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Volumn 2, Issue 7, 2013, Pages 358-372

Synthetic biology of antimicrobial discovery

Author keywords

antibiotics; antimicrobial discovery; bacteriophage; biological engineering; genetic engineering; protein engineering; synthetic biology

Indexed keywords

ACYLTRANSFERASE; AMINOTRANSFERASE; ANTIINFECTIVE AGENT; AROMATASE; BACTERIOCIN; BETA DEFENSIN 1; DAPTOMYCIN; ERYTHROMYCIN; INDOLICIDIN; METHYLTRANSFERASE; NONRIBOSOMAL PEPTIDE SYNTHETASE; OLEANDOMYCIN; OXYGENASE; OXYTETRACYCLINE; PLECTASIN; POLYPEPTIDE ANTIBIOTIC AGENT; TETRACYCLINE; TYLOSIN; VANCOMYCIN;

EID: 84880518252     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/sb300101g     Document Type: Review
Times cited : (31)

References (155)
  • 1
    • 0000819488 scopus 로고
    • Charbon et septicemie
    • Pasteur, L. and Joubert, J. (1877) Charbon et septicemie C. R. Chim. 85, 101-105
    • (1877) C. R. Chim. , vol.85 , pp. 101-105
    • Pasteur, L.1    Joubert, J.2
  • 2
    • 26444526660 scopus 로고
    • The soil as a source of microorganisms antagonistic to disease-producing bacteria
    • Waksman, S. A. and Woodruff, H. B. (1940) The soil as a source of microorganisms antagonistic to disease-producing bacteria J. Bacteriol. 40, 581-600
    • (1940) J. Bacteriol. , vol.40 , pp. 581-600
    • Waksman, S.A.1    Woodruff, H.B.2
  • 3
    • 33847151750 scopus 로고    scopus 로고
    • The antibiotic resistome: The nexus of chemical and genetic diversity
    • Wright, G. D. (2007) The antibiotic resistome: The nexus of chemical and genetic diversity Nat. Rev. Microbiol. 5, 175-186
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 175-186
    • Wright, G.D.1
  • 5
    • 14544294545 scopus 로고    scopus 로고
    • Bioactive microbial metabolites
    • Berdy, J. (2005) Bioactive microbial metabolites J. Antibiot. (Tokyo) 58, 1-26
    • (2005) J. Antibiot. (Tokyo) , vol.58 , pp. 1-26
    • Berdy, J.1
  • 6
    • 84867184096 scopus 로고    scopus 로고
    • Adaptive and mutational resistance: Role of porins and efflux pumps in drug resistance
    • Fernandez, L. and Hancock, R. E. (2012) Adaptive and mutational resistance: Role of porins and efflux pumps in drug resistance Clin. Microbiol. Rev. 25, 661-681
    • (2012) Clin. Microbiol. Rev. , vol.25 , pp. 661-681
    • Fernandez, L.1    Hancock, R.E.2
  • 8
    • 84865531061 scopus 로고    scopus 로고
    • The shared antibiotic resistome of soil bacteria and human pathogens
    • Forsberg, K. J., Reyes, A., Wang, B., Selleck, E. M., Sommer, M. O., and Dantas, G. (2012) The shared antibiotic resistome of soil bacteria and human pathogens Science 337, 1107-1111
    • (2012) Science , vol.337 , pp. 1107-1111
    • Forsberg, K.J.1    Reyes, A.2    Wang, B.3    Selleck, E.M.4    Sommer, M.O.5    Dantas, G.6
  • 9
    • 33744536067 scopus 로고    scopus 로고
    • Antibiotic discovery from actinomycetes: Will a renaissance follow th decline and fall?
    • Baltz, R. H. (2005) Antibiotic discovery from actinomycetes: Will a renaissance follow th decline and fall? SIM News 55, 186-196
    • (2005) SIM News , vol.55 , pp. 186-196
    • Baltz, R.H.1
  • 10
    • 54849405130 scopus 로고    scopus 로고
    • Renaissance in antibacterial discovery from actinomycetes
    • Baltz, R. H. (2008) Renaissance in antibacterial discovery from actinomycetes Curr. Opin. Pharmacol. 8, 557-563
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 557-563
    • Baltz, R.H.1
  • 13
    • 17244375099 scopus 로고    scopus 로고
    • A convergent enantioselective route to structurally diverse 6-deoxytetracycline antibiotics
    • Charest, M. G., Lerner, C. D., Brubaker, J. D., Siegel, D. R., and Myers, A. G. (2005) A convergent enantioselective route to structurally diverse 6-deoxytetracycline antibiotics Science 308, 395-398
    • (2005) Science , vol.308 , pp. 395-398
    • Charest, M.G.1    Lerner, C.D.2    Brubaker, J.D.3    Siegel, D.R.4    Myers, A.G.5
  • 14
    • 42149157706 scopus 로고    scopus 로고
    • Chemical biology of tetracycline antibiotics
    • Zakeri, B. and Wright, G. D. (2008) Chemical biology of tetracycline antibiotics Biochem. Cell Biol. 86, 124-136
    • (2008) Biochem. Cell Biol. , vol.86 , pp. 124-136
    • Zakeri, B.1    Wright, G.D.2
  • 15
    • 33845719937 scopus 로고    scopus 로고
    • Antibacterial discovery and development-The failure of success?
