메뉴 건너뛰기




Volumn , Issue , 2009, Pages 2-1-2-37

Improving protein functions by directed evolution

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84928815653     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (4)

References (230)
  • 1
    • 0035989644 scopus 로고    scopus 로고
    • Genome shuffling of Lactobacillus for improved acid tolerance
    • Patnaik, R., et al. Genome shuffling of Lactobacillus for improved acid tolerance. Nat. Biotechnol., 20(7), 707-12, 2002.
    • (2002) Nat. Biotechnol , vol.20 , Issue.7 , pp. 707-712
    • Patnaik, R.1
  • 2
    • 0037034007 scopus 로고    scopus 로고
    • Genome shuffling leads to rapid phenotypic improvement in bacteria
    • Zhang, Y.X., et al. Genome shuffling leads to rapid phenotypic improvement in bacteria. Nature, 415(6872), 644-46, 2002.
    • (2002) Nature , vol.415 , Issue.6872 , pp. 644-646
    • Zhang, Y.X.1
  • 3
    • 0942301388 scopus 로고    scopus 로고
    • Selection of human cytochrome P450 1A2 mutants with enhanced catalytic activity for heterocyclic amine N-hydroxylation
    • Kim, D. and F.P. Guengerich. Selection of human cytochrome P450 1A2 mutants with enhanced catalytic activity for heterocyclic amine N-hydroxylation. Biochemistry, 43(4), 981-88, 2004.
    • (2004) Biochemistry , vol.43 , Issue.4 , pp. 981-988
    • Kim, D.1    Guengerich, F.P.2
  • 4
    • 21244500925 scopus 로고    scopus 로고
    • Directed evolution of mammalian cytochrome P450 2B1: Mutations outside of the active site enhance the metabolism of several substrates, including the anticancer prodrugs cyclophosphamide and ifosfamide
    • Kumar, S., et al. Directed evolution of mammalian cytochrome P450 2B1: Mutations outside of the active site enhance the metabolism of several substrates, including the anticancer prodrugs cyclophosphamide and ifosfamide. J. Biol. Chem., 280(20), 19569-75, 2005.
    • (2005) J. Biol. Chem , vol.280 , Issue.20 , pp. 19569-19575
    • Kumar, S.1
  • 5
    • 18044368933 scopus 로고    scopus 로고
    • Directed molecular evolution by somatic hypermutation
    • Wang, C.L., D.C. Yang, and M. Wabl. Directed molecular evolution by somatic hypermutation. Protein Eng. Des. Sel., 17(9), 659-64, 2004.
    • (2004) Protein Eng. Des. Sel , vol.17 , Issue.9 , pp. 659-664
    • Wang, C.L.1    Yang, D.C.2    Wabl, M.3
  • 6
    • 0037159205 scopus 로고    scopus 로고
    • Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: Mutational effects on hydride transfer rates
    • Rajagopalan, P.T., S. Lutz, and S.J. Benkovic. Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: Mutational effects on hydride transfer rates. Biochemistry, 41(42), 12618-28, 2002.
    • (2002) Biochemistry , vol.41 , Issue.42 , pp. 12618-12628
    • Rajagopalan, P.T.1    Lutz, S.2    Benkovic, S.J.3
  • 7
    • 0034609556 scopus 로고    scopus 로고
    • Directed molecular evolution of cytochrome c peroxidase
    • Iffland, A., et al. Directed molecular evolution of cytochrome c peroxidase. Biochemistry, 39(35), 10790-98, 2000.
    • (2000) Biochemistry , vol.39 , Issue.35 , pp. 10790-10798
    • Iffland, A.1
  • 8
    • 0038814072 scopus 로고    scopus 로고
    • Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenyl-butyrate
    • Horsman, G.P., et al. Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenyl-butyrate. Chemistry, 9(9), 1933-39, 2003.
    • (2003) Chemistry , vol.9 , Issue.9 , pp. 1933-1939
    • Horsman, G.P.1
  • 9
    • 0014107493 scopus 로고
    • An extracellular Darwinian experiment with a selfduplicating nucleic acid molecule
    • Mills, D.R., R.L. Peterson, and S. Spiegelman. An extracellular Darwinian experiment with a selfduplicating nucleic acid molecule. Proc. Natl. Acad. Sci. uSA, 58(1), 217-24, 1967.
    • (1967) Proc. Natl. Acad. Sci. Usa , vol.58 , Issue.1 , pp. 217-224
    • Mills, D.R.1    Peterson, R.L.2    Spiegelman, S.3
  • 10
    • 0032866310 scopus 로고    scopus 로고
    • Evolution of a cytokine using DNA family shuffling
    • Chang, C.C., et al. Evolution of a cytokine using DNA family shuffling. Nat. Biotechnol., 17(8), 793-97, 1999.
    • (1999) Nat. Biotechnol , vol.17 , Issue.8 , pp. 793-797
    • Chang, C.C.1
  • 11
    • 18544397601 scopus 로고    scopus 로고
    • Directed evolution of high-affinity antibody mimics using mRNA display
    • Xu, L., et al. Directed evolution of high-affinity antibody mimics using mRNA display. Chem. Biol., 9(8), 933-42, 2002.
    • (2002) Chem. Biol , vol.9 , Issue.8 , pp. 933-942
    • Xu, L.1
  • 12
    • 0037417871 scopus 로고    scopus 로고
    • Optimized expression and specific activity of IL-12 by directed molecular evolution
    • Leong, S.R., et al. Optimized expression and specific activity of IL-12 by directed molecular evolution. Proc. Natl. Acad. Sci. uSA, 100(3), 1163-68, 2003.
    • (2003) Proc. Natl. Acad. Sci. Usa , vol.100 , Issue.3 , pp. 1163-1168
    • Leong, S.R.1
  • 13
    • 31344460657 scopus 로고    scopus 로고
    • Context-dependent mutations predominate in an engineered high-affinity single chain antibody fragment
    • Midelfort, K.S. and K.D. Wittrup. Context-dependent mutations predominate in an engineered high-affinity single chain antibody fragment. Protein Sci., 15(2), 324-34, 2006.
    • (2006) Protein Sci , vol.15 , Issue.2 , pp. 324-334
    • Midelfort, K.S.1    Wittrup, K.D.2
  • 14
    • 32344438754 scopus 로고    scopus 로고
    • Directed evolution of adeno-associated virus yields enhanced gene delivery vectors
    • Maheshri, N., et al. Directed evolution of adeno-associated virus yields enhanced gene delivery vectors. Nat. Biotechnol., 24(2), 198-204, 2006.
    • (2006) Nat. Biotechnol , vol.24 , Issue.2 , pp. 198-204
    • Maheshri, N.1
  • 15
    • 33644900247 scopus 로고    scopus 로고
    • Diversification and specialization of HIV protease function during in vitro evolution
    • O’Loughlin T. L., D.N. Greene, and I. Matsumura. Diversification and specialization of HIV protease function during in vitro evolution. Mol. Biol. Evol., 23(4), 764-72, 2006.
    • (2006) Mol. Biol. Evol , vol.23 , Issue.4 , pp. 764-772
    • O'loughlin, T.L.1    Greene, D.N.2    Matsumura, I.3
  • 16
    • 32844470411 scopus 로고    scopus 로고
    • Combinatorial engineering of a gene therapy vector: Directed evolution of adeno-associated virus
    • Perabo, L., et al. Combinatorial engineering of a gene therapy vector: Directed evolution of adeno-associated virus. J. Gene Med., 8(2), 155-62, 2006.
    • (2006) J. Gene Med , vol.8 , Issue.2 , pp. 155-162
    • Perabo, L.1
  • 17
    • 27744457705 scopus 로고    scopus 로고
    • A stable disulfide-free gene-3-protein of phage fd generated by in vitro evolution
    • Kather, I., C.A. Bippes, and F.X. Schmid. A stable disulfide-free gene-3-protein of phage fd generated by in vitro evolution. J. Mol. Biol., 354(3), 666-78, 2005.
    • (2005) J. Mol. Biol , vol.354 , Issue.3 , pp. 666-678
    • Kather, I.1    Bippes, C.A.2    Schmid, F.X.3
  • 18
    • 17844400062 scopus 로고    scopus 로고
    • Identification of a carotenoid oxygenase synthesizing acyclic xanthophylls: Combinatorial biosynthesis and directed evolution
    • Mijts, B.N., P.C. Lee, and C. Schmidt-Dannert. Identification of a carotenoid oxygenase synthesizing acyclic xanthophylls: Combinatorial biosynthesis and directed evolution. Chem. Biol., 12(4), 453-60, 2005.
    • (2005) Chem. Biol , vol.12 , Issue.4 , pp. 453-460
    • Mijts, B.N.1    Lee, P.C.2    Schmidt-Dannert, C.3
  • 19
    • 13844297445 scopus 로고    scopus 로고
    • Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity
    • Lee, P.C., et al. Directed evolution of Escherichia coli farnesyl diphosphate synthase (IspA) reveals novel structural determinants of chain length specificity. Metab. Eng., 7(1), 18-26, 2005.
    • (2005) Metab. Eng , vol.7 , Issue.1 , pp. 18-26
    • Lee, P.C.1
  • 20
    • 14644438601 scopus 로고    scopus 로고
    • Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution
    • Lee, P.C., et al. Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution. Protein Eng. Des. Sel., 17(11), 771-77, 2004.
    • (2004) Protein Eng. Des. Sel , vol.17 , Issue.11 , pp. 771-777
    • Lee, P.C.1
  • 21
    • 1342304132 scopus 로고    scopus 로고
    • Evolution of a pathway to novel long-chain carotenoids
    • Umeno, D. and F.H. Arnold. Evolution of a pathway to novel long-chain carotenoids. J. Bacteriol., 186(5), 1531-36, 2004.
    • (2004) J. Bacteriol , vol.186 , Issue.5 , pp. 1531-1536
    • Umeno, D.1    Arnold, F.H.2
  • 22
    • 0037978128 scopus 로고    scopus 로고
    • A C35 carotenoid biosynthetic pathway
    • Umeno, D. and F.H. Arnold. A C35 carotenoid biosynthetic pathway. Appl. Environ. Microbiol., 69(6), 3573-79, 2003.
    • (2003) Appl. Environ. Microbiol , vol.69 , Issue.6 , pp. 3573-3579
    • Umeno, D.1    Arnold, F.H.2
  • 23
    • 31744450975 scopus 로고    scopus 로고
    • Evolution of new protein topologies through multistep gene rearrangements
    • Peisajovich, S.G., L. Rockah, and D.S. Tawfik. Evolution of new protein topologies through multistep gene rearrangements. Nat. Genet., 38(2), 168-74, 2006.
    • (2006) Nat. Genet , vol.38 , Issue.2 , pp. 168-174
    • Peisajovich, S.G.1    Rockah, L.2    Tawfik, D.S.3
  • 24
    • 11244281311 scopus 로고    scopus 로고
    • The ‘evolvability’ of promiscuous protein functions
    • Aharoni, A., et al. The ‘evolvability’ of promiscuous protein functions. Nat. Genet., 37(1), 73-76, 2005.
    • (2005) Nat. Genet , vol.37 , Issue.1 , pp. 73-76
    • Aharoni, A.1
  • 25
    • 20544449855 scopus 로고    scopus 로고
    • Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins
    • Drummond, D.A., et al. Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. J. Mol. Biol., 350(4), 806-16, 2005.
    • (2005) J. Mol. Biol , vol.350 , Issue.4 , pp. 806-816
    • Drummond, D.A.1
  • 26
    • 31544477181 scopus 로고    scopus 로고
    • Design and evolution of new catalytic activity with an existing protein scaffold
    • Park, H.S., et al. Design and evolution of new catalytic activity with an existing protein scaffold. Science, 311(5760), 535-38, 2006.
    • (2006) Science , vol.311 , Issue.5760 , pp. 535-538
    • Park, H.S.1
  • 27
    • 33644852766 scopus 로고    scopus 로고
    • RAISE: A simple and novel method of generating random insertion and deletion mutations
    • Fujii, R., M. Kitaoka, and K. Hayashi. RAISE: A simple and novel method of generating random insertion and deletion mutations. Nucleic Acids Res., 34(4), e30, 2006.
