메뉴 건너뛰기




Volumn 584, Issue 12, 2010, Pages 2699-2706

Oncogenic mutant forms of EGFR: Lessons in signal transduction and targets for cancer therapy

Author keywords

EGFR; ErbB; Glioblastoma; Kinase; Lung cancer; Mutations

Indexed keywords

ANTINEOPLASTIC AGENT; CETUXIMAB; CHAPERONE; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 7; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; ERLOTINIB; GEFITINIB; HEAT SHOCK PROTEIN 90; LAPATINIB; MITOGEN ACTIVATED PROTEIN KINASE; MONOCLONAL ANTIBODY; MUTANT PROTEIN; ONCOPROTEIN; PANITUMUMAB; PEPTIDE DERIVATIVE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; TRASTUZUMAB; UNCLASSIFIED DRUG;

EID: 77953133384     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.04.019     Document Type: Review
Times cited : (139)

References (106)
  • 1
    • 0019332971 scopus 로고
    • Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes
    • Ushiro H., Cohen S. Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes. J. Biol. Chem. 1980, 255:8363-8365.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8363-8365
    • Ushiro, H.1    Cohen, S.2
  • 2
    • 0019332558 scopus 로고
    • Epidermal growth factor-receptor-protein kinase interactions. Co-purification of receptor and epidermal growth factor-enhanced phosphorylation activity
    • Cohen S., Carpenter G., King L. Epidermal growth factor-receptor-protein kinase interactions. Co-purification of receptor and epidermal growth factor-enhanced phosphorylation activity. J. Biol. Chem. 1980, 255:4834-4842.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4834-4842
    • Cohen, S.1    Carpenter, G.2    King, L.3
  • 3
    • 18644386251 scopus 로고    scopus 로고
    • Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
    • Ogiso H., et al. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 2002, 110:775-787.
    • (2002) Cell , vol.110 , pp. 775-787
    • Ogiso, H.1
  • 4
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X., Gureasko J., Shen K., Cole P.A., Kuriyan J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 2006, 125:1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 5
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ErbB signalling: towards the systems level
    • Citri A., Yarden Y. EGF-ErbB signalling: towards the systems level. Nat. Rev. Mol. Cell Biol. 2006, 7:505-516.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 6
    • 0034773992 scopus 로고    scopus 로고
    • The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities
    • Yarden Y. The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities. Eur. J. Cancer 2001, 37(Suppl. 4):S3-S8.
    • (2001) Eur. J. Cancer , vol.37 , Issue.SUPPL. 4
    • Yarden, Y.1
  • 7
    • 3442890204 scopus 로고    scopus 로고
    • Role of HER receptors family in development and differentiation
    • Casalini P., Iorio M.V., Galmozzi E., Menard S. Role of HER receptors family in development and differentiation. J. Cell. Physiol. 2004, 200:343-350.
    • (2004) J. Cell. Physiol. , vol.200 , pp. 343-350
    • Casalini, P.1    Iorio, M.V.2    Galmozzi, E.3    Menard, S.4
  • 8
    • 0033608993 scopus 로고    scopus 로고
    • The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors
    • Klapper L.N., Glathe S., Vaisman N., Hynes N.E., Andrews G.C., Sela M., Yarden Y. The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors. Proc. Natl. Acad. Sci. USA 1999, 96:4995-5000.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4995-5000
    • Klapper, L.N.1    Glathe, S.2    Vaisman, N.3    Hynes, N.E.4    Andrews, G.C.5    Sela, M.6    Yarden, Y.7
  • 11
    • 14844349947 scopus 로고
    • Epidermal growth factor and transforming growth factor-alpha: differential intracellular routing and processing of ligand-receptor complexes
    • Ebner R., Derynck R. Epidermal growth factor and transforming growth factor-alpha: differential intracellular routing and processing of ligand-receptor complexes. Cell Regul. 1991, 2:599-612.
    • (1991) Cell Regul. , vol.2 , pp. 599-612
    • Ebner, R.1    Derynck, R.2
  • 12
    • 0028358856 scopus 로고
    • Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin
    • Sliwkowski M.X., et al. Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J. Biol. Chem. 1994, 269:14661-14665.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14661-14665
    • Sliwkowski, M.X.1
  • 14
    • 0033614356 scopus 로고    scopus 로고
    • Neuregulin-4: a novel growth factor that acts through the ErbB-4 receptor tyrosine kinase
    • Harari D., Tzahar E., Romano J., Shelly M., Pierce J.H., Andrews G.C., Yarden Y. Neuregulin-4: a novel growth factor that acts through the ErbB-4 receptor tyrosine kinase. Oncogene 1999, 18:2681-2689.
    • (1999) Oncogene , vol.18 , pp. 2681-2689
    • Harari, D.1    Tzahar, E.2    Romano, J.3    Shelly, M.4    Pierce, J.H.5    Andrews, G.C.6    Yarden, Y.7
  • 15
    • 20044390355 scopus 로고    scopus 로고
    • Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity
    • Kochupurakkal B.S., et al. Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity. J. Biol. Chem. 2005, 280:8503-8512.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8503-8512
    • Kochupurakkal, B.S.1
  • 16
    • 32044464123 scopus 로고    scopus 로고
    • Epidermal growth factor receptor (EGFR) signaling in cancer
    • Normanno N., et al. Epidermal growth factor receptor (EGFR) signaling in cancer. Gene 2006, 366:2-16.
