메뉴 건너뛰기




Volumn 26, Issue 22, 2015, Pages 4087-4099

Enhanced dimerization drives ligand-independent activity of mutant epidermal growth factor receptor in lung cancer

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; LIGAND; PHOSPHOTRANSFERASE; QUANTUM DOT; EGFR PROTEIN, HUMAN; EPIDERMAL GROWTH FACTOR DERIVATIVE; PROTEIN AGGREGATE; PROTEIN KINASE INHIBITOR;

EID: 84946771788     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E15-05-0269     Document Type: Article
Times cited : (70)

References (89)
  • 2
    • 77955627615 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity in growth factor binding to an EGF receptor
    • Alvarado D, Klein DE, Lemmon MA (2010). Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell 142, 568-579.
    • (2010) Cell , vol.142 , pp. 568-579
    • Alvarado, D.1    Klein, D.E.2    Ma, L.3
  • 4
    • 84855428923 scopus 로고    scopus 로고
    • Finding the missing links in EGFR
    • Bessman NJ, Lemmon MA (2012). Finding the missing links in EGFR. Nat Struct Mol Biol 19, 1-3.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 1-3
    • Bessman, N.J.1    Ma, L.2
  • 5
    • 0030697807 scopus 로고    scopus 로고
    • PD153035, a tyrosine kinase inhibitor, prevents epidermal growth factor receptor activation and inhibits growth of cancer cells in a receptor number-dependent manner
    • Bos M, Mendelsohn J, Kim YM, Albanell J, Fry DW, Baselga J (1997). PD153035, a tyrosine kinase inhibitor, prevents epidermal growth factor receptor activation and inhibits growth of cancer cells in a receptor number-dependent manner. Clin Cancer Res 3, 2099-2106.
    • (1997) Clin Cancer Res , vol.3 , pp. 2099-2106
    • Bos, M.1    Mendelsohn, J.2    Kim, Y.M.3    Albanell, J.4    Fry, D.W.5    Baselga, J.6
  • 6
    • 0023025941 scopus 로고
    • Ganglioside-mediated modulation of cell growth. Specifc effects of GM3 on tyrosine phos-phorylation of the epidermal growth factor receptor
    • Bremer EG, Schlessinger J, Hakomori S (1986). Ganglioside-mediated modulation of cell growth. Specifc effects of GM3 on tyrosine phos-phorylation of the epidermal growth factor receptor. J Biol Chem 261, 2434-2440.
    • (1986) J Biol Chem , vol.261 , pp. 2434-2440
    • Bremer, E.G.1    Schlessinger, J.2    Hakomori, S.3
  • 8
    • 33748066632 scopus 로고    scopus 로고
    • Kinetic analysis of epidermal growth factor receptor somatic mutant proteins shows increased sensitivity to the epidermal growth factor receptor tyrosine kinase inhibitor, Erlotinib
    • Carey KD, Garton AJ, Romero MS, Kahler J, Thomson S, Ross S, Park F, Haley JD, Gibson N, Sliwkowski MX (2006). Kinetic analysis of epidermal growth factor receptor somatic mutant proteins shows increased sensitivity to the epidermal growth factor receptor tyrosine kinase inhibitor, Erlotinib. Cancer Res 66, 8163-8171.
    • (2006) Cancer Res , vol.66 , pp. 8163-8171
    • Carey, K.D.1    Garton, A.J.2    Romero, M.S.3    Kahler, J.4    Thomson, S.5    Ross, S.6    Park, F.7    Haley, J.D.8    Gibson, N.9    Sliwkowski, M.X.10
  • 9
    • 0024309393 scopus 로고
    • Visualization of epidermal growth factor (EGF) receptor aggregation in plasma membranes by fuo-rescence resonance energy transfer. Correlation of receptor activation with aggregation
    • Carraway KL, Koland JG, Cerione RA (1989). Visualization of epidermal growth factor (EGF) receptor aggregation in plasma membranes by fuo-rescence resonance energy transfer. Correlation of receptor activation with aggregation. J Biol Chem 264, 8699-8707.
