ovarian cancer

Author keywords

CRM197; EGFR; HB EGF; Ovarian cancer; Paclitaxel

Indexed keywords

DIPHTHERIA TOXOID CRM197; HEPARIN BINDING EPIDERMAL GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PACLITAXEL; PROTEIN KINASE B; STRESS ACTIVATED PROTEIN KINASE; ANTINEOPLASTIC AGENT; BACTERIAL PROTEIN; CELL SURFACE RECEPTOR; CRM197 (NON TOXIC VARIANT OF DIPHTHERIA TOXIN); CRM197 (NON-TOXIC VARIANT OF DIPHTHERIA TOXIN); DIPHTHERIA TOXIN; HEPARIN ANTAGONIST; HEPARIN-BINDING EGF-LIKE GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE KINASE; PRIMER DNA; RNA; SIGNAL PEPTIDE; SMALL INTERFERING RNA;

EID: 60549113956     PISSN: 00207136     EISSN: 10970215     Source Type: Journal    
DOI: 10.1002/ijc.24031     Document Type: Article
Times cited : (58)

References (60)
  • 1
    • 0018387446 scopus 로고
    • Promotion of microtubule assembly in vitro by taxol
    • Schiff PB, Fant J, Horwitz SB. Promotion of microtubule assembly in vitro by taxol. Nature 1979;277:665-7.
    • (1979) Nature , vol.277 , pp. 665-667
    • Schiff, P.B.1    Fant, J.2    Horwitz, S.B.3
  • 2
    • 0027619786 scopus 로고
    • Taxol dose intensification and its clinical implications
    • Sarosy G, Reed E. Taxol dose intensification and its clinical implications. J Natl Med Assoc 1993;85:427-31.
    • (1993) J Natl Med Assoc , vol.85 , pp. 427-431
    • Sarosy, G.1    Reed, E.2
  • 3
    • 0028303080 scopus 로고
    • Update on the antitumor activity of paclitaxel in clinical trials
    • Rowinsky EK. Update on the antitumor activity of paclitaxel in clinical trials. Ann Pharmacother 1994;28(5 Suppl):S18-S22.
    • (1994) Ann Pharmacother , vol.28 , Issue.5 SUPPL.
    • Rowinsky, E.K.1
  • 4
    • 0035735754 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases in the response of tumor cells to chemotherapy
    • Fan M, Chambers TC. Role of mitogen-activated protein kinases in the response of tumor cells to chemotherapy. Drug Resist Update 2001;4:253-67.
    • (2001) Drug Resist Update , vol.4 , pp. 253-267
    • Fan, M.1    Chambers, T.C.2
  • 5
    • 0035377357 scopus 로고    scopus 로고
    • Paclitaxel induces prolonged activation of the Ras/MEK/ERK pathway independently of activating the programmed cell death machinery
    • Okano J, Rustgi AK. Paclitaxel induces prolonged activation of the Ras/MEK/ERK pathway independently of activating the programmed cell death machinery. J Biol Chem 2001;276:19555-64.
    • (2001) J Biol Chem , vol.276 , pp. 19555-19564
    • Okano, J.1    Rustgi, A.K.2
  • 6
    • 0031936410 scopus 로고    scopus 로고
    • Specificity within the EGF family/ErbB receptor family signaling network
    • Riese DJ, II, Stern DF. Specificity within the EGF family/ErbB receptor family signaling network. Bioessays 1998;20:41-8.
    • (1998) Bioessays , vol.20 , pp. 41-48
    • Riese II, D.J.1    Stern, D.F.2
  • 7
    • 0025904265 scopus 로고
    • A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF
    • Higashiyama S, Abraham JA, Miller J, Fiddes JC, Klagsbrun M. A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF. Science 1991;251:936-9.
    • (1991) Science , vol.251 , pp. 936-939
    • Higashiyama, S.1    Abraham, J.A.2    Miller, J.3    Fiddes, J.C.4    Klagsbrun, M.5
  • 8
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane- anchored heparin-binding EGF-like growth factor
    • Izumi Y, Hirata M, Hasuwa H, Iwamoto R, Umata T, Miyado K, Tamai Y, Kurisaki T, Sehara-Fujisawa A, Ohno S, Mekada E. A metalloprotease-disintegrin MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane- anchored heparin-binding EGF-like growth factor. EMBO J 1998;17:7260-72.
