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Volumn 88, Issue 6, 2005, Pages 4289-4302

Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2 INTERFERON; INTERFERON RECEPTOR; LIGAND; RECEPTOR SUBUNIT;

EID: 20444452736     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.055855     Document Type: Article
Times cited : (92)

References (50)
  • 1
    • 0003064682 scopus 로고
    • Reduction of dimensionality in biological diffusion processes
    • N. Davidson, editor. W. H. Freeman, New York, NY
    • Adam, G., and M. Delbruck. 1968. Reduction of dimensionality in biological diffusion processes. In Structural Chemistry and Molecular Biology. N. Davidson, editor. W. H. Freeman, New York, NY. 198-215.
    • (1968) Structural Chemistry and Molecular Biology , pp. 198-215
    • Adam, G.1    Delbruck, M.2
  • 3
    • 0028295474 scopus 로고
    • Reduction-of-dimensionality kinetics at reaction-limited cell surface receptors
    • Axelrod, D., and M. D. Wang. 1994. Reduction-of-dimensionality kinetics at reaction-limited cell surface receptors. Biophys. J. 66:588-600.
    • (1994) Biophys. J. , vol.66 , pp. 588-600
    • Axelrod, D.1    Wang, M.D.2
  • 4
    • 0000944250 scopus 로고
    • Allogeneic stimulation of cytotoxic T cells by supported planar membranes
    • Brian, A. A., and H. M. McConnell. 1984. Allogeneic stimulation of cytotoxic T cells by supported planar membranes. Proc. Natl. Acad. Sci. USA. 81:6159-6163.
    • (1984) Proc. Natl. Acad. Sci. USA. , vol.81 , pp. 6159-6163
    • Brian, A.A.1    McConnell, H.M.2
  • 5
    • 0037632418 scopus 로고    scopus 로고
    • The human type I Interferon receptor. NMR structure reveals the molecular basis of ligand binding
    • Chill, J. H., S. R. Quadt, R. Levy, G. Schreiber, and J. Anglister. 2003. The human type I Interferon receptor. NMR structure reveals the molecular basis of ligand binding. Structure (Camb). 11:791-802.
    • (2003) Structure (Camb) , vol.11 , pp. 791-802
    • Chill, J.H.1    Quadt, S.R.2    Levy, R.3    Schreiber, G.4    Anglister, J.5
  • 6
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham, B. C., M. Ultsch, A. M. De Vos, M. G. Mulkerrin, K. R. Clauser, and J. A. Wells. 1991. Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science. 254:821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 7
    • 0031042220 scopus 로고    scopus 로고
    • Contributions of cloned type I interferon receptor subunits to differential ligand binding
    • Cutrone, E. C., and J. A. Langer. 1997. Contributions of cloned type I interferon receptor subunits to differential ligand binding. FEBS Lett. 404:197-202.
    • (1997) FEBS Lett. , vol.404 , pp. 197-202
    • Cutrone, E.C.1    Langer, J.A.2
  • 8
    • 0019018575 scopus 로고
    • The biophysics of ligand-receptor interactions
    • DeLisi, C. 1980. The biophysics of ligand-receptor interactions. Q. Rev. Biophys. 13:201-230.
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 201-230
    • Delisi, C.1
  • 9
    • 0031696253 scopus 로고    scopus 로고
    • Orientation and two-dimensional organization of proteins at chelator lipid interfaces
    • Dorn, I. T., K. Pawlitschko, S. C. Pettinger, and R. Tampe. 1998. Orientation and two-dimensional organization of proteins at chelator lipid interfaces. Biol. Chem. 379:1151-1159.
    • (1998) Biol. Chem. , vol.379 , pp. 1151-1159
    • Dorn, I.T.1    Pawlitschko, K.2    Pettinger, S.C.3    Tampe, R.4
  • 10
    • 0023489716 scopus 로고
    • Direct immunochemical sensing: Basic chemical principles and fundamental limitations
    • Eddowes, M. J. 1987. Direct immunochemical sensing: basic chemical principles and fundamental limitations. Biosensors. 3:1-15.