    • (1989) J Biol Chem , vol.264 , pp. 8699-8707
    • Carraway, K.L.1    Koland, J.G.2    Cerione, R.A.3
  • 11
    • 33947170007 scopus 로고    scopus 로고
    • EGF-independent activation of cell-surface EGF receptors harboring mutations found in Geftinib-sensitive lung cancer
    • Choi SH, Mendrola JM, Lemmon MA (2007). EGF-independent activation of cell-surface EGF receptors harboring mutations found in Geftinib-sensitive lung cancer. Oncogene 26, 1567-1576.
    • (2007) Oncogene , vol.26 , pp. 1567-1576
    • Choi, S.H.1    Mendrola, J.M.2    Ma, L.3
  • 12
    • 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
  • 13
    • 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 AHA, Walker F, Orchard SG, Henderson C, Fuchs D, Rothacker J, Nice EC, Burgess AW (2005). Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-a multidimensional microscopy analysis. J Biol Chem 280, 30392-30399.
    • (2005) J Biol Chem , vol.280 , pp. 30392-30399
    • Aha, C.1    Walker, F.2    Orchard, S.G.3    Henderson, C.4    Fuchs, D.5    Rothacker, J.6    Nice, E.C.7    Burgess, A.W.8
  • 15
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • Dahan M, Lévi S, Luccardini C, Rostaing P, Riveau B, Triller A (2003). Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 302, 442-445.
    • (2003) Science , vol.302 , pp. 442-445
    • Dahan, M.1    Lévi, S.2    Luccardini, C.3    Rostaing, P.4    Riveau, B.5    Triller, A.6
  • 16
    • 23844471971 scopus 로고    scopus 로고
    • Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface
    • Dawson J P, Berger MB, Lin C, Schlessinger J, Lemmon MA, Ferguson KM (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.3    Schlessinger, J.4    Lemmon, M.A.5    Ferguson, K.M.6
  • 17
    • 46249095691 scopus 로고    scopus 로고
    • A spatially restricted increase in receptor mobility is involved in directional sensing during Dictyostelium discoideum chemotaxis
    • De Keijzer S, Sergé A, van Hemert F, Lommerse PHM, Lamers GEM, Spaink H P, Schmidt T, Snaar-Jagalska BE (2008). A spatially restricted increase in receptor mobility is involved in directional sensing during Dictyostelium discoideum chemotaxis. J Cell Sci 121, 1750-1757.
    • (2008) J Cell Sci , vol.121 , pp. 1750-1757
    • De Keijzer, S.1    Sergé, A.2    Van Hemert, F.3    Phm, L.4    Gem, L.5    Spaink, H.P.6    Schmidt, T.7    Snaar-Jagalska, B.E.8
  • 18
    • 82355191588 scopus 로고    scopus 로고
    • Evaluation of fuorophores for optimal performance in localization-based super-resolution imaging
    • Dempsey GT, Vaughan JC, Chen KH, Bates M, Zhuang X (2011). Evaluation of fuorophores for optimal performance in localization-based super-resolution imaging. Nat Methods 8, 1027-1036.
    • (2011) Nat Methods , vol.8 , pp. 1027-1036
    • Dempsey, G.T.1    Vaughan, J.C.2    Chen, K.H.3    Bates, M.4    Zhuang, X.5
  • 20
    • 0015600423 scopus 로고
    • The Viterbi algorithm
    • Forney GD (1973). The Viterbi algorithm. Proc IEEE 61, 268-278.
    • (1973) Proc IEEE , vol.61 , pp. 268-278
    • Forney, G.D.1
  • 21
    • 67349137902 scopus 로고    scopus 로고
    • The EGFRvIII variant in glioblastoma multiforme
    • Gan HK, Kaye AH, Luwor RB (2009). The EGFRvIII variant in glioblastoma multiforme. J Clin Neurosci 16, 748-754.
