메뉴 건너뛰기




Volumn 15, Issue 1, 2015, Pages

Compounds identified by virtual docking to a tetrameric EGFR extracellular domain can modulate Grb2 internalization

Author keywords

Epidermal growth factor receptor; Extracellular domain; Grb2; Protein multimerization

Indexed keywords

ANTINEOPLASTIC AGENT; CETUXIMAB; EPIDERMAL GROWTH FACTOR RECEPTOR; ERLOTINIB; F 09220900; F 12600014; F 21450053; F 25730380; F 25990073; F 27382186; F 31090096; F 32630061; F 33853143; F 34060664; F 52300424; F 52530138; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; TETRAMER; UNCLASSIFIED DRUG; GRB2 PROTEIN, HUMAN; PROTEIN KINASE INHIBITOR;

EID: 84930666116     PISSN: None     EISSN: 14712407     Source Type: Journal    
DOI: 10.1186/s12885-015-1415-6     Document Type: Article
Times cited : (4)

References (46)
  • 1
    • 0034697962 scopus 로고    scopus 로고
    • The EGF receptor provides an essential survival signal for SOS-dependent skin tumor development
    • Sibilia M, Fleischmann A, Behrens A, Stingl L, Carroll J, Watt FM, et al. The EGF receptor provides an essential survival signal for SOS-dependent skin tumor development. Cell. 2000;102(2):211-20.
    • (2000) Cell , vol.102 , Issue.2 , pp. 211-220
    • Sibilia, M.1    Fleischmann, A.2    Behrens, A.3    Stingl, L.4    Carroll, J.5    Watt, F.M.6
  • 2
  • 5
    • 84862513344 scopus 로고    scopus 로고
    • Targeting of a conformationally exposed, tumor-specific epitope of EGFR as a strategy for cancer therapy
    • Gan HK, Burgess AW, Clayton AH, Scott AM. Targeting of a conformationally exposed, tumor-specific epitope of EGFR as a strategy for cancer therapy. Cancer Res. 2012;72(12):2924-30.
    • (2012) Cancer Res , vol.72 , Issue.12 , pp. 2924-2930
    • Gan, H.K.1    Burgess, A.W.2    Clayton, A.H.3    Scott, A.M.4
  • 6
    • 79954586068 scopus 로고    scopus 로고
    • Phase I/II trial of cetuximab and erlotinib in patients with lung adenocarcinoma and acquired resistance to erlotinib
    • Janjigian YY, Azzoli CG, Krug LM, Pereira LK, Rizvi NA, Pietanza MC, et al. Phase I/II trial of cetuximab and erlotinib in patients with lung adenocarcinoma and acquired resistance to erlotinib. Clin Cancer Res. 2011;17(8):2521-7.
    • (2011) Clin Cancer Res , vol.17 , Issue.8 , pp. 2521-2527
    • Janjigian, Y.Y.1    Azzoli, C.G.2    Krug, L.M.3    Pereira, L.K.4    Rizvi, N.A.5    Pietanza, M.C.6
  • 7
    • 84862987061 scopus 로고    scopus 로고
    • Dual targeting of the epidermal growth factor receptor using the combination of cetuximab and erlotinib: preclinical evaluation and results of the phase II DUX study in chemotherapy-refractory, advanced colorectal cancer
    • Weickhardt AJ, Price TJ, Chong G, Gebski V, Pavlakis N, Johns TG, et al. Dual targeting of the epidermal growth factor receptor using the combination of cetuximab and erlotinib: preclinical evaluation and results of the phase II DUX study in chemotherapy-refractory, advanced colorectal cancer. J Clin Oncol. 2012;30(13):1505-12.
    • (2012) J Clin Oncol , vol.30 , Issue.13 , pp. 1505-1512
    • Weickhardt, A.J.1    Price, T.J.2    Chong, G.3    Gebski, V.4    Pavlakis, N.5    Johns, T.G.6
  • 9
    • 84893273182 scopus 로고    scopus 로고
    • Structure-function relationships and supramolecular organization of the EGFR (epidermal growth factor receptor) on the cell surface
    • Needham SR, Zanetti-Domingues LC, Hirsch M, Rolfe DJ, Tynan CJ, Roberts SK, et al. Structure-function relationships and supramolecular organization of the EGFR (epidermal growth factor receptor) on the cell surface. Biochem Soc Trans. 2014;42(1):114-9.
    • (2014) Biochem Soc Trans , vol.42 , Issue.1 , pp. 114-119
    • Needham, S.R.1    Zanetti-Domingues, L.C.2    Hirsch, M.3    Rolfe, D.J.4    Tynan, C.J.5    Roberts, S.K.6
  • 10
    • 10744230127 scopus 로고    scopus 로고
    • An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors
    • Burgess AW, Cho HS, Eigenbrot C, Ferguson KM, Garrett TP, Leahy DJ, et al. An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. Mol Cell. 2003;12(3):541-52.
