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Volumn 2, Issue 5, 2008, Pages 256-272

Stochastic simulations of ErbB homo and heterodimerisation: Potential impacts of receptor conformational state and spatial segregation

Author keywords

[No Author keywords available]

Indexed keywords

FLOW OF SOLIDS; LIGANDS; OLIGOMERIZATION; OLIGOMERS; PATHOLOGY; PROBABILITY; SEGREGATION (METALLOGRAPHY); STOCHASTIC CONTROL SYSTEMS; STOCHASTIC PROGRAMMING;

EID: 54049134792     PISSN: 17518849     EISSN: None     Source Type: Journal    
DOI: 10.1049/iet-syb:20070073     Document Type: Conference Paper
Times cited : (25)

References (63)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • 'Signaling-2000 and beyond'
    • Hunter, T.: 'Signaling-2000 and beyond', Cell, 2000, 100, p. 113-127
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0037145061 scopus 로고    scopus 로고
    • 'Ligand-induced, receptor-mediated dimerization and activation of EGF receptor'
    • Schlessinger, J.: 'Ligand-induced, receptor-mediated dimerization and activation of EGF receptor', Cell, 2002, 110, p. 669-672
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 4
    • 0028955388 scopus 로고
    • 'Epidermal growth factor related peptides and their receptors in human malignancies'
    • Salomon, D.S., Brandt, R., Ciardiello, F., and Normanno, N.: 'Epidermal growth factor related peptides and their receptors in human malignancies', Crit. Rev. Oncol. Hematol., 1995, 19, p. 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
  • 5
    • 0028292482 scopus 로고
    • 'Dysregulation of epidermal growth factor receptor expression in premalignant lesions during head and neck tumorigenesis'
    • Shin, D.M., Ro, J.Y., Hong, W.K., and Hittelman, W.N.: 'Dysregulation of epidermal growth factor receptor expression in premalignant lesions during head and neck tumorigenesis', Cancer Res., 1994, 54, p. 3153-3159
    • (1994) Cancer Res. , vol.54 , pp. 3153-3159
    • Shin, D.M.1    Ro, J.Y.2    Hong, W.K.3    Hittelman, W.N.4
  • 6
    • 0030927973 scopus 로고    scopus 로고
    • 'Epidermal growth factor receptor immunoreactivity in human laryngeal squamous cell carcinoma'
    • Lee, C.S., Redshaw, A., and Boag, G.: 'Epidermal growth factor receptor immunoreactivity in human laryngeal squamous cell carcinoma', Pathology, 1997, 29, p. 251-254
    • (1997) Pathology , vol.29 , pp. 251-254
    • Lee, C.S.1    Redshaw, A.2    Boag, G.3
  • 7
    • 0036728845 scopus 로고    scopus 로고
    • 'Targeted therapy in non-small-cell lung cancer'
    • Herbst, R.S.: 'Targeted therapy in non-small-cell lung cancer', Oncology, 2002, 16, p. 19-24
    • (2002) Oncology , vol.16 , pp. 19-24
    • Herbst, R.S.1
  • 8
    • 0041629450 scopus 로고    scopus 로고
    • 'Status of epidermal growth factor receptor antagonists in the biology and treatment of cancer'
    • Mendelsohn, J., and Baselga, J.: 'Status of epidermal growth factor receptor antagonists in the biology and treatment of cancer', J. Clin. Oncol., 2003, 21, p. 2787-2799
    • (2003) J. Clin. Oncol. , vol.21 , pp. 2787-2799
    • Mendelsohn, J.1    Baselga, J.2
  • 9
    • 0036320471 scopus 로고    scopus 로고
    • 'Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling'
    • Yu, X., Sharma, K.D., Takahashi, T., Iwamoto, R., and Mekada, E.: 'Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling', Mol. Biol. Cell, 2002, 13, p. 2547-2557
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2547-2557
    • Yu, X.1    Sharma, K.D.2    Takahashi, T.3    Iwamoto, R.4    Mekada, E.5
  • 10
    • 0029010607 scopus 로고
    • 'Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation'
    • Gadella, T.W.J., and Jovin, T.M.: 'Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation', J. Cell Biol., 1995, 129, p. 1543-1558
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella, T.W.J.1    Jovin, T.M.2