    • (2006) Gene , vol.366 , pp. 2-16
    • Normanno, N.1
  • 17
    • 0037710530 scopus 로고    scopus 로고
    • Epidermal growth factor receptor family tyrosine kinases as signal integrators and therapeutic targets
    • Barnes C.J., Kumar R. Epidermal growth factor receptor family tyrosine kinases as signal integrators and therapeutic targets. Cancer Metastasis Rev. 2003, 22:301-307.
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 301-307
    • Barnes, C.J.1    Kumar, R.2
  • 18
    • 0030772250 scopus 로고    scopus 로고
    • The autocrine loop of TGF-alpha/EGFR and brain tumors
    • Tang P., Steck P.A., Yung W.K. The autocrine loop of TGF-alpha/EGFR and brain tumors. J. Neurooncol. 1997, 35:303-314.
    • (1997) J. Neurooncol. , vol.35 , pp. 303-314
    • Tang, P.1    Steck, P.A.2    Yung, W.K.3
  • 19
    • 0021281324 scopus 로고
    • Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
    • Downward J., et al. Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences. Nature 1984, 307:521-527.
    • (1984) Nature , vol.307 , pp. 521-527
    • Downward, J.1
  • 20
    • 0026521394 scopus 로고
    • Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails
    • Ekstrand A.J., Sugawa N., James C.D., Collins V.P. Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails. Proc. Natl. Acad. Sci. USA 1992, 89:4309-4313.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4309-4313
    • Ekstrand, A.J.1    Sugawa, N.2    James, C.D.3    Collins, V.P.4
  • 21
    • 0029961912 scopus 로고    scopus 로고
    • A common mutant epidermal growth factor receptor confers enhanced tumorigenicity on human glioblastoma cells by increasing proliferation and reducing apoptosis
    • Nagane M., Coufal F., Lin H., Bogler O., Cavenee W.K., Huang H.J. A common mutant epidermal growth factor receptor confers enhanced tumorigenicity on human glioblastoma cells by increasing proliferation and reducing apoptosis. Cancer Res. 1996, 56:5079-5086.
    • (1996) Cancer Res. , vol.56 , pp. 5079-5086
    • Nagane, M.1    Coufal, F.2    Lin, H.3    Bogler, O.4    Cavenee, W.K.5    Huang, H.J.6
  • 22
    • 33845926387 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation in glioblastoma through novel missense mutations in the extracellular domain
    • Lee J.C., et al. Epidermal growth factor receptor activation in glioblastoma through novel missense mutations in the extracellular domain. PLoS Med. 2006, 3:e485.
    • (2006) PLoS Med. , vol.3
    • Lee, J.C.1
  • 23
    • 0026701674 scopus 로고
    • A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor
    • Gotoh N., Tojo A., Hino M., Yazaki Y., Shibuya M. A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor. Biochem. Biophys. Res. Commun. 1992, 186:768-774.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 768-774
    • Gotoh, N.1    Tojo, A.2    Hino, M.3    Yazaki, Y.4    Shibuya, M.5
  • 24
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib
    • Lynch T.J., et al. Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. N. Engl. J. Med. 2004, 350:2129-2139.
    • (2004) N. Engl. J. Med. , vol.350 , pp. 2129-2139
    • Lynch, T.J.1
  • 25
    • 14644406844 scopus 로고    scopus 로고
    • Somatic mutations of epidermal growth factor receptor in colorectal carcinoma
    • Nagahara H., et al. Somatic mutations of epidermal growth factor receptor in colorectal carcinoma. Clin. Cancer Res. 2005, 11:1368-1371.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 1368-1371
    • Nagahara, H.1
  • 26
    • 33744551470 scopus 로고    scopus 로고
    • Novel mutations of epidermal growth factor receptor in localized prostate cancer
    • Douglas D.A., et al. Novel mutations of epidermal growth factor receptor in localized prostate cancer. Front. Biosci. 2006, 11:2518-2525.
    • (2006) Front. Biosci. , vol.11 , pp. 2518-2525
    • Douglas, D.A.1
  • 27
    • 33947170007 scopus 로고    scopus 로고
    • EGF-independent activation of cell-surface EGF receptors harboring mutations found in gefitinib-sensitive lung cancer
    • Choi S.H., Mendrola J.M., Lemmon M.A. EGF-independent activation of cell-surface EGF receptors harboring mutations found in gefitinib-sensitive lung cancer. Oncogene 2007, 26:1567-1576.
    • (2007) Oncogene , vol.26 , pp. 1567-1576
    • Choi, S.H.1    Mendrola, J.M.2    Lemmon, M.A.3
  • 28
    • 0034163550 scopus 로고    scopus 로고
    • Diversity and frequency of epidermal growth factor receptor mutations in human glioblastomas
    • Frederick L., Wang X.Y., Eley G., James C.D. Diversity and frequency of epidermal growth factor receptor mutations in human glioblastomas. Cancer Res. 2000, 60:1383-1387.
    • (2000) Cancer Res. , vol.60 , pp. 1383-1387
    • Frederick, L.1    Wang, X.Y.2    Eley, G.3    James, C.D.4
  • 29
    • 4644289313 scopus 로고    scopus 로고
    • A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells
    • Wood E.R., et al. A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells. Cancer Res. 2004, 64:6652-6659.
    • (2004) Cancer Res. , vol.64 , pp. 6652-6659
    • Wood, E.R.1
  • 30
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • Jura N., et al. Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 2009, 137:1293-1307.
