메뉴 건너뛰기




Volumn , Issue , 2013, Pages 23-42

Protein engineering as an enabling tool for synthetic biology

Author keywords

Directed evolution; Metabolic engineering; Mutagenesis; Rational design; Recombination; Screening

Indexed keywords


EID: 84882674409     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-394430-6.00002-9     Document Type: Chapter
Times cited : (4)

References (92)
  • 5
    • 79958003499 scopus 로고    scopus 로고
    • Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins
    • Saven J.G. Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins. Curr Opin Chem Biol 2011, 15:452-457.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 452-457
    • Saven, J.G.1
  • 7
    • 84882705918 scopus 로고    scopus 로고
    • Computer graphics, homology modeling, and bioinformatics
    • CRC Press, Boca Raton, S.J. Park, J.R. Cochran (Eds.)
    • Green D.F. Computer graphics, homology modeling, and bioinformatics. Protein Engineering and Design 2009, 223-238. CRC Press, Boca Raton. S.J. Park, J.R. Cochran (Eds.).
    • (2009) Protein Engineering and Design , pp. 223-238
    • Green, D.F.1
  • 8
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham B.C., Wells J.A. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 1989, 244:1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 9
    • 0344348884 scopus 로고    scopus 로고
    • A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A
    • Schwaneberg U., Schmidt-Dannert C., Schmitt J., Schmid R.D. A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A. Anal Biochem 1999, 269:359-366.
    • (1999) Anal Biochem , vol.269 , pp. 359-366
    • Schwaneberg, U.1    Schmidt-Dannert, C.2    Schmitt, J.3    Schmid, R.D.4
  • 10
    • 0035313593 scopus 로고    scopus 로고
    • Improved biocatalysts by directed evolution and rational protein design
    • Bornscheuer U.T., Pohl M. Improved biocatalysts by directed evolution and rational protein design. Curr Opin Chem Biol 2001, 5:137-143.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 137-143
    • Bornscheuer, U.T.1    Pohl, M.2
  • 11
    • 70349770900 scopus 로고    scopus 로고
    • Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules
    • Koide S. Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules. Curr Opin Biotechnol 2009, 20:398-404.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 398-404
    • Koide, S.1
  • 12
    • 84882574619 scopus 로고    scopus 로고
    • Protein engineering using noncanonical amino acids
    • CRC Press, Boca Raton, S.J. Park, J.R. Cochran (Eds.)
    • Yüksel D., Pamuk D., Ivanova Y., Kumar K. Protein engineering using noncanonical amino acids. Protein Engineering and Design 2009, 206-218. CRC Press, Boca Raton. S.J. Park, J.R. Cochran (Eds.).
    • (2009) Protein Engineering and Design , pp. 206-218
    • Yüksel, D.1    Pamuk, D.2    Ivanova, Y.3    Kumar, K.4
  • 13
    • 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
  • 15
    • 0037613335 scopus 로고    scopus 로고
    • Rational design of a calcium-binding protein
    • Yang W., Jones L.M., Isley L., et al. Rational design of a calcium-binding protein. J Am Chem Soc 2003, 125:6165-6171.
    • (2003) J Am Chem Soc , vol.125 , pp. 6165-6171
    • Yang, W.1    Jones, L.M.2    Isley, L.3
  • 17
    • 0005039337 scopus 로고
    • Mutation induction and macromolecular synthesis in bacteria
    • Doudney C., Haas F. Mutation induction and macromolecular synthesis in bacteria. Proc Natl Acad Sci USA 1959, 45:709-772.
    • (1959) Proc Natl Acad Sci USA , vol.45 , pp. 709-772
    • Doudney, C.1    Haas, F.2
  • 18
    • 0015388752 scopus 로고
    • Mutagenicity of chemical carcinogens in Neurospora crassa
    • Ong T., De Serres F. Mutagenicity of chemical carcinogens in Neurospora crassa. Cancer Res 1972, 32:1890-1893.
    • (1972) Cancer Res , vol.32 , pp. 1890-1893
    • Ong, T.1    De Serres, F.2
  • 19
    • 0022390906 scopus 로고
    • A general method for saturation mutagenesis of cloned DNA fragments
    • Myers R.M., Lerman L.S., Maniatis T. A general method for saturation mutagenesis of cloned DNA fragments. Science 1985, 229:242-247.
