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Volumn 104, Issue 3, 2003, Pages 303-309

Structural analysis of the ErbB-2 receptor using monoclonal antibodies: Implications for receptor signalling

Author keywords

Antibody; Ectodomain structure; Epitope; ErbB 2

Indexed keywords

ARGININE; EPIDERMAL GROWTH FACTOR RECEPTOR; GLYCINE; LEUCINE; MITOGEN ACTIVATED PROTEIN KINASE; MONOCLONAL ANTIBODY; ONCOPROTEIN; POLYPEPTIDE; PROTEIN TYROSINE KINASE;

EID: 0037431430     PISSN: 00207136     EISSN: None     Source Type: Journal    
DOI: 10.1002/ijc.10951     Document Type: Article
Times cited : (18)

References (37)
  • 2
    • 0029021518 scopus 로고
    • Heterodimerization and functional interaction between EGF receptor family members: A new signaling paradigm with implications for breast cancer research
    • Earp HS, Dawson TL, Li X, Yu H. Heterodimerization and functional interaction between EGF receptor family members: a new signaling paradigm with implications for breast cancer research. Breast Cancer Res Treat 1995;35:115-32.
    • (1995) Breast Cancer Res Treat , vol.35 , pp. 115-132
    • Earp, H.S.1    Dawson, T.L.2    Li, X.3    Yu, H.4
  • 3
    • 0034600849 scopus 로고    scopus 로고
    • New EMBO members' review: The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye MA, Neve RM, Lane HA, Hynes NE. New EMBO members' review: the ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J 2000;19:3159-67.
    • (2000) EMBO J , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 4
    • 0034000148 scopus 로고    scopus 로고
    • Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor
    • Jorissen RN, Epa VC, Treutlein HR, Garrett TP, Ward CW, Burgess AW. Characterization of a comparative model of the extracellular domain of the epidermal growth factor receptor. Protein Sci 2000;9:310-24.
    • (2000) Protein Sci , vol.9 , pp. 310-324
    • Jorissen, R.N.1    Epa, V.C.2    Treutlein, H.R.3    Garrett, T.P.4    Ward, C.W.5    Burgess, A.W.6
  • 6
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGuire WL. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 1987;235:177-82.
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ullrich, A.5    McGuire, W.L.6
  • 8
    • 0033009389 scopus 로고    scopus 로고
    • Binding specificities and affinities of egf domains for ErbB receptors
    • Jones JT, Akita RW, Sliwkowski MX. Binding specificities and affinities of egf domains for ErbB receptors. FEBS Lett 1999;447:227-31.
    • (1999) FEBS Lett , vol.447 , pp. 227-231
    • Jones, J.T.1    Akita, R.W.2    Sliwkowski, M.X.3
  • 9
    • 0028893444 scopus 로고
    • Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling
    • Graus-Porta D, Beerli RR, Hynes NE. Single-chain antibody-mediated intracellular retention of ErbB-2 impairs Neu differentiation factor and epidermal growth factor signaling. Mol Cell Biol 1995;15:1182-91.
    • (1995) Mol Cell Biol , vol.15 , pp. 1182-1191
    • Graus-Porta, D.1    Beerli, R.R.2    Hynes, N.E.3
  • 10
    • 0028823802 scopus 로고
    • Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2
    • Beerli RR, Graus-Porta D, Woods-Cook K, Chen X, Yarden Y, Hynes NE. Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2. Mol Cell Biol 1995;15:6496-505.
    • (1995) Mol Cell Biol , vol.15 , pp. 6496-6505
    • Beerli, R.R.1    Graus-Porta, D.2    Woods-Cook, K.3    Chen, X.4    Yarden, Y.5    Hynes, N.E.6
  • 11
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of inter receptor interactions determines signal transduction by Neu differentiation factor/neluregulin and epidermal growth factor
    • Tzahar E, Waterman H, Chen X, Levkowitz G, Karunagaran D, Lavi S, Ratzkin BJ, Yarden Y. A hierarchical network of inter receptor interactions determines signal transduction by Neu differentiation factor/neluregulin and epidermal growth factor. Mol Cell Biol 1996;16:5276-87.
    • (1996) Mol Cell Biol , vol.16 , 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
  • 13
    • 0030795612 scopus 로고    scopus 로고
    • The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions
    • Alroy I, Yarden Y. The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand-receptor interactions. FEBS Lett 1997;410:83-6.