    • (1998) EMBO J , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6    Tamai, Y.7    Kurisaki, T.8    Sehara-Fujisawa, A.9    Ohno, S.10    Mekada, E.11
  • 9
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals DF, Courtneidge SA. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 2003;17:7-30.
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 10
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel N, Zwick E, Daub H, Leserer M, Abraham R, Wallasch C, Ullrich A. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 1999; 402:884-8.
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1    Zwick, E.2    Daub, H.3    Leserer, M.4    Abraham, R.5    Wallasch, C.6    Ullrich, A.7
  • 11
    • 0037593847 scopus 로고    scopus 로고
    • The stressand inflammatory cytokine-induced ectodomain shedding of heparinbinding epidermal growth factor-like growth factor is mediated by p38 MAPK, distinct from the 12-O-tetradecanoylphorbol-13-acetateand lysophosphatidic acid-induced signaling cascades
    • Takenobu H, Yamazaki A, Hirata M, Umata T, Mekada E. The stressand inflammatory cytokine-induced ectodomain shedding of heparinbinding epidermal growth factor-like growth factor is mediated by p38 MAPK, distinct from the 12-O-tetradecanoylphorbol-13-acetateand lysophosphatidic acid-induced signaling cascades. J Biol Chem 2003;278:17255-62.
    • (2003) J Biol Chem , vol.278 , pp. 17255-17262
    • Takenobu, H.1    Yamazaki, A.2    Hirata, M.3    Umata, T.4    Mekada, E.5
  • 12
    • 0029118420 scopus 로고
    • Phorbol ester induces the rapid processing of cell surface heparin-binding EGF-like growth factor: Conversion from juxtacrine to paracrine growth factor activity
    • Goishi K, Higashiyama S, Klagsbrun M, Nakano N, Umata T, Ishikawa M, Mekada E, Taniguchi N. Phorbol ester induces the rapid processing of cell surface heparin-binding EGF-like growth factor: conversion from juxtacrine to paracrine growth factor activity. Mol Biol Cell 1995;6:967-80.
    • (1995) Mol Biol Cell , vol.6 , pp. 967-980
    • Goishi, K.1    Higashiyama, S.2    Klagsbrun, M.3    Nakano, N.4    Umata, T.5    Ishikawa, M.6    Mekada, E.7    Taniguchi, N.8
  • 13
    • 0032079871 scopus 로고    scopus 로고
    • Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C
    • Dethlefsen SM, Raab G, Moses MA, Adam RM, Klagsbrun M, Freeman MR. Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C. J Cell Biochem 1998; 69:143-53.
    • (1998) J Cell Biochem , vol.69 , pp. 143-153
    • Dethlefsen, S.M.1    Raab, G.2    Moses, M.A.3    Adam, R.M.4    Klagsbrun, M.5    Freeman, M.R.6
  • 15
    • 0033213984 scopus 로고    scopus 로고
    • The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading
    • Gechtman Z, Alonso JL, Raab G, Ingber DE, Klagsbrun M. The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading. J Biol Chem 1999;274: 28828-35.
    • (1999) J Biol Chem , vol.274 , pp. 28828-28835
    • Gechtman, Z.1    Alonso, J.L.2    Raab, G.3    Ingber, D.E.4    Klagsbrun, M.5
  • 16
    • 0033830725 scopus 로고    scopus 로고
    • Heparin-binding EGF-like growth factor: A juxtacrine growth factor
    • Iwamoto R, Mekada E. Heparin-binding EGF-like growth factor: a juxtacrine growth factor. Cytokine Growth Factor Rev 2000;11:335-44.
    • (2000) Cytokine Growth Factor Rev , vol.11 , pp. 335-344
    • Iwamoto, R.1    Mekada, E.2
  • 17
    • 1642554792 scopus 로고    scopus 로고
    • Dual intracellular signaling by proteolytic cleavage of membrane-anchored heparin-binding EGF-like growth factor
    • Nanba D, Higashiyama S. Dual intracellular signaling by proteolytic cleavage of membrane-anchored heparin-binding EGF-like growth factor. Cytokine Growth Factor Rev 2004;15:13-9.
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 13-19
    • Nanba, D.1    Higashiyama, S.2
  • 18
    • 12344262688 scopus 로고    scopus 로고
    • Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a mediator of multiple physiological and pathological pathways
    • Nishi E, Klagsbrun M. Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a mediator of multiple physiological and pathological pathways. Growth Factors 2004;22:253-60.