    • (1985) Science , vol.229 , pp. 242-247
    • Myers, R.M.1    Lerman, L.S.2    Maniatis, T.3
  • 21
    • 84855440257 scopus 로고    scopus 로고
    • Random mutagenesis using a mutator strain
    • Muteeb G., Sen R. Random mutagenesis using a mutator strain. Methods Mol Biol 2010, 634:411-419.
    • (2010) Methods Mol Biol , vol.634 , pp. 411-419
    • Muteeb, G.1    Sen, R.2
  • 22
    • 3042784274 scopus 로고    scopus 로고
    • Generating mutant libraries using error-prone PCR
    • Cirino P.C., Mayer K.M., Umeno D. Generating mutant libraries using error-prone PCR. Methods Mol Biol 2003, 231:3-10.
    • (2003) Methods Mol Biol , vol.231 , pp. 3-10
    • Cirino, P.C.1    Mayer, K.M.2    Umeno, D.3
  • 23
    • 19644371928 scopus 로고    scopus 로고
    • One-step random mutagenesis by error-prone rolling circle amplification
    • Fujii R., Kitaoka M., Hayashi K. One-step random mutagenesis by error-prone rolling circle amplification. Nucleic Acids Res 2004, 32:e145.
    • (2004) Nucleic Acids Res , vol.32
    • Fujii, R.1    Kitaoka, M.2    Hayashi, K.3
  • 24
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature 1994, 370:389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 25
    • 0032866310 scopus 로고    scopus 로고
    • Evolution of a cytokine using DNA family shuffling
    • Chang C.C.J., Chen T.T., Cox B.W., et al. Evolution of a cytokine using DNA family shuffling. Nat Biotechnol 1999, 17:793-797.
    • (1999) Nat Biotechnol , vol.17 , pp. 793-797
    • Chang, C.C.J.1    Chen, T.T.2    Cox, B.W.3
  • 26
    • 0032885231 scopus 로고    scopus 로고
    • DNA shuffling of subgenomic sequences of subtilisin
    • Ness J.E., Welch M., Giver L., et al. DNA shuffling of subgenomic sequences of subtilisin. Nat Biotechnol 1999, 17:893-896.
    • (1999) Nat Biotechnol , vol.17 , pp. 893-896
    • Ness, J.E.1    Welch, M.2    Giver, L.3
  • 27
    • 1542323289 scopus 로고    scopus 로고
    • Staggered extension process (StEP) in vitro recombination
    • Aguinaldo A.M., Arnold F.H. Staggered extension process (StEP) in vitro recombination. Methods Mol Biol 2003, 231:105-110.
    • (2003) Methods Mol Biol , vol.231 , pp. 105-110
    • Aguinaldo, A.M.1    Arnold, F.H.2
  • 28
    • 84882691805 scopus 로고    scopus 로고
    • In vitro DNA recombination by random priming
    • Esteban O., Woodyer R.D., Zhao H. In vitro DNA recombination by random priming. Methods Mol Biol 2003, 231:99-104.
    • (2003) Methods Mol Biol , vol.231 , pp. 99-104
    • Esteban, O.1    Woodyer, R.D.2    Zhao, H.3
  • 29
    • 1542353447 scopus 로고    scopus 로고
    • RACHITT: gene family shuffling by random chimeragenesis on transient templates
    • Coco W.M. RACHITT: gene family shuffling by random chimeragenesis on transient templates. Methods Mol Biol 2003, 231:111-127.
    • (2003) Methods Mol Biol , vol.231 , pp. 111-127
    • Coco, W.M.1
  • 30
    • 33750026145 scopus 로고    scopus 로고
    • Producing chimeric genes by CLERY: in vitro and in vivo recombination
    • Abécassis V., Pompon D., Truan G. Producing chimeric genes by CLERY: in vitro and in vivo recombination. Methods Mol Biol 2003, 231:165-173.
    • (2003) Methods Mol Biol , vol.231 , pp. 165-173
    • Abécassis, V.1    Pompon, D.2    Truan, G.3
  • 31
    • 80053064386 scopus 로고    scopus 로고
    • Reiterative recombination for the in vivo assembly of libraries of multigene pathways
    • Wingler L.M., Cornish V.W. Reiterative recombination for the in vivo assembly of libraries of multigene pathways. Proc Natl Acad Sci 2011, 108:15135-15140.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 15135-15140
    • Wingler, L.M.1    Cornish, V.W.2
  • 32
    • 2342510292 scopus 로고    scopus 로고
    • Shuffled antibody libraries created by in vivo homologous recombination and yeast surface display
    • Swers J.S., Kellogg B.A., Wittrup K.D. Shuffled antibody libraries created by in vivo homologous recombination and yeast surface display. Nucleic Acids Res 2004, 32:e36.
