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Volumn 79, Issue , 2014, Pages 34-74

The ErbB/HER family of protein-tyrosine kinases and cancer

Author keywords

Breast cancer; Colorectal cancer; Monoclonal antibody therapy; Non small cell lung cancer; Small molecule protein kinase inhibitor; Targeted cancer therapy

Indexed keywords

AFATINIB; ANTINEOPLASTIC AGENT; BLEOMYCIN; CAPECITABINE; CARBOPLATIN; CETUXIMAB; CYTOTOXIC AGENT; DACTINOMYCIN; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; ERLOTINIB; GEFITINIB; HETERODIMER; HOMODIMER; LAPATINIB; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PANITUMUMAB; PERTUZUMAB; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C GAMMA; PROTEIN KINASE B; PROTEIN TYROSINE KINASE; RAF PROTEIN; RAS PROTEIN; TRASTUZUMAB; TRASTUZUMAB EMTANSINE; UNINDEXED DRUG;

EID: 84890041471     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2013.11.002     Document Type: Review
Times cited : (1049)

References (305)
  • 1
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • M.A. Lemmon, and J. Schlessinger Cell signaling by receptor tyrosine kinases Cell 141 2010 1117 1134
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 2
    • 0020583891 scopus 로고
    • The epidermal growth factor (EGF)
    • S. Cohen The epidermal growth factor (EGF) Cancer 51 1983 1787 1791 (Pubitemid 13093942)
    • (1983) Cancer , vol.51 , Issue.10 , pp. 1787-1791
    • Cohen, S.1
  • 4
    • 0020068317 scopus 로고
    • A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles
    • S. Cohen, H. Ushiro, C. Stoscheck, and M. Chinkers A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles J Biol Chem 257 1982 1523 1531 (Pubitemid 12121664)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.3 , pp. 1523-1531
    • Cohen, S.1    Ushiro, H.2    Stoscheck, C.3    Chinkers, M.4
  • 5
    • 0022168220 scopus 로고
    • The EGF receptor: Structure, regulation, and potential role in malignancy
    • D.M. Thompson, and G.N. Gill The EGF receptor: structure, regulation, and potential role in malignancy Cancer Surv 4 1985 767 788
    • (1985) Cancer Surv , vol.4 , pp. 767-788
    • Thompson, D.M.1    Gill, G.N.2
  • 6
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • G. Manning, D.B. Whyte, R. Martinez, T. Hunter, and S. Sudarsanam The protein kinase complement of the human genome Science 298 2002 1912 1934 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 9
    • 0036210469 scopus 로고    scopus 로고
    • Rules and guidelines for mouse gene, allele, and mutation nomenclature: A condensed version
    • DOI 10.1006/geno.2002.6747
    • L.J. Maltais, J.A. Blake, T. Chu, C.M. Lutz, J.T. Eppig, and I. Jackson Rules and guidelines for mouse gene, allele, and mutation nomenclature: a condensed version Genomics 79 2002 471 474 (Pubitemid 34274284)
    • (2002) Genomics , vol.79 , Issue.4 , pp. 471-474
    • Maltais, L.J.1    Blake, J.A.2    Chu, T.3    Lutz, C.M.4    Eppig, J.T.5    Jackson, I.6
  • 11
    • 0021688634 scopus 로고
    • The neu oncogene: An erb-B-related gene encoding a 185,000-M(r) tumour antigen
    • DOI 10.1038/312513a0
    • A.L. Schechter, D.F. Stern, L. Vaidyanathan, S.J. Decker, J.A. Drebin, and M.I. Greene The neu oncogene: an erb-B-related gene encoding a 185,000-Mr tumour antigen Nature 312 1984 513 516 (Pubitemid 15182278)
    • (1984) Nature , vol.312 , Issue.5994 , pp. 513-516
    • Schechter, A.L.1    Stern, D.F.2    Vaidyanathan, L.3
  • 12
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • DOI 10.1038/nrm1962, PII NRM1962
    • A. Citri, and Y. Yarden EGF-ERBB signalling: towards the systems level Nat Rev Mol Cell Biol 7 2006 505 516 (Pubitemid 44036456)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 13
    • 34247863773 scopus 로고    scopus 로고
    • The neuregulin-I/ErbB signaling system in development and disease
    • S. Britsch The neuregulin-I/ErbB signaling system in development and disease Adv Anat Embryol Cell Biol 190 2007 1 6
    • (2007) Adv Anat Embryol Cell Biol , vol.190 , pp. 1-6
    • Britsch, S.1
  • 15
    • 0029074587 scopus 로고
    • Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor
    • P.J. Miettinen, J.E. Berger, J. Meneses, Y. Phung, R.A. Pedersen, and Z. Werb Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor Nature 376 1995 337 341
    • (1995) Nature , vol.376 , pp. 337-341
    • Miettinen, P.J.1    Berger, J.E.2    Meneses, J.3    Phung, Y.4    Pedersen, R.A.5    Werb, Z.6
  • 16
    • 0029064203 scopus 로고
    • Targeted disruption of mouse EGF receptor: Effect of genetic background on mutant phenotype
    • D.W. Threadgill, A.A. Dlugosz, L.A. Hansen, T. Tennenbaum, U. Lichti, and D. Yee Targeted disruption of mouse EGF receptor: effect of genetic background on mutant phenotype Science 269 1995 230 234
    • (1995) Science , vol.269 , pp. 230-234
    • Threadgill, D.W.1    Dlugosz, A.A.2    Hansen, L.A.3    Tennenbaum, T.4    Lichti, U.5    Yee, D.6
  • 17
    • 0028785406 scopus 로고
    • Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor
    • M. Gassmann, F. Casagranda, D. Orioli, H. Simon, C. Lai, and R. Klein Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor Nature 378 1995 390 394
    • (1995) Nature , vol.378 , pp. 390-394
    • Gassmann, M.1    Casagranda, F.2    Orioli, D.3    Simon, H.4    Lai, C.5    Klein, R.6
  • 18
    • 0028884413 scopus 로고
    • Requirement for neuregulin receptor erbB2 in neural and cardiac development
    • K.F. Lee, H. Simon, H. Chen, B. Bates, M.C. Hung, and C. Hauser Requirement for neuregulin receptor erbB2 in neural and cardiac development Nature 378 1995 394 398
    • (1995) Nature , vol.378 , pp. 394-398
    • Lee, K.F.1    Simon, H.2    Chen, H.3    Bates, B.4    Hung, M.C.5    Hauser, C.6
  • 20
    • 0021273420 scopus 로고
    • Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
    • A. Ullrich, L. Coussens, J.S. Hayflick, T.J. Dull, A. Gray, and A.W. Tam Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells Nature 309 1984 418 425 (Pubitemid 14102443)
    • (1984) Nature , vol.309 , Issue.5967 , pp. 418-425
    • Ullrich, A.1    Coussens, L.2    Hayflick, J.S.3
  • 21
    • 0030685131 scopus 로고    scopus 로고
    • A novel juxtamembrane domain isoform of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester
    • DOI 10.1074/jbc.272.42.26761
    • K. Elenius, G. Corfas, S. Paul, C.J. Choi, C. Rio, and G.D. Plowman A novel juxtamembrane domain isoform of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester J Biol Chem 272 1997 26761 26768 (Pubitemid 27458905)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.42 , pp. 26761-26768
    • Elenius, K.1    Corfas, G.2    Paul, S.3    Choi, C.J.4    Rio, C.5    Plowman, G.D.6    Klagsbrun, M.7
  • 22
    • 79952233837 scopus 로고    scopus 로고
    • Trastuzumab has preferential activity against breast cancers driven by ERBB2 homodimers
    • R. Ghosh, A. Narasanna, S.E. Wang, S. Liu, A. Chakrabarty, and J.M. Balko Trastuzumab has preferential activity against breast cancers driven by ERBB2 homodimers Cancer Res 71 2011 1871 1882
    • (2011) Cancer Res , vol.71 , pp. 1871-1882
    • Ghosh, R.1    Narasanna, A.2    Wang, S.E.3    Liu, S.4    Chakrabarty, A.5    Balko, J.M.6
  • 23
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • F. Shi, S.E. Telesco, Y. Liu, R. Radhakrishnan, and M.A. Lemmon ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation Proc Natl Acad Sci USA 107 2010 7692 7697
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7692-7697
    • Shi, F.1    Telesco, S.E.2    Liu, Y.3    Radhakrishnan, R.4    Lemmon, M.A.5
  • 24
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor
    • E. Tzahar, H. Waterman, X. Chen, G. Levkowitz, D. Karunagaran, and S. Lavi A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor Mol Cell Biol 16 1996 5276 5287 (Pubitemid 26315047)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3    Levkowitz, G.4    Karunagaran, D.5    Lavi, S.6    Ratzkin, B.J.7    Yarden, Y.8
  • 25
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • DOI 10.1093/emboj/16.7.1647
    • D. Graus-Porta, R.R. Beerli, J.M. Daly, and N.E. Hynes ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling EMBO J 16 1997 1647 1655 (Pubitemid 27151960)
    • (1997) EMBO Journal , vol.16 , Issue.7 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 27
    • 0034959016 scopus 로고    scopus 로고
    • The Type 1 growth factor receptors and their ligands considered as a complex system
    • DOI 10.1677/erc.0.0080075
    • W.J. Gullick The Type 1 growth factor receptors and their ligands considered as a complex system Endocr Relat Cancer 8 2001 75 82 (Pubitemid 32641350)
    • (2001) Endocrine-Related Cancer , vol.8 , Issue.2 , pp. 75-82
    • Gullick, W.J.1
  • 28
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in egfr signalling and development
    • DOI 10.1038/nrm1548
    • C.P. Blobel ADAMs: key components in EGFR signalling and development Nat Rev Mol Cell Biol 6 2005 32 43 (Pubitemid 40064897)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 32-43
    • Blobel, C.P.1
  • 30
    • 79960923986 scopus 로고    scopus 로고
    • ADAM17: A molecular switch to control inflammation and tissue regeneration
    • J. Scheller, A. Chalaris, C. Garbers, and S. Rose-John ADAM17: a molecular switch to control inflammation and tissue regeneration Trends Immunol 32 2011 380 387
    • (2011) Trends Immunol , vol.32 , pp. 380-387
    • Scheller, J.1    Chalaris, A.2    Garbers, C.3    Rose-John, S.4
  • 31
    • 84876110045 scopus 로고    scopus 로고
    • ADAM17, shedding, TACE as therapeutic targets
    • S. Rose-John ADAM17, shedding, TACE as therapeutic targets Pharmacol Res 71 2013 19 22
    • (2013) Pharmacol Res , vol.71 , pp. 19-22
    • Rose-John, S.1
  • 32
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • DOI 10.1016/S0092-8674(02)00966-2
    • J. Schlessinger Ligand-induced, receptor-mediated dimerization and activation of EGF receptor Cell 110 2002 669 672 (Pubitemid 35283957)
    • (2002) Cell , vol.110 , Issue.6 , pp. 669-672
    • Schlessinger, J.1
  • 33
    • 0033554674 scopus 로고    scopus 로고
    • Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme
    • M. Aritomi, N. Kunishima, T. Okamoto, R. Kuroki, Y. Ota, and K. Morikawa Atomic structure of the GCSF-receptor complex showing a new cytokine-receptor recognition scheme Nature 401 1999 713 717
    • (1999) Nature , vol.401 , pp. 713-717
    • Aritomi, M.1    Kunishima, N.2    Okamoto, T.3    Kuroki, R.4    Ota, Y.5    Morikawa, K.6
  • 37
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • DOI 10.1016/S1097-2765(03)00047-9
    • K.M. Ferguson, M.B. Berger, J.M. Mendrola, H.S. Cho, D.J. Leahy, and M.A. Lemmon EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization Mol Cell 11 2003 507 517 (Pubitemid 36297057)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.-S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 39
    • 0035860766 scopus 로고    scopus 로고
    • Crystal structure of human epidermal growth factor and its dimerization
    • H.S. Lu, J.J. Chai, M. Li, B.R. Huang, C.H. He, and R.C. Bi Crystal structure of human epidermal growth factor and its dimerization J Biol Chem 276 2001 34913 34917
    • (2001) J Biol Chem , vol.276 , pp. 34913-34917
    • Lu, H.S.1    Chai, J.J.2    Li, M.3    Huang, B.R.4    He, C.H.5    Bi, R.C.6
  • 41
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • DOI 10.1126/science.1074611
    • H.S. Cho, and D.J. Leahy Structure of the extracellular region of HER3 reveals an interdomain tether Science 297 2002 1330 1333 (Pubitemid 34913167)
    • (2002) Science , vol.297 , Issue.5585 , pp. 1330-1333
    • Cho, H.-S.1    Leahy, D.J.2
  • 43
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • DOI 10.1038/nature01392
    • H.S. Cho, K. Mason, K.X. Ramyar, A.M. Stanley, S.B. Gabelli, and D.W. Denney Jr. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab Nature 421 2003 756 760 (Pubitemid 36227628)
    • (2003) Nature , vol.421 , Issue.6924 , pp. 756-760
    • Cho, H.-S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5    Denney Jr., D.W.6    Leahy, D.J.7
  • 45
    • 77955627615 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity in growth factor binding to an EGF receptor
    • D. Alvarado, D.E. Klein, and M.A. Lemmon Structural basis for negative cooperativity in growth factor binding to an EGF receptor Cell 142 2010 568 579
    • (2010) Cell , vol.142 , pp. 568-579
    • Alvarado, D.1    Klein, D.E.2    Lemmon, M.A.3
  • 46
    • 84886907697 scopus 로고    scopus 로고
    • Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging
    • J.L. Macdonald-Obermann, S. Adak, R. Landgraf, D. Piwnica-Worms, and L.J. Pike Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging J Biol Chem 288 2013 30773 30784
    • (2013) J Biol Chem , vol.288 , pp. 30773-30784
    • Macdonald-Obermann, J.L.1    Adak, S.2    Landgraf, R.3    Piwnica-Worms, D.4    Pike, L.J.5
  • 47
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • DOI 10.1016/S0092-8674(02)00741-9
    • M. Huse, and J. Kuriyan The conformational plasticity of protein kinases Cell 109 2002 275 282 (Pubitemid 34606870)
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 49
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D.R. Knighton, J.H. Zheng, L.F. Ten Eyck, V.A. Ashford, N.H. Xuong, and S.S. Taylor Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 407 414 (Pubitemid 21917165)
    • (1991) Science , vol.253 , Issue.5018 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 50
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • S.K. Hanks, A.M. Quinn, and T. Hunter The protein kinase family: conserved features and deduced phylogeny of the catalytic domains Science 241 1988 42 52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 51
    • 80053576891 scopus 로고    scopus 로고
    • Protein kinase biochemistry and drug discovery
    • P.A. Schwartz, and B.W. Murray Protein kinase biochemistry and drug discovery Bioorg Chem 39 2011 192 210
    • (2011) Bioorg Chem , vol.39 , pp. 192-210
