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Volumn 23, Issue 5, 2012, Pages 751-757

Recent advances in genetic code engineering in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL COMPOSITIONS; CURRENT FUNCTION; GENERAL TOOLS; GENETIC CODE; GENETIC CODE ENGINEERING; LIVING CELL; MAXIMUM DEGREE; PROTEIN TRANSLATION; PROTEOMES; SOLID BASIS; SYNTHETASES; SYNTHETIC BIOLOGY;

EID: 84867220294     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2011.12.027     Document Type: Review
Times cited : (85)

References (72)
  • 1
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu C.C., Schultz P.G. Adding new chemistries to the genetic code. Annu Rev Biochem 2010, 79:413-444.
    • (2010) Annu Rev Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 2
    • 78649829465 scopus 로고    scopus 로고
    • Residue-specific incorporation of non-canonical amino acids into proteins: recent developments and applications
    • Johnson J.A., Lu Y.Y., Van Deventer J.A., Tirrell D.A. Residue-specific incorporation of non-canonical amino acids into proteins: recent developments and applications. Curr Opin Chem Biol 2010, 14:774-780.
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 774-780
    • Johnson, J.A.1    Lu, Y.Y.2    Van Deventer, J.A.3    Tirrell, D.A.4
  • 3
    • 81155161937 scopus 로고    scopus 로고
    • Advances in the mechanism and understanding of site-selective noncanonical amino acid incorporation
    • Antonczak A.K., Morris J., Tippmann E.M. Advances in the mechanism and understanding of site-selective noncanonical amino acid incorporation. Curr Opin Struct Biol 2011, 21:481-487.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 481-487
    • Antonczak, A.K.1    Morris, J.2    Tippmann, E.M.3
  • 4
    • 77954965356 scopus 로고    scopus 로고
    • Pyrrolysine analogs for translational incorporation into proteins
    • Fekner T., Li X., Chan M.K. Pyrrolysine analogs for translational incorporation into proteins. Eur J Org Chem 2010, 4171-4179.
    • (2010) Eur J Org Chem , pp. 4171-4179
    • Fekner, T.1    Li, X.2    Chan, M.K.3
  • 5
    • 78650155287 scopus 로고    scopus 로고
    • Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach
    • Liu W.S.R., Wang Y.S., Wan W. Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach. Mol Biosyst 2011, 7:38-47.
    • (2011) Mol Biosyst , vol.7 , pp. 38-47
    • Liu, W.S.R.1    Wang, Y.S.2    Wan, W.3
  • 6
    • 0001280314 scopus 로고
    • Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur
    • Cowie D.B., Cohen G.N. Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur. Biochim Biophys Acta 1957, 26:252-261.
    • (1957) Biochim Biophys Acta , vol.26 , pp. 252-261
    • Cowie, D.B.1    Cohen, G.N.2
  • 7
    • 0028498565 scopus 로고
    • Genetically engineered fluoropolymers. synthesis of repetitive polypeptides containing p-fluorophenylalanine residues
    • Yoshikawa E., Fournier M.J., Mason T.L., Tirrell D.A. Genetically engineered fluoropolymers. synthesis of repetitive polypeptides containing p-fluorophenylalanine residues. Macromolecules 1994, 27:5471-5475.
    • (1994) Macromolecules , vol.27 , pp. 5471-5475
    • Yoshikawa, E.1    Fournier, M.J.2    Mason, T.L.3    Tirrell, D.A.4
  • 8
    • 0029064088 scopus 로고
    • High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli
    • Budisa N., Steipe B., Demange P., Eckerskorn C., Kellermann J., Huber R. High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur J Biochem 1995, 230:788-796.
    • (1995) Eur J Biochem , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3    Eckerskorn, C.4    Kellermann, J.5    Huber, R.6
  • 9
    • 0031937870 scopus 로고    scopus 로고
    • Expansion of the genetic code: site-directed p-fluoro-phenylalanine incorporation in Escherichia coli
    • Furter R. Expansion of the genetic code: site-directed p-fluoro-phenylalanine incorporation in Escherichia coli. Protein Sci 1998, 7:419-426.