    • (2004) Nucleic Acids Res , vol.32
    • Swers, J.S.1    Kellogg, B.A.2    Wittrup, K.D.3
  • 33
    • 0026657820 scopus 로고
    • Recombination between similar but not identical DNA sequences during yeast transformation occurs within short stretches of identity
    • Mézard C., Pompon D., Nicolas A. Recombination between similar but not identical DNA sequences during yeast transformation occurs within short stretches of identity. Cell 1992, 70:659-670.
    • (1992) Cell , vol.70 , pp. 659-670
    • Mézard, C.1    Pompon, D.2    Nicolas, A.3
  • 34
    • 3042739160 scopus 로고    scopus 로고
    • The creation of ITCHY hybrid protein libraries
    • Ostermeier M., Lutz S. The creation of ITCHY hybrid protein libraries. Methods Mol Biol 2003, 231:129-142.
    • (2003) Methods Mol Biol , vol.231 , pp. 129-142
    • Ostermeier, M.1    Lutz, S.2
  • 35
    • 3042702522 scopus 로고    scopus 로고
    • Preparation of SCRATCHY hybrid protein libraries
    • Lutz S., Ostermeier M. Preparation of SCRATCHY hybrid protein libraries. Methods Mol Biol 2003, 231:143-151.
    • (2003) Methods Mol Biol , vol.231 , pp. 143-151
    • Lutz, S.1    Ostermeier, M.2
  • 36
    • 34447308723 scopus 로고    scopus 로고
    • Sequence homology-independent protein recombination (SHIPREC)
    • Udit A.K., Silberg J.J., Sieber V. Sequence homology-independent protein recombination (SHIPREC). Methods Mol Biol 2003, 231:153-164.
    • (2003) Methods Mol Biol , vol.231 , pp. 153-164
    • Udit, A.K.1    Silberg, J.J.2    Sieber, V.3
  • 37
    • 73849104591 scopus 로고    scopus 로고
    • USER friendly DNA recombination (USERec): a simple and flexible near homology-independent method for gene library construction
    • Villiers B., Stein V., Hollfelder F. USER friendly DNA recombination (USERec): a simple and flexible near homology-independent method for gene library construction. Protein Eng Des Sel 2010, 23:1-8.
    • (2010) Protein Eng Des Sel , vol.23 , pp. 1-8
    • Villiers, B.1    Stein, V.2    Hollfelder, F.3
  • 38
    • 2342642643 scopus 로고    scopus 로고
    • Directed evolution of protein enzymes using nonhomologous random recombination
    • Bittker J.A., Le B.V., Liu J.M., Liu D.R. Directed evolution of protein enzymes using nonhomologous random recombination. Proc Natl Acad Sci USA 2004, 101:7011-7016.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7011-7016
    • Bittker, J.A.1    Le, B.V.2    Liu, J.M.3    Liu, D.R.4
  • 39
    • 0038799745 scopus 로고    scopus 로고
    • General method for sequence-independent site-directed chimeragenesis
    • Hiraga K., Arnold F.H. General method for sequence-independent site-directed chimeragenesis. J Mol Biol 2003, 330:287-296.
    • (2003) J Mol Biol , vol.330 , pp. 287-296
    • Hiraga, K.1    Arnold, F.H.2
  • 40
    • 33845624902 scopus 로고    scopus 로고
    • Structure-guided SCHEMA recombination of distantly related β-lactamases
    • Meyer M.M., Hochrein L., Arnold F.H. Structure-guided SCHEMA recombination of distantly related β-lactamases. Protein Eng Des Sel 2006, 19:563-570.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 563-570
    • Meyer, M.M.1    Hochrein, L.2    Arnold, F.H.3
  • 41
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based combinatorial protein engineering (SCOPE)
    • O'Maille P.E., Bakhtina M., Tsai M.D. Structure-based combinatorial protein engineering (SCOPE). J Mol Biol 2002, 321:677-691.
