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Volumn 14, Issue 6, 2003, Pages 603-609

Non-canonical amino acids in protein engineering

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; SYNTHETASE; TRANSFER RNA;

EID: 0345549549     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2003.10.011     Document Type: Review
Times cited : (333)

References (56)
  • 1
    • 0001280314 scopus 로고
    • Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulphur
    • Cowie D.B., Cohen G.N. Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulphur. Biochim. Biophys. Acta. 26:1957;252-261.
    • (1957) Biochim. Biophys. Acta , vol.26 , pp. 252-261
    • Cowie, D.B.1    Cohen, G.N.2
  • 2
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson W.A., Horton J.R., LeMaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9:1990;1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 3
    • 0033637431 scopus 로고    scopus 로고
    • Unnatural amino acids as probes of protein structure and function
    • Dougherty D.A. Unnatural amino acids as probes of protein structure and function. Curr. Opin. Chem. Biol. 4:2000;645-652.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 645-652
    • Dougherty, D.A.1
  • 4
    • 0036900746 scopus 로고    scopus 로고
    • Incorporation of non-natural amino acids into proteins
    • Hohsaka T., Sisido M. Incorporation of non-natural amino acids into proteins. Curr. Opin. Chem. Biol. 6:2002;809-815.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 809-815
    • Hohsaka, T.1    Sisido, M.2
  • 5
    • 0034674281 scopus 로고    scopus 로고
    • Expanding the scope of protein biosynthesis by altering the methionyl-tRNA synthetase activity of a bacterial expression host
    • Kiick K.L., van Hest J.C.M., Tirrell D.A. Expanding the scope of protein biosynthesis by altering the methionyl-tRNA synthetase activity of a bacterial expression host. Angew Chem. Int. Ed. Engl. 39:2000;2148-2152.
    • (2000) Angew Chem. Int. Ed. Engl. , vol.39 , pp. 2148-2152
    • Kiick, K.L.1    Van Hest, J.C.M.2    Tirrell, D.A.3
  • 6
    • 0028244324 scopus 로고
    • Substrate-specificity is determined by amino-acid binding pocket size in Escherichia coli phenylalanyl-transfer-RNA synthetase
    • Ibba M., Kast P., Hennecke H. Substrate-specificity is determined by amino-acid binding pocket size in Escherichia coli phenylalanyl-transfer-RNA synthetase. Biochemistry. 33:1994;7107-7112.
    • (1994) Biochemistry , vol.33 , pp. 7107-7112
    • Ibba, M.1    Kast, P.2    Hennecke, H.3
  • 7
    • 0029020345 scopus 로고
    • Relaxing the substrate-specificity of an aminoacyl-transfer-RNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino-acids
    • Ibba M., Hennecke H. Relaxing the substrate-specificity of an aminoacyl-transfer-RNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino-acids. FEBS Lett. 364:1995;272-275.
    • (1995) FEBS Lett. , vol.364 , pp. 272-275
    • Ibba, M.1    Hennecke, H.2
  • 8
    • 0033960066 scopus 로고    scopus 로고
    • Efficient introduction of aryl bromide functionality into proteins in vivo
    • Sharma N., Furter R., Kast P., Tirrell D.A. Efficient introduction of aryl bromide functionality into proteins in vivo. FEBS Lett. 467:2000;37-40.
    • (2000) FEBS Lett. , vol.467 , pp. 37-40
    • Sharma, N.1    Furter, R.2    Kast, P.3    Tirrell, D.A.4
  • 9
    • 0036523420 scopus 로고    scopus 로고
    • Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues
    • Kirshenbaum K., Carrico I.S., Tirrell D.A. Biosynthesis of proteins incorporating a versatile set of phenylalanine analogues. Chembiochem. 3:2002;235-237.
