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Volumn 32, Issue 4, 2004, Pages 1448-1459

Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: Library construction methods for directed evolution

Author keywords

[No Author keywords available]

Indexed keywords

DNA; OLIGONUCLEOTIDE; PROTEIN;

EID: 2542563521     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh315     Document Type: Review
Times cited : (237)

References (80)
  • 2
    • 0036940487 scopus 로고    scopus 로고
    • Towards the directed evolution of hybrid catalysts
    • Reetz,M.T., Rentzsch,M., Pletsch,A. and Maywald,M. (2002) Towards the directed evolution of hybrid catalysts. Chimia, 56, 721-723.
    • (2002) Chimia , vol.56 , pp. 721-723
    • Reetz, M.T.1    Rentzsch, M.2    Pletsch, A.3    Maywald, M.4
  • 3
    • 0035903602 scopus 로고    scopus 로고
    • Investigating and engineering enzymes by genetic selection
    • Taylor,S.V., Kast,P. and Hilvert,D. (2001) Investigating and engineering enzymes by genetic selection. Angew. Chem. Int. Ed. Engl., 40, 3310-3335.
    • (2001) Angew. Chem. Int. Ed. Engl. , vol.40 , pp. 3310-3335
    • Taylor, S.V.1    Kast, P.2    Hilvert, D.3
  • 4
    • 0037304389 scopus 로고    scopus 로고
    • Genetic screens and directed evolution for protein solubility
    • Waldo,G.S. (2003) Genetic screens and directed evolution for protein solubility. Curr. Opin. Chem. Biol., 7, 33-38.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 33-38
    • Waldo, G.S.1
  • 5
    • 0036897839 scopus 로고    scopus 로고
    • Milestones in directed enzyme evolution
    • Tao,H. and Cornish,V.W. (2002) Milestones in directed enzyme evolution. Curr. Opin. Chem. Biol., 6, 858-864.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 858-864
    • Tao, H.1    Cornish, V.W.2
  • 6
    • 0037011406 scopus 로고    scopus 로고
    • Screening and selection methods for large-scale analysis of protein function
    • Lin,H. and Cornish,V.W. (2002) Screening and selection methods for large-scale analysis of protein function. Angew. Chem. Int. Ed. Engl., 41, 4402-4425.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 4402-4425
    • Lin, H.1    Cornish, V.W.2
  • 9
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer,W.P.C. (1993) DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc. Natl Acad. Sci. USA, 91, 10747-10751.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 10
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer,W.P.C. (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature, 370, 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 11
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao,H., Giver,L., Shao,Z., Affholter,J. and Arnold,F. (1998) Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat. Biotechnol., 16, 258-261.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.4    Arnold, F.5
  • 12
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • Ostermeier,M., Shim,J.H. and Benkovic,S.J. (1999) A combinatorial approach to hybrid enzymes independent of DNA homology. Nat. Biotechnol., 17, 1205-1209.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.H.2    Benkovic, S.J.3
  • 13
    • 0032828603 scopus 로고    scopus 로고
    • Directed evolution of an esterase: Screening of enzyme libraries based on pH-indicators and a growth assay
    • Bornscheuer,U.T., Altenbuchner,J. and Meyer,H.H. (1999) Directed evolution of an esterase: screening of enzyme libraries based on pH-indicators and a growth assay. Bioorg. Med. Chem., 7, 2169-2173.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 2169-2173
    • Bornscheuer, U.T.1    Altenbuchner, J.2    Meyer, H.H.3
  • 15
    • 3042824797 scopus 로고    scopus 로고
    • Production of randomly mutated plasmid libraries using mutator strains
    • Nguyen,A.W. and Daugherty,P.S. (2003) Production of randomly mutated plasmid libraries using mutator strains. Methods Mol. Biol., 231, 39-44.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 39-44
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 17
    • 3042784274 scopus 로고    scopus 로고
    • Generating mutant libraries using error-prone PCR
    • Cirino,P.C., Mayer,K.M. and Umeno,D. (2003) Generating mutant libraries using error-prone PCR. Methods Mol. Biol., 231, 3-9.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 3-9
    • Cirino, P.C.1    Mayer, K.M.2    Umeno, D.3
  • 18
    • 0035846958 scopus 로고    scopus 로고
    • In vitro evolution of a beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates
    • Matsumura,I. and Ellington,A.D. (2001) In vitro evolution of a beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates. J. Mol. Biol., 305, 331-339.