  • 11
    • 0035979763 scopus 로고    scopus 로고
    • 'Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain'
    • Moriki, T., Maruyama, H., and Maruyama, I.N.: 'Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain', J. Mol. Biol., 2001, 331, p. 1011-1026
    • (2001) J. Mol. Biol. , vol.331 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 12
    • 0142184429 scopus 로고    scopus 로고
    • 'Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET)'
    • Lidke, D.S., Nagy, P., and Barisas, B.G.: Et al. 'Imaging molecular interactions in cells by dynamic and static fluorescence anisotropy (rFLIM and emFRET)', Biochem. Soc. Trans., 2003, 31, p. 1020-1027
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1020-1027
    • Lidke, D.S.1    Nagy, P.2    Barisas, B.G.3
  • 13
    • 0033779765 scopus 로고    scopus 로고
    • 'Single-molecule imaging of EGFR signalling on the surface of living cells'
    • Sako, Y., Minoghchi, S., and Yanagida, T.: 'Single-molecule imaging of EGFR signalling on the surface of living cells', Nat. Cell. Biol., 2000, 2, p. 168-172
    • (2000) Nat. Cell. Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 14
    • 0031010495 scopus 로고    scopus 로고
    • 'Secondary dimerization between members of the epidermal growth factor receptor family'
    • Gamett, D.C., Pearson, G., Cerione, R.A., and Friedberg, I.: 'Secondary dimerization between members of the epidermal growth factor receptor family', J. Biol. Chem., 1997, 272, p. 12052-12056
    • (1997) J. Biol. Chem. , vol.272 , pp. 12052-12056
    • Gamett, D.C.1    Pearson, G.2    Cerione, R.A.3    Friedberg, I.4
  • 15
    • 0023443196 scopus 로고
    • 'Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding'
    • 0027-8424
    • Boni-Schnetzler, M., and Pilch, P.F.: 'Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding', Proc. Natl. Acad. Sci. USA, 1987, 84, p. 7832-7836 0027-8424
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7832-7836
    • Boni-Schnetzler, M.1    Pilch, P.F.2
  • 16
    • 0023848318 scopus 로고
    • 'Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent'
    • Cochet, C., Kashles, O., Chambaz, E.M., Borrello, I., King, C.R., and Schlessinger, J.: 'Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent', J. Biol. Chem., 1988, 263, p. 3290-3295
    • (1988) J. Biol. Chem. , vol.263 , pp. 3290-3295
    • Cochet, C.1    Kashles, O.2    Chambaz, E.M.3    Borrello, I.4    King, C.R.5    Schlessinger, J.6
  • 17
    • 34447313361 scopus 로고    scopus 로고
    • 'Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis'
    • 10.1529/biophysj.107.105494 0006-3495
    • Saffarian, S., Li, Y., Elson, E.L., and Pike, L.J.: 'Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis', Biophys. J., 2007, 93, p. 1021-1031 10.1529/ biophysj.107.105494 0006-3495
    • (2007) Biophys. J. , vol.93 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pike, L.J.4
  • 18
    • 34447299688 scopus 로고    scopus 로고
    • 'Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy'
    • 0006-3495
    • Liu, P., Sudhaharan, T., and Koh, R.M.L.: Et al. 'Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy', Biophys. J., 2007, 93, p. 684-698 0006-3495
    • (2007) Biophys. J. , vol.93 , pp. 684-698
    • Liu, P.1    Sudhaharan, T.2    Koh, R.M.L.3
  • 19
    • 0025775735 scopus 로고
    • 'Ligand-induced activation of A431 cell epidermal growth factor receptors occurs primarily by an autocrine pathway that acts upon receptors on the surface rather than intracellularly'
    • Van de Vijver, M.J., Kumar, R., and Mendelsohn, J.: 'Ligand-induced activation of A431 cell epidermal growth factor receptors occurs primarily by an autocrine pathway that acts upon receptors on the surface rather than intracellularly', J. Biol. Chem., 1991, 266, p. 7503-7508
