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Volumn 73, Issue 3, 2008, Pages 209-219

Two-sided fluorescence resonance energy transfer for assessing molecular interactions of up to three distinct species in confocal microscopy

Author keywords

1 integrin; abFRET; CD44; dbFRET; ErbB2; Fluorescence resonance energy transfer; Laser scanning confocal microscopy; Receptor tyrosine kinase; Trastuzumab resistance; tsFRET

Indexed keywords

BETA1 INTEGRIN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; HERMES ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; TRASTUZUMAB;

EID: 40049093067     PISSN: 15524922     EISSN: 15524930     Source Type: Journal    
DOI: 10.1002/cyto.a.20489     Document Type: Article
Times cited : (31)

References (43)
  • 1
    • 0021243527 scopus 로고
    • Fluorescence energy transfer measurements on cell surfaces: A critical comparison of steady-state fluorimetric and flow cytometric methods
    • Szollosi J, Tron L, Damjanovich S, Helliwell SH, Arndt-Jovin D, Jovin TM. Fluorescence energy transfer measurements on cell surfaces: A critical comparison of steady-state fluorimetric and flow cytometric methods. Cytometry 1984;5:210-216.
    • (1984) Cytometry , vol.5 , pp. 210-216
    • Szollosi, J.1    Tron, L.2    Damjanovich, S.3    Helliwell, S.H.4    Arndt-Jovin, D.5    Jovin, T.M.6
  • 2
    • 0021273333 scopus 로고
    • Flow cytometric measurement of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell-by-cell basis
    • Tron L, Szollosi J, Damjanovich S, Helliwell SH, Arndt-Jovin DJ, Jovin TM. Flow cytometric measurement of fluorescence resonance energy transfer on cell surfaces. Quantitative evaluation of the transfer efficiency on a cell-by-cell basis. Biophys J 1984;45:939-946.
    • (1984) Biophys J , vol.45 , pp. 939-946
    • Tron, L.1    Szollosi, J.2    Damjanovich, S.3    Helliwell, S.H.4    Arndt-Jovin, D.J.5    Jovin, T.M.6
  • 3
    • 0028924992 scopus 로고
    • Fluorescence resonance energy transfer
    • Clegg RM. Fluorescence resonance energy transfer. Curr Opin Biotechnol 1995;6:103-110.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 103-110
    • Clegg, R.M.1
  • 4
    • 0036176443 scopus 로고    scopus 로고
    • Applications of fluorescence resonance energy transfer for mapping biological membranes
    • Szollosi J, Nagy P, Sebestyen Z, Damjanovich S, Park JW, Matyus L. Applications of fluorescence resonance energy transfer for mapping biological membranes. J Biotechnol 2002;82:251-266.
    • (2002) J Biotechnol , vol.82 , pp. 251-266
    • Szollosi, J.1    Nagy, P.2    Sebestyen, Z.3    Damjanovich, S.4    Park, J.W.5    Matyus, L.6
  • 5
    • 0036628631 scopus 로고    scopus 로고
    • Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer
    • Sebestyen Z, Nagy P, Horvath G, Vamosi G, Debets R, Gratama JW, Alexander DR, Szollosi J. Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer. Cytometry 2002;48:124-35.
    • (2002) Cytometry , vol.48 , pp. 124-135
    • Sebestyen, Z.1    Nagy, P.2    Horvath, G.3    Vamosi, G.4    Debets, R.5    Gratama, J.W.6    Alexander, D.R.7    Szollosi, J.8
  • 6
    • 0032529665 scopus 로고    scopus 로고
    • Application of fluorescence resonance energy transfer in the clinical laboratory: Routine and research. Cytometry: Communications in Clinical
    • Szollosi J, Damjanovich S, Matyus L. Application of fluorescence resonance energy transfer in the clinical laboratory: Routine and research. Cytometry: Communications in Clinical Cytometry 1998;34:159-179.
    • (1998) Cytometry , vol.34 , pp. 159-179
    • Szollosi, J.1    Damjanovich, S.2    Matyus, L.3
  • 8
    • 0344447088 scopus 로고    scopus 로고
    • Intensity-based energy transfer measurements in digital imaging microscopy
    • Nagy P, Vamosi G, Bodnar A, Lockett SJ, Szollosi J. Intensity-based energy transfer measurements in digital imaging microscopy. Eur Biophys J 1998;27:377-389.
    • (1998) Eur Biophys J , vol.27 , pp. 377-389
    • Nagy, P.1    Vamosi, G.2    Bodnar, A.3    Lockett, S.J.4    Szollosi, J.5
  • 9
    • 33748545640 scopus 로고    scopus 로고
    • Imaging molecular interactions in living cells by FRET microscopy
