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Volumn , Issue , 2006, Pages 121-162

Combinatorial Approaches and Molecular Evolution of Homogeneous Catalysts

Author keywords

Combinatorial approaches and molecular evolution; Combinatorial catalysis; Phage display methods and catalytic antibodies

Indexed keywords


EID: 84889460521     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470140475.ch6     Document Type: Chapter
Times cited : (1)

References (153)
  • 2
    • 0003509573 scopus 로고    scopus 로고
    • Directed Molecular Evolution of Proteins
    • Wiley- VCH, Weinheim
    • Brakmann, S. and Johnsson, K., Directed Molecular Evolution of Proteins, Wiley- VCH, Weinheim, 2002.
    • (2002)
    • Brakmann, S.1    Johnsson, K.2
  • 3
    • 3042732096 scopus 로고    scopus 로고
    • Directed evolution of nucleic acid enzymes
    • Joyce, G. F., Directed evolution of nucleic acid enzymes, Annu. Rev. Biochem. 73:791-836 (2004).
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 791-836
    • Joyce, G.F.1
  • 4
    • 85018556001 scopus 로고    scopus 로고
    • Catalytic Antibodies
    • Wiley-VCH, Weinheim
    • Keinan, E., Catalytic Antibodies, Wiley-VCH, Weinheim, 2005.
    • (2005)
    • Keinan, E.1
  • 5
    • 84902432376 scopus 로고    scopus 로고
    • Combinatorial methods in catalysis by metal complexes
    • J. A. McCleverty and T. J. Meyer (eds.), Elsevier, Amsterdam
    • Reetz, M. T., Combinatorial methods in catalysis by metal complexes, in Comprehensive Coordination Chemistry II, J. A. McCleverty and T. J. Meyer (eds.), Elsevier, Amsterdam, 2004, Vol. 9, pp. 509-548.
    • (2004) Comprehensive Coordination Chemistry II , vol.9 , pp. 509-548
    • Reetz, M.T.1
  • 6
    • 4043156436 scopus 로고    scopus 로고
    • Enzyme Functionality: Design, Engineering, and Screening, Marcel Dekker
    • New York
    • Svendsen, A., Enzyme Functionality: Design, Engineering, and Screening, Marcel Dekker, New York, 2004.
    • (2004)
    • Svendsen, A.1
  • 8
    • 0026418434 scopus 로고
    • The atom economy-a search for synthetic efficiency
    • Trost, B. M., The atom economy-a search for synthetic efficiency, Science 254:1471-1477 (1991).
    • (1991) Science , vol.254 , pp. 1471-1477
    • Trost, B.M.1
  • 10
    • 0004169474 scopus 로고
    • Homogeneous Catalysis
    • Wiley-Interscience, New York
    • Parshall, G. W. and Ittel, S. D., Homogeneous Catalysis, Wiley-Interscience, New York, 1992.
    • (1992)
    • Parshall, G.W.1    Ittel, S.D.2
  • 11
    • 33746044681 scopus 로고    scopus 로고
    • Nobel Prizes in chemistry; asymmetric hydrogenation recognised!
    • Brown, J. M., Nobel Prizes in chemistry; asymmetric hydrogenation recognised! Adv. Synth. Catal. 343(8):755-756 (2001).
    • (2001) Adv. Synth. Catal. , vol.343 , Issue.8 , pp. 755-756
    • Brown, J.M.1
  • 12
    • 84889468345 scopus 로고    scopus 로고
    • Nobel Prizes in chemistry 2001; asymmetric oxidation rewarded!
    • Marko, I. E., Nobel Prizes in chemistry 2001; asymmetric oxidation rewarded! Adv. Synth. Catal. 343(8):757-758 (2001).
    • (2001) Adv. Synth. Catal. , vol.343 , Issue.8 , pp. 757-758
    • Marko, I.E.1
  • 13
    • 84889345588 scopus 로고    scopus 로고
    • Angew. Chem. Int.
    • Nobel Prizes 2005: Chemistry, physiology or medicine, physics
    • Nobel Prizes 2005: Chemistry, physiology or medicine, physics, Angew. Chem. Int. Ed 44(43):6982 (2005).
    • (2005) , vol.44 , Issue.43 , pp. 6982
  • 14
    • 11244328504 scopus 로고    scopus 로고
    • Homogeneous Catalysis: Understanding the Art, Kluwer, Dordrecht
    • van Leeuwen, P. W. N. M., Homogeneous Catalysis: Understanding the Art, Kluwer, Dordrecht, 2004.
    • (2004)
    • van Leeuwen, P.W.N.M.1
  • 15
    • 33746899513 scopus 로고    scopus 로고
    • Asymmetric hydrogenations-the Monsanto L-Dopa process
    • H.-U. Blaser and E. Schmidt (eds.), Wiley-VCH, Weinheim
    • Knowles, W. S., Asymmetric hydrogenations-the Monsanto L-Dopa process, in Asymmetric Catalysis on Industrial Scale, H.-U. Blaser and E. Schmidt (eds.), Wiley-VCH, Weinheim, 2004, pp. 23-38.
    • (2004) Asymmetric Catalysis on Industrial Scale , pp. 23-38
    • Knowles, W.S.1
  • 16
    • 0025335121 scopus 로고
    • Design and synthesis of a peptide having chymotrypsin-like esterase activity
    • Hahn, K. W., Klis, W. A., and Stewart, J. M., Design and synthesis of a peptide having chymotrypsin-like esterase activity, Science 248(4962):1544-1547 (1990).
    • (1990) Science , vol.248 , Issue.4962 , pp. 1544-1547
    • Hahn, K.W.1    Klis, W.A.2    Stewart, J.M.3
  • 17
    • 84891017895 scopus 로고    scopus 로고
    • Artificial Enzymes
    • Wiley-VCH, Weinheim
    • Breslow, R., Artificial Enzymes, Wiley-VCH, Weinheim, 2005.
    • (2005)
    • Breslow, R.1
  • 19
    • 0032559208 scopus 로고    scopus 로고
    • Catalytic galactose oxidase models: Biomimetic Cu(II)-phenoxyl-radical reactivity
    • Wang, Y., DuBois, J. L., Hedman, B., Hodgson, K. O., and Stack, T. D. P., Catalytic galactose oxidase models: Biomimetic Cu(II)-phenoxyl-radical reactivity, Science 279(5350):537-540 (1998).
    • (1998) Science , vol.279 , Issue.5350 , pp. 537-540
    • Wang, Y.1    DuBois, J.L.2    Hedman, B.3    Hodgson, K.O.4    Stack, T.D.P.5
  • 20
    • 0031678724 scopus 로고    scopus 로고
    • From structural models of galactose oxidase to homogeneous catalysis: Efficient aerobic oxidation of alcohols
    • Chaudhuri, P., Hess, M., Florke, U., and Wieghardt, K., From structural models of galactose oxidase to homogeneous catalysis: Efficient aerobic oxidation of alcohols, Angew. Chem. Int. Ed. 37(16):2217-2220 (1998).
