메뉴 건너뛰기




Volumn 29, Issue 6, 2007, Pages 558-565

Mutational activation of ErbB family receptor tyrosine kinases: Insights into mechanisms of signal transduction and tumorigenesis

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; TYROSINE KINASE RECEPTOR;

EID: 34250216633     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20582     Document Type: Review
Times cited : (77)

References (65)
  • 2
    • 33747154401 scopus 로고    scopus 로고
    • Targeting EGFR and HER-2 receptor tyrosine kinases for cancer drug discovery and development
    • Kamath S, Buolamwini JK. 2006. Targeting EGFR and HER-2 receptor tyrosine kinases for cancer drug discovery and development. Med Res Rev 26:569-594.
    • (2006) Med Res Rev , vol.26 , pp. 569-594
    • Kamath, S.1    Buolamwini, J.K.2
  • 3
    • 4444309305 scopus 로고    scopus 로고
    • The EGF receptor family as therapeutic targets in breast cancer
    • Lemmon MA. 2003. The EGF receptor family as therapeutic targets in breast cancer. Breast Dis 18:33-43.
    • (2003) Breast Dis , vol.18 , pp. 33-43
    • Lemmon, M.A.1
  • 4
    • 23844471971 scopus 로고    scopus 로고
    • Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface
    • Dawson JP, Berger MB, Lin CC, Schlessinger J, Lemmon MA, et al. 2005. Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface. Mol Cell Biol 25:7734-7742.
    • (2005) Mol Cell Biol , vol.25 , pp. 7734-7742
    • Dawson, J.P.1    Berger, M.B.2    Lin, C.C.3    Schlessinger, J.4    Lemmon, M.A.5
  • 5
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, et al. 2003. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11:507-517.
    • (2003) Mol Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5
  • 6
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho HS, Leahy DJ. 2002 Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297:1330-1333.
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 7
    • 27244461099 scopus 로고    scopus 로고
    • The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand
    • Bouyain S, Longo PA, Li S, Ferguson KM, Leahy DJ. 2005. The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Proc Natl Acad Sci USA 102:15024-15029.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15024-15029
    • Bouyain, S.1    Longo, P.A.2    Li, S.3    Ferguson, K.M.4    Leahy, D.J.5
  • 9
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J. 2006. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125:1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 10
    • 0024023873 scopus 로고
    • Egf binding to its receptor triggers a rapid tyrosine phosphorylation of the erbB-2 protein in the mammary tumor cell line SK-BR-3
    • King CR, Borrello I, Bellot F, Comoglio P, Schlessinger J. 1988. Egf binding to its receptor triggers a rapid tyrosine phosphorylation of the erbB-2 protein in the mammary tumor cell line SK-BR-3. Embo J 7:1647-1651.
    • (1988) Embo J , vol.7 , pp. 1647-1651
    • King, C.R.1    Borrello, I.2    Bellot, F.3    Comoglio, P.4    Schlessinger, J.5
  • 11
    • 0000317172 scopus 로고
    • Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation
    • Honegger AM, Kris RM, Ullrich A, Schlessinger J. 1989. Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation. Proc Natl Acad Sci USA 86:925-929.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 925-929
    • Honegger, A.M.1    Kris, R.M.2    Ullrich, A.3    Schlessinger, J.4
  • 12
    • 0025352677 scopus 로고
    • Evidence for epidermal growth factor (EGF)-induced intermolecular autophosphorylation of the EGF receptors in living cells
    • Honegger AM, Schmidt A, Ullrich A, Schlessinger J. 1990. Evidence for epidermal growth factor (EGF)-induced intermolecular autophosphorylation of the EGF receptors in living cells. Mol Cell Biol 10:4035-4044.
    • (1990) Mol Cell Biol , vol.10 , pp. 4035-4044
    • Honegger, A.M.1    Schmidt, A.2    Ullrich, A.3    Schlessinger, J.4
  • 13
    • 0025085653 scopus 로고
    • Transphosphorylation as a possible mechanism for insulin and epidermal growth factor receptor activation
    • Lammers R, Van Obberghen E, Ballotti R, Schlessinger J, Ullrich A. 1990. Transphosphorylation as a possible mechanism for insulin and epidermal growth factor receptor activation. J Biol Chem 265:16886-16890.
