메뉴 건너뛰기




Volumn 7, Issue 7, 2006, Pages 505-516

EGF-ERBB signalling: Towards the systems level

Author keywords

[No Author keywords available]

Indexed keywords

17 ALLYLAMINO 17 DEMETHOXYGELDANAMYCIN; CANERTINIB; CETUXIMAB; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; ERLOTINIB; GEFITINIB; HEAT SHOCK PROTEIN 90 INHIBITOR; LAPATINIB; LIGAND; PELITINIB; PERTUZUMAB; PHOSPHATIDYLINOSITOL 3 KINASE; TRASTUZUMAB;

EID: 33745828702     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm1962     Document Type: Review
Times cited : (1693)

References (142)
  • 1
    • 0033608993 scopus 로고    scopus 로고
    • The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors
    • Klapper, L. N. et al. The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors. Proc. Natl Acad. Sci. USA 96, 4995-5000 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4995-5000
    • Klapper, L.N.1
  • 5
    • 7644238181 scopus 로고    scopus 로고
    • Biological robustness
    • Kitano, H. Biological robustness. Nature Rev. Genet. 5, 826-837 (2004). An introductory text to systems biology that describes the principles of robustness in biological systems.
    • (2004) Nature Rev. Genet. , vol.5 , pp. 826-837
    • Kitano, H.1
  • 6
    • 33746905531 scopus 로고    scopus 로고
    • Phosphotyrosine interactome of the ErbB-receptor kinase family
    • Schulze, W. X., Deng, L. & Mann, M. Phosphotyrosine interactome of the ErbB-receptor kinase family. Mol. Syst. Biol. 1, 42-54 (2005).
    • (2005) Mol. Syst. Biol. , vol.1 , pp. 42-54
    • Schulze, W.X.1    Deng, L.2    Mann, M.3
  • 7
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • Levkowitz, G. et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol. Cell 4, 1029-1040 (1999). Identified c-Cbl as the phospho-activated ubiquitin-ligase that mediates EGF-receptor degradation.
    • (1999) Mol. Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1
  • 8
    • 0029074587 scopus 로고
    • Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor
    • Miettinen, P. J. et al. Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor. Nature 376, 337-341 (1995).
    • (1995) Nature , vol.376 , pp. 337-341
    • Miettinen, P.J.1
  • 9
    • 0029064203 scopus 로고
    • Targeted disruption of mouse EGF receptor: Effect of genetic background on mutant phenotype
    • Threadgill, D. W. et al. Targeted disruption of mouse EGF receptor: effect of genetic background on mutant phenotype. Science 269, 230-234 (1995).
    • (1995) Science , vol.269 , pp. 230-234
    • Threadgill, D.W.1
  • 10
    • 0029045856 scopus 로고
    • Strain-dependent epithelial defects in mice lacking the EGF receptor
    • Sibilia, M. & Wagner, E. F. Strain-dependent epithelial defects in mice lacking the EGF receptor. Science 269, 234-238 (1995).
    • (1995) Science , vol.269 , pp. 234-238
    • Sibilia, M.1    Wagner, E.F.2
  • 11
    • 0032472938 scopus 로고    scopus 로고
    • A strain-independent postnatal neurodegeneration in mice lacking the EGF receptor
    • Sibilia, M., Steinbach, J. P., Stingl, L., Aguzzi, A. & Wagner, E. F. A strain-independent postnatal neurodegeneration in mice lacking the EGF receptor. EMBO J. 17, 719-731 (1998). References 8-11 describe the phenotypes of Egfr knockouts that show variable defects depending on genetic background.
    • (1998) EMBO J. , vol.17 , pp. 719-731
    • Sibilia, M.1    Steinbach, J.P.2    Stingl, L.3    Aguzzi, A.4    Wagner, E.F.5
  • 12
    • 0032795261 scopus 로고    scopus 로고
    • Targeted inactivation of the EGF and amphiregulin genes reveals distinct roles for EGF receptor ligands in mouse mammary gland development
    • Luetteke, N. C. et al. Targeted inactivation of the EGF and amphiregulin genes reveals distinct roles for EGF receptor ligands in mouse mammary gland development. Development 126, 2739-2750 (1999).
    • (1999) Development , vol.126 , pp. 2739-2750
    • Luetteke, N.C.1
  • 13
    • 0027315183 scopus 로고
    • Mice with null mutations of the TGFα gene have abnormal skin architecture, wavy hair, and curly whiskers and often develop corneal inflammation
    • Mann, G. et al. Mice with null mutations of the TGFα gene have abnormal skin architecture, wavy hair, and curly whiskers and often develop corneal inflammation. Cell 73, 249-261 (1993).
    • (1993) Cell , vol.73 , pp. 249-261
    • Mann, G.1
  • 14
    • 0034950574 scopus 로고    scopus 로고
    • Growth retardation, duodenal lesions, and aberrant ileum architecture in triple null mice lacking EGF, amphiregulin, and TGF-α
    • Troyer, K. L. et al. Growth retardation, duodenal lesions, and aberrant ileum architecture in triple null mice lacking EGF, amphiregulin, and TGF-α. Gastroenterology 121, 68-78 (2001).
    • (2001) Gastroenterology , vol.121 , pp. 68-78
    • Troyer, K.L.1
  • 15
    • 0027297643 scopus 로고
    • TGFα deficiency results in hair follicles and eye abnormalities in targeted and waved-1 mice
    • Luetteke, N. C. et al. TGFα deficiency results in hair follicles and eye abnormalities in targeted and waved-1 mice. Cell 73, 263-278 (1993). References 12-15 describe the phenotypes of knockouts of EGFR ligands, which are milder than the phenotype of the EGFR knockout.
    • (1993) Cell , vol.73 , pp. 263-278
    • Luetteke, N.C.1
  • 16
    • 0028344729 scopus 로고
    • The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase
    • Luetteke, N. C. et al. The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase. Genes Dev. 8, 399-413 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 399-413
    • Luetteke, N.C.1
  • 17
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor
    • Tzahar, E. et al. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol. Cell. Biol. 16, 5276-5287 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5276-5287
    • Tzahar, E.1
  • 18
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • Jones, R. B., Gordus, A., Krall, J. A. & Macbeath, G. A quantitative protein interaction network for the ErbB receptors using protein microarrays. Natures 439, 168-174 (2006).
