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Zhao H., Moore J.C., Volkov A.A., Arnold F.H. Methods for optimizing industrial enzymes by directed evolution. Demain A.L., Davies J.E. Manual of Industrial Microbiology and Biotechnology, 2nd edn. 1999;597-604 ASM Press, Washington, DC.
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Zhao, H.1
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Directed enzyme evolution
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M.C. Flickinger, & S.W. Drew. New York: John Wiley & Sons, Inc
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Arnold F.H., Wintrode P.L. Directed enzyme evolution. Flickinger M.C., Drew S.W. Encyclopedia of Bioprocess Technology: Fermentation, Biocatalysis, and Bioseparation. 1999;971-987 John Wiley & Sons, Inc, New York.
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Arnold, F.H.1
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Directed evolution of enantioselective enzymes for organic chemistry
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Tuning the activity of an enzyme for unusual environments - sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
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Chen K.Q., Arnold F.H. Tuning the activity of an enzyme for unusual environments - sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc Natl Acad Sci USA. 90:1993;5618-5622.
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Molecular evolution by staggered extension process (StEP) in vitro recombination
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Zhao H., Giver L., Affholter J.A., Arnold F.H. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat Biotechnol. 16:1998;258-261.
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Zhao, H.1
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DNA shuffling of a family of genes from diverse species accelerates directed evolution
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Crameri A., Raillard S.A., Bermudez E., Stemmer W.P.C. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature. 391:1998;288-291.
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Crameri, A.1
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9
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0033578095
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Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
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The rapid evolution of a cofactor-free monooxygenase is achieved with the aid of a well-designed, high-throughput screen.
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Joo H., Lin Z., Arnold F.H. Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature. 399:1999;670-673. The rapid evolution of a cofactor-free monooxygenase is achieved with the aid of a well-designed, high-throughput screen.
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Nature
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Joo, H.1
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The power of evolution: Accessing the synthetic potential of P450s
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Chem Biol
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Roberts, G.C.K.1
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11
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A high-throughput digital imaging screen for the discovery and directed evolution of oxygenases
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Joo H., Arisawa A., Lin Z., Arnold F.H. A high-throughput digital imaging screen for the discovery and directed evolution of oxygenases. Chem Biol. 6:1999;699-706.
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Chem Biol
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Joo, H.1
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12
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0032738825
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A microfabricated fluorescence-activated cell sorter
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Describes construction of a disposable, microfabricated fluorescence-activated cell sorter that can be used to screen microbial libraries.
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Fu A.Y., Spence C., Scherer A., Arnold F.H., Quake S.R. A microfabricated fluorescence-activated cell sorter. Nat Biotechnol. 17:1999;1109-1111. Describes construction of a disposable, microfabricated fluorescence-activated cell sorter that can be used to screen microbial libraries.
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Fu, A.Y.1
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13
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0034088553
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Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris
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in press.
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Morawski B., Lin Z., Cirino P., Joo H., Bandara G., Arnold F.H. Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris. Protein Eng. 2000;. in press.
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Protein Eng
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Morawski, B.1
Lin, Z.2
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Bandara, G.5
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14
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Horseradish peroxidase: The analyst's friend
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Ryan O., Smyth M.R., Fágáin C.O. Horseradish peroxidase: the analyst's friend. Essays Biochem. 28:1994;129-146.
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Ryan, O.1
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16
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0033015460
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Rapid protein-folding assay using green fluorescent protein
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GFP expressed as a carboxy-terminal fusion to cytosolic proteins acts as a reporter for protein folding and enables identification of variants that fold efficiently in E. coli.
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Waldo G.S., Standish B.M., Berendzen J., Terwilliger T.C. Rapid protein-folding assay using green fluorescent protein. Nat Biotechnol. 17:1999;691-695. GFP expressed as a carboxy-terminal fusion to cytosolic proteins acts as a reporter for protein folding and enables identification of variants that fold efficiently in E. coli.
