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Volumn 215, Issue 1, 2004, Pages 1-12

Multi-dimensional time-correlated single photon counting (TCSPC) fluorescence lifetime imaging microscopy (FLIM) to detect FRET in cells

Author keywords

FM1 43; GFP; Multi photon; Two photon

Indexed keywords

CELL MEMBRANES; CHROMOPHORES; ENERGY EFFICIENCY; FLUORESCENCE IMAGING; FORSTER RESONANCE ENERGY TRANSFER; PARTICLE BEAMS; PHOTOBLEACHING; PHOTONS; PROTEINS;

EID: 3042541532     PISSN: 00222720     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0022-2720.2004.01343.x     Document Type: Article
Times cited : (131)

References (54)
  • 1
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens, P.I. & Squire, A. (1999) Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol. 9, 48-52.
    • (1999) Trends Cell Biol. , vol.9 , pp. 48-52
    • Bastiaens, P.I.1    Squire, A.2
  • 3
    • 0026584039 scopus 로고
    • Optical analysis of synaptic vesicle recycling at the frog neuromuscular junction
    • Betz, W.J. & Bewick, G.S. (1992) Optical analysis of synaptic vesicle recycling at the frog neuromuscular junction. Science, 255, 200-203.
    • (1992) Science , vol.255 , pp. 200-203
    • Betz, W.J.1    Bewick, G.S.2
  • 5
    • 0036831870 scopus 로고    scopus 로고
    • Two-photon tissue imaging: Seeing the immune system in a fresh light
    • Cahalan, M.D., Parker, I., Wei, S.H. & Miller, M.J. (2002) Two-photon tissue imaging: seeing the immune system in a fresh light. Nat. Rev. Immunol. 2, 872-880.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 872-880
    • Cahalan, M.D.1    Parker, I.2    Wei, S.H.3    Miller, M.J.4
  • 6
  • 8
    • 0025580921 scopus 로고
    • The interactions between plasma membrane depolarization and glutamate receptor activation in the regulation of cytoplasmic free calcium in cultured cerebellar granule cells
    • Courtney, M.J., Lambert, J.J. & Nichols, D.G. (1990) The interactions between plasma membrane depolarization and glutamate receptor activation in the regulation of cytoplasmic free calcium in cultured cerebellar granule cells. J. Neurosci. 10, 3873-3879.
    • (1990) J. Neurosci. , vol.10 , pp. 3873-3879
    • Courtney, M.J.1    Lambert, J.J.2    Nichols, D.G.3
  • 9
    • 0032734205 scopus 로고    scopus 로고
    • Mechanisms of synaptic vesicle recycling illuminated by fluorescent dyes
    • Cousin, M.A. & Robinson, P.J. (1999) Mechanisms of synaptic vesicle recycling illuminated by fluorescent dyes. J. Neurochem. 73, 2227-2239.
    • (1999) J. Neurochem. , vol.73 , pp. 2227-2239
    • Cousin, M.A.1    Robinson, P.J.2
  • 11
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk, W., Strickler, J.H. & Webb, W.W. (1990) Two-photon laser scanning fluorescence microscopy. Science, 248, 73-76.
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 12
    • 0033600807 scopus 로고    scopus 로고
    • Transient, phorbol ester-induced DOC2-Munc13 interactions in vivo
    • Duncan, R.R., Betz, A., Shipston, M.J., Brose, N. & Chow, R.H. (1999a) Transient, phorbol ester-induced DOC2-Munc13 interactions in vivo. J. Biol. Chem. 274, 27347-27350.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27347-27350
    • Duncan, R.R.1    Betz, A.2    Shipston, M.J.3    Brose, N.4    Chow, R.H.5
  • 13
    • 0033568391 scopus 로고    scopus 로고
    • High-efficiency Semliki Forest virus-mediated transduction in bovine adrenal chromaffin cells
    • Duncan, R.R., Don-Wauchope, A.C., Tapechum, S., Shipston, M.J., Chow, R.H. & Estibeiro, P. (1999b) High-efficiency Semliki Forest virus-mediated transduction in bovine adrenal chromaffin cells. Biochem. J. 342, 497-501.
    • (1999) Biochem. J. , vol.342 , pp. 497-501
    • Duncan, R.R.1    Don-Wauchope, A.C.2    Tapechum, S.3    Shipston, M.J.4    Chow, R.H.5    Estibeiro, P.6
  • 15
    • 0030747190 scopus 로고    scopus 로고