    • (2004) Growth Factors , vol.22 , pp. 253-260
    • Nishi, E.1    Klagsbrun, M.2
  • 19
    • 33645540607 scopus 로고    scopus 로고
    • Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy
    • Miyamoto S, Yagi H, Yotsumoto F, Kawarabayashi T, Mekada E. Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy. Cancer Sci 2006;97: 341-7.
    • (2006) Cancer Sci , vol.97 , pp. 341-347
    • Miyamoto, S.1    Yagi, H.2    Yotsumoto, F.3    Kawarabayashi, T.4    Mekada, E.5
  • 22
    • 0028860250 scopus 로고
    • Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity
    • Mitamura T, Higashiyama S, Taniguchi N, Klagsbrun M, Mekada E. Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity. J Biol Chem 1995;270:1015-9.
    • (1995) J Biol Chem , vol.270 , pp. 1015-1019
    • Mitamura, T.1    Higashiyama, S.2    Taniguchi, N.3    Klagsbrun, M.4    Mekada, E.5
  • 23
  • 24
    • 0015919833 scopus 로고
    • Diphtheria toxin and related proteins. I. Isolation and properties of mutant proteins serologically related to diphtheria toxin
    • Uchida T, Pappenheimer AM, Jr, Greany R. Diphtheria toxin and related proteins. I. Isolation and properties of mutant proteins serologically related to diphtheria toxin. J Biol Chem 1973;248:3838-44.
    • (1973) J Biol Chem , vol.248 , pp. 3838-3844
    • Uchida, T.1    Pappenheimer Jr, A.M.2    Greany, R.3
  • 26
    • 0037021437 scopus 로고    scopus 로고
    • Small interfering RNA and gene silencing in transgenic mice and rats
    • Hasuwa H, Kaseda K, Einarsdottir T, Okabe M. Small interfering RNA and gene silencing in transgenic mice and rats. FEBS Lett 2002; 532:227-30.
    • (2002) FEBS Lett , vol.532 , pp. 227-230
    • Hasuwa, H.1    Kaseda, K.2    Einarsdottir, T.3    Okabe, M.4
  • 27
    • 1642351380 scopus 로고    scopus 로고
    • In vivo establishment and characterization of a paclitaxel-resistant human ovarian cancer cell line showing enhanced growth properties and drug-resistance only in vivo
    • Okugawa K, Kobayashi H, Hirakawa T, Sonoda T, Ogura T, Nakano H. In vivo establishment and characterization of a paclitaxel-resistant human ovarian cancer cell line showing enhanced growth properties and drug-resistance only in vivo. J Cancer Res Clin Oncol 2004; 130:178-86.
    • (2004) J Cancer Res Clin Oncol , vol.130 , pp. 178-186
    • Okugawa, K.1    Kobayashi, H.2    Hirakawa, T.3    Sonoda, T.4    Ogura, T.5    Nakano, H.6
  • 28
    • 0028284810 scopus 로고
    • Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity
    • Iwamoto R, Higashiyama S, Mitamura T, Taniguchi N, Klagsbrun M, Mekada E. Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity. EMBO J 1994;13:2322-30.
    • (1994) EMBO J , vol.13 , pp. 2322-2330
    • Iwamoto, R.1    Higashiyama, S.2    Mitamura, T.3    Taniguchi, N.4    Klagsbrun, M.5    Mekada, E.6
  • 29
    • 0028963636 scopus 로고
    • The membrane protein CD9/DRAP27 potentiates the juxtacrine growth factor actiovity of the membrane-anchored heparin-binding EGF-like growth factor
    • Higashiyama S, Iwamoto R, Goishi K, Raab G, Taniguchi N, Klagsbrun M, Mekada E. The membrane protein CD9/DRAP27 potentiates the juxtacrine growth factor actiovity of the membrane-anchored heparin-binding EGF-like growth factor. J Cell Biol 1995;128:929-38.
    • (1995) J Cell Biol , vol.128 , pp. 929-938
    • Higashiyama, S.1    Iwamoto, R.2    Goishi, K.3    Raab, G.4    Taniguchi, N.5    Klagsbrun, M.6    Mekada, E.7
  • 31
    • 0029913172 scopus 로고    scopus 로고
    • Taxol-induced apoptosis and phosphorylation of Bcl-2 protein involves c-Raf-1 and represents a novel c-Raf-1 signal transduction pathway
    • Blagosklonny MV, Schulte T, Nguyen P, Trepel J, Neckers LM. Taxol-induced apoptosis and phosphorylation of Bcl-2 protein involves c-Raf-1 and represents a novel c-Raf-1 signal transduction pathway. Cancer Res 1996;56:1851-4.