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Nat Biotechnol
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Waldo, G.S.1
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17
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0034059496
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Inverting enantioselectivity and increasing total activity of a key enzyme in a multi-enzyme synthesis creates a viable process for production of l-methionine
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Enantioselectivity of a hydantoinase has been inverted by directed evolution. No hydantoinase with selectivity for the L-hydantoin has yet been found in nature.
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May O., Nguyen P.T., Arnold F.H. Inverting enantioselectivity and increasing total activity of a key enzyme in a multi-enzyme synthesis creates a viable process for production of l-methionine. Nat Biotechnol. 18:2000;317-320. Enantioselectivity of a hydantoinase has been inverted by directed evolution. No hydantoinase with selectivity for the L-hydantoin has yet been found in nature.
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Nat Biotechnol
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May, O.1
Nguyen, P.T.2
Arnold, F.H.3
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0033553799
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Measurement of enantiomeric excess by kinetic resolution and mass spectrometry
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Guo J., Wu J., Siuzdak G., Finn M.G. Measurement of enantiomeric excess by kinetic resolution and mass spectrometry. Angew Chem Int Ed Engl. 38:1999;1755-1758.
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Guo, J.1
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0032538361
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Time-resolved IR-thermographic detection and screening of enantioselectivity in catalytic reactions
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Reetz M.T., Becker M.H., Kuhling K.M., Holzwarth A. Time-resolved IR-thermographic detection and screening of enantioselectivity in catalytic reactions. Angew Chem Int Ed Engl. 37:1998;2647-2650.
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Reetz, M.T.1
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21
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0033280672
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Exploring nonnatural evolutionary pathways by saturation mutagenesis: Rapid improvement of protein function
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Miyazaki K., Arnold F.H. Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J Mol Evol. 49:1999;716-720.
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J Mol Evol
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Miyazaki, K.1
Arnold, F.H.2
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22
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0034615775
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Directed evolution study of temperature adaptation in a psychrophilic enzyme
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Although rarely observed in nature, it is physically possible to enhance enzyme thermostability and catalytic activity at low temperature simultaneously.
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Miyazaki K., Wintrode P.L., Grayling R.A., Rubingh D.N., Arnold F.H. Directed evolution study of temperature adaptation in a psychrophilic enzyme. J Mol Biol. 297:2000;1015-1026. Although rarely observed in nature, it is physically possible to enhance enzyme thermostability and catalytic activity at low temperature simultaneously.
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J Mol Biol
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Miyazaki, K.1
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25
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0034712678
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Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases
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Gershenson A., Schauerte J.A., Giver L., Arnold F.H. Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases. Biochemistry. 39:2000;4658-4665.
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Biochemistry
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Gershenson, A.1
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Arnold, F.H.4
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26
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0034620512
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Improving the catalytic activity of a thermophilic enzyme at low temperatures
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cat and not on maintaining high thermostability.
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cat and not on maintaining high thermostability.
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Biochemistry
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Merz, A.1
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Stemmer, W.P.C.6
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Kirschner, K.8
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27
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0033054580
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Directed evolution of the surface chemistry of the reporter enzyme β-glucuronidase
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A nice example of directed evolution with a surprising solution: only one of the multiple amino acid substitutions that confer glutaraldehyde resistance to GUS occurs at a lysine residue.
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Matsamura I., Wallingford J.B., Surana N.K., Vize P.D., Ellington A.D. Directed evolution of the surface chemistry of the reporter enzyme β-glucuronidase. Nat Biotechnol. 17:1999;696-701. A nice example of directed evolution with a surprising solution: only one of the multiple amino acid substitutions that confer glutaraldehyde resistance to GUS occurs at a lysine residue.
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Nat Biotechnol
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Matsamura, I.1
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28
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0034628501
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Directed evolution of new catalytic activity using the α/β-barrel scaffold
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A remarkable example of evolution of a novel function in the scaffold of an α/β-barrel protein. Critical to the success of this study was the combination of rational and evolutionary design principles.
