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Volumn 7, Issue 3, 2012, Pages

Monitoring the size and lateral dynamics of erbb1 enriched membrane domains through live cell plasmon coupling microscopy

Author keywords

[No Author keywords available]

Indexed keywords

DENDRIMER; EPIDERMAL GROWTH FACTOR RECEPTOR; GOLD NANOPARTICLE; ANTIBODY; GOLD; METAL NANOPARTICLE;

EID: 84859047400     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0034175     Document Type: Article
Times cited : (13)

References (75)
  • 1
    • 33645130990 scopus 로고    scopus 로고
    • Signaling through ErbB receptors: Multiple layers of diversity and control
    • Warren CM, Landgraf R, (2006) Signaling through ErbB receptors: Multiple layers of diversity and control. Cellular Signalling 18: 923-933.
    • (2006) Cellular Signalling , vol.18 , pp. 923-933
    • Warren, C.M.1    Landgraf, R.2
  • 4
    • 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
  • 6
    • 34247230905 scopus 로고    scopus 로고
    • Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding
    • Clayton AHA, Tavarnesi ML, Johns TG, (2007) Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding. Biochemistry 46: 4589-4597.
    • (2007) Biochemistry , vol.46 , pp. 4589-4597
    • Clayton, A.H.A.1    Tavarnesi, M.L.2    Johns, T.G.3
  • 7
    • 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, et al. (2005) Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-a multidimensional microscopy analysis. Journal of Biological Chemistry 280: 30392-30399.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 30392-30399
    • Clayton, A.H.A.1    Walker, F.2    Orchard, S.G.3    Henderson, C.4    Fuchs, D.5
  • 8
    • 50349083489 scopus 로고    scopus 로고
    • Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements
    • Szabo A, Horvath G, Szollosi J, Nagy P, (2008) Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements. Biophysical Journal 95: 2086-2096.
    • (2008) Biophysical Journal , vol.95 , pp. 2086-2096
    • Szabo, A.1    Horvath, G.2    Szollosi, J.3    Nagy, P.4
  • 9
    • 77449085280 scopus 로고    scopus 로고
    • Nanoscale imaging of epidermal growth factor receptor clustering effects of inhibitors
    • Abulrob A, Lu Z, Baumann E, Vobornik D, Taylor R, et al. (2010) Nanoscale imaging of epidermal growth factor receptor clustering effects of inhibitors. Journal of Biological Chemistry 285: 3145-3156.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 3145-3156
    • Abulrob, A.1    Lu, Z.2    Baumann, E.3    Vobornik, D.4    Taylor, R.5
  • 10
    • 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, et al. (1999) Activation-dependent clustering of the ErbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. Journal of Cell Science 112: 1733-1741.
    • (1999) Journal of Cell Science , vol.112 , pp. 1733-1741
    • Nagy, P.1    Jenei, A.2    Kirsch, A.K.3    Szollosi, J.4    Damjanovich, S.5
  • 11
    • 34548555698 scopus 로고    scopus 로고
    • Mapping ErbB receptors on breast cancer cell membranes during signal transduction
    • Yang S, Raymond-Stintz MA, Ying W, Zhang J, Lidke DS, et al. (2007) Mapping ErbB receptors on breast cancer cell membranes during signal transduction. Journal of Cell Science 120: 2763-2773.
    • (2007) Journal of Cell Science , vol.120 , pp. 2763-2773
    • Yang, S.1    Raymond-Stintz, M.A.2    Ying, W.3    Zhang, J.4    Lidke, D.S.5
  • 12
    • 77955289201 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation
    • Ariotti N, Liang H, Xu YF, Zhang YQ, Yonekubo Y, et al. (2010) Epidermal growth factor receptor activation remodels the plasma membrane lipid environment to induce nanocluster formation. Molecular and Cellular Biology 30: 3795-3804.
    • (2010) Molecular and Cellular Biology , vol.30 , pp. 3795-3804
    • Ariotti, N.1    Liang, H.2    Xu, Y.F.3    Zhang, Y.Q.4    Yonekubo, Y.5
  • 15
    • 54049134792 scopus 로고    scopus 로고
    • Stochastic simulations of ErbB homo and heterodimerisation: Potential impacts of receptor conformational state and spatial segregation
    • Hsieh MY, Yang S, Raymond-Stinz MA, Steinberg S, Vlachos DG, et al. (2008) Stochastic simulations of ErbB homo and heterodimerisation: Potential impacts of receptor conformational state and spatial segregation. Iet Systems Biology 2: 256-272.
