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Volumn 215, Issue 3, 2004, Pages 281-296

Minimizing photobleaching during confocal microscopy of fluorescent probes bound to chromatin: Role of anoxia and photon flux

Author keywords

3D image reconstruction; Chromomycin A3; eGFP; Imaging; Oxygen; Propidium iodide

Indexed keywords

CHROMOPHORES; CLEANING; DNA; FLUOROPHORES; IMAGE RECONSTRUCTION; IMAGE RESOLUTION; PHOTOBLEACHING; PHOTONS; PROTEINS; REACTION RATES; SIGNAL TO NOISE RATIO;

EID: 4544381360     PISSN: 00222720     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0022-2720.2004.01377.x     Document Type: Article
Times cited : (101)

References (58)
  • 1
    • 0026580198 scopus 로고
    • Reduction of the rate of fluorescence decay of FITC- and carboxyfluorescein- stained cells by anti-FITC antibodies
    • Abuknesha, R.A., al-Mazeedi, H.M. & Price, R.G. (1992) Reduction of the rate of fluorescence decay of FITC- and carboxyfluorescein- stained cells by anti-FITC antibodies. Histochem. J. 24, 73-77.
    • (1992) Histochem. J. , vol.24 , pp. 73-77
    • Abuknesha, R.A.1    Al-Mazeedi, H.M.2    Price, R.G.3
  • 3
    • 0022226126 scopus 로고
    • Fluorescence decay measurements for determining the relative content of ethidium bromide to DNA in situ in cell nuclei
    • Araki, T. & Yamada, M. (1985) Fluorescence decay measurements for determining the relative content of ethidium bromide to DNA in situ in cell nuclei. Histochemistry, 83, 299-301.
    • (1985) Histochemistry , vol.83 , pp. 299-301
    • Araki, T.1    Yamada, M.2
  • 6
    • 0030953638 scopus 로고    scopus 로고
    • Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein
    • Brejc, K., Sixma, T.K., Kitts, P.A., Kain, S.R., Tsien, R.Y., Ormo, M. & Remington, S.J. (1997) Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein. Proc. Natl. Acad. Sci. USA, 94, 2306-2311.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2306-2311
    • Brejc, K.1    Sixma, T.K.2    Kitts, P.A.3    Kain, S.R.4    Tsien, R.Y.5    Ormo, M.6    Remington, S.J.7
  • 7
    • 0025916787 scopus 로고
    • Fluorescence anisotropy decay of ethidium bound to nucleosome core particles. 1. Rotational diffusion indicates an extended structure at low ionic strength
    • Brown, D.W., Libertini, L.J. & Small, E.W. (1991) Fluorescence anisotropy decay of ethidium bound to nucleosome core particles. 1. Rotational diffusion indicates an extended structure at low ionic strength. Biochemistry, 30, 5293-5303.
    • (1991) Biochemistry , vol.30 , pp. 5293-5303
    • Brown, D.W.1    Libertini, L.J.2    Small, E.W.3
  • 8
    • 0000715189 scopus 로고
    • Dynamics of electron transfer between intercalated polycyclic molecules: Effect of interspersed bases
    • Brun, A.M. & Harriman, A. (1992) Dynamics of electron transfer between intercalated polycyclic molecules: effect of interspersed bases. J. Am. Chem. Soc. 114, 3656-3660.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3656-3660
    • Brun, A.M.1    Harriman, A.2
  • 9
    • 0036618994 scopus 로고    scopus 로고
    • A new biophysics approach using photoacoustic spectroscopy to study the DNA-ethidium bromide interaction
    • Bugs, R. & Cornelio, M.L. (2002) A new biophysics approach using photoacoustic spectroscopy to study the DNA-ethidium bromide interaction. Eur Biophys. J. 31, 232-240.
    • (2002) Eur Biophys. J. , vol.31 , pp. 232-240
    • Bugs, R.1    Cornelio, M.L.2
  • 10
    • 0029757121 scopus 로고    scopus 로고
    • Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer
    • Chattoraj, M., King, B.A., Bublitz, G.U. & Boxer, S.G. (1996) Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transfer. Proc. Natl. Acad. Sci. USA, 93, 8362-8367.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8362-8367
    • Chattoraj, M.1    King, B.A.2    Bublitz, G.U.3    Boxer, S.G.4
  • 11
    • 0036293716 scopus 로고    scopus 로고
    • High-order photobleaching of green fluorescent protein inside live cells in two-photon excitation microscopy
    • Chen, T.S., Zeng, S.Q., Luo, Q.M., Zhang, Z.H. & Zhou, W. (2002) High-order photobleaching of green fluorescent protein inside live cells in two-photon excitation microscopy. Biochem. Biophys. Res. Commun, 291, 1272-1275.