    • (1991) J. Biol. Chem. , vol.266 , pp. 7503-7508
    • Van de Vijver, M.J.1    Kumar, R.2    Mendelsohn, J.3
  • 20
    • 2442427510 scopus 로고    scopus 로고
    • 'Induced autocrine signaling through the epidermal growth factor receptor contributes to the response of mammary epithelial cells to tumor necrosis factor alpha'
    • Chen, W.N.U., Woodbury, R.L., and Kathmann, L.E.: Et al. 'Induced autocrine signaling through the epidermal growth factor receptor contributes to the response of mammary epithelial cells to tumor necrosis factor alpha', J. Biol. Chem., 2004, 279, p. 18488-18496
    • (2004) J. Biol. Chem. , vol.279 , pp. 18488-18496
    • Chen, W.N.U.1    Woodbury, R.L.2    Kathmann, L.E.3
  • 21
    • 0036225144 scopus 로고    scopus 로고
    • 'Preformed oligomeric EGF receptors undergo an ectodomain structure change during signalling'
    • 0006-3495
    • Martin-Fernandez, M.L., Tobin, M.J., Jones, S.V., Clarke, D.T., and Jones, G.R.: 'Preformed oligomeric EGF receptors undergo an ectodomain structure change during signalling', Biophys. J., 2002, 82, p. 2415-2427 0006-3495
    • (2002) Biophys. J. , vol.82 , pp. 2415-2427
    • Martin-Fernandez, M.L.1    Tobin, M.J.2    Jones, S.V.3    Clarke, D.T.4    Jones, G.R.5
  • 22
    • 0037162799 scopus 로고    scopus 로고
    • 'Structure of the extracellular region of HER3 reveals an interdomain tether'
    • 10.1126/science.1074611 0036-8075
    • Cho, H.S., and Leahy, D.J.: 'Structure of the extracellular region of HER3 reveals an interdomain tether', Science, 2002, 297, p. 1330-1333 10.1126/science.1074611 0036-8075
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 23
    • 18644370411 scopus 로고    scopus 로고
    • 'Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha'
    • Garrett, T.P.J., McKern, N.M., and Low, M.: Et al. 'Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha', Cell, 2002, 110, p. 763-773
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.P.J.1    McKern, N.M.2    Low, M.3
  • 24
    • 18644386251 scopus 로고    scopus 로고
    • 'Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains'
    • Ogiso, H., Ishitani, R., and Nureki, O.: Et al. 'Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains', Cell, 2002, 110, p. 775-787
    • (2002) Cell , vol.110 , pp. 775-787
    • Ogiso, H.1    Ishitani, R.2    Nureki, O.3
  • 25
    • 0037291769 scopus 로고    scopus 로고
    • 'EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization'
    • Ferguson, K.M., Berger, M.B., Mendrola, J.M., Cho, H.S., Leahy, D.J., and Lemmon, M.A.: 'EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization ', Mol. Cell, 2003, 11, p. 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
  • 26
    • 0742288415 scopus 로고    scopus 로고
    • 'A structure-based model for ligand binding and dimerization of EGF receptors'
    • Klein, P., Mattoon, D., Lemmon, M.A., and Schlessinger, J.: 'A structure-based model for ligand binding and dimerization of EGF receptors', Proc. Natl. Acad. Sci., 2004, 101, p. 929-934
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 929-934
    • Klein, P.1    Mattoon, D.2    Lemmon, M.A.3    Schlessinger, J.4
  • 27
    • 0037112996 scopus 로고    scopus 로고
    • 'Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2'
    • Nagy, P., Vereb, G., and Sebestyen, Z.: Et al. 'Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2', J. Cell Sci., 2002, 115, p. 4251-4262
    • (2002) J. Cell Sci. , vol.115 , pp. 4251-4262
    • Nagy, P.1    Vereb, G.2    Sebestyen, Z.3
  • 28
    • 34548555698 scopus 로고    scopus 로고
    • 'Mapping ErbB receptors on breast cancer cell membranes during signal transduction'
    • Yang, S., Raymond-Stintz, M.A., and Ying, W.: Et al. 'Mapping ErbB receptors on breast cancer cell membranes during signal transduction', J. Cell Sci., 2007, 120, p. 2763-2773