    • Fernandes, P. (2006) Antibacterial discovery and development-the failure of success? Nat. Biotechnol. 24, 1497-1503
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1497-1503
    • Fernandes, P.1
  • 16
    • 65349098181 scopus 로고    scopus 로고
    • Revisiting the modularity of modular polyketide synthases
    • Khosla, C., Kapur, S., and Cane, D. E. (2009) Revisiting the modularity of modular polyketide synthases Curr. Opin. Chem. Biol. 13, 135-143
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 135-143
    • Khosla, C.1    Kapur, S.2    Cane, D.E.3
  • 17
    • 84863632639 scopus 로고    scopus 로고
    • Programmable bacterial catalysis-designing cells for biosynthesis of value-added compounds
    • Lam, C. M., Suarez Diez, M., Godinho, M., and Martins dos Santos, V. A. (2012) Programmable bacterial catalysis-designing cells for biosynthesis of value-added compounds FEBS Lett. 586, 2184-2190
    • (2012) FEBS Lett. , vol.586 , pp. 2184-2190
    • Lam, C.M.1    Suarez Diez, M.2    Godinho, M.3    Martins Dos Santos, V.A.4
  • 18
    • 84859776222 scopus 로고    scopus 로고
    • The future of metabolic engineering and synthetic biology: Towards a systematic practice
    • Yadav, V. G., De Mey, M., Lim, C. G., Ajikumar, P. K., and Stephanopoulos, G. (2012) The future of metabolic engineering and synthetic biology: Towards a systematic practice Metab. Eng. 14, 233-241
    • (2012) Metab. Eng. , vol.14 , pp. 233-241
    • Yadav, V.G.1    De Mey, M.2    Lim, C.G.3    Ajikumar, P.K.4    Stephanopoulos, G.5
  • 19
    • 84859780045 scopus 로고    scopus 로고
    • Spatial organization of enzymes for metabolic engineering
    • Lee, H., DeLoache, W. C., and Dueber, J. E. (2012) Spatial organization of enzymes for metabolic engineering Metab. Eng. 14, 242-251
    • (2012) Metab. Eng. , vol.14 , pp. 242-251
    • Lee, H.1    Deloache, W.C.2    Dueber, J.E.3
  • 20
    • 84859772410 scopus 로고    scopus 로고
    • Synthetic biology and the development of tools for metabolic engineering
    • Keasling, J. D. (2012) Synthetic biology and the development of tools for metabolic engineering Metab. Eng. 14, 189-195
    • (2012) Metab. Eng. , vol.14 , pp. 189-195
    • Keasling, J.D.1
  • 21
    • 84861322005 scopus 로고    scopus 로고
    • Engineering synthetic recursive pathways to generate non-natural small molecules
    • Felnagle, E. A., Chaubey, A., Noey, E. L., Houk, K. N., and Liao, J. C. (2012) Engineering synthetic recursive pathways to generate non-natural small molecules Nat. Chem. Biol. 8, 518-526
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 518-526
    • Felnagle, E.A.1    Chaubey, A.2    Noey, E.L.3    Houk, K.N.4    Liao, J.C.5
  • 22
    • 33845562808 scopus 로고    scopus 로고
    • Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis
    • Lai, J. R., Koglin, A., and Walsh, C. T. (2006) Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis Biochemistry 45, 14869-14879
    • (2006) Biochemistry , vol.45 , pp. 14869-14879
    • Lai, J.R.1    Koglin, A.2    Walsh, C.T.3
  • 23
    • 77649305354 scopus 로고    scopus 로고
    • Natural products version 2.0: Connecting genes to molecules
    • Walsh, C. T. and Fischbach, M. A. (2010) Natural products version 2.0: Connecting genes to molecules J. Am. Chem. Soc. 132, 2469-2493
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2469-2493
    • Walsh, C.T.1    Fischbach, M.A.2
  • 24
    • 68949159560 scopus 로고    scopus 로고
    • The chemical biology of modular biosynthetic enzymes
    • Meier, J. L. and Burkart, M. D. (2009) The chemical biology of modular biosynthetic enzymes Chem. Soc. Rev. 38, 2012-2045
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2012-2045
    • Meier, J.L.1    Burkart, M.D.2
  • 25
    • 33846923183 scopus 로고    scopus 로고
    • Type II polyketide synthases: Gaining a deeper insight into enzymatic teamwork
    • Hertweck, C., Luzhetskyy, A., Rebets, Y., and Bechthold, A. (2007) Type II polyketide synthases: Gaining a deeper insight into enzymatic teamwork Nat. Prod. Rep. 24, 162-190
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 162-190
    • Hertweck, C.1    Luzhetskyy, A.2    Rebets, Y.3    Bechthold, A.4
  • 26
    • 84863651979 scopus 로고    scopus 로고
    • The catalytic diversity of multimodular polyketide synthases: Natural product biosynthesis beyond textbook assembly rules
    • 10.1007/128-2010-113
    • Gulder, T. A., Freeman, M. F., and Piel, J. (2011) The catalytic diversity of multimodular polyketide synthases: Natural product biosynthesis beyond textbook assembly rules Top. Curr. Chem. 10.1007/128-2010-113
    • (2011) Top. Curr. Chem.
