메뉴 건너뛰기




Volumn 178, Issue 1, 2014, Pages 12-22

An amino acid depleted cell-free protein synthesis system for the incorporation of non-canonical amino acid analogs into proteins

Author keywords

Cell free protein synthesis; Residue specific incorporation; Streptavidin; Tryptophan; Unnatural amino acids

Indexed keywords

BIOSYNTHESIS; PROTEINS; CELLS; CYTOLOGY;

EID: 84896454374     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.02.009     Document Type: Article
Times cited : (27)

References (70)
  • 1
    • 84878892281 scopus 로고    scopus 로고
    • Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation
    • Albayrak C., Swartz J.R. Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation. Nucleic Acids Res. 2013, 41:5949-5963.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 5949-5963
    • Albayrak, C.1    Swartz, J.R.2
  • 2
    • 84873479729 scopus 로고    scopus 로고
    • Using E. coli-based cell-free protein synthesis to evaluate the kinetic performance of an orthogonal tRNA and aminoacyl-tRNA synthetase pair
    • Albayrak C., Swartz J.R. Using E. coli-based cell-free protein synthesis to evaluate the kinetic performance of an orthogonal tRNA and aminoacyl-tRNA synthetase pair. Biochem. Biophys. Res. Commun. 2013, 431:291-295.
    • (2013) Biochem. Biophys. Res. Commun. , vol.431 , pp. 291-295
    • Albayrak, C.1    Swartz, J.R.2
  • 4
    • 0034878705 scopus 로고    scopus 로고
    • Selection and characterization of Escherichia coli variants capable of growth on an otherwise toxic tryptophan analogue
    • Bacher J.M., Ellington A.D. Selection and characterization of Escherichia coli variants capable of growth on an otherwise toxic tryptophan analogue. J. Bacteriol. 2001, 183:5414-5425.
    • (2001) J. Bacteriol. , vol.183 , pp. 5414-5425
    • Bacher, J.M.1    Ellington, A.D.2
  • 7
    • 0029793803 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoretic method for assessing the quaternary state and comparative thermostability of avidin and streptavidin
    • Bayer E.A., Ehrlich-Rogozinski S., Wilchek M. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic method for assessing the quaternary state and comparative thermostability of avidin and streptavidin. Electrophoresis 1996, 17:1319-1324.
    • (1996) Electrophoresis , vol.17 , pp. 1319-1324
    • Bayer, E.A.1    Ehrlich-Rogozinski, S.2    Wilchek, M.3
  • 8
    • 0038383546 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis in mapping ion channel function
    • Beene D.L., Dougherty D.A., Lester H.A. Unnatural amino acid mutagenesis in mapping ion channel function. Curr. Opin. Neurobiol. 2003, 13:264-270.
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 264-270
    • Beene, D.L.1    Dougherty, D.A.2    Lester, H.A.3
  • 9
    • 0023728134 scopus 로고
    • Suppression of fluorescence of tryptophan residues in proteins by replacement with 4-fluorotryptophan
    • Bronskill P.M., Wong J.T. Suppression of fluorescence of tryptophan residues in proteins by replacement with 4-fluorotryptophan. Biochem. J 1988, 249:305-308.
    • (1988) Biochem. J , vol.249 , pp. 305-308
    • Bronskill, P.M.1    Wong, J.T.2
  • 10
    • 8344221191 scopus 로고    scopus 로고
    • Designing novel spectral classes of proteins with a tryptophan-expanded genetic code
    • Budisa N., Pal P.P. Designing novel spectral classes of proteins with a tryptophan-expanded genetic code. Biol. Chem. 2004, 385:893-904.
    • (2004) Biol. Chem. , vol.385 , pp. 893-904
    • Budisa, N.1    Pal, P.P.2
  • 13
    • 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. FEBS J. 1995, 230:788-796.
    • (1995) FEBS J. , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3    Eckerskorn, C.4    Kellermann, J.5    Huber, R.6
  • 14
    • 77049113819 scopus 로고    scopus 로고
    • Site-specific incorporation of p-propargyloxyphenylalanine in a cell-free environment for direct protein-protein click conjugation
    • Bundy B.C., Swartz J.R. Site-specific incorporation of p-propargyloxyphenylalanine in a cell-free environment for direct protein-protein click conjugation. Bioconjug. Chem. 2010, 21:255-263.
