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Volumn 328, Issue 5, 2003, Pages 1071-1081

Expansion of the genetic code enables design of a novel "gold" class of green fluorescent proteins

Author keywords

Amino acid incorporation; Chromophore; Genetic code; Green fluorescent protein; Tryptophan

Indexed keywords

GREEN FLUORESCENT PROTEIN; MUTANT PROTEIN; TRYPTOPHAN;

EID: 0037449124     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00364-4     Document Type: Article
Times cited : (188)

References (30)
  • 1
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene-expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., Prasher D.C. Green fluorescent protein as a marker for gene-expression. Science. 263:1994;802-895.
    • (1994) Science , vol.263 , pp. 802-895
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 2
    • 0008566674 scopus 로고    scopus 로고
    • Structure and dynamics of green fluorescent protein
    • Phillips G.N. Structure and dynamics of green fluorescent protein. Curr. Opin. Struct. Biol. 7:1997;821-827.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 821-827
    • Phillips, G.N.1
  • 3
    • 0032621293 scopus 로고    scopus 로고
    • Biophysics of the green fluorescent protein
    • Prendergast F. Biophysics of the green fluorescent protein. Methods Cell Biol. 58:1999;1-18.
    • (1999) Methods Cell Biol. , vol.58 , pp. 1-18
    • Prendergast, F.1
  • 4
    • 0031663369 scopus 로고    scopus 로고
    • Green fluorescent protein
    • Tsien R. Green fluorescent protein. Annu. Rev. Biochem. 67:1999;509-544.
    • (1999) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.1
  • 6
    • 0032928678 scopus 로고    scopus 로고
    • Toward the experimental codon reassignment in vivo: Protein building with an expanded amino acid repertoire
    • Budisa N., Minks C., Alefelder S., Wenger W., Dong F., Moroder L., Huber R. Toward the experimental codon reassignment in vivo: protein building with an expanded amino acid repertoire. FASEB J. 13:1999;41-51.
    • (1999) FASEB J. , vol.13 , pp. 41-51
    • Budisa, N.1    Minks, C.2    Alefelder, S.3    Wenger, W.4    Dong, F.5    Moroder, L.6    Huber, R.7
  • 7
    • 0037021021 scopus 로고    scopus 로고
    • Global replacement of tryptophan with amino-tryptophans generates non-invasive protein-based optical pH sensors
    • Budisa N., Rubini M., Bae J.H., Weyher E., Wenger W., Golbik R., et al. Global replacement of tryptophan with amino-tryptophans generates non-invasive protein-based optical pH sensors. Angew. Chem. Int. Ed. 41:2002;4066-4069.
    • (2002) Angew. Chem. Int. Ed. , vol.41 , pp. 4066-4069
    • Budisa, N.1    Rubini, M.2    Bae, J.H.3    Weyher, E.4    Wenger, W.5    Golbik, R.6
  • 8
    • 0034711436 scopus 로고    scopus 로고
    • Towards new protein engineering: In vivo building and folding of protein shuttles for drug delivery and targeting by the selective pressure incorporation (SPI) method
    • Minks C., Alefelder S., Moroder L., Huber R., Budisa N. Towards new protein engineering: in vivo building and folding of protein shuttles for drug delivery and targeting by the selective pressure incorporation (SPI) method. Tetrahedron. 56:2000;9431-9442.
    • (2000) Tetrahedron , vol.56 , pp. 9431-9442
    • Minks, C.1    Alefelder, S.2    Moroder, L.3    Huber, R.4    Budisa, N.5
  • 9
    • 0034711377 scopus 로고    scopus 로고
    • Protein engineering by in vivo incorporation of non-natural amino acids: Control of incorporation of methionine analogues by methionyl-tRNA synthetase
    • Kiick K.L., Tirrell D.A. Protein engineering by in vivo incorporation of non-natural amino acids: control of incorporation of methionine analogues by methionyl-tRNA synthetase. Tetrahedron. 56:2000;9487-9493.
    • (2000) Tetrahedron , vol.56 , pp. 9487-9493
    • Kiick, K.L.1    Tirrell, D.A.2
  • 10
    • 0034711395 scopus 로고    scopus 로고
    • Development of strategies for the site-specific in vivo incorporation of photoreactive amino acids: P-azidophenylalanine, p-acetylphenylalanine and benzofuranyl-alanine
    • Behrens C., Nielsen J.N., Fan X.-J., Doisy X., Kim K.-J., Praetorius-Ibba M., et al. Development of strategies for the site-specific in vivo incorporation of photoreactive amino acids: p-azidophenylalanine, p-acetylphenylalanine and benzofuranyl-alanine. Tetrahedron. 56:2000;9443-9449.
    • (2000) Tetrahedron , vol.56 , pp. 9443-9449
    • Behrens, C.1    Nielsen, J.N.2    Fan, X.-J.3    Doisy, X.4    Kim, K.-J.5    Praetorius-Ibba, M.6
  • 13
    • 0032905565 scopus 로고    scopus 로고
    • Spectral variants of green fluorescent protein
    • Palm G.J., Wlodawer A. Spectral variants of green fluorescent protein. Method Enzymol. 33:1999;378-394.
    • (1999) Method Enzymol. , vol.33 , pp. 378-394
    • Palm, G.J.1    Wlodawer, A.2
  • 14
    • 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. 93:1996;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
  • 15
    • 0030589442 scopus 로고    scopus 로고
    • Time-resolved spectroscopy of wild-type and mutant green fluorescent proteins reveals excited state deprotonation consistent with fluorophore-protein interactions
    • Lossau H., Kummer A., Heinecke R., Pollinger-Dammer F., Kompa C., Bieser G., et al. Time-resolved spectroscopy of wild-type and mutant green fluorescent proteins reveals excited state deprotonation consistent with fluorophore-protein interactions. Chem. Phys. 213:1996;1-16.