    • Schwartz, P.A.1    Murray, B.W.2
  • 54
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • DOI 10.1016/j.molcel.2004.08.024, PII S1097276504004800
    • B. Nolen, S. Taylor, and G. Ghosh Regulation of protein kinases: controlling activity through activation segment conformation Mol Cell 15 2004 661 675 (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 55
    • 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
    • N. Gotoh, A. Tojo, M. Hino, Y. Yazaki, and M. Shibuya 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 186 1992 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
  • 58
    • 0037429779 scopus 로고    scopus 로고
    • The deaf and the dumb: The biology of ErbB-2 and ErbB-3
    • DOI 10.1016/S0014-4827(02)00101-5
    • A. Citri, K.B. Skaria, and Y. Yarden The deaf and the dumb: the biology of ErbB-2 and ErbB-3 Exp Cell Res 284 2003 54 65 (Pubitemid 36342255)
    • (2003) Experimental Cell Research , vol.284 , Issue.1 , pp. 54-65
    • Citri, A.1    Skaria, K.B.2    Yarden, Y.3
  • 60
    • 84865165294 scopus 로고    scopus 로고
    • Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling
    • Q. Zhang, E. Park, K. Kani, and R. Landgraf Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling Proc Natl Acad Sci USA 109 2012 13237 13242
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 13237-13242
    • Zhang, Q.1    Park, E.2    Kani, K.3    Landgraf, R.4
  • 61
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • S.S. Taylor, and A.P. Kornev Protein kinases: evolution of dynamic regulatory proteins Trends Biochem Sci 36 2011 65 77
    • (2011) Trends Biochem Sci , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 62
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • J. Zhang, P.L. Yang, and N.S. Gray Targeting cancer with small molecule kinase inhibitors Nat Rev Cancer 9 2009 28 39
    • (2009) Nat Rev Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 63
    • 0033583220 scopus 로고    scopus 로고
    • C-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function
    • J.S. Biscardi, M.C. Maa, D.A. Tice, M.E. Cox, T.H. Leu, and S.J. Parsons c-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function J Biol Chem 274 1999 8335 8343
    • (1999) J Biol Chem , vol.274 , pp. 8335-8343
    • Biscardi, J.S.1    Maa, M.C.2    Tice, D.A.3    Cox, M.E.4    Leu, T.H.5    Parsons, S.J.6
  • 64
    • 33745002702 scopus 로고    scopus 로고
    • An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor
    • DOI 10.1016/j.cell.2006.05.013, PII S0092867406005848
    • X. Zhang, J. Gureasko, K. Shen, P.A. Cole, and J. Kuriyan An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor Cell 125 2006 1137 1149 (Pubitemid 43866200)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 65
    • 84855999013 scopus 로고    scopus 로고
    • Mechanics of EGF receptor/ErbB2 kinase activation revealed by luciferase fragment complementation imaging
    • J.L. Macdonald-Obermann, D. Piwnica-Worms, and L.J. Pike Mechanics of EGF receptor/ErbB2 kinase activation revealed by luciferase fragment complementation imaging Proc Natl Acad Sci USA 109 2012 137 142
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 137-142
    • Macdonald-Obermann, J.L.1    Piwnica-Worms, D.2    Pike, L.J.3
  • 68
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • N. Jura, N.F. Endres, K. Engel, S. Deindl, R. Das, and M.H. Lamers Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment Cell 137 2009 1293 1307
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1    Endres, N.F.2    Engel, K.3    Deindl, S.4    Das, R.5    Lamers, M.H.6
  • 70
    • 43749091771 scopus 로고    scopus 로고
    • Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state
    • E.V. Bocharov, K.S. Mineev, P.E. Volynsky, Y.S. Ermolyuk, E.N. Tkach, and A.G. Sobol Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state J Biol Chem 283 2008 6950 6956
    • (2008) J Biol Chem , vol.283 , pp. 6950-6956
    • Bocharov, E.V.1    Mineev, K.S.2    Volynsky, P.E.3    Ermolyuk, Y.S.4    Tkach, E.N.5    Sobol, A.G.6
  • 71
  • 72
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • B. Brosig, and D. Langosch The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues Protein Sci 7 1998 1052 1056 (Pubitemid 28216547)
    • (1998) Protein Science , vol.7 , Issue.4 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 73
    • 67349094494 scopus 로고    scopus 로고
    • Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains
    • C. Escher, F. Cymer, and D. Schneider Two GxxxG-like motifs facilitate promiscuous interactions of the human ErbB transmembrane domains J Mol Biol 389 2009 10 16
    • (2009) J Mol Biol , vol.389 , pp. 10-16
    • Escher, C.1    Cymer, F.2    Schneider, D.3
  • 74
    • 78649548465 scopus 로고    scopus 로고
    • Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor
    • C. Lu, L.Z. Mi, M.J. Grey, J. Zhu, E. Graef, and S. Yokoyama Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor Mol Cell Biol 30 2010 5432 5443
    • (2010) Mol Cell Biol , vol.30 , pp. 5432-5443
    • Lu, C.1    Mi, L.Z.2    Grey, M.J.3    Zhu, J.4    Graef, E.5    Yokoyama, S.6
  • 75
    • 84873280409 scopus 로고    scopus 로고
    • Conformational coupling across the plasma membrane in activation of the EGF receptor
    • N.F. Endres, R. Das, A.W. Smith, A. Arkhipov, E. Kovacs, and Y. Huang Conformational coupling across the plasma membrane in activation of the EGF receptor Cell 152 2013 543 556
    • (2013) Cell , vol.152 , pp. 543-556
    • Endres, N.F.1    Das, R.2    Smith, A.W.3    Arkhipov, A.4    Kovacs, E.5    Huang, Y.6
  • 77
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • I. Chung, R. Akita, R. Vandlen, D. Toomre, J. Schlessinger, and I. Mellman Spatial control of EGF receptor activation by reversible dimerization on living cells Nature 464 2010 783 787
    • (2010) Nature , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 78
    • 80052511894 scopus 로고    scopus 로고
    • Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor
    • L.Z. Mi, C. Lu, Z. Li, N. Nishida, T. Walz, and T.A. Springer Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor Nat Struct Mol Biol 18 2011 984 989
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 984-989
    • Mi, L.Z.1    Lu, C.2    Li, Z.3    Nishida, N.4    Walz, T.5    Springer, T.A.6
  • 79
    • 67649781716 scopus 로고    scopus 로고
    • Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics
    • J. Kästner, H.H. Loeffler, S.K. Roberts, M.L. Martin-Fernandez, and M.D. Winn Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics J Struct Biol 167 2009 117 128
    • (2009) J Struct Biol , vol.167 , pp. 117-128
    • Kästner, J.1    Loeffler, H.H.2    Roberts, S.K.3    Martin-Fernandez, M.L.4    Winn, M.D.5
  • 81
    • 84864367360 scopus 로고    scopus 로고
    • The ERBB network: At last, cancer therapy meets systems biology
    • Y. Yarden, and G. Pines The ERBB network: at last, cancer therapy meets systems biology Nat Rev Cancer 12 2012 553 563
    • (2012) Nat Rev Cancer , vol.12 , pp. 553-563
    • Yarden, Y.1    Pines, G.2
  • 83
    • 63049100044 scopus 로고    scopus 로고
    • Functional selectivity of EGF family peptide growth factors: Implications for cancer
    • K.J. Wilson, J.L. Gilmore, J. Foley, M.A. Lemmon, and D.J. Riese 2nd Functional selectivity of EGF family peptide growth factors: implications for cancer Pharmacol Ther 122 2009 1 8
    • (2009) Pharmacol Ther , vol.122 , pp. 1-8
    • Wilson, K.J.1    Gilmore, J.L.2    Foley, J.3    Lemmon, M.A.4    Riese II, D.J.5
  • 84
    • 67749122122 scopus 로고    scopus 로고
    • Targeting PI3K signalling in cancer: Opportunities, challenges and limitations
    • J.A. Engelman Targeting PI3K signalling in cancer: opportunities, challenges and limitations Nat Rev Cancer 9 2009 550 562
    • (2009) Nat Rev Cancer , vol.9 , pp. 550-562
    • Engelman, J.A.1
  • 86
    • 77956124562 scopus 로고    scopus 로고
    • RAF protein-serine/threonine kinases: Structure and regulation
    • R. Roskoski Jr. RAF protein-serine/threonine kinases: structure and regulation Biochem Biophys Res Commun 399 2010 313 317
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 313-317
    • Roskoski, Jr.R.1
  • 87
    • 84855795110 scopus 로고    scopus 로고
    • MEK1/2 dual-specificity protein kinases: Structure and regulation
    • R. Roskoski Jr. MEK1/2 dual-specificity protein kinases: structure and regulation Biochem Biophys Res Commun 417 2012 5 10
    • (2012) Biochem Biophys Res Commun , vol.417 , pp. 5-10
    • Roskoski, Jr.R.1
  • 88
    • 84862294189 scopus 로고    scopus 로고
    • ERK1/2 MAP kinases: Structure, function, and regulation
    • R. Roskoski Jr. ERK1/2 MAP kinases: structure, function, and regulation Pharmacol Res 66 2012 105 143
    • (2012) Pharmacol Res , vol.66 , pp. 105-143
    • Roskoski, Jr.R.1
  • 89
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
    • E.J. Lowenstein, R.J. Daly, A.G. Batzer, W. Li, B. Margolis, and R. Lammers The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling Cell 70 1992 431 442
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1    Daly, R.J.2    Batzer, A.G.3    Li, W.4    Margolis, B.5    Lammers, R.6
  • 90
    • 0033913657 scopus 로고    scopus 로고
    • The SH2 and SH3 adapter Nck: A two-gene family and a linker between tyrosine kinases and multiple signaling networks
    • W. Li, and H. She The SH2 and SH3 adapter Nck: a two-gene family and a linker between tyrosine kinases and multiple signaling networks Histol Histopathol 15 2000 947 955 (Pubitemid 30488574)
    • (2000) Histology and Histopathology , vol.15 , Issue.3 , pp. 947-955
    • Li, W.1    She, H.2
  • 93
    • 0037163125 scopus 로고    scopus 로고
    • Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation
    • L. Xia, L. Wang, A.S. Chung, S.S. Ivanov, M.Y. Ling, and A.M. Dragoi Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation J Biol Chem 277 2002 30716 33023
    • (2002) J Biol Chem , vol.277 , pp. 30716-33023
    • Xia, L.1    Wang, L.2    Chung, A.S.3    Ivanov, S.S.4    Ling, M.Y.5    Dragoi, A.M.6
  • 94
    • 0037193682 scopus 로고    scopus 로고
    • The identification of a novel human homologue of the SH3 binding glutamic acid-rich (SH3BGR) gene establishes a new family of highly conserved small proteins related to Thioredoxin Superfamily
    • DOI 10.1016/S0378-1119(02)00602-9, PII S0378111902006029
    • M. Mazzocco, M. Maffei, A. Egeo, A. Vergano, P. Arrigo, and R. Di Lisi The identification of a novel human homologue of the SH3 binding glutamic acid-rich (SH3BGR) gene establishes a new family of highly conserved small proteins related to thioredoxin superfamily Gene 291 2002 233 239 (Pubitemid 34722393)
    • (2002) Gene , vol.291 , Issue.1-2 , pp. 233-239
    • Mazzocco, M.1    Maffei, M.2    Egeo, A.3    Vergano, A.4    Arrigo, P.5    Di Lisi, R.6    Ghiotto, F.7    Scartezzini, P.8
  • 95
    • 33845633819 scopus 로고    scopus 로고
    • Biomarker discovery: A proteomic approach for brain cancer profiling
    • DOI 10.1111/j.1349-7006.2007.00374.x
    • A.A. Khalil, and P. James Biomarker discovery: a proteomic approach for brain cancer profiling Cancer Sci 98 2007 201 213 (Pubitemid 44941872)
    • (2007) Cancer Science , vol.98 , Issue.2 , pp. 201-213
    • Khalil, A.A.1    James, P.2
  • 96
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • DOI 10.1038/nrc969
    • J. Downward Targeting RAS signalling pathways in cancer therapy Nat Rev Cancer 3 2003 11 22 (Pubitemid 37328883)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.1 , pp. 11-22
    • Downward, J.1
  • 97
    • 0030896307 scopus 로고    scopus 로고
    • Ras-GTPase activating protein (GAP): A putative effector for Ras
    • DOI 10.1016/S0898-6568(96)00135-0, PII S0898656896001350
    • B. Tocque, I. Delumeau, F. Parker, F. Maurier, M.C. Multon, and F. Schweighoffer Ras-GTPase activating protein (GAP): a putative effector for Ras Cell Signal 9 1997 153 158 (Pubitemid 27186914)
    • (1997) Cellular Signalling , vol.9 , Issue.2 , pp. 153-158
    • Tocque, B.1    Delumeau, I.2    Parker, F.3    Maurier, F.4    Multon, M.-C.5    Schweighoffer, F.6
  • 98
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • DOI 10.1016/j.bbrc.2004.09.171
    • R. Roskoski Jr. Src protein-tyrosine kinase structure and regulation Biochem Biophys Res Commun 324 2004 1155 1164 (Pubitemid 40292143)
    • (2004) Biochemical and Biophysical Research Communications , vol.324 , Issue.4 , pp. 1155-1164
    • Roskoski Jr., R.1
  • 100
    • 0035101089 scopus 로고    scopus 로고
    • Syk: A new player in the field of breast cancer
    • DOI 10.1186/bcr261
    • Z.A. Stewart, and J.A. Pietenpol Syk: a new player in the field of breast cancer Breast Cancer Res 3 2001 5 7 (Pubitemid 32223644)
    • (2001) Breast Cancer Research , vol.3 , Issue.1 , pp. 5-7
    • Stewart, Z.A.1    Pietenpol, J.A.2
  • 101
    • 84873657250 scopus 로고    scopus 로고
    • Mammalian phospholipase C
    • G. Kadamur, and E.M. Ross Mammalian phospholipase C Annu Rev Physiol 75 2013 127 154
    • (2013) Annu Rev Physiol , vol.75 , pp. 127-154
    • Kadamur, G.1    Ross, E.M.2
  • 102
    • 34250703569 scopus 로고    scopus 로고
    • Classical PKC isoforms in cancer
    • DOI 10.1016/j.phrs.2007.04.001, PII S1043661807000795
    • G. Martiny-Baron, and D. Fabbro Classical PKC isoforms in cancer Pharmacol Res 55 2007 477 486 (Pubitemid 46970734)
    • (2007) Pharmacological Research , vol.55 , Issue.6 , pp. 477-486
    • Martiny-Baron, G.1    Fabbro, D.2
  • 103
    • 79953191168 scopus 로고    scopus 로고
    • Protein kinase CÉ as a cancer marker and target for anticancer therapy
    • E. Totoń, E. Ignatowicz, K. Skrzeczkowska, and M. Rybczyńska Protein kinase CÉ as a cancer marker and target for anticancer therapy Pharmacol Rep 63 2011 19 29
    • (2011) Pharmacol Rep , vol.63 , pp. 19-29
    • Totoń, E.1    Ignatowicz, E.2    Skrzeczkowska, K.3    Rybczyńska, M.4
  • 104
    • 84870772239 scopus 로고    scopus 로고
    • Protein kinase C, an elusive therapeutic target?