    • (2010) Bioconjug. Chem. , vol.21 , pp. 255-263
    • Bundy, B.C.1    Swartz, J.R.2
  • 15
    • 23244440886 scopus 로고    scopus 로고
    • An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
    • Calhoun K.A., Swartz J.R. An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol. Prog. 2005, 21:1146-1153.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1146-1153
    • Calhoun, K.A.1    Swartz, J.R.2
  • 17
    • 84894033400 scopus 로고    scopus 로고
    • Synthesis of 2.3mg/ml of protein with an all Escherichia coli cell-free transcription-translation system
    • Caschera F., Noireaux V. Synthesis of 2.3mg/ml of protein with an all Escherichia coli cell-free transcription-translation system. Biochimie 2014, 99:162-168.
    • (2014) Biochimie , vol.99 , pp. 162-168
    • Caschera, F.1    Noireaux, V.2
  • 19
    • 0028910003 scopus 로고
    • Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120
    • Chilkoti A., Tan P.H., Stayton P.S. Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:1754-1758.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1754-1758
    • Chilkoti, A.1    Tan, P.H.2    Stayton, P.S.3
  • 20
    • 84857440093 scopus 로고    scopus 로고
    • Multigene expression in vivo: supremacy of large versus small terminators for T7 RNA polymerase
    • Du L., Villarreal S., Forster A.C. Multigene expression in vivo: supremacy of large versus small terminators for T7 RNA polymerase. Biotechnol. Bioeng. 2012, 109:1043-1050.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1043-1050
    • Du, L.1    Villarreal, S.2    Forster, A.C.3
  • 22
    • 33846894709 scopus 로고    scopus 로고
    • Optimization of protein expression systems for modern drug discovery
    • Forstner M., Leder L., Mayr L.M. Optimization of protein expression systems for modern drug discovery. Expert Rev. Proteomics 2007, 4:67-78.
    • (2007) Expert Rev. Proteomics , vol.4 , pp. 67-78
    • Forstner, M.1    Leder, L.2    Mayr, L.M.3
  • 23
    • 58249085422 scopus 로고    scopus 로고
    • High-level cell-free synthesis yields of proteins containing site-specific non-natural amino acids
    • Goerke A.R., Swartz J.R. High-level cell-free synthesis yields of proteins containing site-specific non-natural amino acids. Biotechnol. Bioeng. 2009, 102:400-416.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 400-416
    • Goerke, A.R.1    Swartz, J.R.2
  • 24
    • 0016263758 scopus 로고
    • Incorporation of tryptophan and its benzo(b)thiophene, 1-methylindole, and indene analogs into protein of Escherichia coli
    • Hall L.E., Hegeman G.D., Bosin T.R. Incorporation of tryptophan and its benzo(b)thiophene, 1-methylindole, and indene analogs into protein of Escherichia coli. Res. Commun. Chem. Pathol. Pharmacol. 1974, 9:145-153.
    • (1974) Res. Commun. Chem. Pathol. Pharmacol. , vol.9 , pp. 145-153
    • Hall, L.E.1    Hegeman, G.D.2    Bosin, T.R.3
  • 25
    • 43049128964 scopus 로고    scopus 로고
    • An expanded set of amino acid analogs for the ribosomal translation of unnatural peptides
    • Hartman M.C., Josephson K., Lin C.W., Szostak J.W. An expanded set of amino acid analogs for the ribosomal translation of unnatural peptides. PloS One 2007, 2:e972.
    • (2007) PloS One , vol.2
    • Hartman, M.C.1    Josephson, K.2    Lin, C.W.3    Szostak, J.W.4
  • 26
    • 0026670753 scopus 로고
    • A new intrinsic fluorescent probe for proteins. Biosynthetic incorporation of 5-hydroxytryptophan into oncomodulin
    • Hogue C.W., Rasquinha I., Szabo A.G., MacManus J.P. A new intrinsic fluorescent probe for proteins. Biosynthetic incorporation of 5-hydroxytryptophan into oncomodulin. FEBS Lett. 1992, 310:269-272.
    • (1992) FEBS Lett. , vol.310 , pp. 269-272
    • Hogue, C.W.1    Rasquinha, I.2    Szabo, A.G.3    MacManus, J.P.4
  • 27
    • 84896452607 scopus 로고    scopus 로고
    • Cell-free protein synthesis from a release factor 1 deficient Escherichia coli activates efficient and multiple site-specific nonstandard amino acid incorporation
    • Hong S.H., Ntai I., Haimovich A.D., Kelleher N.L., Isaacs F.J., Jewett M.C. Cell-free protein synthesis from a release factor 1 deficient Escherichia coli activates efficient and multiple site-specific nonstandard amino acid incorporation. ACS Synth. Biol. 2014, 10.1021/sb400140t.
    • (2014) ACS Synth. Biol.