    • Rat brain p64H1, expression of a new member of the p64 chloride channel protein family in endoplasmic reticulum
    • Duncan, R.R., Westwood, P.K., Boyd, A. & Ashley, R.H. (1997) Rat brain p64H1, expression of a new member of the p64 chloride channel protein family in endoplasmic reticulum. J. Biol. Chem. 272, 23880-23886.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23880-23886
    • Duncan, R.R.1    Westwood, P.K.2    Boyd, A.3    Ashley, R.H.4
  • 16
    • 0036164650 scopus 로고    scopus 로고
    • Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell
    • Elangovan, M., Day, R.N. & Periasamy, A. (2002) Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell. J. Microsc. 205, 3-14.
    • (2002) J. Microsc. , vol.205 , pp. 3-14
    • Elangovan, M.1    Day, R.N.2    Periasamy, A.3
  • 17
  • 18
    • 0036016786 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging in scanning microscopes: Acquisition speed, photon economy and lifetime resolution
    • Gerritsen, H.C., Asselbergs, M.A., Agronskaia, A.V. & Van Sark, W.G. (2002) Fluorescence lifetime imaging in scanning microscopes: acquisition speed, photon economy and lifetime resolution. J. Microsc. 206, 218-224.
    • (2002) J. Microsc. , vol.206 , pp. 218-224
    • Gerritsen, H.C.1    Asselbergs, M.A.2    Agronskaia, A.V.3    Van Sark, W.G.4
  • 19
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon, G.W., Berry, G., Liang, X.H., Levine, B. & Herman, B. (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
  • 20
    • 0021508770 scopus 로고
    • Resolution of mixtures of fluorophores using variable-frequency phase and modulation data
    • Gratton, E., Limkeman, M., Lakowicz, J.R., Maliwal, B.P., Cherek, H. & Laczko, G. (1984) Resolution of mixtures of fluorophores using variable-frequency phase and modulation data. Biophys. J. 46, 479-486.
    • (1984) Biophys. J. , vol.46 , pp. 479-486
    • Gratton, E.1    Limkeman, M.2    Lakowicz, J.R.3    Maliwal, B.P.4    Cherek, H.5    Laczko, G.6
  • 21
    • 0035122528 scopus 로고    scopus 로고
    • Imaging FRET between spectrally similar GFP molecules in single cells
    • Harpur, A.G., Wouters, E.S. & Bastiaens, P.I. (2001) Imaging FRET between spectrally similar GFP molecules in single cells. Nat. Biotechnol. 19, 167-169.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 167-169
    • Harpur, A.G.1    Wouters, E.S.2    Bastiaens, P.I.3
  • 22
    • 0034710922 scopus 로고    scopus 로고
    • Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: Coral red (dsRed) and yellow (Citrine)
    • Heikal, A.A., Hess, S.T., Baird, G.S., Tsien, R.Y. & Webb, W.W. (2000) Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: coral red (dsRed) and yellow (Citrine). Proc. Natl. Acad. Sci. USA, 97, 11996-12001.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11996-12001
    • Heikal, A.A.1    Hess, S.T.2    Baird, G.S.3    Tsien, R.Y.4    Webb, W.W.5
  • 23
    • 33747566427 scopus 로고
    • How many photons are necessary for fluorescence-lifetime measurements?
    • Köllner, M. & Wolfrum, J. (1992) How many photons are necessary for fluorescence-lifetime measurements?. Chem. Phys. Lett. 200, 199-204.
    • (1992) Chem. Phys. Lett. , vol.200 , pp. 199-204
    • Köllner, M.1    Wolfrum, J.2
  • 24
    • 0036721022 scopus 로고    scopus 로고
    • Homomultimerization of the coxsackievirus 2B protein in living cells visualized by fluorescence resonance energy transfer microscopy
    • van Kuppeveld, F.J.W.J., Melchers, P.H., Willems & Gadella, Jr (2002) Homomultimerization of the coxsackievirus 2B protein in living cells visualized by fluorescence resonance energy transfer microscopy. J. Virol. 76, 9446-9456.
    • (2002) J. Virol. , vol.76 , pp. 9446-9456
    • Van Kuppeveld, F.J.W.J.1    Melchers, P.H.2    Willems3    Gadella, Jr.4
  • 25