    • (1998) Angew. Chem. Int. Ed. , vol.37 , Issue.16 , pp. 2217-2220
    • Chaudhuri, P.1    Hess, M.2    Florke, U.3    Wieghardt, K.4
  • 22
    • 0035313673 scopus 로고    scopus 로고
    • Industrial catalysis
    • Zaks, A., Industrial catalysis, Curr. Opin. Chem. Biol. 5:130-136 (2001).
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 130-136
    • Zaks, A.1
  • 23
    • 0345422724 scopus 로고
    • Production of fine chemicals using biocatalysis
    • Liese, A. and Filho, M. V., Production of fine chemicals using biocatalysis, Curr. Opin. Biotechnol. 10:595-603 (1990).
    • (1990) Curr. Opin. Biotechnol. , vol.10 , pp. 595-603
    • Liese, A.1    Filho, M.V.2
  • 24
    • 0000592694 scopus 로고
    • Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesis
    • Gerlt, J. A., Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesis, Chem. Rev. 87:1079-1105 (1987).
    • (1987) Chem. Rev. , vol.87 , pp. 1079-1105
    • Gerlt, J.A.1
  • 25
    • 0023645080 scopus 로고
    • Tinkering with enzymes: What are we learning
    • Knowles, J. R., Tinkering with enzymes: What are we learning, Science 236(4806):1252-1258 (1987).
    • (1987) Science , vol.236 , Issue.4806 , pp. 1252-1258
    • Knowles, J.R.1
  • 26
    • 0023847706 scopus 로고
    • Insights into enzyme function from studies on mutants of dihydrofolate reductase
    • Benkovic, S. J., Fierke, C. A., and Naylor, A. M., Insights into enzyme function from studies on mutants of dihydrofolate reductase, Science 239(4844):1105-1110 (1988).
    • (1988) Science , vol.239 , Issue.4844 , pp. 1105-1110
    • Benkovic, S.J.1    Fierke, C.A.2    Naylor, A.M.3
  • 27
    • 0028859754 scopus 로고
    • Inversion of enantioselectivity in hydrolysis of 1,4-dihydropyridines by point mutation of lipase PS
    • Hirose, Y., Kariya, K., Nakanishi, Y., Kurono, Y., and Achiwa, K., Inversion of enantioselectivity in hydrolysis of 1,4-dihydropyridines by point mutation of lipase PS, Tetrahedron Lett. 36:1063-1066 (1995).
    • (1995) Tetrahedron Lett. , vol.36 , pp. 1063-1066
    • Hirose, Y.1    Kariya, K.2    Nakanishi, Y.3    Kurono, Y.4    Achiwa, K.5
  • 28
    • 84889423084 scopus 로고    scopus 로고
    • Concepts for protein engineering
    • A. Svendsen (ed.), A. Svendsen (ed.), Marcel Dekker, New York
    • Lehmann, M., Concepts for protein engineering, in Enzyme Functionality: Design, Engineering, and Screening, A. Svendsen (ed.), Marcel Dekker, New York, 2004, pp. 1-14.
    • (2004) Enzyme Functionality: Design, Engineering, and Screening , pp. 1-14
    • Lehmann, M.1
  • 29
    • 0035136584 scopus 로고    scopus 로고
    • Optimization of new chiral ligands for the copper-catalysed enantioselective conjugate addition of Et2Zn to nitroolefins by high-throughput screening of a parallel library
    • Ongeri, S., Piarulli, U., Jackson, R. F. W., and Gennari, C., Optimization of new chiral ligands for the copper-catalysed enantioselective conjugate addition of Et2Zn to nitroolefins by high-throughput screening of a parallel library, Eur. J. Org. Chem. 2001(4):803-807 (2001).
    • (2001) Eur. J. Org. Chem. , vol.2001 , Issue.4 , pp. 803-807
    • Ongeri, S.1    Piarulli, U.2    Jackson, R.F.W.3    Gennari, C.4
  • 30
    • 0002718095 scopus 로고    scopus 로고
    • Combinatorial screening of homogeneous catalysis and reaction optimization based on multiplexed capillary electrophoresis
    • Zhang, Y., Gong, X., Zhang, H., Larock, R. C., and Yeung, E. S., Combinatorial screening of homogeneous catalysis and reaction optimization based on multiplexed capillary electrophoresis, J. Combin. Chem. 2:450-452 (2000).
    • (2000) J. Combin. Chem. , vol.2 , pp. 450-452
    • Zhang, Y.1    Gong, X.2    Zhang, H.3    Larock, R.C.4    Yeung, E.S.5
  • 31
    • 0037045239 scopus 로고    scopus 로고
    • Discovery of exceptionally efficient catalysts for solvent-free enantioselective hetero-Diels-Alder reaction
    • Long, J., Hu, J., Shen, X., Ji, B., and Ding, K., Discovery of exceptionally efficient catalysts for solvent-free enantioselective hetero-Diels-Alder reaction, J. Am. Chem. Soc. 124(1):10-11 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , Issue.1 , pp. 10-11
    • Long, J.1    Hu, J.2    Shen, X.3    Ji, B.4    Ding, K.5
  • 32
    • 0000951677 scopus 로고
    • Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid
    • USA
    • Geysen, H. M., Meloen, R. H., and Barteling, S. J., Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid, Proc. Natl. Acad. Sci. USA 81(13):3998-4002 (1984).
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , Issue.13 , pp. 3998-4002
    • Geysen, H.M.1    Meloen, R.H.2    Barteling, S.J.3
  • 33
    • 0000478940 scopus 로고
    • General method for the rapid solid-phase synthesis of large numbers of peptides: Specificity of antigen-antibody interaction at the level of individual amino acids
    • USA
    • Houghten, R. A., General method for the rapid solid-phase synthesis of large numbers of peptides: Specificity of antigen-antibody interaction at the level of individual amino acids, Proc. Natl. Acad. Sci. USA 82(15):5131-5135 (1985).
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , Issue.15 , pp. 5131-5135
    • Houghten, R.A.1
  • 34
    • 0028149989 scopus 로고
    • Recursive deconvolution of combinatorial chemical libraries
    • USA
    • Erb, E., Janda, K. D., and Brenner, S., Recursive deconvolution of combinatorial chemical libraries, Proc. Natl. Acad. Sci. USA 91:11422-11426 (1994).
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 11422-11426
    • Erb, E.1    Janda, K.D.2    Brenner, S.3
  • 35
    • 84868141481 scopus 로고    scopus 로고
    • Introduction to combinatorial chemistry
    • K. C. Nicolaou, R. Hanko, and W. Hartwig (eds.),Wiley-VCH, Weinheim
    • Coffen, D. L. and Luithle, J. E., Introduction to combinatorial chemistry, in Handbook of Combinatorial Chemistry, K. C. Nicolaou, R. Hanko, and W. Hartwig (eds.), Wiley-VCH, Weinheim, 2002, Vol. 1, pp. 10-23.
    • (2002) Handbook of Combinatorial Chemistry , vol.1 , pp. 10-23
    • Coffen, D.L.1    Luithle, J.E.2
  • 36
    • 10244273514 scopus 로고
    • A general solid-phase synthesis strategy for the preparation of 2-pyrrolidinemethanol ligands
    • Liu, G. and Ellman, J. A., A general solid-phase synthesis strategy for the preparation of 2-pyrrolidinemethanol ligands, J. Org. Chem. 60(24):7712-7713 (1995).
