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Volumn 6, Issue 7, 2005, Pages 533-543

Synthetic biology

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT DNA;

EID: 21344458620     PISSN: 14710056     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrg1637     Document Type: Review
Times cited : (698)

References (98)
  • 1
    • 0019202443 scopus 로고
    • Surgery of genes. At the doorstep of synthetic biology
    • Hobom, B. Surgery of genes. At the doorstep of synthetic biology. Medizin. Klinik 75, 14-21 (1980).
    • (1980) Medizin. Klinik , vol.75 , pp. 14-21
    • Hobom, B.1
  • 2
    • 12144284325 scopus 로고    scopus 로고
    • 'Synthetic biology' makes its debut
    • 24 April
    • Rawls, R. 'Synthetic Biology' makes its debut. Chem. Eng. News 49-53 (24 April 2000).
    • (2000) Chem. Eng. News , pp. 49-53
    • Rawls, R.1
  • 3
    • 21344456443 scopus 로고
    • Redesigning life. Organic chemistry and the evolution of protein
    • Benner, S. A. Redesigning life. Organic chemistry and the evolution of protein. Chimia 41, 142-148 (1987).
    • (1987) Chimia , vol.41 , pp. 142-148
    • Benner, S.A.1
  • 5
    • 0037426848 scopus 로고    scopus 로고
    • Act natural
    • Benner, S. A. Act natural. Nature 421, 118 (2003). This paper outlines the importance of pursuing the science of synthetic biology.
    • (2003) Nature , vol.421 , pp. 118
    • Benner, S.A.1
  • 6
    • 37049121735 scopus 로고
    • Centenary Lecture. Biomimetic chemistry
    • Breslow, R. Centenary Lecture. Biomimetic chemistry. Criem. Soc. Rev. 1, 553-580 (1972).
    • (1972) Criem. Soc. Rev. , vol.1 , pp. 553-580
    • Breslow, R.1
  • 7
    • 0000964852 scopus 로고
    • Use of the term 'emergent properties'
    • Comment
    • Salt, G. W. Use of the term 'emergent properties'. Comment. Am. Nat. 113, 145-148 (1979).
    • (1979) Am. Nat. , vol.113 , pp. 145-148
    • Salt, G.W.1
  • 9
    • 2442598411 scopus 로고    scopus 로고
    • Synthetic life
    • Gibbs, W. W. Synthetic life. Sci. Am. 290, 74-81 (2004).
    • (2004) Sci. Am. , vol.290 , pp. 74-81
    • Gibbs, W.W.1
  • 10
    • 3142702816 scopus 로고    scopus 로고
    • Simultaneous runs of the Bayer VERSANT HIV-1 version 3.0 and HCV bDNA version 3.0 quantitative assays on the system 340 platform provide reliable quantitation and improved work flow
    • Elbeik, T. et al. Simultaneous runs of the Bayer VERSANT HIV-1 version 3.0 and HCV bDNA version 3.0 quantitative assays on the system 340 platform provide reliable quantitation and improved work flow. J. Clin. Microbiol. 42, 3120-3127 (2004).
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 3120-3127
    • Elbeik, T.1
  • 11
    • 10744231244 scopus 로고    scopus 로고
    • Multicenter evaluation of the performance characteristics of the Bayer VERSANT HCV RNA 3.0 assay (bDNA)
    • Elbeik, T. et al. Multicenter evaluation of the performance characteristics of the Bayer VERSANT HCV RNA 3.0 assay (bDNA). J. Clin. Microbiol. 42, 563-569 (2004).
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 563-569
    • Elbeik, T.1
  • 12
    • 7444252231 scopus 로고    scopus 로고
    • Redesigning genetics
    • Benner, S. A. Redesigning genetics. Science 306, 625-626 (2004).