    • Gulder, T.A.1    Freeman, M.F.2    Piel, J.3
  • 27
    • 0031127564 scopus 로고    scopus 로고
    • The role of carbohydrates in biologically active natural products
    • Weymouth-Wilson, A. C. (1997) The role of carbohydrates in biologically active natural products Nat. Prod. Rep. 14, 99-110
    • (1997) Nat. Prod. Rep. , vol.14 , pp. 99-110
    • Weymouth-Wilson, A.C.1
  • 28
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen, D. E., Clemons, W. M., Jr., Carter, A. P., Morgan-Warren, R. J., Wimberly, B. T., and Ramakrishnan, V. (2000) The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit Cell 103, 1143-1154
    • (2000) Cell , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Clemons Jr., W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 30
    • 0036523418 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of antibiotics: Challenges and opportunities
    • Walsh, C. T. (2002) Combinatorial biosynthesis of antibiotics: Challenges and opportunities ChemBioChem 3, 125-134
    • (2002) ChemBioChem , vol.3 , pp. 125-134
    • Walsh, C.T.1
  • 31
    • 76649138924 scopus 로고    scopus 로고
    • Genetic engineering of macrolide biosynthesis: Past advances, current state, and future prospects
    • Park, S. R., Han, A. R., Ban, Y. H., Yoo, Y. J., Kim, E. J., and Yoon, Y. J. (2010) Genetic engineering of macrolide biosynthesis: Past advances, current state, and future prospects Appl. Microbiol. Biotechnol. 85, 1227-1239
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1227-1239
    • Park, S.R.1    Han, A.R.2    Ban, Y.H.3    Yoo, Y.J.4    Kim, E.J.5    Yoon, Y.J.6
  • 32
    • 0025081416 scopus 로고
    • An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea
    • Cortes, J., Haydock, S. F., Roberts, G. A., Bevitt, D. J., and Leadlay, P. F. (1990) An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea Nature 348, 176-178
    • (1990) Nature , vol.348 , pp. 176-178
    • Cortes, J.1    Haydock, S.F.2    Roberts, G.A.3    Bevitt, D.J.4    Leadlay, P.F.5
  • 33
    • 0026415106 scopus 로고
    • Modular organization of genes required for complex polyketide biosynthesis
    • Donadio, S., Staver, M. J., McAlpine, J. B., Swanson, S. J., and Katz, L. (1991) Modular organization of genes required for complex polyketide biosynthesis Science 252, 675-679
    • (1991) Science , vol.252 , pp. 675-679
    • Donadio, S.1    Staver, M.J.2    McAlpine, J.B.3    Swanson, S.J.4    Katz, L.5
  • 36
    • 33644950516 scopus 로고    scopus 로고
    • Extender unit and acyl carrier protein specificity of ketosynthase domains of the 6-deoxyerythronolide B synthase
    • Chen, A. Y., Schnarr, N. A., Kim, C. Y., Cane, D. E., and Khosla, C. (2006) Extender unit and acyl carrier protein specificity of ketosynthase domains of the 6-deoxyerythronolide B synthase J. Am. Chem. Soc. 128, 3067-3074
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3067-3074
    • Chen, A.Y.1    Schnarr, N.A.2    Kim, C.Y.3    Cane, D.E.4    Khosla, C.5
  • 37
    • 0037094002 scopus 로고    scopus 로고
    • Functional expression of genes involved in the biosynthesis of the novel polyketide chain extension unit, methoxymalonyl-acyl carrier protein, and engineered biosynthesis of 2-desmethyl-2-methoxy-6-deoxyerythronolide B
    • Kato, Y., Bai, L., Xue, Q., Revill, W. P., Yu, T. W., and Floss, H. G. (2002) Functional expression of genes involved in the biosynthesis of the novel polyketide chain extension unit, methoxymalonyl-acyl carrier protein, and engineered biosynthesis of 2-desmethyl-2-methoxy-6-deoxyerythronolide B J. Am. Chem. Soc. 124, 5268-5269
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5268-5269
    • Kato, Y.1    Bai, L.2    Xue, Q.3    Revill, W.P.4    Yu, T.W.5    Floss, H.G.6
  • 38
    • 0037617464 scopus 로고    scopus 로고
    • Mechanistic analysis of acyl transferase domain exchange in polyketide synthase modules
    • Hans, M., Hornung, A., Dziarnowski, A., Cane, D. E., and Khosla, C. (2003) Mechanistic analysis of acyl transferase domain exchange in polyketide synthase modules J. Am. Chem. Soc. 125, 5366-5374
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5366-5374
    • Hans, M.1    Hornung, A.2    Dziarnowski, A.3    Cane, D.E.4    Khosla, C.5
  • 39
    • 0030723673 scopus 로고    scopus 로고
    • Gain of function mutagenesis of the erythromycin polyketide synthase. 2. Engineered biosynthesis of an eight-membered ring tetraketide lactone
    • Kao, C. M., McPherson, M., McDaniel, R. N., Fu, H., Cane, D. E., and Khosla, C. (1997) Gain of function mutagenesis of the erythromycin polyketide synthase. 2. Engineered biosynthesis of an eight-membered ring tetraketide lactone J. Am. Chem. Soc. 119, 11339-11340
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11339-11340
    • Kao, C.M.1    McPherson, M.2    McDaniel, R.N.3    Fu, H.4    Cane, D.E.5    Khosla, C.6
