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Volumn 95, Issue 1, 2008, Pages 378-389

Quantitative lifetime unmixing of multiexponentially decaying fluorophores using single-frequency fluorescence lifetime imaging microscopy

Author keywords

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Indexed keywords

BIOPOLYMER;

EID: 46749125072     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.125229     Document Type: Article
Times cited : (48)

References (49)
  • 1
    • 26444495476 scopus 로고    scopus 로고
    • New tool to monitor membrane potential by FRET voltage sensitive dye (FRET-VSD) using spectral and fluorescence lifetime imaging microscopy (FLIM). Interest in cell engineering
    • Dumas, D., and J. F. Stoltz. 2005. New tool to monitor membrane potential by FRET voltage sensitive dye (FRET-VSD) using spectral and fluorescence lifetime imaging microscopy (FLIM). Interest in cell engineering. Clin. Hemorheol. Microcirc. 33:293-302.
    • (2005) Clin. Hemorheol. Microcirc , vol.33 , pp. 293-302
    • Dumas, D.1    Stoltz, J.F.2
  • 2
    • 0347505005 scopus 로고    scopus 로고
    • Fluorescence lifetime-resolved pH imaging of living cells
    • Lin, H. J., P. Herman, and J. R. Lakowicz. 2003. Fluorescence lifetime-resolved pH imaging of living cells. Cytometry A. 52:77-89.
    • (2003) Cytometry A , vol.52 , pp. 77-89
    • Lin, H.J.1    Herman, P.2    Lakowicz, J.R.3
  • 3
    • 0027767493 scopus 로고
    • Fluorescence lifetime imaging microscopy (FLIM): Spatial resolution of microstructures on the nanosecond time scale
    • Gadella, T. W. Jr., T. M. Jovin, and R. M. Clegg. 1993. Fluorescence lifetime imaging microscopy (FLIM): spatial resolution of microstructures on the nanosecond time scale. Biophys. Chem. 48:221-239.
    • (1993) Biophys. Chem , vol.48 , pp. 221-239
    • Gadella Jr., T.W.1    Jovin, T.M.2    Clegg, R.M.3
  • 4
    • 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
  • 5
    • 0032535138 scopus 로고    scopus 로고
    • FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes
    • Wouters, F. S., P. I. Bastiaens, K. W. Wirtz, and T. M. Jovin. 1998. FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes. EMBO J. 17:7179-7189.
    • (1998) EMBO J , vol.17 , pp. 7179-7189
    • Wouters, F.S.1    Bastiaens, P.I.2    Wirtz, K.W.3    Jovin, T.M.4
  • 6
    • 12344284052 scopus 로고    scopus 로고
    • Imaging activation of two Ras isoforms simultaneously in a single cell
    • Peyker, A., O. Rocks, and P. I. Bastiaens. 2005. Imaging activation of two Ras isoforms simultaneously in a single cell. ChemBioChem. 6:78-85.
    • (2005) ChemBioChem , vol.6 , pp. 78-85
    • Peyker, A.1    Rocks, O.2    Bastiaens, P.I.3
  • 8
    • 0033545695 scopus 로고    scopus 로고
    • Simultaneous detection of multiple green fluorescent proteins in live cells by fluorescence lifetime imaging microscopy
    • Pepperkok, R., A. Squire, S. Geley, and P. I. Bastiaens. 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
  • 9
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane
    • Verveer, P. J., F. S. Wouters, A. R. Reynolds, and P. I. Bastiaens. 2000. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science. 290:1567-1570.
    • (2000) Science , vol.290 , pp. 1567-1570
    • Verveer, P.J.1    Wouters, F.S.2    Reynolds, A.R.3    Bastiaens, P.I.4
  • 11
    • 0033953954 scopus 로고    scopus 로고
    • Multiple frequency fluorescence lifetime imaging microscopy
    • Squire, A., P. J. Verveer, and P. I. Bastiaens. 2000. Multiple frequency fluorescence lifetime imaging microscopy. J. Microsc. 197:136-149.
    • (2000) J. Microsc , vol.197 , pp. 136-149
    • Squire, A.1    Verveer, P.J.2    Bastiaens, P.I.3
  • 12
    • 0037241265 scopus 로고    scopus 로고
    • Evaluation of global analysis algorithms for single frequency fluorescence lifetime imaging microscopy data
    • Verveer, P. J., and P. I. Bastiaens. 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
  • 13
    • 0034029599 scopus 로고    scopus 로고
    • Global analysis of fluorescence lifetime imaging microscopy data
    • Verveer, P. J., A. Squire, and P. I. Bastiaens. 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
  • 14
    • 17144409955 scopus 로고    scopus 로고
    • AB-plot assisted determination of fluorophore mixtures in a fluorescence lifetime microscope using spectra or quenchers