    • (1998) Protein Sci , vol.7 , pp. 419-426
    • Furter, R.1
  • 10
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L., Brock A., Herberich B., Schultz P.G. Expanding the genetic code of Escherichia coli. Science 2001, 292:498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 12
    • 45949083738 scopus 로고    scopus 로고
    • Synthetic Biology of proteins: tuning GFPs folding and stability with fluoroproline
    • Article no. e1680
    • Steiner T., Hess P., Bae J.H., Wiltschi B., Moroder L., Budisa N. Synthetic Biology of proteins: tuning GFPs folding and stability with fluoroproline. PLoS ONE 2008, 3. Article no. e1680.
    • (2008) PLoS ONE , vol.3
    • Steiner, T.1    Hess, P.2    Bae, J.H.3    Wiltschi, B.4    Moroder, L.5    Budisa, N.6
  • 13
    • 79956069864 scopus 로고    scopus 로고
    • Rational design of protein stability: effect of (2s,4r)-4-fluoroproline on the stability and folding pathway of ubiquitin
    • Crespo M.D., Rubini M. Rational design of protein stability: effect of (2s,4r)-4-fluoroproline on the stability and folding pathway of ubiquitin. PLoS ONE 2011, 6:e19425.
    • (2011) PLoS ONE , vol.6
    • Crespo, M.D.1    Rubini, M.2
  • 14
    • 66049152925 scopus 로고    scopus 로고
    • Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein
    • Wolschner C., Giese A., Kretzschmar H.A., Huber R., Moroder L., Budisa N. Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein. Proc Natl Acad Sci U S A 2009, 106:7756-7761.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7756-7761
    • Wolschner, C.1    Giese, A.2    Kretzschmar, H.A.3    Huber, R.4    Moroder, L.5    Budisa, N.6
  • 15
    • 58849110330 scopus 로고    scopus 로고
    • A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer
    • Brustad E.M., Lemke E.A., Schultz P.G., Deniz A.A. A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer. J Am Chem Soc 2008, 130:17664-17665.
    • (2008) J Am Chem Soc , vol.130 , pp. 17664-17665
    • Brustad, E.M.1    Lemke, E.A.2    Schultz, P.G.3    Deniz, A.A.4
  • 16
    • 79951678678 scopus 로고    scopus 로고
    • Site-specific coupling and sterically controlled formation of multimeric antibody Fab fragments with unnatural amino acids
    • Hutchins B.M., Kazane S.A., Staflin K., Forsyth J.S., Felding-Habermann B., Schultz P.G., Smider V.V. Site-specific coupling and sterically controlled formation of multimeric antibody Fab fragments with unnatural amino acids. J Mol Biol 2011, 406:595-603.
    • (2011) J Mol Biol , vol.406 , pp. 595-603
    • Hutchins, B.M.1    Kazane, S.A.2    Staflin, K.3    Forsyth, J.S.4    Felding-Habermann, B.5    Schultz, P.G.6    Smider, V.V.7
  • 17
    • 78049389374 scopus 로고    scopus 로고
    • Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA
    • Hughes R.A., Ellington A.D. Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA. Nucleic Acids Res 2010, 38:6813-6830.
    • (2010) Nucleic Acids Res , vol.38 , pp. 6813-6830
    • Hughes, R.A.1    Ellington, A.D.2
  • 18
    • 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 U S A 2002, 99:11020-11024.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 19
    • 0037422608 scopus 로고    scopus 로고
    • Addition of the keto functional group to the genetic code of Escherichia coli
    • Wang L., Zhang Z., Brock A., Schultz P.G. Addition of the keto functional group to the genetic code of Escherichia coli. Proc Natl Acad Sci U S A 2003, 100:56-61.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 56-61
    • Wang, L.1    Zhang, Z.2    Brock, A.3    Schultz, P.G.4
  • 22
    • 79951644876 scopus 로고    scopus 로고
    • The de novo engineering of pyrrolysyl-tRNA synthetase for genetic incorporation of l-phenylalanine and its derivatives
    • Wang Y.-S., Russell W.K., Wang Z., Wan W., Dodd L.E., Pai P.-J., Russell D.H., Liu W.R. The de novo engineering of pyrrolysyl-tRNA synthetase for genetic incorporation of l-phenylalanine and its derivatives. Mol Biosyst 2011, 7:714-717.