    • (2004) Science , vol.306 , pp. 625-626
    • Benner, S.A.1
  • 13
    • 0028136665 scopus 로고
    • The application of a modified nucleotide in aptamer selection. Novel thrombin aptamers containing 5-(1-pentynyl)-2′-deoxyuridine
    • Latham, J. A., Johnson, R. & Toole J. J. The application of a modified nucleotide in aptamer selection. Novel thrombin aptamers containing 5-(1-pentynyl)-2′-deoxyuridine. Nucleic Acids Res. 22, 2817-2822 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2817-2822
    • Latham, J.A.1    Johnson, R.2    Toole, J.J.3
  • 14
    • 1342327652 scopus 로고    scopus 로고
    • PCR amplification of DNA containing non-standard base pairs by variants of reverse transcriptase from Human Immunodeficiency Virus-1
    • Sismour, A. M. et al. PCR amplification of DNA containing non-standard base pairs by variants of reverse transcriptase from Human Immunodeficiency Virus-1. Nucleic Acids, Res. 32, 728-735 (2004). This paper describes the first example of an artificial genetic system that can be replicated by enzymes, and highlights some important concepts in the design of genetic systems.
    • (2004) Nucleic Acids, Res. , vol.32 , pp. 728-735
    • Sismour, A.M.1
  • 15
    • 0033610480 scopus 로고    scopus 로고
    • Quantitative analysis of receptors for adenosine nucleotides obtained via in vitro selection from a library incorporating acationic nucleotide analog
    • Battersby, T. R. et al. Quantitative analysis of receptors for adenosine nucleotides obtained via in vitro selection from a library incorporating acationic nucleotide analog. J. Am. Chem. Soc. 121, 9781-9789 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9781-9789
    • Battersby, T.R.1
  • 16
    • 0034688173 scopus 로고    scopus 로고
    • A synthetic oscillatory network of transcriptional regulators
    • Elowitz, M. B. & Leibler, S. A synthetic oscillatory network of transcriptional regulators. Nature 403, 335-338 (2000).
    • (2000) Nature , vol.403 , pp. 335-338
    • Elowitz, M.B.1    Leibler, S.2
  • 17
    • 0034305052 scopus 로고    scopus 로고
    • The past, present and future of molecular computing
    • Ruben, A. J. & Landweber, L. F. The past, present and future of molecular computing. Nature Rev. Mol. Cell Biol. 1, 69-72 (2000).
    • (2000) Nature Rev. Mol. Cell Biol. , vol.1 , pp. 69-72
    • Ruben, A.J.1    Landweber, L.F.2
  • 19
    • 0037803571 scopus 로고    scopus 로고
    • Z-DNA: The long road to biological function
    • Rich, A. & Zhang, S. G. Z-DNA: the long road to biological function. Nature Rev. Genet. 4, 566-572 (2003).
    • (2003) Nature Rev. Genet. , vol.4 , pp. 566-572
    • Rich, A.1    Zhang, S.G.2
  • 20
    • 0026500052 scopus 로고
    • Novel DNA superstructures formed by telomere-like oligomers
    • Sen, D. & Gilbert, W. Novel DNA superstructures formed by telomere-like oligomers. Biochemistry 31, 65-70 (1992).
    • (1992) Biochemistry , vol.31 , pp. 65-70
    • Sen, D.1    Gilbert, W.2
  • 21
    • 0026666130 scopus 로고
    • Trinucleotide can promote metal ion-dependent specific cleavage of RNA
    • Kazakov, S. & Altman, S. A. Trinucleotide can promote metal ion-dependent specific cleavage of RNA. Proc. Natl. Acad. Sci. USA 89, 7939-7943 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7939-7943
    • Kazakov, S.1    Altman, S.A.2
  • 22
    • 6944225455 scopus 로고    scopus 로고
    • Understanding nucleic acids using synthetic chemistry
    • Benner, S. A. Understanding nucleic acids using synthetic chemistry. Acc. Chem. Res. 37, 784-797 (2004).
    • (2004) Acc. Chem. Res. , vol.37 , pp. 784-797
    • Benner, S.A.1
  • 23
    • 6344238781 scopus 로고    scopus 로고
    • Synthetic biology: Starting from scratch
    • Ball, P. Synthetic biology: starting from scratch. Nature 431, 624-626 (2004).
    • (2004) Nature , vol.431 , pp. 624-626
    • Ball, P.1
  • 24
    • 0030727765 scopus 로고    scopus 로고
    • The ups and downs of nucleic acid duplex stability: Structure-stability studies on chemically-modified DNA:RNA duplexes
    • Freier, S. M. & Altmann, K. H. The ups and downs of nucleic acid duplex stability: structure-stability studies on chemically-modified DNA:RNA duplexes Nucleic Acids Res. 25, 4429-4443 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4429-4443
    • Freier, S.M.1    Altmann, K.H.2
  • 25
    • 0014954677 scopus 로고
    • Poly(1-vinyluracil): The preparation and interactions with adenosine derivatives
    • Pitha, J., Pitha P. M. & Ts'o, P. O. Poly(1-vinyluracil): the preparation and interactions with adenosine derivatives. Biochim. Biophys. Acta 204, 39-48 (1970).