    • Hanley, Q. S., and A. H. A. Clayton. 2005. AB-plot assisted determination of fluorophore mixtures in a fluorescence lifetime microscope using spectra or quenchers. J. Microsc. 218:62-67.
    • (2005) J. Microsc , vol.218 , pp. 62-67
    • Hanley, Q.S.1    Clayton, A.H.A.2
  • 15
    • 29144446288 scopus 로고    scopus 로고
    • Polar plot representation for frequency-domain analysis of fluorescence lifetimes
    • Redford, G. I., and R. M. Clegg. 2005. Polar plot representation for frequency-domain analysis of fluorescence lifetimes. J. Fluoresc. 15:805-815.
    • (2005) J. Fluoresc , vol.15 , pp. 805-815
    • Redford, G.I.1    Clegg, R.M.2
  • 16
    • 38349018672 scopus 로고    scopus 로고
    • The phasor approach to fluorescence lifetime imaging analysis
    • Digman, M. A., V. R. Caiolfa, M. Zamai, and E. Gratton. 2008. The phasor approach to fluorescence lifetime imaging analysis. Biophys. J. 94:L14-L16.
    • (2008) Biophys. J , vol.94
    • Digman, M.A.1    Caiolfa, V.R.2    Zamai, M.3    Gratton, E.4
  • 17
    • 0001142223 scopus 로고
    • Resolution of the fluorescence lifetimes in a heterogeneous system by phase and modulation measurements
    • Weber, G. 1981. Resolution of the fluorescence lifetimes in a heterogeneous system by phase and modulation measurements. J. Phys. Chem. 85:949-953.
    • (1981) J. Phys. Chem , vol.85 , pp. 949-953
    • Weber, G.1
  • 18
    • 33947704150 scopus 로고    scopus 로고
    • Improved green and blue fluorescent proteins for expression in bacteria and mammalian cells
    • Kremers, G. J., J. Goedhart, D. J. van den Heuvel, H. C. Gerritsen, and T. W. Gadella Jr. 2007. Improved green and blue fluorescent proteins for expression in bacteria and mammalian cells. Biochemistry. 46:3775-3783.
    • (2007) Biochemistry , vol.46 , pp. 3775-3783
    • Kremers, G.J.1    Goedhart, J.2    van den Heuvel, D.J.3    Gerritsen, H.C.4    Gadella Jr., T.W.5
  • 19
    • 33744779420 scopus 로고    scopus 로고
    • Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET Forster radius
    • Kremers, G. J., J. Goedhart, E. B. van Munster, and T. W. Gadella Jr. 2006. Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET Forster radius. Biochemistry. 45:6570-6580.
    • (2006) Biochemistry , vol.45 , pp. 6570-6580
    • Kremers, G.J.1    Goedhart, J.2    van Munster, E.B.3    Gadella Jr., T.W.4
  • 20
    • 0033572662 scopus 로고    scopus 로고
    • The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo
    • Gray, A., J. Van Der Kaay, and C. P. Downes. 1999. The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositides-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-trisphosphate in vivo. Biochem. J. 344:929-936.
    • (1999) Biochem. J , vol.344 , pp. 929-936
    • Gray, A.1    Van Der Kaay, J.2    Downes, C.P.3
  • 21
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N. C., R. E. Campbell, P. A. Steinbach, B. N. Giepmans, A. E. Palmer, and R. Y. Tsien. 2004. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22:1567-1572.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 22
    • 0742321790 scopus 로고    scopus 로고
    • phiFLIM: A new method to avoid aliasing in frequency-domain fluorescence lifetime imaging microscopy
    • van Munster, E. B., and T. W. Gadella Jr. 2004. phiFLIM: a new method to avoid aliasing in frequency-domain fluorescence lifetime imaging microscopy. J. Microsc. 213:29-38.
    • (2004) J. Microsc , vol.213 , pp. 29-38
    • van Munster, E.B.1    Gadella Jr., T.W.2
  • 24
    • 1942438090 scopus 로고    scopus 로고
    • Suppression of photobleaching-induced artifacts in frequency-domain FLIM by permutation of the recording order
    • van Munster, E. B., and T. W. Gadella Jr. 2004. Suppression of photobleaching-induced artifacts in frequency-domain FLIM by permutation of the recording order. Cytometry. 58A:185-194.
    • (2004) Cytometry , vol.58 A , pp. 185-194
    • van Munster, E.B.1    Gadella Jr., T.W.2
  • 25
    • 0344447088 scopus 로고    scopus 로고
    • Intensity-based energy transfer measurements in digital imaging microscopy
    • Nagy, P., G. Vamosi, A. Bodnar, S. J. Lockett, and J. Szollosi. 1998. Intensity-based energy transfer measurements in digital imaging microscopy. Eur. Biophys. J. 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