    • (2011) Mol Biosyst , vol.7 , pp. 714-717
    • Wang, Y.-S.1    Russell, W.K.2    Wang, Z.3    Wan, W.4    Dodd, L.E.5    Pai, P.-J.6    Russell, D.H.7    Liu, W.R.8
  • 23
    • 79960544618 scopus 로고    scopus 로고
    • Stereochemical basis for engineered pyrrolysyl-tRNA synthetase and the efficient in vivo incorporation of structurally divergent non-native amino acids
    • Takimoto J.K., Dellas N., Noel J.P., Wang L. Stereochemical basis for engineered pyrrolysyl-tRNA synthetase and the efficient in vivo incorporation of structurally divergent non-native amino acids. ACS Chem Biol 2011, 6:733-743.
    • (2011) ACS Chem Biol , vol.6 , pp. 733-743
    • Takimoto, J.K.1    Dellas, N.2    Noel, J.P.3    Wang, L.4
  • 24
    • 77951568311 scopus 로고    scopus 로고
    • A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli
    • Wan W., Huang Y., Wang Z., Russell William K., Pai P.-J., Russell David H., Liu W.R. A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli. Angew Chem Int Ed Engl 2010, 49:3211-3214.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 3211-3214
    • Wan, W.1    Huang, Y.2    Wang, Z.3    Russell William, K.4    Pai, P.-J.5    Russell David, H.6    Liu, W.R.7
  • 25
  • 27
    • 84855455724 scopus 로고    scopus 로고
    • Genetically encoded photocrosslinkers as molecular probes to study g-protein-coupled receptors (GPCRs)
    • [epub]
    • Beck-Sickinger A.G., Budisa N. Genetically encoded photocrosslinkers as molecular probes to study g-protein-coupled receptors (GPCRs). Angew Chem Int Ed Engl 2011, [epub]. 10.1002/anie.201107211.
    • (2011) Angew Chem Int Ed Engl
    • Beck-Sickinger, A.G.1    Budisa, N.2
  • 29
    • 79952670581 scopus 로고    scopus 로고
    • In vivo incorporation of multiple noncanonical amino acids into proteins
    • Hoesl M.G., Budisa N. In vivo incorporation of multiple noncanonical amino acids into proteins. Angew Chem Int Ed Engl 2011, 50:2896-2902.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 2896-2902
    • Hoesl, M.G.1    Budisa, N.2
  • 30
    • 77949772551 scopus 로고    scopus 로고
    • Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome
    • Neumann H., Wang K., Davis L., Garcia-Alai M., Chin J.W. Encoding multiple unnatural amino acids via evolution of a quadruplet-decoding ribosome. Nature 2010, 464:441-444.
    • (2010) Nature , vol.464 , pp. 441-444
    • Neumann, H.1    Wang, K.2    Davis, L.3    Garcia-Alai, M.4    Chin, J.W.5
  • 31
    • 77950922621 scopus 로고    scopus 로고
    • Ribosome evolution for two artificial amino acids in E. coli
    • Hayashi G., Goto Y., Suga H. Ribosome evolution for two artificial amino acids in E. coli. Chem Biol 2010, 17:320-321.
    • (2010) Chem Biol , vol.17 , pp. 320-321
    • Hayashi, G.1    Goto, Y.2    Suga, H.3
  • 32
    • 77955027713 scopus 로고    scopus 로고
    • In vivo double and triple labeling of proteins using synthetic amino acids
    • Lepthien S., Merkel L., Budisa N. In vivo double and triple labeling of proteins using synthetic amino acids. Angew Chem Int Ed Engl 2010, 49:5446-5450.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 5446-5450
    • Lepthien, S.1    Merkel, L.2    Budisa, N.3
  • 33
    • 77955135682 scopus 로고    scopus 로고
    • Parallel incorporation of different fluorinated amino acids: on the way to teflon proteins
    • Merkel L., Schauer M., Antranikian G., Budisa N. Parallel incorporation of different fluorinated amino acids: on the way to teflon proteins. ChemBioChem 2010, 11:1505-1507.
    • (2010) ChemBioChem , vol.11 , pp. 1505-1507
    • Merkel, L.1    Schauer, M.2    Antranikian, G.3    Budisa, N.4
  • 34
    • 79952025193 scopus 로고    scopus 로고
    • Expanding and engineering the genetic code in a single expression experiment
    • Hoesl M.G., Budisa N. Expanding and engineering the genetic code in a single expression experiment. ChemBioChem 2011, 12:552-555.