    • (2009) J Clin Neurosci , vol.16 , pp. 748-754
    • Gan, H.K.1    Kaye, A.H.2    Luwor, R.B.3
  • 27
    • 0037374022 scopus 로고    scopus 로고
    • Coregulation of epidermal growth factor receptor/human epidermal growth factor receptor 2 (HER2) levels and locations: Quantitative analysis of HER2 overexpression effects
    • Hendriks BS, Opresko LK, Wiley HS, Lauffenburger D (2003). Coregulation of epidermal growth factor receptor/human epidermal growth factor receptor 2 (HER2) levels and locations: quantitative analysis of HER2 overexpression effects. Cancer Res 63, 1130-1137.
    • (2003) Cancer Res , vol.63 , pp. 1130-1137
    • Hendriks, B.S.1    Opresko, L.K.2    Wiley, H.S.3    Lauffenburger, D.4
  • 28
    • 25444505624 scopus 로고    scopus 로고
    • Epidermal growth factor-independent transformation of Ba/F3 cells with cancer-derived epidermal growth factor receptor mutants induces Geftinib-sensitive cell cycle progression
    • Jiang J, Greulich H, Jänne PA, Sellers WR, Meyerson M, Griffn JD (2005). Epidermal growth factor-independent transformation of Ba/F3 cells with cancer-derived epidermal growth factor receptor mutants induces Geftinib-sensitive cell cycle progression. Cancer Res 65, 8968-8974.
    • (2005) Cancer Res , vol.65 , pp. 8968-8974
    • Jiang, J.1    Greulich, H.2    Jänne, P.A.3    Sellers, W.R.4    Meyerson, M.5    Griffn, J.D.6
  • 30
    • 67649781716 scopus 로고    scopus 로고
    • Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics
    • Kästner J, Loeffer HH, Roberts SK, Martin-Fernandez ML, Winn MD (2009). Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics. J Struct Biol 167, 117-128.
    • (2009) J Struct Biol , vol.167 , pp. 117-128
    • Kästner, J.1    Loeffer, H.H.2    Roberts, S.K.3    Martin-Fernandez, M.L.4    Winn, M.D.5
  • 32
    • 41049104403 scopus 로고    scopus 로고
    • Studies of distribution, location and dynamic properties of EGFR on the cell surface measured by image correlation spectroscopy
    • Keating E, Nohe A, Petersen NO (2008). Studies of distribution, location and dynamic properties of EGFR on the cell surface measured by image correlation spectroscopy. Eur Biophys J 37, 469-481.
    • (2008) Eur Biophys J , vol.37 , pp. 469-481
    • Keating, E.1    Nohe, A.2    Petersen, N.O.3
  • 35
    • 84878691793 scopus 로고    scopus 로고
    • Exploring higher-order EGFR oligomerisation and phos-phorylation-a combined experimental and theoretical approach
    • Kozer N, Barua D, Orchard S, Nice EC, Burgess AW, Hlavacek WS, Clayton AH (2013). Exploring higher-order EGFR oligomerisation and phos-phorylation-a combined experimental and theoretical approach. Mol Biosyst 9, 1849-1863.
    • (2013) Mol Biosyst , vol.9 , pp. 1849-1863
    • Kozer, N.1    Barua, D.2    Orchard, S.3    Nice, E.C.4    Burgess, A.W.5    Hlavacek, W.S.6    Clayton, A.H.7
  • 36
    • 82955195098 scopus 로고    scopus 로고
    • Evidence for extended YFP-EGFR dimers in the absence of ligand on the surface of living cells
    • Kozer N, Henderson C, Jackson JT, Nice EC, Burgess AW, Clayton AHA (2011). Evidence for extended YFP-EGFR dimers in the absence of ligand on the surface of living cells. Phys Biol 8, 066002.