    • (1995) J. Org. Chem. , vol.60 , Issue.24 , pp. 7712-7713
    • Liu, G.1    Ellman, J.A.2
  • 37
    • 0003554758 scopus 로고    scopus 로고
    • Schiff base catalysts for the asymmetric Strecker reaction identified and optimized from parallel synthetic libraries
    • Sigman, M. S. and Jacobsen, E. N., Schiff base catalysts for the asymmetric Strecker reaction identified and optimized from parallel synthetic libraries, J. Am. Chem. Soc. 120(19):4901-4902 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , Issue.19 , pp. 4901-4902
    • Sigman, M.S.1    Jacobsen, E.N.2
  • 38
    • 0032086681 scopus 로고    scopus 로고
    • Transition-metalmediated reactions in combinatorial synthesis
    • Andres, C. J., Whitehouse, D. L., and Deshpande, M. S., Transition-metalmediated reactions in combinatorial synthesis, Curr. Opin. Chem. Biol. 2(3):353- 362 (1998).
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , Issue.3 , pp. 353-362
    • Andres, C.J.1    Whitehouse, D.L.2    Deshpande, M.S.3
  • 39
    • 52849090660 scopus 로고    scopus 로고
    • Combinatorial-parallel approaches to catalyst discovery and development
    • Gilbertson, S. R., Combinatorial-parallel approaches to catalyst discovery and development, Progress Inorg. Chem. 50:433-471 (2001).
    • (2001) Progress Inorg. Chem. , vol.50 , pp. 433-471
    • Gilbertson, S.R.1
  • 40
    • 0037208308 scopus 로고    scopus 로고
    • Property distributions: Differences between drugs, natural products, and molecules from combinatorial chemistry
    • Feher, M. and Schmidt, J. M., Property distributions: Differences between drugs, natural products, and molecules from combinatorial chemistry, J. Chem. Inform. Comput. Sci. 43(1):218-227 (2003).
    • (2003) J. Chem. Inform. Comput. Sci. , vol.43 , Issue.1 , pp. 218-227
    • Feher, M.1    Schmidt, J.M.2
  • 41
    • 33947547892 scopus 로고
    • Chem. Eng. News
    • Pauling, L., Molecular architecture and biological reactions, Chem. Eng. News 24:1375-1377 (1946).
    • (1946) , vol.24 , pp. 1375-1377
    • Pauling, L.1
  • 42
    • 0003408336 scopus 로고
    • Catalysis in Chemistry and Enzymology
    • McGraw-Hill, New York
    • Jencks, W. P., Catalysis in Chemistry and Enzymology, McGraw-Hill, New York, 1969, p. 288.
    • (1969) , pp. 288
    • Jencks, W.P.1
  • 43
    • 0022991435 scopus 로고
    • Selective chemical catalysis by an antibody
    • Pollack, S. J., Jacobs, J. W., and Schultz, P. G., Selective chemical catalysis by an antibody, Science 234(4783):1570-1573 (1986).
    • (1986) Science , vol.234 , Issue.4783 , pp. 1570-1573
    • Pollack, S.J.1    Jacobs, J.W.2    Schultz, P.G.3
  • 48
    • 0000907895 scopus 로고
    • Crystal and molecular structure of a freebase N-methylporphyrin; N-methyl-5,10,15,20-tetra(p-bromophenyl)porphyrin
    • Lavallee, D. K. and Anderson, O. P., Crystal and molecular structure of a freebase N-methylporphyrin; N-methyl-5,10,15,20-tetra(p-bromophenyl)porphyrin, J. Am. Chem. Soc. 104(17):4707-4708 (1982).
    • (1982) J. Am. Chem. Soc. , vol.104 , Issue.17 , pp. 4707-4708
    • Lavallee, D.K.1    Anderson, O.P.2
  • 49
    • 0025170858 scopus 로고
    • Antibody-catalyzed porphyrin metallation
    • Cochran, A. G. and Schultz, P. G., Antibody-catalyzed porphyrin metallation, Science 249:781-783 (1990).
    • (1990) Science , vol.249 , pp. 781-783
    • Cochran, A.G.1    Schultz, P.G.2
  • 50
    • 0023510298 scopus 로고
    • Evolutionary and somatic selection of the antibody repertoire in the mouse
    • Rajewsky, K., Forester, I., and Cumano, A., Evolutionary and somatic selection of the antibody repertoire in the mouse, Science 238(4830):1088-1094 (1987).
    • (1987) Science , vol.238 , Issue.4830 , pp. 1088-1094
    • Rajewsky, K.1    Forester, I.2    Cumano, A.3
  • 51
    • 0023513107 scopus 로고
    • Development of the primary antibody repertoire
    • Alt, F. W., Blackwell, T. K., and Yancopoulos, G. D., Development of the primary antibody repertoire, Science 238(4830):1079-1087 (1987).
    • (1987) Science , vol.238 , Issue.4830 , pp. 1079-1087
    • Alt, F.W.1    Blackwell, T.K.2    Yancopoulos, G.D.3
  • 52
    • 0022271336 scopus 로고
    • Origin of immune diversity: Genetic variation and selection
    • Honjo, T. and Habu, S., Origin of immune diversity: Genetic variation and selection, Annu. Rev. Biochem. 54:803-830 (1985).
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 803-830
    • Honjo, T.1    Habu, S.2
  • 53
    • 84889350465 scopus 로고    scopus 로고
    • Overview: Amplification of antibody genes
    • in Phage Display: A Laboratory Manual, C. F. Barbas III, D. R. Burton, J. K. Scott, and G. J. Silverman (eds.), Cold Spring Harbor Laboratory Press, New York
    • Burton, D. R., Overview: Amplification of antibody genes, in Phage Display: A Laboratory Manual, C. F. Barbas III, D. R. Burton, J. K. Scott, and G. J. Silverman (eds.), Cold Spring Harbor Laboratory Press, New York, 2001, pp. 8.1-8.3.
    • (2001)
    • Burton, D.R.1
  • 54
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler, G. and Milstein, C., Continuous cultures of fused cells secreting antibody of predefined specificity, Nature 256(5517):495-497 (1975).
    • (1975) Nature , vol.256 , Issue.5517 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 55
    • 0028435991 scopus 로고
    • Hapten design for the generation of catalytic antibodies
    • Thomas, N. R., Hapten design for the generation of catalytic antibodies, Appl. Biochem. Biotechnol. 47:345-372 (1994).
    • (1994) Appl. Biochem. Biotechnol. , vol.47 , pp. 345-372
    • Thomas, N.R.1
  • 56
    • 0029018511 scopus 로고
    • Transition-state stabilization as a measure of the efficiency of antibody catalysis
    • Stewart, J. D. and Benkovic, S. J., Transition-state stabilization as a measure of the efficiency of antibody catalysis, Nature 375(6530):388-391 (1995).
