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Bornscheuer, U. T.; Huisman, G. W.; Kazlauskas, R. J.; Lutz, S.; Moore, J. C.; Robins, K. (9 de mayo de 2012). «Engineering the third wave of biocatalysis». Nature485 (7397): 185-194. PMID22575958. doi:10.1038/nature11117.
Azevedo R; Lohaus R; Srinivasan S; Dang K; Burch C (2006). «Sexual reproduction selects for robustness and negative epistasis in artificial gene networks». Nature440 (7080): 87-90. PMID16511495. doi:10.1038/nature04488.
Bonhoeffer S; Chappey C; Parkin NT; Whitcomb JM; Petropoulos CJ (2004). «Evidence for positive epistasis in HIV-1». Science306 (5701): 1547-50. PMID15567861. doi:10.1126/science.1101786.
Neet, KE; Koshland DE, Jr (Nov 1966). «The conversion of serine at the active site of subtilisin to cysteine: a "chemical mutation".». Proceedings of the National Academy of Sciences of the United States of America56 (5): 1606-11. PMID5230319. doi:10.1073/pnas.56.5.1606.
Sigal, IS; Harwood, BG; Arentzen, R (Dec 1982). «Thiol-beta-lactamase: replacement of the active-site serine of RTEM beta-lactamase by a cysteine residue.». Proceedings of the National Academy of Sciences of the United States of America79 (23): 7157-60. PMID6818541. doi:10.1073/pnas.79.23.7157.
Reetz, MT; Sanchis, J (22 de septiembre de 2008). «Constructing and analyzing the fitness landscape of an experimental evolutionary process.». Chembiochem : a European journal of chemical biology9 (14): 2260-7. PMID18712749. doi:10.1002/cbic.200800371.
A. S. Kondrashov (1988). «Deleterious mutations and the evolution of sexual reproduction». Nature336 (6198): 435-440. PMID3057385. doi:10.1038/336435a0.
Wade, MJ; Goodnight, CJ (Apr 2006). «Cyto-nuclear epistasis: two-locus random genetic drift in hermaphroditic and dioecious species.». Evolution; international journal of organic evolution60 (4): 643-59. PMID16739448. doi:10.1554/05-019.1.
Horovitz, A (1996). «Double-mutant cycles: a powerful tool for analyzing protein structure and function.». Folding and Design1 (6): R121-6. PMID9080186. doi:10.1016/s1359-0278(96)00056-9.
Tokuriki, N; Tawfik, DS (October 2009). «Stability effects of mutations and protein evolvability.». Current Opinion in Structural Biology19 (5): 596-604. PMID19765975. doi:10.1016/j.sbi.2009.08.003.
Bornscheuer, U. T.; Huisman, G. W.; Kazlauskas, R. J.; Lutz, S.; Moore, J. C.; Robins, K. (9 de mayo de 2012). «Engineering the third wave of biocatalysis». Nature485 (7397): 185-194. PMID22575958. doi:10.1038/nature11117.
Azevedo R; Lohaus R; Srinivasan S; Dang K; Burch C (2006). «Sexual reproduction selects for robustness and negative epistasis in artificial gene networks». Nature440 (7080): 87-90. PMID16511495. doi:10.1038/nature04488.
Bonhoeffer S; Chappey C; Parkin NT; Whitcomb JM; Petropoulos CJ (2004). «Evidence for positive epistasis in HIV-1». Science306 (5701): 1547-50. PMID15567861. doi:10.1126/science.1101786.
Neet, KE; Koshland DE, Jr (Nov 1966). «The conversion of serine at the active site of subtilisin to cysteine: a "chemical mutation".». Proceedings of the National Academy of Sciences of the United States of America56 (5): 1606-11. PMID5230319. doi:10.1073/pnas.56.5.1606.
Sigal, IS; Harwood, BG; Arentzen, R (Dec 1982). «Thiol-beta-lactamase: replacement of the active-site serine of RTEM beta-lactamase by a cysteine residue.». Proceedings of the National Academy of Sciences of the United States of America79 (23): 7157-60. PMID6818541. doi:10.1073/pnas.79.23.7157.
Reetz, MT; Sanchis, J (22 de septiembre de 2008). «Constructing and analyzing the fitness landscape of an experimental evolutionary process.». Chembiochem : a European journal of chemical biology9 (14): 2260-7. PMID18712749. doi:10.1002/cbic.200800371.
A. S. Kondrashov (1988). «Deleterious mutations and the evolution of sexual reproduction». Nature336 (6198): 435-440. PMID3057385. doi:10.1038/336435a0.
Wade, MJ; Goodnight, CJ (Apr 2006). «Cyto-nuclear epistasis: two-locus random genetic drift in hermaphroditic and dioecious species.». Evolution; international journal of organic evolution60 (4): 643-59. PMID16739448. doi:10.1554/05-019.1.
Horovitz, A (1996). «Double-mutant cycles: a powerful tool for analyzing protein structure and function.». Folding and Design1 (6): R121-6. PMID9080186. doi:10.1016/s1359-0278(96)00056-9.