  • 40
    • 34247518972 scopus 로고    scopus 로고
    • The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification
    • Zhang, C., Fu, Q., Albermann, C., Li, L., and Thorson, J. S. (2007) The in vitro characterization of the erythronolide mycarosyltransferase EryBV and its utility in macrolide diversification ChemBioChem 8, 385-390
    • (2007) ChemBioChem , vol.8 , pp. 385-390
    • Zhang, C.1    Fu, Q.2    Albermann, C.3    Li, L.4    Thorson, J.S.5
  • 41
    • 26844543758 scopus 로고    scopus 로고
    • In vitro reconstitution of EryCIII activity for the preparation of unnatural macrolides
    • Yuan, Y., Chung, H. S., Leimkuhler, C., Walsh, C. T., Kahne, D., and Walker, S. (2005) In vitro reconstitution of EryCIII activity for the preparation of unnatural macrolides J. Am. Chem. Soc. 127, 14128-14129
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14128-14129
    • Yuan, Y.1    Chung, H.S.2    Leimkuhler, C.3    Walsh, C.T.4    Kahne, D.5    Walker, S.6
  • 44
    • 77955588954 scopus 로고    scopus 로고
    • Using chemobiosynthesis and synthetic mini-polyketide synthases to produce pharmaceutical intermediates in Escherichia coli
    • Menzella, H. G., Carney, J. R., Li, Y., and Santi, D. V. (2010) Using chemobiosynthesis and synthetic mini-polyketide synthases to produce pharmaceutical intermediates in Escherichia coli Appl. Environ. Microbiol. 76, 5221-5227
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5221-5227
    • Menzella, H.G.1    Carney, J.R.2    Li, Y.3    Santi, D.V.4
  • 45
    • 33847076126 scopus 로고    scopus 로고
    • Rational design and assembly of synthetic trimodular polyketide synthases
    • Menzella, H. G., Carney, J. R., and Santi, D. V. (2007) Rational design and assembly of synthetic trimodular polyketide synthases Chem. Biol. 14, 143-151
    • (2007) Chem. Biol. , vol.14 , pp. 143-151
    • Menzella, H.G.1    Carney, J.R.2    Santi, D.V.3
  • 46
    • 33646109072 scopus 로고    scopus 로고
    • Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase
    • Zhang, W., Ames, B. D., Tsai, S. C., and Tang, Y. (2006) Engineered biosynthesis of a novel amidated polyketide, using the malonamyl-specific initiation module from the oxytetracycline polyketide synthase Appl. Environ. Microbiol. 72, 2573-2580
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2573-2580
    • Zhang, W.1    Ames, B.D.2    Tsai, S.C.3    Tang, Y.4
  • 47
    • 0039041428 scopus 로고
    • Biosynthesis of the tetracyclines. VII. 4-Hydroxy-6-methylpretetramid, an intermediate accumulated by a blocked mutant of Streptomyces aureofaciens
    • McCormick, J. R., Joachim, U. H., Jensen, E. R., Johnson, S., and Sjolander, N. O. (1965) Biosynthesis of the tetracyclines. VII. 4-Hydroxy-6-methylpretetramid, an intermediate accumulated by a blocked mutant of Streptomyces aureofaciens J. Am. Chem. Soc. 87, 1793-1794
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 1793-1794
    • McCormick, J.R.1    Joachim, U.H.2    Jensen, E.R.3    Johnson, S.4    Sjolander, N.O.5
  • 48
    • 0014408884 scopus 로고
    • Biosynthesis of the tetracyclines. IX. 4- Aminodedimethylaminoanhydrodemethylchlortetracycline from a mutant of Streptomyces aureofaciens
    • McCormick, J. R., Jensen, E. R., Johnson, S., and Sjolander, N. O. (1968) Biosynthesis of the tetracyclines. IX. 4- Aminodedimethylaminoanhydrodemethylchlortetracycline from a mutant of Streptomyces aureofaciens J. Am. Chem. Soc. 90, 2201-2202
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 2201-2202
    • McCormick, J.R.1    Jensen, E.R.2    Johnson, S.3    Sjolander, N.O.4
  • 49
    • 0014439280 scopus 로고
    • Biosynthesis of the tetracyclines. XII. Anhydrodemethylchlortetracycline from a mutant of Streptomyces aureofaciens
    • McCormick, J. R. and Jensen, E. R. (1969) Biosynthesis of the tetracyclines. XII. Anhydrodemethylchlortetracycline from a mutant of Streptomyces aureofaciens J. Am. Chem. Soc. 91, 206
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 206
    • McCormick, J.R.1    Jensen, E.R.2
  • 50
    • 10144238760 scopus 로고
    • Biosynthesis of the tetracyclines. VIII. Characterization of 4-hydroxy-6-methylpretetramid
    • McCormick, J. R. and Jensen, E. R. (1965) Biosynthesis of the tetracyclines. VIII. Characterization of 4-hydroxy-6-methylpretetramid J. Am. Chem. Soc. 87, 1794-1795
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 1794-1795
    • McCormick, J.R.1    Jensen, E.R.2
  • 52
    • 34548474531 scopus 로고    scopus 로고
    • Investigation of early tailoring reactions in the oxytetracycline biosynthetic pathway
    • Zhang, W., Watanabe, K., Wang, C. C., and Tang, Y. (2007) Investigation of early tailoring reactions in the oxytetracycline biosynthetic pathway J. Biol. Chem. 282, 25717-25725
    • (2007) J. Biol. Chem. , vol.282 , pp. 25717-25725
    • Zhang, W.1    Watanabe, K.2    Wang, C.C.3    Tang, Y.4