    • (2011) Phys Biol , vol.8 , pp. 066002
    • Kozer, N.1    Henderson, C.2    Jackson, J.T.3    Nice, E.C.4    Burgess, A.W.5    Aha, C.6
  • 38
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J (2010). Cell signaling by receptor tyrosine kinases. Cell 141, 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 39
    • 23944486487 scopus 로고    scopus 로고
    • Reaching out for signals: Flopodia 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: flopodia 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
  • 42
    • 38949118663 scopus 로고    scopus 로고
    • Structural basis for EGF receptor inhibition by the therapeutic antibody IMC-11F8
    • Li S, Kussie P, Ferguson KM (2008). Structural basis for EGF receptor inhibition by the therapeutic antibody IMC-11F8. Structure 16, 216-227.
    • (2008) Structure , vol.16 , pp. 216-227
    • Li, S.1    Kussie, P.2    Ferguson, K.M.3
  • 43
    • 17444403242 scopus 로고    scopus 로고
    • Structural basis for inhibition of the epidermal growth factor receptor by Cetuximab
    • Li S, Schmitz KR, Jeffrey PD, Wiltzius JJW, Kussie P, Ferguson KM (2005). Structural basis for inhibition of the epidermal growth factor receptor by Cetuximab. Cancer Cell 7, 301-311.
    • (2005) Cancer Cell , vol.7 , pp. 301-311
    • Li, S.1    Schmitz, K.R.2    Jeffrey, P.D.3    Jjw, W.4    Kussie, P.5    Ferguson, K.M.6
  • 45
    • 78649548465 scopus 로고    scopus 로고
    • Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor
    • Lu C, Mi L-Z, Grey MJ, Zhu J, Graef E, Yokoyama S, Springer TA (2010). Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor. Mol Cell Biol 30, 5432-5443.
    • (2010) Mol Cell Biol , vol.30 , pp. 5432-5443
    • Lu, C.1    Mi, L.-Z.2    Grey, M.J.3    Zhu, J.4    Graef, E.5    Yokoyama, S.6    Springer, T.A.7
  • 46
    • 84868323253 scopus 로고    scopus 로고
    • Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor
    • Lu C, Mi L-Z, Schürpf 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    Schürpf, T.3    Walz, T.4    Springer, T.A.5
  • 48
    • 38349190632 scopus 로고    scopus 로고
    • Heterogeneity in EGF-binding affnities arises from negative cooperativity in an aggregating system
    • Macdonald JL, Pike LJ (2008). Heterogeneity in EGF-binding affnities arises from negative cooperativity in an aggregating system. Proc Natl Acad Sci USA 105, 112-117.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 112-117
    • MacDonald, J.L.1    Pike, L.J.2
  • 49
    • 67649391241 scopus 로고    scopus 로고
    • The intracellular juxtamembrane domain of the epidermal growth factor (EGF) receptor is responsible for the allosteric regulation of EGF binding
    • Macdonald-Obermann JL, Pike LJ (2009). The intracellular juxtamembrane domain of the epidermal growth factor (EGF) receptor is responsible for the allosteric regulation of EGF binding. J Biol Chem 284, 13570-13576.
    • (2009) J Biol Chem , vol.284 , pp. 13570-13576
    • Macdonald-Obermann, J.L.1    Pike, L.J.2
  • 50
    • 0036225144 scopus 로고    scopus 로고
    • Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling
    • Martin-Fernandez ML, 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.L.1    Clarke, D.T.2    Tobin, M.J.3    Jones, S.V.4    Jones, G.R.5
  • 51
    • 0742323362 scopus 로고    scopus 로고
    • The tethered confguration of the EGF receptor extracellular domain exerts only a limited control of receptor function
    • Mattoon D, Klein P, Lemmon MA, Lax I, Schlessinger J (2004). The tethered confguration of the EGF receptor extracellular domain exerts only a limited control of receptor function. Proc Natl Acad Sci USA 101, 923-928.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 923-928
    • Mattoon, D.1    Klein, P.2    Lemmon, M.A.3    Lax, I.4    Schlessinger, J.5
  • 52
    • 22244449320 scopus 로고    scopus 로고
    • An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ERBB) family
    • McLaughlin S, Smith SO, Hayman MJ, Murray D (2005). An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family. J Gen Physiol 126, 41-53.
