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Volumn 9, Issue 3, 2014, Pages

Quantification and kinetic analysis of Grb2-EGFR interaction on micro-patterned surfaces for the characterization of EGFR-modulating substances

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; MONOCLONAL ANTIBODY; PROTEIN TYROSINE KINASE INHIBITOR; TYROSINE KINASE RECEPTOR; VASCULOTROPIN RECEPTOR; 4 (3 CHLOROANILINO) 6,7 DIMETHOXYQUINAZOLINE; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; QUINAZOLINE DERIVATIVE; TYRPHOSTIN;

EID: 84899126115     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0092151     Document Type: Article
Times cited : (44)

References (47)
  • 2
    • 33847696075 scopus 로고    scopus 로고
    • Receptor tyrosine kinases: Mechanisms of activation and signaling
    • DOI 10.1016/j.ceb.2007.02.010, PII S0955067407000245
    • Hubbard SR, Miller WT (2007) Receptor tyrosine kinases: mechanisms of activation and signaling. Curr Opin Cell Biol 19: 117-123. (Pubitemid 46386407)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.2 , pp. 117-123
    • Hubbard, S.R.1    Miller, W.T.2
  • 3
    • 33847718214 scopus 로고    scopus 로고
    • The EGF receptor family: Spearheading a merger of signaling and therapeutics
    • DOI 10.1016/j.ceb.2007.02.008, PII S0955067407000221
    • Bublil EM, Yarden Y (2007) The EGF receptor family: spearheading a merger of signaling and therapeutics. Curr Opin Cell Biol 19: 124-134. (Pubitemid 46386405)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.2 , pp. 124-134
    • Bublil, E.M.1    Yarden, Y.2
  • 4
    • 62749112560 scopus 로고    scopus 로고
    • Annexins-modulators of EGF receptor signalling and trafficking
    • Grewal T, Enrich C (2009) Annexins-modulators of EGF receptor signalling and trafficking. Cell Signal 21: 847-858.
    • (2009) Cell Signal , vol.21 , pp. 847-858
    • Grewal, T.1    Enrich, C.2
  • 6
    • 70349860264 scopus 로고    scopus 로고
    • Growth factor receptor expression in anal squamous lesions: Modifications associated with oncogenic human papillomavirus and human immunodeficiency virus
    • Walker F, Abramowitz L, Benabderrahmane D, Duval X, Descatoire V, et al. (2009) Growth factor receptor expression in anal squamous lesions: modifications associated with oncogenic human papillomavirus and human immunodeficiency virus. Hum Pathol 40: 1517-1527.
    • (2009) Hum Pathol , vol.40 , pp. 1517-1527
    • Walker, F.1    Abramowitz, L.2    Benabderrahmane, D.3    Duval, X.4    Descatoire, V.5
  • 7
    • 0034947649 scopus 로고    scopus 로고
    • EGF mutant receptor vIII as a molecular target in cancer therapy
    • DOI 10.1677/erc.0.0080083
    • Kuan CT, Wikstrand CJ, Bigner DD (2001) EGF mutant receptor vIII as a molecular target in cancer therapy. Endocr Relat Cancer 8: 83-96. (Pubitemid 32641351)
    • (2001) Endocrine-Related Cancer , vol.8 , Issue.2 , pp. 83-96
    • Kuan, C.-T.1    Wikstrand, C.J.2    Bigner, D.D.3
  • 10
    • 39649116928 scopus 로고    scopus 로고
    • EGFR tyrosine kinase inhibitors in lung cancer: An evolving story
    • DOI 10.1146/annurev.med.59.090506.202405
    • Sequist LV, Lynch TJ (2008) EGFR tyrosine kinase inhibitors in lung cancer: an evolving story. Annu Rev Med 59: 429-442. (Pubitemid 351287947)
    • (2008) Annual Review of Medicine , vol.59 , pp. 429-442
    • Sequist, L.V.1    Lynch, T.J.2
  • 11
    • 1842791537 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic properties of EGFR inhibitors under clinical investigation
    • DOI 10.1016/j.ctrv.2003.10.003
    • Thomas SM, Grandis JR (2004) Pharmacokinetic and pharmacodynamic properties of EGFR inhibitors under clinical investigation. Cancer Treat Rev 30: 255-268. (Pubitemid 38477271)
    • (2004) Cancer Treatment Reviews , vol.30 , Issue.3 , pp. 255-268
    • Thomas, S.M.1    Grandis, J.R.2
  • 12
    • 77956268839 scopus 로고    scopus 로고
    • Understanding resistance to EGFR inhibitors-impact on future treatment strategies
    • Wheeler DL, Dunn EF, Harari PM (2010) Understanding resistance to EGFR inhibitors-impact on future treatment strategies. Nat Rev Clin Oncol 7: 493-507.