    • (1970) Biochim. Biophys. Acta , vol.204 , pp. 39-48
    • Pitha, J.1    Pitha, P.M.2    Ts'O, P.O.3
  • 26
    • 0025343509 scopus 로고
    • Oligonucleotides containing flexible nucleoside analogs
    • Schneider, K. C. & Benner, S. A. Oligonucleotides containing flexible nucleoside analogs. J. Am. Chem. Soc. 112, 453-455 (1990).
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 453-455
    • Schneider, K.C.1    Benner, S.A.2
  • 27
    • 7444245899 scopus 로고    scopus 로고
    • PNA technology
    • Nielsen, P. E. PNA technology. Mol. Biotechnol. 26, 233-248 (2004).
    • (2004) Mol. Biotechnol. , vol.26 , pp. 233-248
    • Nielsen, P.E.1
  • 28
    • 0036479123 scopus 로고    scopus 로고
    • Phosphates, DNA, and the search for nonterrean life: A second generation model for genetic molecules
    • Benner, S. A. & Mutter, D. Phosphates, DNA, and the search for nonterrean life: A second generation model for genetic molecules. Bioorg. Chem. 30, 62-80 (2002).
    • (2002) Bioorg. Chem. , vol.30 , pp. 62-80
    • Benner, S.A.1    Mutter, D.2
  • 29
    • 2242462219 scopus 로고    scopus 로고
    • Crystal structure of a B-form DNA duplex containing (L)-α- threofuranosyl (3′→2′) nucleosides: A four-carbon sugar is easily accommodated into the backbone of DNA
    • Wilds, C. J., Wawrzak, Z., Krishnamurthy, R., Eschenmoser, A. & Egli, M. Crystal structure of a B-form DNA duplex containing (L)-α- threofuranosyl (3′→2′) nucleosides: A four-carbon sugar is easily accommodated into the backbone of DNA. J. Am. Chem. Soc. 124, 13716-13721 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13716-13721
    • Wilds, C.J.1    Wawrzak, Z.2    Krishnamurthy, R.3    Eschenmoser, A.4    Egli, M.5
  • 30
    • 0032909507 scopus 로고    scopus 로고
    • Synthesis of 3′-C- And 4′-C-branched oligodeoxynucleotides and the development of locked nucleic acid (LNA)
    • Wengel, J. Synthesis of 3′-C- and 4′-C-branched oligodeoxynucleotides and the development of locked nucleic acid (LNA). Acc. Chem. Res. 32, 301-310 (1999).
    • (1999) Acc. Chem. Res. , vol.32 , pp. 301-310
    • Wengel, J.1
  • 31
    • 0036398838 scopus 로고    scopus 로고
    • From phosphate to bis(methylene) sulfone: Non-ionic backbone linkers in DNA
    • Hutter, D., Blaettler, M. O. & Benner, S. A. From phosphate to bis(methylene) sulfone: Non-ionic backbone linkers in DNA. Helv. Chim. Acta. 85, 2777-2806 (2002).
    • (2002) Helv. Chim. Acta , vol.85 , pp. 2777-2806
    • Hutter, D.1    Blaettler, M.O.2    Benner, S.A.3
  • 33
    • 0029111395 scopus 로고
    • Rates of decomposition of ribose and other sugars. Implications for chemical evolution
    • Larralde, R., Robertson, M. P. & Miller, S. L. Rates of decomposition of ribose and other sugars. Implications for chemical evolution. Proc. Natl Acad. Sci. USA 92, 8158-8160 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8158-8160
    • Larralde, R.1    Robertson, M.P.2    Miller, S.L.3
  • 34
    • 0344326234 scopus 로고    scopus 로고
    • Chemical etiology of nucleic acid structure
    • Eschenmoser, A. Chemical etiology of nucleic acid structure. Science 284, 2118-2124 (1999).
