A. Crameri, S. A. Raillard, E. Bermudez et W. P. Stemmer, « DNA shuffling of a family of genes from diverse species accelerates directed evolution », Nature, vol. 391, no 6664, , p. 288–291 (ISSN0028-0836, PMID9440693, DOI10.1038/34663, lire en ligne, consulté le )
Manfred T. Reetz et José Daniel Carballeira, « Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes », Nature Protocols, vol. 2, no 4, , p. 891–903 (ISSN1750-2799, PMID17446890, DOI10.1038/nprot.2007.72, lire en ligne, consulté le )
Hans Leemhuis, Viktor Stein, Andrew D. Griffiths et Florian Hollfelder, « New genotype-phenotype linkages for directed evolution of functional proteins », Current Opinion in Structural Biology, vol. 15, no 4, , p. 472–478 (ISSN0959-440X, PMID16043338, DOI10.1016/j.sbi.2005.07.006, lire en ligne, consulté le )
Kathryn D. Verhoeven, Olvia C. Altstadt et Sergey N. Savinov, « Intracellular detection and evolution of site-specific proteases using a genetic selection system », Applied Biochemistry and Biotechnology, vol. 166, no 5, , p. 1340–1354 (ISSN1559-0291, PMID22270548, DOI10.1007/s12010-011-9522-6, lire en ligne, consulté le )
Annalee W. Nguyen et Patrick S. Daugherty, « Evolutionary optimization of fluorescent proteins for intracellular FRET », Nature Biotechnology, vol. 23, no 3, , p. 355–360 (ISSN1087-0156, PMID15696158, DOI10.1038/nbt1066, lire en ligne, consulté le )
Yolanda Schaerli et Florian Hollfelder, « The potential of microfluidic water-in-oil droplets in experimental biology », Molecular bioSystems, vol. 5, no 12, , p. 1392–1404 (ISSN1742-2051, PMID20023716, DOI10.1039/b907578j, lire en ligne, consulté le )
Corey J. Wilson, « Rational protein design: developing next-generation biological therapeutics and nanobiotechnological tools », Wiley Interdisciplinary Reviews. Nanomedicine and Nanobiotechnology, vol. 7, no 3, , p. 330–341 (ISSN1939-0041, PMID25348497, DOI10.1002/wnan.1310, lire en ligne, consulté le )
Mike M. Y. Chen, Christopher D. Snow, Christina L. Vizcarra et Stephen L. Mayo, « Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes », Protein engineering, design & selection: PEDS, vol. 25, no 4, , p. 171–178 (ISSN1741-0134, PMID22334757, DOI10.1093/protein/gzs004, lire en ligne, consulté le )
Carlos G. Acevedo-Rocha, Sabrina Hoebenreich et Manfred T. Reetz, « Iterative saturation mutagenesis: a powerful approach to engineer proteins by systematically simulating Darwinian evolution », Methods in Molecular Biology (Clifton, N.J.), vol. 1179, , p. 103–128 (ISSN1940-6029, PMID25055773, DOI10.1007/978-1-4939-1053-3_7, lire en ligne, consulté le )
Helge Jochens et Uwe T. Bornscheuer, « Natural diversity to guide focused directed evolution », Chembiochem: A European Journal of Chemical Biology, vol. 11, no 13, , p. 1861–1866 (ISSN1439-7633, PMID20680978, DOI10.1002/cbic.201000284, lire en ligne, consulté le )
Helge Jochens, Dirk Aerts et Uwe T. Bornscheuer, « Thermostabilization of an esterase by alignment-guided focussed directed evolution », Protein engineering, design & selection: PEDS, vol. 23, no 12, , p. 903–909 (ISSN1741-0134, PMID20947674, DOI10.1093/protein/gzq071, lire en ligne, consulté le )
Pietro Gatti-Lafranconi, Antonino Natalello, Sascha Rehm et Silvia Maria Doglia, « Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation », Journal of Molecular Biology, vol. 395, no 1, , p. 155–166 (ISSN1089-8638, PMID19850050, DOI10.1016/j.jmb.2009.10.026, lire en ligne, consulté le )