    • (2003) Mol Cell , vol.12 , Issue.3 , pp. 541-552
    • Burgess, A.W.1    Cho, H.S.2    Eigenbrot, C.3    Ferguson, K.M.4    Garrett, T.P.5    Leahy, D.J.6
  • 11
    • 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, Lemmon MA. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell. 2003;11(2):507-17.
    • (2003) Mol Cell , vol.11 , Issue.2 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 12
    • 77955627615 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity in growth factor binding to an EGF receptor
    • Alvarado D, Klein DE, Lemmon MA. Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell. 2010;142(4):568-79.
    • (2010) Cell , vol.142 , Issue.4 , pp. 568-579
    • Alvarado, D.1    Klein, D.E.2    Lemmon, M.A.3
  • 13
    • 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. 2005;6(10):942-8.
    • (2005) EMBO Rep , vol.6 , Issue.10 , pp. 942-948
    • Wang, Q.1    Villeneuve, G.2    Wang, Z.3
  • 14
    • 0036696824 scopus 로고    scopus 로고
    • Lateral propagation of EGF signaling after local stimulation is dependent on receptor density
    • Sawano A, Takayama S, Matsuda M, Miyawaki A. Lateral propagation of EGF signaling after local stimulation is dependent on receptor density. Dev Cell. 2002;3(2):245-57.
    • (2002) Dev Cell , vol.3 , Issue.2 , pp. 245-257
    • Sawano, A.1    Takayama, S.2    Matsuda, M.3    Miyawaki, A.4
  • 15
    • 77955289201 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation
    • Ariotti N, Liang H, Xu Y, Zhang Y, Yonekubo Y, Inder K, et al. Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation. Mol Cell Biol. 2010;30(15):3795-804.
    • (2010) Mol Cell Biol , vol.30 , Issue.15 , pp. 3795-3804
    • Ariotti, N.1    Liang, H.2    Xu, Y.3    Zhang, Y.4    Yonekubo, Y.5    Inder, K.6
  • 16
    • 34247230905 scopus 로고    scopus 로고
    • Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding
    • Clayton AH, Tavarnesi ML, Johns TG. Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding. Biochemistry. 2007;46(15):4589-97.
    • (2007) Biochemistry , vol.46 , Issue.15 , pp. 4589-4597
    • Clayton, A.H.1    Tavarnesi, M.L.2    Johns, T.G.3
  • 17
    • 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 AH, Walker F, Orchard SG, Henderson C, Fuchs D, Rothacker J, 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. 2005;280(34):30392-9.
    • (2005) J Biol Chem , vol.280 , Issue.34 , pp. 30392-30399
    • Clayton, A.H.1    Walker, F.2    Orchard, S.G.3    Henderson, C.4    Fuchs, D.5    Rothacker, J.6
  • 18
    • 84878691793 scopus 로고    scopus 로고
    • Exploring higher-order EGFR oligomerisation and phosphorylation-a combined experimental and theoretical approach
    • Kozer N, Barua D, Orchard S, Nice EC, Burgess AW, Hlavacek WS, et al. Exploring higher-order EGFR oligomerisation and phosphorylation-a combined experimental and theoretical approach. Mol Biosyst. 2013;9(7):1849-63.
    • (2013) Mol Biosyst , vol.9 , Issue.7 , pp. 1849-1863
    • Kozer, N.1    Barua, D.2    Orchard, S.3    Nice, E.C.4    Burgess, A.W.5    Hlavacek, W.S.6
  • 20
    • 67649781716 scopus 로고    scopus 로고
    • Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics
    • Kastner J, Loeffler HH, Roberts SK, Martin-Fernandez ML, Winn MD. Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics. J Struct Biol. 2009;167(2):117-28.
    • (2009) J Struct Biol , vol.167 , Issue.2 , pp. 117-128
    • Kastner, J.1    Loeffler, H.H.2    Roberts, S.K.3    Martin-Fernandez, M.L.4    Winn, M.D.5
  • 21
    • 79958071305 scopus 로고    scopus 로고
    • Human epidermal growth factor receptor (EGFR) aligned on the plasma membrane adopts key features of Drosophila EGFR asymmetry
    • Tynan CJ, Roberts SK, Rolfe DJ, Clarke DT, Loeffler HH, Kastner J, et al. Human epidermal growth factor receptor (EGFR) aligned on the plasma membrane adopts key features of Drosophila EGFR asymmetry. Mol Cell Biol. 2011;31(11):2241-52.
    • (2011) Mol Cell Biol , vol.31 , Issue.11 , pp. 2241-2252
    • Tynan, C.J.1    Roberts, S.K.2    Rolfe, D.J.3    Clarke, D.T.4    Loeffler, H.H.5    Kastner, J.6