    • 0030310925 scopus 로고    scopus 로고
    • Emerging applications of fluorescence spectroscopy to cellular imaging: Lifetime imaging, metal-ligand probes, multi-photon excitation and light quenching
    • Lakowicz, J.R. (1996) Emerging applications of fluorescence spectroscopy to cellular imaging: lifetime imaging, metal-ligand probes, multi-photon excitation and light quenching. Scanning Microsc. Suppl. 10, 213-224.
    • (1996) Scanning Microsc. Suppl. , vol.10 , pp. 213-224
    • Lakowicz, J.R.1
  • 29
    • 0026547480 scopus 로고
    • In situ fluorescence analysis using nanosecond decay time imaging
    • Morgan, C.G., Mitchell, A.C. & Murray, A.G. (1992) In situ fluorescence analysis using nanosecond decay time imaging. Trends Anal. Chem. 11, 32-35.
    • (1992) Trends Anal. Chem. , vol.11 , pp. 32-35
    • Morgan, C.G.1    Mitchell, A.C.2    Murray, A.G.3
  • 31
    • 0034110795 scopus 로고    scopus 로고
    • Photobleaching in two-photon excitation microscopy
    • Patterson, G.H. & Piston, D.W. (2000) Photobleaching in two-photon excitation microscopy. Biophys. J. 78, 2159-2162.
    • (2000) Biophys. J. , vol.78 , pp. 2159-2162
    • Patterson, G.H.1    Piston, D.W.2
  • 32
    • 0034633010 scopus 로고    scopus 로고
    • Förster distances between green fluorescent protein pairs
    • Patterson, G.H., Piston, D.W. & Barisas, B.G. (2000) Förster 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
  • 33
    • 0033545695 scopus 로고    scopus 로고
    • Simultaneous detection of multiple green fluorescent proteins in live cells by fluorescence lifetime imaging microscopy
    • Pepperkok, R., Squire, A., Geley, S. & Bastiaens, P.I. (1999) Simultaneous detection of multiple green fluorescent proteins in live cells by fluorescence lifetime imaging microscopy. Curr. Biol. 9, 269-272.
    • (1999) Curr. Biol. , vol.9 , pp. 269-272
    • Pepperkok, R.1    Squire, A.2    Geley, S.3    Bastiaens, P.I.4
  • 34
    • 0032622353 scopus 로고    scopus 로고
    • Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy
    • Periasamy, A. & Day, R.N. (1999) Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy. Methods Cell Biol. 58, 293-314.
    • (1999) Methods Cell Biol. , vol.58 , pp. 293-314
    • Periasamy, A.1    Day, R.N.2
  • 35
    • 0036047349 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging (FLIM) of green fluorescent fusion proteins in living cells
    • Periasamy, A., Elangovan, M., Elliott, E. & Brautigan, D.L. (2002) Fluorescence lifetime imaging (FLIM) of green fluorescent fusion proteins in living cells. Methods Mol. Biol. 183, 89-100.
    • (2002) Methods Mol. Biol. , vol.183 , pp. 89-100
    • Periasamy, A.1    Elangovan, M.2    Elliott, E.3    Brautigan, D.L.4
  • 36
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok, B.A. & Heim, R. (1999) Using GFP in FRET-based applications. Trends Cell Biol. 9, 57-60.
    • (1999) Trends Cell Biol. , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 37
    • 0030087711 scopus 로고    scopus 로고
    • Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo
    • Rizzuto, R., Brini, M., De Giorgi, F., Rossi, R., Heim, R., Tsien, R.Y. & Pozzan, T. (1996) Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo. Curr. Biol. 6, 183-188.
    • (1996) Curr. Biol. , vol.6 , pp. 183-188
    • Rizzuto, R.1    Brini, M.2    De Giorgi, F.3    Rossi, R.4    Heim, R.5    Tsien, R.Y.6    Pozzan, T.7
  • 38
    • 0032211065 scopus 로고    scopus 로고
    • Continuous and transient vesicle cycling at a ribbon synapse
    • Rouze, N.C. & Schwartz, E.A. (1998) Continuous and transient vesicle cycling at a ribbon synapse. J. Neurosci. 18, 8614-8624.
    • (1998) J. Neurosci. , vol.18 , pp. 8614-8624
    • Rouze, N.C.1    Schwartz, E.A.2
  • 39
    • 0037812528 scopus 로고    scopus 로고
    • Four-dimensional multi-photon microscopy with time-correlated singel-photon counting