    • (1987) Biosensors , vol.3 , pp. 1-15
    • Eddowes, M.J.1
  • 11
  • 12
    • 0031309847 scopus 로고    scopus 로고
    • Antibody binding to a functionalized supported lipid layer: A direct acoustic immunosensor
    • Gizeli, E., M. Liley, C. R. Lowe, and H. Vogel. 1997. Antibody binding to a functionalized supported lipid layer: a direct acoustic immunosensor. Anal. Chem. 69:4808-4813.
    • (1997) Anal. Chem. , vol.69 , pp. 4808-4813
    • Gizeli, E.1    Liley, M.2    Lowe, C.R.3    Vogel, H.4
  • 13
    • 0027198367 scopus 로고
    • Antigen-antibody binding and mass transport by convection and diffusion to a surface: A two-dimensional computer model of binding and dissociation kinetics
    • Glaser, R. W. 1993. Antigen-antibody binding and mass transport by convection and diffusion to a surface: a two-dimensional computer model of binding and dissociation kinetics. Anal. Biochem. 213:152-161.
    • (1993) Anal. Biochem. , vol.213 , pp. 152-161
    • Glaser, R.W.1
  • 14
    • 0037064537 scopus 로고    scopus 로고
    • Molecular mechanisms of cytokine receptor activation
    • Grotzinger, J. 2002. Molecular mechanisms of cytokine receptor activation. Biochim. Biophys. Acta. 1592:215-223.
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 215-223
    • Grotzinger, J.1
  • 16
    • 0034157863 scopus 로고    scopus 로고
    • Label-free detection of biomolecular interaction by optical sensors
    • Haake, H. M., A. Schutz, and G. Gauglitz. 2000. Label-free detection of biomolecular interaction by optical sensors. Fresenius J. Anal. Chem. 366:576-585.
    • (2000) Fresenius J. Anal. Chem. , vol.366 , pp. 576-585
    • Haake, H.M.1    Schutz, A.2    Gauglitz, G.3
  • 17
    • 0036194547 scopus 로고    scopus 로고
    • Comparison of reflectometric interference spectroscopy with other instruments for label-free optical detection
    • Hanel, C., and G. Gauglitz. 2002. Comparison of reflectometric interference spectroscopy with other instruments for label-free optical detection. Anal. Bioanal. Chem. 372:91-100.
    • (2002) Anal. Bioanal. Chem. , vol.372 , pp. 91-100
    • Hanel, C.1    Gauglitz, G.2
  • 18
    • 0000291826 scopus 로고
    • Rates of diffusion controlled reactions in one, two and three dimensions
    • Hardt, S. L. 1979. Rates of diffusion controlled reactions in one, two and three dimensions. Biophys. Chem. 10:239-243.
    • (1979) Biophys. Chem. , vol.10 , pp. 239-243
    • Hardt, S.L.1
  • 19
    • 0031679214 scopus 로고    scopus 로고
    • Surface specific kinetics of lipid vesicle adsorption measured with a quartz crystal microbalance
    • Keller, C. A., and B. Kasemo. 1998. Surface specific kinetics of lipid vesicle adsorption measured with a quartz crystal microbalance. Biophys. J. 75:1397-1402.
    • (1998) Biophys. J. , vol.75 , pp. 1397-1402
    • Keller, C.A.1    Kasemo, B.2
  • 20
    • 32744474208 scopus 로고
    • Physical properties of chick interferon
    • Kreuz, L. E., and A. H. Levy. 1965. Physical properties of chick interferon. J. Bacteriol. 89:462-469.
    • (1965) J. Bacteriol. , vol.89 , pp. 462-469
    • Kreuz, L.E.1    Levy, A.H.2
  • 21
    • 0031910469 scopus 로고    scopus 로고
    • Theory for ligand rebinding at cell membrane surfaces
    • Lagerholm, B. C., and N. L. Thompson. 1998. Theory for ligand rebinding at cell membrane surfaces. Biophys. J. 74:1215-1228.