    • Hong, S.H.1    Ntai, I.2    Haimovich, A.D.3    Kelleher, N.L.4    Isaacs, F.J.5    Jewett, M.C.6
  • 28
    • 13444251466 scopus 로고    scopus 로고
    • Electrophoretic behavior of streptavidin complexed to a biotinylated probe: a functional screening assay for biotin-binding proteins
    • Humbert N., Zocchi A., Ward T.R. Electrophoretic behavior of streptavidin complexed to a biotinylated probe: a functional screening assay for biotin-binding proteins. Electrophoresis 2005, 26:47-52.
    • (2005) Electrophoresis , vol.26 , pp. 47-52
    • Humbert, N.1    Zocchi, A.2    Ward, T.R.3
  • 32
    • 0035958733 scopus 로고    scopus 로고
    • Identification of an expanded set of translationally active methionine analogues in Escherichia coli
    • Kiick K.L., Weberskirch R., Tirrell D.A. Identification of an expanded set of translationally active methionine analogues in Escherichia coli. FEBS Lett. 2001, 502:25-30.
    • (2001) FEBS Lett. , vol.502 , pp. 25-30
    • Kiick, K.L.1    Weberskirch, R.2    Tirrell, D.A.3
  • 34
    • 0942286940 scopus 로고    scopus 로고
    • Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli
    • Kim D.M., Swartz J.R. Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli. Biotechnol. Bioeng. 2004, 85:122-129.
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 122-129
    • Kim, D.M.1    Swartz, J.R.2
  • 35
    • 0034681011 scopus 로고    scopus 로고
    • Expression-independent consumption of substrates in cell-free expression system from Escherichia coli
    • Kim R.G., Choi C.Y. Expression-independent consumption of substrates in cell-free expression system from Escherichia coli. J. Biotechnol. 2001, 84:27-32.
    • (2001) J. Biotechnol. , vol.84 , pp. 27-32
    • Kim, R.G.1    Choi, C.Y.2
  • 36
    • 34548235867 scopus 로고    scopus 로고
    • Site-specific incorporation of tryptophan analogues into recombinant proteins in bacterial cells
    • Kwon I., Tirrell D.A. Site-specific incorporation of tryptophan analogues into recombinant proteins in bacterial cells. J. Am. Chem. Soc 2007, 129:10431-10437.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 10431-10437
    • Kwon, I.1    Tirrell, D.A.2
  • 37
    • 0014470838 scopus 로고
    • Incorporation of 5-methyltryptophan into the protein of Escherichia coli 15T- (555-7)
    • Lark K.G. Incorporation of 5-methyltryptophan into the protein of Escherichia coli 15T- (555-7). J. Bact. 1969, 97:980-982.
    • (1969) J. Bact. , vol.97 , pp. 980-982
    • Lark, K.G.1
  • 38
    • 0025194826 scopus 로고
    • 19F nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. An analysis of four tryptophan substitution mutants and their interactions with all-trans-retinol
    • Li E., Qian S.J., Yang N.C., d'Avignon A., Gordon J.I. 19F nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. An analysis of four tryptophan substitution mutants and their interactions with all-trans-retinol. J. Biol. Chem. 1990, 265:11549-11554.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11549-11554
    • Li, E.1    Qian, S.J.2    Yang, N.C.3    d'Avignon, A.4    Gordon, J.I.5
  • 39
    • 80053591961 scopus 로고    scopus 로고
    • Engineered streptavidin monomer and dimer with improved stability and function
    • Lim K.H., Huang H., Pralle A., Park S. Engineered streptavidin monomer and dimer with improved stability and function. Biochemistry 2011, 50:8682-8691.
    • (2011) Biochemistry , vol.50 , pp. 8682-8691
    • Lim, K.H.1    Huang, H.2    Pralle, A.3    Park, S.4
  • 40
    • 23044469032 scopus 로고    scopus 로고
    • Reassignment of sense codons in vivo
    • Link A.J., Tirrell D.A. Reassignment of sense codons in vivo. Methods 2005, 36:291-298.
    • (2005) Methods , vol.36 , pp. 291-298
    • Link, A.J.1    Tirrell, D.A.2
  • 41
    • 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
  • 43
    • 77957920290 scopus 로고    scopus 로고
    • Genetic code mutations: the breaking of a three billion year invariance
    • Mat W.K., Xue H., Wong J.T. Genetic code mutations: the breaking of a three billion year invariance. PloS one 2010, 5:e12206.
