메뉴 건너뛰기




Volumn 6, Issue 4, 2014, Pages

Structure-function relationships of ErbB RTKs in the plasma membrane of living cells

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

EID: 84908657323     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a008961     Document Type: Article
Times cited : (14)

References (83)
  • 1
    • 79953203628 scopus 로고    scopus 로고
    • The effect of cell-ECM adhesion on signalling via the ErbB family of growth factor receptors.
    • Alexi X, Berditchevski F, Odintsova E. 2011. The effect of cell-ECM adhesion on signalling via the ErbB family of growth factor receptors. Biochem Soc Trans 39: 568–573.
    • (2011) Biochem Soc Trans , vol.39 , pp. 568-573
    • Alexi, X.1    Berditchevski, F.2    Odintsova, E.3
  • 4
    • 3042800393 scopus 로고    scopus 로고
    • ErbB3/ HER3 does not homodimerize upon neuregulin binding at the cell surface.
    • Berger MB, Mendrola JM, Lemmon MA. 2004. ErbB3/ HER3 does not homodimerize upon neuregulin binding at the cell surface. FEBS Lett 569: 332–336.
    • (2004) FEBS Lett , vol.569 , pp. 332-336
    • Berger, M.B.1    Mendrola, J.M.2    Lemmon, M.A.3
  • 6
    • 4544302236 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-dependent regulation of integrin-mediated signaling and cell cycle entry in epithelial cells.
    • Bill HM, KnudsenB,Moores SL, Muthuswamy SK, Rao VR, Brugge JS, Miranti CK. 2004. Epidermal growth factor receptor-dependent regulation of integrin-mediated signaling and cell cycle entry in epithelial cells. Mol Cell Biol 24: 8586–8599.
    • (2004) Mol Cell Biol , vol.24 , pp. 8586-8599
    • Bill, H.M.1    Knudsen, B.2    Moores, S.L.3    Muthuswamy, S.K.4    Rao, V.R.5    Brugge, J.S.6    Miranti, C.K.7
  • 7
    • 0348134923 scopus 로고    scopus 로고
    • Quantitative image analysis of cellular protein translocation induced by magnetic mi-crospheres: Application to the EGF receptor.
    • Brock R, Jovin TM. 2003. Quantitative image analysis of cellular protein translocation induced by magnetic mi-crospheres: Application to the EGF receptor. Cytometry 52A: 1–11.
    • (2003) Cytometry , vol.52A , pp. 1-11
    • Brock, R.1    Jovin, T.M.2
  • 8
    • 0033119241 scopus 로고    scopus 로고
    • Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor.
    • Brock R, Hamelers IHL, Jovin TM. 1999. Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor. Cytometry 35: 353–362.
    • (1999) Cytometry , vol.35 , pp. 353-362
    • Brock, R.1    Hamelers, I.H.L.2    Jovin, T.M.3
  • 10
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells.
    • Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I. 2010. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464: 783–787.
    • (2010) Nature , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 11
    • 0037429779 scopus 로고    scopus 로고
    • The deaf and the dumb: The biology of ErbB-2 and ErbB-3.
    • Citri A, Skaria KB, Yarden Y. 2003. The deaf and the dumb: The biology of ErbB-2 and ErbB-3. Exp Cell Res 284: 54– 65.
    • (2003) Exp Cell Res , vol.284 , pp. 54-65
    • Citri, A.1    Skaria, K.B.2    Yarden, Y.3
  • 13
    • 44049105523 scopus 로고    scopus 로고
    • Mapping the number of molecules and brightness in the laser scanning microscope.
    • Digman MA, Dalal R, Horwitz AF, Gratton E. 2008. Mapping the number of molecules and brightness in the laser scanning microscope. Biophys J 94: 2320–2332.
    • (2008) Biophys J , vol.94 , pp. 2320-2332
    • Digman, M.A.1    Dalal, R.2    Horwitz, A.F.3    Gratton, E.4
  • 15
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimeriza-tion.
    • Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ, Lemmon MA. 2003. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimeriza-tion. 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    Lemmon, M.A.6
  • 16
    • 26444452209 scopus 로고    scopus 로고
    • Signal transduction of erbB receptors in trastuzumab (Herceptin) sensitive and resistant cell lines: Local stimulation using magnetic microspheres as assessed by quantitative digital microscopy.
    • Friedländer E, Nagy P, Arndt-Jovin DJ, Jovin TM, Szöllösi J, Vereb G. 2005. Signal transduction of erbB receptors in trastuzumab (Herceptin) sensitive and resistant cell lines: Local stimulation using magnetic microspheres as assessed by quantitative digital microscopy. Cytometry 67A: 161–171.
    • (2005) Cytometry , vol.67A , pp. 161-171
    • Friedländer, E.1    Nagy, P.2    Arndt-Jovin, D.J.3    Jovin, T.M.4    Szöllösi, J.5    Vereb, G.6
  • 17
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy: A ster-eochemical model for tyrosine kinase receptor activation.
    • Gadella TWJ Jr, Jovin TM. 1995. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy: A ster-eochemical model for tyrosine kinase receptor activation. J Cell Biol 129: 1543–1558.
    • (1995) J Cell Biol , vol.129 , pp. 1543-1558
    • Gadella, T.W.J.1    Jovin, T.M.2
  • 18
    • 0025688139 scopus 로고
    • Tyrosine phosphorylation in T cells is regulated by phosphatase activity: Studies with phenylarsine oxide.
    • Garcia-Morales P, Minami Y, Luong E, Klausner RD, Samel-son LE. 1990. Tyrosine phosphorylation in T cells is regulated by phosphatase activity: Studies with phenylarsine oxide. Proc Natl Acad Sci 87: 9255–9259.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 9255-9259
    • Garcia-Morales, P.1    Minami, Y.2    Luong, E.3    Klausner, R.D.4    Samelson, L.E.5
  • 21
    • 84924534058 scopus 로고    scopus 로고
    • TA new method for protein labeling with small molecules based on acyl carrier protein
    • George N. 2006. A new method for protein labeling with small molecules based on acyl carrier protein. Chemistry and chemical genetics, 149 pp. PhD thesis, École Polytechnique Fédérale de Lausanne, Lausanne.
    • (2006) Chemistry and chemical genetics , pp. 149
    • George, N.1
  • 22
    • 15744372318 scopus 로고    scopus 로고
    • Hyaluronan constitutive-ly regulates ErbB2 phosphorylation and signaling complex formation in carcinoma cells.
    • Ghatak S, Misra S, Toole BP. 2005. Hyaluronan constitutive-ly regulates ErbB2 phosphorylation and signaling complex formation in carcinoma cells. J Biol Chem 280: 8875–8883.
    • (2005) J Biol Chem , vol.280 , pp. 8875-8883
    • Ghatak, S.1    Misra, S.2    Toole, B.P.3
  • 25
    • 0042307325 scopus 로고    scopus 로고
    • The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation.
    • Holbro T, Beerli RR, Maurer F, Koziczak M, Barbas CF, Hynes NE. 2003. The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation. Proc Natl Acad Sci 100: 8933–8938.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 8933-8938
    • Holbro, T.1    Beerli, R.R.2    Maurer, F.3    Koziczak, M.4    Barbas, C.F.5    Hynes, N.E.6
  • 26
    • 84899749070 scopus 로고    scopus 로고
    • The genesis of tyrosine phosphorylation.
    • Hunter T. 2014. The genesis of tyrosine phosphorylation. Cold Spring Harb Perspect Biol doi: 10.1101/cshper-spect.a020644.
    • (2014) Cold Spring Harb Perspect Biol
    • Hunter, T.1
  • 27
    • 77957765881 scopus 로고    scopus 로고
    • Direct binding of the EGF-like domain of neuregulin-1 to integrins (avb3 and a6b4) is involved in neuregulin-1/ErbB signaling.