    • Schönle, A., Glatz, M. & Hell, S.W. (2000) Four-dimensional multi-photon microscopy with time-correlated singel-photon counting. Appl. Opt. 39, 6306-6311.
    • (2000) Appl. Opt. , vol.39 , pp. 6306-6311
    • Schönle, A.1    Glatz, M.2    Hell, S.W.3
  • 41
    • 0030855088 scopus 로고    scopus 로고
    • Transport, docking and exocytosis of single secretory granules in live chromaffin cells
    • Steyer, J.A., Horstmann, H. & Almers, W. (1997) Transport, docking and exocytosis of single secretory granules in live chromaffin cells. Nature, 388, 474-478.
    • (1997) Nature , vol.388 , pp. 474-478
    • Steyer, J.A.1    Horstmann, H.2    Almers, W.3
  • 43
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. (1978) Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 45
    • 0142198626 scopus 로고    scopus 로고
    • Photophysics of green and red fluorescent proteins: Implications for quantitative microscopy
    • Subramaniam, V., Hanley, Q.S., Clayton, A.H. & Jovin, T.M. (2003) Photophysics of green and red fluorescent proteins: implications for quantitative microscopy. Methods Enzymol. 360, 178-201.
    • (2003) Methods Enzymol. , vol.360 , pp. 178-201
    • Subramaniam, V.1    Hanley, Q.S.2    Clayton, A.H.3    Jovin, T.M.4
  • 48
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R.Y. (1998) The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 49
    • 0037241265 scopus 로고    scopus 로고
    • Evaluation of global analysis algorithms for single frequency fluorescence lifetime imaging microscopy data
    • Verveer, P.J. & Bastiaens, P.I. (2003) Evaluation of global analysis algorithms for single frequency fluorescence lifetime imaging microscopy data. J. Microsc. 209, 1-7.
    • (2003) J. Microsc. , vol.209 , pp. 1-7
    • Verveer, P.J.1    Bastiaens, P.I.2
  • 50
    • 0034029599 scopus 로고    scopus 로고
    • Global analysis of fluorescence lifetime imaging microscopy data
    • Verveer, P.J., Squire, A. & Bastiaens, P.I. (2000) Global analysis of fluorescence lifetime imaging microscopy data. Biophys. J. 78, 2127-2137.
    • (2000) Biophys. J. , vol.78 , pp. 2127-2137
    • Verveer, P.J.1    Squire, A.2    Bastiaens, P.I.3
  • 51
    • 0034765673 scopus 로고    scopus 로고
    • Applying multiphoton imaging to the study of membrane dynamics in living cells
    • White, J.G., Squirrell, J.M. & Eliceiri, K.W. (2001) Applying multiphoton imaging to the study of membrane dynamics in living cells. Traffic, 2, 775-780.
    • (2001) Traffic , vol.2 , pp. 775-780
    • White, J.G.1    Squirrell, J.M.2    Eliceiri, K.W.3
  • 52
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia, Z. & Liu, Y. (2001) Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81, 2395-2402.
    • (2001) Biophys. J. , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 53
    • 0029780689 scopus 로고    scopus 로고
    • Multiphoton fluorescence excitation: New spectral windows for biological nonlinear microscopy
    • Xu, C., Zipfel, W., Shear, J.B., Williams, R.M. & Webb, W.W. (1996) Multiphoton fluorescence excitation: new spectral windows for biological nonlinear microscopy. Proc. Natl Acad. Sci. USA, 93, 10763-10768.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10763-10768
    • Xu, C.1    Zipfel, W.2    Shear, J.B.3    Williams, R.M.4    Webb, W.W.5
  • 54
    • 0037068837 scopus 로고    scopus 로고
    • A membrane marker leaves synaptic vesicles in milliseconds after exocytosis in retinal bipolar cells
    • Zenisek, D., Steyer, J., Feldman, M. & Almers, W. (2002) A membrane marker leaves synaptic vesicles in milliseconds after exocytosis in retinal bipolar cells. Neuron, 35, 1085.
    • (2002) Neuron , vol.35 , pp. 1085
    • Zenisek, D.1    Steyer, J.2    Feldman, M.3    Almers, W.4


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