    • (2006) Nucleic Acids Res , vol.34 , Issue.4
    • Fujii, R.1    Kitaoka, M.2    Hayashi, K.3
  • 28
    • 19444387807 scopus 로고    scopus 로고
    • Protein evolution by codon-based random deletions
    • Osuna, J., et al. Protein evolution by codon-based random deletions. Nucleic Acids Res., 32(17), e136, 2004.
    • (2004) Nucleic Acids Res , vol.32 , Issue.17
    • Osuna, J.1
  • 29
    • 0036137462 scopus 로고    scopus 로고
    • Random insertion and deletion of arbitrary number of bases for codon-based random mutation of DNAs
    • Murakami, H., T. Hohsaka, and M. Sisido. Random insertion and deletion of arbitrary number of bases for codon-based random mutation of DNAs. Nat. Biotechnol., 20(1), 76-81, 2002.
    • (2002) Nat. Biotechnol , vol.20 , Issue.1 , pp. 76-81
    • Murakami, H.1    Hohsaka, T.2    Sisido, M.3
  • 30
    • 0030669944 scopus 로고    scopus 로고
    • Insertion mutagenesis as a tool in the modification of protein function. Extended substrate specificity conferred by pentapeptide insertions in the omega-loop of TEM-1 beta-lactamase
    • Hayes, F., B. Hallet, and Y. Cao. Insertion mutagenesis as a tool in the modification of protein function. Extended substrate specificity conferred by pentapeptide insertions in the omega-loop of TEM-1 beta-lactamase. J. Biol. Chem., 272(46), 28833-36, 1997.
    • (1997) J. Biol. Chem , vol.272 , Issue.46 , pp. 28833-28836
    • Hayes, F.1    Hallet, B.2    Cao, Y.3
  • 31
    • 0032486517 scopus 로고    scopus 로고
    • Directed evolution of an esterase for the stereoselective resolution of a key intermediate in the synthesis of epothilones
    • Bornscheuer, U.T., J. Altenbuchner, and H.H. Meyer. Directed evolution of an esterase for the stereoselective resolution of a key intermediate in the synthesis of epothilones. Biotechnol. Bioeng., 58(5), 554-59, 1998.
    • (1998) Biotechnol. Bioeng , vol.58 , Issue.5 , pp. 554-559
    • Bornscheuer, U.T.1    Altenbuchner, J.2    Meyer, H.H.3
  • 33
    • 0030832921 scopus 로고    scopus 로고
    • Use of mutator cells as a means for increasing production levels of a recombinant antibody directed against Hepatitis B
    • Coia, G., et al. Use of mutator cells as a means for increasing production levels of a recombinant antibody directed against Hepatitis B. Gene, 201(1-2), 203-9, 1997.
    • (1997) Gene , vol.201 , Issue.1-2 , pp. 203-209
    • Coia, G.1
  • 34
    • 0032853779 scopus 로고    scopus 로고
    • Directed evolution of an esterase from Pseudomonas fluorescens. Random mutagenesis by error-prone PCR or a mutator strain and identification of mutants showing enhanced enantioselectivity by a resorufin-based fluorescence assay
    • Henke, E. and U.T. Bornscheuer. Directed evolution of an esterase from Pseudomonas fluorescens. Random mutagenesis by error-prone PCR or a mutator strain and identification of mutants showing enhanced enantioselectivity by a resorufin-based fluorescence assay. Biol. Chem., 380(7-8), 1029-33, 1999.
    • (1999) Biol. Chem , vol.380 , Issue.7-8 , pp. 1029-1033
    • Henke, E.1    Bornscheuer, U.T.2
  • 35
    • 0021836845 scopus 로고
    • Strategies and applications of in vitro mutagenesis
    • Botstein, D. and D. Shortle. Strategies and applications of in vitro mutagenesis. Science, 229(4719), 1193-201, 1985.
    • (1985) Science , vol.229 , Issue.4719 , pp. 1193-1201
    • Botstein, D.1    Shortle, D.2
  • 36
    • 0013846656 scopus 로고
    • Chromosomal aberrations in synchronized mammalian cells treated with 5-bromo-deoxyuridine and irradiated by ultra-violet light
    • Djordjevic, B. and O. Djordjevic. Chromosomal aberrations in synchronized mammalian cells treated with 5-bromo-deoxyuridine and irradiated by ultra-violet light. Nature, 206(989), 1165-66, 1965.
    • (1965) Nature , vol.206 , Issue.989 , pp. 1165-1166
    • Djordjevic, B.1    Djordjevic, O.2
  • 37
    • 2342590569 scopus 로고    scopus 로고
    • Mechanism of 2-aminopurine-stimulated mutagenesis in Escherichia coli
    • Pitsikas, P., J.M. Patapas, and C.G. Cupples. Mechanism of 2-aminopurine-stimulated mutagenesis in Escherichia coli. Mutat. Res., 550(1-2), 25-32, 2004.
    • (2004) Mutat. Res , vol.550 , Issue.1-2 , pp. 25-32
    • Pitsikas, P.1    Patapas, J.M.2    Cupples, C.G.3
  • 38
    • 2542436872 scopus 로고    scopus 로고
    • A new approach to random mutagenesis in vitro
    • Lai, Y.P., et al. A new approach to random mutagenesis in vitro. Biotechnol. Bioeng., 86(6), 622-27, 2004.
    • (2004) Biotechnol. Bioeng , vol.86 , Issue.6 , pp. 622-627
    • Lai, Y.P.1
  • 39
    • 0019506258 scopus 로고
    • DeMars
    • Reznikoff, C.A. and R. DeMars. In vitro chemical mutagenesis and viral transformation of a human endothelial cell strain. Cancer Res., 41(3), 1114-26, 1981.
    • (1981) Cancer Res , vol.41 , Issue.3 , pp. 1114-1126
    • Reznikoff, C.A.1
  • 40
    • 0020971323 scopus 로고
    • Directed mutagenesis with sodium bisulfite
    • Shortle, D. and D. Botstein. Directed mutagenesis with sodium bisulfite. Methods Enzymol., 100, 457-68, 1983.
    • (1983) Methods Enzymol , vol.100 , pp. 457-468
    • Shortle, D.1    Botstein, D.2
  • 41
    • 0022538668 scopus 로고
    • Mutagenesis by ethidium bromide, proflavine and mitomycin C in the cyanobacterium
    • Tripathi, A.K. and H.D. Kumar. Mutagenesis by ethidium bromide, proflavine and mitomycin C in the cyanobacterium Nostoc sp. Mutat. Res., 174(3), 175-78, 1986.
    • (1986) Nostoc Sp. Mutat. Res , vol.174 , Issue.3 , pp. 175-178
    • Tripathi, A.K.1    Kumar, H.D.2
  • 42
    • 0022348809 scopus 로고
    • On the fidelity of DNA replication: Manganese mutagenesis in vitro
    • Beckman, R.A., A.S. Mildvan, and L.A. Loeb. On the fidelity of DNA replication: Manganese mutagenesis in vitro. Biochemistry, 24(21), 5810-17, 1985.
    • (1985) Biochemistry , vol.24 , Issue.21 , pp. 5810-5817
    • Beckman, R.A.1    Mildvan, A.S.2    Loeb, L.A.3
  • 44
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R.C. and G.F. Joyce. Randomization of genes by PCR mutagenesis. PCR Methods Appl., 2(1), 28-33, 1992.
    • (1992) PCR Methods Appl , vol.2 , Issue.1 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 45
    • 0028816556 scopus 로고
    • Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction
    • Fromant, M., S. Blanquet, and P. Plateau. Direct random mutagenesis of gene-sized DNA fragments using polymerase chain reaction. Anal. Biochem., 224(1), 347-53, 1995.
    • (1995) Anal. Biochem , vol.224 , Issue.1 , pp. 347-353
    • Fromant, M.1    Blanquet, S.2    Plateau, P.3
  • 46
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung, D.W., E. Chen, and D.V. Goeddel. A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique, 1, 11-15, 1989.
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 47
    • 0032478172 scopus 로고    scopus 로고
    • Enzyme engineering reaches the boiling point
    • Arnold, F.H. Enzyme engineering reaches the boiling point. Proc. Natl. Acad. Sci. USA, 95(5), 2035-36, 1998.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.5 , pp. 2035-2036
    • Arnold, F.H.1
  • 48
    • 0030252433 scopus 로고    scopus 로고
    • Tolerance of different proteins for amino acid diversity
    • Suzuki, M., et al. Tolerance of different proteins for amino acid diversity. Mol. Divers, 2(1-2), 111-18, 1996.
    • (1996) Mol. Divers , vol.2 , Issue.1-2 , pp. 111-118
    • Suzuki, M.1
  • 49
    • 0034049316 scopus 로고    scopus 로고
    • Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies
    • Daugherty, P.S., et al. Quantitative analysis of the effect of the mutation frequency on the affinity maturation of single chain Fv antibodies. Proc. Natl. Acad. Sci. USA, 97(5), 2029-34, 2000.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.5 , pp. 2029-2034
    • Daugherty, P.S.1
  • 50
    • 0030737949 scopus 로고    scopus 로고
    • Generation of large libraries of random mutants in Bacillus subtilis by PCR-based plasmid multimerization
    • Shafikhani, S., et al. Generation of large libraries of random mutants in Bacillus subtilis by PCR-based plasmid multimerization. Biotechniques, 23(2), 304-10, 1997.
    • (1997) Biotechniques , vol.23 , Issue.2 , pp. 304-310
    • Shafikhani, S.1
  • 51
    • 14144251690 scopus 로고    scopus 로고
    • Thermodynamic prediction of protein neutrality
    • Bloom, J.D., et al. Thermodynamic prediction of protein neutrality. Proc. Natl. Acad. Sci. USA, 102(3), 606-11, 2005.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.3 , pp. 606-611
    • Bloom, J.D.1
  • 52
    • 0037412184 scopus 로고    scopus 로고
    • Robustness of hen lysozyme monitored by random mutations
    • Kunichika, K., Y. Hashimoto, and T. Imoto. Robustness of hen lysozyme monitored by random mutations. Protein Eng., 15(10), 805-9, 2002.
    • (2002) Protein Eng , vol.15 , Issue.10 , pp. 805-809
    • Kunichika, K.1    Hashimoto, Y.2    Imoto, T.3
  • 53
    • 2342535792 scopus 로고    scopus 로고
    • Sequence saturation mutagenesis (SeSaM): A novel method for directed evolution
    • Wong, T.S., et al. Sequence saturation mutagenesis (SeSaM): A novel method for directed evolution. Nucleic Acids Res., 32(3), e26, 2004.
    • (2004) Nucleic Acids Res , vol.32 , Issue.3
    • Wong, T.S.1
  • 54
    • 19644371928 scopus 로고    scopus 로고
    • One-step random mutagenesis by error-prone rolling circle amplification
    • Fujii, R., M. Kitaoka, and K. Hayashi. One-step random mutagenesis by error-prone rolling circle amplification. Nucleic Acids Res., 32(19), e145, 2004.
    • (2004) Nucleic Acids Res , vol.32 , Issue.19
    • Fujii, R.1    Kitaoka, M.2    Hayashi, K.3
  • 55
    • 0033834791 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective lipase
    • Liebeton, K., et al. Directed evolution of an enantioselective lipase. Chem. Biol., 7(9), 709-18, 2000.
    • (2000) Chem. Biol , vol.7 , Issue.9 , pp. 709-718
    • Liebeton, K.1
  • 56
    • 0030825248 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Random insertion of a variable five amino acid cassette in a target protein
    • Hallet, B., D.J. Sherratt, and F. Hayes. Pentapeptide scanning mutagenesis: Random insertion of a variable five amino acid cassette in a target protein. Nucleic Acids Res., 25(9), 1866-67, 1997.