Fathima Aidha Shaikh et Stephen G. Withers, « Teaching old enzymes new tricks: engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis », Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, vol. 86, no 2, , p. 169–177 (ISSN0829-8211, PMID18443630, DOI10.1139/O07-149, lire en ligne, consulté le )
Manoj Cheriyan, Matthew J. Walters, Brian D. Kang et Laura L. Anzaldi, « Directed evolution of a pyruvate aldolase to recognize a long chain acyl substrate », Bioorganic & Medicinal Chemistry, vol. 19, no 21, , p. 6447–6453 (ISSN1464-3391, PMID21944547, PMCIDPMC3209416, DOI10.1016/j.bmc.2011.08.056, lire en ligne, consulté le )
Miguel D. Toscano, Kenneth J. Woycechowsky et Donald Hilvert, « Minimalist active-site redesign: teaching old enzymes new tricks », Angewandte Chemie (International Ed. in English), vol. 46, no 18, , p. 3212–3236 (ISSN1433-7851, PMID17450624, DOI10.1002/anie.200604205, lire en ligne, consulté le )
Jesse D. Bloom et Frances H. Arnold, « In the light of directed evolution: pathways of adaptive protein evolution », Proceedings of the National Academy of Sciences of the United States of America, vol. 106 Suppl 1, , p. 9995–10000 (ISSN1091-6490, PMID19528653, PMCIDPMC2702793, DOI10.1073/pnas.0901522106, lire en ligne, consulté le )
K. Salehi-Ashtiani et J. W. Szostak, « In vitro evolution suggests multiple origins for the hammerhead ribozyme », Nature, vol. 414, no 6859, , p. 82–84 (ISSN0028-0836, PMID11689947, DOI10.1038/35102081, lire en ligne, consulté le )
William C. Ratcliff, R. Ford Denison, Mark Borrello et Michael Travisano, « Experimental evolution of multicellularity », Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no 5, , p. 1595–1600 (ISSN1091-6490, PMID22307617, PMCIDPMC3277146, DOI10.1073/pnas.1115323109, lire en ligne, consulté le )
Jeffrey E. Barrick, Dong Su Yu, Sung Ho Yoon et Haeyoung Jeong, « Genome evolution and adaptation in a long-term experiment with Escherichia coli », Nature, vol. 461, no 7268, , p. 1243–1247 (ISSN1476-4687, PMID19838166, DOI10.1038/nature08480, lire en ligne, consulté le )
Richard H. Heineman, Ian J. Molineux et James J. Bull, « Evolutionary robustness of an optimal phenotype: re-evolution of lysis in a bacteriophage deleted for its lysin gene », Journal of Molecular Evolution, vol. 61, no 2, , p. 181–191 (ISSN0022-2844, PMID16096681, DOI10.1007/s00239-004-0304-4, lire en ligne, consulté le )
Takuyo Aita, Norio Hamamatsu, Yukiko Nomiya et Hidefumi Uchiyama, « Surveying a local fitness landscape of a protein with epistatic sites for the study of directed evolution », Biopolymers, vol. 64, no 2, , p. 95–105 (ISSN0006-3525, PMID11979520, DOI10.1002/bip.10126, lire en ligne, consulté le )
C. A. Voigt, S. Kauffman et Z. G. Wang, « Rational evolutionary design: the theory of in vitro protein evolution », Advances in Protein Chemistry, vol. 55, , p. 79–160 (ISSN0065-3233, PMID11050933, lire en ligne, consulté le )
S. Sen, V. Venkata Dasu et B. Mandal, « Developments in directed evolution for improving enzyme functions », Applied Biochemistry and Biotechnology, vol. 143, no 3, , p. 212–223 (ISSN0273-2289, PMID18057449, lire en ligne, consulté le )