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1
  • 31
    • 9944246020 scopus 로고    scopus 로고
    • A putative mechanism for downregulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains
    • Landau M., Fleishman S.J., Ben-Tal N. A putative mechanism for downregulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains. Structure 2004, 12:2265-2275.
    • (2004) Structure , vol.12 , pp. 2265-2275
    • Landau, M.1    Fleishman, S.J.2    Ben-Tal, N.3
  • 32
    • 76849098862 scopus 로고    scopus 로고
    • Activity and cellular localization of an oncogenic glioblastoma multiforme-associated EGF receptor mutant possessing a duplicated kinase domain
    • Ozer B.H., Wiepz G.J., Bertics P.J. Activity and cellular localization of an oncogenic glioblastoma multiforme-associated EGF receptor mutant possessing a duplicated kinase domain. Oncogene 2010, 29:855-864.
    • (2010) Oncogene , vol.29 , pp. 855-864
    • Ozer, B.H.1    Wiepz, G.J.2    Bertics, P.J.3
  • 33
    • 0025114687 scopus 로고
    • Identical splicing of aberrant epidermal growth factor receptor transcripts from amplified rearranged genes in human glioblastomas
    • Sugawa N., Ekstrand A.J., James C.D., Collins V.P. Identical splicing of aberrant epidermal growth factor receptor transcripts from amplified rearranged genes in human glioblastomas. Proc. Natl. Acad. Sci. USA 1990, 87:8602-8606.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8602-8606
    • Sugawa, N.1    Ekstrand, A.J.2    James, C.D.3    Collins, V.P.4
  • 35
    • 0028800035 scopus 로고
    • Frequent expression of a mutant epidermal growth factor receptor in multiple human tumors
    • Moscatello D.K., et al. Frequent expression of a mutant epidermal growth factor receptor in multiple human tumors. Cancer Res. 1995, 55:5536-5539.
    • (1995) Cancer Res. , vol.55 , pp. 5536-5539
    • Moscatello, D.K.1
  • 36
    • 33646716077 scopus 로고    scopus 로고
    • Epidermal growth factor receptor variant III mutations in lung tumorigenesis and sensitivity to tyrosine kinase inhibitors
    • Ji H., et al. Epidermal growth factor receptor variant III mutations in lung tumorigenesis and sensitivity to tyrosine kinase inhibitors. Proc. Natl. Acad. Sci. USA 2006, 103:7817-7822.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7817-7822
    • Ji, H.1
  • 37
    • 0030832167 scopus 로고    scopus 로고
    • Cell surface localization and density of the tumor-associated variant of the epidermal growth factor receptor, EGFRvIII
    • Wikstrand C.J., McLendon R.E., Friedman A.H., Bigner D.D. Cell surface localization and density of the tumor-associated variant of the epidermal growth factor receptor, EGFRvIII. Cancer Res. 1997, 57:4130-4140.
    • (1997) Cancer Res. , vol.57 , pp. 4130-4140
    • Wikstrand, C.J.1    McLendon, R.E.2    Friedman, A.H.3    Bigner, D.D.4
  • 38
  • 39
    • 0028863853 scopus 로고
    • Epidermal growth factor ligand-independent, unregulated, cell-transforming potential of a naturally occurring human mutant EGFRvIII gene
    • Batra S.K., Castelino-Prabhu S., Wikstrand C.J., Zhu X., Humphrey P.A., Friedman H.S., Bigner D.D. Epidermal growth factor ligand-independent, unregulated, cell-transforming potential of a naturally occurring human mutant EGFRvIII gene. Cell Growth Differ. 1995, 6:1251-1259.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1251-1259
    • Batra, S.K.1    Castelino-Prabhu, S.2    Wikstrand, C.J.3    Zhu, X.4    Humphrey, P.A.5    Friedman, H.S.6    Bigner, D.D.7
  • 40
    • 43049139913 scopus 로고    scopus 로고
    • Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells
    • Al-Nedawi K., Meehan B., Micallef J., Lhotak V., May L., Guha A., Rak J. Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells. Nat. Cell Biol. 2008, 10:619-624.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 619-624
    • Al-Nedawi, K.1    Meehan, B.2    Micallef, J.3    Lhotak, V.4    May, L.5    Guha, A.6    Rak, J.7
  • 41
    • 25144448293 scopus 로고    scopus 로고
    • Mutations in the epidermal growth factor receptor gene are linked to smoking-independent, lung adenocarcinoma
    • Sonobe M., Manabe T., Wada H., Tanaka F. Mutations in the epidermal growth factor receptor gene are linked to smoking-independent, lung adenocarcinoma. Br. J. Cancer 2005, 93:355-363.
    • (2005) Br. J. Cancer , vol.93 , pp. 355-363
    • Sonobe, M.1    Manabe, T.2    Wada, H.3    Tanaka, F.4
  • 42
    • 20044364940 scopus 로고    scopus 로고
    • Clinical and biological features associated with epidermal growth factor receptor gene mutations in lung cancers
    • Shigematsu H., et al. Clinical and biological features associated with epidermal growth factor receptor gene mutations in lung cancers. J. Natl. Cancer Inst. 2005, 97:339-346.
    • (2005) J. Natl. Cancer Inst. , vol.97 , pp. 339-346
    • Shigematsu, H.1
  • 43
    • 28844501639 scopus 로고    scopus 로고
    • Somatic mutations of epidermal growth factor receptor signaling pathway in lung cancers
    • Shigematsu H., Gazdar A.F. Somatic mutations of epidermal growth factor receptor signaling pathway in lung cancers. Int. J. Cancer 2006, 118:257-262.
