메뉴 건너뛰기




Volumn 73, Issue 5, 1997, Pages 2782-2790

Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; MUTANT PROTEIN;

EID: 0030784698     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78307-3     Document Type: Article
Times cited : (704)

References (35)
  • 2
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Y. Tu, G. Euskirchen, W. W. Ward, and D. C. Prasher. 1994. Green fluorescent protein as a marker for gene expression. Science. 263:802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 3
    • 0029757121 scopus 로고    scopus 로고
    • Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer
    • Chattoraj, M., B. A. King, G. U. Bublitz, and S. G. Boxer. 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
  • 5
    • 0031050445 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): A marker for gene expression in Candida albicans
    • Cormack, B. P., G. Bertram, M. Egerton, N. A. R. Gow, S. Falkow, and A. J. P. Brown. 1997. Green fluorescent protein (GFP): a marker for gene expression in Candida albicans. Microbiolology. 143(Part2): 303-311.
    • (1997) Microbiolology , vol.143 , Issue.PART 2 , pp. 303-311
    • Cormack, B.P.1    Bertram, G.2    Egerton, M.3    Gow, N.A.R.4    Falkow, S.5    Brown, A.J.P.6
  • 6
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B. P., R. H. Valdivia, and S. Falkow. 1996. FACS-optimized mutants of the green fluorescent protein (GFP). Gene. 173:33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 7
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., E. A. Whitchorn, F., Tate, and W. P. C. Stemmer. 1996. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nature Biotechnol. 14:315-319.
    • (1996) Nature Biotechnol. , vol.14 , pp. 315-319
    • Crameri, A.1    Whitchorn, E.A.2    Tate, F.3    Stemmer, W.P.C.4
  • 9
    • 0030600135 scopus 로고    scopus 로고
    • Green fluorescent protein: Applications in biology
    • Gerdes, H.-H., and C. Kaether. 1996. Green fluorescent protein: applications in biology. FEBS Lett. 389:44-47.
    • (1996) FEBS Lett. , vol.389 , pp. 44-47
    • Gerdes, H.-H.1    Kaether, C.2
  • 10
    • 0030111265 scopus 로고    scopus 로고
    • Codon usage limitation in the expression of HIV-1 envelope glycoprotein
    • Haas, J., E.-C. Park, and B. Seed. 1996. Codon usage limitation in the expression of HIV-1 envelope glycoprotein. Curr. Biol. 6:315-324.
    • (1996) Curr. Biol. , vol.6 , pp. 315-324
    • Haas, J.1    Park, E.-C.2    Seed, B.3
  • 11
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim, R., A. B. Cubitt, and R. Y. Tsien. 1995. Improved green fluorescence. Nature. 373:663-664.
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 12
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • Heim, R., D. C. Prasher, and R. Y. Tsien. 1994. Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc. Natl. Acad. Sci. USA. 91:12501-12504.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 13
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R., and R. Y. Tsien. 1996. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr Biol. 6:178-182.
    • (1996) Curr Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 14
    • 0024534818 scopus 로고
    • Resonance energy transfer microscopy
    • D. L. Taylor and Y. Wang, editors. Academic Press, San Diego. CA
    • Herman, B. 1989. Resonance energy transfer microscopy. In Fluorescence Microscopy of Living Cells in Culture. D. L. Taylor and Y. Wang, editors. Academic Press, San Diego. CA. 220-243.
    • (1989) Fluorescence Microscopy of Living Cells in Culture , pp. 220-243
    • Herman, B.1
  • 15
    • 0028777967 scopus 로고
    • Aequorea green fluorescent protein: Expression of the gene and fluorescent characteristics of the recombinant protein
    • Inouye, S., and F. I. Tsuji. 1994. Aequorea green fluorescent protein: expression of the gene and fluorescent characteristics of the recombinant protein. FEBS Lett. 341:277-280.
    • (1994) FEBS Lett. , vol.341 , pp. 277-280
    • Inouye, S.1    Tsuji, F.I.2
  • 16
    • 0029160620 scopus 로고
    • Visualisation of protein transport along the secretory pathway using green fluorescent protein
    • Kaether, C., and H. Gerdes. 1995. Visualisation of protein transport along the secretory pathway using green fluorescent protein. FEBS Lett. 369:267-271.