    • Ieguchi K, Fujita M, Ma Z, Davari P, Taniguchi Y, Sekiguchi K, Wang BZ, Takada YK, Takada Y. 2010. Direct binding of the EGF-like domain of neuregulin-1 to integrins (avb3 and a6b4) is involved in neuregulin-1/ErbB signaling. J Biol Chem 285: 31388–31398.
    • (2010) J Biol Chem , vol.285 , pp. 31388-31398
    • Ieguchi, K.1    Fujita, M.2    Ma, Z.3    Davari, P.4    Taniguchi, Y.5    Sekiguchi, K.6    Wang, B.Z.7    Takada, Y.K.8    Takada, Y.9
  • 33
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor.
    • Lee S-R, Kwon K-S, Kim S-R, Rhee SG. 1998. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J Biol Chem 273: 15366–15372.
    • (1998) J Biol Chem , vol.273 , pp. 15366-15372
    • Lee, S.-R.1    Kwon, K.-S.2    Kim, S.-R.3    Rhee, S.G.4
  • 37
    • 23944486487 scopus 로고    scopus 로고
    • Reaching out for signals: Filopodia sense EGF and respond by directed retrograde transport of activated receptors.
    • Lidke DS, Lidke KA, Rieger B, Jovin TM, Arndt-Jovin DJ. 2005. Reaching out for signals: Filopodia sense EGF and respond by directed retrograde transport of activated receptors. J Cell Biol 170: 619–626.
    • (2005) J Cell Biol , vol.170 , pp. 619-626
    • Lidke, D.S.1    Lidke, K.A.2    Rieger, B.3    Jovin, T.M.4    Arndt-Jovin, D.J.5
  • 39
    • 84868323253 scopus 로고    scopus 로고
    • Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor.
    • Lu C, Mi LZ, Schurpf T, Walz T, Springer TA. 2012. Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor. J Biol Chem 287: 38244– 38253.
    • (2012) J Biol Chem , vol.287 , pp. 38244-38253
    • Lu, C.1    Mi, L.Z.2    Schurpf, T.3    Walz, T.4    Springer, T.A.5
  • 40
    • 0036225144 scopus 로고    scopus 로고
    • Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling.
    • Martin-Fernandez M, Clarke DT, Tobin MJ, Jones SV, Jones GR. 2002. Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling. Biophys J 82: 2415–2427.
    • (2002) Biophys J , vol.82 , pp. 2415-2427
    • Martin-Fernandez, M.1    Clarke, D.T.2    Tobin, M.J.3    Jones, S.V.4    Jones, G.R.5
  • 42
    • 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. 2001. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J Mol Biol 311: 1011–1026.
    • (2001) J Mol Biol , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 44
    • 0033014064 scopus 로고    scopus 로고
    • Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy.
    • Nagy P, Jenei A, Kirsch AK, Szollosi J, Damjanovich S, Jovin TM. 1999. Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J Cell Sci 112: 1733–1741.
    • (1999) J Cell Sci , vol.112 , pp. 1733-1741
    • Nagy, P.1    Jenei, A.2    Kirsch, A.K.3    Szollosi, J.4    Damjanovich, S.5    Jovin, T.M.6
  • 46
    • 12544250996 scopus 로고    scopus 로고
    • Decreased accessibility and lack of activation of erbB2 in JIMT-1, a Herceptin-resistant, MUC-4-expressing breast cancer cell line.
    • Nagy P, Friedländer E, Tanner M, Kapanen AI, Carraway KL, Isola J, Jovin TM. 2005. Decreased accessibility and lack of activation of erbB2 in JIMT-1, a Herceptin-resistant, MUC-4-expressing breast cancer cell line. Cancer Res 65: 473–482.
    • (2005) Cancer Res , vol.65 , pp. 473-482
    • Nagy, P.1    Friedländer, E.2    Tanner, M.3    Kapanen, A.I.4    Carraway, K.L.5    Isola, J.6    Jovin, T.M.7
  • 47
    • 78049239930 scopus 로고    scopus 로고
    • Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis.