    • (1997) Nucleic Acids Res , vol.25 , Issue.9 , pp. 1866-1867
    • Hallet, B.1    Sherratt, D.J.2    Hayes, F.3
  • 57
    • 33644986778 scopus 로고    scopus 로고
    • Frame shuffling: A novel method for in vitro protein evolution
    • Kashiwagi, K., et al. Frame shuffling: A novel method for in vitro protein evolution. Protein Eng. Des. Sel., 19(3), 135-40, 2006.
    • (2006) Protein Eng. Des. Sel , vol.19 , Issue.3 , pp. 135-140
    • Kashiwagi, K.1
  • 58
    • 0030936604 scopus 로고    scopus 로고
    • Creation of libraries with long ORFs by polymerization of a microgene
    • Shiba, K., Y. Takahashi, and T. Noda. Creation of libraries with long ORFs by polymerization of a microgene. Proc. Natl. Acad. Sci. USA, 94(8), 3805-10, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.8 , pp. 3805-3810
    • Shiba, K.1    Takahashi, Y.2    Noda, T.3
  • 59
    • 0033555718 scopus 로고    scopus 로고
    • The effect of high-frequency random mutagenesis on in vitro protein evolution: A study on TEM-1 beta-lactamase
    • Zaccolo, M. and E. Gherardi. The effect of high-frequency random mutagenesis on in vitro protein evolution: A study on TEM-1 beta-lactamase. J. Mol. Biol., 285(2), 775-83, 1999.
    • (1999) J. Mol. Biol , vol.285 , Issue.2 , pp. 775-783
    • Zaccolo, M.1    Gherardi, E.2
  • 60
    • 29144503012 scopus 로고    scopus 로고
    • A statistical analysis of random mutagenesis methods used for directed protein evolution
    • Wong, T.S., et al. A statistical analysis of random mutagenesis methods used for directed protein evolution. J. Mol. Biol., 355(4), 858-71, 2006.
    • (2006) J. Mol. Biol , vol.355 , Issue.4 , pp. 858-871
    • Wong, T.S.1
  • 61
    • 18044397860 scopus 로고    scopus 로고
    • Mathematical expressions useful in the construction, description and evaluation of protein libraries
    • Bosley, A.D. and M. Ostermeier. Mathematical expressions useful in the construction, description and evaluation of protein libraries. Biomol. Eng., 22(1-3), 57-61, 2005.
    • (2005) Biomol. Eng , vol.22 , Issue.1-3 , pp. 57-61
    • Bosley, A.D.1    Ostermeier, M.2
  • 62
    • 0036276555 scopus 로고    scopus 로고
    • S-RNase-mediated gametophytic self-incompatibility is ancestral in eudicots
    • Steinbachs, J.E. and K.E. Holsinger. S-RNase-mediated gametophytic self-incompatibility is ancestral in eudicots. Mol. Biol. Evol., 19(6), 825-29, 2002.
    • (2002) Mol. Biol. Evol , vol.19 , Issue.6 , pp. 825-829
    • Steinbachs, J.E.1    Holsinger, K.E.2
  • 63
    • 0347298800 scopus 로고    scopus 로고
    • S-RNase-mediated self-incompatibility
    • Wang, Y., et al. S-RNase-mediated self-incompatibility. J. Exp. Bot., 54(380), 115-22, 2003.
    • (2003) J. Exp. Bot , vol.54 , Issue.380 , pp. 115-122
    • Wang, Y.1
  • 64
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W.P. Rapid evolution of a protein in vitro by DNA shuffling. Nature, 370(6488), 389-91, 1994.
    • (1994) Nature , vol.370 , Issue.6488 , pp. 389-391
    • Stemmer, W.P.1
  • 65
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri, A., et al. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature, 391(6664), 288-91, 1998.
    • (1998) Nature , vol.391 , Issue.6664 , pp. 288-291
    • Crameri, A.1
  • 66
    • 0036307433 scopus 로고    scopus 로고
    • Analysis of shuffled gene libraries
    • Joern, J.M., P. Meinhold, and F.H. Arnold. Analysis of shuffled gene libraries. J. Mol. Biol., 316(3), 643-56, 2002.
    • (2002) J. Mol. Biol , vol.316 , Issue.3 , pp. 643-656
    • Joern, J.M.1    Meinhold, P.2    Arnold, F.H.3
  • 67
    • 0035854021 scopus 로고    scopus 로고
    • Degenerate oligonucleotide gene shuffling (DOGS): A method for enhancing the frequency of recombination with family shuffling
    • Gibbs, M.D., K.M. Nevalainen, and P.L. Bergquist. Degenerate oligonucleotide gene shuffling (DOGS): A method for enhancing the frequency of recombination with family shuffling. Gene, 271(1), 13-20, 2001.
    • (2001) Gene , vol.271 , Issue.1 , pp. 13-20
    • Gibbs, M.D.1    Nevalainen, K.M.2    Bergquist, P.L.3
  • 69
    • 0033964975 scopus 로고    scopus 로고
    • An effective family shuffling method using singlestranded DNA
    • Kikuchi, M., K. Ohnishi, and S. Harayama. An effective family shuffling method using singlestranded DNA. Gene, 243(1-2), 133-37, 2000.
    • (2000) Gene , vol.243 , Issue.1-2 , pp. 133-137
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 70
    • 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., 231, 111-27, 2003.
    • (2003) Methods Mol. Biol , vol.231 , pp. 111-127
    • Coco, W.M.1
  • 71
    • 27144471889 scopus 로고    scopus 로고
    • Nucleotide exchange and excision technology (NExT) DNA shuffling: A robust method for DNA fragmentation and directed evolution
    • Muller, K.M., et al. Nucleotide exchange and excision technology (NExT) DNA shuffling: A robust method for DNA fragmentation and directed evolution. Nucleic Acids Res., 33(13), e117, 2005.
    • (2005) Nucleic Acids Res , vol.33 , Issue.13
    • Muller, K.M.1
  • 72
    • 0032518181 scopus 로고    scopus 로고
    • Random-priming in vitro recombination: An effective tool for directed evolution
    • Shao, Z., et al. Random-priming in vitro recombination: An effective tool for directed evolution. Nucleic Acids Res., 26(2), 681-83, 1998.
    • (1998) Nucleic Acids Res , vol.26 , Issue.2 , pp. 681-683
    • Shao, Z.1
  • 73
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., et al. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat. Biotechnol., 16(3), 258-61, 1998.
    • (1998) Nat. Biotechnol , vol.16 , Issue.3 , pp. 258-261
    • Zhao, H.1
  • 74
    • 0036901312 scopus 로고    scopus 로고
    • Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently
    • Ness, J.E., et al. Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently. Nat. Biotechnol., 20(12), 1251-55, 2002.
    • (2002) Nat. Biotechnol , vol.20 , Issue.12 , pp. 1251-1255
    • Ness, J.E.1
  • 75
    • 0037415021 scopus 로고    scopus 로고
    • Assembly of designed oligonucleotides as an efficient method for gene recombination: A new tool in directed evolution
    • Zha, D., A. Eipper, and M.T. Reetz. Assembly of designed oligonucleotides as an efficient method for gene recombination: A new tool in directed evolution. Chembiochem. 4(1), 34-39, 2003.
    • (2003) Chembiochem , vol.4 , Issue.1 , pp. 34-39
    • Zha, D.1    Eipper, A.2    Reetz, M.T.3
  • 76
    • 0034667190 scopus 로고    scopus 로고
    • High efficiency family shuffling based on multi-step PCR and in vivo DNA recombination in yeast: Statistical and functional analysis of a combinatorial library between human cytochrome P450 1A1 and 1A2
    • Abecassis, V., D. Pompon, and G. Truan. High efficiency family shuffling based on multi-step PCR and in vivo DNA recombination in yeast: Statistical and functional analysis of a combinatorial library between human cytochrome P450 1A1 and 1A2. Nucleic Acids Res., 28(20), e88, 2000.
    • (2000) Nucleic Acids Res , vol.28 , Issue.20
    • Abecassis, V.1    Pompon, D.2    Truan, G.3
  • 77
    • 0033567665 scopus 로고    scopus 로고
    • Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair
    • Volkov, A.A., Z. Shao, and F.H. Arnold. Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair. Nucleic Acids Res., 27(18), e18, 1999.
    • (1999) Nucleic Acids Res , vol.27 , Issue.18
    • Volkov, A.A.1    Shao, Z.2    Arnold, F.H.3
  • 78
    • 33344465082 scopus 로고    scopus 로고
    • Directed evolution of extradiol dioxygenase by a novel in vivo DNA shuffling
    • Xu, S., et al. Directed evolution of extradiol dioxygenase by a novel in vivo DNA shuffling. Gene, 368, 126-37, 2006.
    • (2006) Gene , vol.368 , pp. 126-137
    • Xu, S.1
  • 79
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • Ostermeier, M., J.H. Shim, and S.J. Benkovic. A combinatorial approach to hybrid enzymes independent of DNA homology. Nat. Biotechnol., 17(12), 1205-9, 1999.
    • (1999) Nat. Biotechnol , vol.17 , Issue.12 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.H.2    Benkovic, S.J.3
  • 80
    • 18044384442 scopus 로고    scopus 로고
    • Directed evolution of (Betaalpha)(8)-barrel enzymes
    • Hocker, B. Directed evolution of (betaalpha)(8)-barrel enzymes. Biomol. Eng., 22(1-3), 31-38, 2005.
    • (2005) Biomol. Eng , vol.22 , Issue.1-3 , pp. 31-38
    • Hocker, B.1
  • 81
    • 0025284257 scopus 로고
    • The evolution of alpha/beta barrel enzymes
    • Farber, G.K. and G.A. Petsko. The evolution of alpha/beta barrel enzymes. Trends Biochem Sci, 15(6), 228-34, 1990.
    • (1990) Trends Biochem Sci , vol.15 , Issue.6 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 82
    • 0035025314 scopus 로고    scopus 로고
    • Libraries of hybrid proteins from distantly related sequences
    • Sieber, V., C.A. Martinez, and F.H. Arnold. Libraries of hybrid proteins from distantly related sequences. Nat. Biotechnol., 19(5), 456-60, 2001.
    • (2001) Nat. Biotechnol , vol.19 , Issue.5 , pp. 456-460
    • Sieber, V.1    Martinez, C.A.2    Arnold, F.H.3
  • 83
    • 0035866186 scopus 로고    scopus 로고
    • Rapid generation of incremental truncation libraries for protein engineering using alpha-phosphothioate nucleotides
    • Lutz, S., M. Ostermeier, and S.J. Benkovic. Rapid generation of incremental truncation libraries for protein engineering using alpha-phosphothioate nucleotides. Nucleic Acids Res., 29(4), e16, 2001.
    • (2001) Nucleic Acids Res , vol.29 , Issue.4
    • Lutz, S.1    Ostermeier, M.2    Benkovic, S.J.3
  • 84
    • 0035949702 scopus 로고    scopus 로고
    • Creating multiple-crossover DNA libraries independent of sequence identity
    • Lutz, S., et al. Creating multiple-crossover DNA libraries independent of sequence identity. Proc. Natl. Acad. Sci. uSA, 98(20), 11248-53, 2001.
    • (2001) Proc. Natl. Acad. Sci. Usa , vol.98 , Issue.20 , pp. 11248-11253
    • Lutz, S.1
  • 85
    • 0642334596 scopus 로고    scopus 로고
    • Enhanced crossover SCRATCHY: Construction and high-throughput screening of a combinatorial library containing multiple non-homologous crossovers
    • Kawarasaki, Y., et al. Enhanced crossover SCRATCHY: Construction and high-throughput screening of a combinatorial library containing multiple non-homologous crossovers. Nucleic Acids Res., 31(21), e126, 2003.
    • (2003) Nucleic Acids Res , vol.31 , Issue.21
    • Kawarasaki, Y.1
  • 86
    • 0035014185 scopus 로고    scopus 로고
    • Directed evolution of proteins by exon shuffling
    • Kolkman, J.A. and W.P. Stemmer. Directed evolution of proteins by exon shuffling. Nat. Biotechnol., 19(5), 423-28, 2001.