    • (2006) Int. J. Cancer , vol.118 , pp. 257-262
    • Shigematsu, H.1    Gazdar, A.F.2
  • 44
    • 36549085536 scopus 로고    scopus 로고
    • Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors
    • Landau M., Ben-Tal N. Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors. Biochim. Biophys. Acta 2008, 1785:12-31.
    • (2008) Biochim. Biophys. Acta , vol.1785 , pp. 12-31
    • Landau, M.1    Ben-Tal, N.2
  • 45
    • 33644500489 scopus 로고    scopus 로고
    • Distinctive activation patterns in constitutively active and gefitinib-sensitive EGFR mutants
    • Chen Y.R., Fu Y.N., Lin C.H., Yang S.T., Hu S.F., Chen Y.T., Tsai S.F., Huang S.F. Distinctive activation patterns in constitutively active and gefitinib-sensitive EGFR mutants. Oncogene 2006, 25:1205-1215.
    • (2006) Oncogene , vol.25 , pp. 1205-1215
    • Chen, Y.R.1    Fu, Y.N.2    Lin, C.H.3    Yang, S.T.4    Hu, S.F.5    Chen, Y.T.6    Tsai, S.F.7    Huang, S.F.8
  • 46
    • 0031961980 scopus 로고    scopus 로고
    • Constitutive activation of phosphatidylinositol 3-kinase by a naturally occurring mutant epidermal growth factor receptor
    • Moscatello D.K., Holgado-Madruga M., Emlet D.R., Montgomery R.B., Wong A.J. Constitutive activation of phosphatidylinositol 3-kinase by a naturally occurring mutant epidermal growth factor receptor. J. Biol. Chem. 1998, 273:200-206.
    • (1998) J. Biol. Chem. , vol.273 , pp. 200-206
    • Moscatello, D.K.1    Holgado-Madruga, M.2    Emlet, D.R.3    Montgomery, R.B.4    Wong, A.J.5
  • 47
    • 3042581834 scopus 로고    scopus 로고
    • Mutant epidermal growth factor receptor displays increased signaling through the phosphatidylinositol-3 kinase/AKT pathway and promotes radioresistance in cells of astrocytic origin
    • Li B., Yuan M., Kim I.A., Chang C.M., Bernhard E.J., Shu H.K. Mutant epidermal growth factor receptor displays increased signaling through the phosphatidylinositol-3 kinase/AKT pathway and promotes radioresistance in cells of astrocytic origin. Oncogene 2004, 23:4594-4602.
    • (2004) Oncogene , vol.23 , pp. 4594-4602
    • Li, B.1    Yuan, M.2    Kim, I.A.3    Chang, C.M.4    Bernhard, E.J.5    Shu, H.K.6
  • 49
    • 26444474990 scopus 로고    scopus 로고
    • Analysis of the epidermal growth factor receptor specific transcriptome: effect of receptor expression level and an activating mutation
    • Pedersen M.W., et al. Analysis of the epidermal growth factor receptor specific transcriptome: effect of receptor expression level and an activating mutation. J. Cell. Biochem. 2005, 96:412-427.
    • (2005) J. Cell. Biochem. , vol.96 , pp. 412-427
    • Pedersen, M.W.1
  • 50
    • 35549013373 scopus 로고    scopus 로고
    • Defective ubiquitinylation of EGFR mutants of lung cancer confers prolonged signaling
    • Shtiegman K., et al. Defective ubiquitinylation of EGFR mutants of lung cancer confers prolonged signaling. Oncogene 2007, 26:6968-6978.
    • (2007) Oncogene , vol.26 , pp. 6968-6978
    • Shtiegman, K.1
  • 51
    • 43749096126 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation in prostate cancer by three novel missense mutations
    • Cai C.Q., et al. Epidermal growth factor receptor activation in prostate cancer by three novel missense mutations. Oncogene 2008, 27:3201-3210.
    • (2008) Oncogene , vol.27 , pp. 3201-3210
    • Cai, C.Q.1
  • 52
    • 33748066632 scopus 로고    scopus 로고
    • Kinetic analysis of epidermal growth factor receptor somatic mutant proteins shows increased sensitivity to the epidermal growth factor receptor tyrosine kinase inhibitor, erlotinib
    • Carey K.D., et al. Kinetic analysis of epidermal growth factor receptor somatic mutant proteins shows increased sensitivity to the epidermal growth factor receptor tyrosine kinase inhibitor, erlotinib. Cancer Res. 2006, 66:8163-8171.
    • (2006) Cancer Res. , vol.66 , pp. 8163-8171
    • Carey, K.D.1
  • 53
    • 0034066072 scopus 로고    scopus 로고
    • Disorders in cell circuitry during multistage carcinogenesis: the role of homeostasis
    • Weinstein I.B. Disorders in cell circuitry during multistage carcinogenesis: the role of homeostasis. Carcinogenesis 2000, 21:857-864.
    • (2000) Carcinogenesis , vol.21 , pp. 857-864
    • Weinstein, I.B.1
  • 54
    • 33746388176 scopus 로고    scopus 로고
    • " Oncogenic shock": explaining oncogene addiction through differential signal attenuation
    • Sharma S.V., Fischbach M.A., Haber D.A., Settleman J. " Oncogenic shock": explaining oncogene addiction through differential signal attenuation. Clin. Cancer Res. 2006, 12:4392s-4395s.
