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Volumn 17, Issue 10, 1999, Pages 969-973

Fluorescent proteins from nonbioluminescent Anthozoa species

Author keywords

Anthozoa; Fluorophore; Green fluorescent protein

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 0032867477     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/13657     Document Type: Article
Times cited : (1602)

References (32)
  • 1
    • 0032404444 scopus 로고    scopus 로고
    • Aequorea victoria bioluminescence moves into an exciting new era
    • Kendall, J.M. & Badminton, M.N. Aequorea victoria bioluminescence moves into an exciting new era. Trends Biotechnol. 16, 216-224 (1998).
    • (1998) Trends Biotechnol. , vol.16 , pp. 216-224
    • Kendall, J.M.1    Badminton, M.N.2
  • 2
    • 0002376324 scopus 로고
    • Quantum efficiency of Cypridina luminescense, with a note on that of Aequorea
    • Johnson, F.H. et al. Quantum efficiency of Cypridina luminescense, with a note on that of Aequorea. J. Cell. Comp. Physiol. 60, 85-104 (1962).
    • (1962) J. Cell. Comp. Physiol. , vol.60 , pp. 85-104
    • Johnson, F.H.1
  • 4
    • 0002757536 scopus 로고
    • Energy transfer processes in bioluminescence
    • Ward, W.W. Energy transfer processes in bioluminescence. Photochem. Photobiol. Rev. 4, 1-57 (1979).
    • (1979) Photochem. Photobiol. Rev. , vol.4 , pp. 1-57
    • Ward, W.W.1
  • 6
    • 0029134629 scopus 로고
    • Using GFP to see the light
    • Prasher, D.C. Using GFP to see the light. Trends Genet. 11, 320-323 (1995).
    • (1995) Trends Genet. , vol.11 , pp. 320-323
    • Prasher, D.C.1
  • 7
    • 0344242958 scopus 로고
    • On the mechanism of the calcium activated bioluminescence of Ctenophora
    • Labas Y.A. On the mechanism of the calcium activated bioluminescence of Ctenophora. Biophysics of Living Cell 4, 83-110 (1973).
    • (1973) Biophysics of Living Cell , vol.4 , pp. 83-110
    • Labas, Y.A.1
  • 8
    • 0018786147 scopus 로고
    • An energy transfer protein in coelenterate bioluminescence: Characterization of the Renilla green-fluorescent protein
    • Ward, W.W. & Cormier, M.J. An energy transfer protein in coelenterate bioluminescence: characterization of the Renilla green-fluorescent protein. J. Biol. Chem. 254, 781-788 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 781-788
    • Ward, W.W.1    Cormier, M.J.2
  • 10
    • 0032052229 scopus 로고    scopus 로고
    • The origins of marine bioluminescence - Turning oxygen defense-mechanisms into deep-sea communication tools
    • Rees, J.F. et al. The origins of marine bioluminescence - turning oxygen defense-mechanisms into deep-sea communication tools. J. Exp. Biol. 201, 1211-1221 (1998).
    • (1998) J. Exp. Biol. , vol.201 , pp. 1211-1221
    • Rees, J.F.1
  • 11
    • 0028976542 scopus 로고
    • Spectral measurements of fluorescence emission in caribbean cnidarians
    • Mazel, C.H. Spectral measurements of fluorescence emission in caribbean cnidarians. Mar. Ecol. Prog. Ser. 120, 185-191 (1995).
    • (1995) Mar. Ecol. Prog. Ser. , vol.120 , pp. 185-191
    • Mazel, C.H.1
  • 12
    • 0000432706 scopus 로고
    • Fluorescence effect from corals irradiated with ultra-violet rays
    • Catala, R. Fluorescence effect from corals irradiated with ultra-violet rays. Nature 183, 949 (1959).
    • (1959) Nature , vol.183 , pp. 949
    • Catala, R.1
  • 13
    • 0000965065 scopus 로고
    • On the physiology of reef corals. VI. Study of the pigments
    • Kawaguti, S. On the physiology of reef corals. VI. Study of the pigments. Palao trop. Biol. Stn. Stud. 2, 617-674 (1944).
    • (1944) Palao Trop. Biol. Stn. Stud. , vol.2 , pp. 617-674
    • Kawaguti, S.1
  • 14
    • 0027952491 scopus 로고
    • Improvement of photosynthesis in zooxanthellate corals by autofluorescent chromatophores
    • Schlichter, D., Meier, U. & Fricke, H.W. Improvement of photosynthesis in zooxanthellate corals by autofluorescent chromatophores. Oecologia 99, 124-131 (1994).
    • (1994) Oecologia , vol.99 , pp. 124-131
    • Schlichter, D.1    Meier, U.2    Fricke, H.W.3
  • 16
    • 0033559113 scopus 로고    scopus 로고