    • (2008) Iet Systems Biology , vol.2 , pp. 256-272
    • Hsieh, M.Y.1    Yang, S.2    Raymond-Stinz, M.A.3    Steinberg, S.4    Vlachos, D.G.5
  • 17
    • 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 DG, Edwards JS, (2005) Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding. FEBS Letters 579: 3043-3047.
    • (2005) FEBS Letters , vol.579 , pp. 3043-3047
    • Mayawala, K.1    Vlachos, D.G.2    Edwards, J.S.3
  • 18
    • 48749095948 scopus 로고    scopus 로고
    • Actin restricts FcεRI diffusion and facilitates antigen-induced receptor immobilization
    • Andrews NL, Lidke KA, Pfeiffer JR, Burns AR, Wilson BS, et al. (2008) Actin restricts FcεRI diffusion and facilitates antigen-induced receptor immobilization. Nature Cell Biology 10: 955-963.
    • (2008) Nature Cell Biology , vol.10 , pp. 955-963
    • Andrews, N.L.1    Lidke, K.A.2    Pfeiffer, J.R.3    Burns, A.R.4    Wilson, B.S.5
  • 19
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules
    • Kusumi A, Nakada C, Ritchie K, Murase K, Suzuki K, et al. (2005) Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules. Annual Review of Biophysics and Biomolecular Structure 34: 351-378.
    • (2005) Annual Review of Biophysics and Biomolecular Structure , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5
  • 21
    • 0024596077 scopus 로고
    • The spectrin network as a barrier to lateral diffusion in erythrocytes - a percolation analysis
    • Saxton MJ, (1989) The spectrin network as a barrier to lateral diffusion in erythrocytes- a percolation analysis. Biophysical Journal 55: 21-28.
    • (1989) Biophysical Journal , vol.55 , pp. 21-28
    • Saxton, M.J.1
  • 22
    • 0020790863 scopus 로고
    • Membrane skeletal dynamics - role in modulation of red-cell deformability, mobility of transmembrane proteins, and shape
    • Sheetz MP, (1983) Membrane skeletal dynamics- role in modulation of red-cell deformability, mobility of transmembrane proteins, and shape. Seminars in Hematology 20: 175-188.
    • (1983) Seminars in Hematology , vol.20 , pp. 175-188
    • Sheetz, M.P.1
  • 23
    • 0037216850 scopus 로고    scopus 로고
    • Lowering the barriers to random walks on the cell surface
    • Tang Q, Edidin M, (2003) Lowering the barriers to random walks on the cell surface. Biophysical Journal 84: 400-407.
    • (2003) Biophysical Journal , vol.84 , pp. 400-407
    • Tang, Q.1    Edidin, M.2
  • 24
    • 0022966969 scopus 로고
    • Restriction of the lateral motion of band-3 in the erythrocyte-membrane by the cytoskeletal network - dependence on spectrin association state
    • Tsuji A, Ohnishi S, (1986) Restriction of the lateral motion of band-3 in the erythrocyte-membrane by the cytoskeletal network- dependence on spectrin association state. Biochemistry 25: 6133-6139.
    • (1986) Biochemistry , vol.25 , pp. 6133-6139
    • Tsuji, A.1    Ohnishi, S.2
  • 25
    • 12344315828 scopus 로고    scopus 로고
    • Transient confinement zones: A type of lipid raft?
    • Chen Y, Yang B, Jacobson K, (2004) Transient confinement zones: A type of lipid raft? Lipids 39: 1115-1119.
    • (2004) Lipids , vol.39 , pp. 1115-1119
    • Chen, Y.1    Yang, B.2    Jacobson, K.3
  • 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, Sebestyen Z, Horvath G, Lockett SJ, et al. (2002) Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2. Journal of Cell Science 115: 4251-4262.