    • (2006) Clin. Cancer Res. , vol.12
    • Sharma, S.V.1    Fischbach, M.A.2    Haber, D.A.3    Settleman, J.4
  • 55
    • 33746347333 scopus 로고    scopus 로고
    • Tyrphostins and other tyrosine kinase inhibitors
    • Levitzki A., Mishani E. Tyrphostins and other tyrosine kinase inhibitors. Annu. Rev. Biochem. 2006, 75:93-109.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 93-109
    • Levitzki, A.1    Mishani, E.2
  • 56
    • 3042619127 scopus 로고    scopus 로고
    • The role of erlotinib (Tarceva, OSI 774) in the treatment of non-small cell lung cancer
    • Perez-Soler R. The role of erlotinib (Tarceva, OSI 774) in the treatment of non-small cell lung cancer. Clin. Cancer Res. 2004, 10:4238s-4240s.
    • (2004) Clin. Cancer Res. , vol.10
    • Perez-Soler, R.1
  • 57
    • 0012381722 scopus 로고    scopus 로고
    • Multi-institutional randomized phase II trial of gefitinib for previously treated patients with advanced non-small-cell lung cancer (The IDEAL 1 Trial) [corrected]
    • Fukuoka M., et al. Multi-institutional randomized phase II trial of gefitinib for previously treated patients with advanced non-small-cell lung cancer (The IDEAL 1 Trial) [corrected]. J. Clin. Oncol. 2003, 21:2237-2246.
    • (2003) J. Clin. Oncol. , vol.21 , pp. 2237-2246
    • Fukuoka, M.1
  • 58
    • 34249933404 scopus 로고    scopus 로고
    • Erlotinib plus gemcitabine compared with gemcitabine alone in patients with advanced pancreatic cancer: a phase III trial of the National Cancer Institute of Canada Clinical Trials Group
    • Moore M.J., et al. Erlotinib plus gemcitabine compared with gemcitabine alone in patients with advanced pancreatic cancer: a phase III trial of the National Cancer Institute of Canada Clinical Trials Group. J. Clin. Oncol. 2007, 25:1960-1966.
    • (2007) J. Clin. Oncol. , vol.25 , pp. 1960-1966
    • Moore, M.J.1
  • 59
    • 53949121341 scopus 로고    scopus 로고
    • Gemcitabine combined with gefitinib in patients with inoperable or metastatic pancreatic cancer: a phase II Study of the Hellenic Cooperative Oncology Group with biomarker evaluation
    • Fountzilas G., et al. Gemcitabine combined with gefitinib in patients with inoperable or metastatic pancreatic cancer: a phase II Study of the Hellenic Cooperative Oncology Group with biomarker evaluation. Cancer Invest. 2008, 26:784-793.
    • (2008) Cancer Invest. , vol.26 , pp. 784-793
    • Fountzilas, G.1
  • 60
    • 33845886440 scopus 로고    scopus 로고
    • Lapatinib plus capecitabine for HER2-positive advanced breast cancer
    • Geyer C.E., et al. Lapatinib plus capecitabine for HER2-positive advanced breast cancer. N. Engl. J. Med. 2006, 355:2733-2743.
    • (2006) N. Engl. J. Med. , vol.355 , pp. 2733-2743
    • Geyer, C.E.1
  • 61
    • 77949884661 scopus 로고    scopus 로고
    • Randomized study of Lapatinib alone or in combination with trastuzumab in women with ErbB2-positive, trastuzumab-refractory metastatic breast cancer
    • Blackwell K.L., et al. Randomized study of Lapatinib alone or in combination with trastuzumab in women with ErbB2-positive, trastuzumab-refractory metastatic breast cancer. J. Clin. Oncol. 2010, 28:1124-1130.
    • (2010) J. Clin. Oncol. , vol.28 , pp. 1124-1130
    • Blackwell, K.L.1
  • 62
    • 0032850677 scopus 로고    scopus 로고
    • Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease
    • Cobleigh M.A., et al. Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease. J. Clin. Oncol. 1999, 17:2639-2648.
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2639-2648
    • Cobleigh, M.A.1
  • 63
    • 0035869407 scopus 로고    scopus 로고
    • Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2
    • Slamon D.J., et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N. Engl. J. Med. 2001, 344:783-792.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 783-792
    • Slamon, D.J.1
  • 64
    • 26844536978 scopus 로고    scopus 로고
    • Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer
    • Romond E.H., et al. Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer. N. Engl. J. Med. 2005, 353:1673-1684.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 1673-1684
    • Romond, E.H.1
  • 65
    • 26844503270 scopus 로고    scopus 로고
    • Trastuzumab after adjuvant chemotherapy in HER2-positive breast cancer
    • Piccart-Gebhart M.J., et al. Trastuzumab after adjuvant chemotherapy in HER2-positive breast cancer. N. Engl. J. Med. 2005, 353:1659-1672.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 1659-1672
    • Piccart-Gebhart, M.J.1
  • 66
    • 34248641115 scopus 로고    scopus 로고
    • Cancer therapeutic antibodies come of age: targeting minimal residual disease
    • Ben-Kasus T., Schechter B., Sela M., Yarden Y. Cancer therapeutic antibodies come of age: targeting minimal residual disease. Mol. Oncol. 2007, 1:42-54.
    • (2007) Mol. Oncol. , vol.1 , pp. 42-54
    • Ben-Kasus, T.1    Schechter, B.2    Sela, M.3    Yarden, Y.4
  • 67
    • 0034076307 scopus 로고    scopus 로고
    • Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets
    • Clynes R.A., Towers T.L., Presta L.G., Ravetch J.V. Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets. Nat. Med. 2000, 6:443-446.