    • (2002) Chembiochem , vol.3 , pp. 235-237
    • Kirshenbaum, K.1    Carrico, I.S.2    Tirrell, D.A.3
  • 11
    • 0037183472 scopus 로고    scopus 로고
    • Attenuation of the editing activity of the Escherichia coli leucyl-tRNA synthetase allows incorporation of novel amino acids into proteins in vivo
    • Tang Y., Tirrell D.A. Attenuation of the editing activity of the Escherichia coli leucyl-tRNA synthetase allows incorporation of novel amino acids into proteins in vivo. Biochemistry. 41:2002;10635-10645.
    • (2002) Biochemistry , vol.41 , pp. 10635-10645
    • Tang, Y.1    Tirrell, D.A.2
  • 13
    • 0035823858 scopus 로고    scopus 로고
    • Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host
    • Tang Y., Tirrell D.A. Biosynthesis of a highly stable coiled-coil protein containing hexafluoroleucine in an engineered bacterial host. J. Am. Chem. Soc. 123:2001;11089-11090.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11089-11090
    • Tang, Y.1    Tirrell, D.A.2
  • 15
    • 0038276996 scopus 로고    scopus 로고
    • Incorporation of trifluoroisoleucine into proteins in vivo
    • Wang P., Tang Y., Tirrell D.A. Incorporation of trifluoroisoleucine into proteins in vivo. J. Am. Chem. Soc. 125:2003;6900-6906.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6900-6906
    • Wang, P.1    Tang, Y.2    Tirrell, D.A.3
  • 16
    • 0035965730 scopus 로고    scopus 로고
    • Programmed self-sorting of coiled coils with leucine and hexafluoroleucine cores
    • Bilgicer B., Xing X., Kumar K. Programmed self-sorting of coiled coils with leucine and hexafluoroleucine cores. J. Am. Chem. Soc. 123:2001;11815- 11816.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11815-11816
    • Bilgicer, B.1    Xing, X.2    Kumar, K.3
  • 17
    • 0037071153 scopus 로고    scopus 로고
    • Synthesis and thermodynamic characterization of self-sorting coiled coils
    • The authors show that the extra stability of fluorinated coiled coils will drive the equilibrium of a mixture of fluorinated and wild-type peptides toward 'self-sorted' homodimers, demonstrating that nonnatural analog incorporation can be used to mediate protein-protein interactions.
    • Bilgicer B., Kumar K. Synthesis and thermodynamic characterization of self-sorting coiled coils. Tetrahedron. 58:2002;4105-4112 The authors show that the extra stability of fluorinated coiled coils will drive the equilibrium of a mixture of fluorinated and wild-type peptides toward 'self-sorted' homodimers, demonstrating that nonnatural analog incorporation can be used to mediate protein-protein interactions.
    • (2002) Tetrahedron , vol.58 , pp. 4105-4112
    • Bilgicer, B.1    Kumar, K.2
  • 19
    • 0037449124 scopus 로고    scopus 로고
    • Expansion of the genetic code enables design of a novel 'gold' class of green fluorescent proteins
    • A striking example of the use of nonnatural amino acids to substantially affect the properties of proteins. The authors incorporate 4-aminotryptophan into the two tryptophan positions of enhanced cyan fluorescent protein (ECFP) to produce gold fluorescent protein (GdFP). GdFP, when compared with the parent ECFP, is red-shifted 69 nm, is more thermostable, and is less apt to aggregate.
    • Bae J.H., Rubini M., Jung G., Wiegand G., Seifert M.H.J., Azim M.K., Kim J.S., Zumbusch A., Holak T.A., Moroder L.et al. Expansion of the genetic code enables design of a novel 'gold' class of green fluorescent proteins. J. Mol. Biol. 328:2003;1071-1081 A striking example of the use of nonnatural amino acids to substantially affect the properties of proteins. The authors incorporate 4-aminotryptophan into the two tryptophan positions of enhanced cyan fluorescent protein (ECFP) to produce gold fluorescent protein (GdFP). GdFP, when compared with the parent ECFP, is red-shifted 69 nm, is more thermostable, and is less apt to aggregate.
