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Volumn 89, Issue 4, 2005, Pages 2736-2749

Quantitative multiphoton spectral imaging and its use for measuring resonance energy transfer

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ARTICLE; CLONING; ENERGY TRANSFER; GENE EXPRESSION; IMAGING SYSTEM; MEASUREMENT; MOUSE; MULTIPHOTON MICROSCOPY; NEUROBLASTOMA CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PROTEIN ANALYSIS; PROTEIN PURIFICATION; QUANTITATIVE ANALYSIS; STOICHIOMETRY;

EID: 25844499242     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.061853     Document Type: Article
Times cited : (161)

References (36)
  • 2
    • 0041837561 scopus 로고    scopus 로고
    • Lighting up cells: Labelling proteins with fluorophores
    • Miyawaki, A., A. Sawano, and T. Kogure. 2003. Lighting up cells: labelling proteins with fluorophores. Nat. Cell Biol. Suppl:S1-S7.
    • (2003) Nat. Cell Biol. , Issue.SUPPL.
    • Miyawaki, A.1    Sawano, A.2    Kogure, T.3
  • 3
    • 1442335323 scopus 로고    scopus 로고
    • Automated high through-put colocalization analysis of multichannel confocal images
    • Kreft, M., I. Milisav, M. Potokar, and R. Zorec. 2004. Automated high through-put colocalization analysis of multichannel confocal images. Comput. Methods Programs Biomed. 74:63-67.
    • (2004) Comput. Methods Programs Biomed. , vol.74 , pp. 63-67
    • Kreft, M.1    Milisav, I.2    Potokar, M.3    Zorec, R.4
  • 4
    • 0035254161 scopus 로고    scopus 로고
    • High resolution, fluorescence deconvolution microscopy and tagging with the autofluorescent tracers CFP, GFP, and YFP to study the structural composition of gap junctions in living cells
    • Falk, M. M., and U. Lauf. 2001. High resolution, fluorescence deconvolution microscopy and tagging with the autofluorescent tracers CFP, GFP, and YFP to study the structural composition of gap junctions in living cells. Microsc. Res. Tech. 52:251-262.
    • (2001) Microsc. Res. Tech. , vol.52 , pp. 251-262
    • Falk, M.M.1    Lauf, U.2
  • 5
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • Manders, E. M., J. Stap, G. J. Brakenhoff, R. van Driel, and J. A. Aten. 1992. Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy. J. Cell Sci. 103:857-862.
    • (1992) J. Cell Sci. , vol.103 , pp. 857-862
    • Manders, E.M.1    Stap, J.2    Brakenhoff, G.J.3    Van Driel, R.4    Aten, J.A.5
  • 6
    • 0027418205 scopus 로고
    • Measurement of co-localization of objects in dual-colour comfocal images
    • Manders, E. M. M., F. J. Verbeek, and J. A. Aten. 1993. Measurement of co-localization of objects in dual-colour comfocal images. J. Microsc. 169:375-382.
    • (1993) J. Microsc. , vol.169 , pp. 375-382
    • Manders, E.M.M.1    Verbeek, F.J.2    Aten, J.A.3
  • 8
    • 0027573254 scopus 로고
    • The four-way DNA junction: A fluorescence resonance energy transfer study
    • Clegg, R. M., A. I. Murchie, and D. M. Lilley. 1993. The four-way DNA junction: a fluorescence resonance energy transfer study. Braz. J. Med. Biol. Res. 26:405-416.
    • (1993) Braz. J. Med. Biol. Res. , vol.26 , pp. 405-416
    • Clegg, R.M.1    Murchie, A.I.2    Lilley, D.M.3
  • 9
    • 4344564695 scopus 로고    scopus 로고
    • Applying spectral fingerprinting to the analysis of FRET images
    • Neher, R. A., and E. Neher. 2004. Applying spectral fingerprinting to the analysis of FRET images. Microsc. Res. Tech. 64:185-195.