    • (2005) J Gen Physiol , vol.126 , pp. 41-53
    • McLaughlin, S.1    Smith, S.O.2    Hayman, M.J.3    Murray, D.4
  • 53
    • 52949142769 scopus 로고    scopus 로고
    • Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs
    • Mi L-Z, Grey MJ, Nishida N, Walz T, Lu C, Springer TA (2008). Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs. Biochemistry 47, 10314-10323.
    • (2008) Biochemistry , vol.47 , pp. 10314-10323
    • Mi, L.-Z.1    Grey, M.J.2    Nishida, N.3    Walz, T.4    Lu, C.5    Springer, T.A.6
  • 54
    • 80052511894 scopus 로고    scopus 로고
    • Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor
    • Mi L-Z, Lu C, Li Z, Nishida N, Walz T, Springer TA (2011). Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor. Nat Struct Mol Biol 18, 984-989.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 984-989
    • Mi, L.-Z.1    Lu, C.2    Li, Z.3    Nishida, N.4    Walz, T.5    Springer, T.A.6
  • 55
    • 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 USA 107, 16524-16529.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 16524-16529
    • Nagy, P.1    Claus, J.2    Jovin, T.M.3    Arndt-Jovin, D.J.4
  • 60
    • 77958478674 scopus 로고    scopus 로고
    • Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer
    • Pao W, Chmielecki J (2010). Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer. Nat Rev Cancer 10, 760-774.
    • (2010) Nat Rev Cancer , vol.10 , pp. 760-774
    • Pao, W.1    Chmielecki, J.2
  • 61
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to geftinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao W, Miller VA, Politi KA, Riely GJ, Somwar R, Zakowski MF, Kris MG, Varmus H (2005). Acquired resistance of lung adenocarcinomas to geftinib or erlotinib is associated with a second mutation in the EGFR kinase domain. PLoS Med 2, e73.
    • (2005) PLoS Med , vol.2 , pp. e73
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3    Riely, G.J.4    Somwar, R.5    Zakowski, M.F.6    Kris, M.G.7    Varmus, H.8
  • 62
    • 4444344330 scopus 로고    scopus 로고
    • EGF receptor gene mutations are common in lung cancers from "never smokers" and are associated with sensitivity of tumors to geftinib and erlotinib
    • Pao W, Miller V, Zakowski M, Doherty J, Politi K, Sarkaria I, Singh B, Heelan R, Rusch V, Fulton L, et al. (2004). EGF receptor gene mutations are common in lung cancers from "never smokers" and are associated with sensitivity of tumors to geftinib and erlotinib. Proc Natl Acad Sci USA 101, 13306-13311.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13306-13311
    • Pao, W.1    Miller, V.2    Zakowski, M.3    Doherty, J.4    Politi, K.5    Sarkaria, I.6    Singh, B.7    Heelan, R.8    Rusch, V.9    Fulton, L.10
  • 65
    • 37549036341 scopus 로고    scopus 로고
    • Current situation of Panitumumab, Matuzumab, Nimotuzumab and Zalutumumab
    • Rivera F, Vega-Villegas ME, Lopez-Brea MF, Marquez R (2008). Current situation of Panitumumab, Matuzumab, Nimotuzumab and Zalutumumab. Acta Oncol 47, 9-19.
    • (2008) Acta Oncol , vol.47 , pp. 9-19
    • Rivera, F.1    Vega-Villegas, M.E.2    Lopez-Brea, M.F.3    Marquez, R.4
  • 66
    • 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
  • 67
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • Schlessinger J (2002). Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 110, 669-672.
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 68
    • 41249094559 scopus 로고    scopus 로고
    • Matuzumab binding to EGFR prevents the conformational rearrangement required for dimerization
    • Schmiedel J, Blaukat A, Li S, Knöchel T, Ferguson KM (2008). Matuzumab binding to EGFR prevents the conformational rearrangement required for dimerization. Cancer Cell 13, 365-373.