    • (1997) FEBS Lett , vol.410 , pp. 83-86
    • Alroy, I.1    Yarden, Y.2
  • 14
    • 0031840484 scopus 로고    scopus 로고
    • ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner
    • Olayioye MA, Graus-Porta D, Beerli RR, Rohrer J, Gay B, Hynes NE. ErbB-1 and ErbB-2 acquire distinct signaling properties dependent upon their dimerization partner. Mol Cell Biol 1998:18:5042-51.
    • (1998) Mol Cell Biol , vol.18 , pp. 5042-5051
    • Olayioye, M.A.1    Graus-Porta, D.2    Beerli, R.R.3    Rohrer, J.4    Gay, B.5    Hynes, N.E.6
  • 15
    • 0036005957 scopus 로고    scopus 로고
    • Molecular modelling in structural biology
    • Forster MJ. Molecular modelling in structural biology. Micron 2002:33:365-84.
    • (2002) Micron , vol.33 , pp. 365-384
    • Forster, M.J.1
  • 16
    • 0035487690 scopus 로고    scopus 로고
    • A tour of structural genomics
    • Brenner SE. A tour of structural genomics. Nat Rev Genet 2001;2:801-9.
    • (2001) Nat Rev Genet , vol.2 , pp. 801-809
    • Brenner, S.E.1
  • 18
    • 0029060529 scopus 로고
    • Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor
    • Ward CW, Hoyne PA, Flegg RH. Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor. Proteins 1995:22:141-53.
    • (1995) Proteins , vol.22 , pp. 141-153
    • Ward, C.W.1    Hoyne, P.A.2    Flegg, R.H.3
  • 20
    • 0035675556 scopus 로고    scopus 로고
    • Anti-ErbB-2 monoclonal antibodies and ErbB-2-directed vaccines
    • Yip YL, Ward RL. Anti-ErbB-2 monoclonal antibodies and ErbB-2-directed vaccines. Cancer Immunol Immunother 2002;50:569-87.
    • (2002) Cancer Immunol Immunother , vol.50 , pp. 569-587
    • Yip, Y.L.1    Ward, R.L.2
  • 21
    • 0035871618 scopus 로고    scopus 로고
    • Identification of epitope regions recognized by tumor inhibitory and stimulatory anti-erbb-2 monoclonal antibodies: Implications for vaccine design
    • Yip YL, Smith G, Koch J, Dubel S, Ward RL. Identification of epitope regions recognized by tumor inhibitory and stimulatory anti-erbb-2 monoclonal antibodies: implications for vaccine design. J Immunol 2001;166;5271-8.
    • (2001) J Immunol , vol.166 , pp. 5271-5278
    • Yip, Y.L.1    Smith, G.2    Koch, J.3    Dubel, S.4    Ward, R.L.5
  • 22
    • 0028816556 scopus 로고
    • Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction
    • Fromant M, Blanquet S, Plateau P. Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction. Anal Biochem 1995;224:347-53.
    • (1995) Anal Biochem , vol.224 , pp. 347-353
    • Fromant, M.1    Blanquet, S.2    Plateau, P.3
  • 23
    • 0025008445 scopus 로고
    • Identification of native protein folds amongst a large number of incorrect models: The calculation of low energy conformations from potentials of mean force
    • Hendlich M, Lackner P, Weitckus S, Floeckner H, Froschauer R, Gottsbacher K, Casari G, Sippl MJ. Identification of native protein folds amongst a large number of incorrect models: the calculation of low energy conformations from potentials of mean force. J Mol Biol 1990;216:167-80.
    • (1990) J Mol Biol , vol.216 , pp. 167-180
    • Hendlich, M.1    Lackner, P.2    Weitckus, S.3    Floeckner, H.4    Froschauer, R.5    Gottsbacher, K.6    Casari, G.7    Sippl, M.J.8
  • 24
    • 0031560777 scopus 로고    scopus 로고
    • Contact area difference (CAD): A robust measure to evaluate accuracy of protein models
    • Abagyan RA, Totrov MM. Contact area difference (CAD): a robust measure to evaluate accuracy of protein models. J Mol Biol 1997;268:678-85.
    • (1997) J Mol Biol , vol.268 , pp. 678-685
    • Abagyan, R.A.1    Totrov, M.M.2
  • 25
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol 1998;280:1-9.
    • (1998) J Mol Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 26
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies DR, Cohen GH. Interactions of protein antigens with antibodies. Proc Natl Acad Sci USA 1996;93:7-12.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 27
    • 0026091927 scopus 로고
    • Mechanistic aspects of the opposing effects of monoclonal antibodies to the ERBB2 receptor on tumor growth