    • (2002) J Mol Biol , vol.321 , pp. 677-691
    • O'Maille, P.E.1    Bakhtina, M.2    Tsai, M.D.3
  • 42
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • Reetz M.T., Carballeira J.D. Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat Protoc 2007, 2:891-903.
    • (2007) Nat Protoc , vol.2 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 43
    • 17644419994 scopus 로고    scopus 로고
    • Directed evolution of specific receptor-ligand pairs for use in the creation of gene switches
    • Chockalingam K., Chen Z., Katzenellenbogen J.A., Zhao H. Directed evolution of specific receptor-ligand pairs for use in the creation of gene switches. Proc Natl Acad Sci USA 2005, 102:5691-5696.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5691-5696
    • Chockalingam, K.1    Chen, Z.2    Katzenellenbogen, J.A.3    Zhao, H.4
  • 44
    • 34548014497 scopus 로고    scopus 로고
    • Incorporating synthetic oligonucleotides via gene reassembly (ISOR): a versatile tool for generating targeted libraries
    • Herman A., Tawfik D.S. Incorporating synthetic oligonucleotides via gene reassembly (ISOR): a versatile tool for generating targeted libraries. Protein Eng Des Sel 2007, 20:219-226.
    • (2007) Protein Eng Des Sel , vol.20 , pp. 219-226
    • Herman, A.1    Tawfik, D.S.2
  • 45
    • 84863337761 scopus 로고    scopus 로고
    • Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes
    • Chen M.M., Snow C.D., Vizcarra C.L., Mayo S.L., Arnold F.H. Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes. Protein Eng Des Sel 2012, 25:171-178.
    • (2012) Protein Eng Des Sel , vol.25 , pp. 171-178
    • Chen, M.M.1    Snow, C.D.2    Vizcarra, C.L.3    Mayo, S.L.4    Arnold, F.H.5
  • 47
    • 54349090614 scopus 로고    scopus 로고
    • Addressing the numbers problem in directed evolution
    • Reetz M.T., Kahakeaw D., Lohmer R. Addressing the numbers problem in directed evolution. Chembiochem 2008, 9:1797-1804.
    • (2008) Chembiochem , vol.9 , pp. 1797-1804
    • Reetz, M.T.1    Kahakeaw, D.2    Lohmer, R.3
  • 48
    • 23044447796 scopus 로고    scopus 로고
    • New genotype-phenotype linkages for directed evolution of functional proteins
    • Leemhuis H., Stein V., Griffiths A.D., Hollfelder F. New genotype-phenotype linkages for directed evolution of functional proteins. Curr Opin Struct Biol 2005, 15:472-478.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 472-478
    • Leemhuis, H.1    Stein, V.2    Griffiths, A.D.3    Hollfelder, F.4
  • 49
    • 23944462537 scopus 로고    scopus 로고
    • Statistics of protein library construction
    • Firth A.E., Patrick W.M. Statistics of protein library construction. Bioinformatics 2005, 21:3314-3315.
    • (2005) Bioinformatics , vol.21 , pp. 3314-3315
    • Firth, A.E.1    Patrick, W.M.2
  • 50
    • 0041765676 scopus 로고    scopus 로고
    • User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries
    • Patrick W.M., Firth A.E., Blackburn J.M. User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries. Protein Eng 2003, 16:451-457.
    • (2003) Protein Eng , vol.16 , pp. 451-457
    • Patrick, W.M.1    Firth, A.E.2    Blackburn, J.M.3
  • 51
    • 18044397860 scopus 로고    scopus 로고
    • Mathematical expressions useful in the construction, description and evaluation of protein libraries
    • Bosley A.D., Ostermeier M. Mathematical expressions useful in the construction, description and evaluation of protein libraries. Biomol Eng 2005, 22:57-61.
    • (2005) Biomol Eng , vol.22 , pp. 57-61
    • Bosley, A.D.1    Ostermeier, M.2
  • 52
    • 0033774619 scopus 로고    scopus 로고
    • Analysis of large libraries of protein mutants using flow cytometry
    • Georgiou G. Analysis of large libraries of protein mutants using flow cytometry. Adv Protein Chem 2001, 55:293-315.
    • (2001) Adv Protein Chem , vol.55 , pp. 293-315
    • Georgiou, G.1
  • 53
    • 84882727067 scopus 로고    scopus 로고
    • Combinatorial enzyme engineering
    • CRC Press, Boca Raton, S.J. Park, J.R. Cochran (Eds.)