    • (2001) Nat. Biotechnol , vol.19 , Issue.5 , pp. 423-428
    • Kolkman, J.A.1    Stemmer, W.P.2
  • 87
    • 19244385868 scopus 로고    scopus 로고
    • Random multi-recombinant PCR for the construction of combinatorial protein libraries
    • Tsuji, T., M. Onimaru, and H. Yanagawa. Random multi-recombinant PCR for the construction of combinatorial protein libraries. Nucleic Acids Res., 29(20), e97, 2001.
    • (2001) Nucleic Acids Res , vol.29 , Issue.20
    • Tsuji, T.1    Onimaru, M.2    Yanagawa, H.3
  • 88
    • 0036901301 scopus 로고    scopus 로고
    • Growth factor engineering by degenerate homoduplex gene family recombination
    • Coco, W.M., et al. Growth factor engineering by degenerate homoduplex gene family recombination. Nat. Biotechnol., 20(12), 1246-50, 2002.
    • (2002) Nat. Biotechnol , vol.20 , Issue.12 , pp. 1246-1250
    • Coco, W.M.1
  • 89
    • 0036788537 scopus 로고    scopus 로고
    • Nucleic acid evolution and minimization by nonhomologous random recombination
    • Bittker, J.A., B.V. Le, and D.R. Liu. Nucleic acid evolution and minimization by nonhomologous random recombination. Nat. Biotechnol., 20(10), 1024-29, 2002.
    • (2002) Nat. Biotechnol , vol.20 , Issue.10 , pp. 1024-1029
    • Bittker, J.A.1    Le, B.V.2    Liu, D.R.3
  • 90
    • 2342642643 scopus 로고    scopus 로고
    • Directed evolution of protein enzymes using nonhomologous random recombination
    • Bittker, J.A., et al. Directed evolution of protein enzymes using nonhomologous random recombination. Proc. Natl. Acad. Sci. uSA, 101(18), 7011-16, 2004.
    • (2004) Proc. Natl. Acad. Sci. Usa , vol.101 , Issue.18 , pp. 7011-7016
    • Bittker, J.A.1
  • 91
    • 0037412178 scopus 로고    scopus 로고
    • Construction of block-shuffled libraries of DNA for evolutionary protein engineering: Y-ligation-based block shuffling
    • Kitamura, K., et al. Construction of block-shuffled libraries of DNA for evolutionary protein engineering: Y-ligation-based block shuffling. Protein Eng., 15(10), 843-53, 2002.
    • (2002) Protein Eng , vol.15 , Issue.10 , pp. 843-853
    • Kitamura, K.1
  • 92
    • 0032850532 scopus 로고    scopus 로고
    • Incremental truncation as a strategy in the engineering of novel biocatalysts
    • Ostermeier, M., A.E. Nixon, and S.J. Benkovic. Incremental truncation as a strategy in the engineering of novel biocatalysts. Bioorg. Med. Chem., 7(10), 2139-44, 1999.
    • (1999) Bioorg. Med. Chem , vol.7 , Issue.10 , pp. 2139-2144
    • Ostermeier, M.1    Nixon, A.E.2    Benkovic, S.J.3
  • 93
    • 0037420903 scopus 로고    scopus 로고
    • Theoretical distribution of truncation lengths in incremental truncation libraries
    • Ostermeier, M. Theoretical distribution of truncation lengths in incremental truncation libraries. Biotechnol. Bioeng., 82(5), 564-77, 2003.
    • (2003) Biotechnol. Bioeng , vol.82 , Issue.5 , pp. 564-577
    • Ostermeier, M.1
  • 94
    • 23944462537 scopus 로고    scopus 로고
    • Statistics of protein library construction
    • Firth, A.E. and W.M. Patrick. Statistics of protein library construction. Bioinformatics, 21(15), 3314-15, 2005.
    • (2005) Bioinformatics , vol.21 , Issue.15 , pp. 3314-3315
    • Firth, A.E.1    Patrick, W.M.2
  • 95
    • 0042430535 scopus 로고    scopus 로고
    • Optimising enzyme function by directed evolution
    • Dalby, P.A. Optimising enzyme function by directed evolution. Curr. Opin. Struct. Biol., 13(4), 5005, 2003.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , Issue.4 , pp. 5005
    • Dalby, P.A.1
  • 96
    • 12344337569 scopus 로고    scopus 로고
    • Focusing mutations into the P fluorescens esterase binding site increases enantioselec-tivity more effectively than distant mutations
    • Park, S., et al. Focusing mutations into the P fluorescens esterase binding site increases enantioselec-tivity more effectively than distant mutations. Chem. Biol., 12(1), 45-54, 2005.
    • (2005) Chem. Biol , vol.12 , Issue.1 , pp. 45-54
    • Park, S.1
  • 97
    • 0031855459 scopus 로고    scopus 로고
    • When blind is better: Protein design by evolution
    • Arnold, F.H. When blind is better: Protein design by evolution. Nat. Biotechnol., 16(7), 617-18, 1998.
    • (1998) Nat. Biotechnol , vol.16 , Issue.7 , pp. 617-618
    • Arnold, F.H.1
  • 98
    • 0042121557 scopus 로고    scopus 로고
    • Removing the redundancy from randomised gene libraries
    • Hughes, M.D., et al. Removing the redundancy from randomised gene libraries. J. Mol. Biol., 331(5), 973-79, 2003.
    • (2003) J. Mol. Biol , vol.331 , Issue.5 , pp. 973-979
    • Hughes, M.D.1
  • 99
    • 0041765676 scopus 로고    scopus 로고
    • User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries
    • Patrick, W.M., A.E. Firth, and J.M. Blackburn. User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries. Protein Eng., 16(6), 451-57, 2003.
    • (2003) Protein Eng , vol.16 , Issue.6 , pp. 451-457
    • Patrick, W.M.1    Firth, A.E.2    Blackburn, J.M.3
  • 100
    • 17644419994 scopus 로고    scopus 로고
    • Directed evolution of specific receptor-ligand pairs for use in the creation of gene switches
    • Chockalingam, K., et al. Directed evolution of specific receptor-ligand pairs for use in the creation of gene switches. Proc. Natl. Acad. Sci. uSA, 102(16), 5691-96, 2005.
    • (2005) Proc. Natl. Acad. Sci. Usa , vol.102 , Issue.16 , pp. 5691-5696
    • Chockalingam, K.1
  • 101
    • 14644433770 scopus 로고    scopus 로고
    • Combinatorial exploration of the catalytic site of a drug-resistant dihydrofolate reductase: Creating alternative functional configurations
    • Schmitzer, A.R., F. Lepine, and J.N. Pelletier. Combinatorial exploration of the catalytic site of a drug-resistant dihydrofolate reductase: Creating alternative functional configurations. Protein Eng. Des. Sel., 17(11), 809-19, 2004.
    • (2004) Protein Eng. Des. Sel , vol.17 , Issue.11 , pp. 809-819
    • Schmitzer, A.R.1    Lepine, F.2    Pelletier, J.N.3
  • 102
    • 22144485602 scopus 로고    scopus 로고
    • Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test
    • Reetz, M.T., et al. Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test. Angew Chem. Int. Ed. Engl., 44(27), 4192-96, 2005.
    • (2005) Angew Chem. Int. Ed. Engl , vol.44 , Issue.27 , pp. 4192-4196
    • Reetz, M.T.1
  • 103
    • 1842525532 scopus 로고    scopus 로고
    • Gene site saturation mutagenesis: A comprehensive mutagenesis approach
    • Kretz, K.A., et al. Gene site saturation mutagenesis: A comprehensive mutagenesis approach. Methods Enzymol., 388, 3-11, 2004.
    • (2004) Methods Enzymol , vol.388 , pp. 3-11
    • Kretz, K.A.1
  • 104
    • 14644390952 scopus 로고    scopus 로고
    • Construction of stabilized proteins by combinatorial consensus mutagenesis
    • Amin, N., et al. Construction of stabilized proteins by combinatorial consensus mutagenesis. Protein Eng. Des. Sel., 17(11), 787-93, 2004.
    • (2004) Protein Eng. Des. Sel , vol.17 , Issue.11 , pp. 787-793
    • Amin, N.1
  • 105
    • 0036289574 scopus 로고    scopus 로고
    • Protein building blocks preserved by recombination
    • Voigt, C.A., et al. Protein building blocks preserved by recombination. Nat. Struct. Biol., 9(7), 553-38, 2002.
    • (2002) Nat. Struct. Biol , vol.9 , Issue.7 , pp. 553-638
    • Voigt, C.A.1
  • 106
    • 1642529522 scopus 로고    scopus 로고
    • FamClash: A method for ranking the activity of engineered enzymes
    • Saraf, M.C., et al. FamClash: A method for ranking the activity of engineered enzymes. Proc. Natl. Acad. Sci. uSA, 101(12), 4142-47, 2004.
    • (2004) Proc. Natl. Acad. Sci. Usa , vol.101 , Issue.12 , pp. 4142-4147
    • Saraf, M.C.1
  • 107
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based combinatorial protein engineering (SCOPE)
    • O’Maille, P.E., M. Bakhtina, and M.D. Tsai. Structure-based combinatorial protein engineering (SCOPE). J. Mol. Biol., 321(4), 677-91, 2002.
    • (2002) J. Mol. Biol , vol.321 , Issue.4 , pp. 677-691
    • O'maille, P.E.1    Bakhtina, M.2    Tsai, M.D.3
  • 108
    • 0038799745 scopus 로고    scopus 로고
    • General method for sequence-independent site-directed chimeragen-esis
    • Hiraga, K. and F.H. Arnold. General method for sequence-independent site-directed chimeragen-esis. J. Mol. Biol., 330(2), 287-96, 2003.
    • (2003) J. Mol. Biol , vol.330 , Issue.2 , pp. 287-296
    • Hiraga, K.1    Arnold, F.H.2
  • 109
    • 0016324662 scopus 로고
    • A microplate method of enzyme-linked immunosorbent assay and its application to malaria
    • Voller, A., et al. A microplate method of enzyme-linked immunosorbent assay and its application to malaria. Bull World Health Organ., 51(2), 209-11, 1974.
    • (1974) Bull World Health Organ , vol.51 , Issue.2 , pp. 209-211
    • Voller, A.1
  • 110
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • Moore, J.C. and F.H. Arnold. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat. Biotechnol., 14(4), 458-67, 1996.
    • (1996) Nat. Biotechnol , vol.14 , Issue.4 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 111
    • 0033620595 scopus 로고    scopus 로고
    • In vitro selection of DNA aptamers to anthrax spores with electrochemiluminescence detection
    • Bruno, J.G. and J.L. Kiel. In vitro selection of DNA aptamers to anthrax spores with electrochemiluminescence detection. Biosens. Bioelectron., 14(5), 457-64, 1999.
    • (1999) Biosens. Bioelectron , vol.14 , Issue.5 , pp. 457-464
    • Bruno, J.G.1    Kiel, J.L.2
  • 112
    • 0024969084 scopus 로고
    • Scintillation proximity assay
    • Bosworth, N. and P. Towers. Scintillation proximity assay. Nature, 341(6238), 167-68, 1989.
    • (1989) Nature , vol.341 , Issue.6238 , pp. 167-168
    • Bosworth, N.1    Towers, P.2
  • 113
    • 0032880709 scopus 로고    scopus 로고
    • Homogeneous fluorescence readouts for miniaturized high-throughput screening: Theory and practice
    • Pope, A.J., U.M. Haupts, and K.J. Moore. Homogeneous fluorescence readouts for miniaturized high-throughput screening: Theory and practice. Drug Discovery Today, 4(8), 350-62, 1999.
    • (1999) Drug Discovery Today , vol.4 , Issue.8 , pp. 350-362
    • Pope, A.J.1    Haupts, U.M.2    Moore, K.J.3
  • 114
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., et al. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nature Biotechnol., 14(3), 315-19, 1996.