    • Nagy P, Claus J, Jovin TM, Arndt-Jovin DJ. 2010. Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis. Proc Natl Acad Sci 107: 16524– 16529.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 16524-16529
    • Nagy, P.1    Claus, J.2    Jovin, T.M.3    Arndt-Jovin, D.J.4
  • 48
    • 37249006253 scopus 로고    scopus 로고
    • Prolonged EGFR signaling by ERBB2-mediated sequestration at the plasma membrane.
    • OffterdingerM, Bastiaens PI. 2008. Prolonged EGFR signaling by ERBB2-mediated sequestration at the plasma membrane. Traffic 9: 147–155.
    • (2008) Traffic , vol.9 , pp. 147-155
    • Offterdinger, M.1    Bastiaens, P.I.2
  • 49
    • 4344560633 scopus 로고    scopus 로고
    • Imaging phosphorylation dynamics of the epidermal growth factor receptor.
    • Offterdinger M, Georget V, Girod A, Bastiaens PI. 2004. Imaging phosphorylation dynamics of the epidermal growth factor receptor. J Biol Chem 279: 36972–36981.
    • (2004) J Biol Chem , vol.279 , pp. 36972-36981
    • Offterdinger, M.1    Georget, V.2    Girod, A.3    Bastiaens, P.I.4
  • 51
    • 33645821892 scopus 로고    scopus 로고
    • On the nature of low- and high-affinity EGF receptors on living
    • Ozcan F, Klein P, Lemmon MA, Lax I, Schlessinger J. 2006. On the nature of low- and high-affinity EGF receptors on living cells. 103: 5735–5740.
    • (2006) cells. , vol.103 , pp. 5735-5740
    • Ozcan, F.1    Klein, P.2    Lemmon, M.A.3    Lax, I.4    Schlessinger, J.5
  • 52
    • 56249134876 scopus 로고    scopus 로고
    • Higher-order association states of cellular ERBB3 probed with photo-cross-linkable aptamers.
    • Park E, Baron R, Landgraf R. 2008. Higher-order association states of cellular ERBB3 probed with photo-cross-linkable aptamers. Biochemistry 47: 11992–12005.
    • (2008) Biochemistry , vol.47 , pp. 11992-12005
    • Park, E.1    Baron, R.2    Landgraf, R.3
  • 54
    • 0038732770 scopus 로고    scopus 로고
    • EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation.
    • Reynolds AR, Tischer C, Verveer PJ, Rocks O, Bastiaens PI. 2003. EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation. Nat Cell Biol 5: 447–453.
    • (2003) Nat Cell Biol , vol.5 , pp. 447-453
    • Reynolds, A.R.1    Tischer, C.2    Verveer, P.J.3    Rocks, O.4    Bastiaens, P.I.5
  • 55
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation.
    • Rhee SG, Bae YS, Lee SR, Kwon J. 2000. Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation. Sci STKE 2000: e1.
    • (2000) Sci STKE , vol.2000 , pp. e1
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 56
    • 0034869825 scopus 로고    scopus 로고
    • The basic biology of HER2.
    • Rubin I, Yarden Y. 2001. The basic biology of HER2. Ann Oncol 12: 3–8.
    • (2001) Ann Oncol , vol.12 , pp. 3-8
    • Rubin, I.1    Yarden, Y.2
  • 57
    • 34447313361 scopus 로고    scopus 로고
    • Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis.
    • Saffarian S, Li Y, Elson EL, Pike LJ. 2007. Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis. Biophys J 93: 1021–1031.
    • (2007) Biophys J , vol.93 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pike, L.J.4
  • 58
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells.
    • Sako Y, Minoghchi S, Yanagida T. 2000. Single-molecule imaging of EGFR signalling on the surface of living cells. Nat Cell Biol 2: 168–172.
    • (2000) Nat Cell Biol , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 59
    • 0347623195 scopus 로고    scopus 로고
    • Imaging filopodia dynamics in the mouse blastocyst.