    • (1995) Nature , vol.375 , Issue.6530 , pp. 388-391
    • Stewart, J.D.1    Benkovic, S.J.2
  • 57
    • 0026263936 scopus 로고
    • Approaches to the design of semisynthetic metal-dependent catalytic antibodies
    • in Catalytic Antibodies, D. J. Chadwick and J. Marsh (eds.), Wiley, Chichester, UK
    • Nakayam, G. R. and Schultz, P. G.,Approaches to the design of semisynthetic metal-dependent catalytic antibodies, in Catalytic Antibodies, D. J. Chadwick and J. Marsh (eds.), Wiley, Chichester, UK, 1991; Ciba Foundation Symp. 159, pp. 72-90.
    • (1991) Ciba Foundation Symp. , vol.159 , pp. 72-90
    • Nakayam, G.R.1    Schultz, P.G.2
  • 58
    • 0001352216 scopus 로고
    • Antibody bait and switch catalysis: A survey of antigens capable of inducing abzymes with acyl-transfer properties
    • Janda, K. D., Weinhouse, M. I., Danon, T., Pacelli, K. A., and Schloeder, D. M., Antibody bait and switch catalysis: A survey of antigens capable of inducing abzymes with acyl-transfer properties, J. Am. Chem. Soc. 113:5427-5434 (1991).
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5427-5434
    • Janda, K.D.1    Weinhouse, M.I.2    Danon, T.3    Pacelli, K.A.4    Schloeder, D.M.5
  • 59
    • 0026294507 scopus 로고
    • Structural aspects of antibodies and antibody-antigen complexesApproaches to the design of semisynthetic metal-dependent catalytic antibodies
    • in Catalytic Antibodies, D. J. Chadwick and J. Marsh (eds.), Wiley, Chichester, UK, 1991
    • Wilson, I. A., Stanfield, R. L., Rini, J. M., Areval, J. H., Schulze-Gahmen, U., Fremont, D. H., and Stura, E. A., Structural aspects of antibodies and antibody-antigen complexes, in Catalytic Antibodies, D. J. Chadwick and J. Marsh (eds.), Wiley, Chichester, UK, 1991; Ciba Foundation Symp. 159, pp. 13-39.
    • (1991) Ciba Foundation Symp. , vol.159 , pp. 13-39
    • Wilson, I.A.1    Stanfield, R.L.2    Rini, J.M.3    Areval, J.H.4    Schulze-Gahmen, U.5    Fremont, D.H.6    Stura, E.A.7
  • 60
    • 0004204457 scopus 로고
    • Introduction to Protein Structure
    • Garland Publishing, New York
    • Tooze, B. C., Introduction to Protein Structure, Garland Publishing, New York, 1991.
    • (1991)
    • Tooze, B.C.1
  • 61
    • 85018194020 scopus 로고    scopus 로고
    • Production of monoclonal catalytic antibodies: Principles and practice, in Catalytic Antibodies
    • Weinheim
    • Kubitz, D. and Keinan, E., Production of monoclonal catalytic antibodies: Principles and practice, in Catalytic Antibodies, E. Keinan (ed.), Wiley-VCH, Weinheim, 2005; pp. 491-504.
    • (2005) Wiley-VCH , pp. 491-504
    • Kubitz, D.1    Keinan, E.2
  • 62
    • 84889265268 scopus 로고    scopus 로고
    • Antibody libraries, in Phage Display: A Laboratory Manual, C. F. Barbas III
    • D. R. Burton, J. K. Scott, and G. J. Silverman (eds.), Cold Spring Harbor Laboratory Press, New York
    • Burton, D. R., Antibody libraries, in Phage Display: A Laboratory Manual, C. F. Barbas III, D. R. Burton, J. K. Scott, and G. J. Silverman (eds.), Cold Spring Harbor Laboratory Press, New York, 2001, pp. 3.1-3.18.
    • (2001)
    • Burton, D.R.1
  • 63
    • 0026641471 scopus 로고
    • Molecular evolution of proteins on filamentous phage. Mimicking the strategy of the immune system
    • Marks, J. D., Hoogenboom, H. R., Griffiths, A. D., and Winter, G., Molecular evolution of proteins on filamentous phage. Mimicking the strategy of the immune system, J. Biol. Chem. 267(23):16007-16010 (1992).
    • (1992) J. Biol. Chem. , vol.267 , Issue.23 , pp. 16007-16010
    • Marks, J.D.1    Hoogenboom, H.R.2    Griffiths, A.D.3    Winter, G.4
  • 64
    • 0014107493 scopus 로고
    • An extracellular Darwinian experiment with a self-duplicating nucleic acid molecule
    • USA
    • Mills, D. R., Peterson, R. L., and Spiegelman, S., An extracellular Darwinian experiment with a self-duplicating nucleic acid molecule, Proc. Natl. Acad. Sci. USA 58:217-224 (1967).
    • (1967) Proc. Natl. Acad. Sci. , vol.58 , pp. 217-224
    • Mills, D.R.1    Peterson, R.L.2    Spiegelman, S.3
  • 65
    • 84974325243 scopus 로고
    • Experimental analysis of precellular evolution
    • Spiegelman, S., Experimental analysis of precellular evolution, Quart. Rev. Biophys. 4:213-253 (1971).
    • (1971) Quart. Rev. Biophys. , vol.4 , pp. 213-253
    • Spiegelman, S.1
  • 67
    • 0842334666 scopus 로고    scopus 로고
    • Survial of the fittest molecule
    • Stemmer, W. and Holland, B., Survial of the fittest molecule, Am. Sci. 91:526-533 (2003).
    • (2003) Am. Sci. , vol.91 , pp. 526-533
    • Stemmer, W.1    Holland, B.2
  • 68
    • 0036973289 scopus 로고    scopus 로고
    • The product of the natural reaction catalyzed by 4-oxalocrotonate tautomerase becomes an affinity label of its mutant
    • Brik, A., Dawson, P. E., and Keinan, E., The product of the natural reaction catalyzed by 4-oxalocrotonate tautomerase becomes an affinity label of its mutant, Bioorg. Med. Chem. 10:3891-3917 (2002).
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 3891-3917
    • Brik, A.1    Dawson, P.E.2    Keinan, E.3
  • 69
    • 85018193901 scopus 로고    scopus 로고
    • In vitro evolution of catalytic antibodies and other proteins via combinatorial libraries
    • in Catalytic Antibodies, E. Keinan (ed.), Wiley-VCH, Weinheim
    • Piran, R. and Keinan, E., In vitro evolution of catalytic antibodies and other proteins via combinatorial libraries, in Catalytic Antibodies, E. Keinan (ed.), Wiley-VCH, Weinheim, 2005, pp. 243-283.
    • (2005) , pp. 243-283
    • Piran, R.1    Keinan, E.2
  • 70
    • 0003463297 scopus 로고
    • Adaptation in Natural and Artificial Systems
    • MIT Press, Cambridge, MA
    • Holland, J. H., Adaptation in Natural and Artificial Systems, MIT Press, Cambridge, MA, 1992.
    • (1992)
    • Holland, J.H.1
  • 71
    • 0029969577 scopus 로고    scopus 로고
    • Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
    • You, L. and Arnold, F. H., Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide, Protein Eng. 9:77-83 (1996).