A. Crameri, S. A. Raillard, E. Bermudez et W. P. Stemmer, « DNA shuffling of a family of genes from diverse species accelerates directed evolution », Nature, vol. 391, no 6664, , p. 288–291 (ISSN0028-0836, PMID9440693, DOI10.1038/34663, lire en ligne, consulté le )
Manfred T. Reetz et José Daniel Carballeira, « Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes », Nature Protocols, vol. 2, no 4, , p. 891–903 (ISSN1750-2799, PMID17446890, DOI10.1038/nprot.2007.72, lire en ligne, consulté le )
William G. T. Willats, « Phage display: practicalities and prospects », Plant Molecular Biology, vol. 50, no 6, , p. 837–854 (ISSN0167-4412, PMID12516857, lire en ligne, consulté le )
Hans Leemhuis, Viktor Stein, Andrew D. Griffiths et Florian Hollfelder, « New genotype-phenotype linkages for directed evolution of functional proteins », Current Opinion in Structural Biology, vol. 15, no 4, , p. 472–478 (ISSN0959-440X, PMID16043338, DOI10.1016/j.sbi.2005.07.006, lire en ligne, consulté le )
Kathryn D. Verhoeven, Olvia C. Altstadt et Sergey N. Savinov, « Intracellular detection and evolution of site-specific proteases using a genetic selection system », Applied Biochemistry and Biotechnology, vol. 166, no 5, , p. 1340–1354 (ISSN1559-0291, PMID22270548, DOI10.1007/s12010-011-9522-6, lire en ligne, consulté le )
Annalee W. Nguyen et Patrick S. Daugherty, « Evolutionary optimization of fluorescent proteins for intracellular FRET », Nature Biotechnology, vol. 23, no 3, , p. 355–360 (ISSN1087-0156, PMID15696158, DOI10.1038/nbt1066, lire en ligne, consulté le )
Yolanda Schaerli et Florian Hollfelder, « The potential of microfluidic water-in-oil droplets in experimental biology », Molecular bioSystems, vol. 5, no 12, , p. 1392–1404 (ISSN1742-2051, PMID20023716, DOI10.1039/b907578j, lire en ligne, consulté le )
Shannon A. Marshall, Greg A. Lazar, Arthur J. Chirino et John R. Desjarlais, « Rational design and engineering of therapeutic proteins », Drug Discovery Today, vol. 8, no 5, , p. 212–221 (ISSN1359-6446, PMID12634013, lire en ligne, consulté le )
Corey J. Wilson, « Rational protein design: developing next-generation biological therapeutics and nanobiotechnological tools », Wiley Interdisciplinary Reviews. Nanomedicine and Nanobiotechnology, vol. 7, no 3, , p. 330–341 (ISSN1939-0041, PMID25348497, DOI10.1002/wnan.1310, lire en ligne, consulté le )
U. T. Bornscheuer et M. Pohl, « Improved biocatalysts by directed evolution and rational protein design », Current Opinion in Chemical Biology, vol. 5, no 2, , p. 137–143 (ISSN1367-5931, PMID11282339, lire en ligne, consulté le )
Mike M. Y. Chen, Christopher D. Snow, Christina L. Vizcarra et Stephen L. Mayo, « Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes », Protein engineering, design & selection: PEDS, vol. 25, no 4, , p. 171–178 (ISSN1741-0134, PMID22334757, DOI10.1093/protein/gzs004, lire en ligne, consulté le )
Carlos G. Acevedo-Rocha, Sabrina Hoebenreich et Manfred T. Reetz, « Iterative saturation mutagenesis: a powerful approach to engineer proteins by systematically simulating Darwinian evolution », Methods in Molecular Biology (Clifton, N.J.), vol. 1179, , p. 103–128 (ISSN1940-6029, PMID25055773, DOI10.1007/978-1-4939-1053-3_7, lire en ligne, consulté le )
Helge Jochens et Uwe T. Bornscheuer, « Natural diversity to guide focused directed evolution », Chembiochem: A European Journal of Chemical Biology, vol. 11, no 13, , p. 1861–1866 (ISSN1439-7633, PMID20680978, DOI10.1002/cbic.201000284, lire en ligne, consulté le )