    • (2002) Journal of Cell Science , vol.115 , pp. 4251-4262
    • Nagy, P.1    Vereb, G.2    Sebestyen, Z.3    Horvath, G.4    Lockett, S.J.5
  • 28
    • 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, et al. (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
  • 29
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in t cells
    • Douglass AD, Vale RD, (2005) Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in t cells. Cell 121: 937-950.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 33
    • 0035207438 scopus 로고    scopus 로고
    • Cell biology beyond the diffraction limit: Near-field scanning optical microscopy
    • de Lange F, Cambi A, Huijbens R, de Bakker B, Rensen W, et al. (2001) Cell biology beyond the diffraction limit: Near-field scanning optical microscopy. Journal of Cell Science 114: 4153-4160.
    • (2001) Journal of Cell Science , vol.114 , pp. 4153-4160
    • de Lange, F.1    Cambi, A.2    Huijbens, R.3    de Bakker, B.4    Rensen, W.5
  • 34
    • 34249945258 scopus 로고    scopus 로고
    • Far-field optical nanoscopy
    • Hell SW, (2007) Far-field optical nanoscopy. Science 316: 1153-1158.
    • (2007) Science , vol.316 , pp. 1153-1158
    • Hell, S.W.1
  • 36
    • 74849096424 scopus 로고    scopus 로고
    • Insights from a nanoparticle minuet: Two-dimensional membrane profiling through silver plasmon ruler tracking
    • Rong GX, Wang HY, Reinhard BM, (2010) Insights from a nanoparticle minuet: Two-dimensional membrane profiling through silver plasmon ruler tracking. Nano Letters 10: 230-238.
    • (2010) Nano Letters , vol.10 , pp. 230-238
    • Rong, G.X.1    Wang, H.Y.2    Reinhard, B.M.3
  • 37
    • 56149123699 scopus 로고    scopus 로고
    • Resolving sub-diffraction limit encounters in nanoparticle tracking using live cell plasmon coupling microscopy
    • Rong GX, Wang HY, Skewis LR, Reinhard BM, (2008) Resolving sub-diffraction limit encounters in nanoparticle tracking using live cell plasmon coupling microscopy. Nano Letters 8: 3386-3393.
    • (2008) Nano Letters , vol.8 , pp. 3386-3393
    • Rong, G.X.1    Wang, H.Y.2    Skewis, L.R.3    Reinhard, B.M.4
  • 38
    • 67651094117 scopus 로고    scopus 로고
    • Monitoring simultaneous distance and orientation changes in discrete dimers of DNA linked gold nanoparticles
    • Wang HY, Reinhard BM, (2009) Monitoring simultaneous distance and orientation changes in discrete dimers of DNA linked gold nanoparticles. Journal of Physical Chemistry C 113: 11215-11222.
    • (2009) Journal of Physical Chemistry C , vol.113 , pp. 11215-11222
    • Wang, H.Y.1    Reinhard, B.M.2
  • 39
    • 77949797533 scopus 로고    scopus 로고
    • Calibration of silver plasmon rulers in the 1-25 nm separation range: Experimental indications of distinct plasmon coupling regimes
    • Yang LL, Wang HY, Yan B, Reinhard BM, (2010) Calibration of silver plasmon rulers in the 1-25 nm separation range: Experimental indications of distinct plasmon coupling regimes. Journal of Physical Chemistry C 114: 4901-4908.
    • (2010) Journal of Physical Chemistry C , vol.114 , pp. 4901-4908
    • Yang, L.L.1    Wang, H.Y.2    Yan, B.3    Reinhard, B.M.4
  • 40
    • 34948837408 scopus 로고    scopus 로고
    • Universal scaling of plasmon coupling in metal nanostructures: Extension from particle pairs to nanoshells
    • Jain PK, El-Sayed MA, (2007) Universal scaling of plasmon coupling in metal nanostructures: Extension from particle pairs to nanoshells. Nano Letters 7: 2854-2858.
    • (2007) Nano Letters , vol.7 , pp. 2854-2858
    • Jain, P.K.1    El-Sayed, M.A.2
  • 41
    • 0142011551 scopus 로고    scopus 로고
    • Interparticle coupling effects on plasmon resonances of nanogold particles
    • Su KH, Wei QH, Zhang X, Mock JJ, Smith DR, et al. (2003) Interparticle coupling effects on plasmon resonances of nanogold particles. Nano Letters 3: 1087-1090.