    • (2001) J. Mol. Biol. , vol.305 , pp. 331-339
    • Matsumura, I.1    Ellington, A.D.2
  • 19
    • 0036656222 scopus 로고    scopus 로고
    • Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis
    • Lingen,B., Grotzinger,J., Kolter,D., Kula,M.R. and Pohl,M. (2002) Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis. Protein Eng., 15, 585-593.
    • (2002) Protein Eng. , vol.15 , pp. 585-593
    • Lingen, B.1    Grotzinger, J.2    Kolter, D.3    Kula, M.R.4    Pohl, M.5
  • 20
    • 0141858719 scopus 로고    scopus 로고
    • Directed evolution of a bacterial alpha-amylase: Toward enhanced pH-performance and higher specific activity
    • Bessler,C., Schmitt,J., Maurer,K.H. and Schmid,R.D. (2003) Directed evolution of a bacterial alpha-amylase: toward enhanced pH-performance and higher specific activity. Protein Sci., 12, 2141-2149.
    • (2003) Protein Sci. , vol.12 , pp. 2141-2149
    • Bessler, C.1    Schmitt, J.2    Maurer, K.H.3    Schmid, R.D.4
  • 21
    • 0029869449 scopus 로고    scopus 로고
    • An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues
    • Zaccolo,M., Williams,D.M., Brown,D.M. and Gheradi,E. (1996) An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues. J. Mol. Biol., 255, 589-603.
    • (1996) J. Mol. Biol. , vol.255 , pp. 589-603
    • Zaccolo, M.1    Williams, D.M.2    Brown, D.M.3    Gheradi, E.4
  • 22
    • 0033555718 scopus 로고    scopus 로고
    • The effect of high-frequency random mutagenesis on in vitro protein evolution: A study on TEM-1 β-lactamase
    • Zaccolo,M. and Gherardi,E. (1999) The effect of high-frequency random mutagenesis on in vitro protein evolution: a study on TEM-1 β-lactamase. J. Mol. Biol., 285, 775-783.
    • (1999) J. Mol. Biol. , vol.285 , pp. 775-783
    • Zaccolo, M.1    Gherardi, E.2
  • 23
    • 0041765676 scopus 로고    scopus 로고
    • User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries
    • Patrick,W.M., Firth,A.E. and Blackburn,J.M. (2003) User-friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries. Protein Eng., 16, 451-457.
    • (2003) Protein Eng. , vol.16 , pp. 451-457
    • Patrick, W.M.1    Firth, A.E.2    Blackburn, J.M.3
  • 24
    • 0041324888 scopus 로고    scopus 로고
    • A comparison of directed evolution approaches using the beta-glucuronidase model system
    • Rowe,L.A., Geddie,M.L., Alexander,O.B. and Matsumura,I. (2003) A comparison of directed evolution approaches using the beta-glucuronidase model system. J. Mol. Biol., 332, 851-860.
    • (2003) J. Mol. Biol. , vol.332 , pp. 851-860
    • Rowe, L.A.1    Geddie, M.L.2    Alexander, O.B.3    Matsumura, I.4
  • 25
    • 0033280672 scopus 로고    scopus 로고
    • Exploring nonnatural evolutionary pathways by saturation mutagenesis: Rapid improvement of protein function
    • Miyazaki,K. and Arnold,F.H. (1999) Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J. Mol. Evol., 49, 716-720.
    • (1999) J. Mol. Evol. , vol.49 , pp. 716-720
    • Miyazaki, K.1    Arnold, F.H.2
  • 26
    • 0036137462 scopus 로고    scopus 로고
    • Random insertion and deletion of arbitrary number of bases for codon-based random mutation of DNAs
    • Murakami,H., Hohsaka,T. and Sisido,M. (2002) Random insertion and deletion of arbitrary number of bases for codon-based random mutation of DNAs. Nat. Biotechnol., 20, 76-81.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 76-81
    • Murakami, H.1    Hohsaka, T.2    Sisido, M.3
  • 27
  • 28
    • 0034548711 scopus 로고    scopus 로고
    • Pentapeptide scanning mutagenesis: Encouraging old proteins to execute unusual tricks
    • Hayes,F. and Hallet,B. (2000) Pentapeptide scanning mutagenesis: encouraging old proteins to execute unusual tricks. Trends Microbiol., 8, 571-577.