    • (1996) Protein Eng. , vol.9 , pp. 77-83
    • You, L.1    Arnold, F.H.2
  • 72
    • 85018193683 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • E. Keinan (ed.), Wiley-VCH, Weinheim
    • Hilvert, D., Critical analysis of antibody catalysis, in Catalytic Antibodies, E. Keinan (ed.), Wiley-VCH, Weinheim, 2005, pp. 30-71.
    • (2005) Catalytic Antibodies , pp. 30-71
    • Hilvert, D.1
  • 73
    • 18044390504 scopus 로고    scopus 로고
    • Directed evolution: Selecting today's biocatalysts
    • Otten, L. G. and Quax, W. J., 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
  • 74
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. C., Rapid evolution of a protein in vitro by DNA shuffling, Nature 370(6488):389-391 (1994).
    • (1994) Nature , vol.370 , Issue.6488 , pp. 389-391
    • Stemmer, W.P.C.1
  • 75
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • USA
    • Stemmer, W. P. C., DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution, Proc. Natl. Acad. Sci. USA 91(22):10747-10751 (1994).
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , Issue.22 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 76
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri, A., Raillard, S.-A., Bermudez, E., and Stemmer, W. P. C., DNA shuffling of a family of genes from diverse species accelerates directed evolution, Nature 391(6664):288-291 (1998).
    • (1998) Nature , vol.391 , Issue.6664 , pp. 288-291
    • Crameri, A.1    Raillard, S.-A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 77
    • 0032814117 scopus 로고    scopus 로고
    • Novel family shuffling methods for the in vitro evolution of enzymes
    • Kikuchi, M., Ohnishi, K., and Harayama, S., Novel family shuffling methods for the in vitro evolution of enzymes, Gene 236(1):159-167 (1999).
    • (1999) Gene , vol.236 , Issue.1 , pp. 159-167
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 78
    • 0033964975 scopus 로고    scopus 로고
    • An effective family shuffling method using single-stranded DNA
    • Kikuchi, M., Ohnishi, K., and Harayama, S., An effective family shuffling method using single-stranded DNA, Gene 243(1-2):133-137 (2000).
    • (2000) Gene , vol.243 , Issue.1-2 , pp. 133-137
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 79
    • 0029124199 scopus 로고
    • Random recombination of antibody single chain Fv sequences after fragmentation with DNase1 in the presence of Mn2+
    • Lorimer, I. A. J. and Pastan, I., Random recombination of antibody single chain Fv sequences after fragmentation with DNase1 in the presence of Mn2+, Nucl. Acids Res. 23(15):3067-3068 (1995).
    • (1995) Nucl. Acids Res. , vol.23 , Issue.15 , pp. 3067-3068
    • Lorimer, I.A.J.1    Pastan, I.2
  • 80
    • 0037114242 scopus 로고    scopus 로고
    • Random DNA fragmentation with endonuclease V: Application to DNA shuffling
    • Miyazaki, K., Random DNA fragmentation with endonuclease V: Application to DNA shuffling, Nucl. Acids Res. 30(24):e139 (2002).
    • (2002) Nucl. Acids Res. , vol.30 , Issue.24
    • Miyazaki, K.1
  • 81
    • 0032518181 scopus 로고    scopus 로고
    • Random-priming in vitro recombination: An effective tool for directed evolution
    • Shao, Z., Zhao, H., Giver, L., and Arnold, F. H., Random-priming in vitro recombination: An effective tool for directed evolution, Nucl. Acids Res. 26(2):681-683 (1998).
    • (1998) Nucl. Acids Res. , vol.26 , Issue.2 , pp. 681-683
    • Shao, Z.1    Zhao, H.2    Giver, L.3    Arnold, F.H.4
  • 83
    • 0035949702 scopus 로고    scopus 로고
    • Creating multiple-crossover DNA libraries independent of sequence identity
    • USA
    • Lutz, S., Ostermeier, M., Moore, G. L., Maranas, C. D., and Benkovic, S. J., Creating multiple-crossover DNA libraries independent of sequence identity, Proc. Natl. Acad. Sci. USA 98(20):11248-11253 (2001).
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , Issue.20 , pp. 11248-11253
    • Lutz, S.1    Ostermeier, M.2    Moore, G.L.3    Maranas, C.D.4    Benkovic, S.J.5
  • 84
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., Giver, L., Shao, Z., Affholter, J. A., and Arnold, F. H., Molecular evolution by staggered extension process (StEP) in vitro recombination, Nature Biotechnol. 16(3):258-261 (1998).
    • (1998) Nature Biotechnol. , vol.16 , Issue.3 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5
  • 86
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • Ostermeier, M., Shim, J. H., and Benkovic, S. J., A combinatorial approach to hybrid enzymes independent of DNA homology, Nature Biotechnol. 17(12):1205- 1209 (1999).
    • (1999) Nature Biotechnol. , vol.17 , Issue.12 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.H.2    Benkovic, S.J.3
  • 87
    • 0035866186 scopus 로고    scopus 로고
    • Rapid generation of incremental truncation libraries for protein engineering using α-phosphothioate nucleotides
    • Lutz, S., Ostermeier, M., and Benkovic, S. J., Rapid generation of incremental truncation libraries for protein engineering using α-phosphothioate nucleotides, Nucl. Acids Res. 29:16(2001).
    • (2001) Nucl. Acids Res. , vol.29 , pp. 16
    • Lutz, S.1    Ostermeier, M.2    Benkovic, S.J.3
  • 88
    • 0035025314 scopus 로고    scopus 로고
    • Libraries of hybrid proteins from distantly related sequences
    • Sieber, V., Martinez, C. A., and Arnold, F. H., Libraries of hybrid proteins from distantly related sequences, Nature Biotechnol. 19:456-460 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 456-460
    • Sieber, V.1    Martinez, C.A.2    Arnold, F.H.3
  • 89
    • 0035014185 scopus 로고    scopus 로고
    • Directed evolution of proteins by exon shuffling
    • Kolkman, J. A. and Stemmer, W. P. C., Directed evolution of proteins by exon shuffling, Nature Biotechnol. 19(5):423-428 (2001).
    • (2001) Nature Biotechnol. , vol.19 , Issue.5 , pp. 423-428
    • Kolkman, J.A.1    Stemmer, W.P.C.2
  • 90
    • 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. H., and Bergquist, P. L., 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.H.2    Bergquist, P.L.3
  • 91
    • 0038799745 scopus 로고    scopus 로고
    • General method for sequence-independent sitedirected chimeragenesis
    • Hiraga, K. and Arnold, F. H., General method for sequence-independent sitedirected chimeragenesis, J. Mol. Biol. 330(2):287-296 (2003).
    • (2003) J. Mol. Biol. , vol.330 , Issue.2 , pp. 287-296
    • Hiraga, K.1    Arnold, F.H.2
  • 92
    • 0037412178 scopus 로고    scopus 로고
    • Construction of block-shuffled libraries of DNA for evolutionary protein engineering: Y-ligation-based block shuffling
    • Kitamura, K., Kinoshita, Y., Narasaki, S., Nemoto, N., Husimi, Y., and Nishigaki, K., Construction of block-shuffled libraries of DNA for evolutionary protein engineering: Y-ligation-based block shuffling, Protein Eng. 15(10):843-853 (2003).