    • D. Mochly-Rosen, K. Das, and K.V. Grimes Protein kinase C, an elusive therapeutic target? Nat Rev Drug Discov 11 2012 937 957
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 937-957
    • Mochly-Rosen, D.1    Das, K.2    Grimes, K.V.3
  • 105
    • 34250669166 scopus 로고    scopus 로고
    • Protein kinase Cε makes the life and death decision
    • DOI 10.1016/j.cellsig.2007.04.008, PII S0898656807001246
    • A. Basu, and U. Sivaprasad Protein kinase CÉ makes the life and death decision Cell Signal 19 2007 1633 1642 (Pubitemid 46935437)
    • (2007) Cellular Signalling , vol.19 , Issue.8 , pp. 1633-1642
    • Basu, A.1    Sivaprasad, U.2
  • 109
    • 0343729328 scopus 로고    scopus 로고
    • Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells
    • T. Tenev, S.A. Böhmer, R. Kaufmann, S. Frese, T. Bittorf, and T. Beckers Perinuclear localization of the protein-tyrosine phosphatase SHP-1 and inhibition of epidermal growth factor-stimulated STAT1/3 activation in A431 cells Eur J Cell Biol 79 2000 261 271 (Pubitemid 30232571)
    • (2000) European Journal of Cell Biology , vol.79 , Issue.4 , pp. 261-271
    • Tenev, T.1    Bohmer, S.-A.2    Kaufmann, R.3    Frese, S.4    Bittorf, T.5    Beckers, T.6    Bohmer, F.-D.7
  • 110
    • 74249102653 scopus 로고    scopus 로고
    • Elevated expression of the tyrosine phosphatase SHP-1 defines a subset of high-grade breast tumors
    • L. Insabato, I. Amelio, M. Quarto, A. Zannetti, F. Tolino, and G. de Mauro Elevated expression of the tyrosine phosphatase SHP-1 defines a subset of high-grade breast tumors Oncology 77 2009 378 384
    • (2009) Oncology , vol.77 , pp. 378-384
    • Insabato, L.1    Amelio, I.2    Quarto, M.3    Zannetti, A.4    Tolino, F.5    De Mauro, G.6
  • 111
    • 0038190924 scopus 로고    scopus 로고
    • Development of an efficient substrate-trapping mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates
    • DOI 10.1074/jbc.M210670200
    • Y.M. Agazie, and M.J. Hayman Development of an efficient substrate-trapping mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates J Biol Chem 278 2003 13952 13958 (Pubitemid 36799937)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13952-13958
    • Agazie, Y.M.1    Hayman, M.J.2
  • 112
    • 66449118043 scopus 로고    scopus 로고
    • Molecular mechanism for SHP2 in promoting HER2-induced signaling and transformation
    • X. Zhou, and Y.M. Agazie Molecular mechanism for SHP2 in promoting HER2-induced signaling and transformation J Biol Chem 284 2009 12226 12234
    • (2009) J Biol Chem , vol.284 , pp. 12226-12234
    • Zhou, X.1    Agazie, Y.M.2
  • 114
    • 0037018146 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
    • DOI 10.1083/jcb.200106056
    • K.E. Longva, F.D. Blystad, E. Stang, A.M. Larsen, L.E. Johannessen, and I.H. Madshus Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies J Cell Biol 156 2002 843 854 (Pubitemid 34839867)
    • (2002) Journal of Cell Biology , vol.156 , Issue.5 , pp. 843-854
    • Longva, K.E.1    Blystad, F.D.2    Stang, E.3    Larsen, A.M.4    Johannessen, L.E.5    Madshus, I.H.6
  • 115
    • 54249151578 scopus 로고    scopus 로고
    • Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation
    • K. Umebayashi, H. Stenmark, and T. Yoshimori Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation Mol Biol Cell 19 2008 3454 3462
    • (2008) Mol Biol Cell , vol.19 , pp. 3454-3462
    • Umebayashi, K.1    Stenmark, H.2    Yoshimori, T.3
  • 116
    • 84858121800 scopus 로고    scopus 로고
    • The role of ubiquitylation in receptor endocytosis and endosomal sorting
    • K. Haglund, and I. Dikic The role of ubiquitylation in receptor endocytosis and endosomal sorting J Cell Sci 125 2012 265 275
    • (2012) J Cell Sci , vol.125 , pp. 265-275
    • Haglund, K.1    Dikic, I.2
  • 117
    • 0017103026 scopus 로고
    • 125I-labeled human epidermal growth factor. Binding, internalization, and degradation in human fibroblasts
    • 125I-labeled human epidermal growth factor. Binding, internalization, and degradation in human fibroblasts J Cell Biol 71 1976 159 171
    • (1976) J Cell Biol , vol.71 , pp. 159-171
    • Carpenter, G.1    Cohen, S.2
  • 118
    • 0027620152 scopus 로고
    • Endocytosis of growth factor receptors
    • A. Sorkin, and C.M. Waters Endocytosis of growth factor receptors Bioessays 15 1993 375 382
    • (1993) Bioessays , vol.15 , pp. 375-382
    • Sorkin, A.1    Waters, C.M.2
  • 119
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • DOI 10.1074/jbc.271.9.5251
    • J. Baulida, M.H. Kraus, M. Alimandi, P.P. Di Fiore, and G. Carpenter All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired J Biol Chem 271 1996 5251 5257 (Pubitemid 26075021)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.9 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5
  • 120
    • 67349270856 scopus 로고    scopus 로고
    • Trafficking of receptor tyrosine kinases to the nucleus
    • G. Carpenter, and H.J. Liao Trafficking of receptor tyrosine kinases to the nucleus Exp Cell Res 315 2009 1556 1566
    • (2009) Exp Cell Res , vol.315 , pp. 1556-1566
    • Carpenter, G.1    Liao, H.J.2
  • 122
    • 77954759289 scopus 로고    scopus 로고
    • Nuclear trafficking of the epidermal growth factor receptor family membrane proteins
    • Y.N. Wang, H. Yamaguchi, J.M. Hsu, and M.C. Hung Nuclear trafficking of the epidermal growth factor receptor family membrane proteins Oncogene 29 2010 3997 4006
    • (2010) Oncogene , vol.29 , pp. 3997-4006
    • Wang, Y.N.1    Yamaguchi, H.2    Hsu, J.M.3    Hung, M.C.4
  • 123
    • 1542284152 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of signal transducers
    • DOI 10.1038/nrm1331
    • L. Xu, and J. Massagué Nucleocytoplasmic shuttling of signal transducers Nat Rev Mol Cell Biol 5 2004 209 219 (Pubitemid 38325802)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.3 , pp. 209-219
    • Xu, L.1    Massague, J.2
  • 124
    • 79959423595 scopus 로고    scopus 로고
    • The structure of the nuclear pore complex
    • A. Hoelz, E.W. Debler, and G. Blobel The structure of the nuclear pore complex Annu Rev Biochem 80 2011 613 643
    • (2011) Annu Rev Biochem , vol.80 , pp. 613-643
    • Hoelz, A.1    Debler, E.W.2    Blobel, G.3
  • 125
    • 84857655359 scopus 로고    scopus 로고
    • The nuclear envelope environment and its cancer connections
    • K.H. Chow, R.E. Factor, and K.S. Ullman The nuclear envelope environment and its cancer connections Nat Rev Cancer 12 2012 196 209
    • (2012) Nat Rev Cancer , vol.12 , pp. 196-209
    • Chow, K.H.1    Factor, R.E.2    Ullman, K.S.3
  • 126
  • 128
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin-β proteins
    • D. Xu, A. Farmer, and Y.M. Chook Recognition of nuclear targeting signals by Karyopherin-β proteins Curr Opin Struct Biol 20 2010 782 790
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 782-790
    • Xu, D.1    Farmer, A.2    Chook, Y.M.3
  • 129
    • 0035575518 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Ran, beta and beyond
    • DOI 10.1016/S0962-8924(01)02144-4, PII S0962892401021444
    • S. Kuersten, M. Ohno, and I.W. Mattaj Nucleocytoplasmic transport: Ran, beta and beyond Trends Cell Biol 11 2001 497 503 (Pubitemid 33079143)
    • (2001) Trends in Cell Biology , vol.11 , Issue.12 , pp. 497-503
    • Kuersten, S.1    Ohno, M.2    Mattaj, I.W.3
  • 130
    • 34249845380 scopus 로고    scopus 로고
    • Characterization of a novel tripartite nuclear localization sequence in the EGFR family
    • S.C. Hsu, and M.C. Hung Characterization of a novel tripartite nuclear localization sequence in the EGFR family J Biol Chem 282 2007 10432 10440
    • (2007) J Biol Chem , vol.282 , pp. 10432-10440
    • Hsu, S.C.1    Hung, M.C.2
  • 131
    • 70350741359 scopus 로고    scopus 로고
    • Nuclear translocation of the epidermal growth factor receptor family membrane tyrosine kinase receptors
    • S.C. Wang, and M.C. Hung Nuclear translocation of the epidermal growth factor receptor family membrane tyrosine kinase receptors Clin Cancer Res 15 2009 6484 6489
    • (2009) Clin Cancer Res , vol.15 , pp. 6484-6489
    • Wang, S.C.1    Hung, M.C.2
  • 133
    • 84881356235 scopus 로고    scopus 로고
    • Mapping C-terminal transactivation domains of the nuclear HER family receptor tyrosine kinase HER3
    • T.M. Brand, M. Iida, N. Luthar, M.J. Wleklinski, M.M. Starr, and D.L. Wheeler Mapping C-terminal transactivation domains of the nuclear HER family receptor tyrosine kinase HER3 PLoS One 8 2013 e71518
    • (2013) PLoS One , vol.8 , pp. 71518
    • Brand, T.M.1    Iida, M.2    Luthar, N.3    Wleklinski, M.J.4    Starr, M.M.5    Wheeler, D.L.6
  • 135
    • 33749072714 scopus 로고    scopus 로고
    • Presenilin-Dependent ErbB4 Nuclear Signaling Regulates the Timing of Astrogenesis in the Developing Brain
    • DOI 10.1016/j.cell.2006.07.037, PII S0092867406012074
    • S.P. Sardi, J. Murtie, S. Koirala, B.A. Patten, and G. Corfas Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain Cell 127 2006 185 197 (Pubitemid 44466644)
    • (2006) Cell , vol.127 , Issue.1 , pp. 185-197
    • Sardi, S.P.1    Murtie, J.2    Koirala, S.3    Patten, B.A.4    Corfas, G.5
  • 136
    • 16444383812 scopus 로고    scopus 로고
    • Developmental profile of ErbB receptors in murine central nervous system: Implications for functional interactions
    • DOI 10.1002/jnr.20381
    • I.J. Fox, and H.I. Kornblum Developmental profile of ErbB receptors in murine central nervous system: implications for functional interactions J Neurosci Res 79 2005 584 597 (Pubitemid 40476437)
    • (2005) Journal of Neuroscience Research , vol.79 , Issue.5 , pp. 584-597
    • Fox, I.J.1    Kornblum, H.I.2
  • 137
    • 70350653741 scopus 로고    scopus 로고
    • Nuclear EGFR contributes to acquired resistance to cetuximab
    • C. Li, M. Iida, E.F. Dunn, A.J. Ghia, and D.L. Wheeler Nuclear EGFR contributes to acquired resistance to cetuximab Oncogene 28 2009 3801 3813
    • (2009) Oncogene , vol.28 , pp. 3801-3813
    • Li, C.1    Iida, M.2    Dunn, E.F.3    Ghia, A.J.4    Wheeler, D.L.5
  • 138
  • 139
    • 33749072019 scopus 로고    scopus 로고
    • Nuclear Signaling by Receptor Tyrosine Kinases: The First Robin of Spring
    • DOI 10.1016/j.cell.2006.09.013, PII S0092867406012049
    • J. Schlessinger, and M.A. Lemmon Nuclear signaling by receptor tyrosine kinases: the first robin of spring Cell 127 2006 45 48 (Pubitemid 44466641)
    • (2006) Cell , vol.127 , Issue.1 , pp. 45-48
    • Schlessinger, J.1    Lemmon, M.A.2
  • 144
    • 34548457234 scopus 로고    scopus 로고
    • The IASLC lung cancer staging project: Proposals for the revision of the TNM stage groupings in the forthcoming (seventh) edition of the TNM classification of malignant tumours
    • DOI 10.1097/JTO.0b013e31812f3c1a, PII 0124389420070800000006
    • P. Goldstraw, J. Crowley, K. Chansky, D.J. Giroux, P.A. Groome, and R. Rami-Porta The IASLC Lung Cancer Staging Project: proposals for the revision of the TNM stage groupings in the forthcoming (seventh) edition of the TNM classification of malignant tumours J Thorac Oncol 2 2007 706 714 Erratum in: J Thorac Oncol 2007;2:985 (Pubitemid 47357522)