    • Cirino P.C., Frei C.S. Combinatorial enzyme engineering. Protein Engineering and Design 2009, 131-152. CRC Press, Boca Raton. S.J. Park, J.R. Cochran (Eds.).
    • (2009) Protein Engineering and Design , pp. 131-152
    • Cirino, P.C.1    Frei, C.S.2
  • 55
    • 79551584386 scopus 로고    scopus 로고
    • Cell surface display systems for protein engineering
    • CRC Press, Boca Raton, S.J. Park, J.R. Cochran (Eds.)
    • Moore S.J., Olsen M.J., Cochran J.R., Cochran F.V. Cell surface display systems for protein engineering. Protein Engineering and Design 2009, 23-50. CRC Press, Boca Raton. S.J. Park, J.R. Cochran (Eds.).
    • (2009) Protein Engineering and Design , pp. 23-50
    • Moore, S.J.1    Olsen, M.J.2    Cochran, J.R.3    Cochran, F.V.4
  • 56
    • 18744388856 scopus 로고    scopus 로고
    • Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
    • Varadarajan N., Gam J., Olsen M.J., Georgiou G., Iverson B.L. Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity. Proc Natl Acad Sci USA 2005, 102:6850-6855.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6850-6855
    • Varadarajan, N.1    Gam, J.2    Olsen, M.J.3    Georgiou, G.4    Iverson, B.L.5
  • 57
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder E.T., Wittrup K.D. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 1997, 15:553-557.
    • (1997) Nat Biotechnol , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 58
    • 58749112914 scopus 로고    scopus 로고
    • Construction and screening of antigen targeted immune yeast surface display antibody libraries
    • [chapter 4: unit 4.7]. doi: 10.1002/0471142956.cy0407s45
    • Miller K.D., Pefaur N.B., Baird C.L. Construction and screening of antigen targeted immune yeast surface display antibody libraries. Curr Protoc Cytom 2008, [chapter 4: unit 4.7]. doi: 10.1002/0471142956.cy0407s45.
    • (2008) Curr Protoc Cytom
    • Miller, K.D.1    Pefaur, N.B.2    Baird, C.L.3
  • 59
    • 13844250741 scopus 로고    scopus 로고
    • High-throughput screens and selections of enzyme-encoding genes
    • Aharoni A., Griffiths A.D., Tawfik D.S. High-throughput screens and selections of enzyme-encoding genes. Curr Opin Struct Biol 2005, 9:210-216.
    • (2005) Curr Opin Struct Biol , vol.9 , pp. 210-216
    • Aharoni, A.1    Griffiths, A.D.2    Tawfik, D.S.3
  • 60
    • 0037413687 scopus 로고    scopus 로고
    • Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization
    • Griffiths A.D., Tawfik D.S. Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization. EMBO J 2003, 22:24-35.
    • (2003) EMBO J , vol.22 , pp. 24-35
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 61
    • 33745339106 scopus 로고    scopus 로고
    • Directed evolution by in vitro compartmentalization
    • Miller O.J., Bernath K., Agresti J.J., et al. Directed evolution by in vitro compartmentalization. Nat Methods 2006, 3:561-570.
    • (2006) Nat Methods , vol.3 , pp. 561-570
    • Miller, O.J.1    Bernath, K.2    Agresti, J.J.3
  • 62
    • 84882662475 scopus 로고    scopus 로고
    • Phage Display Systems for Protein Engineering
    • CRC Press, Boca Raton, S.J. Park, J.R. Cochran (Eds.)
    • Ernst A., Sidhu S.S. Phage Display Systems for Protein Engineering. Protein Engineering and Design 2009, 1-22. CRC Press, Boca Raton. S.J. Park, J.R. Cochran (Eds.).
    • (2009) Protein Engineering and Design , pp. 1-22
    • Ernst, A.1    Sidhu, S.S.2
  • 63
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
    • Baca M., Scanlan T.S., Stephenson R.C., Wells J.A. Phage display of a catalytic antibody to optimize affinity for transition-state analog binding. Proc Natl Acad Sci 1997, 94:10063-10068.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 10063-10068
    • Baca, M.1    Scanlan, T.S.2    Stephenson, R.C.3    Wells, J.A.4
  • 64
    • 0033506261 scopus 로고    scopus 로고
    • Ribosome display: an in vitro method for selection and evolution of antibodies from libraries
    • Schaffitzel C., Hanes J., Jermutus L., Plückthun A. Ribosome display: an in vitro method for selection and evolution of antibodies from libraries. J Immunol Methods 1999, 231:119-135.