    • (2003) Protein Eng. , vol.15 , Issue.10 , pp. 843-853
    • Kitamura, K.1    Kinoshita, Y.2    Narasaki, S.3    Nemoto, N.4    Husimi, Y.5    Nishigaki, K.6
  • 93
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based combinatorial protein engineering (SCOPE)
    • O'Maille, P. E., Bakhtina, M., and Tsai, M.-D., Structure-based combinatorial protein engineering (SCOPE). J. Mol. Biol. 321(4):677-691 (2002).
    • (2002) J. Mol. Biol. , vol.321 , Issue.4 , pp. 677-691
    • O'Maille, P.E.1    Bakhtina, M.2    Tsai, M.-D.3
  • 94
    • 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., Pompon, D., and Truan, G., 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, Nucl. Acids Res. 28:E88 (2000).
    • (2000) Nucl. Acids Res. , vol.28
    • Abecassis, V.1    Pompon, D.2    Truan, G.3
  • 96
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer, W. P. C., Crameri, A., Ha, K. D., Brennan, T. M., and Heyneker, H. L., Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides, Gene 164(1):46-53 (1995).
    • (1995) Gene , vol.164 , Issue.1 , pp. 46-53
    • Stemmer, W.P.C.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 99
    • 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., 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
  • 100
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • Chen, K. and 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(12):5618-5622 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , Issue.12 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 101
    • 0001270261 scopus 로고    scopus 로고
    • Design by directed evolution
    • Arnold, F. H., Design by directed evolution, Acc. Chem. Res. 31:125-131 (1998).
    • (1998) Acc. Chem. Res. , vol.31 , pp. 125-131
    • Arnold, F.H.1
  • 102
    • 0035910597 scopus 로고    scopus 로고
    • Combinatorial and evolution-based methods in the creation of enantioselective catalysts
    • Reetz, M. T., Combinatorial and evolution-based methods in the creation of enantioselective catalysts, Angew. Chem. Int. Ed. 40:284-310 (2001).
    • (2001) Angew. Chem. Int. , vol.40 , pp. 284-310
    • Reetz, M.T.1
  • 103
    • 0005210578 scopus 로고    scopus 로고
    • Directed evolution as a means to create enantioselective enzymes for use in organic chemistry
    • S. Brakmann and K. Johnsson (eds.), Wiley-VCH, Weinheim
    • Reetz, M. T., Directed evolution as a means to create enantioselective enzymes for use in organic chemistry, in Directed Molecular Evolution of Proteins, S. Brakmann and K. Johnsson (eds.), Wiley-VCH, Weinheim, 2002, pp. 245-279.
    • (2002) Directed Molecular Evolution of Proteins , pp. 245-279
    • Reetz, M.T.1
  • 104
    • 0003903343 scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • Cold Spring Harbor Laboratory Press, New York
    • Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, New York, 1989, Vols. 1-3.
    • (1989) , vol.1-3
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 105
    • 11344295557 scopus 로고    scopus 로고
    • Introduction to protein engineering
    • J. L. Cleland and C. S. Craik (eds.), , Wiley-Liss, New York
    • Cleland, J. L., Jones, A. J. S., and Craik, C. S., Introduction to protein engineering, in Protein Engineering: Principles and Practice, J. L. Cleland and C. S. Craik (eds.), Wiley-Liss, New York, 1996, pp. 1-32.
    • (1996) Protein Engineering: Principles and Practice , pp. 1-32
    • Cleland, J.L.1    Jones, A.J.S.2    Craik, C.S.3
  • 106
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • Moore, J. C. and Arnold, F. H., Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents, Nature Biotechnol. 14:458-467 (1996).
    • (1996) Nature Biotechnol. , vol.14 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 107
    • 1942503297 scopus 로고    scopus 로고
    • Controlling the enantioselectivity of enzymes by directed evolution: Practical and theoretical ramifications
    • USA
    • Reetz, M. T., Controlling the enantioselectivity of enzymes by directed evolution: Practical and theoretical ramifications, Proc. Natl. Acad. Sci. USA 101(16):5716- 5722 (2004).
    • (2004) , vol.101 , Issue.16 , pp. 5716-5722
    • Reetz, M.T.1
  • 108
    • 0032491867 scopus 로고    scopus 로고
    • Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution
    • Reetz, M. T., Zonta, A., Schimossek, K., Jaeger, K.-E., and Liebeton, K., Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution, Angew. Chem. Int. Ed. 36(24):2830-2832 (1997).
    • (1997) Angew. Chem. Int. , vol.36 , Issue.24 , pp. 2830-2832
    • Reetz, M.T.1    Zonta, A.2    Schimossek, K.3    Jaeger, K.-E.4    Liebeton, K.5
  • 109
    • 0034603040 scopus 로고    scopus 로고
    • Enantioselective enzymes for organic synthesis created by directed evolution
    • Reetz, M. T. and Jaeger, K.-E., Enantioselective enzymes for organic synthesis created by directed evolution, Chem. Eur. J. 6:407-412 (2000).
    • (2000) Chem. Eur. J. , vol.6 , pp. 407-412
    • Reetz, M.T.1    Jaeger, K.-E.2
  • 110
    • 0035930698 scopus 로고    scopus 로고
    • Complete reversal of enantioselectivity of an enzyme-catalyzed reaction by directed evolution
    • Zha, D., Wilensek, S., Hermes, M., Jaeger, K.-E., and Reetz, M. T., Complete reversal of enantioselectivity of an enzyme-catalyzed reaction by directed evolution, Chem. Commun. 2001(24):2664-2665 (2001).
    • (2001) Chem. Commun. , vol.2001 , Issue.24 , pp. 2664-2665
    • Zha, D.1    Wilensek, S.2    Hermes, M.3    Jaeger, K.-E.4    Reetz, M.T.5
  • 112
    • 0001654813 scopus 로고
    • Filamentous bacteriophage
    • in The Bacteriophages, R. Calendar (ed.), Plenum Press, New York
    • Model, P. and Russel, M., Filamentous bacteriophage, in The Bacteriophages, R. Calendar (ed.), Plenum Press, New York, 1988, Vol. 2, pp. 375-456.
    • (1988) , vol.2 , pp. 375-456
    • Model, P.1    Russel, M.2
  • 113
    • 0000398140 scopus 로고
    • Structure and assembly of the class 1 filamentous bacteriophage
    • in Virus Structure and Assembly, S. Casjens (ed.), Jones & Bartlett, Boston
    • Webster, R. E. and Lopez, J., Structure and assembly of the class 1 filamentous bacteriophage, in Virus Structure and Assembly, S. Casjens (ed.), Jones & Bartlett, Boston, 1985, pp. 235-268.
    • (1985) , pp. 235-268
    • Webster, R.E.1    Lopez, J.2
  • 115
    • 0033199842 scopus 로고    scopus 로고
    • Processing and functional display of the 86 kDa heterodimeric penicillin G acylase on the surface of phage fd
    • Verhaert, R. M. D., van Duin, J., and Quax, W. J., Processing and functional display of the 86 kDa heterodimeric penicillin G acylase on the surface of phage fd, Biochem. J. 342(2):415-422 (1999).