    • (1998) Biophys. J. , vol.74 , pp. 1215-1228
    • Lagerholm, B.C.1    Thompson, N.L.2
  • 22
    • 4143062575 scopus 로고    scopus 로고
    • Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers
    • Lamken, P., S. Lata, M. Gavutis, and J. Piehler. 2004. Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers. J. Mol. Biol. 341:303-318.
    • (2004) J. Mol. Biol. , vol.341 , pp. 303-318
    • Lamken, P.1    Lata, S.2    Gavutis, M.3    Piehler, J.4
  • 23
    • 13844263242 scopus 로고    scopus 로고
    • Stable and functional immobilization of histidine-tagged proteins via multivalent chelator head-groups on a molecular poly(ethylene glycol) brush
    • Lata, S., and J. Piehler. 2005. Stable and functional immobilization of histidine-tagged proteins via multivalent chelator head-groups on a molecular poly(ethylene glycol) brush. Anal. Chem. 77:1096-1105.
    • (2005) Anal. Chem. , vol.77 , pp. 1096-1105
    • Lata, S.1    Piehler, J.2
  • 24
    • 0032188943 scopus 로고    scopus 로고
    • The interleukin-4 site-2 epitope determining binding of the common receptor gamma chain
    • Letzeiter, F., Y. Wang, and W. Sebald. 1998. The interleukin-4 site-2 epitope determining binding of the common receptor gamma chain. Eur. J. Biochem. 257:11-20.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 11-20
    • Letzeiter, F.1    Wang, Y.2    Sebald, W.3
  • 25
    • 0034634053 scopus 로고    scopus 로고
    • Surface-plasmon field-enhanced fluorescence spectroscopy
    • Liebermann, T., and W. Knoll. 2000. Surface-plasmon field-enhanced fluorescence spectroscopy. Colloids Surf. A. 171:115-130.
    • (2000) Colloids Surf. A , vol.171 , pp. 115-130
    • Liebermann, T.1    Knoll, W.2
  • 26
    • 0141503495 scopus 로고    scopus 로고
    • Quartz crystal microbalance: A useful tool for studying thin polymer films and complex biomolecular systems at the solution-surface interface
    • Marx, K. A. 2003. Quartz crystal microbalance: a useful tool for studying thin polymer films and complex biomolecular systems at the solution-surface interface. Biomacromolecules. 4:1099-1120.
    • (2003) Biomacromolecules , vol.4 , pp. 1099-1120
    • Marx, K.A.1
  • 29
    • 0034704093 scopus 로고    scopus 로고
    • New structural and functional aspects of the type I interferon-receptor interaction revealed by comprehensive mutational analysis of the binding interface
    • Piehler, J., L. C. Roisman, and G. Schreiber. 2000. New structural and functional aspects of the type I interferon-receptor interaction revealed by comprehensive mutational analysis of the binding interface. J. Biol. Chem. 275:40425-40433.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40425-40433
    • Piehler, J.1    Roisman, L.C.2    Schreiber, G.3
  • 30
    • 0033612226 scopus 로고    scopus 로고
    • Biophysical analysis of the interaction of human ifnar2 expressed in E-coli with IFN alpha 2
    • Piehler, J., and G. Schreiber. 1999. Biophysical analysis of the interaction of human ifnar2 expressed in E-coli with IFN alpha 2. J. Mol. Biol. 289:57-67.
    • (1999) J. Mol. Biol. , vol.289 , pp. 57-67
    • Piehler, J.1    Schreiber, G.2
  • 31
    • 0035865267 scopus 로고    scopus 로고
    • Fast transient cytokine-receptor interactions monitored in real time by reflectometric interference spectroscopy
    • Piehler, J., and G. Schreiber. 2001. Fast transient cytokine-receptor interactions monitored in real time by reflectometric interference spectroscopy. Anal. Biochem. 289:173-186.