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 1272-1275
    • Chen, T.S.1    Zeng, S.Q.2    Luo, Q.M.3    Zhang, Z.H.4    Zhou, W.5
  • 12
    • 0035384605 scopus 로고    scopus 로고
    • Photophysical properties of fluorescent DNA-dyes bound to single- And double-stranded DNA in aqueous buffered solution
    • Cosa, G., Focsaneanu, K.S., McLean, J.R., McNamee, J.P. & Scaiano, J.C. (2001) Photophysical properties of fluorescent DNA-dyes bound to single- and double-stranded DNA in aqueous buffered solution. Photochem. Photobiol 73, 585-599.
    • (2001) Photochem. Photobiol. , vol.73 , pp. 585-599
    • Cosa, G.1    Focsaneanu, K.S.2    McLean, J.R.3    McNamee, J.P.4    Scaiano, J.C.5
  • 13
    • 0003557851 scopus 로고
    • Acridine orange: A versatile probe of nucleic acids and other cell constituents
    • ed. by M. R. Melamed, M. L. Mendelson and T. Lindmo, Wiley-Liss, New York
    • Darzynkiewicz, Z. & Kapuscinski (1990) Acridine orange: a versatile probe of nucleic acids and other cell constituents. Flow Cytometry and Sorting 2 (ed. by M. R. Melamed, M. L. Mendelson and T. Lindmo), pp. 291-314. Wiley-Liss, New York.
    • (1990) Flow Cytometry and Sorting , vol.2 , pp. 291-314
    • Darzynkiewicz, Z.1    Kapuscinski2
  • 14
    • 0035981150 scopus 로고    scopus 로고
    • (2+) with animal and plant cells in vitro. Mechanism of phototoxicity and conditions for non-invasive oxygen measurements
    • (2+) with animal and plant cells in vitro. Mechanism of phototoxicity and conditions for non-invasive oxygen measurements. J. Photochem. Photobiol. B, 65, 136-144.
    • (2001) J. Photochem. Photobiol. B , vol.65 , pp. 136-144
    • Dobrucki, J.W.1
  • 16
    • 0029135913 scopus 로고
    • Analysis of antifading reagents for fluorescence microscopy
    • Florijn, R.J., Slats, J., Tanke, H.J. & Raap, A.K. (1995) Analysis of antifading reagents for fluorescence microscopy. Cytometry, 19, 177-182.
    • (1995) Cytometry , vol.19 , pp. 177-182
    • Florijn, R.J.1    Slats, J.2    Tanke, H.J.3    Raap, A.K.4
  • 17
    • 0024948025 scopus 로고
    • Antitumour drug-DNA interactions: NMR studies of echinomycin and chromomycin complexes
    • Gao, X.L. & Patel, D.J. (1989a) Antitumour drug-DNA interactions: NMR studies of echinomycin and chromomycin complexes. Q Rev. Biophys. 22, 93-138.
    • (1989) Q Rev. Biophys. , vol.22 , pp. 93-138
    • Gao, X.L.1    Patel, D.J.2
  • 18
    • 0024579256 scopus 로고
    • Solution structure of the chromomycin-DNA complex
    • Gao, X.L. & Patel, D.J. (1989b) Solution structure of the chromomycin-DNA complex. Biochemistry, 28, 751-762.
    • (1989) Biochemistry , vol.28 , pp. 751-762
    • Gao, X.L.1    Patel, D.J.2
  • 19
    • 0025690237 scopus 로고
    • Chromomycin dimer-DNA oligomer complexes. Sequence selectivity and divalent cation specificity
    • Gao, X.L. & Patel, D.J. (1990) Chromomycin dimer-DNA oligomer complexes. Sequence selectivity and divalent cation specificity. Biochemistry, 29, 10940-10956.
    • (1990) Biochemistry , vol.29 , pp. 10940-10956
    • Gao, X.L.1    Patel, D.J.2
  • 20
    • 0019943371 scopus 로고
    • Fluorescence microscopy: Reduced photobleaching of rhodamine and fluorescein protein conjugates by n-propyl gallate
    • Giloh, H. & Sedat, J.W. (1982) Fluorescence microscopy: reduced photobleaching of rhodamine and fluorescein protein conjugates by n-propyl gallate. Science, 217, 1252-1255.