    • (2011) ChemBioChem , vol.12 , pp. 552-555
    • Hoesl, M.G.1    Budisa, N.2
  • 35
    • 79952379382 scopus 로고    scopus 로고
    • A facile and efficient method for the incorporation of multiple unnatural amino acids into a single protein
    • Ayyadurai N., Deepankumar K., Prabhu N.S., Lee S., Yun H. A facile and efficient method for the incorporation of multiple unnatural amino acids into a single protein. Chem Commun 2011, 47:3430-3432.
    • (2011) Chem Commun , vol.47 , pp. 3430-3432
    • Ayyadurai, N.1    Deepankumar, K.2    Prabhu, N.S.3    Lee, S.4    Yun, H.5
  • 36
    • 33645325418 scopus 로고    scopus 로고
    • Efficient incorporation of unnatural amino acids into proteins in Escherichia coli
    • Ryu Y.H., Schultz P.G. Efficient incorporation of unnatural amino acids into proteins in Escherichia coli. Nat Methods 2006, 3:263-265.
    • (2006) Nat Methods , vol.3 , pp. 263-265
    • Ryu, Y.H.1    Schultz, P.G.2
  • 37
    • 70449597245 scopus 로고    scopus 로고
    • Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids
    • Guo J., Charles E.M., Lee H.S., Groff D., Schultz Peter G. Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids. Angew Chem Int Ed Engl 2009, 48:9148-9151.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 9148-9151
    • Guo, J.1    Charles, E.M.2    Lee, H.S.3    Groff, D.4    Schultz Peter, G.5
  • 38
    • 73149104141 scopus 로고    scopus 로고
    • An enhanced system for unnatural amino acid mutagenesis in E. coli
    • Young T.S., Ahmad I., Yin J.A., Schultz P.G. An enhanced system for unnatural amino acid mutagenesis in E. coli. J Mol Biol 2010, 395:361-374.
    • (2010) J Mol Biol , vol.395 , pp. 361-374
    • Young, T.S.1    Ahmad, I.2    Yin, J.A.3    Schultz, P.G.4
  • 39
    • 47749109536 scopus 로고    scopus 로고
    • In vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy
    • Cellitti S.E., Jones D.H., Lagpacan L., Hao X.S., Zhang Q., Hu H.Y., Brittain S.M., Brinker A., Caldwell J., Bursulaya B., et al. In vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy. J Am Chem Soc 2008, 130:9268-9281.
    • (2008) J Am Chem Soc , vol.130 , pp. 9268-9281
    • Cellitti, S.E.1    Jones, D.H.2    Lagpacan, L.3    Hao, X.S.4    Zhang, Q.5    Hu, H.Y.6    Brittain, S.M.7    Brinker, A.8    Caldwell, J.9    Bursulaya, B.10
  • 40
    • 77949757079 scopus 로고    scopus 로고
    • A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli
    • Huang Y., Russell W.K., Wan W., Pai P.J., Russell D.H., Liu W.S. A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli. Mol Biosyst 2010, 6:683-686.
    • (2010) Mol Biosyst , vol.6 , pp. 683-686
    • Huang, Y.1    Russell, W.K.2    Wan, W.3    Pai, P.J.4    Russell, D.H.5    Liu, W.S.6
  • 41
    • 34447342528 scopus 로고    scopus 로고
    • Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion
    • Wang K.H., Neumann H., Peak-Chew S.Y., Chin J.W. Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion. Nat Biotechnol 2007, 25:770-777.
    • (2007) Nat Biotechnol , vol.25 , pp. 770-777
    • Wang, K.H.1    Neumann, H.2    Peak-Chew, S.Y.3    Chin, J.W.4
  • 42
    • 0021334017 scopus 로고
    • A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA nonsense suppressors
    • Ryden S.M., Isaksson L.A. A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA nonsense suppressors. Mol Gen Genet 1984, 193:38-45.
    • (1984) Mol Gen Genet , vol.193 , pp. 38-45
    • Ryden, S.M.1    Isaksson, L.A.2
  • 46
    • 34247103448 scopus 로고    scopus 로고
    • The tmRNA system for translational surveillance and ribosome rescue
    • Moore S.D., Sauer R.T. The tmRNA system for translational surveillance and ribosome rescue. Annu Rev Biochem 2007, 76:101-124.