    • (2001) Anal. Biochem. , vol.289 , pp. 173-186
    • Piehler, J.1    Schreiber, G.2
  • 32
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, J., I. A. Wilson, and S. W. Michnick. 1999. Erythropoietin receptor activation by a ligand-induced conformation change. Science. 283:990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, J.1    Wilson, I.A.2    Michnick, S.W.3
  • 33
    • 0346997045 scopus 로고    scopus 로고
    • The fence and picket structure of the plasma membrane of live cells as revealed by single molecule techniques
    • Ritchie, K., R. Iino, T. Fujiwara, K. Murase, and A. Kusumi. 2003. The fence and picket structure of the plasma membrane of live cells as revealed by single molecule techniques (Review). Mol. Membr. Biol. 20:13-18.
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 13-18
    • Ritchie, K.1    Iino, R.2    Fujiwara, T.3    Murase, K.4    Kusumi, A.5
  • 34
    • 0035818558 scopus 로고    scopus 로고
    • Structure of the interferon-receptor complex determined by distance constraints from double-mutant cycles and flexible docking
    • Roisman, L. C., J. Piehler, J. Y. Trosset, H. A. Scheraga, and G. Schreiber. 2001. Structure of the interferon-receptor complex determined by distance constraints from double-mutant cycles and flexible docking. Proc. Natl. Acad. Sci. USA. 98:13231-13236.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13231-13236
    • Roisman, L.C.1    Piehler, J.2    Trosset, J.Y.3    Scheraga, H.A.4    Schreiber, G.5
  • 35
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: Scientific and practical applications
    • Sackmann, E. 1996. Supported membranes: scientific and practical applications. Science. 271:43-48.
    • (1996) Science , vol.271 , pp. 43-48
    • Sackmann, E.1
  • 36
    • 0032055436 scopus 로고    scopus 로고
    • Screening ligands for membrane protein receptors by total internal reflection fluorescence: The 5-HT3 serotonin receptor
    • Schmid, E. L., A. P. Tain, R. Hovius, and H. Vogel. 1998. Screening ligands for membrane protein receptors by total internal reflection fluorescence: the 5-HT3 serotonin receptor. Anal. Chem. 70:1331-1338.
    • (1998) Anal. Chem. , vol.70 , pp. 1331-1338
    • Schmid, E.L.1    Tain, A.P.2    Hovius, R.3    Vogel, H.4
  • 37
    • 0028150044 scopus 로고
    • Synthesis and characterization of chelator-lipids for reversible immobilization of engineered proteins at self-assembled lipid interfaces
    • Schmitt, L., C. Dietrich, and R. Tampe. 1994. Synthesis and characterization of chelator-lipids for reversible immobilization of engineered proteins at self-assembled lipid interfaces. J. Am. Chem. Soc. 116: 8485-8491.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8485-8491
    • Schmitt, L.1    Dietrich, C.2    Tampe, R.3
  • 38
    • 0030571002 scopus 로고    scopus 로고
    • Analysis of mass transport-limited binding kinetics in evanescent wave biosensors
    • Schuck, P., and A. P. Minton. 1996. Analysis of mass transport-limited binding kinetics in evanescent wave biosensors. Anal. Biochem. 240: 262-272.
    • (1996) Anal. Biochem. , vol.240 , pp. 262-272
    • Schuck, P.1    Minton, A.P.2
  • 39
    • 0642285636 scopus 로고    scopus 로고
    • The interaction of BMP-7 and ActRII implicates a new mode of receptor assembly
    • Sebald, W., and T. D. Mueller. 2003. The interaction of BMP-7 and ActRII implicates a new mode of receptor assembly. Trends Biochem. Sci. 28: 518-521.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 518-521
    • Sebald, W.1    Mueller, T.D.2
  • 40
    • 2442459084 scopus 로고    scopus 로고
    • Plasma membrane rafts and chaperones in cytokine/STAT signaling
    • Sehgal, P. B. 2003. Plasma membrane rafts and chaperones in cytokine/ STAT signaling. Acta Biochim. Pol. 50:583-594.