    • (1996) Nature Biotechnol , vol.14 , Issue.3 , pp. 315-319
    • Crameri, A.1
  • 115
    • 23944495081 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer as a probe of peptide cyclization catalyzed by nonribosomal thioesterase domains
    • Grunewald, J., et al. Fluorescence resonance energy transfer as a probe of peptide cyclization catalyzed by nonribosomal thioesterase domains. Chem. Biol., 12(8), 873-81, 2005.
    • (2005) Chem. Biol , vol.12 , Issue.8 , pp. 873-881
    • Grunewald, J.1
  • 116
    • 0033562573 scopus 로고    scopus 로고
    • Protein microarrays for gene expression and antibody screening
    • Lueking, A., et al. Protein microarrays for gene expression and antibody screening. Anal. Biochem., 270(1), 103-11, 1999.
    • (1999) Anal. Biochem , vol.270 , Issue.1 , pp. 103-111
    • Lueking, A.1
  • 117
    • 0034651008 scopus 로고    scopus 로고
    • UPA, a universal protein array system for quantitative detection of protein-protein, proteinDNA, protein-RNA and protein-ligand interactions
    • Ge, H. UPA, a universal protein array system for quantitative detection of protein-protein, proteinDNA, protein-RNA and protein-ligand interactions. Nucleic Acids Res., 28(2), e3, 2000.
    • (2000) Nucleic Acids Res , vol.28 , Issue.2
    • Ge, H.1
  • 118
    • 0034622925 scopus 로고    scopus 로고
    • Printing proteins as microarrays for high-throughput function determination
    • MacBeath, G. and S.L. Schreiber. Printing proteins as microarrays for high-throughput function determination. Science, 289(5485), 1760-63, 2000.
    • (2000) Science , vol.289 , Issue.5485 , pp. 1760-1763
    • Macbeath, G.1    Schreiber, S.L.2
  • 119
    • 0033199270 scopus 로고    scopus 로고
    • Array biosensor for simultaneous identification of bacterial, viral, and protein analytes
    • Rowe, C.A., et al. Array biosensor for simultaneous identification of bacterial, viral, and protein analytes. Anal. Chem., 71(17), 3846-52, 1999.
    • (1999) Anal. Chem , vol.71 , Issue.17 , pp. 3846-3852
    • Rowe, C.A.1
  • 120
    • 0034651571 scopus 로고    scopus 로고
    • Protein microchips: Use for immunoassay and enzymatic reactions
    • Arenkov, P., et al. Protein microchips: Use for immunoassay and enzymatic reactions. Anal. Biochem., 278(2), 123-31, 2000.
    • (2000) Anal. Biochem , vol.278 , Issue.2 , pp. 123-131
    • Arenkov, P.1
  • 121
    • 0034730034 scopus 로고    scopus 로고
    • Inaugural article: Immunoassays with rolling circle DNA amplification: A versatile platform for ultrasensitive antigen detection
    • Schweitzer, B., et al. Inaugural article: Immunoassays with rolling circle DNA amplification: A versatile platform for ultrasensitive antigen detection. Proc. Natl. Acad. Sci. uSA, 97(18), 10113-19, 2000.
    • (2000) Proc. Natl. Acad. Sci. Usa , vol.97 , Issue.18 , pp. 10113-10119
    • Schweitzer, B.1
  • 122
    • 0033768106 scopus 로고    scopus 로고
    • Analysis of yeast protein kinases using protein chips
    • Zhu, H., et al. Analysis of yeast protein kinases using protein chips. Nat. Genet., 26(3), 283-89, 2000.
    • (2000) Nat. Genet , vol.26 , Issue.3 , pp. 283-289
    • Zhu, H.1
  • 123
    • 25644459220 scopus 로고    scopus 로고
    • Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations
    • Tomatis, P.E., et al. Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations. Proc. Natl. Acad. Sci. uSA, 102(39), 13761-66, 2005.
    • (2005) Proc. Natl. Acad. Sci. Usa , vol.102 , Issue.39 , pp. 13761-13766
    • Tomatis, P.E.1
  • 124
    • 0033015460 scopus 로고    scopus 로고
    • Rapid protein-folding assay using green fluorescent protein
    • Waldo, G.S., et al. Rapid protein-folding assay using green fluorescent protein. Nature Biotechnol., 17(7), 691-95, 1999.
    • (1999) Nature Biotechnol , vol.17 , Issue.7 , pp. 691-695
    • Waldo, G.S.1
  • 125
    • 0347635518 scopus 로고    scopus 로고
    • Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization
    • Aharoni, A., et al. Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization. Proc. Natl. Acad. Sci. uSA, 101(2), 482-87, 2004.
    • (2004) Proc. Natl. Acad. Sci. Usa , vol.101 , Issue.2 , pp. 482-487
    • Aharoni, A.1
  • 126
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by directed evolution
    • van den Berg, S., et al. Improved solubility of TEV protease by directed evolution. J. Biotechnol., 121(3), 291-98, 2006.
    • (2006) J. Biotechnol , vol.121 , Issue.3 , pp. 291-298
    • Van Den Berg, S.1
  • 127
    • 0347130091 scopus 로고    scopus 로고
    • Growth of Escherichia coli coexpressing phosphotriesterase and glycero-phosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source
    • McLoughlin, S.Y., et al. Growth of Escherichia coli coexpressing phosphotriesterase and glycero-phosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source. Appl. Environ. Microbiol., 70(1), 404-12, 2004.
    • (2004) Appl. Environ. Microbiol , vol.70 , Issue.1 , pp. 404-412
    • McLoughlin, S.Y.1
  • 128
    • 0035464767 scopus 로고    scopus 로고
    • Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate
    • Sakamoto, T., et al. Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate. Appl. Environ. Microbiol., 67(9), 3882-87, 2001.
    • (2001) Appl. Environ. Microbiol , vol.67 , Issue.9 , pp. 3882-3887
    • Sakamoto, T.1
  • 129
    • 0032983270 scopus 로고    scopus 로고
    • Progress and variations in two-hybrid and three-hybrid technologies
    • Drees, B.L. Progress and variations in two-hybrid and three-hybrid technologies. Curr. Opin. Chem. Biol., 3(1), 64-70, 1999.
    • (1999) Curr. Opin. Chem. Biol , vol.3 , Issue.1 , pp. 64-70
    • Drees, B.L.1
  • 130
    • 0030272124 scopus 로고    scopus 로고
    • Genetic and biochemical probes for protein-protein interactions
    • McNabb, D.S. and L. Guarente. Genetic and biochemical probes for protein-protein interactions. Curr. Opin. Biotechnol., 7(5), 554-59, 1996.
    • (1996) Curr. Opin. Biotechnol , vol.7 , Issue.5 , pp. 554-559
    • McNabb, D.S.1    Guarente, L.2
  • 131
    • 0031568304 scopus 로고    scopus 로고
    • Two’s company, three’s a crowd: The yeast two hybrid system for mapping molecular interactions
    • Warbrick, E. Two’s company, three’s a crowd: The yeast two hybrid system for mapping molecular interactions. Structure, 5(1), 13-17, 1997.
    • (1997) Structure , vol.5 , Issue.1 , pp. 13-17
    • Warbrick, E.1
  • 132
    • 0030690331 scopus 로고    scopus 로고
    • Tag games in yeast: The two-hybrid system and beyond
    • Brachmann, R.K. and J.D. Boeke. Tag games in yeast: The two-hybrid system and beyond. Curr. Opin. Biotechnol., 8(5), 561-68, 1997.
    • (1997) Curr. Opin. Biotechnol , vol.8 , Issue.5 , pp. 561-568
    • Brachmann, R.K.1    Boeke, J.D.2
  • 133
    • 0033557224 scopus 로고    scopus 로고
    • Yeast forward and reverse ‘n’-hybrid systems
    • Vidal, M. and P. Legrain. Yeast forward and reverse ‘n’-hybrid systems. Nucleic Acids Res., 27(4), 919-29, 1999.
    • (1999) Nucleic Acids Res , vol.27 , Issue.4 , pp. 919-929
    • Vidal, M.1    Legrain, P.2
  • 134
    • 0032404491 scopus 로고    scopus 로고
    • The impact of two-hybrid and related methods on biotechnology
    • Colas, P. and R. Brent. The impact of two-hybrid and related methods on biotechnology. Trends Biotechnol., 16(8), 355-63, 1998.
    • (1998) Trends Biotechnol , vol.16 , Issue.8 , pp. 355-363
    • Colas, P.1    Brent, R.2
  • 135
    • 0035793658 scopus 로고    scopus 로고
    • Cornish
    • Lin, H. and V.W. Cornish. In vivo protein-protein interaction assays: Beyond proteins. Angew Chem. Int. Ed. Engl., 40(5), 871-75, 2001.
    • (2001) Angew Chem. Int. Ed. Engl , vol.40 , Issue.5 , pp. 871-875
    • Lin, H.1
  • 136
    • 0031854986 scopus 로고    scopus 로고
    • Man-made cell-like compartments for molecular evolution
    • Tawfik, D.S. and A.D. Griffiths. Man-made cell-like compartments for molecular evolution. Nat. Biotechnol., 16(7), 652-56, 1998.
    • (1998) Nat. Biotechnol , vol.16 , Issue.7 , pp. 652-656
    • Tawfik, D.S.1    Griffiths, A.D.2
  • 137
    • 0035836707 scopus 로고    scopus 로고
    • Directed evolution of polymerase function by compartmentalized self-replication
    • Ghadessy, F.J., J.L. Ong, and P. Holliger. Directed evolution of polymerase function by compartmentalized self-replication. Proc. Natl. Acad. Sci. uSA, 98(8), 4552-57, 2001.
    • (2001) Proc. Natl. Acad. Sci. Usa , vol.98 , Issue.8 , pp. 4552-4557
    • Ghadessy, F.J.1    Ong, J.L.2    Holliger, P.3
  • 138
    • 0842313326 scopus 로고    scopus 로고
    • Altering the sequence specificity of Haelll methyl-transferase by directed evolution using in vitro compartmentalization
    • Cohen, H.M., D.S. Tawfik, and A.D. Griffiths. Altering the sequence specificity of Haelll methyl-transferase by directed evolution using in vitro compartmentalization. Protein Eng. Des. Sel., 17(1), 3-11, 2004.
    • (2004) Protein Eng. Des. Sel , vol.17 , Issue.1 , pp. 3-11
    • Cohen, H.M.1    Tawfik, D.S.2    Griffiths, A.D.3
  • 139
    • 11844273937 scopus 로고    scopus 로고
    • Directed evolution of protein inhibitors of DNA-nucleases by in vitro compartmentalization (IVC) and nano-droplet delivery
    • Bernath, K., S. Magdassi, and D.S. Tawfik. Directed evolution of protein inhibitors of DNA-nucleases by in vitro compartmentalization (IVC) and nano-droplet delivery. J. Mol. Biol., 345(5), 1015-26, 2005.
    • (2005) J. Mol. Biol , vol.345 , Issue.5 , pp. 1015-1026
    • Bernath, K.1    Magdassi, S.2    Tawfik, D.S.3
  • 140
    • 25844472658 scopus 로고    scopus 로고
    • Direct selection of trans-acting ligase ribozymes by in vitro compartmentalization
    • Levy, M., K.E. Griswold, and A.D. Ellington. Direct selection of trans-acting ligase ribozymes by in vitro compartmentalization. RNA, 11(10), 1555-62, 2005.
    • (2005) RNA , vol.11 , Issue.10 , pp. 1555-1562
    • Levy, M.1    Griswold, K.E.2    Ellington, A.D.3
  • 141
    • 27644566231 scopus 로고    scopus 로고
    • Cell-free selection of zinc finger DNA-binding proteins using in vitro compartmentalization
    • Sepp, A. and Y. Choo. Cell-free selection of zinc finger DNA-binding proteins using in vitro compartmentalization. J. Mol. Biol., 354(2), 212-19, 2005.
    • (2005) J. Mol. Biol , vol.354 , Issue.2 , pp. 212-219
    • Sepp, A.1    Choo, Y.2
  • 142
    • 0346982051 scopus 로고    scopus 로고
    • Phage Display
    • Smith, G.P. and V.A. Petrenko. Phage Display. Chem. Rev., 97(2), 391-410, 1997.