    • (1982) Science , vol.217 , pp. 1252-1255
    • Giloh, H.1    Sedat, J.W.2
  • 21
    • 0034513772 scopus 로고    scopus 로고
    • Green fluorescent protein photobleaching: A model for protein damage by endogenous and exogenous singlet oxygen
    • Greenbaum, L., Rothmann, C., Lavie, R. & Malik, Z. (2000) Green fluorescent protein photobleaching: a model for protein damage by endogenous and exogenous singlet oxygen. Biol. Chem. 381, 1251-1258.
    • (2000) Biol. Chem. , vol.381 , pp. 1251-1258
    • Greenbaum, L.1    Rothmann, C.2    Lavie, R.3    Malik, Z.4
  • 22
    • 0035033890 scopus 로고    scopus 로고
    • Autofluorescent proteins in single-molecule research: Applications to live cell imaging microscopy
    • Harms, G.S., Cognet, L., Lommerse, P.H., Blab, G.A. & Schmidt, T. (2001) Autofluorescent proteins in single-molecule research: applications to live cell imaging microscopy. Biophys. J. 80, 2396-2408.
    • (2001) Biophys. J. , vol.80 , pp. 2396-2408
    • Harms, G.S.1    Cognet, L.2    Lommerse, P.H.3    Blab, G.A.4    Schmidt, T.5
  • 23
    • 0032506222 scopus 로고    scopus 로고
    • Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy
    • Haupts, U., Maiti, S., Schwille, P. & Webb, W.W. (1998) Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. USA, 95, 13573-13578.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13573-13578
    • Haupts, U.1    Maiti, S.2    Schwille, P.3    Webb, W.W.4
  • 24
    • 0017241350 scopus 로고
    • Quantum efficiency independence of the time integrated emission from a fluorescent molecule
    • Hirschfeld, T. (1976) Quantum efficiency independence of the time integrated emission from a fluorescent molecule. Appl. Opt. 15, 3135-3139.
    • (1976) Appl. Opt. , vol.15 , pp. 3135-3139
    • Hirschfeld, T.1
  • 25
    • 0032568321 scopus 로고    scopus 로고
    • Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells
    • Kanda, T., Sullivan, K.F. & Wahl, G.M. (1998) Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells. Curr. Biol. 8, 377-385.
    • (1998) Curr. Biol. , vol.8 , pp. 377-385
    • Kanda, T.1    Sullivan, K.F.2    Wahl, G.M.3
  • 26
    • 0034819772 scopus 로고    scopus 로고
    • Photobleaching of asymmetric cyanines used for fluorescence imaging of single DNA molecules
    • Kanony, C., Akerman, B. & Tuite, E. (2001) Photobleaching of asymmetric cyanines used for fluorescence imaging of single DNA molecules. J. Am. Chem. Soc. 123, 7985-7995.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7985-7995
    • Kanony, C.1    Akerman, B.2    Tuite, E.3
  • 27
    • 0022801215 scopus 로고
    • Fluorescence photobleaching recovery techniques for translational and slow rotational diffusion in solution and on cell surfaces
    • Koppel, D.E. (1986) Fluorescence photobleaching recovery techniques for translational and slow rotational diffusion in solution and on cell surfaces. Biochem. Soc. Trans. 14, 842-845.
    • (1986) Biochem. Soc. Trans. , vol.14 , pp. 842-845
    • Koppel, D.E.1
  • 28
    • 0036356831 scopus 로고    scopus 로고
    • Intracellular photobleaching of 5,10,15,20-tetrakis (m-hydroxyphenyl) chlorin (Foscan) exhibits a complex dependence on oxygen level and fluence rate
    • Kunz, L. & MacRobert, A.J. (2002) Intracellular photobleaching of 5,10,15,20-tetrakis (m-hydroxyphenyl) chlorin (Foscan) exhibits a complex dependence on oxygen level and fluence rate. Photochem. Photobiol. 75, 28-35.
    • (2002) Photochem. Photobiol. , vol.75 , pp. 28-35
    • Kunz, L.1    MacRobert, A.J.2
  • 29
    • 0003018251 scopus 로고
    • A flash photolysis study of fluorescein
    • Lindqvist, L. (1960) A flash photolysis study of fluorescein. Arkiv Kemi. 16, 79-138.