    • (2007) Journal of Thoracic Oncology , vol.2 , Issue.8 , pp. 706-714
    • Goldstraw, P.1    Crowley, J.2    Chansky, K.3    Giroux, D.J.4    Groome, P.A.5    Rami-Porta, R.6    Postmus, P.E.7    Rusch, V.8    Sobin, L.9
  • 147
    • 84871538217 scopus 로고    scopus 로고
    • Systematic review and meta-analysis of randomised, phase II/III trials adding bevacizumab to platinum-based chemotherapy as first-line treatment in patients with advanced non-small-cell lung cancer
    • Erratum in: Ann Oncol 2013;24:1133
    • J.C. Soria, A. Mauguen, M. Reck, A.B. Sandler, N. Saijo, and D.H. Johnson Systematic review and meta-analysis of randomised, phase II/III trials adding bevacizumab to platinum-based chemotherapy as first-line treatment in patients with advanced non-small-cell lung cancer Ann Oncol 24 2013 20 30 Erratum in: Ann Oncol 2013;24:1133
    • (2013) Ann Oncol , vol.24 , pp. 20-30
    • Soria, J.C.1    Mauguen, A.2    Reck, M.3    Sandler, A.B.4    Saijo, N.5    Johnson, D.H.6
  • 148
    • 77953683770 scopus 로고    scopus 로고
    • Targeting nanoparticles to cancer
    • M. Wang, and M. Thanou Targeting nanoparticles to cancer Pharmacol Res 62 2010 90 99
    • (2010) Pharmacol Res , vol.62 , pp. 90-99
    • Wang, M.1    Thanou, M.2
  • 151
    • 5644296647 scopus 로고    scopus 로고
    • Gefitinib (Iressa, ZD 1839) monotherapy for pretreated advanced non-small cell lung cancer in IDEAL 1 and 2: Tumor response is not clinically relevantly predictable from tumor EGFR membrane staining alone
    • [abstract O-242]
    • R. Bailey, M. Kris, and M. Wolf Gefitinib (Iressa, ZD 1839) monotherapy for pretreated advanced non-small cell lung cancer in IDEAL 1 and 2: tumor response is not clinically relevantly predictable from tumor EGFR membrane staining alone Lung Cancer 41 2003 S71 [abstract O-242]
    • (2003) Lung Cancer , vol.41 , pp. 71
    • Bailey, R.1    Kris, M.2    Wolf, M.3
  • 152
    • 24644458654 scopus 로고    scopus 로고
    • FDA drug approval summary: Erlotinib (Tarceva®) tablets
    • DOI 10.1634/theoncologist.10-7-461
    • M.H. Cohen, J.R. Johnson, Y.F. Chen, R. Sridhara, and R. Pazdur FDA drug approval summary: erlotinib (Tarceva) tablets Oncologist 10 2005 461 466 (Pubitemid 41266326)
    • (2005) Oncologist , vol.10 , Issue.7 , pp. 461-466
    • Cohen, M.H.1    Johnson, J.R.2    Chen, Y.-F.3    Sridhara, R.4    Pazdur, R.5
  • 153
    • 84873870877 scopus 로고    scopus 로고
    • Skin rash could predict the response to EGFR tyrosine kinase inhibitor and the prognosis for patients with non-small cell lung cancer: A systematic review and meta-analysis
    • H.B. Liu, Y. Wu, T.F. Lv, Y.W. Yao, Y.Y. Xiao, and D.M. Yuan Skin rash could predict the response to EGFR tyrosine kinase inhibitor and the prognosis for patients with non-small cell lung cancer: a systematic review and meta-analysis PLoS One 8 2013 e55128
    • (2013) PLoS One , vol.8 , pp. 55128
    • Liu, H.B.1    Wu, Y.2    Lv, T.F.3    Yao, Y.W.4    Xiao, Y.Y.5    Yuan, D.M.6
  • 157
    • 84877147943 scopus 로고    scopus 로고
    • Uncommon epidermal growth factor receptor mutations in non-small cell lung cancer and their mechanisms of EGFR tyrosine kinase inhibitors sensitivity and resistance
    • E. Massarelli, F.M. Johnson, H.S. Erickson, I.I. Wistuba, and V. Papadimitrakopoulou Uncommon epidermal growth factor receptor mutations in non-small cell lung cancer and their mechanisms of EGFR tyrosine kinase inhibitors sensitivity and resistance Lung Cancer 80 2013 235 241
    • (2013) Lung Cancer , vol.80 , pp. 235-241
    • Massarelli, E.1    Johnson, F.M.2    Erickson, H.S.3    Wistuba, I.I.4    Papadimitrakopoulou, V.5
  • 158
    • 77958478674 scopus 로고    scopus 로고
    • Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer
    • W. Pao, and J. Chmielecki Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer Nat Rev Cancer 10 2010 760 774
    • (2010) Nat Rev Cancer , vol.10 , pp. 760-774
    • Pao, W.1    Chmielecki, J.2
  • 160
    • 75249087060 scopus 로고    scopus 로고
    • Gefitinib versus cisplatin plus docetaxel in patients with non-small-cell lung cancer harbouring mutations of the epidermal growth factor receptor (WJTOG3405): An open label, randomised phase 3 trial
    • T. Mitsudomi, S. Morita, Y. Yatabe, S. Negoro, I. Okamoto, and J. Tsurutani Gefitinib versus cisplatin plus docetaxel in patients with non-small-cell lung cancer harbouring mutations of the epidermal growth factor receptor (WJTOG3405): an open label, randomised phase 3 trial Lancet Oncol 11 2010 121 128
    • (2010) Lancet Oncol , vol.11 , pp. 121-128
    • Mitsudomi, T.1    Morita, S.2    Yatabe, Y.3    Negoro, S.4    Okamoto, I.5    Tsurutani, J.6
  • 161
    • 69949186250 scopus 로고    scopus 로고
    • Screening for epidermal growth factor receptor mutations in lung cancer
    • R. Rosell, T. Moran, C. Queralt, R. Porta, F. Cardenal, and C. Camps Screening for epidermal growth factor receptor mutations in lung cancer N Engl J Med 361 2009 958 967
    • (2009) N Engl J Med , vol.361 , pp. 958-967
    • Rosell, R.1    Moran, T.2    Queralt, C.3    Porta, R.4    Cardenal, F.5    Camps, C.6
  • 162
    • 33847406095 scopus 로고    scopus 로고
    • Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity
    • DOI 10.1016/j.ccr.2006.12.017, PII S1535610807000281
    • C.H. Yun, T.J. Boggon, Y. Li, M.S. Woo, H. Greulich, and M. Meyerson Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity Cancer Cell 11 2007 217 227 (Pubitemid 46349842)
    • (2007) Cancer Cell , vol.11 , Issue.3 , 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
  • 165
    • 0028106163 scopus 로고
    • Epidermal growth factor receptor tyrosine kinase. Investigation of catalytic mechanism, structure-based searching and discovery of a potent inhibitor
    • W.H. Ward, P.N. Cook, A.M. Slater, D.H. Davies, G.A. Holdgate, and L.R. Green Epidermal growth factor receptor tyrosine kinase. Investigation of catalytic mechanism, structure-based searching and discovery of a potent inhibitor Biochem Pharmacol 48 1994 659 666
    • (1994) Biochem Pharmacol , vol.48 , pp. 659-666
    • Ward, W.H.1    Cook, P.N.2    Slater, A.M.3    Davies, D.H.4    Holdgate, G.A.5    Green, L.R.6
  • 166
    • 0015759232 scopus 로고
    • In vitro cultivation of human tumors: Establishment of cell lines derived from a series of solid tumors
    • D.J. Giard, S.A. Aaronson, G.J. Todaro, P. Arnstein, J.H. Kersey, and H. Dosik In vitro cultivation of human tumors: establishment of cell lines derived from a series of solid tumors J Natl Cancer Inst 51 1973 1417 1423
    • (1973) J Natl Cancer Inst , vol.51 , pp. 1417-1423
    • Giard, D.J.1    Aaronson, S.A.2    Todaro, G.J.3    Arnstein, P.4    Kersey, J.H.5    Dosik, H.6
  • 167
    • 0020478357 scopus 로고
    • Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: Kinetic mechanism for the bovine skeletal muscle catalytic subunit
    • P.F. Cook, M.E. Neville Jr., K.E. Vrana, F.T. Hartl, and R. Roskoski Jr. Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit Biochemistry 21 1982 5794 5799
    • (1982) Biochemistry , vol.21 , pp. 5794-5799
    • Cook, P.F.1    Neville, Jr.M.E.2    Vrana, K.E.3    Hartl, F.T.4    Roskoski, Jr.R.5
  • 168
    • 0032564322 scopus 로고    scopus 로고
    • Characterization and kinetic mechanism of catalytic domain of human vascular endothelial growth factor receptor-2 tyrosine kinase (VEGFR2 TK), a key enzyme in angiogenesis
    • DOI 10.1021/bi981291f
    • C.V. Parast, B. Mroczkowski, C. Pinko, S. Misialek, G. Khambatta, and K. Appelt Characterization and kinetic mechanism of catalytic domain of human vascular endothelial growth factor receptor-2 tyrosine kinase (VEGFR2 TK), a key enzyme in angiogenesis Biochemistry 37 1998 16788 16801 (Pubitemid 28543942)
    • (1998) Biochemistry , vol.37 , Issue.47 , pp. 16788-16801
    • Parast, C.V.1    Mroczkowski, B.2    Pinko, C.3    Misialek, S.4    Khambatta, G.5    Appelt, K.6
  • 170
    • 0029130763 scopus 로고
    • Tyrosine kinase inhibitors. 5. Synthesis and structure-activity relationships for 4-[(phenylmethyl) amino]- and 4-(phenylamino)quinazolines as potent adenosine 5′-triphosphate binding site inhibitors of the tyrosine kinase domain of the epidermal growth factor receptor
    • G.W. Rewcastle, W.A. Denny, A.J. Bridges, H. Zhou, D.R. Cody, and A. McMichael Tyrosine kinase inhibitors. 5. Synthesis and structure-activity relationships for 4-[(phenylmethyl) amino]- and 4-(phenylamino)quinazolines as potent adenosine 5′-triphosphate binding site inhibitors of the tyrosine kinase domain of the epidermal growth factor receptor J Med Chem 38 1995 3482 3487
    • (1995) J Med Chem , vol.38 , pp. 3482-3487
    • Rewcastle, G.W.1    Denny, W.A.2    Bridges, A.J.3    Zhou, H.4    Cody, D.R.5    McMichael, A.6
  • 174
    • 49149118719 scopus 로고    scopus 로고
    • BIBW2992, an irreversible EGFR/HER2 inhibitor highly effective in preclinical lung cancer models
    • D. Li, L. Ambrogio, T. Shimamura, S. Kubo, M. Takahashi, and L.R. Chirieac BIBW2992, an irreversible EGFR/HER2 inhibitor highly effective in preclinical lung cancer models Oncogene 27 2008 4702 4711
    • (2008) Oncogene , vol.27 , pp. 4702-4711
    • Li, D.1    Ambrogio, L.2    Shimamura, T.3    Kubo, S.4    Takahashi, M.5    Chirieac, L.R.6
  • 175
    • 84867621201 scopus 로고    scopus 로고
    • Target binding properties and cellular activity of afatinib (BIBW 2992), an irreversible ErbB family blocker
    • F. Solca, G. Dahl, A. Zoephel, G. Bader, M. Sanderson, and C. Klein Target binding properties and cellular activity of afatinib (BIBW 2992), an irreversible ErbB family blocker J Pharmacol Exp Ther 343 2012 342 350
    • (2012) J Pharmacol Exp Ther , vol.343 , pp. 342-350
    • Solca, F.1    Dahl, G.2    Zoephel, A.3    Bader, G.4    Sanderson, M.5    Klein, C.6
  • 176
    • 77951951659 scopus 로고    scopus 로고
    • Clinical outcomes in non-small-cell lung cancer patients with EGFR mutations: Pooled analysis
    • L. Paz-Ares, D. Soulières, I. Melezínek, J. Moecks, L. Keil, and T. Mok Clinical outcomes in non-small-cell lung cancer patients with EGFR mutations: pooled analysis J Cell Mol Med 14 2010 51 69
    • (2010) J Cell Mol Med , vol.14 , pp. 51-69
    • Paz-Ares, L.1    Soulières, D.2    Melezínek, I.3    Moecks, J.4    Keil, L.5    Mok, T.6
  • 179
    • 84872288990 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase (ALK): Structure, oncogenic activation, and pharmacological inhibition
    • R. Roskoski Jr. Anaplastic lymphoma kinase (ALK): structure, oncogenic activation, and pharmacological inhibition Pharmacol Res 68 2013 68 94
    • (2013) Pharmacol Res , vol.68 , pp. 68-94
    • Roskoski, Jr.R.1
  • 181
    • 84883017405 scopus 로고    scopus 로고
    • The preclinical profile of crizotinib for the treatment of non-small-cell lung cancer and other neoplastic disorders