    • (2003) Nano Letters , vol.3 , pp. 1087-1090
    • Su, K.H.1    Wei, Q.H.2    Zhang, X.3    Mock, J.J.4    Smith, D.R.5
  • 42
    • 79851471478 scopus 로고    scopus 로고
    • Optical sizing of immunolabel clusters through multispectral plasmon coupling microscopy
    • Wang HY, Rong GX, Yan B, Yang LL, Reinhard BM, (2011) Optical sizing of immunolabel clusters through multispectral plasmon coupling microscopy. Nano Letters 11: 498-504.
    • (2011) Nano Letters , vol.11 , pp. 498-504
    • Wang, H.Y.1    Rong, G.X.2    Yan, B.3    Yang, L.L.4    Reinhard, B.M.5
  • 43
    • 80052059401 scopus 로고    scopus 로고
    • Illuminating epidermal growth factor receptor densities on filopodia through plasmon coupling
    • Wang J, Boriskina SV, Wang HY, 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.Y.3    Reinhard, B.M.4
  • 44
    • 72249099098 scopus 로고    scopus 로고
    • Dynamic imaging of molecular assemblies in live cells based on nanoparticle plasmon resonance coupling
    • Aaron J, Travis K, Harrison N, Sokolov K, (2009) Dynamic imaging of molecular assemblies in live cells based on nanoparticle plasmon resonance coupling. Nano Letters 9: 3612-3618.
    • (2009) Nano Letters , vol.9 , pp. 3612-3618
    • Aaron, J.1    Travis, K.2    Harrison, N.3    Sokolov, K.4
  • 45
    • 63849123029 scopus 로고    scopus 로고
    • Molecular imaging and quantitative measurement of epidermal growth factor receptor expression in live cancer cells using immunolabeled gold nanoparticles
    • Crow MJ, Grant G, Provenzale JM, Wax A, (2009) Molecular imaging and quantitative measurement of epidermal growth factor receptor expression in live cancer cells using immunolabeled gold nanoparticles. American Journal of Roentgenology 192: 1021-1028.
    • (2009) American Journal of Roentgenology , vol.192 , pp. 1021-1028
    • Crow, M.J.1    Grant, G.2    Provenzale, J.M.3    Wax, A.4
  • 46
    • 80655137897 scopus 로고    scopus 로고
    • Monitoring of receptor dimerization using plasmonic coupling of gold nanoparticles
    • Crow MJ, Seekell K, Ostrander JH, Wax A, (2011) Monitoring of receptor dimerization using plasmonic coupling of gold nanoparticles. ACS Nano 5: 8532-8540.
    • (2011) ACS Nano , vol.5 , pp. 8532-8540
    • Crow, M.J.1    Seekell, K.2    Ostrander, J.H.3    Wax, A.4
  • 47
    • 0032505018 scopus 로고    scopus 로고
    • Light-scattering submicroscopic particles as highly fluorescent analogs and their use as tracer labels in clinical and biological applications - ii. Experimental characterization
    • Yguerabide J, Yguerabide EE, (1998) Light-scattering submicroscopic particles as highly fluorescent analogs and their use as tracer labels in clinical and biological applications- ii. Experimental characterization. Analytical Biochemistry 262: 157-176.
    • (1998) Analytical Biochemistry , vol.262 , pp. 157-176
    • Yguerabide, J.1    Yguerabide, E.E.2
  • 48
    • 0032504940 scopus 로고    scopus 로고
    • Light-scattering submicroscopic particles as highly fluorescent analogs and their use as tracer labels in clinical and biological applications - i. Theory
    • Yguerabide J, Yguerabide EE, (1998) Light-scattering submicroscopic particles as highly fluorescent analogs and their use as tracer labels in clinical and biological applications- i. Theory. Analytical Biochemistry 262: 137-156.
    • (1998) Analytical Biochemistry , vol.262 , pp. 137-156
    • Yguerabide, J.1    Yguerabide, E.E.2
  • 50
    • 78650273375 scopus 로고    scopus 로고
    • A simple backscattering microscope for fast tracking of biological molecules
    • Sowa Y, Steel BC, Berry RM, (2010) A simple backscattering microscope for fast tracking of biological molecules. Review of Scientific Instruments 81: 113704.
    • (2010) Review of Scientific Instruments , vol.81 , pp. 113704
    • Sowa, Y.1    Steel, B.C.2    Berry, R.M.3
  • 51
    • 77952262873 scopus 로고    scopus 로고
    • Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution
    • Ueno H, Nishikawa S, Iino R, Tabata KV, Sakakihara S, et al. (2010) Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution. Biophysical Journal 98: 2014-2023.