    • (2006) Natures , vol.439 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    Macbeath, G.4
  • 19
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida, J., Kraus, M. H., Alimandi, M., Di Fiore, P. P. & Carpenter, G. All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. J. Biol. Chem. 271, 5251-5257 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5
  • 20
    • 0033605560 scopus 로고    scopus 로고
    • ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors
    • Worthylake, R., Opresko, L. K. & Wiley, H. S. ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors. J. Biol. Chem. 274, 8865-8874 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8865-8874
    • Worthylake, R.1    Opresko, L.K.2    Wiley, H.S.3
  • 21
    • 0032526729 scopus 로고    scopus 로고
    • Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers
    • Lenferink, A. E. et al. Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers. EMBO J. 17, 3385-3397 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3385-3397
    • Lenferink, A.E.1
  • 22
    • 2142843806 scopus 로고    scopus 로고
    • Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions
    • Pinkas-Kramarski, R. et al. Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions. EMBO J. 15, 2452-2467 (1996). Shows that ERBB2, rather than functioning as an autonomous, ligand-activated receptor, is a shared co-receptor that amplifies the signalling potential of the other ERBBs.
    • (1996) EMBO J. , vol.15 , pp. 2452-2467
    • Pinkas-Kramarski, R.1
  • 23
    • 0033564877 scopus 로고    scopus 로고
    • The C-terminus of the kinase-defective neuregulin receptor ErbB-3 confers mitogenic superiority and dictates endocytic routing
    • Waterman, H., Alroy, I., Strano, S., Seger, R. & Yarden, Y. The C-terminus of the kinase-defective neuregulin receptor ErbB-3 confers mitogenic superiority and dictates endocytic routing. EMBO J. 18, 3348-3358 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3348-3358
    • Waterman, H.1    Alroy, I.2    Strano, S.3    Seger, R.4    Yarden, Y.5
  • 24
    • 0029162564 scopus 로고
    • Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3
    • Wallasch, C. et al. Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. EMBO J. 14, 4267-4275 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4267-4275
    • Wallasch, C.1
  • 25
    • 0031827634 scopus 로고    scopus 로고
    • Expression of the c-erbB-4/HER4 protein and mRNA in normal human fetal and adult tissues and in a survey of nine solid tumour types
    • Srinivisan, R., Poulsom, R., Hurst, H. C. & Gullick, W. Expression of the c-erbB-4/HER4 protein and mRNA in normal human fetal and adult tissues and in a survey of nine solid tumour types. J. Pathol. 185, 236-245 (1998).
    • (1998) J. Pathol. , vol.185 , pp. 236-245
    • Srinivisan, R.1    Poulsom, R.2    Hurst, H.C.3    Gullick, W.4
  • 26
    • 0034616385 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme is required for cleavage of erbB4/HER4
    • Rio, C., Buxbaum, J. D., Peschon, J. J. & Corfas, G. Tumor necrosis factor-α-converting enzyme is required for cleavage of erbB4/HER4. J. Biol. Chem. 275, 10379-10387 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 10379-10387
    • Rio, C.1    Buxbaum, J.D.2    Peschon, J.J.3    Corfas, G.4
  • 27
    • 0033594546 scopus 로고    scopus 로고
    • Characterization of a naturally occurring ErbB4 isoform that does not bind or activate phosphatidyl inositol 3-kinase
    • Elenius, K. et al. Characterization of a naturally occurring ErbB4 isoform that does not bind or activate phosphatidyl inositol 3-kinase. Oncogene 18, 2607-2615 (1999).
    • (1999) Oncogene , vol.18 , pp. 2607-2615
    • Elenius, K.1
  • 28
    • 0035824391 scopus 로고    scopus 로고
    • γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni, C. Y., Murphy, M. P., Golde, T. E. & Carpenter, G. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294, 2179-2181 (2001). Description of ERBB4 cleavage that leads to formation of a soluble intracellular domain, which might function independently of the membrane-associated receptor.
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 29
    • 0028827104 scopus 로고
    • Multiple essential functions of neuregulin in development
    • Meyer, D. & Birchmeier, C. Multiple essential functions of neuregulin in development. Nature 378, 386-390 (1995).
    • (1995) Nature , vol.378 , pp. 386-390
    • Meyer, D.1    Birchmeier, C.2
  • 30
    • 0028884413 scopus 로고
    • Requirement for neuregulin receptor erbB2 in neural and cardiac development
    • Lee, K. F. et al. Requirement for neuregulin receptor erbB2 in neural and cardiac development. Nature 378, 394-398 (1995).
    • (1995) Nature , vol.378 , pp. 394-398
    • Lee, K.F.1
  • 31
    • 0028785406 scopus 로고
    • Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor
    • Gassmann, M. et al. Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor. Nature 378, 390-394 (1995).
    • (1995) Nature , vol.378 , pp. 390-394
    • Gassmann, M.1
  • 32
    • 0030685807 scopus 로고    scopus 로고
    • Severe neuropathies in mice with targeted mutations in the ErbB3 receptor
    • Riethmacher, D. et al. Severe neuropathies in mice with targeted mutations in the ErbB3 receptor. Nature 389, 725-730 (1997).
    • (1997) Nature , vol.389 , pp. 725-730
    • Riethmacher, D.1
  • 33
    • 10744230127 scopus 로고    scopus 로고
    • An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors
    • Burgess, A. W. et al. An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol. Cell 12, 541-552 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 541-552
    • Burgess, A.W.1
  • 34
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella, T. W. & Jovin, T. M. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol. 129, 1543-1558 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella, T.W.1    Jovin, T.M.2
  • 35
    • 0031028273 scopus 로고    scopus 로고
    • Two EGF molecules contribute additively to stabilization of the EGFR dimer
    • Lemmon, M. A. et al. Two EGF molecules contribute additively to stabilization of the EGFR dimer. EMBO J. 16, 281-294 (1997).