    • (1960) Arkiv Kemi. , vol.16 , pp. 79-138
    • Lindqvist, L.1
  • 30
    • 0027495902 scopus 로고
    • Comparison of anti-fading agents used in fluorescence microscopy: Image analysis and laser confocal microscopy study
    • Longin, A., Souchier, C., Ffrench, M. & Bryon, P.A. (1993) Comparison of anti-fading agents used in fluorescence microscopy: image analysis and laser confocal microscopy study. J. Histochem. Cytochem. 41, 1833-1840.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1833-1840
    • Longin, A.1    Souchier, C.2    Ffrench, M.3    Bryon, P.A.4
  • 32
    • 0026066232 scopus 로고
    • Characteristics of an infinite life span diploid human fibroblast cell strain and a near-diploid strain arising from a clone of cells expressing a transfected v-myc oncogene
    • Morgan, T.L., Yang, D.J., Fry, D.G., Hurlin, P.J., Kohler, S.K., Maher, V.M. & McCormick, J.J. (1991) Characteristics of an infinite life span diploid human fibroblast cell strain and a near-diploid strain arising from a clone of cells expressing a transfected v-myc oncogene. Exp. Cell Res. 197, 125-136.
    • (1991) Exp. Cell Res. , vol.197 , pp. 125-136
    • Morgan, T.L.1    Yang, D.J.2    Fry, D.G.3    Hurlin, P.J.4    Kohler, S.K.5    Maher, V.M.6    McCormick, J.J.7
  • 33
    • 0030062051 scopus 로고    scopus 로고
    • Fading correction for fluorescence quantitation in confocal microscopy
    • Nagelhus, T.A., Slupphaug, G., Krokan, H.E. & Lindmo, T. (1996) Fading correction for fluorescence quantitation in confocal microscopy. Cytometry, 23, 187-195.
    • (1996) Cytometry , vol.23 , pp. 187-195
    • Nagelhus, T.A.1    Slupphaug, G.2    Krokan, H.E.3    Lindmo, T.4
  • 34
    • 0017372923 scopus 로고
    • Mechanism of ethidium bromide fluorescence enhancement on binding to nucleic acids
    • Olmsted, J. III & Kearns, D.R. (1977) Mechanism of ethidium bromide fluorescence enhancement on binding to nucleic acids. Biochemistry, 16, 3647-3654.
    • (1977) Biochemistry , vol.16 , pp. 3647-3654
    • Olmsted III, J.1    Kearns, D.R.2
  • 35
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson, G.H., Knobel, S.M., Sharif, W.D., Kain, S.R. & Piston, D.W. (1997) Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J. 73, 2782-2790.
    • (1997) Biophys. J. , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 36
    • 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
  • 37
    • 0002633701 scopus 로고
    • Fundamental limits in confocal microscopy
    • ed. by J. B. Pawley, Plenum Press, New York
    • Pawley, J. (1995) Fundamental limits in confocal microscopy. Handbook of Biological Confcocal Microscopy (ed. by J. B. Pawley), pp. 19-37. Plenum Press, New York.
    • (1995) Handbook of Biological Confcocal Microscopy , pp. 19-37
    • Pawley, J.1
  • 38
    • 0016272796 scopus 로고
    • A microfluorimetric study of translational diffusion in erythrocyte membranes
    • Peters, R., Peters, J., Tews, K.H. & Bahr, W. (1974) A microfluorimetric study of translational diffusion in erythrocyte membranes. Biochim. Biophys. Acta, 367, 282-294.
    • (1974) Biochim. Biophys. Acta , vol.367 , pp. 282-294
    • Peters, R.1    Peters, J.2    Tews, K.H.3    Bahr, W.4
  • 39
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R.D. & Misteli, T. (2000) High mobility of proteins in the mammalian cell nucleus. Nature, 404, 604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 40
    • 0030741606 scopus 로고    scopus 로고
    • Imaging individual green fluorescent proteins
    • Pierce, D.W., Hom-Booher, N. & Vale, R.D. (1997) Imaging individual green fluorescent proteins. Nature, 388, 338.
    • (1997) Nature , vol.388 , pp. 338
    • Pierce, D.W.1    Hom-Booher, N.2    Vale, R.D.3
  • 41
    • 85023069409 scopus 로고    scopus 로고
    • Biophysics of the green fluorescent protein
    • Green Fluorescent Proteins (ed. by K. F. Sullivan and S. A. Kay)
    • Prendergast, E.G. (1999) Biophysics of the green fluorescent protein. Green Fluorescent Proteins (ed. by K. F. Sullivan and S. A. Kay). Meth. Cell Biol. 58, 1-18.