  • 26
    • 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
  • 27
    • 1942487298 scopus 로고    scopus 로고
    • Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission
    • van Rheenen, J., M. Langeslag, and K. Jalink. 2004. Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission. Biophys. J. 86:2517-2529.
    • (2004) Biophys. J , vol.86 , pp. 2517-2529
    • van Rheenen, J.1    Langeslag, M.2    Jalink, K.3
  • 28
    • 0342547337 scopus 로고    scopus 로고
    • Gadella, T. W. Jr., G. Vereb Jr., A. E. Hadri, H. Rohrig, J. Schmidt, M. John, J. Schell, and T. Bisseling. 1997. Microspectroscopic imaging of nodulation factor-binding sites on living Vicia sativa roots using a novel bioactive fluorescent nodulation factor. Biophys. J. 72:1986-1996.
    • Gadella, T. W. Jr., G. Vereb Jr., A. E. Hadri, H. Rohrig, J. Schmidt, M. John, J. Schell, and T. Bisseling. 1997. Microspectroscopic imaging of nodulation factor-binding sites on living Vicia sativa roots using a novel bioactive fluorescent nodulation factor. Biophys. J. 72:1986-1996.
  • 29
    • 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
  • 30
    • 25844499242 scopus 로고    scopus 로고
    • Quantitative multiphoton spectral imaging and its use for measuring resonance energy transfer
    • Thaler, C., S. V. Koushik, P. S. Blank, and S. S. Vogel. 2005. Quantitative multiphoton spectral imaging and its use for measuring resonance energy transfer. Biophys. J. 89:2736-2749.
    • (2005) Biophys. J , vol.89 , pp. 2736-2749
    • Thaler, C.1    Koushik, S.V.2    Blank, P.S.3    Vogel, S.S.4
  • 31
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney, C., and G. Danuser. 2003. FRET or no FRET: a quantitative comparison. Biophys. J. 84:3992-4010.
    • (2003) Biophys. J , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 32
    • 18644377743 scopus 로고    scopus 로고
    • Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins
    • Borst, J. W., M. A. Hink, A. van Hoek, and A. J. Visser. 2005. Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins. J. Fluoresc. 15:153-160.
    • (2005) J. Fluoresc , vol.15 , pp. 153-160
    • Borst, J.W.1    Hink, M.A.2    van Hoek, A.3    Visser, A.J.4
  • 33
    • 0033514515 scopus 로고    scopus 로고
    • Dynamic and quantitative Ca2+ measurements using improved cameleons
    • Miyawaki, A., O. Griesbeck, R. Heim, and R. Y. Tsien. 1999. Dynamic and quantitative Ca2+ measurements using improved cameleons. Proc. Natl. Acad. Sci. USA. 96:2135-2140.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2135-2140
    • Miyawaki, A.1    Griesbeck, O.2    Heim, R.3    Tsien, R.Y.4
  • 34
    • 20444383852 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching
    • Van Munster, E. B., G. J. Kremers, M. J. Adjobo-Hermans, and T. W. Gadella Jr. 2005. Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching. J. Microsc. 218:253-262.
    • (2005) J. Microsc , vol.218 , pp. 253-262
    • Van Munster, E.B.1    Kremers, G.J.2    Adjobo-Hermans, M.J.3    Gadella Jr., T.W.4
  • 36
    • 0034094370 scopus 로고    scopus 로고
    • Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer
    • Vanderklish, P. W., L. A. Krushel, B. H. Holst, J. A. Gally, K. L. Crossin, and G. M. Edelman. 2000. Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA. 97:2253-2258.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2253-2258
    • Vanderklish, P.W.1    Krushel, L.A.2    Holst, B.H.3    Gally, J.A.4    Crossin, K.L.5    Edelman, G.M.6
  • 37
    • 0037178132 scopus 로고    scopus 로고
    • Diheteroarylethenes as thermally stable photoswitchable acceptors in photochromic fluorescence resonance energy transfer (pcFRET)
    • Giordano, L., T. M. Jovin, M. Irie, and E. A. Jares-Erijman. 2002. Diheteroarylethenes as thermally stable photoswitchable acceptors in photochromic fluorescence resonance energy transfer (pcFRET). J. Am. Chem. Soc. 124:7481-7489.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 7481-7489
    • Giordano, L.1    Jovin, T.M.2    Irie, M.3    Jares-Erijman, E.A.4
  • 38
    • 0442278168 scopus 로고    scopus 로고
    • Resonance energy transfer for assessing the molecular integrity of proteins for local delivery
    • Wu, D., and E. R. Edelman. 2004. Resonance energy transfer for assessing the molecular integrity of proteins for local delivery. Biotechnol. Bioeng. 85:406-412.