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Altamirano M.M., Blackburn J.M., Aguayo C., Fersht A.R. Directed evolution of new catalytic activity using the α/β-barrel scaffold. Nature. 403:2000;617-622. A remarkable example of evolution of a novel function in the scaffold of an α/β-barrel protein. Critical to the success of this study was the combination of rational and evolutionary design principles.
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(2000)
Nature
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Altamirano, M.M.1
Blackburn, J.M.2
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Fersht, A.R.4
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29
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0032956429
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Engineering a regulatable enzyme for homogenous immunoassays
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This paper describes how phage display can be exploited to generate regulatable variants of β-lactamase.
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Legendre D., Soumillon P., Fastrez J. Engineering a regulatable enzyme for homogenous immunoassays. Nat Biotechnol. 17:1999;67-72. This paper describes how phage display can be exploited to generate regulatable variants of β-lactamase.
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Nat Biotechnol
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Legendre, D.1
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0032784511
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Design of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution
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Doi N., Yanagawa H. Design of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution. FEBS Lett. 453:1999;305-307.
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FEBS Lett
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Doi, N.1
Yanagawa, H.2
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31
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0033037012
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Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling
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DNA family shuffling of two genes results in the creation of chimeras with function that is significantly improved over any of the parental enzymes.
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Christians F.C., Scapozza L., Crameri A., Folkers G., Stemmer W.P.C. Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling. Nat Biotechnol. 17:1999;259-264. DNA family shuffling of two genes results in the creation of chimeras with function that is significantly improved over any of the parental enzymes.
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(1999)
Nat Biotechnol
, vol.17
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Christians, F.C.1
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32
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Tuning biphenyl dioxygenase for extended substrate specificity
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Bruhlmann F., Chen W. Tuning biphenyl dioxygenase for extended substrate specificity. Biotechnol Bioeng. 63:1999;544-551.
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Biotechnol Bioeng
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Novel family shuffling methods for the in vitro evolution of enzymes
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Kikuchi M., Ohnishi K., Harayama S. Novel family shuffling methods for the in vitro evolution of enzymes. Gene. 236:1999;159-167.
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Gene
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Kikuchi, M.1
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35
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0032885231
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DNA shuffling of subgenomic sequences of subtilisin
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Chimeras possessing all combinations of properties of individual parents and chimeras significantly improved over any of the parental enzymes for each single property are identified in a family shuffling library.
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Ness J.E., Welch M., Giver L., Bueno M., Cherry J.R., Borchert T.V., Stemmer W.P.C., Minshull J. DNA shuffling of subgenomic sequences of subtilisin. Nat Biotechnol. 17:1999;893-896. Chimeras possessing all combinations of properties of individual parents and chimeras significantly improved over any of the parental enzymes for each single property are identified in a family shuffling library.
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(1999)
Nat Biotechnol
, vol.17
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Ness, J.E.1
Welch, M.2
Giver, L.3
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Stemmer, W.P.C.7
Minshull, J.8
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37
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17444363724
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A combinatorial approach to hybrid enzymes independent of DNA homology
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The authors describe a method to create functional interspecies hybrids in a manner independent of DNA sequence homology.
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Ostermeier M., Shim J.H., Benkovic S.J. A combinatorial approach to hybrid enzymes independent of DNA homology. Nat Biotechnol. 17:1999;1205-1209. The authors describe a method to create functional interspecies hybrids in a manner independent of DNA sequence homology.
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(1999)
Nat Biotechnol
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Ostermeier, M.1
Shim, J.H.2
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0032850532
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Incremental truncation as a strategy in the engineering of novel biocatalysts
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Ostermeier M., Nixon A.E., Benkovic S.J. Incremental truncation as a strategy in the engineering of novel biocatalysts. Bioorg Med Chem. 7:1999;2139-2144.
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Ostermeier, M.1
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39
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0033567665
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Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair
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Volkov A.A., Shao Z., Arnold F.H. Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair. Nucleic Acids Res. 27:1999;e18.
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Nucleic Acids Res
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Volkov, A.A.1
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Arnold, F.H.3
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