  • 55
    • 77956243990 scopus 로고    scopus 로고
    • Oxytetracycline biosynthesis
    • Pickens, L. B. and Tang, Y. (2010) Oxytetracycline biosynthesis J. Biol. Chem. 285, 27509-27515
    • (2010) J. Biol. Chem. , vol.285 , pp. 27509-27515
    • Pickens, L.B.1    Tang, Y.2
  • 56
    • 84865515585 scopus 로고    scopus 로고
    • Synthetic biological approaches to natural product biosynthesis
    • Winter, J. M. and Tang, Y. (2012) Synthetic biological approaches to natural product biosynthesis Curr. Opin. Biotechnol. 23, 736-743
    • (2012) Curr. Opin. Biotechnol. , vol.23 , pp. 736-743
    • Winter, J.M.1    Tang, Y.2
  • 57
    • 77950574401 scopus 로고    scopus 로고
    • Heterologous expression of the oxytetracycline biosynthetic pathway in Myxococcus xanthus
    • Stevens, D. C., Henry, M. R., Murphy, K. A., and Boddy, C. N. (2010) Heterologous expression of the oxytetracycline biosynthetic pathway in Myxococcus xanthus Appl. Environ. Microbiol. 76, 2681-2683
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2681-2683
    • Stevens, D.C.1    Henry, M.R.2    Murphy, K.A.3    Boddy, C.N.4
  • 58
    • 70349546337 scopus 로고    scopus 로고
    • Identification of OxyE as an ancillary oxygenase during tetracycline biosynthesis
    • Wang, P., Zhang, W., Zhan, J., and Tang, Y. (2009) Identification of OxyE as an ancillary oxygenase during tetracycline biosynthesis ChemBioChem 10, 1544-1550
    • (2009) ChemBioChem , vol.10 , pp. 1544-1550
    • Wang, P.1    Zhang, W.2    Zhan, J.3    Tang, Y.4
  • 59
    • 43249112810 scopus 로고    scopus 로고
    • Identifying the minimal enzymes required for anhydrotetracycline biosynthesis
    • Zhang, W., Watanabe, K., Cai, X., Jung, M. E., Tang, Y., and Zhan, J. (2008) Identifying the minimal enzymes required for anhydrotetracycline biosynthesis J. Am. Chem. Soc. 130, 6068-6069
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6068-6069
    • Zhang, W.1    Watanabe, K.2    Cai, X.3    Jung, M.E.4    Tang, Y.5    Zhan, J.6
  • 60
    • 0028246660 scopus 로고
    • Molecular requirements for the inhibition of the tetracycline antiport protein and the effect of potent inhibitors on the growth of tetracycline-resistant bacteria
    • Nelson, M. L., Park, B. H., and Levy, S. B. (1994) Molecular requirements for the inhibition of the tetracycline antiport protein and the effect of potent inhibitors on the growth of tetracycline-resistant bacteria J. Med. Chem. 37, 1355-1361
    • (1994) J. Med. Chem. , vol.37 , pp. 1355-1361
    • Nelson, M.L.1    Park, B.H.2    Levy, S.B.3
  • 61
    • 35448986243 scopus 로고    scopus 로고
    • The chemistry and biology of the tetracyclines
    • Chapter 11, Academic Press, Waltham, MA
    • Nelson, M. L. (2002) in The Chemistry and Biology of the Tetracyclines, Annual Reports in Medicinal Chemistry, Vol. 37, Chapter 11, pp 105-114, Academic Press, Waltham, MA.
    • (2002) Annual Reports in Medicinal Chemistry , vol.37 , pp. 105-114
    • Nelson, M.L.1
  • 62
    • 0034973583 scopus 로고    scopus 로고
    • Tetracycline antibiotics: Mode of action, applications, molecular biology, and epidemiology of bacterial resistance
    • Chopra, I. and Roberts, M. (2001) Tetracycline antibiotics: Mode of action, applications, molecular biology, and epidemiology of bacterial resistance Microbiol. Mol. Biol. Rev. 65, 232-260
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 232-260
    • Chopra, I.1    Roberts, M.2
  • 64
    • 59849119654 scopus 로고    scopus 로고
    • Recombineering: A homologous recombination-based method of genetic engineering
    • Sharan, S. K., Thomason, L. C., Kuznetsov, S. G., and Court, D. (2009) Recombineering: A homologous recombination-based method of genetic engineering Nat. Protoc. 4, 206-223
    • (2009) Nat. Protoc. , vol.4 , pp. 206-223
    • Sharan, S.K.1    Thomason, L.C.2    Kuznetsov, S.G.3    Court, D.4
  • 65
    • 0036953835 scopus 로고    scopus 로고
    • Genetic engineering using homologous recombination
    • Court, D. L., Sawitzke, J. A., and Thomason, L. C. (2002) Genetic engineering using homologous recombination Annu. Rev. Genet. 36, 361-388
    • (2002) Annu. Rev. Genet. , vol.36 , pp. 361-388
    • Court, D.L.1    Sawitzke, J.A.2    Thomason, L.C.3
  • 66
    • 0035810938 scopus 로고    scopus 로고
    • High efficiency mutagenesis, repair, and engineering of chromosomal DNA using single-stranded oligonucleotides
    • Ellis, H. M., Yu, D., DiTizio, T., and Court, D. L. (2001) High efficiency mutagenesis, repair, and engineering of chromosomal DNA using single-stranded oligonucleotides Proc. Natl. Acad. Sci. U.S.A. 98, 6742-6746
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6742-6746
    • Ellis, H.M.1    Yu, D.2    Ditizio, T.3    Court, D.L.4
  • 67
    • 78049348201 scopus 로고    scopus 로고
    • DNA construction: Homemade or ordered out?