Helge Jochens, Dirk Aerts et Uwe T. Bornscheuer, « Thermostabilization of an esterase by alignment-guided focussed directed evolution », Protein engineering, design & selection: PEDS, vol. 23, no 12, , p. 903–909 (ISSN1741-0134, PMID20947674, DOI10.1093/protein/gzq071, lire en ligne, consulté le )
Pietro Gatti-Lafranconi, Antonino Natalello, Sascha Rehm et Silvia Maria Doglia, « Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation », Journal of Molecular Biology, vol. 395, no 1, , p. 155–166 (ISSN1089-8638, PMID19850050, DOI10.1016/j.jmb.2009.10.026, lire en ligne, consulté le )
H. Zhao et F. H. Arnold, « Directed evolution converts subtilisin E into a functional equivalent of thermitase », Protein Engineering, vol. 12, no 1, , p. 47–53 (ISSN0269-2139, PMID10065710, lire en ligne, consulté le )
R. E. Hawkins, S. J. Russell et G. Winter, « Selection of phage antibodies by binding affinity. Mimicking affinity maturation », Journal of Molecular Biology, vol. 226, no 3, , p. 889–896 (ISSN0022-2836, PMID1507232, lire en ligne, consulté le )
Fathima Aidha Shaikh et Stephen G. Withers, « Teaching old enzymes new tricks: engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis », Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, vol. 86, no 2, , p. 169–177 (ISSN0829-8211, PMID18443630, DOI10.1139/O07-149, lire en ligne, consulté le )
Manoj Cheriyan, Matthew J. Walters, Brian D. Kang et Laura L. Anzaldi, « Directed evolution of a pyruvate aldolase to recognize a long chain acyl substrate », Bioorganic & Medicinal Chemistry, vol. 19, no 21, , p. 6447–6453 (ISSN1464-3391, PMID21944547, PMCIDPMC3209416, DOI10.1016/j.bmc.2011.08.056, lire en ligne, consulté le )
G. MacBeath, P. Kast et D. Hilvert, « Redesigning enzyme topology by directed evolution », Science (New York, N.Y.), vol. 279, no 5358, , p. 1958–1961 (ISSN0036-8075, PMID9506949, lire en ligne, consulté le )
Miguel D. Toscano, Kenneth J. Woycechowsky et Donald Hilvert, « Minimalist active-site redesign: teaching old enzymes new tricks », Angewandte Chemie (International Ed. in English), vol. 46, no 18, , p. 3212–3236 (ISSN1433-7851, PMID17450624, DOI10.1002/anie.200604205, lire en ligne, consulté le )
M. Höss, P. Jaruga, T. H. Zastawny et M. Dizdaroglu, « DNA damage and DNA sequence retrieval from ancient tissues », Nucleic Acids Research, vol. 24, no 7, , p. 1304–1307 (ISSN0305-1048, PMID8614634, lire en ligne, consulté le )
Jesse D. Bloom et Frances H. Arnold, « In the light of directed evolution: pathways of adaptive protein evolution », Proceedings of the National Academy of Sciences of the United States of America, vol. 106 Suppl 1, , p. 9995–10000 (ISSN1091-6490, PMID19528653, PMCIDPMC2702793, DOI10.1073/pnas.0901522106, lire en ligne, consulté le )
K. Salehi-Ashtiani et J. W. Szostak, « In vitro evolution suggests multiple origins for the hammerhead ribozyme », Nature, vol. 414, no 6859, , p. 82–84 (ISSN0028-0836, PMID11689947, DOI10.1038/35102081, lire en ligne, consulté le )
M. Sumper et R. Luce, « Evidence for de novo production of self-replicating and environmentally adapted RNA structures by bacteriophage Qbeta replicase », Proceedings of the National Academy of Sciences of the United States of America, vol. 72, no 1, , p. 162–166 (ISSN0027-8424, PMID1054493, lire en ligne, consulté le )