    • (1990) J Biol Chem , vol.265 , pp. 16886-16890
    • Lammers, R.1    Van Obberghen, E.2    Ballotti, R.3    Schlessinger, J.4    Ullrich, A.5
  • 14
    • 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 TP, McKern NM, Lou M, Elleman TC, Adams TE, et al. 2003. 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) Mol Cell , vol.11 , pp. 495-505
    • Garrett, T.P.1    McKern, N.M.2    Lou, M.3    Elleman, T.C.4    Adams, T.E.5
  • 15
    • 33646814947 scopus 로고    scopus 로고
    • Gilmore JL, Gallo RM, Riese DJ 2nd. 2006. The epidermal growth factor receptor (EGFR)-S442F mutant displays increased affinity for neuregulin-2beta and agonist-independent coupling with downstream signalling events. Biochem J 396:79-88.
    • Gilmore JL, Gallo RM, Riese DJ 2nd. 2006. The epidermal growth factor receptor (EGFR)-S442F mutant displays increased affinity for neuregulin-2beta and agonist-independent coupling with downstream signalling events. Biochem J 396:79-88.
  • 16
    • 0033009389 scopus 로고    scopus 로고
    • Binding specificities and affinities of egf domains for ErbB receptors
    • Jones JT, Akita RW, Sliwkowski MX. 1999. Binding specificities and affinities of egf domains for ErbB receptors. FEBS Lett 447:227-231.
    • (1999) FEBS Lett , vol.447 , pp. 227-231
    • Jones, J.T.1    Akita, R.W.2    Sliwkowski, M.X.3
  • 17
    • 0031705405 scopus 로고    scopus 로고
    • ErbB tyrosine kinases and the two neuregulin families constitute a ligand-receptor network
    • Pinkas-Kramarski R, Shelly M, Guarino BC, Wang LM, Lyass L, et al. 1998. ErbB tyrosine kinases and the two neuregulin families constitute a ligand-receptor network. Mol Cell Biol 18:6090-6101.
    • (1998) Mol Cell Biol , vol.18 , pp. 6090-6101
    • Pinkas-Kramarski, R.1    Shelly, M.2    Guarino, B.C.3    Wang, L.M.4    Lyass, L.5
  • 18
    • 0033513584 scopus 로고    scopus 로고
    • ErbB tyrosine kinases and the two neuregulin families constitute a ligand-receptor network
    • Pinkas-Kramarski R, Shelly M, Guarino BC, Wang LM, Lyass L, et al. 1999. ErbB tyrosine kinases and the two neuregulin families constitute a ligand-receptor network. Mol Cell Biol 19:8695.
    • (1999) Mol Cell Biol , vol.19 , pp. 8695
    • Pinkas-Kramarski, R.1    Shelly, M.2    Guarino, B.C.3    Wang, L.M.4    Lyass, L.5
  • 19
    • 85135102226 scopus 로고    scopus 로고
    • Gilmore JL, Riese DJ 2nd. 2004. secErbB4-26/549 antagonizes ligand-induced ErbB4 tyrosine phosphorylation. Oncol Res 14:589-602.
    • Gilmore JL, Riese DJ 2nd. 2004. secErbB4-26/549 antagonizes ligand-induced ErbB4 tyrosine phosphorylation. Oncol Res 14:589-602.
  • 20
    • 0034954124 scopus 로고    scopus 로고
    • The type III epidermal growth factor receptor mutation. Biological significance and potential target for anti-cancer therapy
    • Pedersen MW, Meltorn M, Damstrup L, Poulsen HS, 2001. The type III epidermal growth factor receptor mutation. Biological significance and potential target for anti-cancer therapy. Ann Oncol 12:745-760.
    • (2001) Ann Oncol , vol.12 , pp. 745-760
    • Pedersen, M.W.1    Meltorn, M.2    Damstrup, L.3    Poulsen, H.S.4
  • 21
    • 0030787340 scopus 로고    scopus 로고
    • Receptor dimerization is not a factor in the signalling activity of a transforming variant epidermal growth factor receptor (EGFRvIII)
    • Chu CT, Everiss KD, Wikstrand CJ, Batra SK, Kung HJ, et al. 1997. Receptor dimerization is not a factor in the signalling activity of a transforming variant epidermal growth factor receptor (EGFRvIII). Biochem J 324:855-861.