    • (1995) FEBS Lett. , vol.369 , pp. 267-271
    • Kaether, C.1    Gerdes, H.2
  • 17
    • 0022543860 scopus 로고
    • Probing the structure of the cytoplasm
    • Luhy-Phelps, K., D. L. Taylor, and F. Lanni. 1986. Probing the structure of the cytoplasm. J. Cell Biol. 102:2015-2022.
    • (1986) J. Cell Biol. , vol.102 , pp. 2015-2022
    • Luhy-Phelps, K.1    Taylor, D.L.2    Lanni, F.3
  • 18
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman, I., R. Fuchs, and A. Helenius. 1986. Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem. 55:663-700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 19
    • 0029898330 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between blue-emitling and red-shifted excitation derivatives of the green fluorescent protein
    • Mitra, R. D., C. M. Silva, and D. C. Youvan. 1996. Fluorescence resonance energy transfer between blue-emitling and red-shifted excitation derivatives of the green fluorescent protein. Gene. 173:13-17.
    • (1996) Gene , vol.173 , pp. 13-17
    • Mitra, R.D.1    Silva, C.M.2    Youvan, D.C.3
  • 20
    • 0016156057 scopus 로고
    • Intermolecular energy transfer in the biolumincscent system of Aquorea
    • Morise, H., O. Shimomura, F. H. Johnson, and J. Winant. 1974. Intermolecular energy transfer in the biolumincscent system of Aquorea. Biochemistry. 13:2656-2662.
    • (1974) Biochemistry , vol.13 , pp. 2656-2662
    • Morise, H.1    Shimomura, O.2    Johnson, F.H.3    Winant, J.4
  • 21
    • 0028850321 scopus 로고
    • Quantitative imaging of green fluorescent protein in cultured cells: Comparison of microscopic techniques, use in fusion proteins and detection limits
    • Niswender, K. D., S. M. Blackman, L. Rohde, M. A. Magnuson, and D. W. Piston. 1995. Quantitative imaging of green fluorescent protein in cultured cells: comparison of microscopic techniques, use in fusion proteins and detection limits. J. Microsc. 180:109-116.
    • (1995) J. Microsc. , vol.180 , pp. 109-116
    • Niswender, K.D.1    Blackman, S.M.2    Rohde, L.3    Magnuson, M.A.4    Piston, D.W.5
  • 22
    • 0029586689 scopus 로고
    • Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells
    • Ogawa, H., S. Inouye, F. I. Tsuji, K. Yasuda and K. Umesono. 1995. Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells. Proc. Natl. Acad. Sci. USA. 92:11899-11903.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11899-11903
    • Ogawa, H.1    Inouye, S.2    Tsuji, F.I.3    Yasuda, K.4    Umesono, K.5
  • 23
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M., A. B. Cubitt, K. Kallio, L. A. Gross, R. Y. Tsien, and S. J. Remington. 1996. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 273:1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 24
    • 84972273353 scopus 로고
    • Imaging of cellular dynamics by two-photon excitation microscopy
    • Piston, D. W., B. D. Bennett, and G. Ying. 1995. Imaging of cellular dynamics by two-photon excitation microscopy. Microsc. Microanal. 1:25-34.
    • (1995) Microsc. Microanal. , vol.1 , pp. 25-34
    • Piston, D.W.1    Bennett, B.D.2    Ying, G.3
  • 25
    • 0026578325 scopus 로고
    • Primary structure of the Aequorca victoria green-fluorescent protein
    • Prasher, D. C., V. K. Eckenrode, W. W. Ward, F. G. Prendergast, and M. J. Cormier. 1992. Primary structure of the Aequorca victoria green-fluorescent protein. Gene. 111:229-233.