    • (1999) Science , vol.284 , pp. 2118-2124
    • Eschenmoser, A.1
  • 36
    • 0347482479 scopus 로고    scopus 로고
    • Nucleobase pairing in expanded Watson-Crick-like genetic information systems
    • Geyer, C. R., Battersby, T. R. & Benner, S. A. Nucleobase pairing in expanded Watson-Crick-like genetic information systems. Structure 11, 1485-1498 (2003).
    • (2003) Structure , vol.11 , pp. 1485-1498
    • Geyer, C.R.1    Battersby, T.R.2    Benner, S.A.3
  • 37
    • 4043150758 scopus 로고    scopus 로고
    • Escherichia coli DNA polymerase I (Klenow fragment) uses a hydrogen-bonding fork from Arg(668) to the primer terminus and incoming deoxynucleotide triphosphate to catalyze DNA replication
    • Meyer, A. S., Blandino, M. & Spratt, T. E. Escherichia coli DNA polymerase I (Klenow fragment) uses a hydrogen-bonding fork from Arg(668) to the primer terminus and incoming deoxynucleotide triphosphate to catalyze DNA replication. J. Biol. Chem. 279, 33043-33046 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 33043-33046
    • Meyer, A.S.1    Blandino, M.2    Spratt, T.E.3
  • 38
    • 0344235337 scopus 로고    scopus 로고
    • Expanding the genetic alphabet. Non-epimerizing nucleoside with the pyDDA hydrogen bonding pattern
    • Mutter, D. & Benner, S. A. Expanding the genetic alphabet. Non-epimerizing nucleoside with the pyDDA hydrogen bonding pattern. J. Org. Chem. 68, 9839-9842 (2003).
    • (2003) J. Org. Chem. , vol.68 , pp. 9839-9842
    • Mutter, D.1    Benner, S.A.2
  • 39
    • 2442675347 scopus 로고    scopus 로고
    • Artificial genetic systems: Exploiting the 'aromaticity' formalism to improve the tautomeric ratio for isoguanosine derivatives
    • Martinot, T. A. & Benner, S. A. Artificial genetic systems: exploiting the 'aromaticity' formalism to improve the tautomeric ratio for isoguanosine derivatives. J. Org. Chem 69, 3972-3975 (2004).
    • (2004) J. Org. Chem , vol.69 , pp. 3972-3975
    • Martinot, T.A.1    Benner, S.A.2
  • 40
    • 0030815923 scopus 로고    scopus 로고
    • A branched DNA signal amplification assay for quantification of nucleic acid targets below 100 molecules/ml
    • Collins, M. L. et al. A branched DNA signal amplification assay for quantification of nucleic acid targets below 100 molecules/ml. Nucleic Acids Res. 25, 2979-2984 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2979-2984
    • Collins, M.L.1
  • 41
    • 21344434240 scopus 로고
    • Genetic studies of Lac repressor
    • Schmeissner, U. & Miller, J. H. Genetic studies of Lac repressor. Experientia 32, 811-811 (1976).
    • (1976) Experientia , vol.32 , pp. 811-811
    • Schmeissner, U.1    Miller, J.H.2
  • 42
    • 0027951524 scopus 로고
    • Synthetic DNA and biology (Nobel lecture)
    • Smith, M. Synthetic DNA and biology (Nobel lecture). Angew. Chem. Int. Ed. Engl. 33, 1214-1221 (1994).
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1214-1221
    • Smith, M.1
  • 43
    • 0020694602 scopus 로고
    • Protein engineering
    • Ulmer, K. M. Protein engineering. Science 219, 666-671 (1983).
    • (1983) Science , vol.219 , pp. 666-671
    • Ulmer, K.M.1
  • 44
    • 21344458951 scopus 로고
    • Engineering nonaqueous solvent-compatible enzymes
    • Arnold, F. H. et al. Engineering nonaqueous solvent-compatible enzymes. ACS Symp. Ser. 516, 109-113 (1993).
    • (1993) ACS Symp. Ser. , vol.516 , pp. 109-113
    • Arnold, F.H.1
  • 45
    • 8744220371 scopus 로고    scopus 로고
    • Inverse thinking about double mutants of enzymes
    • Mildvan, A. S. Inverse thinking about double mutants of enzymes. Biochemistry 43, 14517-14520 (2004).