    • (1997) EMBO J. , vol.16 , pp. 281-294
    • Lemmon, M.A.1
  • 36
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako, Y., Minoghchi, S. & Yanagida, T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nature Cell Biol. 2, 168-172 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 37
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki, T., Maruyama, H. & Maruyama, I. N. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J. Mol. Biol. 311, 1011-1026 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 38
    • 24044436190 scopus 로고    scopus 로고
    • Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A-multidimensional microscopy analysis
    • Clayton, A. H. et al. Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A- multidimensional microscopy analysis. J. Biol. Chem. 280, 30392-30399 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 30392-30399
    • Clayton, A.H.1
  • 39
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha
    • Garrett, T. P. et al. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. Cell 110, 763-773 (2002).
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.P.1
  • 40
    • 18644386251 scopus 로고    scopus 로고
    • Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
    • Ogiso, H. et al. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 110, 775-787 (2002). References 39 and 40 describe the structures of the ligand-bound extracellular domain of the EGFR and reveal the basis of ligand-induced receptor activation.
    • (2002) Cell , vol.110 , pp. 775-787
    • Ogiso, H.1
  • 41
    • 0037291226 scopus 로고    scopus 로고
    • The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors
    • Garrett, T. P. et al. The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors. Mol. Cell 11, 495-505 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 495-505
    • Garrett, T.P.1
  • 42
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyroisne-dependent signaling networks by quantitative proteomics
    • Blagoev, B., Ong, S. E., Kratchmarova, I. & Mann, M. Temporal analysis of phosphotyroisne-dependent signaling networks by quantitative proteomics. Nature Biotechnol. 22, 1139-1145 (2004). Demonstration of the power of new high-throughput techniques for accumulation of quantitative information regarding signalling events.
    • (2004) Nature Biotechnol. , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 43
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang, Y. et al. Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 4, 1240-1250 (2005).
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1
  • 44
    • 0042093610 scopus 로고    scopus 로고
    • The connectivity structure, giant strong component and centrality of metabolic networks
    • Ma, H. W. & Zeng, A. P. The connectivity structure, giant strong component and centrality of metabolic networks. Bioinformatics 19, 1423-1430 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 1423-1430
    • Ma, H.W.1    Zeng, A.P.2
  • 46
    • 0035850895 scopus 로고    scopus 로고
    • Phenotypic plasticity in the interactions and evolution of species
    • Agrawal, A. A. Phenotypic plasticity in the interactions and evolution of species. Science 294, 321-326 (2001).
    • (2001) Science , vol.294 , pp. 321-326
    • Agrawal, A.A.1
  • 47
    • 0028034549 scopus 로고
    • Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells
    • Okutani, T. et al. Grb2/Ash binds directly to tyrosines 1068 and 1086 and indirectly to tyrosine 1148 of activated human epidermal growth factor receptors in intact cells. J. Biol. Chem. 269, 31310-31314 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 31310-31314
    • Okutani, T.1
  • 48
    • 0028040812 scopus 로고
    • Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor
    • Batzer, A. G., Rotin, D., Urena, J. M., Skolnik, E. Y. & Schlessinger, J. Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Mol. Cell. Biol. 14, 5192-5201 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5192-5201
    • Batzer, A.G.1    Rotin, D.2    Urena, J.M.3    Skolnik, E.Y.4    Schlessinger, J.5
  • 49
    • 0036469898 scopus 로고    scopus 로고
    • A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling
    • Waterman, H. et al. A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. EMBO J. 21, 303-313 (2002).
    • (2002) EMBO J. , vol.21 , pp. 303-313
    • Waterman, H.1
  • 50
    • 0037339887 scopus 로고    scopus 로고
    • Grb2 Regulates Internalization of EGF receptors through clathrin-coated pits
    • Jiang, X., Huang, F., Marusyk, A. & Sorkin, A. Grb2 Regulates Internalization of EGF receptors through clathrin-coated pits. Mol. Biol. Cell. 14, 858-870 (2003).
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 858-870
    • Jiang, X.1    Huang, F.2    Marusyk, A.3    Sorkin, A.4
  • 51
    • 0034676456 scopus 로고    scopus 로고
    • Feedback control of intercellular signalling in development
    • Freeman, M. Feedback control of intercellular signalling in development. Nature 408, 313-319 (2000).
    • (2000) Nature , vol.408 , pp. 313-319
    • Freeman, M.1
  • 52
    • 0035871383 scopus 로고    scopus 로고
    • Analysis of the transcriptional program induced by Raf in epithelial cells
    • Schulze, A., Lehmann, K., Jefferies, H. B., McMahon, M. & Downward, J. Analysis of the transcriptional program induced by Raf in epithelial cells. Genes Dev. 15, 981-994 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 981-994
    • Schulze, A.1    Lehmann, K.2    Jefferies, H.B.3    McMahon, M.4    Downward, J.5
  • 53
    • 1342322686 scopus 로고    scopus 로고
    • Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion
    • Schafer, B., Gschwind, A. & Ullrich, A. Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion. Oncogene 23, 991-999 (2004).
    • (2004) Oncogene , vol.23 , pp. 991-999
    • Schafer, B.1    Gschwind, A.2    Ullrich, A.3
  • 54
    • 0037429692 scopus 로고    scopus 로고
    • Trafficking of the ErbB receptors and its influence on signaling
    • Wiley, H. S. Trafficking of the ErbB receptors and its influence on signaling. Exp. Cell Res. 284, 78-88 (2003).
    • (2003) Exp. Cell Res. , vol.284 , pp. 78-88
    • Wiley, H.S.1
  • 55
    • 22344439386 scopus 로고    scopus 로고
    • The C. elegans homolog of the mammalian tumor suppressor Dep-1/Scc1 inhibits EGFR signaling to regulate binary cell fate decisions
    • Berset, T. A., Hoier, E. F. & Hajnal, A. The C. elegans homolog of the mammalian tumor suppressor Dep-1/Scc1 inhibits EGFR signaling to regulate binary cell fate decisions. Genes Dev. 19, 1328-1340 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 1328-1340
    • Berset, T.A.1    Hoier, E.F.2    Hajnal, A.3
  • 56
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • Haj, F. G., Verveer, P. J., Squire, A., Neel, B. G. & Bastiaens, P. I. Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 295, 1708-1711 (2002).