    • (2004) Biotechnol. Bioeng , vol.85 , pp. 406-412
    • Wu, D.1    Edelman, E.R.2
  • 39
    • 0032488791 scopus 로고    scopus 로고
    • Fluorescent, sequence-selective peptide detection by synthetic small molecules
    • Chen, C. T., H. Wagner, and W. C. Still. 1998. Fluorescent, sequence-selective peptide detection by synthetic small molecules. Science. 279:851-853.
    • (1998) Science , vol.279 , pp. 851-853
    • Chen, C.T.1    Wagner, H.2    Still, W.C.3
  • 40
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP
    • Ganesan, S., S. M. Ameer-Beg, T. T. Ng, B. Vojnovic, and F. S. Wouters. 2006. A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc. Natl. Acad. Sci. USA. 103:4089-4094.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, F.S.5
  • 41
    • 0345306724 scopus 로고    scopus 로고
    • A purple-blue chromoprotein from Goniopora tenuidens belongs to the DsRed subfamily of GFP-like proteins
    • Martynov, V. I., B. I. Maksimov, N. Y. Martynova, A. A. Pakhomov, N. G. Gurskaya, and S. A. Lukyanov. 2003. A purple-blue chromoprotein from Goniopora tenuidens belongs to the DsRed subfamily of GFP-like proteins. J. Biol. Chem. 278:46288-46292.
    • (2003) J. Biol. Chem , vol.278 , pp. 46288-46292
    • Martynov, V.I.1    Maksimov, B.I.2    Martynova, N.Y.3    Pakhomov, A.A.4    Gurskaya, N.G.5    Lukyanov, S.A.6
  • 43
    • 23644453291 scopus 로고    scopus 로고
    • Multiparameter imaging for the analysis of intracellular signaling
    • Schultz, C., A. Schleifenbaum, J. Goedhart, and T. W. Gadella Jr. 2005. Multiparameter imaging for the analysis of intracellular signaling. ChemBioChem. 6:1323-1330.
    • (2005) ChemBioChem , vol.6 , pp. 1323-1330
    • Schultz, C.1    Schleifenbaum, A.2    Goedhart, J.3    Gadella Jr., T.W.4
  • 44
    • 26444599595 scopus 로고    scopus 로고
    • Development and characterization of green fluorescent protein mutants with altered lifetimes
    • Scruggs, A. W., C. L. Flores, R. Wachter, and N. W. Woodbury. 2005. Development and characterization of green fluorescent protein mutants with altered lifetimes. Biochemistry. 44:13377-13384.
    • (2005) Biochemistry , vol.44 , pp. 13377-13384
    • Scruggs, A.W.1    Flores, C.L.2    Wachter, R.3    Woodbury, N.W.4
  • 45
    • 28444451587 scopus 로고    scopus 로고
    • Fluorescence lifetime heterogeneity resolution in the frequency domain by lifetime moments analysis
    • Esposito, A., H. C. Gerritsen, and F. S. Wouters. 2005. Fluorescence lifetime heterogeneity resolution in the frequency domain by lifetime moments analysis. Biophys. J. 89:4286-4299.
    • (2005) Biophys. J , vol.89 , pp. 4286-4299
    • Esposito, A.1    Gerritsen, H.C.2    Wouters, F.S.3
  • 47
    • 10044227172 scopus 로고    scopus 로고
    • Evolution of new nonantibody proteins via iterative somatic hypermutation
    • Wang, L., W. C. Jackson, P. A. Steinbach, and R. Y. Tsien. 2004. Evolution of new nonantibody proteins via iterative somatic hypermutation. Proc. Natl. Acad. Sci. USA. 101:16745-16749.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16745-16749
    • Wang, L.1    Jackson, W.C.2    Steinbach, P.A.3    Tsien, R.Y.4
  • 48
    • 0002223754 scopus 로고    scopus 로고
    • Fluorescence lifetime-resolved imaging microscopy: A general description of lifetime-resolved imaging measurements
    • J. Slavík, editor. Plenum Press, New York
    • Clegg, R. M., and P. C. Scheider. 1996. Fluorescence lifetime-resolved imaging microscopy: a general description of lifetime-resolved imaging measurements. In Fluorescence Microscopy and Fluorescent Probes. J. Slavík, editor. Plenum Press, New York. 15-33.
    • (1996) Fluorescence Microscopy and Fluorescent Probes , pp. 15-33
    • Clegg, R.M.1    Scheider, P.C.2
  • 49
    • 0003127798 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy (FLIM): Instrumentation and applications
    • 2nd ed. W. Mason, editor. Academic Press, London
    • Gadella, T. W. 1999. Fluorescence lifetime imaging microscopy (FLIM): instrumentation and applications. In Fluorescent and Luminescent Probes, 2nd ed. W. Mason, editor. Academic Press, London. 467-479.
    • (1999) Fluorescent and Luminescent Probes , pp. 467-479
    • Gadella, T.W.1


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