    • (2007) J. Cell Sci. , vol.120 , pp. 2763-2773
    • Yang, S.1    Raymond-Stintz, M.A.2    Ying, W.3
  • 29
    • 0032998181 scopus 로고    scopus 로고
    • 'Anomalous diffusion of major histocompatibility complex class I molecules on HeLa cells determined by single particle tracking'
    • 0006-3495
    • Smith, P.R., Morrison, I.E.G., Wilson, K.M., Fernandez, N., and Cherry, R.J.: 'Anomalous diffusion of major histocompatibility complex class I molecules on HeLa cells determined by single particle tracking', Biophys. J., 1999, 76, p. 3331-3344 0006-3495
    • (1999) Biophys. J. , vol.76 , pp. 3331-3344
    • Smith, P.R.1    Morrison, I.E.G.2    Wilson, K.M.3    Fernandez, N.4    Cherry, R.J.5
  • 30
    • 0027504198 scopus 로고
    • 'Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells'
    • 0006-3495
    • Kusumi, A., Sako, Y., and Yamamoto, M.: 'Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells', Biophys. J., 1993, 65, p. 2021-2040 0006-3495
    • (1993) Biophys. J. , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 31
    • 2942662120 scopus 로고    scopus 로고
    • 'Ultrafine membrane compartments for molecular diffusion as revealed by single molecule techniques'
    • 10.1529/biophysj.103.035717 0006-3495
    • Murase, K., Fujiwara, T., and Umemura, Y.: Et al. 'Ultrafine membrane compartments for molecular diffusion as revealed by single molecule techniques', Biophys. J., 2004, 86, p. 4075-4093 10.1529/ biophysj.103.035717 0006-3495
    • (2004) Biophys. J. , vol.86 , pp. 4075-4093
    • Murase, K.1    Fujiwara, T.2    Umemura, Y.3
  • 32
    • 0036214457 scopus 로고    scopus 로고
    • 'Relationship of lipid rafts to transient confinement zones detected by single particle tracking'
    • 0006-3495
    • Dietrich, C., Yang, B., Fujiwara, T., Kusumi, A., and Jacobson, K.: 'Relationship of lipid rafts to transient confinement zones detected by single particle tracking', Biophys. J., 2002, 82, p. 274-284 0006-3495
    • (2002) Biophys. J. , vol.82 , pp. 274-284
    • Dietrich, C.1    Yang, B.2    Fujiwara, T.3    Kusumi, A.4    Jacobson, K.5
  • 33
    • 34247857560 scopus 로고    scopus 로고
    • 'Multiple association states between glycine and gephyrin identified by SPT analysis'
    • 10.1529/biophysj.106.095596 0006-3495
    • Ehrensperger, M.-V., Hanus, C., Vannier, C., Triller, A., and Dahan, M.: ' Multiple association states between glycine and gephyrin identified by SPT analysis', Biophys. J., 2007, 92, p. 3706-3718 10.1529/ biophysj.106.095596 0006-3495
    • (2007) Biophys. J. , vol.92 , pp. 3706-3718
    • Ehrensperger, M.-V.1    Hanus, C.2    Vannier, C.3    Triller, A.4    Dahan, M.5
  • 34
    • 0030222116 scopus 로고    scopus 로고
    • 'Cell surface organization by the membrane skeleton'
    • Kusumi, A., and Sako, Y.: 'Cell surface organization by the membrane skeleton', Curr. Biol. Cell Biol., 1996, 8, p. 566-574
    • (1996) Curr. Biol. Cell Biol. , vol.8 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 35
    • 33748579946 scopus 로고    scopus 로고
    • 'Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography'
    • Morone, N., Fujiwara, T., and Murase, K.: Et al. 'Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography', J. Cell. Biol., 2006, 174, p. 851-862
    • (2006) J. Cell. Biol. , vol.174 , pp. 851-862
    • Morone, N.1    Fujiwara, T.2    Murase, K.3
  • 36
    • 34247861082 scopus 로고    scopus 로고
    • 'Plasma membrane-associated proteins are clustered into islands attached to the cytoskeleton'
    • 0027-8424
    • Lillemeier, B.F., Pfeiffer, J.R., Surviladze, Z., Wilson, B.S., and Davis, M.M.: 'Plasma membrane-associated proteins are clustered into islands attached to the cytoskeleton', Proc. Natl. Acad. Sci. USA, 2006, 103, p. 18992-18997 0027-8424
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18992-18997