    • Carr, P. A. (2010) DNA construction: Homemade or ordered out? Nat. Methods 7, 887-889
    • (2010) Nat. Methods , vol.7 , pp. 887-889
    • Carr, P.A.1
  • 69
    • 70350475417 scopus 로고    scopus 로고
    • Idempotent vector design for standard assembly of Biobricks
    • Knight, T. (2003) Idempotent vector design for standard assembly of Biobricks DSpace http://hdl.handle.net/1721.1/21168
    • (2003) DSpace
    • Knight, T.1
  • 71
    • 65849183178 scopus 로고    scopus 로고
    • Golden gate shuffling: A one-pot DNA shuffling method based on type IIs restriction enzymes
    • Engler, C., Gruetzner, R., Kandzia, R., and Marillonnet, S. (2009) Golden gate shuffling: A one-pot DNA shuffling method based on type IIs restriction enzymes PLoS One 4, e5553
    • (2009) PLoS One , vol.4 , pp. 5553
    • Engler, C.1    Gruetzner, R.2    Kandzia, R.3    Marillonnet, S.4
  • 72
    • 68149136937 scopus 로고    scopus 로고
    • Circular polymerase extension cloning of complex gene libraries and pathways
    • Quan, J. and Tian, J. (2009) Circular polymerase extension cloning of complex gene libraries and pathways PLoS One 4, e6441
    • (2009) PLoS One , vol.4 , pp. 6441
    • Quan, J.1    Tian, J.2
  • 73
    • 68949161807 scopus 로고    scopus 로고
    • Programming cells by multiplex genome engineering and accelerated evolution
    • Wang, H. H., Isaacs, F. J., Carr, P. A., Sun, Z. Z., Xu, G., Forest, C. R., and Church, G. M. (2009) Programming cells by multiplex genome engineering and accelerated evolution Nature 460, 894-898
    • (2009) Nature , vol.460 , pp. 894-898
    • Wang, H.H.1    Isaacs, F.J.2    Carr, P.A.3    Sun, Z.Z.4    Xu, G.5    Forest, C.R.6    Church, G.M.7
  • 75
    • 0025757012 scopus 로고
    • Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution
    • Abrahmsen, L., Tom, J., Burnier, J., Butcher, K. A., Kossiakoff, A., and Wells, J. A. (1991) Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution Biochemistry (N. Y.) 30, 4151-4159
    • (1991) Biochemistry (N. Y.) , vol.30 , pp. 4151-4159
    • Abrahmsen, L.1    Tom, J.2    Burnier, J.3    Butcher, K.A.4    Kossiakoff, A.5    Wells, J.A.6
  • 77
    • 32544440280 scopus 로고    scopus 로고
    • Phage display systems and their applications
    • Paschke, M. (2006) Phage display systems and their applications Appl. Microbiol. Biotechnol. 70, 2-11
    • (2006) Appl. Microbiol. Biotechnol. , vol.70 , pp. 2-11
    • Paschke, M.1
  • 78
    • 80052628399 scopus 로고    scopus 로고
    • Bacterial display in combinatorial protein engineering
    • Lofblom, J. (2011) Bacterial display in combinatorial protein engineering Biotechnol. J. 6, 1115-1129
    • (2011) Biotechnol. J. , vol.6 , pp. 1115-1129
    • Lofblom, J.1
  • 79
    • 34648832245 scopus 로고    scopus 로고
    • Yeast surface display for protein engineering and characterization
    • Gai, S. A. and Wittrup, K. D. (2007) Yeast surface display for protein engineering and characterization Curr. Opin. Struct. Biol. 17, 467-473
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 467-473
    • Gai, S.A.1    Wittrup, K.D.2
  • 80
    • 84555196342 scopus 로고    scopus 로고
    • Ribosome display: A perspective
    • Pluckthun, A. (2012) Ribosome display: A perspective Methods Mol. Biol. 805, 3-28
    • (2012) Methods Mol. Biol. , vol.805 , pp. 3-28
    • Pluckthun, A.1
  • 81
    • 33947167309 scopus 로고    scopus 로고
    • Selection of single domain binding proteins by covalent DNA display
    • Bertschinger, J., Grabulovski, D., and Neri, D. (2007) Selection of single domain binding proteins by covalent DNA display Protein Eng., Des. Sel. 20, 57-68
    • (2007) Protein Eng., Des. Sel. , vol.20 , pp. 57-68
    • Bertschinger, J.1    Grabulovski, D.2    Neri, D.3
  • 82
    • 79955534060 scopus 로고    scopus 로고
    • A system for the continuous directed evolution of biomolecules
    • Esvelt, K. M., Carlson, J. C., and Liu, D. R. (2011) A system for the continuous directed evolution of biomolecules Nature 472, 499-503
    • (2011) Nature , vol.472 , pp. 499-503
    • Esvelt, K.M.1    Carlson, J.C.2    Liu, D.R.3
  • 83
    • 67650472128 scopus 로고    scopus 로고
    • Traceless protein splicing utilizing evolved split inteins
    • Lockless, S. W. and Muir, T. W. (2009) Traceless protein splicing utilizing evolved split inteins Proc. Natl. Acad. Sci. U.S.A. 106, 10999-11004
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10999-11004
    • Lockless, S.W.1    Muir, T.W.2
  • 84
    • 33748551323 scopus 로고    scopus 로고
    • Protein splicing in cis and in trans
    • Saleh, L. and Perler, F. B. (2006) Protein splicing in cis and in trans Chem. Rec. 6, 183-193
    • (2006) Chem. Rec. , vol.6 , pp. 183-193
    • Saleh, L.1    Perler, F.B.2
  • 85
    • 77950842894 scopus 로고    scopus 로고
    • Spontaneous intermolecular amide bond formation between side chains for irreversible peptide targeting
    • Zakeri, B. and Howarth, M. (2010) Spontaneous intermolecular amide bond formation between side chains for irreversible peptide targeting J. Am. Chem. Soc. 132, 4526-4527
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4526-4527
    • Zakeri, B.1    Howarth, M.2
  • 87
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: Logic, machinery, and mechanisms
    • Fischbach, M. A. and Walsh, C. T. (2006) Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: Logic, machinery, and mechanisms Chem. Rev. 106, 3468-3496