    • R. Roskoski Jr. The preclinical profile of crizotinib for the treatment of non-small-cell lung cancer and other neoplastic disorders Expert Opin Drug Discov 8 2013 1165 1179
    • (2013) Expert Opin Drug Discov , vol.8 , pp. 1165-1179
    • Roskoski, Jr.R.1
  • 182
    • 84866360342 scopus 로고    scopus 로고
    • Prevalence, clinicopathologic associations, and molecular spectrum of ERBB2 (HER2) tyrosine kinase mutations in lung adenocarcinomas
    • M.E. Arcila, J.E. Chaft, K. Nafa, S. Roy-Chowdhuri, C. Lau, and M. Zaidinski Prevalence, clinicopathologic associations, and molecular spectrum of ERBB2 (HER2) tyrosine kinase mutations in lung adenocarcinomas Clin Cancer Res 18 2012 4910 4918
    • (2012) Clin Cancer Res , vol.18 , pp. 4910-4918
    • Arcila, M.E.1    Chaft, J.E.2    Nafa, K.3    Roy-Chowdhuri, S.4    Lau, C.5    Zaidinski, M.6
  • 183
    • 33745057881 scopus 로고    scopus 로고
    • HER2 mutation and response to trastuzumab therapy in non-small-cell lung cancer [15]
    • DOI 10.1056/NEJMc060020
    • F. Cappuzzo, L. Bemis, and M. Varella-Garcia HER2 mutation and response to trastuzumab therapy in non-small-cell lung cancer N Engl J Med 354 2006 2619 2621 (Pubitemid 43882374)
    • (2006) New England Journal of Medicine , vol.354 , Issue.24 , pp. 2619-2621
    • Cappuzzo, F.1    Bemis, L.2    Varella-Garcia, M.3
  • 184
    • 84858002759 scopus 로고    scopus 로고
    • Clinical activity of afatinib (BIBW 2992) in patients with lung adenocarcinoma with mutations in the kinase domain of HER2/neu
    • J. De Grève, E. Teugels, C. Geers, L. Decoster, D. Galdermans, and J. De Mey Clinical activity of afatinib (BIBW 2992) in patients with lung adenocarcinoma with mutations in the kinase domain of HER2/neu Lung Cancer 76 2012 123 127
    • (2012) Lung Cancer , vol.76 , pp. 123-127
    • De Grève, J.1    Teugels, E.2    Geers, C.3    Decoster, L.4    Galdermans, D.5    De Mey, J.6
  • 185
    • 0021348486 scopus 로고
    • Steroid-hormone receptors in breast cancer
    • J.L. Wittliff Steroid-hormone receptors in breast cancer Cancer 53 1984 630 643
    • (1984) Cancer , vol.53 , pp. 630-643
    • Wittliff, J.L.1
  • 186
    • 84863707351 scopus 로고    scopus 로고
    • Cancer treatment and survivorship statistics, 2012
    • Erratum in: CA Cancer J Clin 2012;62:348
    • R. Siegel, C. DeSantis, K. Virgo, K. Stein, A. Mariotto, and T. Smith Cancer treatment and survivorship statistics, 2012 CA Cancer J Clin 62 2012 220 241 Erratum in: CA Cancer J Clin 2012;62:348
    • (2012) CA Cancer J Clin , vol.62 , pp. 220-241
    • Siegel, R.1    Desantis, C.2    Virgo, K.3    Stein, K.4    Mariotto, A.5    Smith, T.6
  • 187
    • 33947285105 scopus 로고    scopus 로고
    • Docetaxel/anthracycline combinations for breast cancer treatment
    • G. von Minckwitz Docetaxel/anthracycline combinations for breast cancer treatment Expert Opin Pharmacother 8 2007 485 495
    • (2007) Expert Opin Pharmacother , vol.8 , pp. 485-495
    • Von Minckwitz, G.1
  • 188
    • 0037068741 scopus 로고    scopus 로고
    • Anti-tumor activity of GW572016: A dual tyrosine kinase inhibitor blocks EGF activation of EGFR/erbB2 and downstream Erk1/2 and AKT pathways
    • W. Xia, R.J. Mullin, B.R. Keith, L.H. Liu, H. Ma, and D.W. Rusnak Anti-tumor activity of GW572016: a dual tyrosine kinase inhibitor blocks EGF activation of EGFR/erbB2 and downstream Erk1/2 and AKT pathways Oncogene 21 2002 6255 6263
    • (2002) Oncogene , vol.21 , pp. 6255-6263
    • Xia, W.1    Mullin, R.J.2    Keith, B.R.3    Liu, L.H.4    Ma, H.5    Rusnak, D.W.6
  • 190
    • 84864539047 scopus 로고    scopus 로고
    • Systematic review of lapatinib in combination with letrozole compared with other first-line treatments for hormone receptor positive (HR+) and HER2+ advanced or metastatic breast cancer (MBC)
    • R. Riemsma, C.A. Forbes, M.M. Amonkar, K. Lykopoulos, J.R. Diaz, and J. Kleijnen Systematic review of lapatinib in combination with letrozole compared with other first-line treatments for hormone receptor positive (HR+) and HER2+ advanced or metastatic breast cancer (MBC) Curr Med Res Opin 28 2012 1263 1279
    • (2012) Curr Med Res Opin , vol.28 , pp. 1263-1279
    • Riemsma, R.1    Forbes, C.A.2    Amonkar, M.M.3    Lykopoulos, K.4    Diaz, J.R.5    Kleijnen, J.6
  • 191
    • 84886442748 scopus 로고    scopus 로고
    • Human breast cancer cells harboring a gatekeeper T798M mutation in HER2 overexpress EGFR ligands and are sensitive to dual inhibition of EGFR and HER2
    • B.N. Rexer, R. Ghosh, A. Narasanna, M.V. Estrada, A. Chakrabarty, and Y. Song Human breast cancer cells harboring a gatekeeper T798M mutation in HER2 overexpress EGFR ligands and are sensitive to dual inhibition of EGFR and HER2 Clin Cancer Res 19 2013 5390 5401
    • (2013) Clin Cancer Res , vol.19 , pp. 5390-5401
    • Rexer, B.N.1    Ghosh, R.2    Narasanna, A.3    Estrada, M.V.4    Chakrabarty, A.5    Song, Y.6
  • 192
    • 84862118767 scopus 로고    scopus 로고
    • Overcoming treatment resistance in HER2-positive breast cancer: Potential strategies
    • F. Puglisi, A.M. Minisini, C. De Angelis, and G. Arpino Overcoming treatment resistance in HER2-positive breast cancer: potential strategies Drugs 72 2012 1175 1193
    • (2012) Drugs , vol.72 , pp. 1175-1193
    • Puglisi, F.1    Minisini, A.M.2    De Angelis, C.3    Arpino, G.4
  • 193
    • 0024478054 scopus 로고
    • P185(HER2) monoclonal antibody has antiproliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor
    • R.M. Hudziak, G.D. Lewis, M. Winget, B.M. Fendly, H.M. Shepard, and A. Ullrich p185HER2 monoclonal antibody has antiproliferative effects in vitro and sensitizes human breast tumor cells to tumor necrosis factor Mol Cell Biol 9 1989 1165 1172 (Pubitemid 19071685)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.3 , pp. 1165-1172
    • Hudziak, R.M.1    Lewis, G.D.2    Winget, M.3    Fendly, B.M.4    Shepard, H.M.5    Ullrich, A.6
  • 196
    • 79955515055 scopus 로고    scopus 로고
    • Is cardiotoxicity being adequately assessed in current trials of cytotoxic and targeted agents in breast cancer?
    • S. Verma, and M.S. Ewer Is cardiotoxicity being adequately assessed in current trials of cytotoxic and targeted agents in breast cancer? Ann Oncol 22 2011 1011 1018
    • (2011) Ann Oncol , vol.22 , pp. 1011-1018
    • Verma, S.1    Ewer, M.S.2
  • 197
    • 0035169666 scopus 로고    scopus 로고
    • Mechanism of action of trastuzumab and scientific update
    • J. Baselga, J. Albanell, M.A. Molina, and J. Arribas Mechanism of action of trastuzumab and scientific update Semin Oncol 28 2001 4 11 (Pubitemid 33065104)
    • (2001) Seminars in Oncology , vol.28 , Issue.5 SUPPL. 16 , pp. 4-11
    • Baselga, J.1    Albanell, J.2    Molina, M.A.3    Arribas, J.4
  • 198
    • 37549011436 scopus 로고    scopus 로고
    • Elements related to heterogeneity of antibody-dependent cell cytotoxicity in patients under trastuzumab therapy for primary operable breast cancer overexpressing Her2
    • S. Varchetta, N. Gibelli, B. Oliviero, E. Nardini, R. Gennari, and G. Gatti Elements related to heterogeneity of antibody-dependent cell cytotoxicity in patients under trastuzumab therapy for primary operable breast cancer overexpressing Her2 Cancer Res 67 2007 11991 11999
    • (2007) Cancer Res , vol.67 , pp. 11991-11999
    • Varchetta, S.1    Gibelli, N.2    Oliviero, B.3    Nardini, E.4    Gennari, R.5    Gatti, G.6
  • 199
    • 84883821225 scopus 로고    scopus 로고
    • Antibody therapeutics in cancer
    • M.X. Sliwkowski, and I. Mellman Antibody therapeutics in cancer Science 341 2013 1192 1198
    • (2013) Science , vol.341 , pp. 1192-1198
    • Sliwkowski, M.X.1    Mellman, I.2
  • 200
    • 34347395733 scopus 로고    scopus 로고
    • Trastuzumab - Mechanism of action and use in clinical practice
    • DOI 10.1056/NEJMra043186
    • C.A. Hudis Trastuzumab - mechanism of action and use in clinical practice N Engl J Med 357 2007 39 51 (Pubitemid 47026733)
    • (2007) New England Journal of Medicine , vol.357 , Issue.1 , pp. 39-51
    • Hudis, C.A.1
  • 201
    • 55849126233 scopus 로고    scopus 로고
    • Signal integration: A framework for understanding the efficacy of therapeutics targeting the human EGFR family
    • H.M. Shepard, C.M. Brdlik, and H. Schreiber Signal integration: a framework for understanding the efficacy of therapeutics targeting the human EGFR family J Clin Invest 118 2008 3574 3581
    • (2008) J Clin Invest , vol.118 , pp. 3574-3581
    • Shepard, H.M.1    Brdlik, C.M.2    Schreiber, H.3
  • 202
    • 84861516765 scopus 로고    scopus 로고
    • Intrinsic and acquired resistance to HER2-targeted therapies in HER2 gene-amplified breast cancer: Mechanisms and clinical implications
    • B.N. Rexer, and C.L. Arteaga Intrinsic and acquired resistance to HER2-targeted therapies in HER2 gene-amplified breast cancer: mechanisms and clinical implications Crit Rev Oncog 17 2012 1 16
    • (2012) Crit Rev Oncog , vol.17 , pp. 1-16
    • Rexer, B.N.1    Arteaga, C.L.2
  • 203
    • 1842605531 scopus 로고    scopus 로고
    • Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
    • DOI 10.1016/S1535-6108(04)00083-2, PII S1535610804000832
    • M.C. Franklin, K.D. Carey, F.F. Vajdos, D.J. Leahy, A.M. de Vos, and M.X. Sliwkowski Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex Cancer Cell 5 2004 317 328 (Pubitemid 38482068)
    • (2004) Cancer Cell , vol.5 , Issue.4 , pp. 317-328
    • Franklin, M.C.1    Carey, K.D.2    Vajdos, F.F.3    Leahy, D.J.4    De Vos, A.M.5    Sliwkowski, M.X.6
  • 204
    • 84862914692 scopus 로고    scopus 로고
    • Pertuzumab plus trastuzumab plus docetaxel for metastatic breast cancer
    • J. Baselga, J. Cortés, S.B. Kim, S.A. Im, R. Hegg, and Y.H. Im Pertuzumab plus trastuzumab plus docetaxel for metastatic breast cancer N Engl J Med 366 2012 109 119
    • (2012) N Engl J Med , vol.366 , pp. 109-119
    • Baselga, J.1    Cortés, J.2    Kim, S.B.3    Im, S.A.4    Hegg, R.5    Im, Y.H.6
  • 205
    • 84884564646 scopus 로고    scopus 로고
    • First FDA approval of dual anti-HER2 regimen: Pertuzumab in combination with trastuzumab and docetaxel for HER2-positive metastatic breast cancer
    • G.M. Blumenthal, N.S. Scher, P. Cortazar, S. Chattopadhyay, S. Tang, and P. Song First FDA approval of dual anti-HER2 regimen: pertuzumab in combination with trastuzumab and docetaxel for HER2-positive metastatic breast cancer Clin Cancer Res 19 2013 4911 4916
    • (2013) Clin Cancer Res , vol.19 , pp. 4911-4916
    • Blumenthal, G.M.1    Scher, N.S.2    Cortazar, P.3    Chattopadhyay, S.4    Tang, S.5    Song, P.6
  • 207
    • 33644600485 scopus 로고    scopus 로고
    • Humanization of a recombinant monoclonal antibody to produce a therapeutic HER dimerization inhibitor, pertuzumab
    • C.W. Adams, D.E. Allison, K. Flagella, L. Presta, J. Clarke, and N. Dybdal Humanization of a recombinant monoclonal antibody to produce a therapeutic HER dimerization inhibitor, pertuzumab Cancer Immunol Immunother 55 2006 717 727
    • (2006) Cancer Immunol Immunother , vol.55 , pp. 717-727
    • Adams, C.W.1    Allison, D.E.2    Flagella, K.3    Presta, L.4    Clarke, J.5    Dybdal, N.6