    • (2000) Trends Microbiol. , vol.8 , pp. 571-577
    • Hayes, F.1    Hallet, B.2
  • 29
    • 0037092188 scopus 로고    scopus 로고
    • Generating segmental mutations in haloalkane dehalogenase: A novel part in the directed evolution toolbox
    • Pikkemaat,M.G. and Janssen,D.B. (2002) Generating segmental mutations in haloalkane dehalogenase: a novel part in the directed evolution toolbox. Nucleic Acids Res., 30, e35.
    • (2002) Nucleic Acids Res. , vol.30
    • Pikkemaat, M.G.1    Janssen, D.B.2
  • 30
    • 0032519301 scopus 로고    scopus 로고
    • Combinatorial library diversity: Probability assessment of library populations
    • Ward,B. and Juehne,T. (1998) Combinatorial library diversity: probability assessment of library populations. Nucleic Acids Res., 26, 879-886.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 879-886
    • Ward, B.1    Juehne, T.2
  • 31
    • 0034643921 scopus 로고    scopus 로고
    • A new randomization assay reveals unexpected elements of sequence bias in model 'randomized' gene libraries: Implications for biopanning
    • Palfrey,D., Picardo,M. and Hine,A.V. (2000) A new randomization assay reveals unexpected elements of sequence bias in model 'randomized' gene libraries: implications for biopanning. Gene, 251, 91-99.
    • (2000) Gene , vol.251 , pp. 91-99
    • Palfrey, D.1    Picardo, M.2    Hine, A.V.3
  • 32
    • 0028559783 scopus 로고
    • Trinucleotide phosphoramidites: Ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis
    • Virnekaes,B., Ge,L., Plueckthun,A. Schneider,K.C., Wellnhofer,G. and Moroney,S.E. (1994) Trinucleotide phosphoramidites: ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis. Nucleic Acids Res., 22, 5600-5607.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5600-5607
    • Virnekaes, B.1    Ge, L.2    Plueckthun, A.3    Schneider, K.C.4    Wellnhofer, G.5    Moroney, S.E.6
  • 33
    • 1842586731 scopus 로고    scopus 로고
    • Efficient flexible access to fully protected trinucleotides suitable for DNA synthesis by automated phosphoramidite chemistry
    • Zehl,A., Starke,A., Cech,D., Hartsch,T., Merkl,R. and Fritz,H.J. (1996) Efficient and flexible access to fully protected trinucleotides suitable for DNA synthesis by automated phosphoramidite chemistry. Chem. Commun. Chem. Soc., 2677-2678.
    • (1996) Chem. Commun. Chem. Soc. , pp. 2677-2678
    • Zehl, A.1    Starke, A.2    Cech, D.3    Hartsch, T.4    Merkl, R.5    Fritz, H.J.6
  • 34
    • 0029810446 scopus 로고    scopus 로고
    • A convenient approach to the synthesis of trinucleotide phosphoramidites-synthons for the generation of oligonucleotide/peptide libraries
    • Kayushin,A., Korosteleva,M., Miroshnikov,A., Zubov,D., Kosch,W. and Piel,N. (1996) A convenient approach to the synthesis of trinucleotide phosphoramidites-synthons for the generation of oligonucleotide/peptide libraries. Nucleic Acids Res., 24, 3748-3755.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3748-3755
    • Kayushin, A.1    Korosteleva, M.2    Miroshnikov, A.3    Zubov, D.4    Kosch, W.5    Piel, N.6
  • 35
    • 0034514421 scopus 로고    scopus 로고
    • Large-scale solid-phase preparation of 3′-unprotected trinucleotide phosphotriesters-precursors for synthesis of trinucleotide phosphoramidites
    • Kayushin,A., Korosteleva,M. and Miroshnikov,A. (2000) Large-scale solid-phase preparation of 3′-unprotected trinucleotide phosphotriesters-precursors for synthesis of trinucleotide phosphoramidites. Nucleosides Nucleotides Nucleic Acids, 19, 1967-1976.