    • (2003) J. Mol. Biol. , vol.328 , pp. 1071-1081
    • Bae, J.H.1    Rubini, M.2    Jung, G.3    Wiegand, G.4    Seifert, M.H.J.5    Azim, M.K.6    Kim, J.S.7    Zumbusch, A.8    Holak, T.A.9    Moroder, L.10
  • 22
    • 0035876180 scopus 로고    scopus 로고
    • Incorporation of β-selenolo 3,2-β pyrrolyl-alanine into proteins for phase determination in protein X-ray crystallography
    • Bae J.H., Alefelder S., Kaiser J.T., Friedrich R., Moroder L., Huber R., Budisa N. Incorporation of β-selenolo 3,2-β pyrrolyl-alanine into proteins for phase determination in protein X-ray crystallography. J. Mol. Biol. 309:2001;925-936.
    • (2001) J. Mol. Biol. , vol.309 , pp. 925-936
    • Bae, J.H.1    Alefelder, S.2    Kaiser, J.T.3    Friedrich, R.4    Moroder, L.5    Huber, R.6    Budisa, N.7
  • 23
    • 0037039298 scopus 로고    scopus 로고
    • Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
    • Kiick K.L., Saxon E., Tirrell D.A., Bertozzi C.R. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc. Natl. Acad. Sci. USA. 99:2002;19-24.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 19-24
    • Kiick, K.L.1    Saxon, E.2    Tirrell, D.A.3    Bertozzi, C.R.4
  • 24
    • 0041692305 scopus 로고    scopus 로고
    • Cell surface labeling of Escherichia coli via copper(I)-catalyzed [3+2] cycloaddition
    • A method of selecting for incorporation of non-canonical amino acids at the single-cell level. The authors incorporate the analog azidohomoalanine into E. coli outer membrane protein C and then chemoselectively react the analog with a biotinylated alkyne. After staining with a fluorescent avidin, cells incorporating the analog were readily distinguished from wild-type cells by flow cytometry.
    • Link A.J., Tirrell D.A. Cell surface labeling of Escherichia coli via copper(I)-catalyzed [3+2] cycloaddition. J. Am. Chem. Soc. 125:2003;11164-11165 A method of selecting for incorporation of non-canonical amino acids at the single-cell level. The authors incorporate the analog azidohomoalanine into E. coli outer membrane protein C and then chemoselectively react the analog with a biotinylated alkyne. After staining with a fluorescent avidin, cells incorporating the analog were readily distinguished from wild-type cells by flow cytometry.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11164-11165
    • Link, A.J.1    Tirrell, D.A.2
  • 25
    • 0024968835 scopus 로고
    • A general-method for site-specific incorporation of unnatural amino-acids into proteins
    • Noren C.J., Anthony-Cahill S.J., Griffith M.C., Schultz P.G. A general-method for site-specific incorporation of unnatural amino-acids into proteins. Science. 244:1989;182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 26
    • 0000652848 scopus 로고
    • Biosynthetic site-specific incorporation of a non-natural amino-acid into a polypeptide
    • Bain J.D., Glabe C.G., Dix T.A., Chamberlin A.R., Diala E.S. Biosynthetic site-specific incorporation of a non-natural amino-acid into a polypeptide. J. Am. Chem. Soc. 111:1989;8013-8014.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8013-8014
    • Bain, J.D.1    Glabe, C.G.2    Dix, T.A.3    Chamberlin, A.R.4    Diala, E.S.5
  • 29
    • 0033534674 scopus 로고    scopus 로고
    • Backbone mutations in transmembrane domains of a ligand-gated ion channel: Implications for the mechanism of gating
    • England P.M., Zhang Y.N., Dougherty D.A., Lester H.A. Backbone mutations in transmembrane domains of a ligand-gated ion channel: implications for the mechanism of gating. Cell. 96:1999;89-98.