D. R. Mills, R. L. Peterson et S. Spiegelman, « An extracellular Darwinian experiment with a self-duplicating nucleic acid molecule », Proceedings of the National Academy of Sciences of the United States of America, vol. 58, no 1, , p. 217–224 (ISSN0027-8424, PMID5231602, lire en ligne, consulté le )
J. H. Marden, M. R. Wolf et K. E. Weber, « Aerial performance of Drosophila melanogaster from populations selected for upwind flight ability », The Journal of Experimental Biology, vol. 200, no Pt 21, , p. 2747–2755 (ISSN0022-0949, PMID9418031, lire en ligne, consulté le )
William C. Ratcliff, R. Ford Denison, Mark Borrello et Michael Travisano, « Experimental evolution of multicellularity », Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no 5, , p. 1595–1600 (ISSN1091-6490, PMID22307617, PMCIDPMC3277146, DOI10.1073/pnas.1115323109, lire en ligne, consulté le )
Jeffrey E. Barrick, Dong Su Yu, Sung Ho Yoon et Haeyoung Jeong, « Genome evolution and adaptation in a long-term experiment with Escherichia coli », Nature, vol. 461, no 7268, , p. 1243–1247 (ISSN1476-4687, PMID19838166, DOI10.1038/nature08480, lire en ligne, consulté le )
Richard H. Heineman, Ian J. Molineux et James J. Bull, « Evolutionary robustness of an optimal phenotype: re-evolution of lysis in a bacteriophage deleted for its lysin gene », Journal of Molecular Evolution, vol. 61, no 2, , p. 181–191 (ISSN0022-2844, PMID16096681, DOI10.1007/s00239-004-0304-4, lire en ligne, consulté le )
Takuyo Aita, Norio Hamamatsu, Yukiko Nomiya et Hidefumi Uchiyama, « Surveying a local fitness landscape of a protein with epistatic sites for the study of directed evolution », Biopolymers, vol. 64, no 2, , p. 95–105 (ISSN0006-3525, PMID11979520, DOI10.1002/bip.10126, lire en ligne, consulté le )
F. H. Arnold, P. L. Wintrode, K. Miyazaki et A. Gershenson, « How enzymes adapt: lessons from directed evolution », Trends in Biochemical Sciences, vol. 26, no 2, , p. 100–106 (ISSN0968-0004, PMID11166567, lire en ligne, consulté le )
C. A. Voigt, S. Kauffman et Z. G. Wang, « Rational evolutionary design: the theory of in vitro protein evolution », Advances in Protein Chemistry, vol. 55, , p. 79–160 (ISSN0065-3233, PMID11050933, lire en ligne, consulté le )
S. Sen, V. Venkata Dasu et B. Mandal, « Developments in directed evolution for improving enzyme functions », Applied Biochemistry and Biotechnology, vol. 143, no 3, , p. 212–223 (ISSN0273-2289, PMID18057449, lire en ligne, consulté le )
A. Crameri, S. A. Raillard, E. Bermudez et W. P. Stemmer, « DNA shuffling of a family of genes from diverse species accelerates directed evolution », Nature, vol. 391, no 6664, , p. 288–291 (ISSN0028-0836, PMID9440693, DOI10.1038/34663, lire en ligne, consulté le )
Manfred T. Reetz et José Daniel Carballeira, « Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes », Nature Protocols, vol. 2, no 4, , p. 891–903 (ISSN1750-2799, PMID17446890, DOI10.1038/nprot.2007.72, lire en ligne, consulté le )
William G. T. Willats, « Phage display: practicalities and prospects », Plant Molecular Biology, vol. 50, no 6, , p. 837–854 (ISSN0167-4412, PMID12516857, lire en ligne, consulté le )
Hans Leemhuis, Viktor Stein, Andrew D. Griffiths et Florian Hollfelder, « New genotype-phenotype linkages for directed evolution of functional proteins », Current Opinion in Structural Biology, vol. 15, no 4, , p. 472–478 (ISSN0959-440X, PMID16043338, DOI10.1016/j.sbi.2005.07.006, lire en ligne, consulté le )