    • (1999) Meth. Cell Biol. , vol.58 , pp. 1-18
    • Prendergast, E.G.1
  • 42
    • 17444451965 scopus 로고    scopus 로고
    • Fluorescence lifetime, precision calorimetry, and fluorescence energy transfer measurements in the study of normal and tumoral chromatin structure
    • Radu, L., Preoteasa, V., Radulescu, I. & Radu, S. (1997) Fluorescence lifetime, precision calorimetry, and fluorescence energy transfer measurements in the study of normal and tumoral chromatin structure. J. Mol Struct. 408/409, 191-194.
    • (1997) J. Mol Struct. , vol.408-409 , pp. 191-194
    • Radu, L.1    Preoteasa, V.2    Radulescu, I.3    Radu, S.4
  • 43
    • 0029910067 scopus 로고    scopus 로고
    • Interactions of intercalating fluorochromes with DNA analyzed by conventional and fluorescence lifetime flow cytometry utilizing deuterium oxide
    • Sailer, B.L., Nastasi, A.J., Valdez, J.G., Steinkamp, J.A. & Crissman, H.A. (1996) Interactions of intercalating fluorochromes with DNA analyzed by conventional and fluorescence lifetime flow cytometry utilizing deuterium oxide. Cytometry, 25, 164-172.
    • (1996) Cytometry , vol.25 , pp. 164-172
    • Sailer, B.L.1    Nastasi, A.J.2    Valdez, J.G.3    Steinkamp, J.A.4    Crissman, H.A.5
  • 44
    • 0029057619 scopus 로고
    • Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy
    • Song, L., Hennink, E.J., Young, I.T. & Tanke, H.J. (1995) Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy. Biophys. J. 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
  • 45
    • 0030966142 scopus 로고    scopus 로고
    • Influence of fluorochrome labeling density on the photobleaching kinetics of fluorescein in microscopy
    • Song, L., van Gijlswijk, R.P., Young, I.T. & Tanke, H.J. (1997) Influence of fluorochrome labeling density on the photobleaching kinetics of fluorescein in microscopy. Cytometry, 27, 213-223.
    • (1997) Cytometry , vol.27 , pp. 213-223
    • Song, L.1    Van Gijlswijk, R.P.2    Young, I.T.3    Tanke, H.J.4
  • 46
    • 0030029881 scopus 로고    scopus 로고
    • Influence of the triplet excited state on the photobleaching kinetics of fluorescein in microscopy
    • Song, L., Varma, C.A., Verhoeven, J.W. & Tanke, H.J. (1996) Influence of the triplet excited state on the photobleaching kinetics of fluorescein in microscopy. Biophys. J. 70, 2959-2968.
    • (1996) Biophys. J. , vol.70 , pp. 2959-2968
    • Song, L.1    Varma, C.A.2    Verhoeven, J.W.3    Tanke, H.J.4
  • 47
    • 0026785419 scopus 로고
    • Quantitative foot-printing analysis of the chromomycin A3-DNA interaction
    • Stankus, A., Goodisman, J. & Dabrowiak, J.C. (1992) Quantitative foot-printing analysis of the chromomycin A3-DNA interaction. Biochemistry, 31, 9310-9318.
    • (1992) Biochemistry , vol.31 , pp. 9310-9318
    • Stankus, A.1    Goodisman, J.2    Dabrowiak, J.C.3
  • 48
    • 0031907408 scopus 로고    scopus 로고
    • Contrast, resolution, pixelation, dynamic range and signal to noise ratio: Fundamental its to resolution in fluorescence light microscopy
    • Stelzer, E.H.K. (1998) Contrast, resolution, pixelation, dynamic range and signal to noise ratio: fundamental its to resolution in fluorescence light microscopy. J. Microsc. 189, 15-24.
    • (1998) J. Microsc. , vol.189 , pp. 15-24
    • Stelzer, E.H.K.1
  • 49
    • 0026577623 scopus 로고
    • Epitope mapping by photobleaching fluorescence resonance energy transfer measurements using a laser scanning microscope system
    • Szabo, G. Jr, Pine, P.S., Weaver, J.L., Kasari, M. & Aszalos, A. (1992) Epitope mapping by photobleaching fluorescence resonance energy transfer measurements using a laser scanning microscope system. Biophys. J. 61, 661-670.