    • (1996) Cancer Res , vol.56 , pp. 1851-1854
    • Blagosklonny, M.V.1    Schulte, T.2    Nguyen, P.3    Trepel, J.4    Neckers, L.M.5
  • 32
    • 0029130410 scopus 로고
    • Rapid induction of heparin-binding epidermal growth factor/diphtheria toxin receptor expression by Raf and Ras oncogenes
    • McCarthy SA, Samuels ML, Pritchard CA, Abraham JA, McMahon M. Rapid induction of heparin-binding epidermal growth factor/diphtheria toxin receptor expression by Raf and Ras oncogenes. Genes Dev 1995;9:1953-64.
    • (1995) Genes Dev , vol.9 , pp. 1953-1964
    • McCarthy, S.A.1    Samuels, M.L.2    Pritchard, C.A.3    Abraham, J.A.4    McMahon, M.5
  • 33
    • 34047153280 scopus 로고    scopus 로고
    • Heparinbinding EGF-like growth factor is an early response gene to chemotherapy and contributes to chemotherapy resistance
    • Wang F, Liu R, Lee SW, Sloss CM, Couget J, Cusack JC. Heparinbinding EGF-like growth factor is an early response gene to chemotherapy and contributes to chemotherapy resistance. Oncogene 2007; 26:2006-16.
    • (2007) Oncogene , vol.26 , pp. 2006-2016
    • Wang, F.1    Liu, R.2    Lee, S.W.3    Sloss, C.M.4    Couget, J.5    Cusack, J.C.6
  • 34
    • 0033213984 scopus 로고    scopus 로고
    • The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading
    • Goechtman Z, Alonso JL, Raab G, Ingber DE, Klagsbrun M. The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading. J Biol Chem 1999; 274:28828-35.
    • (1999) J Biol Chem , vol.274 , pp. 28828-28835
    • Goechtman, Z.1    Alonso, J.L.2    Raab, G.3    Ingber, D.E.4    Klagsbrun, M.5
  • 36
    • 0035839518 scopus 로고    scopus 로고
    • BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparinbinding EGF-like growth factor: A unique role for proHB-EGF in cell survival regulation
    • Lin J, Hutchinson L, Gaston SM, Raab G, Freeman MR. BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparinbinding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation. J Biol Chem 201;267:30127-32.
    • J Biol Chem , vol.201 , Issue.267 , pp. 30127-30132
    • Lin, J.1    Hutchinson, L.2    Gaston, S.M.3    Raab, G.4    Freeman, M.R.5
  • 37
    • 0242425875 scopus 로고    scopus 로고
    • Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF
    • Nanba D, Mammoto A, Hashimoto K, Higashiyama S. Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF. J Cell Biol 2003;163:489-502.
    • (2003) J Cell Biol , vol.163 , pp. 489-502
    • Nanba, D.1    Mammoto, A.2    Hashimoto, K.3    Higashiyama, S.4
  • 38
    • 34447529461 scopus 로고    scopus 로고
    • The carboxyl-terminal fragment of pro-HB-EGF reverses Bcl6-mediated gene repression
    • Kinugasa Y, Hieda M, Hori M, Higashiyama S. The carboxyl-terminal fragment of pro-HB-EGF reverses Bcl6-mediated gene repression. J Biol Chem 2007;282:14797-806.
    • (2007) J Biol Chem , vol.282 , pp. 14797-14806
    • Kinugasa, Y.1    Hieda, M.2    Hori, M.3    Higashiyama, S.4
  • 44
    • 0032496242 scopus 로고    scopus 로고
    • BAG-1L protein enhances androgen receptor function
    • Froesch BA, Takayama S, Reed JC. BAG-1L protein enhances androgen receptor function. J Biol Chem 1998;273:11660-6.
    • (1998) J Biol Chem , vol.273 , pp. 11660-11666
    • Froesch, B.A.1    Takayama, S.2    Reed, J.C.3
  • 45
    • 0029937303 scopus 로고    scopus 로고
    • Bcl-2 interacting protein BAG-1, binds to and activates the kinase. Raf-1
    • Wang HG, Takayama S, Rapp UR, Reed JC. Bcl-2 interacting protein BAG-1, binds to and activates the kinase. Raf-1. Proc Natl Acad Sci USA 1996;93:7063-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7063-7068
    • Wang, H.G.1    Takayama, S.2    Rapp, U.R.3    Reed, J.C.4
  • 46
    • 0344200100 scopus 로고    scopus 로고
    • A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity
    • Schneikert J, Heubner S, Martin E, Cato AC. A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. J Cell Biol 1999;146:929-40.