    • (2007) Annu Rev Biochem , vol.76 , pp. 101-124
    • Moore, S.D.1    Sauer, R.T.2
  • 49
    • 77954820676 scopus 로고    scopus 로고
    • Quadruplet codons: one small step for a ribosome, one giant leap for proteins
    • Chen I.A., Schindlinger M. Quadruplet codons: one small step for a ribosome, one giant leap for proteins. Bioessays 2010, 32:650-654.
    • (2010) Bioessays , vol.32 , pp. 650-654
    • Chen, I.A.1    Schindlinger, M.2
  • 51
    • 79953706300 scopus 로고    scopus 로고
    • Change of tRNA identity leads to a divergent orthogonal histidyl-tRNA synthetase/tRNAHis pair
    • Yuan J., Gogakos T., Babina A.M., Söll D., Randau L. Change of tRNA identity leads to a divergent orthogonal histidyl-tRNA synthetase/tRNAHis pair. Nucleic Acids Res 2011, 39:2286-2293.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2286-2293
    • Yuan, J.1    Gogakos, T.2    Babina, A.M.3    Söll, D.4    Randau, L.5
  • 52
    • 77950824636 scopus 로고    scopus 로고
    • De novo generation of mutually orthogonal aminoacyl-tRNA synthetase/tRNA pairs
    • Neumann H., Slusarczyk A.L., Chin J.W. De novo generation of mutually orthogonal aminoacyl-tRNA synthetase/tRNA pairs. J Am Chem Soc 2010, 132:2142-2144.
    • (2010) J Am Chem Soc , vol.132 , pp. 2142-2144
    • Neumann, H.1    Slusarczyk, A.L.2    Chin, J.W.3
  • 53
    • 36448968253 scopus 로고    scopus 로고
    • Elongation factor tu mutants expand amino acid tolerance of protein biosynthesis system
    • Doi Y., Ohtsuki T., Shimizu Y., Ueda T., Sisido M. Elongation factor tu mutants expand amino acid tolerance of protein biosynthesis system. J Am Chem Soc 2007, 129:14458-14462.
    • (2007) J Am Chem Soc , vol.129 , pp. 14458-14462
    • Doi, Y.1    Ohtsuki, T.2    Shimizu, Y.3    Ueda, T.4    Sisido, M.5
  • 55
    • 70349515119 scopus 로고    scopus 로고
    • The many levels of control on bacterial selenoprotein synthesis
    • Yoshizawa S., Böck A. The many levels of control on bacterial selenoprotein synthesis. Biochim Biophys Acta 2009, 1790:1404-1414.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1404-1414
    • Yoshizawa, S.1    Böck, A.2
  • 57
    • 0345549549 scopus 로고    scopus 로고
    • Non-canonical amino acids in protein engineering
    • Link A.J., Mock M.L., Tirrell D.A. Non-canonical amino acids in protein engineering. Curr Opin Biotechnol 2003, 14:603-609.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 603-609
    • Link, A.J.1    Mock, M.L.2    Tirrell, D.A.3
  • 58
    • 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 1999, 38:10649-10659.
    • (1999) Biochemistry , vol.38 , pp. 10649-10659
    • Minks, C.1    Huber, R.2    Moroder, L.3    Budisa, N.4
  • 59
    • 0042522511 scopus 로고    scopus 로고
    • Global incorporation of norleucine in place of methionine in cytochrome P450 BM-3 heme domain increases peroxygenase activity
    • Cirino P.C., Tang Y., Takahashi K., Tirrell D.A., Arnold F.H. Global incorporation of norleucine in place of methionine in cytochrome P450 BM-3 heme domain increases peroxygenase activity. Biotechnol Bioeng 2003, 83:729-734.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 729-734
    • Cirino, P.C.1    Tang, Y.2    Takahashi, K.3    Tirrell, D.A.4    Arnold, F.H.5
  • 60
    • 48649092556 scopus 로고    scopus 로고
    • Efficient N-terminal glycoconjugation of proteins by the N-end rule
    • Merkel L., Beckmann H.S.G., Wittmann V., Budisa N. Efficient N-terminal glycoconjugation of proteins by the N-end rule. ChemBioChem 2008, 9:1220-1224.