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.5
  • 57
    • 14844299757 scopus 로고    scopus 로고
    • Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling
    • Kario, E. et al. Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling. J. Biol. Chem. 280, 7038-7048 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 7038-7048
    • Kario, E.1
  • 58
    • 0036847930 scopus 로고    scopus 로고
    • Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signaling pathway
    • Hanafusa, H., Torii, S., Yasunaga, T. & Nishida, E. Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signaling pathway. Nature Cell Biol. 4, 850-858 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 850-858
    • Hanafusa, H.1    Torii, S.2    Yasunaga, T.3    Nishida, E.4
  • 59
    • 0032841608 scopus 로고    scopus 로고
    • Sprouty is a general inhibitor of receptor tyrosine kinase signaling
    • Reich, A., Sapir, A. & Shilo, B. Sprouty is a general inhibitor of receptor tyrosine kinase signaling. Development 126, 4139-4147 (1999).
    • (1999) Development , vol.126 , pp. 4139-4147
    • Reich, A.1    Sapir, A.2    Shilo, B.3
  • 60
    • 0036479310 scopus 로고    scopus 로고
    • Sprouty2 inhibits the Ras/MAP kinase pathway by inhibiting the activation of Raf
    • Yusoff, P. et al. Sprouty2 inhibits the Ras/MAP kinase pathway by inhibiting the activation of Raf. J. Biol. Chem. 277, 3195-3201 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 3195-3201
    • Yusoff, P.1
  • 61
    • 0242684548 scopus 로고    scopus 로고
    • Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops
    • Rubin, C. et al. Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops. Curr. Biol. 13, 297-307 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 297-307
    • Rubin, C.1
  • 62
    • 8744267487 scopus 로고    scopus 로고
    • The leucine-rich repeat protein LRIG1 is a negative regulator of ErbB family receptor tyrosine kinases
    • Laederich, M. B. et al. The leucine-rich repeat protein LRIG1 is a negative regulator of ErbB family receptor tyrosine kinases. J. Biol. Chem. 279, 47050-47056 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 47050-47056
    • Laederich, M.B.1
  • 63
    • 20844462896 scopus 로고    scopus 로고
    • LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation
    • Gur, G. et al. LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation. EMBO J. 23, 3270-3281 (2004).
    • (2004) EMBO J. , vol.23 , pp. 3270-3281
    • Gur, G.1
  • 64
    • 0035700605 scopus 로고    scopus 로고
    • Mig-6 is a negative regulator of the epidermal growth factor receptor signal
    • Hackel, P. O., Gishizky, M. & Ullrich, A. Mig-6 is a negative regulator of the epidermal growth factor receptor signal. Biol. Chem. 382, 1649-1662 (2001).
    • (2001) Biol. Chem. , vol.382 , pp. 1649-1662
    • Hackel, P.O.1    Gishizky, M.2    Ullrich, A.3
  • 65
    • 0037136702 scopus 로고    scopus 로고
    • Expression of RALT, a feedback inhibitor of ErbB receptors, is subjected to an integrated transcriptional and post-translational control
    • Fiorini, M. et al. Expression of RALT, a feedback inhibitor of ErbB receptors, is subjected to an integrated transcriptional and post-translational control. Oncogene 21, 6530-6539 (2002).
    • (2002) Oncogene , vol.21 , pp. 6530-6539
    • Fiorini, M.1
  • 66
    • 0038037236 scopus 로고    scopus 로고
    • Feedback inhibition by RALT controls signal output by the ErbB network
    • Anastasi, S. et al. Feedback inhibition by RALT controls signal output by the ErbB network. Oncogene 22, 4221-4234 (2003).
    • (2003) Oncogene , vol.22 , pp. 4221-4234
    • Anastasi, S.1
  • 67
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford, S. L. & Lindquist, S. Hsp90 as a capacitor for morphological evolution. Nature 396, 336-342 (1998).
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 69
    • 1942431966 scopus 로고    scopus 로고
    • The Achilles heel of ErbB-2/HER2: Regulation by the Hsp90 chaperone machine and potential for pharmacological intervention
    • Citri, A., Kochupurakkal, B. S. & Yarden, Y. The Achilles heel of ErbB-2/HER2: regulation by the Hsp90 chaperone machine and potential for pharmacological intervention. Cell Cycle 3, 51-60 (2003).
    • (2003) Cell Cycle , vol.3 , pp. 51-60
    • Citri, A.1    Kochupurakkal, B.S.2    Yarden, Y.3
  • 70
    • 0029812759 scopus 로고    scopus 로고
    • c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271, 22796-22801 (1996). Early evidence which shows that HSP90 is a regulator of the ERBB network by modulating the stability of ERBB2.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 71
    • 12144266330 scopus 로고    scopus 로고
    • Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation
    • Citri, A. et al. Hsp90 restrains ErbB-2/HER2 signalling by limiting heterodimer formation. EMBO Rep. 5, 1165-1170 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 1165-1170
    • Citri, A.1
  • 72
    • 0037224231 scopus 로고    scopus 로고
    • Identification of ErbB2 kinase domain motifs required for geldanamycin-induced degradation
    • Tikhomirov, O. & Carpenter, G. Identification of ErbB2 kinase domain motifs required for geldanamycin-induced degradation. Cancer Res. 63, 39-43 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 39-43
    • Tikhomirov, O.1    Carpenter, G.2
  • 73
    • 15544372341 scopus 로고    scopus 로고
    • Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex
    • Xu, W. et al. Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. Nature Struct Mol. Biol. 12, 120-126 (2005).
    • (2005) Nature Struct Mol. Biol. , vol.12 , pp. 120-126
    • Xu, W.1
  • 74
    • 27344439995 scopus 로고    scopus 로고
    • Control of epidermal growth factor receptor endocytosis by receptor dimerization, rather than receptor kinase activation
    • Wang, Q., Villeneuve, G. & Wang, Z. Control of epidermal growth factor receptor endocytosis by receptor dimerization, rather than receptor kinase activation. EMBO Rep. 6, 942-948 (2005).
    • (2005) EMBO Rep. , vol.6 , pp. 942-948
    • Wang, Q.1    Villeneuve, G.2    Wang, Z.3
  • 75
    • 0028916337 scopus 로고
    • Endocytosis and lysosomal targeting of epidermal growth factor receptors are mediated by distinct sequences independent of the tyrosine kinase domain
    • Opresko, L. K. et al. Endocytosis and lysosomal targeting of epidermal growth factor receptors are mediated by distinct sequences independent of the tyrosine kinase domain. J. Biol. Chem. 270, 4325-4333 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 4325-4333
    • Opresko, L.K.1
  • 76
    • 0023663092 scopus 로고
    • Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing
    • Honegger, A., M. et al. Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing. Cell 51, 199-209 (1987).