    • (2000) Nucleosides Nucleotides Nucleic Acids , vol.19 , pp. 1967-1976
    • Kayushin, A.1    Korosteleva, M.2    Miroshnikov, A.3
  • 36
    • 0035260476 scopus 로고    scopus 로고
    • Orthogonal combinatorial mutagenesis: A codon-level combinatorial mutagenesis method useful for low multiplicity amino acid-scanning protocols
    • Gaytan,P., Yanez,J., Sanchez,F. and Soberon,X. (2001) Orthogonal combinatorial mutagenesis: a codon-level combinatorial mutagenesis method useful for low multiplicity and amino acid-scanning protocols. Nucleic Acids Res., 29, e9.
    • (2001) Nucleic Acids Res. , vol.29
    • Gaytan, P.1    Yanez, J.2    Sanchez, F.3    Soberon, X.4
  • 37
    • 0032170417 scopus 로고    scopus 로고
    • Combination of DMT-mononucleotide and Fmoc-trinucleotide phosphoramidites in oligonucleotide synthesis affords an automatable codon-level mutagenesis method
    • Gaytan,P., Yanez,J., Sanchez,F., Mackie,H. and Soberon,X. (1998) Combination of DMT-mononucleotide and Fmoc-trinucleotide phosphoramidites in oligonucleotide synthesis affords an automatable codon-level mutagenesis method. Chem. Biol., 5, 519-527.
    • (1998) Chem. Biol. , vol.5 , pp. 519-527
    • Gaytan, P.1    Yanez, J.2    Sanchez, F.3    Mackie, H.4    Soberon, X.5
  • 39
    • 0027082901 scopus 로고
    • Antibody engineering by codon-based mutagenesis in a filamentous phage vector system
    • Glaser,S.M., Yelton,D.E. and Huse,W.D. (1992) Antibody engineering by codon-based mutagenesis in a filamentous phage vector system. J. Immunol., 149, 3903-3913.
    • (1992) J. Immunol. , vol.149 , pp. 3903-3913
    • Glaser, S.M.1    Yelton, D.E.2    Huse, W.D.3
  • 41
    • 0035464767 scopus 로고    scopus 로고
    • Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate
    • Sakamoto,T., Joern,J.M., Arisawa,A. and Arnold,F.H. (2001) Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate. Appl. Environ. Microbiol., 67, 3882-3887.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3882-3887
    • Sakamoto, T.1    Joern, J.M.2    Arisawa, A.3    Arnold, F.H.4
  • 42
    • 0038814072 scopus 로고    scopus 로고
    • Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate
    • Horsman,G.P., Liu,A.M., Henke,E., Bornscheuer,U.T. and Kazlauskas,R.J. (2003) Mutations in distant residues moderately increase the enantioselectivity of Pseudomonas fluorescens esterase towards methyl 3bromo-2-methylpropanoate and ethyl 3phenylbutyrate. Chemistry, 9, 1933-1939.
    • (2003) Chemistry , vol.9 , pp. 1933-1939
    • Horsman, G.P.1    Liu, A.M.2    Henke, E.3    Bornscheuer, U.T.4    Kazlauskas, R.J.5
  • 43
    • 0038070162 scopus 로고    scopus 로고
    • Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: The role of alanine 230 in acceptor subsite +1
    • Leemhuis,H., Rozeboom,H.J., Wilbrink,M., Euverink,G.J., Dijkstra,B.W. and Dijkhuizen,L. (2003) Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1. Biochemistry, 42, 7518-7526.