    • (1997) Biochem J , vol.324 , pp. 855-861
    • Chu, C.T.1    Everiss, K.D.2    Wikstrand, C.J.3    Batra, S.K.4    Kung, H.J.5
  • 22
    • 0035895916 scopus 로고    scopus 로고
    • Glycosylation-induced conformational modification positively regulates receptor-receptor association: A study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells
    • Fernandes H, Cohen S, Bishayee S. 2001. Glycosylation-induced conformational modification positively regulates receptor-receptor association: a study with an aberrant epidermal growth factor receptor (EGFRvIII/DeltaEGFR) expressed in cancer cells. J Biol Chem 276: 5375-5383.
    • (2001) J Biol Chem , vol.276 , pp. 5375-5383
    • Fernandes, H.1    Cohen, S.2    Bishayee, S.3
  • 23
    • 4444263448 scopus 로고    scopus 로고
    • The tumor-specific de 2-7 epidermal growth factor receptor (EGFR) promotes cells survival and heterodimerizes with the wild-type EGFR
    • Luwor RB, Zhu HJ, Walker F, Vitali AA, Perera RM, et al. 2004. The tumor-specific de 2-7 epidermal growth factor receptor (EGFR) promotes cells survival and heterodimerizes with the wild-type EGFR. Oncogene 23: 6095-6104.
    • (2004) Oncogene , vol.23 , pp. 6095-6104
    • Luwor, R.B.1    Zhu, H.J.2    Walker, F.3    Vitali, A.A.4    Perera, R.M.5
  • 24
    • 33845926387 scopus 로고    scopus 로고
    • Epidermal Growth Factor Receptor Activation in Glioblastoma through Novel Missense Mutations in the Extracellular Domain
    • Lee JC, Vivanco I, Beroukhim R, Huang JH, Feng WL, et al. 2006. Epidermal Growth Factor Receptor Activation in Glioblastoma through Novel Missense Mutations in the Extracellular Domain. PLoS Med 3: e485.
    • (2006) PLoS Med , vol.3
    • Lee, J.C.1    Vivanco, I.2    Beroukhim, R.3    Huang, J.H.4    Feng, W.L.5
  • 25
    • 0037429728 scopus 로고    scopus 로고
    • Ligand-independent oncogenic signaling by the epidermal growth factor receptor: V-ErbB as a paradigm
    • Boerner JL, Danielsen A, Maihle NJ. 2003. Ligand-independent oncogenic signaling by the epidermal growth factor receptor: v-ErbB as a paradigm. Exp Cell Res 284:111-121.
    • (2003) Exp Cell Res , vol.284 , pp. 111-121
    • Boerner, J.L.1    Danielsen, A.2    Maihle, N.J.3
  • 26
    • 0021281324 scopus 로고
    • Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
    • Downward J, Yarden Y, Mayes E, Scrace G, Totty N, et al. 1984. Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences. Nature 307:521-527.
    • (1984) Nature , vol.307 , pp. 521-527
    • Downward, J.1    Yarden, Y.2    Mayes, E.3    Scrace, G.4    Totty, N.5
  • 27
    • 0035989898 scopus 로고    scopus 로고
    • Penington DJ, Bryant I, Riese DJ 2nd. 2002. Constitutively active ErbB4 and ErbB2 mutants exhibit distinct biological activities. Cell Growth Differ 13:247-256.
    • Penington DJ, Bryant I, Riese DJ 2nd. 2002. Constitutively active ErbB4 and ErbB2 mutants exhibit distinct biological activities. Cell Growth Differ 13:247-256.
  • 28
    • 0037456676 scopus 로고    scopus 로고
    • A constitutively active ErbB4 mutant inhibits drug-resistant colony formation by the DU-145 and PC-3 human prostate tumor cell lines
    • Williams EE, Trout LJ, Gallo RM, Pitfield SE, Bryant I, et al. 2003. A constitutively active ErbB4 mutant inhibits drug-resistant colony formation by the DU-145 and PC-3 human prostate tumor cell lines. Cancer Lett 192:67-74.