    • (1987) Cell , vol.51 , pp. 199-209
    • Honegger, A.M.1
  • 77
    • 0028335378 scopus 로고
    • Regulation of postendocytic trafficking of the epidermal growth factor receptor through endosomal retention
    • Herbst, J. J., Opresko, L. K., Walsh, B. J., Lauffenburger, D. A. & Wiley, H. S. Regulation of postendocytic trafficking of the epidermal growth factor receptor through endosomal retention. J. Biol. Chem. 269, 12865-12873 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12865-12873
    • Herbst, J.J.1    Opresko, L.K.2    Walsh, B.J.3    Lauffenburger, D.A.4    Wiley, H.S.5
  • 78
    • 1842591231 scopus 로고    scopus 로고
    • Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases
    • Marmor, M. D. & Yarden, Y. Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases. Oncogene 23, 2057-2070 (2004).
    • (2004) Oncogene , vol.23 , pp. 2057-2070
    • Marmor, M.D.1    Yarden, Y.2
  • 79
    • 0030036079 scopus 로고    scopus 로고
    • Requirement for the adapter protein GRB2 in EGF receptor endocytosis
    • Wang, Z. & Moran, M. F. Requirement for the adapter protein GRB2 in EGF receptor endocytosis. Science 272, 1935-1938 (1996).
    • (1996) Science , vol.272 , pp. 1935-1938
    • Wang, Z.1    Moran, M.F.2
  • 80
    • 0037075606 scopus 로고    scopus 로고
    • The endophilin-CIN85-Cbl complex mediates ligand-dependent down regulation of c-Met
    • Petrelli, A. et al. The endophilin-CIN85-Cbl complex mediates ligand-dependent down regulation of c-Met. Nature 416, 187-190 (2002).
    • (2002) Nature , vol.416 , pp. 187-190
    • Petrelli, A.1
  • 81
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • Soubeyran, P., Kowanetz, K., Szymkiewicz, I., Langdon, W. Y. & Dikic, I. Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416, 183-187 (2002).
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 82
    • 18544383164 scopus 로고    scopus 로고
    • Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
    • Katz, M. et al. Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 3, 740-751 (2002).
    • (2002) Traffic , vol.3 , pp. 740-751
    • Katz, M.1
  • 83
    • 0037187597 scopus 로고    scopus 로고
    • A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • Polo, S. et al. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451-455 (2002).
    • (2002) Nature , vol.416 , pp. 451-455
    • Polo, S.1
  • 84
    • 3142742326 scopus 로고    scopus 로고
    • Tal, a Tsg 101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding
    • Amit, I. et al. Tal, a Tsg 101-specific E3 ubiquitin ligase, regulates receptor endocytosis and retrovirus budding. Genes Dev. 18, 1737-1752 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 1737-1752
    • Amit, I.1
  • 86
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • Di Guglielmo, G. M., Baass, P. C., Ou, W. J., Posner, B. I. & Bergeron, J. J. Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 13, 4269-4277 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4269-4277
    • Di Guglielmo, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 87
    • 0036787904 scopus 로고    scopus 로고
    • Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival
    • Wang, Y., Pennock, S., Chen, X. & Wang, Z. Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival. Mol. Cell. Biol. 22, 7279-7290 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7279-7290
    • Wang, Y.1    Pennock, S.2    Chen, X.3    Wang, Z.4
  • 88
    • 1642417606 scopus 로고    scopus 로고
    • APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment
    • Miaczynska, M. et al. APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment. Cell 116, 445-456 (2004).
    • (2004) Cell , vol.116 , pp. 445-456
    • Miaczynska, M.1
  • 89
    • 0029764504 scopus 로고    scopus 로고
    • Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation
    • Vecchi, M., Baulida, J. & Carpenter, G. Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation. J. Biol. Chem. 271, 18989-18995 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 18989-18995
    • Vecchi, M.1    Baulida, J.2    Carpenter, G.3
  • 90
    • 8444243682 scopus 로고    scopus 로고
    • The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
    • Williams, C. C. et al. The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J. Cell. Biol. 167, 469-478 (2004).
    • (2004) J. Cell. Biol. , vol.167 , pp. 469-478
    • Williams, C.C.1
  • 91
    • 0042858208 scopus 로고    scopus 로고
    • WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus
    • Komuro, A., Nagai, M., Navin, N. E. & Sudol, M. WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus. J. Biol. Chem. 278, 33334-33341 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 33334-33341
    • Komuro, A.1    Nagai, M.2    Navin, N.E.3    Sudol, M.4
  • 92
    • 1542358888 scopus 로고    scopus 로고
    • Ligand-regulated association of ErbB-4 to the transcriptional co-activator YAP65 controls transcription at the nuclear level
    • Omerovic, J. et al. Ligand-regulated association of ErbB-4 to the transcriptional co-activator YAP65 controls transcription at the nuclear level. Exp. Cell Res. 294, 469-479 (2004).
    • (2004) Exp. Cell Res. , vol.294 , pp. 469-479
    • Omerovic, J.1
  • 93
    • 23044492008 scopus 로고    scopus 로고
    • WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function
    • Aqeilan, R. I. et al. WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function. Cancer Res. 65, 6764-6772 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 6764-6772
    • Aqeilan, R.I.1
  • 94
    • 4544376914 scopus 로고    scopus 로고
    • Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2
    • Wang, S. C. et al. Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2. Cancer Cell 6, 251-261 (2004).
    • (2004) Cancer Cell , vol.6 , pp. 251-261
    • Wang, S.C.1
  • 95
    • 20444423286 scopus 로고    scopus 로고
    • Nuclear interaction of EGFR and STAT3 in the activation of the iNOS/NO pathway
    • Lo, H. W. et al. Nuclear interaction of EGFR and STAT3 in the activation of the iNOS/NO pathway. Cancer Cell 7, 575-589 (2005).