    • (2003) Biochemistry , vol.42 , pp. 7518-7526
    • Leemhuis, H.1    Rozeboom, H.J.2    Wilbrink, M.3    Euverink, G.J.4    Dijkstra, B.W.5    Dijkhuizen, L.6
  • 44
    • 0037401692 scopus 로고    scopus 로고
    • Directed evolution of N-acetylneuraminic acid aldolase to catalyze enantiomeric aldol reactions
    • Wada,M., Hsu,C.C., Franke,D., Mitchell,M., Heine,A., Wilson,I. and Wong,C.H. (2003) Directed evolution of N-acetylneuraminic acid aldolase to catalyze enantiomeric aldol reactions. Bioorg. Med. Chem., 11, 2091-2098.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 2091-2098
    • Wada, M.1    Hsu, C.C.2    Franke, D.3    Mitchell, M.4    Heine, A.5    Wilson, I.6    Wong, C.H.7
  • 45
    • 0037399074 scopus 로고    scopus 로고
    • Directed evolution of O(6)-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo
    • Juillerat,A., Gronemeyer,T., Keppler,A., Gendreizig,S., Pick,H., Vogel,H. and Johnsson,K. (2003) Directed evolution of O(6)-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo. Chem. Biol., 10, 313-317.
    • (2003) Chem. Biol. , vol.10 , pp. 313-317
    • Juillerat, A.1    Gronemeyer, T.2    Keppler, A.3    Gendreizig, S.4    Pick, H.5    Vogel, H.6    Johnsson, K.7
  • 48
    • 1842842876 scopus 로고    scopus 로고
    • Creating random mutagenesis libraries using megaprimer PCR of whole plasmid
    • 1033-1034
    • Miyazaki,K. and Takenouchi,M. (2002) Creating random mutagenesis libraries using megaprimer PCR of whole plasmid. Biotechniques, 33, 1033-1034, 1036-1038.
    • (2002) Biotechniques , vol.33 , pp. 1036-1038
    • Miyazaki, K.1    Takenouchi, M.2
  • 49
    • 3042784273 scopus 로고    scopus 로고
    • Creating random mutagenesis libraries by megaprimer PCR of whole plasmid (MEGAWHOP)
    • Miyazaki,K. (2003) Creating random mutagenesis libraries by megaprimer PCR of whole plasmid (MEGAWHOP). Methods Mol. Biol., 231, 23-28.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 23-28
    • Miyazaki, K.1
  • 50
    • 0037415021 scopus 로고    scopus 로고
    • Assembly of designed oligonucleotides as an efficient method for gene recombination: A new tool in directed evolution
    • Zha,D., Eipper,A. and Reetz,M.T. (2003) Assembly of designed oligonucleotides as an efficient method for gene recombination: a new tool in directed evolution. Chembiochemistry, 4, 34-39.
    • (2003) Chembiochemistry , vol.4 , pp. 34-39
    • Zha, D.1    Eipper, A.2    Reetz, M.T.3
  • 52
    • 0036841628 scopus 로고    scopus 로고
    • Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit
    • 1162 1158-1160
    • Hogrefe,H.H., Cline,J., Youngblood,G.L. and Allen,R.M. (2002) Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit. Biotechniques, 33, 1158-1160, 1162, 1164-1165.
    • (2002) Biotechniques , vol.33 , pp. 1164-1165
    • Hogrefe, H.H.1    Cline, J.2    Youngblood, G.L.3    Allen, R.M.4
  • 54
  • 55
    • 1542323289 scopus 로고    scopus 로고
    • Staggered extension process (StEP) in vitro recombination
    • Aguinaldo,A.M. and Arnold,F.H. (2003) Staggered extension process (StEP) in vitro recombination. Methods Mol. Biol., 231, 105-110.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 105-110
    • Aguinaldo, A.M.1    Arnold, F.H.2
  • 57
    • 1542353447 scopus 로고    scopus 로고
    • RACHITT: Gene family shuffling by Random Chimeragenesis on Transient Templates
    • Coco,W.M. (2003) RACHITT: Gene family shuffling by Random Chimeragenesis on Transient Templates. Methods Mol. Biol., 231, 111-127.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 111-127
    • Coco, W.M.1
  • 58
    • 0035866186 scopus 로고    scopus 로고
    • Rapid generation of incremental truncation libraries for protein engineering using alpha-phosphothioate nucleotides
    • Lutz,S., Ostermeier,M. and Benkovic,S.J. (2001) Rapid generation of incremental truncation libraries for protein engineering using alpha-phosphothioate nucleotides. Nucleic Acids Res., 29, e16.