    • (2004) Biochemistry , vol.43 , pp. 14517-14520
    • Mildvan, A.S.1
  • 46
    • 0023645080 scopus 로고
    • Tinkering with enzymes: What are we learning?
    • Knowles, J. R. Tinkering with enzymes: what are we learning? Science 236, 1252-1258 (1987).
    • (1987) Science , vol.236 , pp. 1252-1258
    • Knowles, J.R.1
  • 47
    • 0036301488 scopus 로고    scopus 로고
    • Detecting compensatory covariation signals in protein evolution using reconstructed ancestral sequences
    • Fukami-Kobayashi, K., Schreiber, D. R. & Benner, S. A. Detecting compensatory covariation signals in protein evolution using reconstructed ancestral sequences. J. Mol. Biol. 319, 729-743 (2002).
    • (2002) J. Mol. Biol. , vol.319 , pp. 729-743
    • Fukami-Kobayashi, K.1    Schreiber, D.R.2    Benner, S.A.3
  • 49
    • 0033615719 scopus 로고    scopus 로고
    • Catalysts, anticatalysts, and receptors for unactivated phosphate diesters in water
    • Zepik, H. & Benner, S. A. Catalysts, anticatalysts, and receptors for unactivated phosphate diesters in water. J. Org. Chem. 64, 8080-8083 (1999).
    • (1999) J. Org. Chem. , vol.64 , pp. 8080-8083
    • Zepik, H.1    Benner, S.A.2
  • 51
    • 0034193592 scopus 로고    scopus 로고
    • Recent advances in the design and construction of synthetic peptides: For the love of basics or just for the technology of it
    • Mayo, K. H. Recent advances in the design and construction of synthetic peptides: for the love of basics or just for the technology of it. Trends Biotechnol. 18, 212-217 (2000).
    • (2000) Trends Biotechnol. , vol.18 , pp. 212-217
    • Mayo, K.H.1
  • 53
    • 3042655537 scopus 로고    scopus 로고
    • Computational design of a biologically active enzyme
    • Dwyer, M. A., Looger, L. L. & Hellinga, H. W. Computational design of a biologically active enzyme. Science 304, 1967-1971 (2004). This paper illustrates the progress made in the de novo design of biological molecules.
    • (2004) Science , vol.304 , pp. 1967-1971
    • Dwyer, M.A.1    Looger, L.L.2    Hellinga, H.W.3
  • 54
    • 5444230250 scopus 로고    scopus 로고
    • Preprocessing of rotamers for protein design calculations
    • Shah, P. S., Hom, G. K. & Mayo, S. L. Preprocessing of rotamers for protein design calculations. J. Comput. Chem. 25, 1797-1800 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1797-1800
    • Shah, P.S.1    Hom, G.K.2    Mayo, S.L.3
  • 55
    • 4344684651 scopus 로고    scopus 로고
    • X-ray structure analysis of a designed olilgomeric miniprotein reveals a discrete quaternary architecture
    • Ali, M. H., Peisach, E., Allen, K. N. & Imperiali, B. X-ray structure analysis of a designed olilgomeric miniprotein reveals a discrete quaternary architecture. Proc. Natl Acad. Sci. USA 101, 12183-12188 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12183-12188
    • Ali, M.H.1    Peisach, E.2    Allen, K.N.3    Imperiali, B.4
  • 56
    • 0035843136 scopus 로고    scopus 로고
    • Combinatorial and computational challenges for biocatalyst design
    • Arnold, F. H. Combinatorial and computational challenges for biocatalyst design. Nature 409, 253-257 (2001).
    • (2001) Nature , vol.409 , pp. 253-257
    • Arnold, F.H.1
  • 57
    • 0028902065 scopus 로고
    • Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles
    • First, E. A. & Fersht, A. R. Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles. Biochemistry 34, 5030-5043 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5030-5043
    • First, E.A.1    Fersht, A.R.2
  • 58
    • 0029023051 scopus 로고
    • A single residue in DNA polymerases of the Escherichia coli DNA polymerase I family is critical for distinguishing between deoxy- And dideoxyribonucleotides
    • Tabor, S. & Richardson, C. C. A single residue in DNA polymerases of the Escherichia coli DNA polymerase I family is critical for distinguishing between deoxy- and dideoxyribonucleotides. Proc. Natl Acad. Sci. USA 92, 6339-6343 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6339-6343
    • Tabor, S.1    Richardson, C.C.2
  • 60
    • 0004792589 scopus 로고
    • Atomic coordinates and structure factors for two helical configurations of polypeptide chains
    • Pauling, L. & Corey, R. B. Atomic coordinates and structure factors for two helical configurations of polypeptide chains. Proc. Natl Acad. Sci. USA, 37, 235-240 (1951).
