메뉴 건너뛰기




Volumn 92, Issue 9, 2007, Pages 3098-3104

Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: Theory and application

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN;

EID: 34247599842     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.099424     Document Type: Article
Times cited : (84)

References (30)
  • 1
    • 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
  • 2
    • 0026675654 scopus 로고
    • Transmembrane signaling: The joy of aggregation
    • Metzger, H. 1992. Transmembrane signaling: the joy of aggregation. J. Immunol. 149:1477-1487.
    • (1992) J. Immunol , vol.149 , pp. 1477-1487
    • Metzger, H.1
  • 3
    • 0023156382 scopus 로고
    • Self-phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation
    • Yarden, Y., and J. Schlessinger. 1987. Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation. Biochemistry. 26:1434-1442.
    • (1987) Biochemistry , vol.26 , pp. 1434-1442
    • Yarden, Y.1    Schlessinger, J.2
  • 4
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye, M. A., R. M. Neve, H. A. Lane, and N. E. Hynes. 2000. The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J. 19:3159-3167.
    • (2000) EMBO J , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 5
    • 0024392570 scopus 로고
    • Rotational and translational diffusion in membranes measured by fluorescence and phosphorescence methods
    • Jovin, T. M., and W. L. Vaz. 1989. Rotational and translational diffusion in membranes measured by fluorescence and phosphorescence methods. Methods Enzymol. 172:471-513.
    • (1989) Methods Enzymol , vol.172 , pp. 471-513
    • Jovin, T.M.1    Vaz, W.L.2
  • 6
    • 0347741641 scopus 로고    scopus 로고
    • Analysis of membrane protein cluster densities and sizes in situ by image correlation spectroscopy
    • Petersen, N., C. Brown, A. Kaminski, J. Rocheleau, M. Srivastava, and P. W. Wiseman. 1998. Analysis of membrane protein cluster densities and sizes in situ by image correlation spectroscopy. Faraday Discuss. 111:289-305.
    • (1998) Faraday Discuss , vol.111 , pp. 289-305
    • Petersen, N.1    Brown, C.2    Kaminski, A.3    Rocheleau, J.4    Srivastava, M.5    Wiseman, P.W.6
  • 7
    • 0035984645 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy for the detection and study of single molecules in biology
    • Medina, M. A., and P. Schwille. 2002. Fluorescence correlation spectroscopy for the detection and study of single molecules in biology. Bioessays. 24:758-764.
    • (2002) Bioessays , vol.24 , pp. 758-764
    • Medina, M.A.1    Schwille, P.2
  • 10
    • 76949127690 scopus 로고
    • Polarization of the fluorescence of macromolecules. I. Theory and experimental method
    • Weber, G. 1952. Polarization of the fluorescence of macromolecules. I. Theory and experimental method. Biochem. J. 51:145-155.
    • (1952) Biochem. J , vol.51 , pp. 145-155
    • Weber, G.1
  • 11
    • 34250910546 scopus 로고
    • Über den einflub der konzentration auf die polarization der fluoreszenz von fartstoffosungen
    • Gaviola, E., and P. Pringsheim. 1924. Über den einflub der konzentration auf die polarization der fluoreszenz von fartstoffosungen Z. Physik. 1:24-36.
    • (1924) Z. Physik , vol.1 , pp. 24-36
    • Gaviola, E.1    Pringsheim, P.2
  • 13
    • 0000556311 scopus 로고    scopus 로고
    • The dynamics of electronic energy transfer in novel multiporphytin functionalized dendrimers: A time-resolved fluorescence anisotropy study
    • Yeow, E. K. L., K. P. Ghiggino, J. N. H. Reek, M. J. Crossley, A. W. Bosman, A. P. H. J. Schenning, and E. W. Meijer. 2000. The dynamics of electronic energy transfer in novel multiporphytin functionalized dendrimers: a time-resolved fluorescence anisotropy study. J. Phys. Chem. B. 104:2596-2606.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 2596-2606
    • Yeow, E.K.L.1    Ghiggino, K.P.2    Reek, J.N.H.3    Crossley, M.J.4    Bosman, A.W.5    Schenning, A.P.H.J.6    Meijer, E.W.7
  • 14
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • Runnels, L. W., and S. F. Scarlata. 1995. Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys. J. 69:1569-1583.
    • (1995) Biophys. J , vol.69 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 15
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and S. Mayor. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 16
    • 0031870450 scopus 로고    scopus 로고
    • Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer
    • Blackman, S. M., D. W. Piston, and A. H. Beth. 1998. Oligomeric state of human erythrocyte band 3 measured by fluorescence resonance energy homotransfer. Biophys. J. 75:1117-1130.
    • (1998) Biophys. J , vol.75 , pp. 1117-1130
    • Blackman, S.M.1    Piston, D.W.2    Beth, A.H.3
  • 17
    • 0028359878 scopus 로고
    • Glycophorin A helical transmembrane domains dimerize in phospholipid bilayers: A resonance energy transfer study
    • Adair, B. D., and D. M. Engelman. 1994. Glycophorin A helical transmembrane domains dimerize in phospholipid bilayers: a resonance energy transfer study. Biochemistry. 33:5539-5544.
    • (1994) Biochemistry , vol.33 , pp. 5539-5544
    • Adair, B.D.1    Engelman, D.M.2
  • 18
    • 0032575512 scopus 로고    scopus 로고
    • Membrane-mediated assembly of annexins studied by site-directed spin labeling
    • Langen, R., J. M. Isas, H. Luecke, H. T. Haigler, and W. L. Hubbell. 1998. Membrane-mediated assembly of annexins studied by site-directed spin labeling. J. Biol. Chem. 273:22453-22457.
    • (1998) J. Biol. Chem , vol.273 , pp. 22453-22457
    • Langen, R.1    Isas, J.M.2    Luecke, H.3    Haigler, H.T.4    Hubbell, W.L.5
  • 19
    • 85030513909 scopus 로고    scopus 로고
    • Joseph, R. Lakowicz 1999, Principles of Fluorescence Spectroscopy. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Joseph, R. Lakowicz 1999, Principles of Fluorescence Spectroscopy. Kluwer Academic Publishers, Dordrecht, The Netherlands.
  • 20
    • 5644226253 scopus 로고    scopus 로고
    • Dynamic and static fluorescence anisotropy in biological microscopy (rFcim and emFret)
    • Jovin, T. M., D. S. Lidke, and J. N. Post. 2004. Dynamic and static fluorescence anisotropy in biological microscopy (rFcim and emFret). SPIE Proc. 5323:1-12.
    • (2004) SPIE Proc , vol.5323 , pp. 1-12
    • Jovin, T.M.1    Lidke, D.S.2    Post, J.N.3
  • 23
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma, P., R. Varma, R. C. Sarasij, K. Gousset, G. Krishnamoorthy, M. Rao, and S. Mayor. 2004. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell. 116:577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Gousset, K.4    Krishnamoorthy, G.5    Rao, M.6    Mayor, S.7
  • 26
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki, T., H. Maruyama, I.N. Maruyama. 2001. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J. Mol. Biol. 311:1011-1026.
    • (2001) J. Mol. Biol , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 27
    • 0346875543 scopus 로고    scopus 로고
    • Optical bioimaging: From living tissue to a single molecule: single-molecule visualization of cell signaling processes of epidermal growth factor receptor
    • Sako, Y., J. Ichinose, M. Morimatsu, K. Ohta, and T. Uyemura. 2003. Optical bioimaging: from living tissue to a single molecule: single-molecule visualization of cell signaling processes of epidermal growth factor receptor. J. Pharmacol. Sci. 93:253-258.
    • (2003) J. Pharmacol. Sci , vol.93 , pp. 253-258
    • Sako, Y.1    Ichinose, J.2    Morimatsu, M.3    Ohta, K.4    Uyemura, T.5
  • 28
    • 0022668919 scopus 로고
    • Microaggregation of hormone-occupied epidermal growth factor receptors on plasma membrane preparations
    • Zidovetzki, R., Y. Yarden, J. Schlessinger, and T. M. Jovin. 1986. Microaggregation of hormone-occupied epidermal growth factor receptors on plasma membrane preparations. EMBO J. 5:247-250.
    • (1986) EMBO J , vol.5 , pp. 247-250
    • Zidovetzki, R.1    Yarden, Y.2    Schlessinger, J.3    Jovin, T.M.4
  • 29
    • 0033014064 scopus 로고    scopus 로고
    • Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy
    • Nagy, P., A. Jenei, A. K. Kirsch, J. Szollosi, S. Damjanovich, and T. M. Jovin. 1999. Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J. Cell Sci. 112:1733-1741.
    • (1999) J. Cell Sci , vol.112 , pp. 1733-1741
    • Nagy, P.1    Jenei, A.2    Kirsch, A.K.3    Szollosi, J.4    Damjanovich, S.5    Jovin, T.M.6
  • 30
    • 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, A. H., F. Walker, S. G. Orchard, C. Henderson, D. Fuchs, J. Rothacker, E. C. Nice, and A. W. Burgess. 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
    • Clayton, A.H.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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.