    • (2003) Cancer Lett , vol.192 , pp. 67-74
    • Williams, E.E.1    Trout, L.J.2    Gallo, R.M.3    Pitfield, S.E.4    Bryant, I.5
  • 29
    • 0031842104 scopus 로고    scopus 로고
    • Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface
    • Burke CL, Stern DF. 1998. Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface. Mol Cell Biol 18:5371-5379.
    • (1998) Mol Cell Biol , vol.18 , pp. 5371-5379
    • Burke, C.L.1    Stern, D.F.2
  • 30
    • 0027986757 scopus 로고
    • Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors
    • Siegel PM, Dankort DL, Hardy WR, Muller WJ. 1994. Novel activating mutations in the neu proto-oncogene involved in induction of mammary tumors. Mol Cell Biol 14:7068-7077.
    • (1994) Mol Cell Biol , vol.14 , pp. 7068-7077
    • Siegel, P.M.1    Dankort, D.L.2    Hardy, W.R.3    Muller, W.J.4
  • 31
    • 0037085373 scopus 로고    scopus 로고
    • The single transmembrane domains of ErbB receptors self-associate in cell membranes
    • Mendrola JM, Berger MB, King MC, Lemmon MA. 2002. The single transmembrane domains of ErbB receptors self-associate in cell membranes. J Biol Chem 277:4704-4712.
    • (2002) J Biol Chem , vol.277 , pp. 4704-4712
    • Mendrola, J.M.1    Berger, M.B.2    King, M.C.3    Lemmon, M.A.4
  • 32
    • 0020117514 scopus 로고
    • Identification of a phosphoprotein specifically induced by the transforming DNA of rat neuroblastomas
    • Padhy LC, Shih C, Cowing D, Finkelstein R, Weinberg RA. 1982. Identification of a phosphoprotein specifically induced by the transforming DNA of rat neuroblastomas. Cell 28:865-871.
    • (1982) Cell , vol.28 , pp. 865-871
    • Padhy, L.C.1    Shih, C.2    Cowing, D.3    Finkelstein, R.4    Weinberg, R.A.5
  • 33
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • Bargmann CI, Hung MC, Weinberg RA. 1986. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185 Cell 45:649-657.
    • (1986) Cell , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 34
    • 0029881315 scopus 로고    scopus 로고
    • Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor
    • Smith SO, Smith CS, Bormann BJ. 1996. Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor. Nat Struct Biol 3:252-258.
    • (1996) Nat Struct Biol , vol.3 , pp. 252-258
    • Smith, S.O.1    Smith, C.S.2    Bormann, B.J.3
  • 35
    • 0037199467 scopus 로고    scopus 로고
    • Transmembrane interactions in the activation of the Neu receptor tyrosine kinase
    • Smith SO, Smith C, Shekar S, Peersen O, Ziliox M, et al. 2002. Transmembrane interactions in the activation of the Neu receptor tyrosine kinase. Biochemistry 41:9321-9332.
    • (2002) Biochemistry , vol.41 , pp. 9321-9332
    • Smith, S.O.1    Smith, C.2    Shekar, S.3    Peersen, O.4    Ziliox, M.5
  • 36
    • 0012597802 scopus 로고
    • Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene
    • Bargmann CI, Weinberg RA. 1988. Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene. Proc Natl Acad Sci USA 85:5394-5398.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5394-5398
    • Bargmann, C.I.1    Weinberg, R.A.2
  • 37
    • 0024042025 scopus 로고
    • Oncogenic activation of the neuencoded receptor protein by point mutation and deletion
    • Bargmann CI, Weinberg RA. 1988. Oncogenic activation of the neuencoded receptor protein by point mutation and deletion. Embo J 7:2043-2052.
    • (1988) Embo J , vol.7 , pp. 2043-2052
    • Bargmann, C.I.1    Weinberg, R.A.2
  • 38
    • 0030614530 scopus 로고    scopus 로고
    • Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
    • Burke CL, Lemmon MA, Coren BA, Engelman DM, Stern DF. 1997. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 14:687-696.
    • (1997) Oncogene , vol.14 , pp. 687-696
    • Burke, C.L.1    Lemmon, M.A.2    Coren, B.A.3    Engelman, D.M.4    Stern, D.F.5
  • 39
    • 0029101843 scopus 로고
    • SHC and GRB-2 are constitutively by an epidermal growth factor receptor with a point mutation in the transmembrane domain
    • Miloso M, Mazzotti M, Vass WC, Beguinot L. 1995. SHC and GRB-2 are constitutively by an epidermal growth factor receptor with a point mutation in the transmembrane domain. J Biol Chem 270:19557-19562.