    • (2000) Nat. Med. , vol.6 , pp. 443-446
    • Clynes, R.A.1    Towers, T.L.2    Presta, L.G.3    Ravetch, J.V.4
  • 68
    • 65349116059 scopus 로고    scopus 로고
    • Cetuximab plus chemotherapy in patients with advanced non-small-cell lung cancer (FLEX): an open-label randomised phase III trial
    • Pirker R., et al. Cetuximab plus chemotherapy in patients with advanced non-small-cell lung cancer (FLEX): an open-label randomised phase III trial. Lancet 2009, 373:1525-1531.
    • (2009) Lancet , vol.373 , pp. 1525-1531
    • Pirker, R.1
  • 69
    • 42649145667 scopus 로고    scopus 로고
    • Wild-type KRAS is required for panitumumab efficacy in patients with metastatic colorectal cancer
    • Amado R.G., et al. Wild-type KRAS is required for panitumumab efficacy in patients with metastatic colorectal cancer. J. Clin. Oncol. 2008, 26:1626-1634.
    • (2008) J. Clin. Oncol. , vol.26 , pp. 1626-1634
    • Amado, R.G.1
  • 70
    • 63549091810 scopus 로고    scopus 로고
    • Review article: panitumumab - a fully human anti-EGFR monoclonal antibody for treatment of metastatic colorectal cancer
    • Peeters M., Balfour J., Arnold D. Review article: panitumumab - a fully human anti-EGFR monoclonal antibody for treatment of metastatic colorectal cancer. Aliment. Pharmacol. Ther. 2008.
    • (2008) Aliment. Pharmacol. Ther.
    • Peeters, M.1    Balfour, J.2    Arnold, D.3
  • 71
    • 34247251270 scopus 로고    scopus 로고
    • A phase I clinical trial with monoclonal antibody ch806 targeting transitional state and mutant epidermal growth factor receptors
    • Scott A.M., et al. A phase I clinical trial with monoclonal antibody ch806 targeting transitional state and mutant epidermal growth factor receptors. Proc. Natl. Acad. Sci. USA 2007, 104:4071-4076.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4071-4076
    • Scott, A.M.1
  • 72
    • 0141790037 scopus 로고    scopus 로고
    • Epidermal growth factor receptor VIII peptide vaccination is efficacious against established intracerebral tumors
    • Heimberger A.B., et al. Epidermal growth factor receptor VIII peptide vaccination is efficacious against established intracerebral tumors. Clin. Cancer Res. 2003, 9:4247-4254.
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4247-4254
    • Heimberger, A.B.1
  • 73
    • 33846213523 scopus 로고    scopus 로고
    • Retargeted oncolytic measles strains entering via the EGFRvIII receptor maintain significant antitumor activity against gliomas with increased tumor specificity
    • Allen C., et al. Retargeted oncolytic measles strains entering via the EGFRvIII receptor maintain significant antitumor activity against gliomas with increased tumor specificity. Cancer Res. 2006, 66:11840-11850.
    • (2006) Cancer Res. , vol.66 , pp. 11840-11850
    • Allen, C.1
  • 74
    • 33847406095 scopus 로고    scopus 로고
    • Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity
    • Yun C.H., Boggon T.J., Li Y., Woo M.S., Greulich H., Meyerson M., Eck M.J. Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell 2007, 11:217-227.
    • (2007) Cancer Cell , vol.11 , pp. 217-227
    • Yun, C.H.1    Boggon, T.J.2    Li, Y.3    Woo, M.S.4    Greulich, H.5    Meyerson, M.6    Eck, M.J.7
  • 75
    • 13844317894 scopus 로고    scopus 로고
    • EGFR mutation and resistance of non-small-cell lung cancer to gefitinib
    • Kobayashi S., et al. EGFR mutation and resistance of non-small-cell lung cancer to gefitinib. N. Engl. J. Med. 2005, 352:786-792.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 786-792
    • Kobayashi, S.1
  • 76
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao W., Miller V.A., Politi K.A., Riely G.J., Somwar R., Zakowski M.F., Kris M.G., Varmus H. Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain. PLoS Med. 2005, 2:e73.
    • (2005) PLoS Med. , vol.2
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3    Riely, G.J.4    Somwar, R.5    Zakowski, M.F.6    Kris, M.G.7    Varmus, H.8
  • 77
    • 28444455958 scopus 로고    scopus 로고
    • Inherited susceptibility to lung cancer may be associated with the T790M drug resistance mutation in EGFR
    • Bell D.W., et al. Inherited susceptibility to lung cancer may be associated with the T790M drug resistance mutation in EGFR. Nat. Genet. 2005, 37:1315-1316.
    • (2005) Nat. Genet. , vol.37 , pp. 1315-1316
    • Bell, D.W.1
  • 78
    • 27744606737 scopus 로고    scopus 로고
    • Molecular determinants of the response of glioblastomas to EGFR kinase inhibitors
    • Mellinghoff I.K., et al. Molecular determinants of the response of glioblastomas to EGFR kinase inhibitors. N. Engl. J. Med. 2005, 353:2012-2024.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 2012-2024
    • Mellinghoff, I.K.1
  • 79
    • 40949135397 scopus 로고    scopus 로고
    • PIK3CA mutation/PTEN expression status predicts response of colon cancer cells to the epidermal growth factor receptor inhibitor cetuximab
    • Jhawer M., et al. PIK3CA mutation/PTEN expression status predicts response of colon cancer cells to the epidermal growth factor receptor inhibitor cetuximab. Cancer Res. 2008, 68:1953-1961.