    • Amplification of cDNA ends based on template-switching effect and step-out PCR
    • Matz, M. et al. Amplification of cDNA ends based on template-switching effect and step-out PCR. Nucleic Acids Res. 27, 1558-1560 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1558-1560
    • Matz, M.1
  • 17
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormö, M. et al. Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395 (1996).
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormö, M.1
  • 18
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L.G. & Phillips, G.N., Jr. The molecular structure of green fluorescent protein. Nat. Biotechnol. 14, 1246-1251 (1996).
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips G.N., Jr.3
  • 19
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S. & von Heijne, G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6 (1997).
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 20
    • 0027465627 scopus 로고
    • Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein
    • Cody, C.W., Prasher, D.C., Westler, W.M., Prendergast, F.G. & Ward, W.W. Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. Biochemistry 32, 1212-1218 (1993).
    • (1993) Biochemistry , vol.32 , pp. 1212-1218
    • Cody, C.W.1    Prasher, D.C.2    Westler, W.M.3    Prendergast, F.G.4    Ward, W.W.5
  • 21
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim, R., Cubitt, A.B. & Tsien, R.Y. Improved green fluorescence. Nature 373, 663-664 (1995).
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 23
    • 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. Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transfer. Proc. Natl. Acad. Sci. USA 93, 8362-8367 (1996).
    • (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
  • 24
    • 0030953638 scopus 로고    scopus 로고
    • Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein
    • Brejc, K. et al. Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein. Proc. Natl. Acad. Sci. USA 94, 2306-2311 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2306-2311
    • Brejc, K.1
  • 25
    • 0029061274 scopus 로고
    • Green-fluorescent protein mutants with altered fluorescence excitation spectra
    • Ehrig, T., O'Kane, D.J. & Prendergast, F.G. Green-fluorescent protein mutants with altered fluorescence excitation spectra. FEBS Lett. 367, 163-166 (1995).
    • (1995) FEBS Lett. , vol.367 , pp. 163-166
    • Ehrig, T.1    O'Kane, D.J.2    Prendergast, F.G.3
  • 26
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 27
    • 0024460181 scopus 로고
    • Improved retroviral vectors for gene transfer and expression
    • Miller, A.D. & Rosman, G.J. Improved retroviral vectors for gene transfer and expression Biotechniques 7, 980-990 (1989).
    • (1989) Biotechniques , vol.7 , pp. 980-990
    • Miller, A.D.1    Rosman, G.J.2
  • 28
    • 0028846720 scopus 로고
    • The homeobox-containing gene XANF-1 may control development of the Spemann organizer
    • Zaraisky, A.G. et al. The homeobox-containing gene XANF-1 may control development of the Spemann organizer. Development 121, 3839-3847 (1995).
    • (1995) Development , vol.121 , pp. 3839-3847
    • Zaraisky, A.G.1
  • 29
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159 (1987).
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 30
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. & Hippel, P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326 (1989).
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Hippel, P.H.2
  • 31
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • Wetlaufer, D.B. Ultraviolet spectra of proteins and amino acids. Adv. Protein Chem. 17, 303-390 (1962).
    • (1962) Adv. Protein Chem. , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 32
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins
    • Mach, H., Middaugh, C.R. & Lewis, R.V. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal. Biochem. 200, 74-80 (1992).
    • (1992) Anal. Biochem. , vol.200 , pp. 74-80
    • Mach, H.1    Middaugh, C.R.2    Lewis, R.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.