    • Lillemeier, B.F.1    Pfeiffer, J.R.2    Surviladze, Z.3    Wilson, B.S.4    Davis, M.M.5
  • 37
    • 33744927122 scopus 로고    scopus 로고
    • 'Modeling the effects of HER/ErbB1-3 coexpression on receptor dimerization and biological response'
    • 10.1529/biophysj.105.080580 0006-3495
    • Shankaran, H., Wiley, H.S., and Resat, H.: 'Modeling the effects of HER/ ErbB1-3 coexpression on receptor dimerization and biological response', Biophys. J., 2006, 90, p. 3993-4009 10.1529/biophysj.105.080580 0006-3495
    • (2006) Biophys. J. , vol.90 , pp. 3993-4009
    • Shankaran, H.1    Wiley, H.S.2    Resat, H.3
  • 38
    • 33645429016 scopus 로고
    • 'Exact stochastic simulation of coupled chemical reactions'
    • 10.1021/j100540a008 0022-3654
    • Gillespie, D.T.: 'Exact stochastic simulation of coupled chemical reactions', J. Phys. Chem., 1977, 81, p. 2340-2361 10.1021/j100540a008 0022-3654
    • (1977) J. Phys. Chem. , vol.81 , pp. 2340-2361
    • Gillespie, D.T.1
  • 39
    • 27744484465 scopus 로고    scopus 로고
    • 'Characterizing the topography of membrane receptors and signaling molecules from spatial patterns obtained using nanometer-scale electron-dense probes and electron microscopy'
    • 0047-7206
    • Zhang, J., Leiderman, K., Pfeiffer, J.R., Wilson, B.S., Oliver, J.M., and Steinberg, S.L.: 'Characterizing the topography of membrane receptors and signaling molecules from spatial patterns obtained using nanometer-scale electron-dense probes and electron microscopy', Micron, 2006, 37, p. 14-34 0047-7206
    • (2006) Micron , vol.37 , pp. 14-34
    • Zhang, J.1    Leiderman, K.2    Pfeiffer, J.R.3    Wilson, B.S.4    Oliver, J.M.5    Steinberg, S.L.6
  • 40
    • 0034708826 scopus 로고    scopus 로고
    • 'Cross-talk between epidermal growth factor receptor and c-Met signal pathways in transformed cells'
    • Jo, M., Stolz, D.B., Esplen, J.E., Dorko, K., Michalopoulos, G.K., and Strom, S.C.: 'Cross-talk between epidermal growth factor receptor and c-Met signal pathways in transformed cells', J. Biol. Chem., 2000, 275, p. 8806-8811
    • (2000) J. Biol. Chem. , vol.275 , pp. 8806-8811
    • Jo, M.1    Stolz, D.B.2    Esplen, J.E.3    Dorko, K.4    Michalopoulos, G.K.5    Strom, S.C.6
  • 41
    • 2542472339 scopus 로고    scopus 로고
    • 'Markers for detergent-resistant lipid rafts occupy distinct and dynamic domains in native membranes'
    • Wilson, B.S., Steinberg, S.L., and Liederman, K.: Et al. 'Markers for detergent-resistant lipid rafts occupy distinct and dynamic domains in native membranes', Mol. Biol. Cell, 2004, 15, p. 2580-2592
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2580-2592
    • Wilson, B.S.1    Steinberg, S.L.2    Liederman, K.3
  • 42
    • 38049095130 scopus 로고    scopus 로고
    • 'Markov random field modeling of the spatial distribution of proteins on cell membranes'
    • 0092-8240
    • Zhang, J., Steinberg, S., Wilson, B.S., Oliver, J.M., and Williams, L.: 'Markov random field modeling of the spatial distribution of proteins on cell membranes', Bull. Math. Biol., 2008, 70, p. 297-;321 0092-8240
    • (2008) Bull. Math. Biol. , vol.70 , pp. 297-321
    • Zhang, J.1    Steinberg, S.2    Wilson, B.S.3    Oliver, J.M.4    Williams, L.5
  • 43
    • 0037931402 scopus 로고    scopus 로고
    • 'Quantitative analysis of HER2-mediated effects on HER2 and epidermal growth factor receptor endocytosis: Distribution of homo- and heterodimers depends on relative HER2 levels'
    • Hendriks, B.S., Opresko, L.K., Wiley, H.S., and Lauffenburger, D.A.: 'Quantitative analysis of HER2-mediated effects on HER2 and epidermal growth factor receptor endocytosis: Distribution of homo- and heterodimers depends on relative HER2 levels', J. Biol. Chem., 2003, 278, p. 23343-23351
    • (2003) J. Biol. Chem. , vol.278 , pp. 23343-23351