    • (1999) J Cell Biol , vol.146 , pp. 929-940
    • Schneikert, J.1    Heubner, S.2    Martin, E.3    Cato, A.C.4
  • 51
    • 0035133227 scopus 로고    scopus 로고
    • Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1
    • Kim AH, Khursigara G, Sun X, Franke TF, Chao MV. Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1. Mol Cell Biol 2001;21:893-901.
    • (2001) Mol Cell Biol , vol.21 , pp. 893-901
    • Kim, A.H.1    Khursigara, G.2    Sun, X.3    Franke, T.F.4    Chao, M.V.5
  • 52
    • 0037169526 scopus 로고    scopus 로고
    • Akt (protein kinase B) negatively regulates SEK1 by means of protein phosphorylation
    • Park HS, Kim MS, Huh SH, Park J, Chung J, Kang SS, Choi EJ. Akt (protein kinase B) negatively regulates SEK1 by means of protein phosphorylation. J Biol Chem 2002;277:2573-8.
    • (2002) J Biol Chem , vol.277 , pp. 2573-2578
    • Park, H.S.1    Kim, M.S.2    Huh, S.H.3    Park, J.4    Chung, J.5    Kang, S.S.6    Choi, E.J.7
  • 54
    • 0345256652 scopus 로고    scopus 로고
    • Cysplatin: Mode of cytotoxic action and molecular basis of resistance
    • Siddik ZH. Cysplatin: mode of cytotoxic action and molecular basis of resistance. Oncogene 2003;22:7265-79.
    • (2003) Oncogene , vol.22 , pp. 7265-7279
    • Siddik, Z.H.1
  • 55
    • 0034326803 scopus 로고    scopus 로고
    • Inhibition of BAD phosphorylation either at serine 112 via extracellular signal-regulated protein kinase cascade or at serine 136 via Akt cascade sensitizes human ovarian cancer cells to cisplatin
    • Hayakawa J, Ohmichi M, Kurachi H, Kanda Y, Hisamoto K, Nishio Y, Adachi K, Tasaka K, Kanzaki T, Murata Y. Inhibition of BAD phosphorylation either at serine 112 via extracellular signal-regulated protein kinase cascade or at serine 136 via Akt cascade sensitizes human ovarian cancer cells to cisplatin. Cancer Res 2000;60:5988-94.
    • (2000) Cancer Res , vol.60 , pp. 5988-5994
    • Hayakawa, J.1    Ohmichi, M.2    Kurachi, H.3    Kanda, Y.4    Hisamoto, K.5    Nishio, Y.6    Adachi, K.7    Tasaka, K.8    Kanzaki, T.9    Murata, Y.10
  • 56
    • 0033539525 scopus 로고    scopus 로고
    • A model-based approach for assessing in vivo combination therapy interactions
    • Lopez AM, Pegram MD, Slamon DJ, Landaw EM. A model-based approach for assessing in vivo combination therapy interactions. Proc Natl Acad Sci USA 1999;96:13023-8.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13023-13028
    • Lopez, A.M.1    Pegram, M.D.2    Slamon, D.J.3    Landaw, E.M.4
  • 57
  • 58
    • 0036462583 scopus 로고    scopus 로고
    • EGF receptor targeting in therapy-resistant human tumors
    • Schmidt M, Lichtner RB. EGF receptor targeting in therapy-resistant human tumors. Drug Resist Update 2002;5:11-18.
    • (2002) Drug Resist Update , vol.5 , pp. 11-18
    • Schmidt, M.1    Lichtner, R.B.2
  • 59
    • 52449113579 scopus 로고    scopus 로고
    • Suppression of proHB-EGF carboxy-terminal fragment nuclear translocation: A new molecular target therapy for gastric cancer
    • Shimura T, Kataoka H, Ogasawara N, Kubota E, Sasaki M, Tanida S, Joh T. Suppression of proHB-EGF carboxy-terminal fragment nuclear translocation: a new molecular target therapy for gastric cancer. Clin Cancer Res 2008;14:3956-65.
    • (2008) Clin Cancer Res , vol.14 , pp. 3956-3965
    • Shimura, T.1    Kataoka, H.2    Ogasawara, N.3    Kubota, E.4    Sasaki, M.5    Tanida, S.6    Joh, T.7


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