    • (2008) ChemBioChem , vol.9 , pp. 1220-1224
    • Merkel, L.1    Beckmann, H.S.G.2    Wittmann, V.3    Budisa, N.4
  • 62
    • 79954552494 scopus 로고    scopus 로고
    • Controlled and oriented immobilization of protein by site-specific incorporation of unnatural amino acid
    • Seo M.H., Han J., Jin Z., Lee D.W., Park H.S., Kim H.S. Controlled and oriented immobilization of protein by site-specific incorporation of unnatural amino acid. Anal Chem 2011, 83:2841-2845.
    • (2011) Anal Chem , vol.83 , pp. 2841-2845
    • Seo, M.H.1    Han, J.2    Jin, Z.3    Lee, D.W.4    Park, H.S.5    Kim, H.S.6
  • 64
    • 80054036727 scopus 로고    scopus 로고
    • A photocrosslinking assay for reporting protein interactions in polyketide and fatty acid synthases
    • Ye Z.X., Bair M., Desai H., Williams G.J. A photocrosslinking assay for reporting protein interactions in polyketide and fatty acid synthases. Mol Biosyst 2011, 7:3152-3156.
    • (2011) Mol Biosyst , vol.7 , pp. 3152-3156
    • Ye, Z.X.1    Bair, M.2    Desai, H.3    Williams, G.J.4
  • 65
    • 5044219778 scopus 로고    scopus 로고
    • The site-specific incorporation of p-iodo-l-phenylalanine into proteins for structure determination
    • Xie J., Wang L., Wu N., Brock A., Spraggon G., Schultz P.G. The site-specific incorporation of p-iodo-l-phenylalanine into proteins for structure determination. Nat Biotechnol 2004, 22:1297-1301.
    • (2004) Nat Biotechnol , vol.22 , pp. 1297-1301
    • Xie, J.1    Wang, L.2    Wu, N.3    Brock, A.4    Spraggon, G.5    Schultz, P.G.6
  • 66
    • 0037428005 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis of green fluorescent protein
    • Wang L., Xie J., Deniz A.A., Schultz P.G. Unnatural amino acid mutagenesis of green fluorescent protein. J Org Chem 2002, 68:174-176.
    • (2002) J Org Chem , vol.68 , pp. 174-176
    • Wang, L.1    Xie, J.2    Deniz, A.A.3    Schultz, P.G.4
  • 67
    • 72949091045 scopus 로고    scopus 로고
    • Synthesis of threefold glycosylated proteins using click chemistry and genetically encoded unnatural amino acids
    • Kaya E., Gutsmiedl K., Vrabel M., Muller M., Thumbs P., Carell T. Synthesis of threefold glycosylated proteins using click chemistry and genetically encoded unnatural amino acids. ChemBioChem 2009, 10:2858-2861.
    • (2009) ChemBioChem , vol.10 , pp. 2858-2861
    • Kaya, E.1    Gutsmiedl, K.2    Vrabel, M.3    Muller, M.4    Thumbs, P.5    Carell, T.6
  • 69
    • 74049111572 scopus 로고    scopus 로고
    • Genetic incorporation of an aliphatic keto-containing amino acid into proteins for their site-specific modifications
    • Huang Y., Wan W., Russell W.K., Pai P.-J., Wang Z., Russell D.H., Liu W. Genetic incorporation of an aliphatic keto-containing amino acid into proteins for their site-specific modifications. Bioorg Med Chem Lett 2010, 20:878-880.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 878-880
    • Huang, Y.1    Wan, W.2    Russell, W.K.3    Pai, P.-J.4    Wang, Z.5    Russell, D.H.6    Liu, W.7
  • 71
    • 56049106840 scopus 로고    scopus 로고
    • Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N-epsilon-(o-azidobenzyloxycarbonyl) lysine for site-specific protein modification
    • Yanagisawa T., Ishii R., Fukunaga R., Kobayashi T., Sakamoto K., Yokoyama S. Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N-epsilon-(o-azidobenzyloxycarbonyl) lysine for site-specific protein modification. Chem Biol 2008, 15:1187-1197.
    • (2008) Chem Biol , vol.15 , pp. 1187-1197
    • Yanagisawa, T.1    Ishii, R.2    Fukunaga, R.3    Kobayashi, T.4    Sakamoto, K.5    Yokoyama, S.6


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