    • (1999) Biochem. J. , vol.342 , Issue.2 , pp. 415-422
    • Verhaert, R.M.D.1    van Duin, J.2    Quax, W.J.3
  • 116
    • 0037150506 scopus 로고    scopus 로고
    • Antibody design by man and nature
    • Wentworth, Jr., P., Antibody design by man and nature, Science 296(5576):2247- 2249 (2002).
    • (2002) Science , vol.296 , Issue.5576 , pp. 2247-2249
    • Wentworth Jr., P.1
  • 117
    • 0042820890 scopus 로고    scopus 로고
    • Investigation of phage display for the directed evolution of enzymes
    • S. Brakmann and K. Johnsson (eds.), Wiley-VCH, Weinheim
    • Soumillion, P. and Fastrez, J., Investigation of phage display for the directed evolution of enzymes, in Directed Molecular Evolution of Proteins, S. Brakmann and K. Johnsson (eds.), Wiley-VCH, Weinheim, 2002, pp. 79-110.
    • (2002) Directed Molecular Evolution of Proteins , pp. 79-110
    • Soumillion, P.1    Fastrez, J.2
  • 118
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
    • USA
    • Baca, M., Scanlan, T. S., Stephenson, R. C., and Wells, J. A., Phage display of a catalytic antibody to optimize affinity for transition-state analog binding, Proc. Natl. Acad. Sci. USA 94:10063-10068 (1997).
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 10063-10068
    • Baca, M.1    Scanlan, T.S.2    Stephenson, R.C.3    Wells, J.A.4
  • 120
    • 0020417286 scopus 로고
    • Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymena
    • Kruger, K., Grabowski, P. J., Zaug, A. J., Sands, J., Gottschling, D. E., and Cech, T. R., Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymena, Cell 31:147-157 (1982).
    • (1982) Cell , vol.31 , pp. 147-157
    • Kruger, K.1    Grabowski, P.J.2    Zaug, A.J.3    Sands, J.4    Gottschling, D.E.5    Cech, T.R.6
  • 121
    • 0022649937 scopus 로고
    • The intervening sequence RNA of Tetrahymena is an enzyme
    • Zaug, A. J. and Cech, T. R., The intervening sequence RNA of Tetrahymena is an enzyme, Science 231:470-475 (1986).
    • (1986) Science , vol.231 , pp. 470-475
    • Zaug, A.J.1    Cech, T.R.2
  • 122
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., and Altman, S., The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme, Cell 35:849-857 (1983).
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 123
    • 0000917638 scopus 로고    scopus 로고
    • In vitro selection of catalytic polynucleotides
    • Breaker, R. R., In vitro selection of catalytic polynucleotides, Chem. Rev. 97:371- 390 (1997).
    • (1997) Chem. Rev. , vol.97 , pp. 371-390
    • Breaker, R.R.1
  • 124
    • 0025332385 scopus 로고
    • Selection in vitro of an RNA enzyme that specifically cleaves single-stranded DNA
    • Robertson, D. L. and Joyce, G. F., Selection in vitro of an RNA enzyme that specifically cleaves single-stranded DNA, Nature 344(6265):367-368 (1990).
    • (1990) Nature , vol.344 , Issue.6265 , pp. 367-368
    • Robertson, D.L.1    Joyce, G.F.2
  • 125
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington, A. D. and Szostak, J. W., In vitro selection of RNA molecules that bind specific ligands, Nature 346(6287):818-822 (1990).
    • (1990) Nature , vol.346 , Issue.6287 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 126
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. and Gold, L., Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase, Science 249(4968):505- 510 (1990).
    • (1990) Science , vol.249 , Issue.4968 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 127
  • 128
    • 0027488624 scopus 로고
    • Isolation of new ribozymes from a large pool of random sequences
    • Bartel, D. P. and Szostak, J. W., Isolation of new ribozymes from a large pool of random sequences, Science 261(5127):1411-1418 (1993).
    • (1993) Science , vol.261 , Issue.5127 , pp. 1411-1418
    • Bartel, D.P.1    Szostak, J.W.2
  • 129
    • 0003648954 scopus 로고    scopus 로고
    • Bioconjugate Techniques
    • Academic Press, San Diego
    • Hermanson, G. T., Bioconjugate Techniques, Academic Press, San Diego, 1996.
    • (1996)
    • Hermanson, G.T.1
  • 130
    • 0030832285 scopus 로고    scopus 로고
    • In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules
    • USA
    • Haller, A. A. and Sarnow, P., In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules, Proc. Natl. Acad. Sci. USA 94(16):8521-8526 (1997).
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , Issue.16 , pp. 8521-8526
    • Haller, A.A.1    Sarnow, P.2
  • 131
    • 0032853242 scopus 로고    scopus 로고
    • In vitro selection of functional nucleic acids
    • Wilson, D. S. and Szostak, J. W., In vitro selection of functional nucleic acids, Annu. Rev. Biochem. 68:611-647 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 611-647
    • Wilson, D.S.1    Szostak, J.W.2
  • 132
    • 0030072640 scopus 로고    scopus 로고
    • Chance and necessity in the selection of nucleic acid catalysts
    • Lorsch, J. R. and Szostak, J. W., Chance and necessity in the selection of nucleic acid catalysts, Acc. Chem. Res. 29:103-110 (1996).
    • (1996) Acc. Chem. Res. , vol.29 , pp. 103-110
    • Lorsch, J.R.1    Szostak, J.W.2
  • 133
    • 0030498356 scopus 로고    scopus 로고
    • The Ca2+ ion as a cofactor for a novel RNAcleaving deoxyribozyme
    • Faulhammer, D. and Famulok, M., The Ca2+ ion as a cofactor for a novel RNAcleaving deoxyribozyme, Angew. Chem. Int. Ed. 35:2837-2841 (1996).
    • (1996) Angew. Chem. Int. , vol.35 , pp. 2837-2841
    • Faulhammer, D.1    Famulok, M.2
  • 134
    • 0032568656 scopus 로고    scopus 로고
    • An amino acid as a cofactor for a catalytic polynucleotide
    • USA
    • Roth, A. and Breaker, R. R., An amino acid as a cofactor for a catalytic polynucleotide, Proc. Natl. Acad. Sci. USA 95(11):6027-6031 (1998).
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , Issue.11 , pp. 6027-6031
    • Roth, A.1    Breaker, R.R.2
  • 135
    • 0008451711 scopus 로고    scopus 로고
    • Porphyrin metallation catalyzed by a small RNA molecule
    • Conn, M. M., Prudent, J. R., and Schultz, P. G., Porphyrin metallation catalyzed by a small RNA molecule, J. Am. Chem. Soc. 118:7012-7013 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7012-7013
    • Conn, M.M.1    Prudent, J.R.2    Schultz, P.G.3
  • 136
    • 0029746712 scopus 로고    scopus 로고
    • A catalytic DNA for porphyrin metallation
    • Li, Y. and Sen, D., A catalytic DNA for porphyrin metallation, Nature Struct. Biol. 3:743-747 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 743-747
    • Li, Y.1    Sen, D.2
  • 137
    • 0003481596 scopus 로고
    • Enzyme Structure and Mechanism
    • 2nd ed.; Freeman, New York
    • Fersht, A., Enzyme Structure and Mechanism, 2nd ed.; Freeman, New York, 1985.