    • (1999) Cell , vol.96 , pp. 89-98
    • England, P.M.1    Zhang, Y.N.2    Dougherty, D.A.3    Lester, H.A.4
  • 30
    • 0038506126 scopus 로고    scopus 로고
    • Site-specific incorporation of unnatural amino acids into receptors expressed in mammalian cells
    • A general method for the introduction of non-canonical amino acids into proteins in mammalian cells.
    • Monahan S.L., Lester H.A., Dougherty D.A. Site-specific incorporation of unnatural amino acids into receptors expressed in mammalian cells. Chem. Biol. 10:2003;573-580 A general method for the introduction of non-canonical amino acids into proteins in mammalian cells.
    • (2003) Chem. Biol. , vol.10 , pp. 573-580
    • Monahan, S.L.1    Lester, H.A.2    Dougherty, D.A.3
  • 31
    • 0037189891 scopus 로고    scopus 로고
    • In vitro selection of mRNA display libraries containing an unnatural amino acid
    • Li S.W., Millward S., Roberts R. In vitro selection of mRNA display libraries containing an unnatural amino acid. J. Am. Chem. Soc. 124:2002;9972-9973.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9972-9973
    • Li, S.W.1    Millward, S.2    Roberts, R.3
  • 32
    • 0037065314 scopus 로고    scopus 로고
    • Position-specific incorporation of a fluorophore-quencher pair into a single streptavidin through orthogonal four-base codon/anticodon pairs
    • Taki M., Hohsaka T., Murakami H., Taira K., Sisido M. Position-specific incorporation of a fluorophore-quencher pair into a single streptavidin through orthogonal four-base codon/anticodon pairs. J. Am. Chem. Soc. 124:2002;14586-14590.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14586-14590
    • Taki, M.1    Hohsaka, T.2    Murakami, H.3    Taira, K.4    Sisido, M.5
  • 33
    • 0037151668 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between unnatural amino acids in a structurally modified dihydrofolate reductase
    • Anderson R.D., Zhou J., Hecht S.M. Fluorescence resonance energy transfer between unnatural amino acids in a structurally modified dihydrofolate reductase. J. Am. Chem. Soc. 124:2002;9674-9675.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9674-9675
    • Anderson, R.D.1    Zhou, J.2    Hecht, S.M.3
  • 34
    • 0037176865 scopus 로고    scopus 로고
    • Chemically mediated site-specific proteolysis. Alteration of protein-protein interaction
    • Wang B.X., Brown K.C., Lodder M., Craik C.S., Hecht S.M. Chemically mediated site-specific proteolysis. Alteration of protein-protein interaction. Biochemistry. 41:2002;2805-2813.
    • (2002) Biochemistry , vol.41 , pp. 2805-2813
    • Wang, B.X.1    Brown, K.C.2    Lodder, M.3    Craik, C.S.4    Hecht, S.M.5
  • 35
    • 0037167581 scopus 로고    scopus 로고
    • Site-specific incorporation of (aminooxy)acetic acid into proteins
    • Eisenhauer B.M., Hecht S.M. Site-specific incorporation of (aminooxy)acetic acid into proteins. Biochemistry. 41:2002;11472-11478.
    • (2002) Biochemistry , vol.41 , pp. 11472-11478
    • Eisenhauer, B.M.1    Hecht, S.M.2
  • 36
    • 0031937870 scopus 로고    scopus 로고
    • Expansion of the genetic code: Site-directed p-fluorophenylalanine incorporation in Escherichia coli
    • Furter R. Expansion of the genetic code: Site-directed p-fluorophenylalanine incorporation in Escherichia coli. Protein Sci. 7:1998;419-426.
    • (1998) Protein Sci. , vol.7 , pp. 419-426
    • Furter, R.1
  • 37
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • A robust method for the evolution of aminoacyl-tRNA synthetase specificity.