    • (1992) Biophys. J. , vol.61 , pp. 661-670
    • Szabo Jr., G.1    Pine, P.S.2    Weaver, J.L.3    Kasari, M.4    Aszalos, A.5
  • 50
    • 0034692589 scopus 로고    scopus 로고
    • Fluorescence imaging of pyrene-labeled lipids in living cells
    • Tanhuanpaa, K., Virtanen, J. & Somerharju, P. (2000) Fluorescence imaging of pyrene-labeled lipids in living cells. Biochim. Biophys. Acta, 1497, 308-320.
    • (2000) Biochim. Biophys. Acta , vol.1497 , pp. 308-320
    • Tanhuanpaa, K.1    Virtanen, J.2    Somerharju, P.3
  • 51
    • 0024661533 scopus 로고
    • A study of some polypyridylruthenium (II) complexes as DNA binders and photocleavage reagents
    • Tossi, A.B. & Kelly, J.M. (1989) A study of some polypyridylruthenium (II) complexes as DNA binders and photocleavage reagents. Photochem. Photobiol. 49, 545-556.
    • (1989) Photochem. Photobiol. , vol.49 , pp. 545-556
    • Tossi, A.B.1    Kelly, J.M.2
  • 52
    • 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
  • 53
    • 0003760907 scopus 로고
    • Fluorophores for Confocal Microscopy. Photophysics and Photochemistry
    • ed. by J. B. Pawley, Plenum Press, New York
    • Tsien, R.Y. & Waggoner (1995) Fluorophores for Confocal Microscopy. Photophysics and Photochemistry. Handbook of Biological Confocal Microscopy 2 (ed. by J. B. Pawley), pp. 267-279. Plenum Press, New York.
    • (1995) Handbook of Biological Confocal Microscopy , vol.2 , pp. 267-279
    • Tsien, R.Y.1    Waggoner2
  • 54
    • 0003192391 scopus 로고
    • Switch-over of the mechanism of primary processes in the photo-oxidation of xanthene dyes as revealed by the oxygen consumption experiments
    • Usui, Y., Itoh, K. & Koizumi, M. (1965) Switch-over of the mechanism of primary processes in the photo-oxidation of xanthene dyes as revealed by the oxygen consumption experiments. Bull. Chem. Soc. Jpn 38, 1015-1022.
    • (1965) Bull. Chem. Soc. Jpn. , vol.38 , pp. 1015-1022
    • Usui, Y.1    Itoh, K.2    Koizumi, M.3
  • 55
    • 0032101903 scopus 로고    scopus 로고
    • Heterogeneous photobleaching in confocal microscopy caused by differences in refractive index and excitation mode
    • Van Oostveldt, P., Verhaegen, F. & Messens, K. (1998) Heterogeneous photobleaching in confocal microscopy caused by differences in refractive index and excitation mode. Cytometry, 32, 137-146.
    • (1998) Cytometry , vol.32 , pp. 137-146
    • Van Oostveldt, P.1    Verhaegen, F.2    Messens, K.3
  • 56
    • 0033065308 scopus 로고    scopus 로고
    • Shedding light on the dark and weakly fluorescent states of green fluorescent proteins
    • Weber, W., Helms, V., McCammon, J.A. & Langhoff, P.W. (1999) Shedding light on the dark and weakly fluorescent states of green fluorescent proteins. Proc. Natl. Acad. Sci. USA, 96, 6177-6182.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6177-6182
    • Weber, W.1    Helms, V.2    McCammon, J.A.3    Langhoff, P.W.4
  • 57
    • 0023369196 scopus 로고
    • An evaluation of confocal versus conventional imaging of biological structures by fluorescence light microscopy
    • White, J.G., Amos, W.B. & Fordham, M. (1987) An evaluation of confocal versus conventional imaging of biological structures by fluorescence light microscopy. J. Cell Biol. 105, 41-48.
    • (1987) J. Cell Biol. , vol.105 , pp. 41-48
    • White, J.G.1    Amos, W.B.2    Fordham, M.3
  • 58
    • 0023148860 scopus 로고
    • Photostability studies of phycobiliprotein fluorescent labels
    • White, J.C. & Stryer, L. (1987) Photostability studies of phycobiliprotein fluorescent labels. Anal. Biochem. 161, 442-452.
    • (1987) Anal. Biochem. , vol.161 , pp. 442-452
    • White, J.C.1    Stryer, L.2


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