    • (1996) Chem. Phys. , vol.213 , pp. 1-16
    • Lossau, H.1    Kummer, A.2    Heinecke, R.3    Pollinger-Dammer, F.4    Kompa, C.5    Bieser, G.6
  • 16
    • 33845279805 scopus 로고
    • Ground-state and excited-state protonation of aminoquinoxalines
    • Waluk J., Rettig W., Spangetlarsen J. Ground-state and excited-state protonation of aminoquinoxalines. J. Phys. Chem. 92:1988;6930-6935.
    • (1988) J. Phys. Chem. , vol.92 , pp. 6930-6935
    • Waluk, J.1    Rettig, W.2    Spangetlarsen, J.3
  • 17
    • 0000559252 scopus 로고
    • Excited-state and ground-state proton-transfer reactions in 5-aminoindole
    • Sinha H.K., Dogra S.K., Krishnamurthy M. Excited-state and ground-state proton-transfer reactions in 5-aminoindole. Bull. Chem. Soc. Jpn. 60:1987;4401-4407.
    • (1987) Bull. Chem. Soc. Jpn , vol.60 , pp. 4401-4407
    • Sinha, H.K.1    Dogra, S.K.2    Krishnamurthy, M.3
  • 18
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F., Moss L.G., Phillips G.N. The molecular structure of green fluorescent protein. Nature Biotechnol. 14:1996;1246-1251.
    • (1996) Nature Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips, G.N.3
  • 20
    • 0028881975 scopus 로고
    • SURFNET - A program for visualizing molecular-surfaces, cavities, and intermolecular interactions
    • Laskowski R.A. SURFNET - a program for visualizing molecular-surfaces, cavities, and intermolecular interactions. J. Mol. Graph. 13:1995;323-330.
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 21
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck P. Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 75:1998;1503-1512.
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 22
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias D.A., Violin J.D., Newton A.C., Tsien R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 296:2002;913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 23
    • 0033578445 scopus 로고    scopus 로고
    • Atomic mutations at the single tryptophan residue of human recombinant annexin V: Effects on structure, stability and activity
    • Minks C., Huber R., Moroder L., Budisa N. Atomic mutations at the single tryptophan residue of human recombinant annexin V: effects on structure, stability and activity. Biochemistry. 38:1999;10649-10659.
    • (1999) Biochemistry , vol.38 , pp. 10649-10659
    • Minks, C.1    Huber, R.2    Moroder, L.3    Budisa, N.4
  • 24
    • 0034973192 scopus 로고    scopus 로고
    • Proteins with beta-(thienopyrrolyl)alanines as alternative chromophores and pharmaceutically active amino acids
    • Budisa N., Alefelder S., Bae J.H., Golbik R., Minks C., Huber R., Moroder L. Proteins with beta-(thienopyrrolyl)alanines as alternative chromophores and pharmaceutically active amino acids. Protein Sci. 10:2001;1281-1292.
    • (2001) Protein Sci. , vol.10 , pp. 1281-1292
    • Budisa, N.1    Alefelder, S.2    Bae, J.H.3    Golbik, R.4    Minks, C.5    Huber, R.6    Moroder, L.7
  • 25
    • 0012392952 scopus 로고    scopus 로고
    • Semiconductor nanocrystals as fluorescent biological labels
    • Bruchez M., Moronne M., Gin P., Weiss S., Alivisatos A.P. Semiconductor nanocrystals as fluorescent biological labels. Science. 281:1998;2013-2016.
    • (1998) Science , vol.281 , pp. 2013-2016
    • Bruchez, M.1    Moronne, M.2    Gin, P.3    Weiss, S.4    Alivisatos, A.P.5
  • 26
    • 0032566763 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for ultrasensitive nonisotopic detection
    • Chan W.C.W., Nie S. Quantum dot bioconjugates for ultrasensitive nonisotopic detection. Science. 281:1998;2016-2018.
    • (1998) Science , vol.281 , pp. 2016-2018
    • Chan, W.C.W.1    Nie, S.2
  • 27
    • 0031929949 scopus 로고    scopus 로고
    • Residue-specific bioincorporation of non-natural biologically active amino acids into proteins as possible drug carriers. Structure and stability of per-thiaproline mutant of annexin V
    • Budisa N., Minks C., Medrano F.J., Lutz J., Huber R., Moroder L. Residue-specific bioincorporation of non-natural biologically active amino acids into proteins as possible drug carriers. Structure and stability of per-thiaproline mutant of annexin V. Proc. Natl Acad. Sci. USA. 95:1998;455-459.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 455-459
    • Budisa, N.1    Minks, C.2    Medrano, F.J.3    Lutz, J.4    Huber, R.5    Moroder, L.6
  • 28
    • 0242554102 scopus 로고    scopus 로고
    • Expression of "tailor-made" proteins via incorporation of synthetic amino acids by using cell-free protein synthesis
    • J.R. Swartz. Berlin: Springer. In press
    • Budisa N. Expression of "tailor-made" proteins via incorporation of synthetic amino acids by using cell-free protein synthesis. Swartz J.R. Cell Free Protein Expression. 2003;Springer, Berlin. In press.
    • (2003) Cell Free Protein Expression
    • Budisa, N.1
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 30
    • 0028922586 scopus 로고
    • LIGPLOT-a program to generate schematic diagrams of protein ligand interactions
    • Wallace A.C., Laskowski R.A., Thornton J.M. LIGPLOT-a program to generate schematic diagrams of protein ligand interactions. Protein Eng. 8:1995;127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.