    • Wang L., Brock A., Herberich B., Schultz P.G. Expanding the genetic code of Escherichia coli. Science. 292:2001;498-500 A robust method for the evolution of aminoacyl-tRNA synthetase specificity.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 38
    • 0037422608 scopus 로고    scopus 로고
    • Addition of the keto functional group to the genetic code of Escherichia coli
    • Wang L., Zhang Z.W., Brock A., Schultz P.G. Addition of the keto functional group to the genetic code of Escherichia coli. Proc. Natl. Acad. Sci. USA. 100:2003;56-61.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 56-61
    • Wang, L.1    Zhang, Z.W.2    Brock, A.3    Schultz, P.G.4
  • 39
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli
    • Chin J.W., Martin A.B., King D.S., Wang L., Schultz P.G. Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli. Proc. Natl. Acad. Sci. USA. 99:2002;11020-11024.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 42
    • 0037021352 scopus 로고    scopus 로고
    • In vivo photocrosslinking with unnatural amino acid mutagenesis
    • Chin J.W., Schultz P.G. In vivo photocrosslinking with unnatural amino acid mutagenesis. Chembiochem. 3:2002;1135-1137.
    • (2002) Chembiochem. , vol.3 , pp. 1135-1137
    • Chin, J.W.1    Schultz, P.G.2
  • 44
    • 0037428005 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis of green fluorescent protein
    • Wang L., Xie J.M., Deniz A.A., Schultz P.G. Unnatural amino acid mutagenesis of green fluorescent protein. J. Org. Chem. 68:2003;174-176.
    • (2003) J. Org. Chem. , vol.68 , pp. 174-176
    • Wang, L.1    Xie, J.M.2    Deniz, A.A.3    Schultz, P.G.4
  • 45
    • 0041520960 scopus 로고    scopus 로고
    • An expanded eukaryotic genetic code
    • A new selection scheme for the evolution of aminoacyl-tRNA synthetases in yeast.
    • Chin J.W., Cropp T.A., Anderson J.C., Mukherji M., Zhang Z.W., Schultz P.G. An expanded eukaryotic genetic code. Science. 301:2003;964-967 A new selection scheme for the evolution of aminoacyl-tRNA synthetases in yeast.
    • (2003) Science , vol.301 , pp. 964-967
    • Chin, J.W.1    Cropp, T.A.2    Anderson, J.C.3    Mukherji, M.4    Zhang, Z.W.5    Schultz, P.G.6
  • 47
    • 0036787635 scopus 로고    scopus 로고
    • An efficient system for the evolution of aminoacyl-tRNA synthetase specificity
    • Santoro S.W., Wang L., Herbrich B., King D.S., Schultz P.G. An efficient system for the evolution of aminoacyl-tRNA synthetase specificity. Nat. Biotechnol. 20:2002;1044-1048.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1044-1048
    • Santoro, S.W.1    Wang, L.2    Herbrich, B.3    King, D.S.4    Schultz, P.G.5
  • 48
    • 0037157082 scopus 로고    scopus 로고
    • A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins
    • Datta D., Wang P., Carrico I.S., Mayo S.L., Tirrell D.A. A designed phenylalanyl-tRNA synthetase variant allows efficient in vivo incorporation of aryl ketone functionality into proteins. J. Am. Chem. Soc. 124:2002;5652-5653.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5652-5653
    • Datta, D.1    Wang, P.2    Carrico, I.S.3    Mayo, S.L.4    Tirrell, D.A.5
  • 49
    • 0037076411 scopus 로고    scopus 로고
    • Structure-based design of mutant Methanococcus jannaschii tyrosyl-tRNA synthetase for incorporation of O-methyl-L-tyrosine
    • Zhang D., Vaidehi N., Goddard W.A. III, Danzer J.F., Debe D. Structure-based design of mutant Methanococcus jannaschii tyrosyl-tRNA synthetase for incorporation of O-methyl-L-tyrosine. Proc. Natl. Acad. Sci. USA. 99:2002;6579-6584.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6579-6584
    • Zhang, D.1    Vaidehi, N.2    Goddard III, W.A.3    Danzer, J.F.4    Debe, D.5
  • 50
    • 0038547955 scopus 로고    scopus 로고
    • Enhanced D-amino acid incorporation into protein by modified ribosomes
    • A promising start on engineering ribosomes for the incorporation of novel amino acids.