    • (2008) Cancer Res. , vol.68 , pp. 1953-1961
    • Jhawer, M.1
  • 80
    • 33646228635 scopus 로고    scopus 로고
    • KRAS mutation status is predictive of response to cetuximab therapy in colorectal cancer
    • Lievre A., et al. KRAS mutation status is predictive of response to cetuximab therapy in colorectal cancer. Cancer Res. 2006, 66:3992-3995.
    • (2006) Cancer Res. , vol.66 , pp. 3992-3995
    • Lievre, A.1
  • 81
    • 73349094741 scopus 로고    scopus 로고
    • Analysis of PTEN, BRAF, and EGFR status in determining benefit from cetuximab therapy in wild-type KRAS metastatic colon cancer
    • Laurent-Puig P., et al. Analysis of PTEN, BRAF, and EGFR status in determining benefit from cetuximab therapy in wild-type KRAS metastatic colon cancer. J. Clin. Oncol. 2009, 27:5924-5930.
    • (2009) J. Clin. Oncol. , vol.27 , pp. 5924-5930
    • Laurent-Puig, P.1
  • 82
    • 10844231985 scopus 로고    scopus 로고
    • Mutations of the epidermal growth factor receptor gene in lung cancer: biological and clinical implications
    • Kosaka T., Yatabe Y., Endoh H., Kuwano H., Takahashi T., Mitsudomi T. Mutations of the epidermal growth factor receptor gene in lung cancer: biological and clinical implications. Cancer Res. 2004, 64:8919-8923.
    • (2004) Cancer Res. , vol.64 , pp. 8919-8923
    • Kosaka, T.1    Yatabe, Y.2    Endoh, H.3    Kuwano, H.4    Takahashi, T.5    Mitsudomi, T.6
  • 83
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl L.H., Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75:271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 84
    • 1842782331 scopus 로고    scopus 로고
    • Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance
    • Sangster T.A., Lindquist S., Queitsch C. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays 2004, 26:348-362.
    • (2004) Bioessays , vol.26 , pp. 348-362
    • Sangster, T.A.1    Lindquist, S.2    Queitsch, C.3
  • 85
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation
    • Whitesell L., Mimnaugh E.G., De Costa B., Myers C.E., Neckers L.M. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 1994, 91:8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 86
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An W.G., Schulte T.W., Neckers L.M. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ. 2000, 11:355-360.
    • (2000) Cell Growth Differ. , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 87
    • 33644694046 scopus 로고    scopus 로고
    • Hsp90 inhibitor 17-AAG reduces ErbB2 levels and inhibits proliferation of the trastuzumab resistant breast tumor cell line JIMT-1
    • Zsebik B., Citri A., Isola J., Yarden Y., Szollosi J., Vereb G. Hsp90 inhibitor 17-AAG reduces ErbB2 levels and inhibits proliferation of the trastuzumab resistant breast tumor cell line JIMT-1. Immunol. Lett. 2006, 104:146-155.
    • (2006) Immunol. Lett. , vol.104 , pp. 146-155
    • Zsebik, B.1    Citri, A.2    Isola, J.3    Yarden, Y.4    Szollosi, J.5    Vereb, G.6
  • 88
    • 22244485706 scopus 로고    scopus 로고
    • Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins
    • Shimamura T., Lowell A.M., Engelman J.A., Shapiro G.I. Epidermal growth factor receptors harboring kinase domain mutations associate with the heat shock protein 90 chaperone and are destabilized following exposure to geldanamycins. Cancer Res. 2005, 65:6401-6408.
    • (2005) Cancer Res. , vol.65 , pp. 6401-6408
    • Shimamura, T.1    Lowell, A.M.2    Engelman, J.A.3    Shapiro, G.I.4
  • 89
    • 44649083135 scopus 로고    scopus 로고
    • Hsp90 inhibition suppresses mutant EGFR-T790M signaling and overcomes kinase inhibitor resistance
    • Shimamura T., et al. Hsp90 inhibition suppresses mutant EGFR-T790M signaling and overcomes kinase inhibitor resistance. Cancer Res. 2008, 68:5827-5838.
    • (2008) Cancer Res. , vol.68 , pp. 5827-5838
    • Shimamura, T.1
  • 90
    • 0012999148 scopus 로고    scopus 로고
    • Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII
    • Lavictoire S.J., Parolin D.A., Klimowicz A.C., Kelly J.F., Lorimer I.A. Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII. J. Biol. Chem. 2003, 278:5292-5299.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5292-5299
    • Lavictoire, S.J.1    Parolin, D.A.2    Klimowicz, A.C.3    Kelly, J.F.4    Lorimer, I.A.5
  • 91
    • 33746899628 scopus 로고    scopus 로고
    • Association with HSP90 inhibits Cbl-mediated down-regulation of mutant epidermal growth factor receptors
    • Yang S., Qu S., Perez-Tores M., Sawai A., Rosen N., Solit D.B., Arteaga C.L. Association with HSP90 inhibits Cbl-mediated down-regulation of mutant epidermal growth factor receptors. Cancer Res. 2006, 66:6990-6997.