  • 208
    • 56449129810 scopus 로고    scopus 로고
    • Targeting HER2-positive breast cancer with trastuzumab-DM1, an antibody-cytotoxic drug conjugate
    • G.D. Lewis Phillips, G. Li, D.L. Dugger, L.M. Crocker, K.L. Parsons, and E. Mai Targeting HER2-positive breast cancer with trastuzumab-DM1, an antibody-cytotoxic drug conjugate Cancer Res 68 2008 9280 9290
    • (2008) Cancer Res , vol.68 , pp. 9280-9290
    • Lewis Phillips, G.D.1    Li, G.2    Dugger, D.L.3    Crocker, L.M.4    Parsons, K.L.5    Mai, E.6
  • 209
    • 84868520609 scopus 로고    scopus 로고
    • Trastuzumab emtansine for HER2-positive advanced breast cancer
    • Erratum in: N Engl J Med 2013;368:2442
    • S. Verma, D. Miles, L. Gianni, I.E. Krop, M. Welslau, and J. Baselga Trastuzumab emtansine for HER2-positive advanced breast cancer N Engl J Med 367 2012 1783 1791 Erratum in: N Engl J Med 2013;368:2442
    • (2012) N Engl J Med , vol.367 , pp. 1783-1791
    • Verma, S.1    Miles, D.2    Gianni, L.3    Krop, I.E.4    Welslau, M.5    Baselga, J.6
  • 210
    • 80054092983 scopus 로고    scopus 로고
    • Trastuzumab emtansine: A unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer
    • P.M. LoRusso, D. Weiss, E. Guardino, S. Girish, and M.X. Sliwkowski Trastuzumab emtansine: a unique antibody-drug conjugate in development for human epidermal growth factor receptor 2-positive cancer Clin Cancer Res 17 2011 6437 6447
    • (2011) Clin Cancer Res , vol.17 , pp. 6437-6447
    • Lorusso, P.M.1    Weiss, D.2    Guardino, E.3    Girish, S.4    Sliwkowski, M.X.5
  • 211
    • 84876011018 scopus 로고    scopus 로고
    • Phase II randomized study of trastuzumab emtansine versus trastuzumab plus docetaxel in patients with human epidermal growth factor receptor 2-positive metastatic breast cancer
    • S.A. Hurvitz, L. Dirix, J. Kocsis, G.V. Bianchi, J. Lu, and J. Vinholes Phase II randomized study of trastuzumab emtansine versus trastuzumab plus docetaxel in patients with human epidermal growth factor receptor 2-positive metastatic breast cancer J Clin Oncol 31 2013 1157 1163
    • (2013) J Clin Oncol , vol.31 , pp. 1157-1163
    • Hurvitz, S.A.1    Dirix, L.2    Kocsis, J.3    Bianchi, G.V.4    Lu, J.5    Vinholes, J.6
  • 213
    • 0141788346 scopus 로고    scopus 로고
    • STI-571: An anticancer protein-tyrosine kinase inhibitor
    • DOI 10.1016/j.bbrc.2003.08.055
    • R. Roskoski Jr. STI-571: an anticancer protein-tyrosine kinase inhibitor Biochem Biophys Res Commun 309 2003 709 717 (Pubitemid 37122587)
    • (2003) Biochemical and Biophysical Research Communications , vol.309 , Issue.4 , pp. 709-717
    • Roskoski Jr., R.1
  • 216
  • 217
    • 84555196106 scopus 로고    scopus 로고
    • BRCA1 and BRCA2: Different roles in a common pathway of genome protection
    • R. Roy, J. Chun, and S.N. Powell BRCA1 and BRCA2: different roles in a common pathway of genome protection Nat Rev Cancer 12 2011 68 78
    • (2011) Nat Rev Cancer , vol.12 , pp. 68-78
    • Roy, R.1    Chun, J.2    Powell, S.N.3
  • 221
    • 59049091281 scopus 로고    scopus 로고
    • Meta-analysis of risk reduction estimates associated with risk-reducing salpingo-oophorectomy in BRCA1 or BRCA2 mutation carriers
    • T.R. Rebbeck, N.D. Kauff, and S.M. Domchek Meta-analysis of risk reduction estimates associated with risk-reducing salpingo-oophorectomy in BRCA1 or BRCA2 mutation carriers J Natl Cancer Inst 101 2009 80 87
    • (2009) J Natl Cancer Inst , vol.101 , pp. 80-87
    • Rebbeck, T.R.1    Kauff, N.D.2    Domchek, S.M.3
  • 222
    • 77956193440 scopus 로고    scopus 로고
    • Association of risk-reducing surgery in BRCA1 or BRCA2 mutation carriers with cancer risk and mortality
    • S.M. Domchek, T.M. Friebel, C.F. Singer, D.G. Evans, H.T. Lynch, and C. Isaacs Association of risk-reducing surgery in BRCA1 or BRCA2 mutation carriers with cancer risk and mortality J Am Med Assoc 304 2010 967 975
    • (2010) J Am Med Assoc , vol.304 , pp. 967-975
    • Domchek, S.M.1    Friebel, T.M.2    Singer, C.F.3    Evans, D.G.4    Lynch, H.T.5    Isaacs, C.6
  • 223
    • 78649663174 scopus 로고    scopus 로고
    • BRCA mutations in the management of breast cancer: The state of the art
    • S.A. Narod BRCA mutations in the management of breast cancer: the state of the art Nat Rev Clin Oncol 7 2010 702 707
    • (2010) Nat Rev Clin Oncol , vol.7 , pp. 702-707
    • Narod, S.A.1
  • 224
    • 84886448607 scopus 로고    scopus 로고
    • Tamoxifen and risk of contralateral breast cancer for BRCA1 and BRCA2 mutation carriers
    • K.A. Phillips, R.L. Milne, M.A. Rookus, M.B. Daly, A.C. Antoniou, and S. Peock Tamoxifen and risk of contralateral breast cancer for BRCA1 and BRCA2 mutation carriers J Clin Oncol 31 2013 3091 3099
    • (2013) J Clin Oncol , vol.31 , pp. 3091-3099
    • Phillips, K.A.1    Milne, R.L.2    Rookus, M.A.3    Daly, M.B.4    Antoniou, A.C.5    Peock, S.6
  • 226
    • 84886295592 scopus 로고    scopus 로고
    • Towards the goal of personalized medicine in gastric cancer - Time to move beyond HER2 inhibition. Part I: Targeting receptor tyrosine kinase gene amplification
    • J. Lee, and S.H. Ou Towards the goal of personalized medicine in gastric cancer - time to move beyond HER2 inhibition. Part I: Targeting receptor tyrosine kinase gene amplification Discov Med 15 2013 333 341
    • (2013) Discov Med , vol.15 , pp. 333-341
    • Lee, J.1    Ou, S.H.2
  • 228
    • 77956262693 scopus 로고    scopus 로고
    • Trastuzumab in combination with chemotherapy versus chemotherapy alone for treatment of HER2-positive advanced gastric or gastro-oesophageal junction cancer (ToGA): A phase 3, open-label, randomised controlled trial
    • Y.J. Bang, E. Van Cutsem, A. Feyereislova, H.C. Chung, L. Shen, and A. Sawaki Trastuzumab in combination with chemotherapy versus chemotherapy alone for treatment of HER2-positive advanced gastric or gastro-oesophageal junction cancer (ToGA): a phase 3, open-label, randomised controlled trial Lancet 376 2010 687 697
    • (2010) Lancet , vol.376 , pp. 687-697
    • Bang, Y.J.1    Van Cutsem, E.2    Feyereislova, A.3    Chung, H.C.4    Shen, L.5    Sawaki, A.6
  • 229
    • 17444403242 scopus 로고    scopus 로고
    • Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
    • DOI 10.1016/j.ccr.2005.03.003
    • S. Li, K.R. Schmitz, P.D. Jeffrey, J.J. Wiltzius, P. Kussie, and K.M. Ferguson Structural basis for inhibition of the epidermal growth factor receptor by cetuximab Cancer Cell 7 2005 301 311 (Pubitemid 40544648)
    • (2005) Cancer Cell , vol.7 , Issue.4 , pp. 301-311
    • Li, S.1    Schmitz, K.R.2    Jeffrey, P.D.3    Wiltzius, J.J.W.4    Kussie, P.5    Ferguson, K.M.6
  • 230
    • 0021254542 scopus 로고
    • Monoclonal anti-epidermal growth factor receptor antibodies which are inhibitors of epidermal growth factor binding and antagonists of epidermal growth factor-stimulated tyrosine protein kinase activity
    • G.N. Gill, T. Kawamoto, C. Cochet, A. Le, J.D. Sato, and H. Masui Monoclonal anti-epidermal growth factor receptor antibodies which are inhibitors of epidermal growth factor binding and antagonists of epidermal growth factor binding and antagonists of epidermal growth factor-stimulated tyrosine protein kinase activity J Biol Chem 259 1984 7755 7760 (Pubitemid 14081190)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.12 , pp. 7755-7760
    • Gill, G.N.1    Kawamoto, T.2    Cochet, C.3
  • 231
    • 0028819660 scopus 로고
    • Biological efficacy of a chimeric antibody to the epidermal growth factor receptor in a human tumor xenograft model
    • N.I. Goldstein, M. Prewett, K. Zuklys, P. Rockwell, and J. Mendelsohn Biological efficacy of a chimeric antibody to the epidermal growth factor receptor in a human tumor xenograft model Clin Cancer Res 1 1995 1311 1318
    • (1995) Clin Cancer Res , vol.1 , pp. 1311-1318
    • Goldstein, N.I.1    Prewett, M.2    Zuklys, K.3    Rockwell, P.4    Mendelsohn, J.5
  • 232
    • 0028116305 scopus 로고
    • Antibody-induced epidermal growth factor receptor dimerization mediates inhibition of autocrine proliferation of A431 squamous carcinoma cells
    • Z. Fan, Y. Lu, X. Wu, and J. Mendelsohn Antibody-induced epidermal growth factor receptor dimerization mediates inhibition of autocrine proliferation of A431 squamous carcinoma cells J Biol Chem 269 1994 27595 27602 (Pubitemid 24346592)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.44 , pp. 27595-27602
    • Fan, Z.1    Lu, Y.2    Wu, X.3    Mendelsohn, J.4
  • 233
    • 2142641698 scopus 로고    scopus 로고
    • Phase II trial of cetuximab in patients with refractory colorectal cancer that expresses the epidermal growth factor receptor
    • DOI 10.1200/JCO.2004.10.182
    • L.B. Saltz, N.J. Meropol, P.J. Loehrer Sr., M.N. Needle, J. Kopit, and R.J. Mayer Phase II trial of cetuximab in patients with refractory colorectal cancer that expresses the epidermal growth factor receptor J Clin Oncol 22 2004 1201 1208 (Pubitemid 41079832)
    • (2004) Journal of Clinical Oncology , vol.22 , Issue.7 , pp. 1201-1208
    • Saltz, L.B.1    Meropol, N.J.2    Loehrer Sr., P.J.3    Needle, M.N.4    Kopit, J.5    Mayer, R.J.6
  • 236
    • 17844362179 scopus 로고    scopus 로고
    • Gene copy number for epidermal growth factor receptor (EGFR) and clinical response to antiEGFR treatment in colorectal cancer: A cohort study
    • DOI 10.1016/S1470-2045(05)70102-9, PII S1470204505701029
    • M. Moroni, S. Veronese, S. Benvenuti, G. Marrapese, A. Sartore-Bianchi, and F. Di Nicolantonio Gene copy number for epidermal growth factor receptor (EGFR) and clinical response to antiEGFR treatment in colorectal cancer: a cohort study Lancet Oncol 6 2005 279 286 (Pubitemid 40590264)
    • (2005) Lancet Oncology , vol.6 , Issue.5 , pp. 279-286
    • Moroni, M.1    Veronese, S.2    Benvenuti, S.3    Marrapese, G.4    Sartore-Bianchi, A.5    Di Nicolantonio, F.6    Gambacorta, M.7    Siena, S.8    Bardelli, A.9
  • 238
    • 0035117355 scopus 로고    scopus 로고
    • Development of ABX-EGF, a fully human anti-EGF receptor monoclonal antibody, for cancer therapy
    • DOI 10.1016/S1040-8428(00)00134-7, PII S1040842800001347
    • X.D. Yang, X.C. Jia, J.R. Corvalan, P. Wang, and C.G. Davis Development of ABX-EGF, a fully human anti-EGF receptor monoclonal antibody, for cancer therapy Crit Rev Oncol Hematol 38 2001 17 23 (Pubitemid 32194591)
    • (2001) Critical Reviews in Oncology/Hematology , vol.38 , Issue.1 , pp. 17-23
    • Yang, X.-D.1    Jia, X.-C.2    Corvalan, J.R.F.3    Wang, P.4    Davis, C.G.5
  • 239
    • 34548289390 scopus 로고    scopus 로고
    • FDA drug approval summary: Panitumumab (Vectibix™)
    • DOI 10.1634/theoncologist.12-5-577
    • R.M. Giusti, K.A. Shastri, M.H. Cohen, P. Keegan, and R. Pazdur FDA drug approval summary: panitumumab (Vectibix) Oncologist 12 2007 577 583 (Pubitemid 350012121)
    • (2007) Oncologist , vol.12 , Issue.5 , pp. 577-583
    • Giusti, R.M.1    Shastri, K.A.2    Cohen, M.H.3    Keegan, P.4    Pazdur, R.5
  • 240
    • 84857050570 scopus 로고    scopus 로고