    • (1997) Chem. Rev , vol.97 , Issue.2 , pp. 391-410
    • Smith, G.P.1    Petrenko, V.A.2
  • 143
    • 0033638492 scopus 로고    scopus 로고
    • Phage display in pharmaceutical biotechnology
    • Sidhu, S.S. Phage display in pharmaceutical biotechnology. Curr. Opin. Biotechnol., 11(6), 610-16, 2000.
    • (2000) Curr. Opin. Biotechnol , vol.11 , Issue.6 , pp. 610-616
    • Sidhu, S.S.1
  • 144
    • 0032901290 scopus 로고    scopus 로고
    • Phage-display technology—finding a needle in a vast molecular haystack
    • Rodi, D.J. and L. Makowski. Phage-display technology—finding a needle in a vast molecular haystack. Curr. Opin. Biotechnol., 10(1), 87-93, 1999.
    • (1999) Curr. Opin. Biotechnol , vol.10 , Issue.1 , pp. 87-93
    • Rodi, D.J.1    Makowski, L.2
  • 145
    • 0033178525 scopus 로고    scopus 로고
    • Beyond binding: Using phage display to select for structure, folding and enzymatic activity in proteins
    • Forrer, P., S. Jung, and A. Pluckthun. Beyond binding: Using phage display to select for structure, folding and enzymatic activity in proteins. Curr. Opin. Struct. Biol., 9(4), 514-20, 1999.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , Issue.4 , pp. 514-520
    • Forrer, P.1    Jung, S.2    Pluckthun, A.3
  • 146
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith, G.P. Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science, 228(4705), 1315-17, 1985.
    • (1985) Science , vol.228 , Issue.4705 , pp. 1315-1317
    • Smith, G.P.1
  • 147
    • 0033987925 scopus 로고    scopus 로고
    • Exploiting recombination in single bacteria to make large phage antibody libraries
    • Sblattero, D. and A. Bradbury. Exploiting recombination in single bacteria to make large phage antibody libraries. Nat. Biotechnol., 18(1), 75-80, 2000.
    • (2000) Nat. Biotechnol , vol.18 , Issue.1 , pp. 75-80
    • Sblattero, D.1    Bradbury, A.2
  • 148
    • 0024780688 scopus 로고
    • Filamentous fusion phage cloning vectors for the study of epitopes and design of vaccines
    • Parmley, S.F. and G.P. Smith. Filamentous fusion phage cloning vectors for the study of epitopes and design of vaccines. Adv. Exp. Med. Biol., 251, 215-18, 1989.
    • (1989) Adv. Exp. Med. Biol , vol.251 , pp. 215-218
    • Parmley, S.F.1    Smith, G.P.2
  • 149
    • 0027723182 scopus 로고
    • Display of biologically active proteins on the surface of filamentous phages: A cDNA cloning system for selection of functional gene products linked to the genetic information responsible for their production
    • Crameri, R. and M. Suter. Display of biologically active proteins on the surface of filamentous phages: A cDNA cloning system for selection of functional gene products linked to the genetic information responsible for their production. Gene, 137(1), 69-75, 1993.
    • (1993) Gene , vol.137 , Issue.1 , pp. 69-75
    • Crameri, R.1    Suter, M.2
  • 150
    • 0036976219 scopus 로고    scopus 로고
    • A cell-penetrating peptide from a novel pVII-plX phage-displayed random peptide library
    • Gao, C., et al. A cell-penetrating peptide from a novel pVII-plX phage-displayed random peptide library. Bioorg. Med. Chem., 10(12), 4057-65, 2002.
    • (2002) Bioorg. Med. Chem , vol.10 , Issue.12 , pp. 4057-4065
    • Gao, C.1
  • 151
    • 29144523028 scopus 로고    scopus 로고
    • Multivalent display system on filamentous bacteriophage pVII minor coat protein
    • Kwasnikowski, P., P. Kristensen, and W.T. Markiewicz. Multivalent display system on filamentous bacteriophage pVII minor coat protein. J. Immunol. Methods, 307(1-2), 135-43, 2005.
    • (2005) J. Immunol. Methods , vol.307 , Issue.1-2 , pp. 135-143
    • Kwasnikowski, P.1    Kristensen, P.2    Markiewicz, W.T.3
  • 152
    • 24144498674 scopus 로고    scopus 로고
    • Screening for PreS specific binding ligands with a phage displayed peptides library
    • Deng, Q., et al. Screening for PreS specific binding ligands with a phage displayed peptides library. World J. Gastroenterol., 11(26), 4018-23, 2005.
    • (2005) World J. Gastroenterol , vol.11 , Issue.26 , pp. 4018-4023
    • Deng, Q.1
  • 153
    • 0036792077 scopus 로고    scopus 로고
    • A method for the generation of combinatorial antibody libraries using pIX phage display
    • Gao, C., et al. A method for the generation of combinatorial antibody libraries using pIX phage display. Proc. Natl. Acad. Sci. uSA, 99(20), 12612-16, 2002.
    • (2002) Proc. Natl. Acad. Sci. Usa , vol.99 , Issue.20 , pp. 12612-12616
    • Gao, C.1
  • 154
    • 0033853776 scopus 로고    scopus 로고
    • Natural and designer binding sites made by phage display technology
    • Hoogenboom, H.R. and P. Chames. Natural and designer binding sites made by phage display technology. Immunol. Today, 21(8), 371-8, 2000.
    • (2000) Immunol. Today , vol.21 , Issue.8 , pp. 371-378
    • Hoogenboom, H.R.1    Chames, P.2
  • 156
    • 13144283684 scopus 로고    scopus 로고
    • A glycosidase antibody elicited against a chair-like transition state analog by in vitro immunization
    • Yu, J., et al. A glycosidase antibody elicited against a chair-like transition state analog by in vitro immunization. Proc. Natl. Acad. Sci. uSA, 95(6), 2880-84, 1998.
    • (1998) Proc. Natl. Acad. Sci. Usa , vol.95 , Issue.6 , pp. 2880-2884
    • Yu, J.1
  • 157
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
    • Baca, M., et al. Phage display of a catalytic antibody to optimize affinity for transition-state analog binding. Proc. Natl. Acad. Sci. uSA, 94(19), 10063-68, 1997.
    • (1997) Proc. Natl. Acad. Sci. Usa , vol.94 , Issue.19 , pp. 10063-10068
    • Baca, M.1
  • 158
    • 0031037466 scopus 로고    scopus 로고
    • Chemical selection for catalysis in combinatorial antibody libraries
    • Janda, K.D., et al. Chemical selection for catalysis in combinatorial antibody libraries. Science, 275(5302), 945-48, 1997.
    • (1997) Science , vol.275 , Issue.5302 , pp. 945-948
    • Janda, K.D.1
  • 159
    • 0027994717 scopus 로고
    • Toward a code for the interactions of zinc fingers with DNA: Selection of randomized fingers displayed on phage
    • Choo, Y. and A. Klug. Toward a code for the interactions of zinc fingers with DNA: Selection of randomized fingers displayed on phage. Proc. Natl. Acad. Sci. uSA, 91(23), 11163-67, 1994.
    • (1994) Proc. Natl. Acad. Sci. Usa , vol.91 , Issue.23 , pp. 11163-11167
    • Choo, Y.1    Klug, A.2
  • 160
    • 0028227930 scopus 로고
    • Wells
    • Jamieson, A.C., S.H. Kim, and J.A. Wells. In vitro selection of zinc fingers with altered DNA-binding specificity. Biochemistry, 33(19), 5689-95, 1994.
    • (1994) Biochemistry , vol.33 , Issue.19 , pp. 5689-5695
    • Jamieson, A.C.1    Kim, S.H.2
  • 161
    • 0028328872 scopus 로고
    • Zinc finger phage: Affinity selection of fingers with new DNA-binding specificities
    • Rebar, E.J. and C.O. Pabo. Zinc finger phage: Affinity selection of fingers with new DNA-binding specificities. Science, 263(5147), 671-73, 1994.
    • (1994) Science , vol.263 , Issue.5147 , pp. 671-673
    • Rebar, E.J.1    Pabo, C.O.2
  • 162
    • 0033515005 scopus 로고    scopus 로고
    • Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold
    • Beste, G., et al. Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc. Natl. Acad. Sci. uSA, 96(5), 1898-903, 1999.
    • (1999) Proc. Natl. Acad. Sci. Usa , vol.96 , Issue.5 , pp. 1898-1903
    • Beste, G.1
  • 163
    • 0034646561 scopus 로고    scopus 로고
    • A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin
    • Schlehuber, S., G. Beste, and A. Skerra. A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin. J. Mol. Biol., 297(5), 1105-20, 2000.
    • (2000) J. Mol. Biol , vol.297 , Issue.5 , pp. 1105-1120
    • Schlehuber, S.1    Beste, G.2    Skerra, A.3
  • 164
    • 0028175483 scopus 로고
    • Selection of beta-lactamase on filamentous bacteriophage by catalytic activity
    • Soumillion, P., et al. Selection of beta-lactamase on filamentous bacteriophage by catalytic activity. J. Mol. Biol., 237(4), 415-22, 1994.
    • (1994) J. Mol. Biol , vol.237 , Issue.4 , pp. 415-422
    • Soumillion, P.1
  • 165
    • 0033582608 scopus 로고    scopus 로고
    • A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage
    • Demartis, S., et al. A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage. J. Mol. Biol., 286(2), 617-33, 1999.
    • (1999) J. Mol. Biol , vol.286 , Issue.2 , pp. 617-633
    • Demartis, S.1
  • 166
    • 0032168985 scopus 로고    scopus 로고
    • A method for directed evolution and functional cloning of enzymes
    • Pedersen, H., et al. A method for directed evolution and functional cloning of enzymes. Proc. Natl. Acad. Sci. uSA, 95(18), 10523-28, 1998.
    • (1998) Proc. Natl. Acad. Sci. Usa , vol.95 , Issue.18 , pp. 10523-10528
    • Pedersen, H.1
  • 167
    • 0033578390 scopus 로고    scopus 로고
    • Selection for improved subtiligases by phage display
    • Atwell, S. and J.A. Wells. Selection for improved subtiligases by phage display. Proc. Natl. Acad. Sci. uSA, 96(17), 9497-502, 1999.
    • (1999) Proc. Natl. Acad. Sci. Usa , vol.96 , Issue.17 , pp. 9497-9502
    • Atwell, S.1    Wells, J.A.2
  • 168
    • 0035795425 scopus 로고    scopus 로고
    • Selection of metalloenzymes by catalytic activity using phage display and catalytic elution
    • Ponsard, I., et al. Selection of metalloenzymes by catalytic activity using phage display and catalytic elution. Chembiochem, 2(4), 253-59, 2001.
    • (2001) Chembiochem , vol.2 , Issue.4 , pp. 253-259
    • Ponsard, I.1
  • 169
    • 0026594374 scopus 로고
    • Transport and anchoring of beta-lactamase to the external surface of Escherichia coli
    • Francisco, J.A., C.F. Earhart, and G. Georgiou. Transport and anchoring of beta-lactamase to the external surface of Escherichia coli. Proc. Natl. Acad. Sci. uSA, 89(7), 2713-17, 1992.
    • (1992) Proc. Natl. Acad. Sci. Usa , vol.89 , Issue.7 , pp. 2713-2717
    • Francisco, J.A.1    Earhart, C.F.2    Georgiou, G.3
  • 170
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder, E.T. and K.D. Wittrup. Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol., 15(6), 553-57, 1997.
    • (1997) Nat. Biotechnol , vol.15 , Issue.6 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 171
    • 0032052263 scopus 로고    scopus 로고
    • Baculovirus surface display: Construction and screening of a eukaryotic epitope library
    • Ernst, W., et al. Baculovirus surface display: Construction and screening of a eukaryotic epitope library. Nucleic Acids Res., 26(7), 1718-23, 1998.
    • (1998) Nucleic Acids Res , vol.26 , Issue.7 , pp. 1718-1723
    • Ernst, W.1
  • 172
    • 0032824531 scopus 로고    scopus 로고
    • The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides
    • Christmann, A., et al. The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides. Protein Eng., 12(9), 797-806, 1999.