    • (1951) Proc. Natl Acad. Sci. USA , vol.37 , pp. 235-240
    • Pauling, L.1    Corey, R.B.2
  • 61
    • 0022501924 scopus 로고
    • Design and biological activity of analogs of growth hormone releasing factor with potential amphiphilic helical carboxyl termini
    • Velicelebi, G., Patthi, S. & Kaiser, E. T. Design and biological activity of analogs of growth hormone releasing factor with potential amphiphilic helical carboxyl termini. Proc. Natl Acad. Sci. USA 83, 5397-5399 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 5397-5399
    • Velicelebi, G.1    Patthi, S.2    Kaiser, E.T.3
  • 62
    • 0019497821 scopus 로고
    • Design, synthesis and characterization of a cyto-toxic peptide with melittin-like activity
    • Degrade, W. F., Kezdy, F. J. & Kaiser, E. T. Design, synthesis and characterization of a cyto-toxic peptide with melittin-like activity. J. Am. Chem. Soc. 103, 679-681 (1981).
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 679-681
    • Degrade, W.F.1    Kezdy, F.J.2    Kaiser, E.T.3
  • 66
    • 0035865080 scopus 로고    scopus 로고
    • A chiroselective peptide replicator
    • Saghatelian, A., Yokobayashi, Y., Soteni, K. & Ghadiri, M. R. A chiroselective peptide replicator. Nature 409, 797-801 (2001). The chiroselective peptide replicator developed in this article illustrates the modular design aspects of synthetic biology and the ability to replicate information in a peptide based system.
    • (2001) Nature , vol.409 , pp. 797-801
    • Saghatelian, A.1    Yokobayashi, Y.2    Soteni, K.3    Ghadiri, M.R.4
  • 67
    • 0027453389 scopus 로고
    • Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides
    • Johnsson, K., Allemann, R. K., Widmer, H. & Benner, S. A. Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides. Nature 365, 530-532 (1993).
    • (1993) Nature , vol.365 , pp. 530-532
    • Johnsson, K.1    Allemann, R.K.2    Widmer, H.3    Benner, S.A.4
  • 68
    • 0036009270 scopus 로고    scopus 로고
    • Design of a folded, conformationally stable oxaloacetate decarboxylase
    • Taylor, S. E., Rutherford, T. J. & Allemann, R. K. Design of a folded, conformationally stable oxaloacetate decarboxylase. J. Chem. Soc. Perkin Trans. 2, 751-755 (2002).
    • (2002) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 751-755
    • Taylor, S.E.1    Rutherford, T.J.2    Allemann, R.K.3
  • 69
    • 4344668644 scopus 로고    scopus 로고
    • Nucleophilic and general acid catalysis at physiological pH by a designed miniature esterase
    • Nicoll, A. J. & Allemann, R. K. Nucleophilic and general acid catalysis at physiological pH by a designed miniature esterase. Org. Biomol. Chem. 2, 2175-2180 (2004).
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 2175-2180
    • Nicoll, A.J.1    Allemann, R.K.2
  • 70
    • 4143131151 scopus 로고    scopus 로고
    • De novo design of catalytic proteins
    • Kaplan, J. & DeGrado, W. F. De novo design of catalytic proteins. Proc. Natl Acad. Sci. USA 101, 11566-11570 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11566-11570
    • Kaplan, J.1    Degrado, W.F.2
  • 71
    • 0037051643 scopus 로고    scopus 로고
    • A modular assembly strategy for improving the substrate specificity of small catalytic peptides
    • Tanaka, F. & Barbas, C. F. A modular assembly strategy for improving the substrate specificity of small catalytic peptides. J. Am. Chem. Soc. 124, 3510-3511 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3510-3511
    • Tanaka, F.1    Barbas, C.F.2
  • 73
    • 0024256764 scopus 로고
    • Interpreting the behavior of enzymes. Purpose or pedigree?