    • (2008) Cancer Cell , vol.13 , pp. 365-373
    • Schmiedel, J.1    Blaukat, A.2    Li, S.3    Knöchel, T.4    Ferguson, K.M.5
  • 69
    • 84923322056 scopus 로고    scopus 로고
    • Fluorogen-activating proteins provide tunable labeling densities for tracking Fc?RI independent of IgE
    • Schwartz SL, Yan Q, Telmer CA, Lidke KA, Bruchez M P, Lidke DS (2015). Fluorogen-activating proteins provide tunable labeling densities for tracking Fc?RI independent of IgE. ACS Chem Biol 10, 539-546.
    • (2015) ACS Chem Biol , vol.10 , pp. 539-546
    • Schwartz, S.L.1    Yan, Q.2    Telmer, C.A.3    Lidke, K.A.4    Bruchez, M.P.5    Lidke, D.S.6
  • 70
    • 79959637365 scopus 로고    scopus 로고
    • Quantifcation of biological interactions with particle image cross-correlation spectros-copy (PICCS)
    • Semrau S, Holtzer L, González-Gaitán M, Schmidt T (2011). Quantifcation of biological interactions with particle image cross-correlation spectros-copy (PICCS). Biophys J 100, 1810-1818.
    • (2011) Biophys J , vol.100 , pp. 1810-1818
    • Semrau, S.1    Holtzer, L.2    González-Gaitán, M.3    Schmidt, T.4
  • 71
    • 80255137569 scopus 로고    scopus 로고
    • Probing protein heterogeneity in the plasma membrane using PALM and pair correlation analysis
    • Lippincott-Schwartz J
    • Sengupta P, Jovanovic-Talisman T, Skoko D, Renz M, Veatch SL, Lippincott-Schwartz J (2011). Probing protein heterogeneity in the plasma membrane using PALM and pair correlation analysis. Nat Methods 8, 969-975.
    • (2011) Nat Methods , vol.8 , pp. 969-975
    • Sengupta, P.1    Jovanovic-Talisman, T.2    Skoko, D.3    Renz, M.4    Veatch, S.L.5
  • 72
    • 84860870716 scopus 로고    scopus 로고
    • Oncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerization
    • Shan Y, Eastwood M P, Zhang X, Kim ET, Arkhipov A, Dror RO, Jumper J, Kuriyan J, Shaw DE (2012). Oncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerization. Cell 149, 860-870.
    • (2012) Cell , vol.149 , pp. 860-870
    • Shan, Y.1    Eastwood, M.P.2    Zhang, X.3    Kim, E.T.4    Arkhipov, A.5    Dror, R.O.6    Jumper, J.7    Kuriyan, J.8    De, S.9
  • 73
  • 74
    • 84887891725 scopus 로고    scopus 로고
    • Distinct stages of stimulated FceRI receptor clustering and immobilization are identifed through superresolution imaging
    • Shelby SA, Holowka D, Baird B, Veatch SL (2013). Distinct stages of stimulated FceRI receptor clustering and immobilization are identifed through superresolution imaging. Biophys J 105, 2343-2354.
    • (2013) Biophys J , vol.105 , pp. 2343-2354
    • Shelby, S.A.1    Holowka, D.2    Baird, B.3    Veatch, S.L.4
  • 75
    • 77952216273 scopus 로고    scopus 로고
    • Fast, single-molecule localization that achieves theoretically minimum uncertainty
    • Smith CS, Joseph N, Rieger B, Lidke KA (2010). Fast, single-molecule localization that achieves theoretically minimum uncertainty. Nat Methods 7, 373-375.