    • Hendriks, B.S.1    Opresko, L.K.2    Wiley, H.S.3    Lauffenburger, D.A.4
  • 44
    • 0028358856 scopus 로고
    • 'Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin'
    • Sliwkowski, M.X., Schaefer, G., and Akita, R.W.: Et al. 'Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin', J. Biol. Chem., 1994, 269, p. 14661-14665
    • (1994) J. Biol. Chem. , vol.269 , pp. 14661-14665
    • Sliwkowski, M.X.1    Schaefer, G.2    Akita, R.W.3
  • 45
    • 20244367576 scopus 로고    scopus 로고
    • 'Bivalence of EGF-like ligands drives the ErbB signaling network'
    • Tzahar, E., Pinkas-Kramarski, R., and Moyer, J.D.: Et al. 'Bivalence of EGF-like ligands drives the ErbB signaling network', EMBO J., 1997, 16, p. 4938-4950
    • (1997) EMBO J. , vol.16 , pp. 4938-4950
    • Tzahar, E.1    Pinkas-Kramarski, R.2    Moyer, J.D.3
  • 46
    • 3042800393 scopus 로고    scopus 로고
    • 'ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface'
    • Berger, M.B., Mendrola, J.M., and Lemmon, M.A.: 'ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface', FEBS Lett., 2004, 569, p. 332-336
    • (2004) FEBS Lett. , vol.569 , pp. 332-336
    • Berger, M.B.1    Mendrola, J.M.2    Lemmon, M.A.3
  • 47
    • 0026833077 scopus 로고
    • 'Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation response'
    • Starbuck, C., and Lauffenburger, D.A.: 'Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation response', Biotechnol. Prog., 1992, 8, p. 132-143
    • (1992) Biotechnol. Prog. , vol.8 , pp. 132-143
    • Starbuck, C.1    Lauffenburger, D.A.2
  • 48
    • 17844375949 scopus 로고    scopus 로고
    • 'Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response'
    • 10.1529/biophysj.104.053330 0006-3495
    • Uyemura, T., Takagi, H., Yanagida, T., and Sako, Y.: 'Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response', Biophys. J., 2005, 88, p. 3720-3730 10.1529/biophysj.104.053330 0006-3495
    • (2005) Biophys. J. , vol.88 , pp. 3720-3730
    • Uyemura, T.1    Takagi, H.2    Yanagida, T.3    Sako, Y.4
  • 49
    • 32044469862 scopus 로고    scopus 로고
    • 'A network model of early events in epidermal growth factor receptor signaling that accounts for combinatorial complexity'
    • Blinov, M.L., Faeder, J.R., Goldstein, B., and Hlavacek, W.S.: 'A network model of early events in epidermal growth factor receptor signaling that accounts for combinatorial complexity', Biosystems, 2006, 83, p. 136-151
    • (2006) Biosystems , vol.83 , pp. 136-151
    • Blinov, M.L.1    Faeder, J.R.2    Goldstein, B.3    Hlavacek, W.S.4
  • 50
    • 0037213006 scopus 로고    scopus 로고
    • 'Computational modeling of the EGF-receptor system: A paradigm for systems biology'
    • Wiley, H.S., Shvartsman, S.Y., and Lauffenburger, D.A.: 'Computational modeling of the EGF-receptor system: A paradigm for systems biology', Trends. Cell Biol., 2003, 13, p. 43-50
    • (2003) Trends. Cell Biol. , vol.13 , pp. 43-50
    • Wiley, H.S.1    Shvartsman, S.Y.2    Lauffenburger, D.A.3
  • 51
    • 0342333608 scopus 로고    scopus 로고
    • 'MCell: Generalized Monte Carlo computer simulation of synaptic transmission and chemical signaling'
    • Bartol, T.M., Stiles, J.R., Salpeter, M.M., Salpeter, E.E., and SeGnowski, T.J.: 'MCell: generalized Monte Carlo computer simulation of synaptic transmission and chemical signaling', Soc. Neurosci. Abs., 1996, 22, p. 1742
    • (1996) Soc. Neurosci. Abs. , vol.22 , pp. 1742
    • Bartol, T.M.1    Stiles, J.R.2    Salpeter, M.M.3    Salpeter, E.E.4    Sejnowski, T.J.5
  • 52
    • 0034961694 scopus 로고    scopus 로고
    • 'Stochsim: Modeling of stochastic biomolecular processes'
    • Le NoMere, N., and Shimizu, T.S.: 'Stochsim: modeling of stochastic biomolecular processes', Bioinformatics, 2001, 6, p. 575-576