    • (1999) J Immunol Methods , vol.231 , pp. 119-135
    • Schaffitzel, C.1    Hanes, J.2    Jermutus, L.3    Plückthun, A.4
  • 65
    • 0037333841 scopus 로고    scopus 로고
    • MRNA display: ligand discovery, interaction analysis and beyond
    • Takahashi T.T., Austin R.J., Roberts R.W. mRNA display: ligand discovery, interaction analysis and beyond. Trends Biochem Sci 2003, 28:159-165.
    • (2003) Trends Biochem Sci , vol.28 , pp. 159-165
    • Takahashi, T.T.1    Austin, R.J.2    Roberts, R.W.3
  • 66
    • 18044391361 scopus 로고    scopus 로고
    • Covalent DNA display as a novel tool for directed evolution of proteins in vitro
    • Bertschinger J., Neri D. Covalent DNA display as a novel tool for directed evolution of proteins in vitro. Protein Eng Des Sel 2004, 17:699-707.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 699-707
    • Bertschinger, J.1    Neri, D.2
  • 67
    • 1542297763 scopus 로고    scopus 로고
    • CIS display: in vitro selection of peptides from libraries of protein-DNA complexes
    • Odegrip R., Coomber D., Eldridge B., et al. CIS display: in vitro selection of peptides from libraries of protein-DNA complexes. Proc Natl Acad Sci USA 2004, 101:2806-2810.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2806-2810
    • Odegrip, R.1    Coomber, D.2    Eldridge, B.3
  • 68
    • 84859240125 scopus 로고    scopus 로고
    • Cell-free display systems for protein engineering
    • CRC Press, Boca Raton, S.J. Park, J.R. Cochran (Eds.)
    • Barendt P.A., Sarkar C.A. Cell-free display systems for protein engineering. Protein Engineering and Design 2009, 51-82. CRC Press, Boca Raton. S.J. Park, J.R. Cochran (Eds.).
    • (2009) Protein Engineering and Design , pp. 51-82
    • Barendt, P.A.1    Sarkar, C.A.2
  • 69
    • 33748904554 scopus 로고    scopus 로고
    • Ribosome-display technology: applications for directed evolution of functional proteins
    • Yan X., Xu Z. Ribosome-display technology: applications for directed evolution of functional proteins. Drug Discov Today 2006, 11:911-916.
    • (2006) Drug Discov Today , vol.11 , pp. 911-916
    • Yan, X.1    Xu, Z.2
  • 70
    • 0037077593 scopus 로고    scopus 로고
    • In vitro selection for catalytic activity with ribosome display
    • Amstutz P., Pelletier J.N., Guggisberg A., et al. In vitro selection for catalytic activity with ribosome display. J Am Chem Soc 2002, 124:9396-9403.
    • (2002) J Am Chem Soc , vol.124 , pp. 9396-9403
    • Amstutz, P.1    Pelletier, J.N.2    Guggisberg, A.3
  • 72
    • 33750982135 scopus 로고    scopus 로고
    • In vitro evolution of single-chain antibodies using mRNA display
    • Fukuda I., Kojoh K., Tabata N., et al. In vitro evolution of single-chain antibodies using mRNA display. Nucleic Acids Res 2006, 34:e127.
    • (2006) Nucleic Acids Res , vol.34
    • Fukuda, I.1    Kojoh, K.2    Tabata, N.3
  • 73
    • 46649102519 scopus 로고    scopus 로고
    • A novel genetic selection system for improved enantioselectivity of Bacillus subtilis lipase A
    • Boersma Y.L., Dröge M.J., Van Der Sloot A.M., et al. A novel genetic selection system for improved enantioselectivity of Bacillus subtilis lipase A. Chembiochem 2008, 9:1110-1115.
    • (2008) Chembiochem , vol.9 , pp. 1110-1115
    • Boersma, Y.L.1    Dröge, M.J.2    Van Der Sloot, A.M.3
  • 74
    • 34547689731 scopus 로고    scopus 로고
    • Emergence of novel functions in transcriptional regulators by regression to stem protein types
    • Galvão T.C., Mencía M., de Lorenzo V. Emergence of novel functions in transcriptional regulators by regression to stem protein types. Mol Microbiol 2007, 65:907-919.