    • Salas-Vidal E, Lomeli H. 2004. Imaging filopodia dynamics in the mouse blastocyst. Dev Biol 265: 75–89.
    • (2004) Dev Biol , vol.265 , pp. 75-89
    • Salas-Vidal, E.1    Lomeli, H.2
  • 60
    • 84875477894 scopus 로고    scopus 로고
    • Inhibitors of PI(4,5)P2 synthesis reveal dynamic regulation of IgE receptor signaling by phosphoinositides in RBL mast cells.
    • Santos Mde S, Naal RM, Baird B, Holowka D. 2013. Inhibitors of PI(4,5)P2 synthesis reveal dynamic regulation of IgE receptor signaling by phosphoinositides in RBL mast cells. Mol Pharmacol 83: 793–804.
    • (2013) Mol Pharmacol , vol.83 , pp. 793-804
    • Santos Mde, S.1    Naal, R.M.2    Baird, B.3    Holowka, D.4
  • 61
    • 62649134382 scopus 로고    scopus 로고
    • Interaction of antibodies with ErbB receptor extracellular regions.
    • Schmitz KR, Ferguson KM. 2009. Interaction of antibodies with ErbB receptor extracellular regions. Exp Cell Res 315: 659–670.
    • (2009) Exp Cell Res , vol.315 , pp. 659-670
    • Schmitz, K.R.1    Ferguson, K.M.2
  • 62
    • 84885028426 scopus 로고    scopus 로고
    • VEGFR and type-V RTK activation and signaling.
    • Shibuya M. 2013. VEGFR and type-V RTK activation and signaling. Cold Spring Harb Perspect Biol doi: 10.1101/ cshperspect.a009092.
    • (2013) Cold Spring Harb Perspect Biol
    • Shibuya, M.1
  • 65
    • 84877122657 scopus 로고    scopus 로고
    • Computational study of EGFR inhibition: Molecular dynamics studies on the active and inactive protein conformations.
    • Songtawee N, Gleeson MP, Choowongkomon K. 2013. Computational study of EGFR inhibition: Molecular dynamics studies on the active and inactive protein conformations. J Mol Model 19: 497–509.
    • (2013) J Mol Model , vol.19 , pp. 497-509
    • Songtawee, N.1    Gleeson, M.P.2    Choowongkomon, K.3
  • 66
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor.
    • Stamos J, Sliwkowski MX, Eigenbrot C. 2002. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J Biol Chem 277: 46265–46272.
    • (2002) J Biol Chem , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 67
    • 50349083489 scopus 로고    scopus 로고
    • Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements.
    • SzabóA, Horváth G, SzöllŐsi J, Nagy P. 2008. Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements. Biophys J 95: 2086–2096.
    • (2008) Biophys J , vol.95 , pp. 2086-2096
    • Szabó, A.1    Horváth, G.2    SzöllŐsi, J.3    Nagy, P.4
  • 70
    • 0037375256 scopus 로고    scopus 로고
    • PC12 cell activation by epidermal growth factor receptor: Role of autophosphorylation sites.
    • Tyson DR, Larkin S, Hamai Y, Bradshaw RA. 2003. PC12 cell activation by epidermal growth factor receptor: Role of autophosphorylation sites. Int J Dev Neurosci 21: 63–74.
    • (2003) Int J Dev Neurosci , vol.21 , pp. 63-74
    • Tyson, D.R.1    Larkin, S.2    Hamai, Y.3    Bradshaw, R.A.4
  • 71
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane.
    • Verveer PJ, Wouters FS, Reynolds AR, Bastiaens PI. 2000. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science 290: 1567–1570.
    • (2000) Science , vol.290 , pp. 1567-1570
    • Verveer, P.J.1    Wouters, F.S.2    Reynolds, A.R.3    Bastiaens, P.I.4
  • 74
    • 0032948524 scopus 로고    scopus 로고
    • Endocytosis deficiency of epidermal growth factor (EGF) receptor-ErbB2 heterodimers in response to EGF stimulation.