    • (2010) Nat Rev Clin Oncol , vol.7 , pp. 493-507
    • Wheeler, D.L.1    Dunn, E.F.2    Harari, P.M.3
  • 13
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • DOI 10.1038/nrc1609
    • Hynes NE, Lane HA (2005) ERBB receptors and cancer: the complexity of targeted inhibitors. Nat Rev Cancer 5: 341-354. (Pubitemid 40637826)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 15
    • 77953023817 scopus 로고    scopus 로고
    • In situ analysis of tyrosine phosphorylation networks by FLIM on cell arrays
    • Grecco HE, Roda-Navarro P, Girod A, Hou J, Frahm T, et al. (2010) In situ analysis of tyrosine phosphorylation networks by FLIM on cell arrays. Nat Methods 7: 467-472.
    • (2010) Nat Methods , vol.7 , pp. 467-472
    • Grecco, H.E.1    Roda-Navarro, P.2    Girod, A.3    Hou, J.4    Frahm, T.5
  • 16
    • 33646148263 scopus 로고    scopus 로고
    • Quantitative methods for the analysis of protein phosphorylation in drug development
    • Olive DM (2004) Quantitative methods for the analysis of protein phosphorylation in drug development. Expert Rev Proteomics 1: 327-341.
    • (2004) Expert Rev Proteomics , vol.1 , pp. 327-341
    • Olive, D.M.1
  • 17
    • 77955794430 scopus 로고    scopus 로고
    • Multiplexed evaluation of a cell-based assay for the detection of antidrug neutralizing antibodies to panitumumab in human serum using automated fluorescent microscopy
    • Pennucci J, Swanson S, Kaliyaperumal A, Gupta S (2010) Multiplexed evaluation of a cell-based assay for the detection of antidrug neutralizing antibodies to panitumumab in human serum using automated fluorescent microscopy. J Biomol Screen 15: 644-652.
    • (2010) J Biomol Screen , vol.15 , pp. 644-652
    • Pennucci, J.1    Swanson, S.2    Kaliyaperumal, A.3    Gupta, S.4
  • 18
    • 84857748374 scopus 로고    scopus 로고
    • Domain-based biosensor assay to screen for epidermal growth factor receptor modulators in live cells
    • Antczak C, Bermingham A, Calder P, Malkov D, Song K, et al. (2012) Domain-based biosensor assay to screen for epidermal growth factor receptor modulators in live cells. Assay Drug Dev Technol 10: 24-36.
    • (2012) Assay Drug Dev Technol , vol.10 , pp. 24-36
    • Antczak, C.1    Bermingham, A.2    Calder, P.3    Malkov, D.4    Song, K.5
  • 19
    • 84859075784 scopus 로고    scopus 로고
    • VEGF-induced endothelial cell migration requires urokinase receptor (uPAR)-dependent integrin redistribution
    • Alexander RA, Prager GW, Mihaly-Bison J, Uhrin P, Sunzenauer S, et al. (2012) VEGF-induced endothelial cell migration requires urokinase receptor (uPAR)-dependent integrin redistribution. Cardiovasc Res 94: 125-135.
    • (2012) Cardiovasc Res , vol.94 , pp. 125-135
    • Alexander, R.A.1    Prager, G.W.2    Mihaly-Bison, J.3    Uhrin, P.4    Sunzenauer, S.5
  • 21
    • 57049187658 scopus 로고    scopus 로고
    • Micropatterning for quantitative analysis of protein-protein interactions in living cells
    • Schwarzenbacher M, Kaltenbrunner M, Brameshuber M, Hesch C, Paster W, et al. (2008) Micropatterning for quantitative analysis of protein-protein interactions in living cells. Nat Methods 5: 1053-1060.
    • (2008) Nat Methods , vol.5 , pp. 1053-1060
    • Schwarzenbacher, M.1    Kaltenbrunner, M.2    Brameshuber, M.3    Hesch, C.4    Paster, W.5
  • 22
    • 84883035228 scopus 로고    scopus 로고
    • Determination of binding curves via protein micropatterning in vitro and in living cells
    • Sunzenauer S, Zojer V, Brameshuber M, Trols A, Weghuber J, et al. (2013) Determination of binding curves via protein micropatterning in vitro and in living cells. Cytometry A 83: 847-854.