    • (1999) Protein Eng , vol.12 , Issue.9 , pp. 797-806
    • Christmann, A.1
  • 173
    • 0031663081 scopus 로고    scopus 로고
    • Antibody affinity maturation using bacterial surface display
    • Daugherty, P.S., et al. Antibody affinity maturation using bacterial surface display. Protein Eng., 11(9), 825-32, 1998.
    • (1998) Protein Eng , vol.11 , Issue.9 , pp. 825-832
    • Daugherty, P.S.1
  • 174
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder, E.T., K.S. Midelfort, and K.D. Wittrup. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc. Natl. Acad. Sci. uSA, 97(20), 10701-5, 2000.
    • (2000) Proc. Natl. Acad. Sci. Usa , vol.97 , Issue.20 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 175
    • 0033545862 scopus 로고    scopus 로고
    • Selection of functional T cell receptor mutants from a yeast surface-display library
    • Kieke, M.C., et al. Selection of functional T cell receptor mutants from a yeast surface-display library. Proc. Natl. Acad. Sci. uSA, 96(10), 5651-56, 1999.
    • (1999) Proc. Natl. Acad. Sci. Usa , vol.96 , Issue.10 , pp. 5651-5656
    • Kieke, M.C.1
  • 176
    • 0033772183 scopus 로고    scopus 로고
    • Function-based isolation of novel enzymes from a large library
    • Olsen, M.J., et al. Function-based isolation of novel enzymes from a large library. Nat. Biotechnol., 18(10), 1071-74, 2000.
    • (2000) Nat. Biotechnol , vol.18 , Issue.10 , pp. 1071-1074
    • Olsen, M.J.1
  • 177
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis, L.C., R.R. Bhatt, and W.J. Dower. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc. Natl. Acad. Sci. uSA, 91(19), 9022-26, 1994.
    • (1994) Proc. Natl. Acad. Sci. Usa , vol.91 , Issue.19 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 178
    • 0030974119 scopus 로고    scopus 로고
    • Pluckthun
    • Hanes, J. and A. Pluckthun. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. uSA, 94(10), 4937-42, 1997.
    • (1997) Proc. Natl. Acad. Sci. Usa , vol.94 , Issue.10 , pp. 4937-4942
    • Hanes, J.1
  • 179
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts, R.W. and J.W. Szostak. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. uSA, 94(23), 12297-302, 1997.
    • (1997) Proc. Natl. Acad. Sci. Usa , vol.94 , Issue.23 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 180
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: Bonding of mRNA bearing puromycin at the 3’-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
    • Nemoto, N., et al. In vitro virus: Bonding of mRNA bearing puromycin at the 3’-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro. FEBS Lett., 414(2), 405-8, 1997.
    • (1997) FEBS Lett , vol.414 , Issue.2 , pp. 405-408
    • Nemoto, N.1
  • 181
    • 0026546880 scopus 로고
    • Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor
    • Cull, M.G., J.F. Miller, and PJ. Schatz. Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor. Proc. Natl. Acad. Sci. uSA, 89(5), 1865-69, 1992.
    • (1992) Proc. Natl. Acad. Sci. Usa , vol.89 , Issue.5 , pp. 1865-1869
    • Cull, M.G.1    Miller, J.F.2    Schatz, P.J.3
  • 182
    • 23044501802 scopus 로고    scopus 로고
    • Evolving strategies for enzyme engineering
    • Bloom, J.D., et al. Evolving strategies for enzyme engineering. Curr. Opin. Struct. Biol., 15(4), 447-52, 2005.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , Issue.4 , pp. 447-452
    • Bloom, J.D.1
  • 183
    • 20444368826 scopus 로고    scopus 로고
    • Laboratory evolution of catabolic enzymes and pathways
    • Parales, R.E. and J.L. Ditty. Laboratory evolution of catabolic enzymes and pathways. Curr. Opin. Biotechnol., 16(3), 315-25, 2005.
    • (2005) Curr. Opin. Biotechnol , vol.16 , Issue.3 , pp. 315-325
    • Parales, R.E.1    Ditty, J.L.2
  • 184
    • 18044398220 scopus 로고    scopus 로고
    • Directed evolution of biocatalytic processes
    • Hibbert, E.G., et al. Directed evolution of biocatalytic processes. Biomol. Eng., 22(1-3), 11-19, 2005.
    • (2005) Biomol. Eng , vol.22 , Issue.1-3 , pp. 11-19
    • Hibbert, E.G.1
  • 185
    • 23444450226 scopus 로고    scopus 로고
    • Semi-rational approaches to engineering enzyme activity: Combining the benefits of directed evolution and rational design
    • Chica, R.A., N. Doucet, and J.N. Pelletier. Semi-rational approaches to engineering enzyme activity: Combining the benefits of directed evolution and rational design. Curr. Opin. Biotechnol., 16(4), 378-84, 2005.
    • (2005) Curr. Opin. Biotechnol , vol.16 , Issue.4 , pp. 378-384
    • Chica, R.A.1    Doucet, N.2    Pelletier, J.N.3
  • 186
    • 0035813878 scopus 로고    scopus 로고
    • Directed evolution and biocatalysis
    • Powell, K.A., et al. Directed evolution and biocatalysis. Angew Chem. Int. Ed. Engl., 40(21), 3948-59, 2001.
    • (2001) Angew Chem. Int. Ed. Engl , vol.40 , Issue.21 , pp. 3948-3959
    • Powell, K.A.1
  • 187
    • 18044390504 scopus 로고    scopus 로고
    • Directed evolution: Selecting today’s biocatalysts
    • Otten, L.G. and W.J. Quax. Directed evolution: Selecting today’s biocatalysts. Biomol. Eng., 22(1-3), 1-9, 2005.
    • (2005) Biomol. Eng , vol.22 , Issue.1-3 , pp. 1-9
    • Otten, L.G.1    Quax, W.J.2
  • 188
    • 33645781503 scopus 로고    scopus 로고
    • Directed evolution strategies for improved enzymatic performance
    • Hibbert, E.G. and P.A. Dalby. Directed evolution strategies for improved enzymatic performance. Microb. Cell. Fact, 4, 1-6, 2005.
    • (2005) Microb. Cell. Fact , vol.4 , pp. 1-6
    • Hibbert, E.G.1    Dalby, P.A.2
  • 189
    • 12144282243 scopus 로고    scopus 로고
    • Directed evolution of enzymes for biocatalysis and the life sciences
    • Williams, G.J., A.S. Nelson, and A. Berry. Directed evolution of enzymes for biocatalysis and the life sciences. Cell. Mol. Life Sci., 61(24), 3034-46, 2004.
    • (2004) Cell. Mol. Life Sci , vol.61 , Issue.24 , pp. 3034-3046
    • Williams, G.J.1    Nelson, A.S.2    Berry, A.3
  • 190
    • 25844525807 scopus 로고    scopus 로고
    • Improving the catalytic activity of Candida antarctica lipase B by circular permutation
    • Qian, Z. and S. Lutz. Improving the catalytic activity of Candida antarctica lipase B by circular permutation. J. Am. Chem. Soc., 127(39), 13466-67, 2005.
    • (2005) J. Am. Chem. Soc , vol.127 , Issue.39 , pp. 13466-13467
    • Qian, Z.1    Lutz, S.2
  • 191
    • 2442668927 scopus 로고    scopus 로고
    • Discovery and directed evolution of a glyphosate tolerance gene
    • Castle, L.A., et al. Discovery and directed evolution of a glyphosate tolerance gene. Science, 304(5674), 1151-54, 2004.
    • (2004) Science , vol.304 , Issue.5674 , pp. 1151-1154
    • Castle, L.A.1
  • 192
    • 0033768504 scopus 로고    scopus 로고
    • Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars
    • Fong, S., et al. Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars. Chem. Biol., 7(11), 873-83, 2000.
    • (2000) Chem. Biol , vol.7 , Issue.11 , pp. 873-883
    • Fong, S.1
  • 193
    • 4143066086 scopus 로고    scopus 로고
    • Altering the substrate specificity of organophospho-rus hydrolase for enhanced hydrolysis of chlorpyrifos
    • Cho, C.M., A. Mulchandani, and W. Chen. Altering the substrate specificity of organophospho-rus hydrolase for enhanced hydrolysis of chlorpyrifos. Appl. Environ. Microbiol., 70(8), 4681-85, 2004.
    • (2004) Appl. Environ. Microbiol , vol.70 , Issue.8 , pp. 4681-4685
    • Cho, C.M.1    Mulchandani, A.2    Chen, W.3
  • 194
    • 0034833072 scopus 로고    scopus 로고
    • Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes
    • Raillard, S., et al. Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes. Chem. Biol., 8(9), 891-98, 2001.
    • (2001) Chem. Biol , vol.8 , Issue.9 , pp. 891-898
    • Raillard, S.1
  • 195
    • 0037452525 scopus 로고    scopus 로고
    • Altering substrate specificity of phosphatidylcholine-preferring phospholipase C of Bacillus cereus by random mutagenesis of the headgroup binding site
    • Antikainen, N.M., et al. Altering substrate specificity of phosphatidylcholine-preferring phospholipase C of Bacillus cereus by random mutagenesis of the headgroup binding site. Biochemistry, 42(6), 1603-10, 2003.
    • (2003) Biochemistry , vol.42 , Issue.6 , pp. 1603-1610
    • Antikainen, N.M.1
  • 196
    • 1342310509 scopus 로고    scopus 로고
    • Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase
    • Rothman, S.C., M. Voorhies, and J.F. Kirsch. Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase. Protein Sci., 13(3), 763-72, 2004.
    • (2004) Protein Sci , vol.13 , Issue.3 , pp. 763-772
    • Rothman, S.C.1    Voorhies, M.2    Kirsch, J.F.3
  • 197
    • 0029079958 scopus 로고
    • Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis
    • Onuffer, J.J. and J.F. Kirsch. Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis. Protein Sci., 4(9), 1750-57, 1995.
    • (1995) Protein Sci , vol.4 , Issue.9 , pp. 1750-1757
    • Onuffer, J.J.1    Kirsch, J.F.2
  • 198
    • 0036787635 scopus 로고    scopus 로고
    • An efficient system for the evolution of aminoacyl-tRNA synthetase specificity
    • Santoro, S.W., et al. An efficient system for the evolution of aminoacyl-tRNA synthetase specificity. Nat. Biotechnol., 20(10), 1044-48, 2002.
    • (2002) Nat. Biotechnol , vol.20 , Issue.10 , pp. 1044-1048
    • Santoro, S.W.1
  • 199
    • 3342911436 scopus 로고    scopus 로고
    • Directed evolution of epoxide hydrolase from A. Radiobacter toward higher enanti-oselectivity by error-prone PCR and DNA shuffling
    • van Loo, B., et al. Directed evolution of epoxide hydrolase from A. radiobacter toward higher enanti-oselectivity by error-prone PCR and DNA shuffling. Chem. Biol., 11(7), 981-90, 2004.
    • (2004) Chem. Biol , vol.11 , Issue.7 , pp. 981-990
    • Van Loo, B.1
  • 200
    • 26844523510 scopus 로고    scopus 로고
    • Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration
    • Johannes, T.W., R.D. Woodyer, and H. Zhao. Directed evolution of a thermostable phosphite dehydrogenase for NAD(P)H regeneration. Appl. Environ. Microbiol., 71(10), 5728-34, 2005.
    • (2005) Appl. Environ. Microbiol , vol.71 , Issue.10 , pp. 5728-5734
    • Johannes, T.W.1    Woodyer, R.D.2    Zhao, H.3
  • 201
    • 0032573217 scopus 로고    scopus 로고
    • Directed evolution of a thermostable esterase
    • Giver, L., et al. Directed evolution of a thermostable esterase. Proc. Natl. Acad. Sci. uSA, 95(22), 12809-13, 1998.