    • Stancovski I, Hurwitz E, Leitner O, Ullrich A, Yarden Y, Sela M. Mechanistic aspects of the opposing effects of monoclonal antibodies to the ERBB2 receptor on tumor growth. Proc Natl Acad Sci USA 1991;88:8691-5.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8691-8695
    • Stancovski, I.1    Hurwitz, E.2    Leitner, O.3    Ullrich, A.4    Yarden, Y.5    Sela, M.6
  • 28
    • 0028229715 scopus 로고
    • A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP kinase pathway
    • Ben-Levy R, Paterson HF, Marshall CJ, Yarden Y. A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP kinase pathway. EMBO J 1994;13:3302-11.
    • (1994) EMBO J , vol.13 , pp. 3302-3311
    • Ben-Levy, R.1    Paterson, H.F.2    Marshall, C.J.3    Yarden, Y.4
  • 29
    • 0026793456 scopus 로고
    • Growth factor signaling by receptor tyrosine kinases
    • Schlessinger J, Ullrich A. Growth factor signaling by receptor tyrosine kinases. Neuron 1992;9:383-91.
    • (1992) Neuron , vol.9 , pp. 383-391
    • Schlessinger, J.1    Ullrich, A.2
  • 30
    • 0030959114 scopus 로고    scopus 로고
    • A subclass of tumor-inhibitory monoclonal antibodies to Erbb-2/Her2 blocks crosstalk with growth factor receptors
    • Klapper LN, Vaisman N, Hurwitz E, Pinkaskramarski R, Yarden Y, Sela M. A subclass of tumor-inhibitory monoclonal antibodies to Erbb-2/Her2 blocks crosstalk with growth factor receptors. Oncogene 1997;14:2099-109.
    • (1997) Oncogene , vol.14 , pp. 2099-2109
    • Klapper, L.N.1    Vaisman, N.2    Hurwitz, E.3    Pinkaskramarski, R.4    Yarden, Y.5    Sela, M.6
  • 32
    • 0026575750 scopus 로고
    • Distances between the antigen-binding sites of three murine antibody subclasses measured using neutron and X-ray scattering
    • Sosnick TR, Benjamin DC, Novotny J, Seeger PA, Trewhella J. Distances between the antigen-binding sites of three murine antibody subclasses measured using neutron and X-ray scattering. Biochemistry 1992;31:1779-86.
    • (1992) Biochemistry , vol.31 , pp. 1779-1786
    • Sosnick, T.R.1    Benjamin, D.C.2    Novotny, J.3    Seeger, P.A.4    Trewhella, J.5
  • 33
    • 0025873538 scopus 로고
    • Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor: A low resolution projection structure of the ligand-binding domain
    • Lax I, Mitra AK, Ravera C, Hurwitz DR, Rubinstein M, Ullrich A, Stroud RM, Schlessinger J. Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor: a low resolution projection structure of the ligand-binding domain. J Biol Chem 1991;266:13828-33.
    • (1991) J Biol Chem , vol.266 , pp. 13828-13833
    • Lax, I.1    Mitra, A.K.2    Ravera, C.3    Hurwitz, D.R.4    Rubinstein, M.5    Ullrich, A.6    Stroud, R.M.7    Schlessinger, J.8
  • 34
    • 0035967525 scopus 로고    scopus 로고
    • Evidence for an alphahelix → pi-bulge helicity modulation for the neu/erbB-2 membrane-spanning segment
    • Goetz M, Carlotti C, Bontems F, Dufourc EJ. Evidence for an alphahelix → pi-bulge helicity modulation for the neu/erbB-2 membrane-spanning segment. Biochemistry 2001;40:6534-40.
    • (2001) Biochemistry , vol.40 , pp. 6534-6540
    • Goetz, M.1    Carlotti, C.2    Bontems, F.3    Dufourc, E.J.4
  • 35
    • 0033786730 scopus 로고    scopus 로고
    • Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase
    • Bell CA, Tynan JA, Hart KC, Meyer AN, Robertson SC, Donoghue DJ. Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase. Mol Biol Cell 2000;11:3589-99.
    • (2000) Mol Biol Cell , vol.11 , pp. 3589-3599
    • Bell, C.A.1    Tynan, J.A.2    Hart, K.C.3    Meyer, A.N.4    Robertson, S.C.5    Donoghue, D.J.6
  • 36
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki T, Maruyama H, Maruyama IN. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J Mol Biol 2001;311:1011-26.
    • (2001) J Mol Biol , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 37
    • 0035102191 scopus 로고    scopus 로고
    • The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely orieted, hydrophobic motif
    • Constantinescu SN, Huang LJ, Nam H, Lodish HF. The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely orieted, hydrophobic motif. Mol Cell 2001;7:377-85.
    • (2001) Mol Cell , vol.7 , pp. 377-385
    • Constantinescu, S.N.1    Huang, L.J.2    Nam, H.3    Lodish, H.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.