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 583-594
    • Sehgal, P.B.1
  • 41
    • 2442716797 scopus 로고    scopus 로고
    • Mechanistic diversity of cytokine receptor signaling across cell membranes
    • Stroud, R. M., and J. A. Wells. 2004. Mechanistic diversity of cytokine receptor signaling across cell membranes. Sci. STKE. 2004:re7.
    • (2004) Sci. STKE , vol.2004
    • Stroud, R.M.1    Wells, J.A.2
  • 42
    • 0034733672 scopus 로고    scopus 로고
    • Cross talk between interferon-gamma and -alpha/beta signaling components in caveolar membrane domains
    • Takaoka, A., Y. Mitani, H. Suemori, M. Sato, T. Yokochi, S. Noguchi, N. Tanaka, and T. Taniguchi. 2000. Cross talk between interferon-gamma and -alpha/beta signaling components in caveolar membrane domains. Science. 288:2357-2360.
    • (2000) Science , vol.288 , pp. 2357-2360
    • Takaoka, A.1    Mitani, Y.2    Suemori, H.3    Sato, M.4    Yokochi, T.5    Noguchi, S.6    Tanaka, N.7    Taniguchi, T.8
  • 43
    • 0020794259 scopus 로고
    • Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy
    • Thompson, N. L., and D. Axelrod. 1983. Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy. Biophys. J. 43:103-114.
    • (1983) Biophys. J. , vol.43 , pp. 103-114
    • Thompson, N.L.1    Axelrod, D.2
  • 44
    • 0031051658 scopus 로고    scopus 로고
    • Equilibrium, kinetics, diffusion and self-association of proteins at membrane surfaces: Measurement by total internal reflection fluorescence microscopy
    • Thompson, N. L., A. W. Drake, L. Chen, and W. Vanden Broek. 1997. Equilibrium, kinetics, diffusion and self-association of proteins at membrane surfaces: measurement by total internal reflection fluorescence microscopy. Photochem. Photobiol. 65:39-46.
    • (1997) Photochem. Photobiol. , vol.65 , pp. 39-46
    • Thompson, N.L.1    Drake, A.W.2    Chen, L.3    Vanden Broek, W.4
  • 45
    • 0031015134 scopus 로고    scopus 로고
    • Total internal reflection fluorescence: Applications in cellular biophysics
    • Thompson, N. L., and B. C. Lagerholm. 1997. Total internal reflection fluorescence: applications in cellular biophysics. Curr. Opin. Biotechnol. 8:58-64.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 58-64
    • Thompson, N.L.1    Lagerholm, B.C.2
  • 46
    • 0027525336 scopus 로고
    • Total internal reflection fluorescence microscopy: Application to substrate-supported planar membranes
    • Thompson, N. L., K. H. Pearce, and H. V. Hsieh. 1993. Total internal reflection fluorescence microscopy: application to substrate-supported planar membranes. Eur. Biophys. J. 22:367-378.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 367-378
    • Thompson, N.L.1    Pearce, K.H.2    Hsieh, H.V.3
  • 47
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A., and J. Schlessinger. 1990. Signal transduction by receptors with tyrosine kinase activity. Cell. 61:203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 48
    • 0011328355 scopus 로고    scopus 로고
    • When bivalent proteins might walk across cell surfaces
    • Vanden Broek, W., and N. L. Thompson. 1996. When bivalent proteins might walk across cell surfaces. J. Phys. Chem. 100:11471-11479.
    • (1996) J. Phys. Chem. , vol.100 , pp. 11471-11479
    • Vanden Broek, W.1    Thompson, N.L.2
  • 49
    • 0026690869 scopus 로고
    • Reaction rate enhancement by surface diffusion of adsorbates
    • Wang, D., S. Y. Gou, and D. Axelrod. 1992. Reaction rate enhancement by surface diffusion of adsorbates. Biophys. Chem. 43:117-137.
    • (1992) Biophys. Chem. , vol.43 , pp. 117-137
    • Wang, D.1    Gou, S.Y.2    Axelrod, D.3


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