    • (1995) J Biol Chem , vol.270 , pp. 19557-19562
    • Miloso, M.1    Mazzotti, M.2    Vass, W.C.3    Beguinot, L.4
  • 40
    • 33846296953 scopus 로고    scopus 로고
    • A constitutively active ERBB4/HER4 allele with enhanced transcriptional coactivation and cell-killing activities
    • Vidal GA, Clark DE, Marrero L, Jones FE. 2007. A constitutively active ERBB4/HER4 allele with enhanced transcriptional coactivation and cell-killing activities. Oncogene 26:462-466.
    • (2007) Oncogene , vol.26 , pp. 462-466
    • Vidal, G.A.1    Clark, D.E.2    Marrero, L.3    Jones, F.E.4
  • 41
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib
    • Lynch TJ, Bell DW, Sordella R, Gurubhagavatula S, Okimoto RA, et al. 2004. 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) N Engl J Med , vol.350 , pp. 2129-2139
    • Lynch, T.J.1    Bell, D.W.2    Sordella, R.3    Gurubhagavatula, S.4    Okimoto, R.A.5
  • 42
    • 4143066760 scopus 로고    scopus 로고
    • Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways
    • Sordella R, Bell DW, Haber DA, Settleman J, 2004. Gefitinib-sensitizing EGFR mutations in lung cancer activate anti-apoptotic pathways. Science 305:1163-1167.
    • (2004) Science , vol.305 , pp. 1163-1167
    • Sordella, R.1    Bell, D.W.2    Haber, D.A.3    Settleman, J.4
  • 43
    • 12744253732 scopus 로고    scopus 로고
    • Effect of epidermal growth factor receptor mutations on the response to epidermal growth factor receptor tyrosine kinase inhibitors: Target-based populations for target-based drugs
    • Calvo E, Rowinsky EK. 2004. Effect of epidermal growth factor receptor mutations on the response to epidermal growth factor receptor tyrosine kinase inhibitors: target-based populations for target-based drugs. Clinical lung cancer 6 Suppl 1:S35-S42.
    • (2004) Clinical lung cancer , vol.6 , Issue.SUPPL. 1
    • Calvo, E.1    Rowinsky, E.K.2
  • 44
    • 24744450387 scopus 로고    scopus 로고
    • Epidermal growth factor receptor mutations in patients with non-small cell lung cancer
    • Johnson BE, Janne PA. 2005. Epidermal growth factor receptor mutations in patients with non-small cell lung cancer. Cancer Res 65: 7525-7529.
    • (2005) Cancer Res , vol.65 , pp. 7525-7529
    • Johnson, B.E.1    Janne, P.A.2
  • 45
    • 33744807493 scopus 로고    scopus 로고
    • EGF receptor mutations in lung cancer: From humans to mice and maybe back to humans
    • Arteaga CL. 2006. EGF receptor mutations in lung cancer: from humans to mice and maybe back to humans. Cancer cell 9:421-423.
    • (2006) Cancer cell , vol.9 , pp. 421-423
    • Arteaga, C.L.1
  • 46
    • 33749677330 scopus 로고    scopus 로고
    • Ji H, Sharpless NE, Wong KK. 2006. EGFR targeted therapy: view from biological standpoint. Cell cycle (Georgetown, Tex) 5:2072-2076.
    • Ji H, Sharpless NE, Wong KK. 2006. EGFR targeted therapy: view from biological standpoint. Cell cycle (Georgetown, Tex) 5:2072-2076.
  • 47
    • 25444505624 scopus 로고    scopus 로고
    • Epidermal growth factor-independent transformation of Ba/F3 cells with cancer-derived epidermal growth factor receptor mutants induces gefitinib-sensitive cell cycle progression
    • Jiang J, Greulich H, Janne PA, Sellers WR, Meyerson M, et al. 2005. Epidermal growth factor-independent transformation of Ba/F3 cells with cancer-derived epidermal growth factor receptor mutants induces gefitinib-sensitive cell cycle progression. Cancer Res 65: 8968-8974.