    • (1985)
    • Fersht, A.1
  • 138
    • 6344219578 scopus 로고    scopus 로고
    • Deoxyribozymes: DNA catalysts for bioorganic chemistry
    • Silverman, S. K., Deoxyribozymes: DNA catalysts for bioorganic chemistry, Org. Biomol. Chem. 2:2701-2706 (2004).
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 2701-2706
    • Silverman, S.K.1
  • 139
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids
    • Watson, J. D. and Crick, F. H. C., Molecular structure of nucleic acids, Nature 171:737-738 (1953).
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 140
    • 0036240768 scopus 로고    scopus 로고
    • Deoxyribozymes: New activities and new applications
    • Emilsson, G. M. and Breaker, R. R., Deoxyribozymes: New activities and new applications, Cell. Mol. Life Sci. 59:596-607 (2002).
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 596-607
    • Emilsson, G.M.1    Breaker, R.R.2
  • 141
    • 23644453112 scopus 로고    scopus 로고
    • DNA catalysis: Potential, limitations, open questions
    • Peracchi, A., DNA catalysis: Potential, limitations, open questions, ChemBio- Chem 6:1316-1322 (2005).
    • (2005) ChemBio- Chem , vol.6 , pp. 1316-1322
    • Peracchi, A.1
  • 142
    • 0030482173 scopus 로고    scopus 로고
    • In vitro selection of self-cleaving DNAs
    • Carmi, N., Shultz, L. A., and Breaker, R. R., In vitro selection of self-cleaving DNAs, Chem. Biol. 3(12):1039-1046 (1996).
    • (1996) Chem. Biol. , vol.3 , Issue.12 , pp. 1039-1046
    • Carmi, N.1    Shultz, L.A.2    Breaker, R.R.3
  • 143
    • 0037131433 scopus 로고    scopus 로고
    • New transition-metal-dependent DNAzymes as efficient endonucleases and as selective metal biosensors
    • Lu, Y., New transition-metal-dependent DNAzymes as efficient endonucleases and as selective metal biosensors, Chem. Eur. J. 8(20):4588-4596 (2002).
    • (2002) Chem. Eur. J. , vol.8 , Issue.20 , pp. 4588-4596
    • Lu, Y.1
  • 144
    • 11144330098 scopus 로고    scopus 로고
    • Natural and engineered nucleic acids as tools to explore biology
    • Breaker, R. R., Natural and engineered nucleic acids as tools to explore biology, Nature 432:838-845 (2004).
    • (2004) Nature , vol.432 , pp. 838-845
    • Breaker, R.R.1
  • 145
    • 0035070585 scopus 로고    scopus 로고
    • Immobilized RNA switches for the analysis of complex chemical and biological mixtures
    • Seetharaman, S., Zivarts, M., Sudarsan, N., and Breaker, R. R., Immobilized RNA switches for the analysis of complex chemical and biological mixtures, Nature Biotechnol. 19(4):336-341 (2001).
    • (2001) Nature Biotechnol. , vol.19 , Issue.4 , pp. 336-341
    • Seetharaman, S.1    Zivarts, M.2    Sudarsan, N.3    Breaker, R.R.4
  • 146
    • 0013319804 scopus 로고    scopus 로고
    • The Heck reaction and related carbopallidation reactions
    • E.-I. Negishi (ed.), Wiley, New York
    • Larhed, M. and Hallbert, A., The Heck reaction and related carbopallidation reactions, in Handbook of Organopalladium Chemistry for Organic Synthesis, E.-I. Negishi (ed.), Wiley, New York, 2002, Vol. 1, pp. 1135-1178.
    • (2002) Handbook of Organopalladium Chemistry for Organic Synthesis , vol.1 , pp. 1135-1178
    • Larhed, M.1    Hallbert, A.2
  • 147
    • 84889265695 scopus 로고    scopus 로고
    • Development of homogeneous catalysts using molecular evolution
    • Vannela, R. and Woo, L. K., Development of homogeneous catalysts using molecular evolution, Abstract of Papers, 232nd American Chemical Society National Meeting, San Francisco, CA, Sept. 10-14, 2006 (2006), INOR-087.
    • (2006) Abstract of Papers , vol.2006 , pp. 10-14
    • Vannela, R.1    Woo, L.K.2
  • 148
    • 0342313543 scopus 로고    scopus 로고
    • Evolution of DNA and RNA as catalysts for chemical reactions
    • Jaschke, A. and Seelig, B., Evolution of DNA and RNA as catalysts for chemical reactions, Curr. Opin. Chem. Biol. 4(3):257-262 (2000).
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , Issue.3 , pp. 257-262
    • Jaschke, A.1    Seelig, B.2
  • 149
    • 0032568617 scopus 로고    scopus 로고
    • Nucleic acid enzymes: Playing with a fuller deck
    • USA
    • Joyce, G. F., Nucleic acid enzymes: Playing with a fuller deck, Proc. Natl. Acad. Sci. USA 95:5845-5847 (1998).
    • (1998) , vol.95 , pp. 5845-5847
    • Joyce, G.F.1
  • 150
    • 0036851660 scopus 로고    scopus 로고
    • Replacing the nucleobases in DNA with designer molecules
    • Kool, E. T., Replacing the nucleobases in DNA with designer molecules, Acc. Chem. Res. 35:936-943 (2002).
    • (2002) Acc. Chem. Res. , vol.35 , pp. 936-943
    • Kool, E.T.1
  • 151
    • 0037131476 scopus 로고    scopus 로고
    • Polymerase recognition of unnatural base pairs
    • Yu, C., Henry, A. A., Romesberg, F. E., and Schultz, P. G., Polymerase recognition of unnatural base pairs, Angew. Chem. Int. Ed. 41(20):3841-3844 (2002).
    • (2002) , vol.41 , Issue.20 , pp. 3841-3844
    • Yu, C.1    Henry, A.A.2    Romesberg, F.E.3    Schultz, P.G.4
  • 152
    • 0034835786 scopus 로고    scopus 로고
    • Efforts toward expansion of the genetic alphabet: Replication of DNA with three base pairs
    • Tae, E. L., Wu, Y., Xia, G., Schultz, P. G., and Romesberg, F. E., Efforts toward expansion of the genetic alphabet: Replication of DNA with three base pairs, J. Am. Chem. Soc. 123(30):7439-7440 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , Issue.30 , pp. 7439-7440
    • Tae, E.L.1    Wu, Y.2    Xia, G.3    Schultz, P.G.4    Romesberg, F.E.5
  • 153
    • 24744453533 scopus 로고    scopus 로고
    • The promise and peril of continuous in vitro evolution
    • Johns, G. C. and Joyce, G. F., The promise and peril of continuous in vitro evolution, J. Mol. Evol. 61:253-263 (2005).
    • (2005) J. Mol. Evol. , vol.61 , pp. 253-263
    • Johns, G.C.1    Joyce, G.F.2


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