    • Jares-Erijman EA, Jovin TM. Imaging molecular interactions in living cells by FRET microscopy. Curr Opin Chem Biol 2006;10:409-416.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 409-416
    • Jares-Erijman, E.A.1    Jovin, T.M.2
  • 10
    • 0030795612 scopus 로고    scopus 로고
    • The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions
    • Alroy I, Yarden Y. The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand-receptor interactions. FEBS Lett 1997;410:83-86.
    • (1997) FEBS Lett , vol.410 , pp. 83-86
    • Alroy, I.1    Yarden, Y.2
  • 11
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGuire WL. Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 1987;235:177-182.
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ullrich, A.5    McGuire, W.L.6
  • 14
    • 0034707581 scopus 로고    scopus 로고
    • ErbB2 is necessary for induction of carcinoma cell invasion by ErbB family receptor tyrosine kinases
    • Spencer KS, Graus-Porta D, Leng J, Hynes NE, Klemke RL. ErbB2 is necessary for induction of carcinoma cell invasion by ErbB family receptor tyrosine kinases. J Cell Biol 2000;148:385-97.
    • (2000) J Cell Biol , vol.148 , pp. 385-397
    • Spencer, K.S.1    Graus-Porta, D.2    Leng, J.3    Hynes, N.E.4    Klemke, R.L.5
  • 15
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • Graus-Porta D, Beerli RR, Daly JM, Hynes NE. ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J 1997;16:1647-1655.
    • (1997) EMBO J , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 17
    • 0027395858 scopus 로고
    • Role of integrins and other cell adhesion molecules in tumor progression and metastasis
    • Albelda SM. Role of integrins and other cell adhesion molecules in tumor progression and metastasis. Lab Invest 1993;68:4-17.
    • (1993) Lab Invest , vol.68 , pp. 4-17
    • Albelda, S.M.1
  • 18
    • 0029043481 scopus 로고
    • Alteration of expression in integrin β 1-subunit correlates with invasion and metastasis in colorectal cancer
    • Fujita S, Watanabe M, Kubota T, Teramoto T, Kitajima M. Alteration of expression in integrin β 1-subunit correlates with invasion and metastasis in colorectal cancer. Cancer Lett 1995;91:145-149.
    • (1995) Cancer Lett , vol.91 , pp. 145-149
    • Fujita, S.1    Watanabe, M.2    Kubota, T.3    Teramoto, T.4    Kitajima, M.5
  • 21
    • 5044238876 scopus 로고    scopus 로고
    • Integrin signalling during tumour progression
    • Guo W, Giancotti FG. Integrin signalling during tumour progression. Nat Rev Mol Cell Biol 2004;5:816-826.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 816-826
    • Guo, W.1    Giancotti, F.G.2
  • 22
    • 0033367737 scopus 로고    scopus 로고
    • Complexity of signal transduction mediated by ErbB2: Clues to the potential of receptor-targeted cancer therapy
    • Nagy P, Jenei A, Damjanovich S, Jovin TM, Szollosi J. Complexity of signal transduction mediated by ErbB2: Clues to the potential of receptor-targeted cancer therapy. Pathol Oncol Res 1999;5:255-271.
    • (1999) Pathol Oncol Res , vol.5 , pp. 255-271
    • Nagy, P.1    Jenei, A.2    Damjanovich, S.3    Jovin, T.M.4    Szollosi, J.5
  • 23
    • 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, Jovin TM. Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J Cell Sci 1999;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
  • 24
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998;14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 29
    • 0029741379 scopus 로고    scopus 로고
    • Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin
    • Bastiaens PI, Majoul IV, Verveer PJ, Soling HD, Jovin TM. Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J 1996;15:4246-4253.
    • (1996) EMBO J , vol.15 , pp. 4246-4253
    • Bastiaens, P.I.1    Majoul, I.V.2    Verveer, P.J.3    Soling, H.D.4    Jovin, T.M.5
  • 30
    • 40049110365 scopus 로고    scopus 로고
    • Vereb G, Meyer CK, Jovin TM. Novel microscope-based approaches for the investigation of protein-protein interactions in signal transduction. In: Heilmeyer LMG, editor. Interacting Protein Domains. Their Role in Signal and Energy Transduction, 102, NATO ASI Series, H: Cell Biology. Berlin, Heidelberg: Springer Verlag; 1997. pp 49-52.