    • Benner, S. A. & Ellington, A. D. Interpreting the behavior of enzymes. Purpose or pedigree? CRC Crit. Rev. Biochem. 23, 369-426 (1988).
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 369-426
    • Benner, S.A.1    Ellington, A.D.2
  • 74
    • 0031995123 scopus 로고    scopus 로고
    • New directions in metabolic engineering
    • Jacobsen, J. R. & Khosla, C. New directions in metabolic engineering. Curr. Opin. Chem. Biol. 2, 133-137 (1998). This paper presents some of the recent work in metabolic engineering that is typically used in synthetic biology.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 133-137
    • Jacobsen, J.R.1    Khosla, C.2
  • 75
    • 21344449225 scopus 로고
    • Strain selection in citric acid fermentation. A review
    • Das, A. Strain selection in citric acid fermentation. A review. Curr. Sci. 41, 593-596 (1972).
    • (1972) Curr. Sci. , vol.41 , pp. 593-596
    • Das, A.1
  • 76
    • 0036261666 scopus 로고    scopus 로고
    • Engineering of Ralstonia eutropha for production of poly(3- hydroxybutyrate-co-3-hydroxyhexanoate) from fructose and solid-state properties of the copolymer
    • Fukui, T., Abe, H. & Doi, Y. Engineering of Ralstonia eutropha for production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from fructose and solid-state properties of the copolymer. Biomacromolecules 3, 618-624 (2002).
    • (2002) Biomacromolecules , vol.3 , pp. 618-624
    • Fukui, T.1    Abe, H.2    Doi, Y.3
  • 77
    • 0038391517 scopus 로고    scopus 로고
    • Engineering a mevalonate pathway in Escherichia coli for production of terpenoids
    • Martin, V. J., Pitera, D. J., Withers, S. T., Newman, J. D. & Keasling, J. D. Engineering a mevalonate pathway in Escherichia coli for production of terpenoids. Nature Biotech. 21, 796-802 (2003). The development of a bacterial strain that can synthesize pharmaceuticals illustrates the power of synthetic biology as a tool for technology.
    • (2003) Nature Biotech. , vol.21 , pp. 796-802
    • Martin, V.J.1    Pitera, D.J.2    Withers, S.T.3    Newman, J.D.4    Keasling, J.D.5
  • 78
    • 0346328227 scopus 로고    scopus 로고
    • Metabolic engineering for drug discovery and development
    • Khosla, C. & Keasling, J. D. Metabolic engineering for drug discovery and development. Nature Rev. Drug Discov. 2, 1019-1025 (2003). This paper highlights the complexity that is required to engineer a metabolic pathway successfully.
    • (2003) Nature Rev. Drug Discov. , vol.2 , pp. 1019-1025
    • Khosla, C.1    Keasling, J.D.2
  • 79
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • Lim, W. A. The modular logic of signaling proteins: Building allosteric switches from simple binding domains. Curr. Opin. Struct. Biol. 12, 61-68 (2002). This paper lays the foundation for designing complex logic networks.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 80
    • 0141483011 scopus 로고    scopus 로고
    • Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins
    • Howard, P. L., Chia, M. C., Del Rizzo, S., Liu, F. F. & Pawson, T. Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins. Proc. Natl Acad. Sci. USA 100, 11267-11272 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11267-11272
    • Howard, P.L.1    Chia, M.C.2    Del Rizzo, S.3    Liu, F.F.4    Pawson, T.5
  • 81
    • 0037079012 scopus 로고    scopus 로고
    • Engineered gene circuits
    • Hasty, J., McMillen, D. & Collins, J. J. Engineered gene circuits. Nature 420, 224-230 (2004).
    • (2004) Nature , vol.420 , pp. 224-230
    • Hasty, J.1    McMillen, D.2    Collins, J.J.3
  • 83
    • 0042360338 scopus 로고    scopus 로고
    • A deoxyribozyme-based molecular automaton
    • Stojanovic, M. N. & Stefanovic, D. A deoxyribozyme-based molecular automaton. Nature Biotech. 21, 1069-1074 (2003). This paper illustrates not only the ability to develop interactive logic networks, but also some of the new kinds of technology that synthetic biology is producing.
    • (2003) Nature Biotech. , vol.21 , pp. 1069-1074
    • Stojanovic, M.N.1    Stefanovic, D.2
  • 84
    • 10744229298 scopus 로고    scopus 로고
    • Synthetic biology. Time for a synthetic biology Asilomar?