    • (2010) Biophysical Journal , vol.98 , pp. 2014-2023
    • Ueno, H.1    Nishikawa, S.2    Iino, R.3    Tabata, K.V.4    Sakakihara, S.5
  • 52
    • 64849093051 scopus 로고    scopus 로고
    • Single nanoparticle tracking-based detection of membrane receptor-ligand interactions
    • Yang Y-H, Nam J-M, (2009) Single nanoparticle tracking-based detection of membrane receptor-ligand interactions. Analytical Chemistry 81: 2564-2568.
    • (2009) Analytical Chemistry , vol.81 , pp. 2564-2568
    • Yang, Y.-H.1    Nam, J.-M.2
  • 53
    • 2942662120 scopus 로고    scopus 로고
    • Ultrafine membrane compartments for molecular diffusion as revealed by single molecule techniques
    • Murase K, Fujiwara T, Umemura Y, Suzuki K, Iino R, et al. (2004) Ultrafine membrane compartments for molecular diffusion as revealed by single molecule techniques. Biophysical Journal 86: 4075-4093.
    • (2004) Biophysical Journal , vol.86 , pp. 4075-4093
    • Murase, K.1    Fujiwara, T.2    Umemura, Y.3    Suzuki, K.4    Iino, R.5
  • 54
    • 17844389341 scopus 로고    scopus 로고
    • Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques
    • Suzuki K, Ritchie K, Kajikawa E, Fujiwara T, Kusumi A, (2005) Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques. Biophysical Journal 88: 3659-3680.
    • (2005) Biophysical Journal , vol.88 , pp. 3659-3680
    • Suzuki, K.1    Ritchie, K.2    Kajikawa, E.3    Fujiwara, T.4    Kusumi, A.5
  • 55
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets ED, Lee GM, Simson R, Jacobson K, (1997) Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane. Biochemistry 36: 12449-12458.
    • (1997) Biochemistry , vol.36 , pp. 12449-12458
    • Sheets, E.D.1    Lee, G.M.2    Simson, R.3    Jacobson, K.4
  • 57
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • Prescher JA, Dube DH, Bertozzi CR, (2004) Chemical remodelling of cell surfaces in living animals. Nature 430: 873-877.
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1    Dube, D.H.2    Bertozzi, C.R.3
  • 58
    • 0023082137 scopus 로고
    • Receptors for epidermal growth-factor and other polypeptide mitogens
    • Carpenter G, (1987) Receptors for epidermal growth-factor and other polypeptide mitogens. Annual Review of Biochemistry 56: 881-914.
    • (1987) Annual Review of Biochemistry , vol.56 , pp. 881-914
    • Carpenter, G.1
  • 59
    • 0037213006 scopus 로고    scopus 로고
    • Computational modeling of the EGF-receptor system: A paradigm for systems biology
    • Wiley HS, Shvartsman SY, Lauffenburger DA, (2003) Computational modeling of the EGF-receptor system: A paradigm for systems biology. Trends in Cell Biology 13: 43-50.
    • (2003) Trends in Cell Biology , vol.13 , pp. 43-50
    • Wiley, H.S.1    Shvartsman, S.Y.2    Lauffenburger, D.A.3
  • 61
    • 0032696038 scopus 로고    scopus 로고
    • Regulated migration of epidermal growth factor receptor from caveolae
    • Mineo C, Gill GN, Anderson GW, (1999) Regulated migration of epidermal growth factor receptor from caveolae. Journal of Biological Chemistry 274: 30636-30643.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 30636-30643
    • Mineo, C.1    Gill, G.N.2    Anderson, G.W.3
  • 62
    • 0037166323 scopus 로고    scopus 로고
    • Sequestration of epidermal growth factor receptors in non-caveolar lipid rafts inhibits ligand binding
    • Roepstorff K, Thomsen P, Sandvig K, van Deurs B, (2002) Sequestration of epidermal growth factor receptors in non-caveolar lipid rafts inhibits ligand binding. Journal of Biological Chemistry 277: 18954-18960.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 18954-18960
    • Roepstorff, K.1    Thomsen, P.2    Sandvig, K.3    van Deurs, B.4
  • 63
    • 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. Biophysical Journal 93: 1021-1031.