    • (2005) Cancer Res , vol.65 , pp. 8968-8974
    • Jiang, J.1    Greulich, H.2    Janne, P.A.3    Sellers, W.R.4    Meyerson, M.5
  • 48
    • 28444478439 scopus 로고    scopus 로고
    • Oncogenic transformation by inhibitor-sensitive and -resistant EGFR mutants
    • Greulich H, Chen TH, Feng W, Janne PA, Alvarez JV, et al. 2005. Oncogenic transformation by inhibitor-sensitive and -resistant EGFR mutants. PLoS Med 2:e313.
    • (2005) PLoS Med , vol.2
    • Greulich, H.1    Chen, T.H.2    Feng, W.3    Janne, P.A.4    Alvarez, J.V.5
  • 49
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao W, Miller VA, Politi KA, Riely GJ, Somwar R, et al. 2005. Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain PLoS Med 2:e73
    • (2005) PLoS Med , vol.2
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3    Riely, G.J.4    Somwar, R.5
  • 50
    • 23844444080 scopus 로고    scopus 로고
    • An alternative inhibitor overcomes resistance caused by a mutation of the epidermal growth factor receptor
    • Kobayashi S, Ji H, Yuza Y, Meyerson M, Wong KK, et al. 2005. An alternative inhibitor overcomes resistance caused by a mutation of the epidermal growth factor receptor. Cancer Res 65:7096-7101.
    • (2005) Cancer Res , vol.65 , pp. 7096-7101
    • Kobayashi, S.1    Ji, H.2    Yuza, Y.3    Meyerson, M.4    Wong, K.K.5
  • 51
    • 33846220461 scopus 로고    scopus 로고
    • Epidermal growth factor receptor kinase domain mutations in esophageal and pancreatic adenocarcinomas
    • Kwak EL, Jankowski J, Thayer SP, Lauwers GY, Brannigan BW, et al. 2006. Epidermal growth factor receptor kinase domain mutations in esophageal and pancreatic adenocarcinomas. Clin Cancer Res 12:4283-4287.
    • (2006) Clin Cancer Res , vol.12 , pp. 4283-4287
    • Kwak, E.L.1    Jankowski, J.2    Thayer, S.P.3    Lauwers, G.Y.4    Brannigan, B.W.5
  • 52
    • 28444455958 scopus 로고    scopus 로고
    • Inherited susceptibility to lung cancer may be associated with the T790M drug resistance mutation in EGFR
    • Bell DW, Gore I, Okimoto RA, Godin-Heymann N, Sordella R, et al. 2005. Inherited susceptibility to lung cancer may be associated with the T790M drug resistance mutation in EGFR. Nat Genet 37:1315-1316.
    • (2005) Nat Genet , vol.37 , pp. 1315-1316
    • Bell, D.W.1    Gore, I.2    Okimoto, R.A.3    Godin-Heymann, N.4    Sordella, R.5
  • 53
    • 4944232647 scopus 로고    scopus 로고
    • Lung cancer: Intragenic ERBB2 kinase mutations in tumours
    • Stephens P, Hunter C, Bignell G, Edkins S, Davies H, et al. 2004. Lung cancer: intragenic ERBB2 kinase mutations in tumours. Nature 431:525-526.
    • (2004) Nature , vol.431 , pp. 525-526
    • Stephens, P.1    Hunter, C.2    Bignell, G.3    Edkins, S.4    Davies, H.5
  • 55
    • 20144386787 scopus 로고    scopus 로고
    • Somatic mutations of the HER2 kinase domain in lung adenocarcinomas
    • Shigematsu H, Takahashi T, Nomura M, Majmudar K, Suzuki M, et al. 2005. Somatic mutations of the HER2 kinase domain in lung adenocarcinomas. Cancer Res 65:1642-1646.
    • (2005) Cancer Res , vol.65 , pp. 1642-1646
    • Shigematsu, H.1    Takahashi, T.2    Nomura, M.3    Majmudar, K.4    Suzuki, M.5
  • 56
    • 33745727112 scopus 로고    scopus 로고
    • HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors
    • Wang SE, Narasanna A, Perez-Torres M, Xiang B, Wu FY, et al. 2006. HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. Cancer cell 10:25-38.