  • 22
    • 0029665883 scopus 로고    scopus 로고
    • Structural analysis of p185c-neu and epidermal growth factor receptor tyrosine kinases: oligomerization of kinase domains
    • Murali R, Brennan PJ, Kieber-Emmons T, Greene MI. Structural analysis of p185c-neu and epidermal growth factor receptor tyrosine kinases: oligomerization of kinase domains. Proc Natl Acad Sci U S A. 1996;93(13):6252-7.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.13 , pp. 6252-6257
    • Murali, R.1    Brennan, P.J.2    Kieber-Emmons, T.3    Greene, M.I.4
  • 24
    • 0041923790 scopus 로고    scopus 로고
    • Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3
    • Chen CH, Chernis GA, Hoang VQ, Landgraf R. Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3. Proc Natl Acad Sci U S A. 2003;100(16):9226-31.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.16 , pp. 9226-9231
    • Chen, C.H.1    Chernis, G.A.2    Hoang, V.Q.3    Landgraf, R.4
  • 25
    • 84865165294 scopus 로고    scopus 로고
    • Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling
    • Zhang Q, Park E, Kani K, Landgraf R. Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling. Proc Natl Acad Sci U S A. 2012;109(33):13237-42.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.33 , pp. 37-42
    • Zhang, Q.1    Park, E.2    Kani, K.3    Landgraf, R.4
  • 26
    • 0034713838 scopus 로고    scopus 로고
    • Heregulin reverses the oligomerization of HER3
    • Landgraf R, Eisenberg D. Heregulin reverses the oligomerization of HER3. Biochemistry. 2000;39(29):8503-11.
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8503-8511
    • Landgraf, R.1    Eisenberg, D.2
  • 27
    • 56249134876 scopus 로고    scopus 로고
    • Higher-order association states of cellular ERBB3 probed with photo-cross-linkable aptamers
    • Park E, Baron R, Landgraf R. Higher-order association states of cellular ERBB3 probed with photo-cross-linkable aptamers. Biochemistry. 2008;47(46):11992-2005.
    • (2008) Biochemistry , vol.47 , Issue.46 , pp. 11992-12005
    • Park, E.1    Baron, R.2    Landgraf, R.3
  • 28
    • 12144289984 scopus 로고    scopus 로고
    • Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner RA, Banks JL, Murphy RB, Halgren TA, Klicic JJ, Mainz DT, et al. Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem. 2004;47(7):1739-49.
    • (2004) J Med Chem , vol.47 , Issue.7 , pp. 1739-1749
    • Friesner, R.A.1    Banks, J.L.2    Murphy, R.B.3    Halgren, T.A.4    Klicic, J.J.5    Mainz, D.T.6
  • 29
    • 33750124980 scopus 로고    scopus 로고
    • Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes
    • Friesner RA, Murphy RB, Repasky MP, Frye LL, Greenwood JR, Halgren TA, et al. Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes. J Med Chem. 2006;49(21):6177-96.
    • (2006) J Med Chem , vol.49 , Issue.21 , pp. 6177-6196
    • Friesner, R.A.1    Murphy, R.B.2    Repasky, M.P.3    Frye, L.L.4    Greenwood, J.R.5    Halgren, T.A.6
  • 30
    • 1642310340 scopus 로고    scopus 로고
    • Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening
    • Halgren TA, Murphy RB, Friesner RA, Beard HS, Frye LL, Pollard WT, et al. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J Med Chem. 2004;47(7):1750-9.
    • (2004) J Med Chem , vol.47 , Issue.7 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6
  • 31
    • 78951489049 scopus 로고    scopus 로고
    • Feedback regulation of EGFR signalling: decision making by early and delayed loops
    • Avraham R, Yarden Y. Feedback regulation of EGFR signalling: decision making by early and delayed loops. Nat Rev Mol Cell Biol. 2011;12(2):104-17.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , Issue.2 , pp. 104-117
    • Avraham, R.1    Yarden, Y.2
  • 32
    • 84872869007 scopus 로고    scopus 로고
    • Targeting C4-demethylating genes in the cholesterol pathway sensitizes cancer cells to EGF receptor inhibitors via increased EGF receptor degradation