    • (1998) Proc. Natl. Acad. Sci. Usa , vol.95 , Issue.22 , pp. 12809-12813
    • Giver, L.1
  • 202
    • 0142215371 scopus 로고    scopus 로고
    • Directed evolution of Thermotoga neapolitana xylose isomerase: High activity on glucose at low temperature and low pH
    • Sriprapundh, D., C. Vieille, and J.G. Zeikus. Directed evolution of Thermotoga neapolitana xylose isomerase: High activity on glucose at low temperature and low pH. Protein Eng., 16(9), 683-90, 2003.
    • (2003) Protein Eng , vol.16 , Issue.9 , pp. 683-690
    • Sriprapundh, D.1    Vieille, C.2    Zeikus, J.G.3
  • 203
    • 18044366809 scopus 로고    scopus 로고
    • A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents
    • Hao, J. and A. Berry. A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents. Protein Eng. Des. Sel., 17(9), 689-97, 2004.
    • (2004) Protein Eng. Des. Sel , vol.17 , Issue.9 , pp. 689-697
    • Hao, J.1    Berry, A.2
  • 204
    • 0032885231 scopus 로고    scopus 로고
    • DNA shuffling of subgenomic sequences of subtilisin
    • Ness, J.E., et al. DNA shuffling of subgenomic sequences of subtilisin. Nat. Biotechnol., 17(9), 893-96, 1999.
    • (1999) Nat. Biotechnol , vol.17 , Issue.9 , pp. 893-896
    • Ness, J.E.1
  • 205
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D.P., et al. Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J. Biol. Chem., 264(33), 19659-65, 1989.
    • (1989) J. Biol. Chem , vol.264 , Issue.33 , pp. 19659-19665
    • Dumas, D.P.1
  • 206
    • 17144364646 scopus 로고    scopus 로고
    • Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state
    • Roodveldt, C. and D.S. Tawfik. Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state. Protein Eng. Des. Sel., 18(1), 51-58, 2005.
    • (2005) Protein Eng. Des. Sel , vol.18 , Issue.1 , pp. 51-58
    • Roodveldt, C.1    Tawfik, D.S.2
  • 207
    • 0037458084 scopus 로고    scopus 로고
    • Optimization of protein therapeutics by directed evolution
    • Vasserot, A.P., et al. Optimization of protein therapeutics by directed evolution. Drug Discov. Today, 8(3), 118-26, 2003.
    • (2003) Drug Discov. Today , vol.8 , Issue.3 , pp. 118-126
    • Vasserot, A.P.1
  • 208
    • 0035424404 scopus 로고    scopus 로고
    • Advances in directed protein evolution by recursive genetic recombination: Applications to therapeutic proteins
    • Kurtzman, A.L., et al. Advances in directed protein evolution by recursive genetic recombination: Applications to therapeutic proteins. Curr Opin Biotechnol, 12(4), 361-70, 2001.
    • (2001) Curr Opin Biotechnol , vol.12 , Issue.4 , pp. 361-370
    • Kurtzman, A.L.1
  • 209
    • 3242713239 scopus 로고    scopus 로고
    • In vitro evolution of proteins for drug development
    • Delagrave, S. and D.J. Murphy. In vitro evolution of proteins for drug development. Assay Drug Dev. Technol., 1(1 Pt 2), 187-98, 2003.
    • (2003) Assay Drug Dev. Technol , vol.1 , Issue.1 , pp. 187-198
    • Delagrave, S.1    Murphy, D.J.2
  • 210
    • 0036845827 scopus 로고    scopus 로고
    • DNA shuffling: Induced molecular breeding to produce new generation long-lasting vaccines
    • Marshall, S.H. DNA shuffling: Induced molecular breeding to produce new generation long-lasting vaccines. Biotechnol. Adv., 20(3-4), 229-38, 2002.
    • (2002) Biotechnol. Adv , vol.20 , Issue.3-4 , pp. 229-238
    • Marshall, S.H.1
  • 211
    • 0041931084 scopus 로고    scopus 로고
    • The enzyme as drug: Application of enzymes as pharmaceuticals
    • Vellard, M. The enzyme as drug: Application of enzymes as pharmaceuticals. Curr. Opin. Biotechnol., 14(4), 444-450, 2003.
    • (2003) Curr. Opin. Biotechnol , vol.14 , Issue.4 , pp. 444-450
    • Vellard, M.1
  • 212
    • 0030722164 scopus 로고    scopus 로고
    • Applications of DNA shuffling to pharmaceuticals and vaccines
    • Patten, P.A., R.J. Howard, and W.P. Stemmer. Applications of DNA shuffling to pharmaceuticals and vaccines. Curr. Opin. Biotechnol., 8(6), 724-33, 1997.
    • (1997) Curr. Opin. Biotechnol , vol.8 , Issue.6 , pp. 724-733
    • Patten, P.A.1    Howard, R.J.2    Stemmer, W.P.3
  • 213
    • 0032496168 scopus 로고    scopus 로고
    • Selection of heregulin variants having higher affinity for the ErbB3 receptor by monovalent phage display
    • Ballinger, M.D., et al. Selection of heregulin variants having higher affinity for the ErbB3 receptor by monovalent phage display. J. Biol. Chem., 273(19), 11675-84, 1998.
    • (1998) J. Biol. Chem , vol.273 , Issue.19 , pp. 11675-11684
    • Ballinger, M.D.1
  • 214
    • 0036123295 scopus 로고    scopus 로고
    • Enhancing the anticoagulant potency of soluble tissue factor mutants by increasing their affinity to factor Vila
    • Yang, J.H., et al. Enhancing the anticoagulant potency of soluble tissue factor mutants by increasing their affinity to factor Vila. Thrombosis and Haemostasis, 87(3), 450-58, 2002.
    • (2002) Thrombosis and Haemostasis , vol.87 , Issue.3 , pp. 450-458
    • Yang, J.H.1
  • 215
    • 0032568558 scopus 로고    scopus 로고
    • Stepwise in vitro affinity maturation of Vitaxin, an alpha(V)beta(3)-specific humanized mAb
    • Wu, H.R., et al. Stepwise in vitro affinity maturation of Vitaxin, an alpha(v)beta(3)-specific humanized mAb. Proc. Natl. Acad. Sci. uSA, 95(11), 6037-42, 1998.
    • (1998) Proc. Natl. Acad. Sci. Usa , vol.95 , Issue.11 , pp. 6037-6042
    • Wu, H.R.1
  • 216
    • 0344573809 scopus 로고    scopus 로고
    • Growth hormone binding affinity for its receptor surpasses the requirements for cellular activity
    • Pearce, K.H., Jr., et al. Growth hormone binding affinity for its receptor surpasses the requirements for cellular activity. Biochemistry, 38(1), 81-89, 1999.
    • (1999) Biochemistry , vol.38 , Issue.1 , pp. 81-89
    • Pearce, K.H.1
  • 217
    • 0033664270 scopus 로고    scopus 로고
    • Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display
    • Hanes, J., et al. Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display. Nat. Biotechnol., 18(12), 1287-92, 2000.
    • (2000) Nat. Biotechnol , vol.18 , Issue.12 , pp. 1287-1292
    • Hanes, J.1
  • 218
    • 0029833999 scopus 로고    scopus 로고
    • The biologic activity and molecular characterization of a novel synthetic interferon-alpha species, consensus interferon
    • Blatt, L.M., et al. The biologic activity and molecular characterization of a novel synthetic interferon-alpha species, consensus interferon. J. Interferon Cytokine Res., 16(7), 489-99, 1996.
    • (1996) J. Interferon Cytokine Res , vol.16 , Issue.7 , pp. 489-499
    • Blatt, L.M.1
  • 219
    • 0032866310 scopus 로고    scopus 로고
    • Evolution of a cytokine using DNA family shuffling
    • Chang, C.C.J., et al. Evolution of a cytokine using DNA family shuffling. Nat. Biotechnol., 17(8), 793-97, 1999.
    • (1999) Nat. Biotechnol , vol.17 , Issue.8 , pp. 793-797
    • Chang, C.C.J.1
  • 220
    • 33644870699 scopus 로고    scopus 로고
    • New enzyme for reductive cancer chemotherapy, YieF, and its improvement by directed evolution
    • Barak, Y., et al. New enzyme for reductive cancer chemotherapy, YieF, and its improvement by directed evolution. Mol. Cancer Ther., 5(1), 97-103, 2006.
    • (2006) Mol. Cancer Ther , vol.5 , Issue.1 , pp. 97-103
    • Barak, Y.1
  • 221
    • 0034426015 scopus 로고    scopus 로고
    • Molecular breeding of viruses
    • Soong, N.W., et al. Molecular breeding of viruses. Nat. Genet., 25(4), 436-39, 2000.
    • (2000) Nat. Genet , vol.25 , Issue.4 , pp. 436-439
    • Soong, N.W.1
  • 222
    • 0033675531 scopus 로고    scopus 로고
    • Breeding of retroviruses by DNA shuffling for improved stability and processing yields
    • Powell, S.K., et al. Breeding of retroviruses by DNA shuffling for improved stability and processing yields. Nat. Biotechnol., 18(12), 1279-82, 2000.
    • (2000) Nat. Biotechnol , vol.18 , Issue.12 , pp. 1279-1282
    • Powell, S.K.1
  • 223
    • 32344438754 scopus 로고    scopus 로고
    • Directed evolution of adeno-associated virus yields enhanced gene delivery vectors
    • Maheshri, N., et al. Directed evolution of adeno-associated virus yields enhanced gene delivery vectors. Nat. Biotechnol., 24(2), 198-204, 2006.
    • (2006) Nat. Biotechnol , vol.24 , Issue.2 , pp. 198-204
    • Maheshri, N.1
  • 224
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R.A. Enzyme recruitment in evolution of new function. Ann. Rev. Microbiol., 30, 409-25, 1976.
    • (1976) Ann. Rev. Microbiol , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 225
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • Copley, S.D. Enzymes with extra talents: Moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol., 7(2), 265-72, 2003.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , Issue.2 , pp. 265-272
    • Copley, S.D.1
  • 226
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution—a 60-year-old hypothesis revisited
    • James, L.C. and D.S. Tawfik. Conformational diversity and protein evolution—a 60-year-old hypothesis revisited. Trends Biochem. Sci., 28(7), 361-68, 2003.
    • (2003) Trends Biochem. Sci , vol.28 , Issue.7 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 227
    • 9744279773 scopus 로고    scopus 로고
    • Divergent evolution in the enolase superfamily: The interplay of mechanism and specificity
    • Gerlt, J.A., P.C. Babbitt, and I. Rayment. Divergent evolution in the enolase superfamily: The interplay of mechanism and specificity. Arch. Biochem. Biophys., 433(1), 59-70, 2005.
    • (2005) Arch. Biochem. Biophys , vol.433 , Issue.1 , pp. 59-70
    • Gerlt, J.A.1    Babbitt, P.C.2    Rayment, I.3
  • 228
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O’Brien, PJ. and D. Herschlag. Catalytic promiscuity and the evolution of new enzymatic activities. Chem. Biol., 6(4), R91-R105, 1999.
    • (1999) Chem. Biol , vol.6 , Issue.4 , pp. RR91-R105
    • O'brien, P.J.1    Herschlag, D.2
  • 229
    • 18044364063 scopus 로고    scopus 로고
    • Rapid creation of a novel protein function by in vitro coevolution
    • Chen, Z. and H. Zhao. Rapid creation of a novel protein function by in vitro coevolution. J. Mol. Biol., 348(5), 1273-82, 2005.
    • (2005) J. Mol. Biol , vol.348 , Issue.5 , pp. 1273-1282
    • Chen, Z.1    Zhao, H.2
  • 230
    • 33646178621 scopus 로고    scopus 로고
    • Designed divergent evolution of enzyme function
    • Yoshikuni, Y., T.E. Ferrin, and J.D. Keasling. Designed divergent evolution of enzyme function. Nature, 440(7087), 1078-1082, 2006.
    • (2006) Nature , vol.440 , Issue.7087 , pp. 1078-1082
    • Yoshikuni, Y.1    Ferrin, T.E.2    Keasling, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.