    • First-line panitumumab plus irinotecan/5-fluorouracil/leucovorin treatment in patients with metastatic colorectal cancer
    • C.H. Köhne, R. Hofheinz, L. Mineur, H. Letocha, R. Greil, and J. Thaler First-line panitumumab plus irinotecan/5-fluorouracil/leucovorin treatment in patients with metastatic colorectal cancer J Cancer Res Clin Oncol 138 2012 65 72
    • (2012) J Cancer Res Clin Oncol , vol.138 , pp. 65-72
    • Köhne, C.H.1    Hofheinz, R.2    Mineur, L.3    Letocha, H.4    Greil, R.5    Thaler, J.6
  • 242
    • 84872921660 scopus 로고    scopus 로고
    • Regorafenib monotherapy for previously treated metastatic colorectal cancer (CORRECT): An international, multicentre, randomised, placebo-controlled, phase 3 trial
    • A. Grothey, E. Van Cutsem, A. Sobrero, S. Siena, A. Falcone, and M. Ychou Regorafenib monotherapy for previously treated metastatic colorectal cancer (CORRECT): an international, multicentre, randomised, placebo-controlled, phase 3 trial Lancet 381 2013 303 312
    • (2013) Lancet , vol.381 , pp. 303-312
    • Grothey, A.1    Van Cutsem, E.2    Sobrero, A.3    Siena, S.4    Falcone, A.5    Ychou, M.6
  • 243
    • 79954499886 scopus 로고    scopus 로고
    • Regorafenib (BAY 73-4506): A new oral multikinase inhibitor of angiogenic, stromal and oncogenic receptor tyrosine kinases with potent preclinical antitumor activity
    • S.M. Wilhelm, J. Dumas, L. Adnane, M. Lynch, C.A. Carter, and G. Schütz Regorafenib (BAY 73-4506): a new oral multikinase inhibitor of angiogenic, stromal and oncogenic receptor tyrosine kinases with potent preclinical antitumor activity Int J Cancer 129 2011 245 255
    • (2011) Int J Cancer , vol.129 , pp. 245-255
    • Wilhelm, S.M.1    Dumas, J.2    Adnane, L.3    Lynch, M.4    Carter, C.A.5    Schütz, G.6
  • 245
    • 33947370773 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF) signaling in tumor progression
    • DOI 10.1016/j.critrevonc.2007.01.006, PII S1040842807000182
    • R. Roskoski Jr. Vascular endothelial growth factor (VEGF) signaling in tumor progression Crit Rev Oncol Hematol 62 2007 179 213 (Pubitemid 46679285)
    • (2007) Critical Reviews in Oncology/Hematology , vol.62 , Issue.3 , pp. 179-213
    • Roskoski Jr., R.1
  • 246
    • 27744551009 scopus 로고    scopus 로고
    • Structure and regulation of Kit protein-tyrosine kinase - The stem cell factor receptor
    • DOI 10.1016/j.bbrc.2005.09.150, PII S0006291X05021790
    • R. Roskoski Jr. Structure and regulation of Kit protein-tyrosine kinase - the stem cell factor receptor Biochem Biophys Res Commun 338 2005 1307 1315 (Pubitemid 41608395)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.3 , pp. 1307-1315
    • Roskoski Jr., R.1
  • 249
    • 84877058668 scopus 로고    scopus 로고
    • Approval summary: Cetuximab in combination with cisplatin or carboplatin and 5-fluorouracil for the first-line treatment of patients with recurrent locoregional or metastatic squamous cell head and neck cancer
    • M.H. Cohen, H. Chen, S. Shord, C. Fuchs, K. He, and H. Zhao Approval summary: cetuximab in combination with cisplatin or carboplatin and 5-fluorouracil for the first-line treatment of patients with recurrent locoregional or metastatic squamous cell head and neck cancer Oncologist 18 2013 460 466
    • (2013) Oncologist , vol.18 , pp. 460-466
    • Cohen, M.H.1    Chen, H.2    Shord, S.3    Fuchs, C.4    He, K.5    Zhao, H.6
  • 251
    • 77951709577 scopus 로고    scopus 로고
    • Preoperative/neoadjuvant therapy in pancreatic cancer: A systematic review and meta-analysis of response and resection percentages
    • S. Gillen, T. Schuster, C. Meyer Zum Büschenfelde, H. Friess, and J. Kleeff Preoperative/neoadjuvant therapy in pancreatic cancer: a systematic review and meta-analysis of response and resection percentages PLoS Med 7 2010 e1000267
    • (2010) PLoS Med , vol.7 , pp. 1000267
    • Gillen, S.1    Schuster, T.2    Meyer Zum Büschenfelde, C.3    Friess, H.4    Kleeff, J.5
  • 252
    • 84881523670 scopus 로고    scopus 로고
    • Mechanisms of resistance to chemotherapeutic and anti-angiogenic drugs as novel targets for pancreatic cancer therapy
    • A. Tamburrino, G. Piro, C. Carbone, G. Tortora, and D. Melisi Mechanisms of resistance to chemotherapeutic and anti-angiogenic drugs as novel targets for pancreatic cancer therapy Front Pharmacol 4 2013 56
    • (2013) Front Pharmacol , vol.4 , pp. 56
    • Tamburrino, A.1    Piro, G.2    Carbone, C.3    Tortora, G.4    Melisi, D.5
  • 256
    • 84857097612 scopus 로고    scopus 로고
    • Pancreatic cancer: Medical management (novel chemotherapeutics)
    • D. Páez, M.J. Labonte, and H.J. Lenz Pancreatic cancer: medical management (novel chemotherapeutics) Gastroenterol Clin North Am 41 2012 189 209
    • (2012) Gastroenterol Clin North Am , vol.41 , pp. 189-209
    • Páez, D.1    Labonte, M.J.2    Lenz, H.J.3
  • 257
    • 6044241807 scopus 로고    scopus 로고
    • The correlation between cytoplasmic overexpression of epidermal growth factor receptor and tumor aggressiveness: Poor prognosis in patients with pancreatic ductal adenocarcinoma
    • S. Ueda, S. Ogata, H. Tsuda, N. Kawarabayashi, M. Kimura, and Y. Sugiura The correlation between cytoplasmic overexpression of epidermal growth factor receptor and tumor aggressiveness: poor prognosis in patients with pancreatic ductal adenocarcinoma Pancreas 29 2004 e1 e8
    • (2004) Pancreas , vol.29
    • Ueda, S.1    Ogata, S.2    Tsuda, H.3    Kawarabayashi, N.4    Kimura, M.5    Sugiura, Y.6
  • 258
    • 0036690404 scopus 로고    scopus 로고
    • Effects of the epidermal growth factor receptor inhibitor OSI-774, Tarceva, on downstream signaling pathways and apoptosis in human pancreatic adenocarcinoma
    • S.S. Ng, M.S. Tsao, T. Nicklee, and D.W. Hedley Effects of the epidermal growth factor receptor inhibitor OSI-774, Tarceva, on downstream signaling pathways and apoptosis in human pancreatic adenocarcinoma Mol Cancer Ther 1 2002 777 783
    • (2002) Mol Cancer Ther , vol.1 , pp. 777-783
    • Ng, S.S.1    Tsao, M.S.2    Nicklee, T.3    Hedley, D.W.4
  • 260
    • 65549150854 scopus 로고    scopus 로고
    • Phase III trial of bevacizumab in combination with gemcitabine and erlotinib in patients with metastatic pancreatic cancer
    • E. Van Cutsem, W.L. Vervenne, J. Bennouna, Y. Humblet, S. Gill, and J.L. Van Laethem Phase III trial of bevacizumab in combination with gemcitabine and erlotinib in patients with metastatic pancreatic cancer J Clin Oncol 27 2009 2231 2237
    • (2009) J Clin Oncol , vol.27 , pp. 2231-2237
    • Van Cutsem, E.1    Vervenne, W.L.2    Bennouna, J.3    Humblet, Y.4    Gill, S.5    Van Laethem, J.L.6
  • 261
    • 0024292722 scopus 로고
    • Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes
    • C. Almoguera, D. Shibata, K. Forrester, J. Martin, N. Arnheim, and M. Perucho Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes Cell 53 1988 549 554
    • (1988) Cell , vol.53 , pp. 549-554
    • Almoguera, C.1    Shibata, D.2    Forrester, K.3    Martin, J.4    Arnheim, N.5    Perucho, M.6
  • 263
    • 84868023931 scopus 로고    scopus 로고
    • CBTRUS statistical report: Primary brain and central nervous system tumors diagnosed in the United States in 2005-2009
    • Erratum in: Neuro-Oncol 2013;15:646-7
    • T.A. Dolecek, J.M. Propp, N.E. Stroup, and C. Kruchko CBTRUS statistical report: primary brain and central nervous system tumors diagnosed in the United States in 2005-2009 Neuro-oncol 14 2012 1 49 Erratum in: Neuro-Oncol 2013;15:646-7
    • (2012) Neuro-oncol , vol.14 , pp. 1-49
    • Dolecek, T.A.1    Propp, J.M.2    Stroup, N.E.3    Kruchko, C.4
  • 266
    • 84863009497 scopus 로고    scopus 로고
    • Molecular characteristics and pathways of Avastin for the treatment of glioblastoma multiforme
    • M. Spasic, F. Chow, C. Tu, D.T. Nagasawa, and I. Yang Molecular characteristics and pathways of Avastin for the treatment of glioblastoma multiforme Neurosurg Clin N Am 23 2012 417 427
    • (2012) Neurosurg Clin N Am , vol.23 , pp. 417-427
    • Spasic, M.1    Chow, F.2    Tu, C.3    Nagasawa, D.T.4    Yang, I.5
  • 267
    • 77956868654 scopus 로고    scopus 로고
    • Epidermal growth factor receptor in glioma: Signal transduction, neuropathology, imaging, and radioresistance
    • K.J. Hatanpaa, S. Burma, D. Zhao, and A.A. Habib Epidermal growth factor receptor in glioma: signal transduction, neuropathology, imaging, and radioresistance Neoplasia 12 2010 675 684
    • (2010) Neoplasia , vol.12 , pp. 675-684
    • Hatanpaa, K.J.1    Burma, S.2    Zhao, D.3    Habib, A.A.4
  • 268
    • 0025790916 scopus 로고
    • Genes for epidermal growth factor receptor, transforming growth factor α, and epidermal growth factor and their expression in human gliomas in vivo
    • A.J. Ekstrand, C.D. James, W.K. Cavenee, B. Seliger, R.F. Pettersson, and V.P. Collins Genes for epidermal growth factor receptor, transforming growth factor α, and epidermal growth factor and their expression in human gliomas in vivo Cancer Res 51 1991 2164 2172
    • (1991) Cancer Res , vol.51 , pp. 2164-2172
    • Ekstrand, A.J.1    James, C.D.2    Cavenee, W.K.3    Seliger, B.4    Pettersson, R.F.5    Collins, V.P.6
  • 270
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • DOI 10.1016/S0169-409X(00)00129-0, PII S0169409X00001290
    • C.A. Lipinski, F. Lombardo, B.W. Dominy, and P.J. Feeney Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Adv Drug Deliv Rev 46 2001 3 26 (Pubitemid 33653411)
    • (2000) Advanced Drug Delivery Reviews , vol.46 , Issue.1-3 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 271
    • 0035553174 scopus 로고    scopus 로고
    • The effects of the novel, reversible epidermal growth factor receptor/ErbB-2 tyrosine kinase inhibitor, GW2016, on the growth of human normal and tumor-derived cell lines in vitro and in vivo
    • D.W. Rusnak, K. Lackey, K. Affleck, E.R. Wood, K.J. Alligood, and N. Rhodes The effects of the novel, reversible epidermal growth factor receptor/ErbB-2 tyrosine kinase inhibitor, GW2016, on the growth of human normal and tumor-derived cell lines in vitro and in vivo Mol Cancer Ther 1 2001 85 94
    • (2001) Mol Cancer Ther , vol.1 , pp. 85-94
    • Rusnak, D.W.1    Lackey, K.2    Affleck, K.3    Wood, E.R.4    Alligood, K.J.5    Rhodes, N.6
  • 272
    • 84866879823 scopus 로고    scopus 로고
    • The influence of lipophilicity in drug discovery and design
    • J.A. Arnott, and S.L. Planey The influence of lipophilicity in drug discovery and design Expert Opin Drug Discov 86 10 2012 3 75
    • (2012) Expert Opin Drug Discov , vol.86 , Issue.10 , pp. 3-75
    • Arnott, J.A.1    Planey, S.L.2
  • 273
    • 77956186444 scopus 로고    scopus 로고
    • Medicinal chemistry by the numbers: The physicochemistry, thermodynamics and kinetics of modern drug design
    • G.F. Smith Medicinal chemistry by the numbers: the physicochemistry, thermodynamics and kinetics of modern drug design Prog Med Chem 48 2009 1 29
    • (2009) Prog Med Chem , vol.48 , pp. 1-29
    • Smith, G.F.1
  • 274
    • 80052974259 scopus 로고    scopus 로고