    • (2005) Cancer Cell , vol.7 , pp. 575-589
    • Lo, H.W.1
  • 96
    • 33644524741 scopus 로고    scopus 로고
    • Cell signalling dynamics in time and space
    • Kholodenko, B. N. Cell signalling dynamics in time and space. Nature Rev. Mol. Cell. Biol. 7, 165-176 (2006).
    • (2006) Nature Rev. Mol. Cell. Biol. , vol.7 , pp. 165-176
    • Kholodenko, B.N.1
  • 97
    • 29144435996 scopus 로고    scopus 로고
    • Computational modelling of the receptor-tyrosine-kinase-activated MAPK pathway
    • Orton, R. J. et al. Computational modelling of the receptor-tyrosine- kinase-activated MAPK pathway. Biochem. J. 392, 249-261 (2005).
    • (2005) Biochem. J. , vol.392 , pp. 249-261
    • Orton, R.J.1
  • 98
    • 0019404817 scopus 로고
    • A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands
    • Wiley, H. S. & Cunningham, D. D. A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands. Cell 25, 433-440 (1981).
    • (1981) Cell , vol.25 , pp. 433-440
    • Wiley, H.S.1    Cunningham, D.D.2
  • 99
    • 0026833077 scopus 로고
    • Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses
    • Starbuck, C. & Lauffenburger, D. A. Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses. Biotechnol. Prog. 8, 132-143 (1992).
    • (1992) Biotechnol. Prog. , vol.8 , pp. 132-143
    • Starbuck, C.1    Lauffenburger, D.A.2
  • 100
    • 0025908557 scopus 로고
    • The role of tyrosine kinase activity in endocytosis, compartmentation, and down-regulation of the epidermal growth factor receptor
    • Wiley, H. S. et al. The role of tyrosine kinase activity in endocytosis, compartmentation, and down-regulation of the epidermal growth factor receptor. J. Biol. Chem. 266, 11083-11094 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 11083-11094
    • Wiley, H.S.1
  • 101
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • Kholodenko, B. N., Demin, O. V., Moehren, G. & Hoek, J. B. Quantification of short term signaling by the epidermal growth factor receptor. J. Biol. Chem. 274, 30169-30181 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 30169-30181
    • Kholodenko, B.N.1    Demin, O.V.2    Moehren, G.3    Hoek, J.B.4
  • 102
    • 0036212767 scopus 로고    scopus 로고
    • Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors
    • Schoeberl, B., Eichler-Jonsson, C., Gilles, E. D. & Muller, G. Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors. Nature Biotechnol. 20, 370-375 (2002). References 101 and 102 describe the first attempts to formulate models of the early events following activation of the EGFR. These two models function as platforms for developing more complex models of EGFR signalling.
    • (2002) Nature Biotechnol. , vol.20 , pp. 370-375
    • Schoeberl, B.1    Eichler-Jonsson, C.2    Gilles, E.D.3    Muller, G.4
  • 103
    • 0041843750 scopus 로고    scopus 로고
    • An integrated model of epidermal growth factor receptor trafficking and signal transduction
    • Resat, H., Ewald, J. A., Dixon, D. A. & Wiley, H. S. An integrated model of epidermal growth factor receptor trafficking and signal transduction. Biophys. J. 85, 730-743 (2003).
    • (2003) Biophys. J. , vol.85 , pp. 730-743
    • Resat, H.1    Ewald, J.A.2    Dixon, D.A.3    Wiley, H.S.4
  • 104
    • 0346688723 scopus 로고    scopus 로고
    • Self-organization of polarized cell signaling via autocrine circuits: Computational model analysis
    • Maly, I. V., Wiley, H. S. & Lauffenburger, D. A. Self-organization of polarized cell signaling via autocrine circuits: computational model analysis. Biophys. J. 86, 10-22 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 10-22
    • Maly, I.V.1    Wiley, H.S.2    Lauffenburger, D.A.3
  • 105
    • 33746889808 scopus 로고    scopus 로고
    • A comprehensive pathway map of epidermal growth factor receptor signaling
    • Oda, K., Matsuoka, Y., Funahashi, A. & Kitano, H. A comprehensive pathway map of epidermal growth factor receptor signaling. Mol. Syst. Biol. 1, 8-24 (2005).
    • (2005) Mol. Syst. Biol. , vol.1 , pp. 8-24
    • Oda, K.1    Matsuoka, Y.2    Funahashi, A.3    Kitano, H.4
  • 107
    • 0032531927 scopus 로고    scopus 로고
    • Pathogenic poxviruses reveal viral strategies to exploit the ErbB signaling network
    • Tzahar, E. et al. Pathogenic poxviruses reveal viral strategies to exploit the ErbB signaling network. EMBO J. 17, 5948-5963 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5948-5963
    • Tzahar, E.1
  • 108
    • 0032556454 scopus 로고    scopus 로고
    • Analysis of receptor internalization as a mechanism for modulating signal transduction
    • Haugh, J. M. & Lauffenburger, D. A. Analysis of receptor internalization as a mechanism for modulating signal transduction. J. Theoret. Biol. 195, 187-218 (1998).
    • (1998) J. Theoret. Biol. , vol.195 , pp. 187-218
    • Haugh, J.M.1    Lauffenburger, D.A.2
  • 109
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib
    • Lynch, T. J. et al. Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. N. Engl. J. Med. 350, 2129-2139 (2004).
    • (2004) N. Engl. J. Med. , vol.350 , pp. 2129-2139
    • Lynch, T.J.1
  • 110
    • 2342624080 scopus 로고    scopus 로고
    • EGFR mutations in lung cancer: Correlation with clinical response to gefitinib therapy
    • Paez, J. G. et al. EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy. Science 304, 1497-1500 (2004).