    • (2006) Cancer cell , vol.10 , pp. 25-38
    • Wang, S.E.1    Narasanna, A.2    Perez-Torres, M.3    Xiang, B.4    Wu, F.Y.5
  • 57
    • 33746905531 scopus 로고    scopus 로고
    • Phosphotyrosine interactome of the ErbB-receptor kinase family
    • Schulze WX, Deng L, Mann M. 2005. Phosphotyrosine interactome of the ErbB-receptor kinase family. Mol Syst Biol 1:0008.
    • (2005) Mol Syst Biol , vol.1 , pp. 0008
    • Schulze, W.X.1    Deng, L.2    Mann, M.3
  • 58
    • 4744342856 scopus 로고    scopus 로고
    • Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation
    • Grovdal LM, Stang E, Sorkin A, Madshus IH. 2004. Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation. Exp Cell Res 300:388-395.
    • (2004) Exp Cell Res , vol.300 , pp. 388-395
    • Grovdal, L.M.1    Stang, E.2    Sorkin, A.3    Madshus, I.H.4
  • 59
    • 0036469898 scopus 로고    scopus 로고
    • A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling
    • Waterman H, Katz M, Rubin C, Shtiegman K, Lavi S, et al. 2002. A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. Embo J 21:303-313.
    • (2002) Embo J , vol.21 , pp. 303-313
    • Waterman, H.1    Katz, M.2    Rubin, C.3    Shtiegman, K.4    Lavi, S.5
  • 60
    • 0037339887 scopus 로고    scopus 로고
    • Grb2 regulates internalization of EGF receptors through clathrin-coated pits
    • Jiang X, Huang F, Marusyk A, Sorkin A. 2003. Grb2 regulates internalization of EGF receptors through clathrin-coated pits. Molecular biology of the cell 14:858-870.
    • (2003) Molecular biology of the cell , vol.14 , pp. 858-870
    • Jiang, X.1    Huang, F.2    Marusyk, A.3    Sorkin, A.4
  • 61
    • 14844334946 scopus 로고    scopus 로고
    • Growth factor receptor binding protein 2-mediated recruitment of the RING domain of Cbl to the epidermal growth factor receptor is essential and sufficient to support receptor endocytosis
    • Huang F, Sorkin A. 2005. Growth factor receptor binding protein 2-mediated recruitment of the RING domain of Cbl to the epidermal growth factor receptor is essential and sufficient to support receptor endocytosis. Molec Biol Cell 16:1268-1281.
    • (2005) Molec Biol Cell , vol.16 , pp. 1268-1281
    • Huang, F.1    Sorkin, A.2
  • 62
    • 33748316606 scopus 로고    scopus 로고
    • Gallo RM, Bryant I, Fry R, Williams EE, Riese DJ 2nd. 2006. Phosphorylation of ErbB4 on Tyr1056 is critical for inhibition of colony formation by prostate tumor cell lines. Biochem Biophys Res Commun 349:372-382.
    • Gallo RM, Bryant I, Fry R, Williams EE, Riese DJ 2nd. 2006. Phosphorylation of ErbB4 on Tyr1056 is critical for inhibition of colony formation by prostate tumor cell lines. Biochem Biophys Res Commun 349:372-382.
  • 63
    • 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 NE, Sudol M. 2003. 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) J Biol Chem , vol.278 , pp. 33334-33341
    • Komuro, A.1    Nagai, M.2    Navin, N.E.3    Sudol, M.4
  • 64
    • 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, Puggioni EM, Napoletano S, Visco V, Fraioli R, et al. 2004. 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) Exp Cell Res , vol.294 , pp. 469-479
    • Omerovic, J.1    Puggioni, E.M.2    Napoletano, S.3    Visco, V.4    Fraioli, R.5
  • 65
    • 23044492008 scopus 로고    scopus 로고
    • WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function
    • Aqeilan RI, Donati V, Palamarchuk A, Trapasso F, Kaou M, et al. 2005. WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function. Cancer Res 65:6764-6772.
    • (2005) Cancer Res , vol.65 , pp. 6764-6772
    • Aqeilan, R.I.1    Donati, V.2    Palamarchuk, A.3    Trapasso, F.4    Kaou, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.