    • (2013) Cytometry A , vol.83 , pp. 847-854
    • Sunzenauer, S.1    Zojer, V.2    Brameshuber, M.3    Trols, A.4    Weghuber, J.5
  • 23
    • 77956061639 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in the live cell plasma membrane by quantifying prey redistribution upon bait micropatterning
    • Weghuber J, Brameshuber M, Sunzenauer S, Lehner M, Paar C, et al. (2010) Detection of protein-protein interactions in the live cell plasma membrane by quantifying prey redistribution upon bait micropatterning. Methods Enzymol 472: 133-151.
    • (2010) Methods Enzymol , vol.472 , pp. 133-151
    • Weghuber, J.1    Brameshuber, M.2    Sunzenauer, S.3    Lehner, M.4    Paar, C.5
  • 26
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
    • Lowenstein EJ, Daly RJ, Batzer AG, Li W, Margolis B, et al. (1992) The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell 70: 431-442.
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1    Daly, R.J.2    Batzer, A.G.3    Li, W.4    Margolis, B.5
  • 29
    • 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: 2005 0008.
    • (2005) Mol Syst Biol , vol.1
    • Schulze, W.X.1    Deng, L.2    Mann, M.3
  • 31
    • 84873145428 scopus 로고    scopus 로고
    • Inhibition of triple-negative breast cancer models by combinations of antibodies to EGFR
    • Ferraro DA, Gaborit N, Maron R, Cohen-Dvashi H, Porat Z, et al. (2013) Inhibition of triple-negative breast cancer models by combinations of antibodies to EGFR. Proc Natl Acad Sci U S A 110: 1815-1820.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1815-1820
    • Ferraro, D.A.1    Gaborit, N.2    Maron, R.3    Cohen-Dvashi, H.4    Porat, Z.5
  • 32
    • 12344271123 scopus 로고    scopus 로고
    • Additive interaction of gefitinib ('Iressa', ZD1839) and ionising radiation in human tumour cells in vitro
    • DOI 10.1038/sj.bjc.6602242
    • Giocanti N, Hennequin C, Rouillard D, Defrance R, Favaudon V (2004) Additive interaction of gefitinib ('Iressa', ZD1839) and ionising radiation in human tumour cells in vitro. Br J Cancer 91: 2026-2033. (Pubitemid 40128769)
    • (2004) British Journal of Cancer , vol.91 , Issue.12 , pp. 2026-2033
    • Giocanti, N.1    Hennequin, C.2    Rouillard, D.3    Defrance, R.4    Favaudon, V.5
  • 33
    • 84455174523 scopus 로고    scopus 로고
    • Epidermal growth factor-stimulated human cervical cancer cell growth is associated with EGFR and cyclin D1 activation, independent of COX-2 expression levels
    • Narayanan R, Kim HN, Narayanan NK, Nargi D, Narayanan B (2012) Epidermal growth factor-stimulated human cervical cancer cell growth is associated with EGFR and cyclin D1 activation, independent of COX-2 expression levels. Int J Oncol 40: 13-20.
    • (2012) Int J Oncol , vol.40 , pp. 13-20
    • Narayanan, R.1    Kim, H.N.2    Narayanan, N.K.3    Nargi, D.4    Narayanan, B.5
  • 34
    • 77953167957 scopus 로고    scopus 로고
    • Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor
    • Goh LK, Huang F, Kim W, Gygi S, Sorkin A (2010) Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor. J Cell Biol 189: 871-883.
    • (2010) J Cell Biol , vol.189 , pp. 871-883
    • Goh, L.K.1    Huang, F.2    Kim, W.3    Gygi, S.4    Sorkin, A.5
  • 35
    • 48549088895 scopus 로고    scopus 로고
    • Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • Sigismund S, Argenzio E, Tosoni D, Cavallaro E, Polo S, et al. (2008) Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Dev Cell 15: 209-219.
    • (2008) Dev Cell , vol.15 , pp. 209-219
    • Sigismund, S.1    Argenzio, E.2    Tosoni, D.3    Cavallaro, E.4    Polo, S.5
  • 36
    • 62649159446 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • Sorkin A, Goh LK (2009) Endocytosis and intracellular trafficking of ErbBs. Exp Cell Res 315: 683-696.
    • (2009) Exp Cell Res , vol.315 , pp. 683-696
    • Sorkin, A.1    Goh, L.K.2
  • 37
    • 0037339887 scopus 로고    scopus 로고
    • Grb2 regulates internalization of EGF receptors through clathrin-coated pits
    • DOI 10.1091/mbc.E02-08-0532
    • Jiang X, Huang F, Marusyk A, Sorkin A (2003) Grb2 regulates internalization of EGF receptors through clathrin-coated pits. Mol Biol Cell 14: 858-870. (Pubitemid 36337438)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.3 , pp. 858-870
    • Jiang, X.1    Huang, F.2    Marusyk, A.3    Sorkin, A.4
  • 38
    • 33645741605 scopus 로고    scopus 로고
    • A novel endocytic mechanism of epidermal growth factor receptor sequestration and internalization
    • Orth JD, Krueger EW, Weller SG, McNiven MA (2006) A novel endocytic mechanism of epidermal growth factor receptor sequestration and internalization. Cancer Res 66: 3603-3610.