    • (2006) Chem. Rev. , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 89
    • 33845709126 scopus 로고    scopus 로고
    • Molecular engineering approaches to peptide, polyketide and other antibiotics
    • Baltz, R. H. (2006) Molecular engineering approaches to peptide, polyketide and other antibiotics Nat. Biotechnol. 24, 1533-1540
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1533-1540
    • Baltz, R.H.1
  • 91
    • 68149132445 scopus 로고    scopus 로고
    • Structural insights into nonribosomal peptide enzymatic assembly lines
    • Koglin, A. and Walsh, C. T. (2009) Structural insights into nonribosomal peptide enzymatic assembly lines Nat. Prod. Rep. 26, 987-1000
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 987-1000
    • Koglin, A.1    Walsh, C.T.2
  • 92
    • 77951294519 scopus 로고    scopus 로고
    • Nonribosomal peptide synthetases: Structures and dynamics
    • Strieker, M., Tanovic, A., and Marahiel, M. A. (2010) Nonribosomal peptide synthetases: Structures and dynamics Curr. Opin. Struct. Biol. 20, 234-240
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 234-240
    • Strieker, M.1    Tanovic, A.2    Marahiel, M.A.3
  • 93
    • 68149132445 scopus 로고    scopus 로고
    • Structural insights into nonribosomal peptide enzymatic assembly lines
    • Koglin, A. and Walsh, C. T. (2009) Structural insights into nonribosomal peptide enzymatic assembly lines Nat. Prod. Rep. 26, 987-1000
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 987-1000
    • Koglin, A.1    Walsh, C.T.2
  • 94
    • 14844339524 scopus 로고    scopus 로고
    • Glycopeptide and lipoglycopeptide antibiotics
    • Kahne, D., Leimkuhler, C., Lu, W., and Walsh, C. (2005) Glycopeptide and lipoglycopeptide antibiotics Chem. Rev. 105, 425-448
    • (2005) Chem. Rev. , vol.105 , pp. 425-448
    • Kahne, D.1    Leimkuhler, C.2    Lu, W.3    Walsh, C.4
  • 98
    • 2942665465 scopus 로고    scopus 로고
    • The safety and efficacy of daptomycin for the treatment of complicated skin and skin-structure infections
    • Daptomycin 98-01 and 99-01 Investigators
    • Arbeit, R. D., Maki, D., Tally, F. P., Campanaro, E., Eisenstein, B. I., and Daptomycin 98-01 and 99-01 Investigators (2004) The safety and efficacy of daptomycin for the treatment of complicated skin and skin-structure infections Clin. Infect. Dis. 38, 1673-1681
    • (2004) Clin. Infect. Dis. , vol.38 , pp. 1673-1681
    • Arbeit, R.D.1    Maki, D.2    Tally, F.P.3    Campanaro, E.4    Eisenstein, B.I.5
  • 99
    • 20444384347 scopus 로고    scopus 로고
    • Inhibition of daptomycin by pulmonary surfactant: In vitro modeling and clinical impact
    • Silverman, J. A., Mortin, L. I., Vanpraagh, A. D., Li, T., and Alder, J. (2005) Inhibition of daptomycin by pulmonary surfactant: In vitro modeling and clinical impact J. Infect. Dis. 191, 2149-2152
    • (2005) J. Infect. Dis. , vol.191 , pp. 2149-2152
    • Silverman, J.A.1    Mortin, L.I.2    Vanpraagh, A.D.3    Li, T.4    Alder, J.5
  • 100
    • 64749086503 scopus 로고    scopus 로고
    • Structure and function of the glycopeptide N-methyltransferase MtfA, a tool for the biosynthesis of modified glycopeptide antibiotics
    • Shi, R., Lamb, S. S., Zakeri, B., Proteau, A., Cui, Q., Sulea, T., Matte, A., Wright, G. D., and Cygler, M. (2009) Structure and function of the glycopeptide N-methyltransferase MtfA, a tool for the biosynthesis of modified glycopeptide antibiotics Chem. Biol. 16, 401-410
    • (2009) Chem. Biol. , vol.16 , pp. 401-410
    • Shi, R.1    Lamb, S.S.2    Zakeri, B.3    Proteau, A.4    Cui, Q.5    Sulea, T.6    Matte, A.7    Wright, G.D.8    Cygler, M.9
  • 101
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms Nature 415, 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 102
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E. and Sahl, H. G. (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotechnol. 24, 1551-1557
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 103
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: How different are they?
    • Henriques, S. T., Melo, M. N., and Castanho, M. A. (2006) Cell-penetrating peptides and antimicrobial peptides: How different are they? Biochem. J. 399, 1-7
    • (2006) Biochem. J. , vol.399 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.3
  • 104
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R. E. and Sahl, H. G. (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies Nat. Biotechnol. 24, 1551-1557
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 105
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo, M. N., Ferre, R., and Castanho, M. A. (2009) Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations Nat. Rev. Microbiol. 7, 245-250
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3
  • 106
    • 0242386506 scopus 로고    scopus 로고
    • Binding affinities of host-guest, protein-ligand, and protein-transition-state complexes
    • Houk, K. N., Leach, A. G., Kim, S. P., and Zhang, X. (2003) Binding affinities of host-guest, protein-ligand, and protein-transition-state complexes Angew. Chem., Int. Ed. 42, 4872-4897
    • (2003) Angew. Chem., Int. Ed. , vol.42 , pp. 4872-4897
    • Houk, K.N.1    Leach, A.G.2    Kim, S.P.3    Zhang, X.4
  • 107
    • 33847073370 scopus 로고    scopus 로고
    • Expanding the metabolic engineering toolbox: More options to engineer cells