    • Improving drug candidates by design: A focus on physicochemical properties as a means of improving compound disposition and safety
    • N.A. Meanwell Improving drug candidates by design: a focus on physicochemical properties as a means of improving compound disposition and safety Chem Res Toxicol 24 2011 1420 1456
    • (2011) Chem Res Toxicol , vol.24 , pp. 1420-1456
    • Meanwell, N.A.1
  • 275
    • 35748934487 scopus 로고    scopus 로고
    • The influence of drug-like concepts on decision-making in medicinal chemistry
    • DOI 10.1038/nrd2445, PII NRD2445
    • P.D. Leeson, and B. Springthorpe The influence of drug-like concepts on decision-making in medicinal chemistry Nat Rev Drug Discov 6 2007 881 890 (Pubitemid 350042396)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.11 , pp. 881-890
    • Leeson, P.D.1    Springthorpe, B.2
  • 277
    • 0000636701 scopus 로고
    • The initial clinical trial of nitrogen mustard
    • A. Gilman The initial clinical trial of nitrogen mustard Am J Surg 105 1963 574 578
    • (1963) Am J Surg , vol.105 , pp. 574-578
    • Gilman, A.1
  • 279
    • 84873620874 scopus 로고    scopus 로고
    • Understanding the mechanism of cytochrome P450 3A4: Recent advances and remaining problems
    • I.F. Sevrioukova, and T.L. Poulos Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems Dalton Trans 42 2013 3116 3126
    • (2013) Dalton Trans , vol.42 , pp. 3116-3126
    • Sevrioukova, I.F.1    Poulos, T.L.2
  • 280
    • 43749104916 scopus 로고    scopus 로고
    • Intestinal first-pass metabolism of CYP3A4 substrates
    • M. Kato Intestinal first-pass metabolism of CYP3A4 substrates Drug Metab Pharmacokinet 23 2008 87 94
    • (2008) Drug Metab Pharmacokinet , vol.23 , pp. 87-94
    • Kato, M.1
  • 282
    • 3142523464 scopus 로고    scopus 로고
    • Effects of regular consumption of grapefruit juice on the pharmacokinetics of simvastatin
    • DOI 10.1111/j.1365-2125.2004.02095.x
    • J.J. Lilja, M. Neuvonen, and P.J. Neuvonen Effects of regular consumption of grapefruit juice on the pharmacokinetics of simvastatin Br J Clin Pharmacol 58 2004 56 60 (Pubitemid 38901467)
    • (2004) British Journal of Clinical Pharmacology , vol.58 , Issue.1 , pp. 56-60
    • Lilja, J.J.1    Neuvonen, M.2    Neuvonen, P.J.3
  • 284
    • 0031894195 scopus 로고    scopus 로고
    • Long-term follow-up of a phase III study of three versus four cycles of bleomycin, etoposide, and cisplatin in favorable-prognosis germ-cell tumors: The Indiana University experience
    • S.B. Saxman, D. Finch, R. Gonin, and L.H. Einhorn Long-term follow-up of a phase III study of three versus four cycles of bleomycin, etoposide, and cisplatin in favorable-prognosis germ-cell tumors: the Indiana University experience J Clin Oncol 16 1998 702 706 (Pubitemid 28135618)
    • (1998) Journal of Clinical Oncology , vol.16 , Issue.2 , pp. 702-706
    • Saxman, S.B.1    Finch, D.2    Gonin, R.3    Einhorn, L.H.4
  • 286
  • 287
  • 288
    • 84855866971 scopus 로고    scopus 로고
    • Current management of gestational trophoblastic neoplasia
    • D.P. Goldstein, and R.S. Berkowitz Current management of gestational trophoblastic neoplasia Hematol Oncol Clin North Am 26 2012 111 131
    • (2012) Hematol Oncol Clin North Am , vol.26 , pp. 111-131
    • Goldstein, D.P.1    Berkowitz, R.S.2
  • 289
    • 84874984511 scopus 로고    scopus 로고
    • Combination chemotherapy for primary treatment of high-risk gestational trophoblastic tumour
    • L. Deng, J. Zhang, T. Wu, and T.A. Lawrie Combination chemotherapy for primary treatment of high-risk gestational trophoblastic tumour Cochrane Database Syst Rev 1 2013 CD005196
    • (2013) Cochrane Database Syst Rev , vol.1 , pp. 005196
    • Deng, L.1    Zhang, J.2    Wu, T.3    Lawrie, T.A.4
  • 290
    • 59949084951 scopus 로고    scopus 로고
    • Clinical cancer advances 2008: Major research advances in cancer treatment, prevention, and screening - A report from the American Society of Clinical Oncology
    • Erratum in: J Clin Oncol 2009;27:3070-1
    • E. Winer, J. Gralow, L. Diller, B. Karlan, P. Loehrer, and L. Pierce Clinical cancer advances 2008: major research advances in cancer treatment, prevention, and screening - a report from the American Society of Clinical Oncology J Clin Oncol 27 2009 812 826 Erratum in: J Clin Oncol 2009;27:3070-1
    • (2009) J Clin Oncol , vol.27 , pp. 812-826
    • Winer, E.1    Gralow, J.2    Diller, L.3    Karlan, B.4    Loehrer, P.5    Pierce, L.6
  • 291
    • 80755125625 scopus 로고    scopus 로고
    • Selection of therapy: Rational decisions based on molecular events
    • J.S. Khorashad, and M.W. Deininger Selection of therapy: rational decisions based on molecular events Hematol Oncol Clin North Am 25 2011 1009 1023
    • (2011) Hematol Oncol Clin North Am , vol.25 , pp. 1009-1023
    • Khorashad, J.S.1    Deininger, M.W.2
  • 292
    • 84904380175 scopus 로고    scopus 로고
    • The chronic leukemias
    • L. Goldman, A. Schafer, W. Arend, 24th ed. Elsevier Saunders Philadelphia
    • H. Kantarjian, and S. O'Brien The chronic leukemias L. Goldman, A. Schafer, W. Arend, Cecil medicine 24th ed. 2012 Elsevier Saunders Philadelphia 1209 1218
    • (2012) Cecil Medicine , pp. 1209-1218
    • Kantarjian, H.1    O'Brien, S.2
  • 293
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • D. Hanahan, and R.A. Weinberg Hallmarks of cancer: the next generation Cell 144 2011 646 674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 295
    • 77953687871 scopus 로고    scopus 로고
    • HER2 targeting as a two-sided strategy for breast cancer diagnosis and treatment: Outlook and recent implications in nanomedical approaches
    • M. Colombo, F. Corsi, D. Foschi, E. Mazzantini, S. Mazzucchelli, and C. Morasso HER2 targeting as a two-sided strategy for breast cancer diagnosis and treatment: outlook and recent implications in nanomedical approaches Pharmacol Res 62 2010 150 165
    • (2010) Pharmacol Res , vol.62 , pp. 150-165
    • Colombo, M.1    Corsi, F.2    Foschi, D.3    Mazzantini, E.4    Mazzucchelli, S.5    Morasso, C.6
  • 296
    • 75149130051 scopus 로고    scopus 로고
    • Targeting the cancer kinome through polypharmacology
    • Z.A. Knight, H. Lin, and K.M. Shokat Targeting the cancer kinome through polypharmacology Nat Rev Cancer 10 2010 130 137
    • (2010) Nat Rev Cancer , vol.10 , pp. 130-137
    • Knight, Z.A.1    Lin, H.2    Shokat, K.M.3
  • 297
    • 84885021477 scopus 로고    scopus 로고
    • Drug rechallenge and treatment beyond progression-implications for drug resistance
    • E.A. Kuczynski, D.J. Sargent, A. Grothey, and R.S. Kerbel Drug rechallenge and treatment beyond progression-implications for drug resistance Nat Rev Clin Oncol 10 2013 571 587
    • (2013) Nat Rev Clin Oncol , vol.10 , pp. 571-587
    • Kuczynski, E.A.1    Sargent, D.J.2    Grothey, A.3    Kerbel, R.S.4
  • 298
    • 0942287932 scopus 로고    scopus 로고
    • Effect of re-treatment with gefitinib ('Iressa', ZD1839) after acquisition of resistance
    • T. Kurata, K. Tamura, H. Kaneda, T. Nogami, H. Uejima, and Asai Go Go Effect of re-treatment with gefitinib ('Iressa', ZD1839) after acquisition of resistance Ann Oncol 15 2004 173 174
    • (2004) Ann Oncol , vol.15 , pp. 173-174
    • Kurata, T.1    Tamura, K.2    Kaneda, H.3    Nogami, T.4    Uejima, H.5    Go Go, A.6
  • 299
    • 20444456682 scopus 로고    scopus 로고
    • Retreatment of lung adenocarcinoma patients with gefitinib who had experienced favorable results from their initial treatment with this selective epidermal growth factor receptor inhibitor: A report of three cases
    • S. Yano, E. Nakataki, S. Ohtsuka, M. Inayama, H. Tomimoto, and N. Edakuni Retreatment of lung adenocarcinoma patients with gefitinib who had experienced favorable results from their initial treatment with this selective epidermal growth factor receptor inhibitor: a report of three cases Oncol Res 15 2005 107 111 (Pubitemid 40825922)
    • (2005) Oncology Research , vol.15 , Issue.2 , pp. 107-111
    • Yano, S.1    Nakataki, E.2    Ohtsuka, S.3    Inayama, M.4    Tomimoto, H.5    Edakuni, N.6    Kakiuchi, S.7    Nishikubo, N.8    Muguruma, H.9    Sone, S.10
  • 300
    • 58149132001 scopus 로고    scopus 로고
    • Lung cancer response to gefitinib, then erlotinib, then gefitinib again
    • A.S. Wong, K.Y. Seto, T.M. Chin, and R.A. Soo Lung cancer response to gefitinib, then erlotinib, then gefitinib again J Thorac Oncol 3 2008 1077 1078
    • (2008) J Thorac Oncol , vol.3 , pp. 1077-1078
    • Wong, A.S.1    Seto, K.Y.2    Chin, T.M.3    Soo, R.A.4
  • 301
    • 84861735070 scopus 로고    scopus 로고
    • Treatment selection in metastatic renal cell carcinoma: Expert consensus
    • B. Escudier, C. Szczylik, C. Porta, and M. Gore Treatment selection in metastatic renal cell carcinoma: expert consensus Nat Rev Clin Oncol 9 2012 327 337
    • (2012) Nat Rev Clin Oncol , vol.9 , pp. 327-337
    • Escudier, B.1    Szczylik, C.2    Porta, C.3    Gore, M.4
  • 302
    • 80053531654 scopus 로고    scopus 로고
    • Disease flare after tyrosine kinase inhibitor discontinuation in patients with EGFR-mutant lung cancer and acquired resistance to erlotinib or gefitinib: Implications for clinical trial design
    • J.E. Chaft, G.R. Oxnard, C.S. Sima, M.G. Kris, V.A. Miller, and G.J. Riely Disease flare after tyrosine kinase inhibitor discontinuation in patients with EGFR-mutant lung cancer and acquired resistance to erlotinib or gefitinib: implications for clinical trial design Clin Cancer Res 17 2011 6298 6303
    • (2011) Clin Cancer Res , vol.17 , pp. 6298-6303
    • Chaft, J.E.1    Oxnard, G.R.2    Sima, C.S.3    Kris, M.G.4    Miller, V.A.5    Riely, G.J.6
  • 303
    • 84890018871 scopus 로고    scopus 로고
    • Emerging paradigms in the development of resistance to tyrosine kinase inhibitors in lung cancer
    • J.F. Gainor, and A.T. Shaw Emerging paradigms in the development of resistance to tyrosine kinase inhibitors in lung cancer J Clin Oncol 31 2013 3987 3996
    • (2013) J Clin Oncol , vol.31 , pp. 3987-3996
    • Gainor, J.F.1    Shaw, A.T.2
  • 304
    • 84865553918 scopus 로고    scopus 로고
    • Cetuximab rechallenge in metastatic colorectal cancer patients: How to come away from acquired resistance?
    • D. Santini, B. Vincenzi, R. Addeo, C. Garufi, G. Masi, and M. Scartozzi Cetuximab rechallenge in metastatic colorectal cancer patients: how to come away from acquired resistance? Ann Oncol 23 2012 2313 2318
    • (2012) Ann Oncol , vol.23 , pp. 2313-2318
    • Santini, D.1    Vincenzi, B.2    Addeo, R.3    Garufi, C.4    Masi, G.5    Scartozzi, M.6
  • 305
    • 84886719809 scopus 로고    scopus 로고
    • Cancer drugs in the United States: Justum pretium - The just price
    • H.M. Kantarjian, T. Fojo, M. Mathisen, and L.A. Zwelling Cancer drugs in the United States: justum pretium - the just price J Clin Oncol 31 2013 3600 3604
    • (2013) J Clin Oncol , vol.31 , pp. 3600-3604
    • Kantarjian, H.M.1    Fojo, T.2    Mathisen, M.3    Zwelling, L.A.4


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