    • (2006) Cancer Res , vol.66 , pp. 3603-3610
    • Orth, J.D.1    Krueger, E.W.2    Weller, S.G.3    McNiven, M.A.4
  • 39
    • 0037178805 scopus 로고    scopus 로고
    • Effect of tyrosine kinase inhibitors on clathrin-coated pit recruitment and internalization of epidermal growth factor receptor
    • DOI 10.1074/jbc.M201595200
    • Sorkina T, Huang F, Beguinot L, Sorkin A (2002) Effect of tyrosine kinase inhibitors on clathrin-coated pit recruitment and internalization of epidermal growth factor receptor. J Biol Chem 277: 27433-27441. (Pubitemid 34951764)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27433-27441
    • Sorkina, T.1    Huang, F.2    Beguinot, L.3    Sorkin, A.4
  • 40
    • 0028955388 scopus 로고
    • Epidermal growth factor-related peptides and their receptors in human malignancies
    • Salomon DS, Brandt R, Ciardiello F, Normanno N (1995) Epidermal growth factor-related peptides and their receptors in human malignancies. Crit Rev Oncol Hematol 19: 183-232.
    • (1995) Crit Rev Oncol Hematol , vol.19 , pp. 183-232
    • Salomon, D.S.1    Brandt, R.2    Ciardiello, F.3    Normanno, N.4
  • 41
    • 0036362221 scopus 로고    scopus 로고
    • Epidermal growth factor receptor dependence in human tumors: More than just expression?
    • Arteaga CL (2002) Epidermal growth factor receptor dependence in human tumors: more than just expression? Oncologist 7 Suppl 4: 31-39.
    • (2002) Oncologist , vol.7 , Issue.SUPPL. 4 , pp. 31-39
    • Arteaga, C.L.1
  • 42
    • 0028040812 scopus 로고
    • Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor
    • Batzer AG, Rotin D, Urena JM, Skolnik EY, Schlessinger J (1994) Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Mol Cell Biol 14: 5192-5201.
    • (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
  • 43
    • 84877977567 scopus 로고    scopus 로고
    • Microplate-compatible total internal reflection fluorescence microscopy for receptor pharmacology
    • Chen M, Zaytseva NV, Wu Q, Li M, Fang Y (2013) Microplate-compatible total internal reflection fluorescence microscopy for receptor pharmacology. Applied Physics Letters 102.
    • (2013) Applied Physics Letters , pp. 102
    • Chen, M.1    Zaytseva, N.V.2    Wu, Q.3    Li, M.4    Fang, Y.5
  • 44
    • 84899052980 scopus 로고    scopus 로고
    • Live cell fluorescence imaging reveals high stoichiometry of Grb2 binding to the EGF receptor sustained during endocytosis
    • Fortian A, Sorkin A (2013) Live cell fluorescence imaging reveals high stoichiometry of Grb2 binding to the EGF receptor sustained during endocytosis. J Cell Sci.
    • (2013) J Cell Sci
    • Fortian, A.1    Sorkin, A.2
  • 45
    • 84865560488 scopus 로고    scopus 로고
    • Fast rebinding increases dwell time of Src homology 2 (SH2)-containing proteins near the plasma membrane
    • Oh D, Ogiue-Ikeda M, Jadwin JA, Machida K, Mayer BJ, et al. (2012) Fast rebinding increases dwell time of Src homology 2 (SH2)-containing proteins near the plasma membrane. Proc Natl Acad Sci U S A 109: 14024-14029.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 14024-14029
    • Oh, D.1    Ogiue-Ikeda, M.2    Jadwin, J.A.3    Machida, K.4    Mayer, B.J.5
  • 47
    • 84887567274 scopus 로고    scopus 로고
    • EGFR endocytosis requires its kinase activity and N-terminal transmembrane dimerization motif
    • Heukers R, Vermeulen JF, Fereidouni F, Bader AN, Voortman J, et al. (2013) EGFR endocytosis requires its kinase activity and N-terminal transmembrane dimerization motif. J Cell Sci.
    • (2013) J Cell Sci
    • Heukers, R.1    Vermeulen, J.F.2    Fereidouni, F.3    Bader, A.N.4    Voortman, J.5


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