    • (2007) Mol Microbiol , vol.65 , pp. 907-919
    • Galvão, T.C.1    Mencía, M.2    de Lorenzo, V.3
  • 75
    • 79951801949 scopus 로고    scopus 로고
    • Cooperative amino acid changes shift the response of the σ54-dependent regulator XylR from natural m-xylene towards xenobiotic 2, 4-dinitrotoluene
    • de las Heras A., de Lorenzo V. Cooperative amino acid changes shift the response of the σ54-dependent regulator XylR from natural m-xylene towards xenobiotic 2, 4-dinitrotoluene. Mol Microbiol 2011, 79:1248-1259.
    • (2011) Mol Microbiol , vol.79 , pp. 1248-1259
    • de las Heras, A.1    de Lorenzo, V.2
  • 76
    • 55849108542 scopus 로고    scopus 로고
    • Stable implantation of orthogonal sensor circuits in gram-negative bacteria for environmental release
    • de Las Heras A., Carreño C.A., de Lorenzo V. Stable implantation of orthogonal sensor circuits in gram-negative bacteria for environmental release. Environ Microbiol 2008, 10:3305-3316.
    • (2008) Environ Microbiol , vol.10 , pp. 3305-3316
    • de Las Heras, A.1    Carreño, C.A.2    de Lorenzo, V.3
  • 77
    • 79955571009 scopus 로고    scopus 로고
    • In situ detection of aromatic compounds with biosensor Pseudomonas putida cells preserved and delivered to soil in water-soluble gelatin capsules
    • de las Heras A., de Lorenzo V. In situ detection of aromatic compounds with biosensor Pseudomonas putida cells preserved and delivered to soil in water-soluble gelatin capsules. Anal Bioanal Chem 2011, 400:1093-1104.
    • (2011) Anal Bioanal Chem , vol.400 , pp. 1093-1104
    • de las Heras, A.1    de Lorenzo, V.2
  • 78
    • 77955132053 scopus 로고    scopus 로고
    • AraC protein, regulation of the l-arabinose operon in Escherichia coli, and the light switch mechanism of AraC action
    • Schleif R. AraC protein, regulation of the l-arabinose operon in Escherichia coli, and the light switch mechanism of AraC action. FEMS Microbiol Rev 2010, 34:779-796.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 779-796
    • Schleif, R.1
  • 79
    • 42149120662 scopus 로고    scopus 로고
    • AraC regulatory protein mutants with altered effector specificity
    • Tang S.Y., Fazelinia H., Cirino P.C. AraC regulatory protein mutants with altered effector specificity. J Am Chem Soc 2008, 130:5267-5271.
    • (2008) J Am Chem Soc , vol.130 , pp. 5267-5271
    • Tang, S.Y.1    Fazelinia, H.2    Cirino, P.C.3
  • 80
    • 67651030513 scopus 로고    scopus 로고
    • Biosynthesis of plant isoprenoids: perspectives for microbial engineering
    • Kirby J., Keasling J.D. Biosynthesis of plant isoprenoids: perspectives for microbial engineering. Annu Rev Plant Biol 2009, 60:335-355.
    • (2009) Annu Rev Plant Biol , vol.60 , pp. 335-355
    • Kirby, J.1    Keasling, J.D.2
  • 81
    • 79251580632 scopus 로고    scopus 로고
    • Design and application of a mevalonate-responsive regulatory protein
    • Tang S.Y., Cirino P.C. Design and application of a mevalonate-responsive regulatory protein. Angew Chem Int Ed 2011, 50:1084-1086.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 1084-1086
    • Tang, S.Y.1    Cirino, P.C.2
  • 82
    • 84882715653 scopus 로고    scopus 로고
    • Protein and RNA engineering to customize microbial molecular reporting
    • Gredell J.A., Frei C.S., Cirino P.C. Protein and RNA engineering to customize microbial molecular reporting. Biotechnol J 2011.
    • (2011) Biotechnol J
    • Gredell, J.A.1    Frei, C.S.2    Cirino, P.C.3
  • 83
    • 0037140747 scopus 로고    scopus 로고
    • Deoxygenation of polyhydroxybenzenes: an alternative strategy for the benzene-free synthesis of aromatic chemicals
    • Hansen C.A., Frost J. Deoxygenation of polyhydroxybenzenes: an alternative strategy for the benzene-free synthesis of aromatic chemicals. J Am Chem Soc 2002, 124:5926-5927.