    • (2001) Nucleic Acids Res. , vol.29
    • Lutz, S.1    Ostermeier, M.2    Benkovic, S.J.3
  • 59
    • 3042739160 scopus 로고    scopus 로고
    • The creation of ITCHY hybrid protein libraries
    • Ostermeier,M. and Lutz,S. (2003) The creation of ITCHY hybrid protein libraries. Methods Mol. Biol., 231, 129-141.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 129-141
    • Ostermeier, M.1    Lutz, S.2
  • 60
    • 3042702522 scopus 로고    scopus 로고
    • Preparation of SCRATCHY hybrid protein libraries: Size- In-frame selection of nucleic acid sequences
    • Lutz,S. and Ostermeier,M. (2003) Preparation of SCRATCHY hybrid protein libraries: size- and in-frame selection of nucleic acid sequences. Methods Mol. Biol., 231, 143-151.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 143-151
    • Lutz, S.1    Ostermeier, M.2
  • 61
    • 0038606300 scopus 로고    scopus 로고
    • Forced evolution of a herbicide detoxifying glutathione transferase
    • Dixon,D.P., McEwen,A.G., Lapthorn,A.J. and Edwards,R. (2003) Forced evolution of a herbicide detoxifying glutathione transferase. J. Biol. Chem., 278, 23930-23935.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23930-23935
    • Dixon, D.P.1    McEwen, A.G.2    Lapthorn, A.J.3    Edwards, R.4
  • 62
    • 0038521054 scopus 로고    scopus 로고
    • Significantly enhanced stability of glucose dehydrogenase by directed evolution
    • Baik,S.H., Ide,T., Yoshida,H., Kagami,O. and Harayama,S. (2003) Significantly enhanced stability of glucose dehydrogenase by directed evolution. Appl. Microbiol. Biotechnol., 61, 329-335.
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 329-335
    • Baik, S.H.1    Ide, T.2    Yoshida, H.3    Kagami, O.4    Harayama, S.5
  • 63
    • 0037114242 scopus 로고    scopus 로고
    • Random DNA fragmentation with endonuclease V: Application to DNA shuffling
    • Miyazaki,K. (2002) Random DNA fragmentation with endonuclease V: application to DNA shuffling. Nucleic Acids Res., 30, e139.
    • (2002) Nucleic Acids Res. , vol.30
    • Miyazaki, K.1
  • 64
    • 0036842594 scopus 로고    scopus 로고
    • Laboratory evolution of a soluble self-sufficient highly active alkane hydroxylase
    • Glieder,A., Farinas,E.T. and Arnold,F.H. (2002) Laboratory evolution of a soluble, self-sufficient, highly active alkane hydroxylase. Nat. Biotechnol., 20, 1135-1139.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1135-1139
    • Glieder, A.1    Farinas, E.T.2    Arnold, F.H.3
  • 65
    • 0035183586 scopus 로고    scopus 로고
    • Expression stabilization of galactose oxidase in Escherichia coli by directed evolution
    • Sun,L., Petrounia,I.P., Yagasaki,M., Bandara,G. and Arnold,F.H. (2001) Expression and stabilization of galactose oxidase in Escherichia coli by directed evolution. Protein Eng., 14, 699-704.
    • (2001) Protein Eng. , vol.14 , pp. 699-704
    • Sun, L.1    Petrounia, I.P.2    Yagasaki, M.3    Bandara, G.4    Arnold, F.H.5
  • 67
    • 0036606766 scopus 로고    scopus 로고
    • eCodonOpt: A systematic computational framework for optimizing codon usage in directed evolution experiments
    • Moore,G.L. and Maranas,C.D. (2002) eCodonOpt: a systematic computational framework for optimizing codon usage in directed evolution experiments. Nucleic Acids Res., 30, 2407-2416.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2407-2416
    • Moore, G.L.1    Maranas, C.D.2
  • 68
  • 69
    • 0032814117 scopus 로고    scopus 로고
    • Novel family shuffling methods for the in vitro evolution of enzymes
    • Kikuchi,M., Ohnishi,K. and Harayama,S. (1999) Novel family shuffling methods for the in vitro evolution of enzymes. Gene, 236, 159-167.