    • Sukhanova A, Gorin A, Serebriiskii IG, Gabitova L, Zheng H, Restifo D, et al. Targeting C4-demethylating genes in the cholesterol pathway sensitizes cancer cells to EGF receptor inhibitors via increased EGF receptor degradation. Cancer discovery. 2013;3(1):96-111.
    • (2013) Cancer discovery , vol.3 , Issue.1 , pp. 96-111
    • Sukhanova, A.1    Gorin, A.2    Serebriiskii, I.G.3    Gabitova, L.4    Zheng, H.5    Restifo, D.6
  • 33
    • 84880441014 scopus 로고    scopus 로고
    • Temporal regulation of EGF signalling networks by the scaffold protein Shc1
    • Zheng Y, Zhang C, Croucher DR, Soliman MA, St-Denis N, Pasculescu A, et al. Temporal regulation of EGF signalling networks by the scaffold protein Shc1. Nature. 2013;499(7457):166-71.
    • (2013) Nature , vol.499 , Issue.7457 , pp. 166-171
    • Zheng, Y.1    Zhang, C.2    Croucher, D.R.3    Soliman, M.A.4    St-Denis, N.5    Pasculescu, A.6
  • 35
    • 84919393755 scopus 로고    scopus 로고
    • Monensin inhibits epidermal growth factor receptor trafficking and activation: synergistic cytotoxicity in combination with EGFR inhibitors
    • Dayekh K, Johnson-Obaseki S, Corsten M, Villeneuve PJ, Sekhon HS, Weberpals JI, et al. Monensin inhibits epidermal growth factor receptor trafficking and activation: synergistic cytotoxicity in combination with EGFR inhibitors. Mol Cancer Ther. 2014;13(11):2559-71.
    • (2014) Mol Cancer Ther , vol.13 , Issue.11 , pp. 2559-2571
    • Dayekh, K.1    Johnson-Obaseki, S.2    Corsten, M.3    Villeneuve, P.J.4    Sekhon, H.S.5    Weberpals, J.I.6
  • 37
    • 0030054907 scopus 로고    scopus 로고
    • Anti-tumor and cell cycle responses in KB cells treated with a chimeric anti-EGFR monoclonal antibody in combination with cisplatin
    • Prewett M, Rockwell P, Rose C, Goldstein N. Anti-tumor and cell cycle responses in KB cells treated with a chimeric anti-EGFR monoclonal antibody in combination with cisplatin. Int J Oncol. 1996;9(2):217-24.
    • (1996) Int J Oncol , vol.9 , Issue.2 , pp. 217-224
    • Prewett, M.1    Rockwell, P.2    Rose, C.3    Goldstein, N.4
  • 40
    • 17444403242 scopus 로고    scopus 로고
    • Structural basis for inhibition of the epidermal growth factor receptor by cetuximab
    • Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM. Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell. 2005;7(4):301-11.
    • (2005) Cancer Cell , vol.7 , Issue.4 , pp. 301-311
    • Li, S.1    Schmitz, K.R.2    Jeffrey, P.D.3    Wiltzius, J.J.4    Kussie, P.5    Ferguson, K.M.6
  • 41
    • 84876732401 scopus 로고    scopus 로고
    • Impact of quaternary structure dynamics on allosteric drug discovery
    • Jaffe EK. Impact of quaternary structure dynamics on allosteric drug discovery. Curr Top Med Chem. 2013;13(1):55-63.
    • (2013) Curr Top Med Chem , vol.13 , Issue.1 , pp. 55-63
    • Jaffe, E.K.1
  • 42
    • 84987615742 scopus 로고    scopus 로고
    • Allosteric modulation of protein oligomerization: an emerging approach to drug design
    • Gabizon R, Friedler A. Allosteric modulation of protein oligomerization: an emerging approach to drug design. Frontiers in chemistry. 2014;2:9.
    • (2014) Frontiers in chemistry , vol.2 , pp. 9
    • Gabizon, R.1    Friedler, A.2
  • 43
    • 84882787658 scopus 로고    scopus 로고
    • Structural rearrangement of ebola virus VP40 begets multiple functions in the virus life cycle
    • Bornholdt ZA, Noda T, Abelson DM, Halfmann P, Wood MR, Kawaoka Y, et al. Structural rearrangement of ebola virus VP40 begets multiple functions in the virus life cycle. Cell. 2013;154(4):763-74.
    • (2013) Cell , vol.154 , Issue.4 , pp. 763-774
    • Bornholdt, Z.A.1    Noda, T.2    Abelson, D.M.3    Halfmann, P.4    Wood, M.R.5    Kawaoka, Y.6
  • 45
    • 84857828499 scopus 로고    scopus 로고
    • Allostery and the dynamic oligomerization of porphobilinogen synthase
    • Jaffe EK, Lawrence SH. Allostery and the dynamic oligomerization of porphobilinogen synthase. Arch Biochemi Biophys. 2012;519(2):144-53.
    • (2012) Arch Biochemi Biophys , vol.519 , Issue.2 , pp. 144-153
    • Jaffe, E.K.1    Lawrence, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.