    • (2002) J Am Chem Soc , vol.124 , pp. 5926-5927
    • Hansen, C.A.1    Frost, J.2
  • 84
    • 0032309342 scopus 로고    scopus 로고
    • Recent trends in high-energy materials
    • Agrawal J. Recent trends in high-energy materials. Prog Energy Combust Sci 1998, 24:1-30.
    • (1998) Prog Energy Combust Sci , vol.24 , pp. 1-30
    • Agrawal, J.1
  • 85
    • 0032569804 scopus 로고    scopus 로고
    • New pathway to polyketides in plants
    • Eckermann S., Schröder G., Schmidt J., et al. New pathway to polyketides in plants. Nature 1998, 396:387-390.
    • (1998) Nature , vol.396 , pp. 387-390
    • Eckermann, S.1    Schröder, G.2    Schmidt, J.3
  • 86
    • 58549111802 scopus 로고    scopus 로고
    • Expanding metabolism for biosynthesis of nonnatural alcohols
    • Zhang K., Sawaya M.R., Eisenberg D.S., Liao J.C. Expanding metabolism for biosynthesis of nonnatural alcohols. Proc Natl Acad Sci 2008, 105:20653-20658.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 20653-20658
    • Zhang, K.1    Sawaya, M.R.2    Eisenberg, D.S.3    Liao, J.C.4
  • 87
    • 52649129870 scopus 로고    scopus 로고
    • DNA coding for mutant isopropylmalate synthase L-leucine-producing microorganism and method for producing L-leucine. In United States Patent
    • Gusyatiner MM, Lunts MG, Kozlov YI, Ivanovskaya LV, Voroshilova EB. DNA coding for mutant isopropylmalate synthase L-leucine-producing microorganism and method for producing L-leucine. In United States Patent, 2002.
    • (2002)
    • Gusyatiner, M.M.1    Lunts, M.G.2    Kozlov, Y.I.3    Ivanovskaya, L.V.4    Voroshilova, E.B.5
  • 88
    • 84860211608 scopus 로고    scopus 로고
    • A synthetic recursive "+1" pathway for carbon chain elongation
    • Marcheschi R.J., Li H., Zhang K., et al. A synthetic recursive "+1" pathway for carbon chain elongation. ACS Chem Biol 2012, 7:689-697.
    • (2012) ACS Chem Biol , vol.7 , pp. 689-697
    • Marcheschi, R.J.1    Li, H.2    Zhang, K.3
  • 89
    • 77950899704 scopus 로고    scopus 로고
    • Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine
    • Zhang K., Li H., Cho K.M., Liao J.C. Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine. Proc Natl Acad Sci 2010, 107:6234-6239.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 6234-6239
    • Zhang, K.1    Li, H.2    Cho, K.M.3    Liao, J.C.4
  • 90
    • 3042777950 scopus 로고    scopus 로고
    • Creation of a shikimate pathway variant
    • Ran N., Draths K., Frost J. Creation of a shikimate pathway variant. J Am Chem Soc 2004, 126:6856-6857.
    • (2004) J Am Chem Soc , vol.126 , pp. 6856-6857
    • Ran, N.1    Draths, K.2    Frost, J.3
  • 91
    • 34249012749 scopus 로고    scopus 로고
    • Directed evolution of 2-keto-3-deoxy-6-phosphogalactonate aldolase to replace 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase
    • Ran N., Frost J.W. Directed evolution of 2-keto-3-deoxy-6-phosphogalactonate aldolase to replace 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase. J Am Chem Soc 2007, 129:6130-6139.
    • (2007) J Am Chem Soc , vol.129 , pp. 6130-6139
    • Ran, N.1    Frost, J.W.2
  • 92
    • 1642457254 scopus 로고    scopus 로고
    • Metabolic engineering for microbial production of shikimic acid
    • Krämer M., Bongaerts J., Bovenberg R., et al. Metabolic engineering for microbial production of shikimic acid. Metab Eng 2003, 5:277-283.
    • (2003) Metab Eng , vol.5 , pp. 277-283
    • Krämer, M.1    Bongaerts, J.2    Bovenberg, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.