    • (2004) Science , vol.304 , pp. 1497-1500
    • Paez, J.G.1
  • 111
    • 4444344330 scopus 로고    scopus 로고
    • EGF receptor gene mutations are common in lung cancers from 'never smokers' and are associated with sensitivity of tumors to gefitinib and erlotinib
    • Pao, W. et al. EGF receptor gene mutations are common in lung cancers from 'never smokers' and are associated with sensitivity of tumors to gefitinib and erlotinib. Proc. Natl Acad. Sci. USA 101, 13306-13311 (2004). References 109-111 describe identification of activating mutations within the kinase domain of the EGFR. Patients whose tumours bear these mutations respond better to treatment with EGFR-specific kinase inhibitors.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 13306-13311
    • Pao, W.1
  • 112
    • 5644293135 scopus 로고    scopus 로고
    • Gefitinib induces apoptosis in the EGFRL858R non-small-cell lung cancer cell line H3255
    • Tracy, S. et al. Gefitinib induces apoptosis in the EGFRL858R non-small-cell lung cancer cell line H3255. Cancer Res. 64, 7241-7244 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 7241-7244
    • Tracy, S.1
  • 113
    • 4143066760 scopus 로고    scopus 로고
    • Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways
    • Sordella, R., Bell, D. W., Haber, D. A. & Settleman, J. Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways. Science 305, 1163-1167 (2004).
    • (2004) Science , vol.305 , pp. 1163-1167
    • Sordella, R.1    Bell, D.W.2    Haber, D.A.3    Settleman, J.4
  • 114
    • 14844366111 scopus 로고    scopus 로고
    • ErbB-3 mediates phosphoinositide 3-kinase activity in gefitinib-sensitive non-small cell lung cancer cell lines
    • Engelman, J. A. et al. ErbB-3 mediates phosphoinositide 3-kinase activity in gefitinib-sensitive non-small cell lung cancer cell lines. Proc. Natl Acad. Sci. USA 102, 3788-3793 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3788-3793
    • Engelman, J.A.1
  • 115
    • 20144386787 scopus 로고    scopus 로고
    • Somatic mutations of the HER2 kinase domain in lung adenocarcinomas
    • Shigematsu, H. et al. Somatic mutations of the HER2 kinase domain in lung adenocarcinomas. Cancer Res. 65, 1642-1646 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 1642-1646
    • Shigematsu, H.1
  • 116
    • 0026521394 scopus 로고
    • Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails
    • Ekstrand, A. J., Sugawa, N., James, C. D. & Collins, V. P. Amplified and rearranged epidermal growth factor receptor genes in human glioblastomas reveal deletions of sequences encoding portions of the N- and/or C-terminal tails. Proc. Natl Acad. Sci. USA 89, 4309-4313 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4309-4313
    • Ekstrand, A.J.1    Sugawa, N.2    James, C.D.3    Collins, V.P.4
  • 117
    • 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
    • Ekstrand, A. J. et al. 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, 2164-2172 (1991).
    • (1991) Cancer Res. , vol.51 , pp. 2164-2172
    • Ekstrand, A.J.1
  • 118
    • 27744503993 scopus 로고    scopus 로고
    • Clinical significance of EGFR amplification and the aberrant EGFRvIII transcript in conventionally treated astrocytic gliomas
    • Liu, L. et al. Clinical significance of EGFR amplification and the aberrant EGFRvIII transcript in conventionally treated astrocytic gliomas. J. Mol. Med. 83, 917-926 (2005).
    • (2005) J. Mol. Med. , vol.83 , pp. 917-926
    • Liu, L.1
  • 119
    • 14444288522 scopus 로고    scopus 로고
    • The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling
    • Huang, H. S. et al. The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling. J. Biol. Chem. 272, 2927-2935 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 2927-2935
    • Huang, H.S.1
  • 121
    • 0037215106 scopus 로고    scopus 로고
    • Targeting epidermal growth factor receptor in head and neck cancer
    • Ford, A. C. & Grandis, J. R. Targeting epidermal growth factor receptor in head and neck cancer. Head Neck 25, 67-73 (2003).
    • (2003) Head Neck , vol.25 , pp. 67-73
    • Ford, A.C.1    Grandis, J.R.2
  • 122
    • 0042208398 scopus 로고    scopus 로고
    • The Her-2/neu gene and protein in breast cancer 2003: Biomarker and target of therapy
    • Ross, J. S. et al. The Her-2/neu gene and protein in breast cancer 2003: biomarker and target of therapy. Oncologist 8, 307-325 (2003).
    • (2003) Oncologist , vol.8 , pp. 307-325
    • Ross, J.S.1
  • 123
    • 0024337144 scopus 로고
    • Studies of the HER-2/neu protooncogene in human breast and ovarian cancer
    • Slamon, D. J. et al. Studies of the HER-2/neu protooncogene in human breast and ovarian cancer. Science 244, 707-712 (1989). The first study to show that ERBB2 amplification predicts poor prognosis for breast cancer patients.
    • (1989) Science , vol.244 , pp. 707-712
    • Slamon, D.J.1
  • 124
    • 0032460777 scopus 로고    scopus 로고
    • Clinical results of transhiatal esophagectomy for carcinoma of the lower thoracic esophagus according to biological markers
    • Hirai, T. et al. Clinical results of transhiatal esophagectomy for carcinoma of the lower thoracic esophagus according to biological markers. Dis. Esophagus 11, 221-225 (1998).
    • (1998) Dis. Esophagus , vol.11 , pp. 221-225
    • Hirai, T.1
  • 125
    • 0010622002 scopus 로고
    • Immunohistochemical evidence of autocrine growth factors in adenocarcinoma of the human lung
    • Tateishi, M., Ishida, T., Mitsudomi, T., Kaneko, S. & Sugimachi, K. Immunohistochemical evidence of autocrine growth factors in adenocarcinoma of the human lung. Cancer Res. 12, 1183-1188 (1990).
    • (1990) Cancer Res. , vol.12 , pp. 1183-1188
    • Tateishi, M.1    Ishida, T.2    Mitsudomi, T.3    Kaneko, S.4    Sugimachi, K.5
  • 126
    • 33645984545 scopus 로고    scopus 로고
    • Constitutive neuregulin-1/ErbB signaling contributes to human vestibular schwannoma proliferation
    • Hansen, M. R., Roehm, P. C., Chatterjee, P. & Green, S. H. Constitutive neuregulin-1/ErbB signaling contributes to human vestibular schwannoma proliferation. Glia 53, 593-600 (2006).
    • (2006) Glia , vol.53 , pp. 593-600
    • Hansen, M.R.1    Roehm, P.C.2    Chatterjee, P.3    Green, S.H.4
  • 127
    • 0037429739 scopus 로고    scopus 로고
    • The epidermal growth factor system in Caenorhabditis elegans
    • Moghal, N. & Sternberg, P. W. The epidermal growth factor system in Caenorhabditis elegans. Exp. Cell Res. 284, 150-159 (2003).