    • (2010) PloS one , vol.5
    • Mat, W.K.1    Xue, H.2    Wong, J.T.3
  • 44
    • 59649103752 scopus 로고    scopus 로고
    • Biosynthesis and stability of coiled-coil peptides containing (2S,4R)-5,5,5-trifluoroleucine and (2S,4S)-5,5,5-trifluoroleucine
    • Montclare J.K., Son S., Clark G.A., Kumar K., Tirrell D.A. Biosynthesis and stability of coiled-coil peptides containing (2S,4R)-5,5,5-trifluoroleucine and (2S,4S)-5,5,5-trifluoroleucine. Chembiochem 2009, 10:84-86.
    • (2009) Chembiochem , vol.10 , pp. 84-86
    • Montclare, J.K.1    Son, S.2    Clark, G.A.3    Kumar, K.4    Tirrell, D.A.5
  • 46
    • 20444397413 scopus 로고    scopus 로고
    • Quantitation of protein expression in a cell-free system: efficient detection of yields and 19F NMR to identify folded protein
    • Neerathilingam M., Greene L.H., Colebrooke S.A., Campbell I.D., Staunton D. Quantitation of protein expression in a cell-free system: efficient detection of yields and 19F NMR to identify folded protein. J. Biomol. NMR 2005, 31:11-19.
    • (2005) J. Biomol. NMR , vol.31 , pp. 11-19
    • Neerathilingam, M.1    Greene, L.H.2    Colebrooke, S.A.3    Campbell, I.D.4    Staunton, D.5
  • 47
    • 84859498501 scopus 로고    scopus 로고
    • Performance analysis of orthogonal pairs designed for an expanded eukaryotic genetic code
    • Nehring S., Budisa N., Wiltschi B. Performance analysis of orthogonal pairs designed for an expanded eukaryotic genetic code. PloS one 2012, 7:e31992.
    • (2012) PloS one , vol.7
    • Nehring, S.1    Budisa, N.2    Wiltschi, B.3
  • 48
    • 84857440637 scopus 로고    scopus 로고
    • High-yield cell-free protein synthesis for site-specific incorporation of unnatural amino acids at two sites
    • Ozawa K., Loscha K.V., Kuppan K.V., Loh C.T., Dixon N.E., Otting G. High-yield cell-free protein synthesis for site-specific incorporation of unnatural amino acids at two sites. Biochem. Biophys. Res. Commun. 2012, 418:652-656.
    • (2012) Biochem. Biophys. Res. Commun. , vol.418 , pp. 652-656
    • Ozawa, K.1    Loscha, K.V.2    Kuppan, K.V.3    Loh, C.T.4    Dixon, N.E.5    Otting, G.6
  • 49
    • 59149092144 scopus 로고    scopus 로고
    • Effects of tryptophan residue fluorination on streptavidin stability and biotin-streptavidin interactions via molecular dynamics simulations
    • Panek J.J., Ward T.R., Jezierska A., Novic M. Effects of tryptophan residue fluorination on streptavidin stability and biotin-streptavidin interactions via molecular dynamics simulations. J. Mol. Model. 2009, 15:257-266.
    • (2009) J. Mol. Model. , vol.15 , pp. 257-266
    • Panek, J.J.1    Ward, T.R.2    Jezierska, A.3    Novic, M.4
  • 50
    • 0016713512 scopus 로고
    • Incorporation of fluorotryptophans into proteins of Escherichia coli
    • Pratt E.A., Ho C. Incorporation of fluorotryptophans into proteins of Escherichia coli. Biochemistry 1975, 14:3035-3040.
    • (1975) Biochemistry , vol.14 , pp. 3035-3040
    • Pratt, E.A.1    Ho, C.2
  • 51
    • 0001951544 scopus 로고
    • Coupled transcription-translation in prokaryotic cell-free systems
    • IRL Press, Oxford, B. Higgins (Ed.)
    • Pratt J. Coupled transcription-translation in prokaryotic cell-free systems. Transcription and Translation - A Practical Approach 1985, IRL Press, Oxford. B. Higgins (Ed.).
    • (1985) Transcription and Translation - A Practical Approach
    • Pratt, J.1
  • 52
    • 84892365296 scopus 로고    scopus 로고
    • Engine out of the chassis: cell-free protein synthesis and its uses
    • Rosenblum G., Cooperman B.S. Engine out of the chassis: cell-free protein synthesis and its uses. FEBS Lett. 2014, 588:261-268.