    • (2007) Biophysical Journal , vol.93 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pike, L.J.4
  • 64
    • 28144465612 scopus 로고    scopus 로고
    • Calibration of dynamic molecular rule based on plasmon coupling between gold nanoparticles
    • Reinhard BM, Siu M, Agarwal H, Alivisatos AP, Liphardt J, (2005) Calibration of dynamic molecular rule based on plasmon coupling between gold nanoparticles. Nano Letters 5: 2246-2252.
    • (2005) Nano Letters , vol.5 , pp. 2246-2252
    • Reinhard, B.M.1    Siu, M.2    Agarwal, H.3    Alivisatos, A.P.4    Liphardt, J.5
  • 65
    • 79952843405 scopus 로고    scopus 로고
    • Optimizing gold nanoparticle cluster configurations (n< = 7) for array applications
    • Yan B, Boriskina SV, Reinhard BM, (2011) Optimizing gold nanoparticle cluster configurations (n< = 7) for array applications. Journal of Physical Chemistry C 115: 4578-4583.
    • (2011) Journal of Physical Chemistry C , vol.115 , pp. 4578-4583
    • Yan, B.1    Boriskina, S.V.2    Reinhard, B.M.3
  • 66
    • 84857263854 scopus 로고    scopus 로고
    • Design and implementation of noble metal nanoparticle cluster arrays for plasmon enhanced biosensing
    • Yan B, Boriskina SV, Reinhard BM, (2011) Design and implementation of noble metal nanoparticle cluster arrays for plasmon enhanced biosensing. Journal of Physical Chemistry C 115: 24437-24453.
    • (2011) Journal of Physical Chemistry C , vol.115 , pp. 24437-24453
    • Yan, B.1    Boriskina, S.V.2    Reinhard, B.M.3
  • 69
    • 35948993741 scopus 로고    scopus 로고
    • Determining if a system is heterogeneous: The analysis of single molecule rotational correlation functions and their limitations
    • Wei CYJ, Lu CY, Kim YH, Bout DAV, (2007) Determining if a system is heterogeneous: The analysis of single molecule rotational correlation functions and their limitations. Journal of Fluorescence 17: 797-804.
    • (2007) Journal of Fluorescence , vol.17 , pp. 797-804
    • Wei, C.Y.J.1    Lu, C.Y.2    Kim, Y.H.3    Bout, D.A.V.4
  • 70
    • 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
    • Kusumi A, Sako Y, Yamamoto M, (1993) Confined lateral diffusion of membrane-receptors as studied by single-particle tracking (nanovid microscopy)- effects of calcium-induced differentiation in cultured epithelial-cells. Biophysical Journal 65: 2021-2040.
    • (1993) Biophysical Journal , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 71
    • 23244442694 scopus 로고    scopus 로고
    • Cholesterol dictates the freedom of EGF receptors and HER2 in the plane of the membrane
    • Orr G, Hu DH, Ozcelik S, Opresko LK, Wiley HS, et al. (2005) Cholesterol dictates the freedom of EGF receptors and HER2 in the plane of the membrane. Biophysical Journal 89: 1362-1373.
    • (2005) Biophysical Journal , vol.89 , pp. 1362-1373
    • Orr, G.1    Hu, D.H.2    Ozcelik, S.3    Opresko, L.K.4    Wiley, H.S.5
  • 73
    • 0031958201 scopus 로고    scopus 로고
    • Structure of the erythrocyte membrane skeleton as observed by atomic force microscopy
    • Takeuchi M, Miyamoto H, Sako Y, Komizu H, Kusumi A, (1998) Structure of the erythrocyte membrane skeleton as observed by atomic force microscopy. Biophysical Journal 74: 2171-2183.
    • (1998) Biophysical Journal , vol.74 , pp. 2171-2183
    • Takeuchi, M.1    Miyamoto, H.2    Sako, Y.3    Komizu, H.4    Kusumi, A.5
  • 74
    • 78651304653 scopus 로고    scopus 로고
    • Mean square displacement analysis of single-particle trajectories with localization error: Brownian motion in an isotropic medium
    • Michalet X, (2010) Mean square displacement analysis of single-particle trajectories with localization error: Brownian motion in an isotropic medium. Physical Review E 82: 041914.
    • (2010) Physical Review E , vol.82 , pp. 041914
    • Michalet, X.1


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