    • (2010) Nat Methods , vol.7 , pp. 373-375
    • Smith, C.S.1    Joseph, N.2    Rieger, B.3    Lidke, K.A.4
  • 79
    • 37649013040 scopus 로고    scopus 로고
    • Epidermal growth factor receptor juxtamem-brane region regulates allosteric tyrosine kinase activation
    • Thiel KW, Carpenter G (2007). Epidermal growth factor receptor juxtamem-brane region regulates allosteric tyrosine kinase activation. Proc Natl Acad Sci USA 104, 19238-19243.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19238-19243
    • Thiel, K.W.1    Carpenter, G.2
  • 81
    • 84893258774 scopus 로고    scopus 로고
    • The spatiotemporal organization of ERBB receptors: Insights from microscopy
    • Valley CC, Lidke KA, Lidke DS (2014). The spatiotemporal organization of ErbB receptors: insights from microscopy. Cold Spring Harb Perspect Biol 6, a020735.
    • (2014) Cold Spring Harb Perspect Biol , vol.6 , pp. a020735
    • Valley, C.C.1    Lidke, K.A.2    Lidke, D.S.3
  • 83
    • 84857580744 scopus 로고    scopus 로고
    • Correlation functions quantify super-resolution images and estimate apparent clustering due to over-counting
    • Veatch SL, Machta BB, Shelby SA, Chiang EN, Holowka DA, Baird BA (2012). Correlation functions quantify super-resolution images and estimate apparent clustering due to over-counting. PLoS One 7, e31457.
    • (2012) PLoS One , vol.7 , pp. e31457
    • Veatch, S.L.1    Machta, B.B.2    Shelby, S.A.3    Chiang, E.N.4    Holowka, D.A.5    Baird, B.A.6
  • 85
    • 38549132873 scopus 로고    scopus 로고
    • Single-molecule imaging and fuorescence lifetime imaging microscopy show different structures for high-and low-affnity epidermal growth factor receptors in A431 cells
    • Webb SED, Roberts SK, Needham SR, Tynan CJ, Rolfe DJ, Winn MD, Clarke DT, Barraclough R, Martin-Fernandez ML (2008). Single-molecule imaging and fuorescence lifetime imaging microscopy show different structures for high-and low-affnity epidermal growth factor receptors in A431 cells. Biophys J 94, 803-819.
    • (2008) Biophys J , vol.94 , pp. 803-819
    • Sed, W.1    Roberts, S.K.2    Needham, S.R.3    Tynan, C.J.4    Rolfe, D.J.5    Winn, M.D.6    Clarke, D.T.7    Barraclough, R.8    Martin-Fernandez, M.L.9
  • 86
    • 33847406095 scopus 로고    scopus 로고
    • Structures of lung cancer-derived EGFR mutants and inhibitor complexes: Mechanism of activation and insights into differential inhibitor sensitivity
    • Yun C-H, Boggon TJ, Li Y, Woo MS, Greulich H, Meyerson M, Eck MJ (2007). Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity. Cancer Cell 11, 217-227.
    • (2007) Cancer Cell , vol.11 , pp. 217-227
    • Yun, C.-H.1    Boggon, T.J.2    Li, Y.3    Woo, M.S.4    Greulich, H.5    Meyerson, M.6    Eck, M.J.7
  • 88
    • 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
  • 89
    • 84883049567 scopus 로고    scopus 로고
    • Dynamic conformational transitions of the EGF receptor in living mammalian cells determined by FRET and fuorescence lifetime imaging microscopy
    • Ziomkiewicz I, Loman A, Klement R, Fritsch C, Klymchenko AS, Bunt G, Jo-vin TM, Arndt-Jovin DJ (2013). Dynamic conformational transitions of the EGF receptor in living mammalian cells determined by FRET and fuorescence lifetime imaging microscopy. Cytometry A 83, 794-805.
    • (2013) Cytometry A , vol.83 , pp. 794-805
    • Ziomkiewicz, I.1    Loman, A.2    Klement, R.3    Fritsch, C.4    Klymchenko, A.S.5    Bunt, G.6    Jo-Vin, T.M.7    Arndt-Jovin, D.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.