Kathryn D. Verhoeven, Olvia C. Altstadt et Sergey N. Savinov, « Intracellular detection and evolution of site-specific proteases using a genetic selection system », Applied Biochemistry and Biotechnology, vol. 166, no 5, , p. 1340–1354 (ISSN1559-0291, PMID22270548, DOI10.1007/s12010-011-9522-6, lire en ligne, consulté le )
Annalee W. Nguyen et Patrick S. Daugherty, « Evolutionary optimization of fluorescent proteins for intracellular FRET », Nature Biotechnology, vol. 23, no 3, , p. 355–360 (ISSN1087-0156, PMID15696158, DOI10.1038/nbt1066, lire en ligne, consulté le )
Yolanda Schaerli et Florian Hollfelder, « The potential of microfluidic water-in-oil droplets in experimental biology », Molecular bioSystems, vol. 5, no 12, , p. 1392–1404 (ISSN1742-2051, PMID20023716, DOI10.1039/b907578j, lire en ligne, consulté le )
Shannon A. Marshall, Greg A. Lazar, Arthur J. Chirino et John R. Desjarlais, « Rational design and engineering of therapeutic proteins », Drug Discovery Today, vol. 8, no 5, , p. 212–221 (ISSN1359-6446, PMID12634013, lire en ligne, consulté le )
Corey J. Wilson, « Rational protein design: developing next-generation biological therapeutics and nanobiotechnological tools », Wiley Interdisciplinary Reviews. Nanomedicine and Nanobiotechnology, vol. 7, no 3, , p. 330–341 (ISSN1939-0041, PMID25348497, DOI10.1002/wnan.1310, lire en ligne, consulté le )
U. T. Bornscheuer et M. Pohl, « Improved biocatalysts by directed evolution and rational protein design », Current Opinion in Chemical Biology, vol. 5, no 2, , p. 137–143 (ISSN1367-5931, PMID11282339, lire en ligne, consulté le )
Mike M. Y. Chen, Christopher D. Snow, Christina L. Vizcarra et Stephen L. Mayo, « Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes », Protein engineering, design & selection: PEDS, vol. 25, no 4, , p. 171–178 (ISSN1741-0134, PMID22334757, DOI10.1093/protein/gzs004, lire en ligne, consulté le )
Carlos G. Acevedo-Rocha, Sabrina Hoebenreich et Manfred T. Reetz, « Iterative saturation mutagenesis: a powerful approach to engineer proteins by systematically simulating Darwinian evolution », Methods in Molecular Biology (Clifton, N.J.), vol. 1179, , p. 103–128 (ISSN1940-6029, PMID25055773, DOI10.1007/978-1-4939-1053-3_7, lire en ligne, consulté le )
Helge Jochens et Uwe T. Bornscheuer, « Natural diversity to guide focused directed evolution », Chembiochem: A European Journal of Chemical Biology, vol. 11, no 13, , p. 1861–1866 (ISSN1439-7633, PMID20680978, DOI10.1002/cbic.201000284, lire en ligne, consulté le )
Helge Jochens, Dirk Aerts et Uwe T. Bornscheuer, « Thermostabilization of an esterase by alignment-guided focussed directed evolution », Protein engineering, design & selection: PEDS, vol. 23, no 12, , p. 903–909 (ISSN1741-0134, PMID20947674, DOI10.1093/protein/gzq071, lire en ligne, consulté le )
Pietro Gatti-Lafranconi, Antonino Natalello, Sascha Rehm et Silvia Maria Doglia, « Evolution of stability in a cold-active enzyme elicits specificity relaxation and highlights substrate-related effects on temperature adaptation », Journal of Molecular Biology, vol. 395, no 1, , p. 155–166 (ISSN1089-8638, PMID19850050, DOI10.1016/j.jmb.2009.10.026, lire en ligne, consulté le )