    • Dedkova L.M., Fahmi N.E., Golovine S.Y., Hecht S.M. Enhanced D-amino acid incorporation into protein by modified ribosomes. J. Am. Chem. Soc. 125:2003;6616-6617 A promising start on engineering ribosomes for the incorporation of novel amino acids.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6616-6617
    • Dedkova, L.M.1    Fahmi, N.E.2    Golovine, S.Y.3    Hecht, S.M.4
  • 51
    • 0035970290 scopus 로고    scopus 로고
    • Expanding the genetic code: Selection of efficient suppressors of four-base codons and identification of 'shifty' four-base codons with a library approach in Escherichia coli
    • Magliery T.J., Anderson J.C., Schultz P.G. Expanding the genetic code: selection of efficient suppressors of four-base codons and identification of 'shifty' four-base codons with a library approach in Escherichia coli. J. Mol. Biol. 307:2001;755-769.
    • (2001) J. Mol. Biol. , vol.307 , pp. 755-769
    • Magliery, T.J.1    Anderson, J.C.2    Schultz, P.G.3
  • 52
    • 0035444292 scopus 로고    scopus 로고
    • Five-base codons for incorporation of nonnatural amino acids into proteins
    • Hohsaka T., Ashizuka Y., Murakami H., Sisido M. Five-base codons for incorporation of nonnatural amino acids into proteins. Nucleic Acids Res. 29:2001;3646-3651.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3646-3651
    • Hohsaka, T.1    Ashizuka, Y.2    Murakami, H.3    Sisido, M.4
  • 53
    • 0036008851 scopus 로고    scopus 로고
    • Exploring the limits of codon and anticodon size
    • Anderson J.C., Magliery T.J., Schultz P.G. Exploring the limits of codon and anticodon size. Chem. Biol. 9:2002;237-244.
    • (2002) Chem. Biol. , vol.9 , pp. 237-244
    • Anderson, J.C.1    Magliery, T.J.2    Schultz, P.G.3
  • 54
    • 0043028469 scopus 로고    scopus 로고
    • Adaptation of an orthogonal archaeal leucyl-tRNA and synthetase pair for four-base, amber, and opal suppression
    • Anderson J.C., Schultz P.G. Adaptation of an orthogonal archaeal leucyl-tRNA and synthetase pair for four-base, amber, and opal suppression. Biochemistry. 42:2003;9598-9608.
    • (2003) Biochemistry , vol.42 , pp. 9598-9608
    • Anderson, J.C.1    Schultz, P.G.2
  • 55
    • 0037870583 scopus 로고    scopus 로고
    • Breaking the degeneracy of the genetic code
    • An illustration of the use of a heterologous synthetase/tRNA pair to break the degeneracy of the phenylalanine codons in E. coli.
    • Kwon I., Kirshenbaum K., Tirrell D.A. Breaking the degeneracy of the genetic code. J. Am. Chem. Soc. 125:2003;7512-7513 An illustration of the use of a heterologous synthetase/tRNA pair to break the degeneracy of the phenylalanine codons in E. coli.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7512-7513
    • Kwon, I.1    Kirshenbaum, K.2    Tirrell, D.A.3
  • 56
    • 0038044525 scopus 로고    scopus 로고
    • In vitro selection for sense codon suppression
    • Frankel A., Roberts R.W. In vitro selection for sense codon suppression. RNA. 9:2003;780-786.
    • (2003) RNA , vol.9 , pp. 780-786
    • Frankel, A.1    Roberts, R.W.2


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