    • Ferber, D. Synthetic biology. Time for a synthetic biology Asilomar? Science 303, 159 (2004).
    • (2004) Science , vol.303 , pp. 159
    • Ferber, D.1
  • 85
    • 0037047595 scopus 로고    scopus 로고
    • Chemical synthesis of poliovirus cDNA: Generation of infectious virus in the absence of natural template
    • Cello, J., Paul, A. V. & Wimmer, E. J. Chemical synthesis of poliovirus cDNA: Generation of infectious virus in the absence of natural template. Science 297, 1016-1018 (2002). The chemical synthesis of poliovirus cDNA described in this article illustrates the ability to synthesize life; the paper also discusses the dangers of synthetic biology and organism engineering.
    • (2002) Science , vol.297 , pp. 1016-1018
    • Cello, J.1    Paul, A.V.2    Wimmer, E.J.3
  • 87
    • 1842633364 scopus 로고    scopus 로고
    • Ten suggestions to strengthen the science of ecology
    • Belovsky, G. E. et al. Ten suggestions to strengthen the science of ecology. Bioscience 54, 345-351 (2004).
    • (2004) Bioscience , vol.54 , pp. 345-351
    • Belovsky, G.E.1
  • 88
    • 0042658199 scopus 로고    scopus 로고
    • RNA, the first macromolecular catalyst: The ribosome is a ribozyme
    • Steitz, T. A. & Moore, P. B. RNA, the first macromolecular catalyst: the ribosome is a ribozyme. Trends Biochem. Sci. 28, 411-418 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 411-418
    • Steitz, T.A.1    Moore, P.B.2
  • 89
    • 0037237858 scopus 로고    scopus 로고
    • A complexity-based risk assessment of low-cost planetary missions: When is a mission too fast and too cheap?
    • Bearden, D. A. A complexity-based risk assessment of low-cost planetary missions: when is a mission too fast and too cheap? Acta Astronaut. 52, 371-379 (2003).
    • (2003) Acta Astronaut. , vol.52 , pp. 371-379
    • Bearden, D.A.1
  • 91
    • 0003454816 scopus 로고
    • (eds Lakatos, I. & Musgrave, A.) Cambridge Univ. Press
    • Masterman, M. in Criticism and the Growth of Knowledge (eds Lakatos, I. & Musgrave, A.) 59-89 (Cambridge Univ. Press, 1970).
    • (1970) Criticism and the Growth of Knowledge , pp. 59-89
    • Masterman, M.1
  • 92
    • 0014389759 scopus 로고
    • Recent advances in the chemistry of natural products
    • Woodward, R. B. Recent advances in the chemistry of natural products. Pure Appl. Chem. 17, 519-547 (1968).
    • (1968) Pure Appl. Chem. , vol.17 , pp. 519-547
    • Woodward, R.B.1
  • 93
    • 0037436155 scopus 로고    scopus 로고
    • Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms
    • Park, S. H., Zarrinpar, A. & Lim, W. A. Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms. Science 299, 1061-1064 (2003).
    • (2003) Science , vol.299 , pp. 1061-1064
    • Park, S.H.1    Zarrinpar, A.2    Lim, W.A.3
  • 94
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda, K. E., Scott, J. A., Mullins, R. D. & Lim, W. A. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290, 801-806 (2000).
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 95
    • 9944220618 scopus 로고    scopus 로고
    • Rewiring cell signaling: The logic and plasticity of eukaryotic protein circuitry
    • Dueber, J. E., Yeh, B. J., Bhattacharyya, R. P. & Lim, W. A. Rewiring cell signaling: the logic and plasticity of eukaryotic protein circuitry. Curr. Opin. Struct. Biol. 14, 690-699 (2004).
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 690-699
    • Dueber, J.E.1    Yeh, B.J.2    Bhattacharyya, R.P.3    Lim, W.A.4
  • 96
    • 0032764518 scopus 로고    scopus 로고
    • Global transposon mutagenesis and a minimal mycoplasma genome
    • Hutchison, C. A. et al. Global transposon mutagenesis and a minimal mycoplasma genome. Science 286, 2165-2169 (1999).
    • (1999) Science , vol.286 , pp. 2165-2169
    • Hutchison, C.A.1


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