    • (2006) Cancer Res. , vol.66 , pp. 6990-6997
    • Yang, S.1    Qu, S.2    Perez-Tores, M.3    Sawai, A.4    Rosen, N.5    Solit, D.B.6    Arteaga, C.L.7
  • 93
    • 0017167185 scopus 로고
    • The clonal evolution of tumor cell populations
    • Nowell P.C. The clonal evolution of tumor cell populations. Science 1976, 194:23-28.
    • (1976) Science , vol.194 , pp. 23-28
    • Nowell, P.C.1
  • 95
    • 12344318499 scopus 로고    scopus 로고
    • Expanding fields of genetically altered cells in head and neck squamous carcinogenesis
    • Braakhuis B.J., Leemans C.R., Brakenhoff R.H. Expanding fields of genetically altered cells in head and neck squamous carcinogenesis. Semin. Cancer Biol. 2005, 15:113-120.
    • (2005) Semin. Cancer Biol. , vol.15 , pp. 113-120
    • Braakhuis, B.J.1    Leemans, C.R.2    Brakenhoff, R.H.3
  • 96
    • 72949092456 scopus 로고    scopus 로고
    • Novel mutant-selective EGFR kinase inhibitors against EGFR T790M
    • Zhou W., et al. Novel mutant-selective EGFR kinase inhibitors against EGFR T790M. Nature 2009, 462:1070-1074.
    • (2009) Nature , vol.462 , pp. 1070-1074
    • Zhou, W.1
  • 97
    • 33846552656 scopus 로고    scopus 로고
    • Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3
    • Sergina N.V., Rausch M., Wang D., Blair J., Hann B., Shokat K.M., Moasser M.M. Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3. Nature 2007, 445:437-441.
    • (2007) Nature , vol.445 , pp. 437-441
    • Sergina, N.V.1    Rausch, M.2    Wang, D.3    Blair, J.4    Hann, B.5    Shokat, K.M.6    Moasser, M.M.7
  • 98
    • 34249075147 scopus 로고    scopus 로고
    • MET amplification leads to gefitinib resistance in lung cancer by activating ErbB3 signaling
    • Engelman J.A., et al. MET amplification leads to gefitinib resistance in lung cancer by activating ErbB3 signaling. Science 2007, 316:1039-1043.
    • (2007) Science , vol.316 , pp. 1039-1043
    • Engelman, J.A.1
  • 99
    • 0021332973 scopus 로고
    • Retinoblastoma: clues to human oncogenesis
    • Murphree A.L., Benedict W.F. Retinoblastoma: clues to human oncogenesis. Science 1984, 223:1028-1033.
    • (1984) Science , vol.223 , pp. 1028-1033
    • Murphree, A.L.1    Benedict, W.F.2
  • 100
    • 33847405751 scopus 로고    scopus 로고
    • Inhibition of fibroblast to myofibroblast transition by halofuginone contributes to the chemotherapy-mediated antitumoral effect
    • Sheffer Y., et al. Inhibition of fibroblast to myofibroblast transition by halofuginone contributes to the chemotherapy-mediated antitumoral effect. Mol. Cancer Ther. 2007, 6:570-577.
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 570-577
    • Sheffer, Y.1
  • 101
    • 33947732977 scopus 로고    scopus 로고
    • Angiogenesis: an organizing principle for drug discovery?
    • Folkman J. Angiogenesis: an organizing principle for drug discovery?. Nat. Rev. Drug Discov. 2007, 6:273-286.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 273-286
    • Folkman, J.1
  • 102
    • 69849106072 scopus 로고    scopus 로고
    • Quality of life and disease-related symptoms in previously treated Japanese patients with non-small-cell lung cancer: results of a randomized phase III study (V-15-32) of gefitinib versus docetaxel
    • Sekine I., et al. Quality of life and disease-related symptoms in previously treated Japanese patients with non-small-cell lung cancer: results of a randomized phase III study (V-15-32) of gefitinib versus docetaxel. Ann. Oncol. 2009, 20:1483-1488.
    • (2009) Ann. Oncol. , vol.20 , pp. 1483-1488
    • Sekine, I.1
  • 103
    • 69949162760 scopus 로고    scopus 로고
    • Gefitinib or carboplatin-paclitaxel in pulmonary adenocarcinoma
    • Mok T.S., et al. Gefitinib or carboplatin-paclitaxel in pulmonary adenocarcinoma. N. Engl. J. Med. 2009, 361:947-957.
    • (2009) N. Engl. J. Med. , vol.361 , pp. 947-957
    • Mok, T.S.1
  • 104
    • 0025993791 scopus 로고
    • Deletion-mutant epidermal growth factor receptor in human gliomas: effects of type II mutation on receptor function
    • Humphrey P.A., et al. Deletion-mutant epidermal growth factor receptor in human gliomas: effects of type II mutation on receptor function. Biochem. Biophys. Res. Commun. 1991, 178:1413-1420.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 1413-1420
    • Humphrey, P.A.1
  • 105
    • 2342624080 scopus 로고    scopus 로고
    • EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy
    • Paez J.G., et al. EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy. Science 2004, 304:1497-1500.
    • (2004) Science , vol.304 , pp. 1497-1500
    • Paez, J.G.1
  • 106
    • 28444478439 scopus 로고    scopus 로고
    • Oncogenic transformation by inhibitor-sensitive and -resistant EGFR mutants
    • Greulich H., et al. Oncogenic transformation by inhibitor-sensitive and -resistant EGFR mutants. PLoS Med. 2005, 2:e313.
    • (2005) PLoS Med. , vol.2
    • Greulich, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.