    • (1999) Gene , vol.236 , pp. 159-167
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 70
    • 0033964975 scopus 로고    scopus 로고
    • An effective family shuffling method using single-stranded DNA
    • Kikuchi,M., Ohnishi,K. and Harayama,S. (2000) An effective family shuffling method using single-stranded DNA. Gene, 243, 133-137.
    • (2000) Gene , vol.243 , pp. 133-137
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 71
    • 1542263494 scopus 로고    scopus 로고
    • Family shuffling with single-stranded DNA
    • Zha,W., Zhu,T. and Zhao,H. (2003) Family shuffling with single-stranded DNA. Methods Mol. Biol., 231, 91-97.
    • (2003) Methods Mol. Biol. , vol.231 , pp. 91-97
    • Zha, W.1    Zhu, T.2    Zhao, H.3
  • 72
    • 0035854021 scopus 로고    scopus 로고
    • Degenerate oligonucleotide gene shuffling (DOGS): A method for enhancing the frequency of recombination with family shuffling
    • Gibbs,M.D., Nevalainen,K.M. and Bergquist,P.L. (2001) Degenerate oligonucleotide gene shuffling (DOGS): a method for enhancing the frequency of recombination with family shuffling. Gene, 271, 13-20.
    • (2001) Gene , vol.271 , pp. 13-20
    • Gibbs, M.D.1    Nevalainen, K.M.2    Bergquist, P.L.3
  • 73
    • 0036933287 scopus 로고    scopus 로고
    • A universal vector-based system for nucleic acid reading-frame selection
    • Lutz,S., Fast,W. and Benkovic,S.J. (2002) A universal, vector-based system for nucleic acid reading-frame selection. Protein Eng., 15, 1025-1030.
    • (2002) Protein Eng. , vol.15 , pp. 1025-1030
    • Lutz, S.1    Fast, W.2    Benkovic, S.J.3
  • 75
    • 0642334596 scopus 로고    scopus 로고
    • Enhanced crossover SCRATCHY: Construction high-throughput screening of a combinatorial library containing multiple non-homologous crossovers
    • Kawarasaki,Y., Griswold,K.E., Stevenson,J.D., Selzer,T., Benkovic,S.J., Iverson,B.L. and Georgiou,G. (2003) Enhanced crossover SCRATCHY: construction and high-throughput screening of a combinatorial library containing multiple non-homologous crossovers. Nucleic Acids Res., 31, e126.
    • (2003) Nucleic Acids Res. , vol.31
    • Kawarasaki, Y.1    Griswold, K.E.2    Stevenson, J.D.3    Selzer, T.4    Benkovic, S.J.5    Iverson, B.L.6    Georgiou, G.7
  • 76
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based combinatorial protein engineering (SCOPE)
    • O'Maille,P.E., Bakhtina,M. and Tsai,M.D. (2002) Structure-based combinatorial protein engineering (SCOPE). J. Mol. Biol., 321, 677-691.
    • (2002) J. Mol. Biol. , vol.321 , pp. 677-691
    • O'Maille, P.E.1    Bakhtina, M.2    Tsai, M.D.3
  • 77
    • 0038799745 scopus 로고    scopus 로고
    • General method for sequence-independent site-directed chimeragenesis
    • Hiraga,K. and Arnold,F.H. (2003) General method for sequence-independent site-directed chimeragenesis. J. Mol. Biol., 330, 287-296.
    • (2003) J. Mol. Biol. , vol.330 , pp. 287-296
    • Hiraga, K.1    Arnold, F.H.2
  • 80
    • 0031587291 scopus 로고    scopus 로고
    • Strategies for the in vitro evolution of protein function: Enzyme evolution by random recombination of improved sequences
    • Moore,J.C., Jin,H.-M., Kuchner,O. and Arnold,F.H. (1997) Strategies for the in vitro evolution of protein function: enzyme evolution by random recombination of improved sequences. J. Mol. Biol., 272, 336-347.
    • (1997) J. Mol. Biol. , vol.272 , pp. 336-347
    • Moore, J.C.1    Jin, H.-M.2    Kuchner, O.3    Arnold, F.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.