H. Zhao et F. H. Arnold, « Directed evolution converts subtilisin E into a functional equivalent of thermitase », Protein Engineering, vol. 12, no 1, , p. 47–53 (ISSN0269-2139, PMID10065710, lire en ligne, consulté le )
R. E. Hawkins, S. J. Russell et G. Winter, « Selection of phage antibodies by binding affinity. Mimicking affinity maturation », Journal of Molecular Biology, vol. 226, no 3, , p. 889–896 (ISSN0022-2836, PMID1507232, lire en ligne, consulté le )
Fathima Aidha Shaikh et Stephen G. Withers, « Teaching old enzymes new tricks: engineering and evolution of glycosidases and glycosyl transferases for improved glycoside synthesis », Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, vol. 86, no 2, , p. 169–177 (ISSN0829-8211, PMID18443630, DOI10.1139/O07-149, lire en ligne, consulté le )
Manoj Cheriyan, Matthew J. Walters, Brian D. Kang et Laura L. Anzaldi, « Directed evolution of a pyruvate aldolase to recognize a long chain acyl substrate », Bioorganic & Medicinal Chemistry, vol. 19, no 21, , p. 6447–6453 (ISSN1464-3391, PMID21944547, PMCIDPMC3209416, DOI10.1016/j.bmc.2011.08.056, lire en ligne, consulté le )
G. MacBeath, P. Kast et D. Hilvert, « Redesigning enzyme topology by directed evolution », Science (New York, N.Y.), vol. 279, no 5358, , p. 1958–1961 (ISSN0036-8075, PMID9506949, lire en ligne, consulté le )
Miguel D. Toscano, Kenneth J. Woycechowsky et Donald Hilvert, « Minimalist active-site redesign: teaching old enzymes new tricks », Angewandte Chemie (International Ed. in English), vol. 46, no 18, , p. 3212–3236 (ISSN1433-7851, PMID17450624, DOI10.1002/anie.200604205, lire en ligne, consulté le )
M. Höss, P. Jaruga, T. H. Zastawny et M. Dizdaroglu, « DNA damage and DNA sequence retrieval from ancient tissues », Nucleic Acids Research, vol. 24, no 7, , p. 1304–1307 (ISSN0305-1048, PMID8614634, lire en ligne, consulté le )
Jesse D. Bloom et Frances H. Arnold, « In the light of directed evolution: pathways of adaptive protein evolution », Proceedings of the National Academy of Sciences of the United States of America, vol. 106 Suppl 1, , p. 9995–10000 (ISSN1091-6490, PMID19528653, PMCIDPMC2702793, DOI10.1073/pnas.0901522106, lire en ligne, consulté le )
K. Salehi-Ashtiani et J. W. Szostak, « In vitro evolution suggests multiple origins for the hammerhead ribozyme », Nature, vol. 414, no 6859, , p. 82–84 (ISSN0028-0836, PMID11689947, DOI10.1038/35102081, lire en ligne, consulté le )
M. Sumper et R. Luce, « Evidence for de novo production of self-replicating and environmentally adapted RNA structures by bacteriophage Qbeta replicase », Proceedings of the National Academy of Sciences of the United States of America, vol. 72, no 1, , p. 162–166 (ISSN0027-8424, PMID1054493, lire en ligne, consulté le )
D. R. Mills, R. L. Peterson et S. Spiegelman, « An extracellular Darwinian experiment with a self-duplicating nucleic acid molecule », Proceedings of the National Academy of Sciences of the United States of America, vol. 58, no 1, , p. 217–224 (ISSN0027-8424, PMID5231602, lire en ligne, consulté le )
J. H. Marden, M. R. Wolf et K. E. Weber, « Aerial performance of Drosophila melanogaster from populations selected for upwind flight ability », The Journal of Experimental Biology, vol. 200, no Pt 21, , p. 2747–2755 (ISSN0022-0949, PMID9418031, lire en ligne, consulté le )
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