    • Vereb G, Meyer CK, Jovin TM. Novel microscope-based approaches for the investigation of protein-protein interactions in signal transduction. In: Heilmeyer LMG, editor. Interacting Protein Domains. Their Role in Signal and Energy Transduction, Volume 102, NATO ASI Series, H: Cell Biology. Berlin, Heidelberg: Springer Verlag; 1997. pp 49-52.
  • 31
    • 16644374278 scopus 로고    scopus 로고
    • Cytometry of fluorescence resonance energy transfer
    • Vereb G, Matko J, Szollosi J. Cytometry of fluorescence resonance energy transfer. Methods Cell Biol 2004;75:105-152.
    • (2004) Methods Cell Biol , vol.75 , pp. 105-152
    • Vereb, G.1    Matko, J.2    Szollosi, J.3
  • 32
    • 40049090299 scopus 로고    scopus 로고
    • Van Balen R, Koelma D, Ten Kate TR, Mosterd B, Smeulders AWM. Scillmage: A Multi-layered Environment for Use and Development of Image Processing Software. In: H.I. Christiansen and J.L. Crowley, editors. Experimental Environments for Computer Vision and Image Processing. Singapore: World Scientific Publishing Co.; 1994; pp 107-126.
    • Van Balen R, Koelma D, Ten Kate TR, Mosterd B, Smeulders AWM. Scillmage: A Multi-layered Environment for Use and Development of Image Processing Software. In: H.I. Christiansen and J.L. Crowley, editors. Experimental Environments for Computer Vision and Image Processing. Singapore: World Scientific Publishing Co.; 1994; pp 107-126.
  • 33
  • 35
    • 33644694046 scopus 로고    scopus 로고
    • Hsp90 inhibitor 17-AAG reduces ErbB2 levels and inhibits proliferation of the trastuzumab resistant breast tumor cell line JIMT-1
    • Zsebik B, Citri A, Isola J, Yarden Y, Szollosi J, Vereb G. Hsp90 inhibitor 17-AAG reduces ErbB2 levels and inhibits proliferation of the trastuzumab resistant breast tumor cell line JIMT-1. Immunol Lett 2006;104:146-155.
    • (2006) Immunol Lett , vol.104 , pp. 146-155
    • Zsebik, B.1    Citri, A.2    Isola, J.3    Yarden, Y.4    Szollosi, J.5    Vereb, G.6
  • 36
    • 19444380683 scopus 로고    scopus 로고
    • Selecting the right fluorophores and flow cytometer for fluorescence resonance energy transfer measurements
    • Horvath G, Petras M, Szentesi G, Fabian A, Park JW, Vereb G, Szollosi J. Selecting the right fluorophores and flow cytometer for fluorescence resonance energy transfer measurements. Cytometry Part A 2005;65A:148-157.
    • (2005) Cytometry Part A , vol.65 A , pp. 148-157
    • Horvath, G.1    Petras, M.2    Szentesi, G.3    Fabian, A.4    Park, J.W.5    Vereb, G.6    Szollosi, J.7
  • 37
    • 0029057619 scopus 로고
    • Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy
    • Song L, Hennink EJ, Young IT, Tanke HJ. Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy. Biophys J 1995;68:2588-2600.
    • (1995) Biophys J , vol.68 , pp. 2588-2600
    • Song, L.1    Hennink, E.J.2    Young, I.T.3    Tanke, H.J.4
  • 41
    • 33845927961 scopus 로고    scopus 로고
    • Dissecting and reducing the heterogeneity of excited-state energy transport in DNA-based photonic wires
    • Heilemann M, Kasper R, Tinnefeld P, Sauer M. Dissecting and reducing the heterogeneity of excited-state energy transport in DNA-based photonic wires. J Am Chem Soc 2006;128:16864-16875.
    • (2006) J Am Chem Soc , vol.128 , pp. 16864-16875
    • Heilemann, M.1    Kasper, R.2    Tinnefeld, P.3    Sauer, M.4
  • 42
    • 33847142268 scopus 로고    scopus 로고
    • Multicolor single-molecule spectroscopy with alternating laser excitation for the investigation of interactions and dynamics
    • Ross J, Buschkamp P, Fetting D, Donnermeyer A, Roth CM, Tinnefeld P. Multicolor single-molecule spectroscopy with alternating laser excitation for the investigation of interactions and dynamics. J Phys Chem B 2007;111:321-326.
    • (2007) J Phys Chem B , vol.111 , pp. 321-326
    • Ross, J.1    Buschkamp, P.2    Fetting, D.3    Donnermeyer, A.4    Roth, C.M.5    Tinnefeld, P.6
  • 43
    • 15744403602 scopus 로고    scopus 로고
    • Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells
    • Galperin E, Verkhusha VV, Sorkin A. Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells. Nat Methods 2004;1:209-217.
    • (2004) Nat Methods , vol.1 , pp. 209-217
    • Galperin, E.1    Verkhusha, V.V.2    Sorkin, A.3


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