    • (2004) Microsc. Res. Tech. , vol.64 , pp. 185-195
    • Neher, R.A.1    Neher, E.2
  • 11
    • 0034947940 scopus 로고    scopus 로고
    • Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase
    • Geiser, M., R. Cebe, D. Drewello, and R. Schmitz. 2001. Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase. Biotechniques. 31:88-90, 92.
    • (2001) Biotechniques , vol.31 , pp. 88-90
    • Geiser, M.1    Cebe, R.2    Drewello, D.3    Schmitz, R.4
  • 12
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • Rizzo, M. A., G. H. Springer, B. Granada, and D. W. Piston. 2004. An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22:445-449.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 13
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T., K. Ibata, E. S. Park, M. Kubota, K. Mikoshiba, and A. Miyawaki. 2002. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20:87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 14
    • 0346874407 scopus 로고    scopus 로고
    • A flow cytometric method to detect protein-protein interaction in living cells by directly visualizing donor fluorophore quenching during CFP → YFP fluorescence resonance energy transfer (FRET)
    • He, L., D. P. Olson, X. Wu, T. S. Karpova, J. G. McNally, and P. E. Lipsky. 2003. A flow cytometric method to detect protein-protein interaction in living cells by directly visualizing donor fluorophore quenching during CFP → YFP fluorescence resonance energy transfer (FRET). Cytometry. 55A:71-85.
    • (2003) Cytometry , vol.55 A , pp. 71-85
    • He, L.1    Olson, D.P.2    Wu, X.3    Karpova, T.S.4    McNally, J.G.5    Lipsky, P.E.6
  • 15
    • 0035893654 scopus 로고    scopus 로고
    • Functional expression and FRET analysis of green fluorescent proteins fused to G-protein subunits in rat sympathetic neurons
    • Ruiz-Velasco, V., and S. R. Ikeda. 2001. Functional expression and FRET analysis of green fluorescent proteins fused to G-protein subunits in rat sympathetic neurons. J. Physiol. 537:679-692.
    • (2001) J. Physiol. , vol.537 , pp. 679-692
    • Ruiz-Velasco, V.1    Ikeda, S.R.2
  • 17
    • 0002804044 scopus 로고
    • Fluorescence lifetime imaging, a new tool in confocal microscopy
    • J. Pawley, editor. Plenum Press, New York
    • Draaijer, A., R. Sanders, and H. Gerritsen. 1995. Fluorescence lifetime imaging, a new tool in confocal microscopy. In Handbook of Biological Confocal Microscopy, 2nd ed. J. Pawley, editor. Plenum Press, New York. 491-505.
    • (1995) Handbook of Biological Confocal Microscopy, 2nd Ed. , pp. 491-505
    • Draaijer, A.1    Sanders, R.2    Gerritsen, H.3
  • 19
    • 0002855636 scopus 로고
    • Enumeration of components in complex systems by fluorescence spectrophotimetry
    • Weber, G. 1961. Enumeration of components in complex systems by fluorescence spectrophotimetry. Nature. 190:27-29.
    • (1961) Nature , vol.190 , pp. 27-29
    • Weber, G.1
  • 20
    • 0038199783 scopus 로고    scopus 로고
    • Spectral imaging and its applications in live cell microscopy
    • Zimmermann, T., J. Rietdorf, and R. Pepperkok. 2003. Spectral imaging and its applications in live cell microscopy. FEBS Lett. 546:87-92.
    • (2003) FEBS Lett. , vol.546 , pp. 87-92
    • Zimmermann, T.1    Rietdorf, J.2    Pepperkok, R.3
  • 22
    • 0035205294 scopus 로고    scopus 로고
    • Multi-spectral imaging and linear unmixing add a whole new dimension to laser scanning fluorescence microscopy
    • Dickinson, M. E., G. Bearman, S. Tille, R. Lansford, and S. E. Fraser. 2001. Multi-spectral imaging and linear unmixing add a whole new dimension to laser scanning fluorescence microscopy. Biotechniques. 31:1272-1278.