    • (2014) FEBS Lett. , vol.588 , pp. 261-268
    • Rosenblum, G.1    Cooperman, B.S.2
  • 54
    • 0014429843 scopus 로고
    • The effect of amino acid analogues on alkaline phosphatase. Formation in Escherichia coli K-12. II. Replacement of tryptophan by azatryptophan and by tryptazan
    • Schlesinger S. The effect of amino acid analogues on alkaline phosphatase. Formation in Escherichia coli K-12. II. Replacement of tryptophan by azatryptophan and by tryptazan. J. Biol. Chem. 1968, 243:3877-3883.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3877-3883
    • Schlesinger, S.1
  • 56
    • 0023650543 scopus 로고
    • The codon Adaptation Index - a measure of directional synonymous codon usage bias, and its potential applications
    • Sharp P.M., Li W.H. The codon Adaptation Index - a measure of directional synonymous codon usage bias, and its potential applications. Nucleic Acids Res. 1987, 15:1281-1295.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1281-1295
    • Sharp, P.M.1    Li, W.H.2
  • 58
    • 23044507132 scopus 로고    scopus 로고
    • Four-base codon/anticodon strategy and non-enzymatic aminoacylation for protein engineering with non-natural amino acids
    • Sisido M., Ninomiya K., Ohtsuki T., Hohsaka T. Four-base codon/anticodon strategy and non-enzymatic aminoacylation for protein engineering with non-natural amino acids. Methods 2005, 36:270-278.
    • (2005) Methods , vol.36 , pp. 270-278
    • Sisido, M.1    Ninomiya, K.2    Ohtsuki, T.3    Hohsaka, T.4
  • 59
    • 0042203718 scopus 로고    scopus 로고
    • A novel immobilization method of an active protein via in vitro N-terminal specific incorporation system of nonnatural amino acids
    • Taki M., Sawata S.Y., Taira K. A novel immobilization method of an active protein via in vitro N-terminal specific incorporation system of nonnatural amino acids. Nucleic Acids Res. Suppl. 2001, 1:197-198.
    • (2001) Nucleic Acids Res. Suppl. , vol.1 , pp. 197-198
    • Taki, M.1    Sawata, S.Y.2    Taira, K.3
  • 61
    • 33749863636 scopus 로고    scopus 로고
    • Protein chip fabrication by capture of nascent polypeptides
    • Tao S.C., Zhu H. Protein chip fabrication by capture of nascent polypeptides. Nat. Biotechnol. 2006, 24:1253-1254.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1253-1254
    • Tao, S.C.1    Zhu, H.2
  • 63
    • 34547775169 scopus 로고    scopus 로고
    • Position-specific incorporation of biotinylated non-natural amino acids into a protein in a cell-free translation system
    • Watanabe T., Muranaka N., Iijima I., Hohsaka T. Position-specific incorporation of biotinylated non-natural amino acids into a protein in a cell-free translation system. Biochem. Biophys. Res. Commun. 2007, 361:794-799.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 794-799
    • Watanabe, T.1    Muranaka, N.2    Iijima, I.3    Hohsaka, T.4
  • 64
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski J.R., Zougman A., Nagaraj N., Mann M. Universal sample preparation method for proteome analysis. Nat. Methods 2009, 6:359-362.
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 65
    • 0009719233 scopus 로고
    • Membership mutation of the genetic code: loss of fitness by tryptophan
    • Wong J.T. Membership mutation of the genetic code: loss of fitness by tryptophan. Proc. Natl. Acad. Sci. U.S.A. 1983, 80:6303-6306.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 6303-6306
    • Wong, J.T.1
  • 66
    • 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
  • 67
    • 84862829177 scopus 로고    scopus 로고
    • Simplifying and streamlining Escherichia coli-based cell-free protein synthesis
    • Yang W.C., Patel K.G., Wong H.E., Swartz J.R. Simplifying and streamlining Escherichia coli-based cell-free protein synthesis. Biotechnol. Prog. 2012, 28:413-420.
    • (2012) Biotechnol. Prog. , vol.28 , pp. 413-420
    • Yang, W.C.1    Patel, K.G.2    Wong, H.E.3    Swartz, J.R.4
  • 69
    • 79956158054 scopus 로고    scopus 로고
    • Microscale to manufacturing scale-up of cell-free cytokine production - a new approach for shortening protein production development timelines
    • Zawada J.F., Yin G., Steiner A.R., Yang J., Naresh A., Roy S.M., Gold D.S., Heinsohn H.G., Murray C.J. Microscale to manufacturing scale-up of cell-free cytokine production - a new approach for shortening protein production development timelines. Biotechnol. Bioeng. 2011, 108:1570-1578.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1570-1578
    • Zawada, J.F.1    Yin, G.2    Steiner, A.R.3    Yang, J.4    Naresh, A.5    Roy, S.M.6    Gold, D.S.7    Heinsohn, H.G.8    Murray, C.J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.