    • (2003) Exp. Cell Res. , vol.284 , pp. 150-159
    • Moghal, N.1    Sternberg, P.W.2
  • 128
    • 0037429688 scopus 로고    scopus 로고
    • Signaling by the Drosophila epidermal growth factor receptor pathway during development
    • Shilo, B. Z. Signaling by the Drosophila epidermal growth factor receptor pathway during development. Exp. Cell Res. 284, 140-149 (2003).
    • (2003) Exp. Cell Res. , vol.284 , pp. 140-149
    • Shilo, B.Z.1
  • 129
    • 0033947243 scopus 로고    scopus 로고
    • Evolutionary analysis of the ErbB receptor and ligand families
    • Stein, R. A. & Staros, J. V. Evolutionary analysis of the ErbB receptor and ligand families. J. Mol. Evol. 50, 397-412 (2000).
    • (2000) J. Mol. Evol. , vol.50 , pp. 397-412
    • Stein, R.A.1    Staros, J.V.2
  • 130
    • 0028267221 scopus 로고
    • Computer simulated evolution of a network of cell-signaling molecules
    • Bray, D. & Lay, S. Computer simulated evolution of a network of cell-signaling molecules. Biophys. J. 66, 972-977 (1994).
    • (1994) Biophys. J. , vol.66 , pp. 972-977
    • Bray, D.1    Lay, S.2
  • 131
    • 0344010691 scopus 로고    scopus 로고
    • Cancer robustness: Tumour tactics
    • Kitano, H. Cancer robustness: tumour tactics. Nature 426, 125 (2003).
    • (2003) Nature , vol.426 , pp. 125
    • Kitano, H.1
  • 132
    • 0000188718 scopus 로고    scopus 로고
    • Highly optimized tolerance: Robustness and design in complex systems
    • Carlson, J. M. & Doyle, J. Highly optimized tolerance: robustness and design in complex systems. Phys. Rev. Lett. 84, 2529-2532 (2000).
    • (2000) Phys. Rev. Lett. , vol.84 , pp. 2529-2532
    • Carlson, J.M.1    Doyle, J.2
  • 133
    • 0034076307 scopus 로고    scopus 로고
    • Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets
    • Clynes, R. A., Towers, T. L., Presta, L. G. & Ravetch, J. V. Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets. Nature Med. 6, 443-446 (2000).
    • (2000) Nature Med. , vol.6 , pp. 443-446
    • Clynes, R.A.1    Towers, T.L.2    Presta, L.G.3    Ravetch, J.V.4
  • 134
    • 5144226211 scopus 로고    scopus 로고
    • PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients
    • Nagata, Y. et al. PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients. Cancer Cell 6, 117-127 (2004).
    • (2004) Cancer Cell , vol.6 , pp. 117-127
    • Nagata, Y.1
  • 135
    • 0036284422 scopus 로고    scopus 로고
    • Targeting multiple Her-2 epitopes with monoclonal antibodies results in improved antigrowth activity of a human breast cancer cell line in vitro and in vivo
    • Spiridon, C. I. et al. Targeting multiple Her-2 epitopes with monoclonal antibodies results in improved antigrowth activity of a human breast cancer cell line in vitro and in vivo. Clin. Cancer Res. 8, 1720-1730 (2002).
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1720-1730
    • Spiridon, C.I.1
  • 136
    • 13844306484 scopus 로고    scopus 로고
    • Synergistic down-regulation of receptor tyrosine kinases by combinations of mAbs: Implications for cancer immunotherapy
    • Friedman, L. M. et al. Synergistic down-regulation of receptor tyrosine kinases by combinations of mAbs: implications for cancer immunotherapy. Proc. Natl Acad. Sci. USA 102, 1915-1920 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1915-1920
    • Friedman, L.M.1
  • 137
    • 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
    • Xia, W. et al. 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, 6255-6263 (2002).
    • (2002) Oncogene , vol.21 , pp. 6255-6263
    • Xia, W.1
  • 138
    • 18444404925 scopus 로고    scopus 로고
    • Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: Implications for cancer therapy
    • Citri, A. et al. Drug-induced ubiquitylation and degradation of ErbB receptor tyrosine kinases: implications for cancer therapy. EMBO J. 21, 2407-2417 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2407-2417
    • Citri, A.1
  • 139
    • 0018569942 scopus 로고
    • A mathematic model for relating the drug sensitivity of tumors to their spontaneous mutation rate
    • Goldie, J. H. & Coldman, A. J. A mathematic model for relating the drug sensitivity of tumors to their spontaneous mutation rate. Cancer Treat. Rep. 63, 1727-1733 (1979).
    • (1979) Cancer Treat. Rep. , vol.63 , pp. 1727-1733
    • Goldie, J.H.1    Coldman, A.J.2
  • 140
    • 0033590602 scopus 로고    scopus 로고
    • Augmentation of a humanized anti-HER2 mAb 4D5 induced growth inhibition by a human-mouse chimeric anti-EGF receptor mAb C225
    • Ye, D., Mendelsohn, J. & Fan, Z. Augmentation of a humanized anti-HER2 mAb 4D5 induced growth inhibition by a human-mouse chimeric anti-EGF receptor mAb C225. Oncogene 18, 731-738 1999).
    • Oncogene , vol.18 , pp. 731-7381999
    • Ye, D.1    Mendelsohn, J.2    Fan, Z.3
  • 141
    • 0035869407 scopus 로고    scopus 로고
    • Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2
    • Slamon, D. J. et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N. Engl. J. Med. 344, 783-792 (2001).
    • (2001) N. Engl. J. Med. , vol.344 , pp. 783-792
    • Slamon, D.J.1
  • 142
    • 2942652871 scopus 로고    scopus 로고
    • Mechanisms of tamoxifen resistance: Increased estrogen receptor-HER2/neu cross-talk in ER/HER2-positive breast cancer
    • Shou, J. et al. Mechanisms of tamoxifen resistance: increased estrogen receptor-HER2/neu cross-talk in ER/HER2-positive breast cancer. J. Natl Cancer Inst. 96, 926-935 (2004).
    • (2004) J. Natl Cancer Inst. , vol.96 , pp. 926-935
    • Shou, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.