    • (1992) Gene , vol.111 , pp. 229-233
    • Prasher, D.C.1    Eckenrode, V.K.2    Ward, W.W.3    Prendergast, F.G.4    Cormier, M.J.5
  • 26
    • 0030087711 scopus 로고    scopus 로고
    • Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo
    • Rizzuto, R., M. Brini, F. D. Giorgi, R. Rossi, R. Heim, R. Y. Tsien, and T. Pozzan. 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    Giorgi, F.D.3    Rossi, R.4    Heim, R.5    Tsien, R.Y.6    Pozzan, T.7
  • 27
    • 0002440925 scopus 로고
    • Appendix A: Bacterial media, antibiotics, and bacterial strains
    • C. Nolan, editor. Cold Spring Harbor Laboratory. Cold Spring Harbor. NY. A.2
    • Sambrook, J., H. F. Fritsch, and T. Maniatis. 1989a. Appendix A: bacterial media, antibiotics, and bacterial strains. In Molecular Cloning: A laboratory Manual. C. Nolan, editor. Cold Spring Harbor Laboratory. Cold Spring Harbor. NY. A.2.
    • (1989) Molecular Cloning: A Laboratory Manual
    • Sambrook, J.1    Fritsch, H.F.2    Maniatis, T.3
  • 28
    • 0000163138 scopus 로고
    • Site-directed mutagensis of cloned DNA
    • C. Nolan, editor. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989b. Site-directed mutagensis of cloned DNA. In Molecular Cloning: A Laboratory Manual. C. Nolan, editor. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. 15.74-15.79.
    • (1989) Molecular Cloning: A Laboratory Manual , pp. 1574-1579
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 29
    • 0000364208 scopus 로고
    • Resolution, background rejection, and signal-to-noise in widefield and confocal microscopy
    • Sandison, D. R., D. W. Piston, R. M. Williams and W. W. Webb. 1995. Resolution, background rejection, and signal-to-noise in widefield and confocal microscopy. Appl. Optics. 34:3576-3588.
    • (1995) Appl. Optics. , vol.34 , pp. 3576-3588
    • Sandison, D.R.1    Piston, D.W.2    Williams, R.M.3    Webb, W.W.4
  • 30
    • 0030452512 scopus 로고    scopus 로고
    • Mutations that suppress the thermosensitivity of green fluorescent protein
    • Siemering, K. R., R. Golbik, R. Sever, and J. Haseloff. 1996. Mutations that suppress the thermosensitivity of green fluorescent protein. Curr. Biol. 6:1653-1663.
    • (1996) Curr. Biol. , vol.6 , pp. 1653-1663
    • Siemering, K.R.1    Golbik, R.2    Sever, R.3    Haseloff, J.4
  • 31
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • D. V. Goeddel, editor. Academic Press. San Diego, CA
    • Studier, F. W., A. H. Rosenberg, J. J. Dunn and J. W. Dubendorff. 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. D. V. Goeddel, editor. Academic Press. San Diego, CA. 60-89.
    • (1990) Methods Enzymol. , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 32
    • 0002870111 scopus 로고
    • Properties of the coelenterate green-fluorescent protein
    • M. A. DeLuca and W. D. McElroy, editors. Academic Press, New York
    • Ward, W. W. 1981. Properties of the coelenterate green-fluorescent protein. In Bioluminescence and Chemiluminesccnce. M. A. DeLuca and W. D. McElroy, editors. Academic Press, New York. 235-242.
    • (1981) Bioluminescence and Chemiluminesccnce , pp. 235-242
    • Ward, W.W.1
  • 34
    • 0029780689 scopus 로고    scopus 로고
    • Mutliphoton fluorescence excitation: New spectral windows for nonlinear microscopy
    • Xu, C., W. Zipfel, J. B. Shear, R. M. Williams, and W. W. Webb. 1996 Mutliphoton fluorescence excitation: new spectral windows for 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
  • 35
    • 0029909407 scopus 로고    scopus 로고
    • Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein
    • Yang, T.-T L. Cheng, and S. R. Kain. 1996. Optimized codon usage and chromophore mutations provide enhanced sensitivity with the green fluorescent protein. Nucleic Acids Res. 24:4592-4593.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4592-4593
    • Yang, T.-T.1    Cheng, L.2    Kain, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.