    • Wang Z, Zhang L, Yeung TK, Chen X. 1999. Endocytosis deficiency of epidermal growth factor (EGF) receptor-ErbB2 heterodimers in response to EGF stimulation. Mol Biol Cell 10: 1621–1636.
    • (1999) Mol Biol Cell , vol.10 , pp. 1621-1636
    • Wang, Z.1    Zhang, L.2    Yeung, T.K.3    Chen, X.4
  • 75
    • 80052059401 scopus 로고    scopus 로고
    • Illuminating epidermal growth factor receptor densities on filopodia through plasmon coupling.
    • Wang J, Boriskina SV, Wang H, Reinhard BM. 2011. Illuminating epidermal growth factor receptor densities on filopodia through plasmon coupling. ACS Nano 5: 6619– 6628.
    • (2011) ACS Nano , vol.5 , pp. 6619-6628
    • Wang, J.1    Boriskina, S.V.2    Wang, H.3    Reinhard, B.M.4
  • 77
    • 0023156382 scopus 로고
    • Self-phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation.
    • Yarden Y, Schlessinger J. 1987. Self-phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation. Biochemistry 26: 1434–1442.
    • (1987) Biochemistry , vol.26 , pp. 1434-1442
    • Yarden, Y.1    Schlessinger, J.2
  • 78
    • 34250670453 scopus 로고    scopus 로고
    • Site-specific protein labeling by Sfp phosphopantetheinyl transferase.
    • Yin J, Lin A, Golan D, Walsh C. 2006. Site-specific protein labeling by Sfp phosphopantetheinyl transferase. Nat Protoc 1: 280–285.
    • (2006) Nat Protoc , vol.1 , pp. 280-285
    • Yin, J.1    Lin, A.2    Golan, D.3    Walsh, C.4
  • 79
    • 34447641458 scopus 로고    scopus 로고
    • Epidermal growth factor receptor tyrosine kinase is modulated by GM3 interaction with N-linked GlcNAc termini of the receptor.
    • Yoon SJ, Nakayama K, Hikita T, Handa K, Hakomori SI. 2006. Epidermal growth factor receptor tyrosine kinase is modulated by GM3 interaction with N-linked GlcNAc termini of the receptor. Proc Natl Acad Sci 103: 18987– 18991.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 18987-18991
    • Yoon, S.J.1    Nakayama, K.2    Hikita, T.3    Handa, K.4    Hakomori, S.I.5
  • 80
    • 0033947684 scopus 로고    scopus 로고
    • Integrin a2b1-depen-dent EGF receptor activation at cell-cell contact sites.
    • Yu X, Miyamoto S, Mekada E. 2000. Integrin a2b1-depen-dent EGF receptor activation at cell-cell contact sites. J Cell Sci 113: 2139–2147.
    • (2000) J Cell Sci , vol.113 , pp. 2139-2147
    • Yu, X.1    Miyamoto, S.2    Mekada, E.3
  • 81
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells.
    • Zacharias DA, Violin JD, Newton AC, Tsien RY. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296: 913–916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 83
    • 84883049567 scopus 로고    scopus 로고
    • Dynamic conformational transitions of the EGF receptor in living mammalian cells determined by FRETand fluorescence lifetime imaging microscopy.
    • Ziomkiewicz I, Loman A, Klement R, Fritsch C, Klym-chenko A, Bunt G, Jovin TM, Arndt-Jovin DJ. 2013. Dynamic conformational transitions of the EGF receptor in living mammalian cells determined by FRETand fluorescence lifetime imaging microscopy. Cytometry A 83A: 794–805.
    • (2013) Cytometry A , vol.83A , pp. 794-805
    • Ziomkiewicz, I.1    Loman, A.2    Klement, R.3    Fritsch, C.4    Klymchenko, A.5    Bunt, G.6    Jovin, T.M.7    Arndt-Jovin, D.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.