    • (2001) Bioinformatics , vol.6 , pp. 575-576
    • Le Novere, N.1    Shimizu, T.S.2
  • 53
    • 33748520215 scopus 로고    scopus 로고
    • 'Stochastic simulation of chemical reactions with spatial resolution and single molecule detail'
    • 1478-3967
    • Andrews, S.S., and Bray, D.: 'Stochastic simulation of chemical reactions with spatial resolution and single molecule detail', Phys. Biol., 2006, 1, p. 137-151 1478-3967
    • (2006) Phys. Biol. , vol.1 , pp. 137-151
    • Andrews, S.S.1    Bray, D.2
  • 54
    • 29244454300 scopus 로고    scopus 로고
    • 'Green's-function reaction dynamics: A particle-based approach for simulating biochemical networks in time and space'
    • 0021-9606
    • Van Zon, J.S., and ten Wolde, P.R.: 'Green's-function reaction dynamics: a particle-based approach for simulating biochemical networks in time and space', J. Chem. Phys., 2005, 123, p. 1-16 0021-9606
    • (2005) J. Chem. Phys. , vol.123 , pp. 1-16
    • Van Zon, J.S.1    ten Wolde, P.R.2
  • 55
    • 33645821892 scopus 로고    scopus 로고
    • 'On the nature of low- and high-affinity EGF receptors on living cells'
    • Ozcan, F., Klein, P., Lemmon, M.A., Lax, I., and Schlessinger, J.: 'On the nature of low- and high-affinity EGF receptors on living cells', PNAS, 2006, 103, p. 5735-5740
    • (2006) PNAS , vol.103 , pp. 5735-5740
    • Ozcan, F.1    Klein, P.2    Lemmon, M.A.3    Lax, I.4    Schlessinger, J.5
  • 56
    • 0026708050 scopus 로고
    • 'Implications of epidermal growth factor (EGF) induced EGF receptor aggregation'
    • 0006-3495
    • Wofsy, C., Goldstein, B., Lund, K., and Wiley, H.S.: 'Implications of epidermal growth factor (EGF) induced EGF receptor aggregation', Biophys. J., 1992, 63, p. 98-110 0006-3495
    • (1992) Biophys. J. , vol.63 , pp. 98-110
    • Wofsy, C.1    Goldstein, B.2    Lund, K.3    Wiley, H.S.4
  • 57
    • 20444409504 scopus 로고    scopus 로고
    • 'Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding'
    • Mayawala, K., Vlachos, D.G., and Edwards, J.S.: 'Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding', FEBS Lett., 2005, 579, p. 3043-3047
    • (2005) FEBS Lett. , vol.579 , pp. 3043-3047
    • Mayawala, K.1    Vlachos, D.G.2    Edwards, J.S.3
  • 58
    • 0025967975 scopus 로고
    • 'Three classes of epidermal growth factor receptors on Hela cells'
    • Berkers, J.A., van Bergen en Henegouwen, P.M., and Boonstra, J.: 'Three classes of epidermal growth factor receptors on Hela cells', J. Biol. Chem., 1991, 266, p. 922-927
    • (1991) J. Biol. Chem. , vol.266 , pp. 922-927
    • Berkers, J.A.1    van Bergen en Henegouwen, P.M.2    Boonstra, J.3
  • 60
    • 34248353815 scopus 로고    scopus 로고
    • 'Probability-based model of protein-protein interactions on biological timescales'
    • Tournier, A., Fitzjohn, P., and Bates, P.: 'Probability-based model of protein-protein interactions on biological timescales', Algorithms Mol. Biol., 2006, 1, p. 60
    • (2006) Algorithms Mol. Biol. , vol.1 , pp. 60
    • Tournier, A.1    Fitzjohn, P.2    Bates, P.3
  • 62
    • 0018101150 scopus 로고
    • 'Models for the specific adhesion of cells to cells'
    • 0036-8075
    • Bell, G.I.: 'Models for the specific adhesion of cells to cells', Science, 1978, 200, p. 618-627 0036-8075
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 63
    • 0035890437 scopus 로고    scopus 로고
    • 'Three-dimensional simulations of reversible bimolecular reactions: The simple target problem'
    • 10.1063/1.1412609 0021-9606
    • Popov, A.V., and Agmon, N.: 'Three-dimensional simulations of reversible bimolecular reactions: The simple target problem', J. Chem. Phys., 2001, 115, p. 8921-8932 10.1063/1.1412609 0021-9606
    • (2001) J. Chem. Phys. , vol.115 , pp. 8921-8932
    • Popov, A.V.1    Agmon, N.2


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