    • (2001) Biotechniques , vol.31 , pp. 1272-1278
    • Dickinson, M.E.1    Bearman, G.2    Tille, S.3    Lansford, R.4    Fraser, S.E.5
  • 24
    • 0034633010 scopus 로고    scopus 로고
    • Forster distances between green fluorescent protein pairs
    • Patterson, G. H., D. W. Piston, and B. G. Barisas. 2000. Forster distances between green fluorescent protein pairs. Anal. Biochem. 284:438-440.
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 25
    • 0003718955 scopus 로고    scopus 로고
    • Wiley-VCH, Weinheim, Germany. 387 p.
    • Valeur, B. 2002. Molecular Fluorescence. Wiley-VCH, Weinheim, Germany. 387 p.
    • (2002) Molecular Fluorescence
    • Valeur, B.1
  • 26
    • 0001033803 scopus 로고    scopus 로고
    • Structural basis for self-association and receptor recognition of human TRAF2
    • Park, Y. C., V. Burkitt, A. R. Villa, L. Tong, and H. Wu. 1999. Structural basis for self-association and receptor recognition of human TRAF2. Nature. 398:533-538.
    • (1999) Nature , vol.398 , pp. 533-538
    • Park, Y.C.1    Burkitt, V.2    Villa, A.R.3    Tong, L.4    Wu, H.5
  • 27
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein beta gamma dimer at 2.1 Å resolution
    • Sondek, J., A. Bohm, D. G. Lambright, H. E. Hamm, and P. B. Sigler. 1996. Crystal structure of a G-protein beta gamma dimer at 2.1 Å resolution. Nature. 379:369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 28
    • 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., J. Szollosi, S. Damjanovich, S. H. Helliwell, D. J. Arndt-Jovin, and T. M. Jovin. 1984. 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. 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
  • 29
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon, G. W., G. Berry, X. H. Liang, B. Levine, and B. Herman. 1998. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 74:2702-2713.
    • (1998) Biophys. J. , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 30
    • 0036924067 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based stoichiometry in living cells
    • Hoppe, A., K. Christensen, and J. A. Swanson. 2002. Fluorescence resonance energy transfer-based stoichiometry in living cells. Biophys. J. 83:3652-3664.
    • (2002) Biophys. J. , vol.83 , pp. 3652-3664
    • Hoppe, A.1    Christensen, K.2    Swanson, J.A.3
  • 31
    • 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. Jr., and T. M. Jovin. 1995. 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. 129:1543-1558.
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella Jr., T.W.1    Jovin, T.M.2
  • 32
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy, A. K. 2001. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods. 24:289-296.
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 33
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe, H., and A. Periasamy. 2005. Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16:19-27.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 34
    • 0141509840 scopus 로고    scopus 로고
    • Quantitative imaging of protein-protein interactions by multiphoton fluorescence lifetime imaging microscopy using a streak camera
    • Krishnan, R. V., A. Masuda, V. E. Centonze, and B. Herman. 2003. Quantitative imaging of protein-protein interactions by multiphoton fluorescence lifetime imaging microscopy using a streak camera. J. Biomed. Opt. 8:362-367.
    • (2003) J. Biomed. Opt. , vol.8 , pp. 362-367
    • Krishnan, R.V.1    Masuda, A.2    Centonze, V.E.3    Herman, B.4
  • 35
    • 0742286846 scopus 로고    scopus 로고
    • Optimizing imaging parameters for the separation of multiple labels in a fluorescence image
    • Neher, R., and E. Neher. 2004. Optimizing imaging parameters for the separation of multiple labels in a fluorescence image. J. Microsc. 213:46-62.
    • (2004) J. Microsc. , vol.213 , pp. 46-62
    • Neher, R.1    Neher, E.2
  • 36
    • 0242353872 scopus 로고    scopus 로고
    • Nonlinear magic: Multiphoton microscopy in the biosciences
    • Zipfel, W. R., R. M. Williams, and W. W. Webb. 2003. Nonlinear magic: multiphoton microscopy in the biosciences. Nat. Biotechnol. 21:1369-1377.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1369-1377
    • Zipfel, W.R.1    Williams, R.M.2    Webb, W.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.