    • Tyo, K. E., Alper, H. S., and Stephanopoulos, G. N. (2007) Expanding the metabolic engineering toolbox: More options to engineer cells Trends Biotechnol. 25, 132-137
    • (2007) Trends Biotechnol. , vol.25 , pp. 132-137
    • Tyo, K.E.1    Alper, H.S.2    Stephanopoulos, G.N.3
  • 108
    • 69349092183 scopus 로고    scopus 로고
    • Coupling molecular dynamics simulations with experiments for the rational design of indolicidin-analogous antimicrobial peptides
    • Tsai, C. W., Hsu, N. Y., Wang, C. H., Lu, C. Y., Chang, Y., Tsai, H. H., and Ruaan, R. C. (2009) Coupling molecular dynamics simulations with experiments for the rational design of indolicidin-analogous antimicrobial peptides J. Mol. Biol. 392, 837-854
    • (2009) J. Mol. Biol. , vol.392 , pp. 837-854
    • Tsai, C.W.1    Hsu, N.Y.2    Wang, C.H.3    Lu, C.Y.4    Chang, Y.5    Tsai, H.H.6    Ruaan, R.C.7
  • 109
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • Chan, D. I., Prenner, E. J., and Vogel, H. J. (2006) Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action Biochim. Biophys. Acta 1758, 1184-1202
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 110
    • 0030997215 scopus 로고    scopus 로고
    • Improved activity of a synthetic indolicidin analog
    • Falla, T. J. and Hancock, R. E. (1997) Improved activity of a synthetic indolicidin analog Antimicrob. Agents Chemother. 41, 771-775
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 771-775
    • Falla, T.J.1    Hancock, R.E.2
  • 111
    • 60749130267 scopus 로고    scopus 로고
    • Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs
    • Cherkasov, A., Hilpert, K., Jenssen, H., Fjell, C. D., Waldbrook, M., Mullaly, S. C., Volkmer, R., and Hancock, R. E. (2009) Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs ACS Chem. Biol. 4, 65-74
    • (2009) ACS Chem. Biol. , vol.4 , pp. 65-74
    • Cherkasov, A.1    Hilpert, K.2    Jenssen, H.3    Fjell, C.D.4    Waldbrook, M.5    Mullaly, S.C.6    Volkmer, R.7    Hancock, R.E.8
  • 113
    • 33645834508 scopus 로고    scopus 로고
    • Experimental evolution of resistance to an antimicrobial peptide
    • Perron, G. G., Zasloff, M., and Bell, G. (2006) Experimental evolution of resistance to an antimicrobial peptide Proc. Biol. Sci. 273, 251-256
    • (2006) Proc. Biol. Sci. , vol.273 , pp. 251-256
    • Perron, G.G.1    Zasloff, M.2    Bell, G.3
  • 115
    • 64549112594 scopus 로고    scopus 로고
    • Design and activity of a 'dual-targeted' antimicrobial peptide
    • He, J., Anderson, M. H., Shi, W., and Eckert, R. (2009) Design and activity of a 'dual-targeted' antimicrobial peptide Int. J. Antimicrob. Agents 33, 532-537
    • (2009) Int. J. Antimicrob. Agents , vol.33 , pp. 532-537
    • He, J.1    Anderson, M.H.2    Shi, W.3    Eckert, R.4
  • 116
    • 0000378637 scopus 로고
    • On the antibacterial action of cultures of a Penicillium, with special reference to their use in the isolation of B. influenzae
    • Fleming, A. (1929) On the antibacterial action of cultures of a Penicillium, with special reference to their use in the isolation of B. influenzae Br. J. Exp. Pathol. 10, 226-236
    • (1929) Br. J. Exp. Pathol. , vol.10 , pp. 226-236
    • Fleming, A.1
  • 117
    • 84860389302 scopus 로고    scopus 로고
    • The next generation of bacteriophage therapy
    • Lu, T. K. and Koeris, M. S. (2011) The next generation of bacteriophage therapy Curr. Opin. Microbiol. 14, 524-531
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 524-531
    • Lu, T.K.1    Koeris, M.S.2
  • 119
    • 80053937055 scopus 로고    scopus 로고
    • The antibiotic R&D pipeline: An update
    • Jabes, D. (2011) The antibiotic R&D pipeline: An update Curr. Opin. Microbiol. 14, 564-569
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 564-569
    • Jabes, D.1
  • 120
    • 84868663036 scopus 로고    scopus 로고
    • Turning a new phage
    • Gravitz, L. (2012) Turning a new phage Nat. Med. 18, 1318-1320
    • (2012) Nat. Med. , vol.18 , pp. 1318-1320
    • Gravitz, L.1
  • 121
    • 84861387333 scopus 로고    scopus 로고
    • Sticky situations: Key components that control bacterial surface attachment
    • Petrova, O. E. and Sauer, K. (2012) Sticky situations: Key components that control bacterial surface attachment J. Bacteriol. 194, 2413-2425
    • (2012) J. Bacteriol. , vol.194 , pp. 2413-2425
    • Petrova, O.E.1    Sauer, K.2
  • 123
  • 124
    • 22144463151 scopus 로고    scopus 로고
    • Biofilms and antibiotic therapy: Is there a role for combating bacterial resistance by the use of novel drug delivery systems?
    • Smith, A. W. (2005) Biofilms and antibiotic therapy: Is there a role for combating bacterial resistance by the use of novel drug delivery systems? Adv. Drug Delivery Rev. 57, 1539-1550
    • (2005) Adv. Drug Delivery Rev. , vol.57 , pp. 1539-1550
    • Smith, A.W.1
  • 125
    • 77952549113 scopus 로고    scopus 로고
    • A tale of two pili: Assembly and function of pili in bacteria
    • Kline, K. A., Dodson, K. W., Caparon, M. G., and Hultgren, S. J. (2010) A tale of two pili: Assembly and function of pili in bacteria Trends Microbiol. 18, 224-232
    • (2010) Trends Microbiol. , vol.18 , pp. 224-232
    • Kline, K.A.1    Dodson, K.W.2    Caparon, M.G.3    Hultgren, S.J.4
  • 126
    • 33749184817 scopus 로고    scopus 로고
    • Pili with strong attachments: Gram-positive bacteria do it differently
    • Scott, J. R. and Zahner, D. (2006) Pili with strong attachments: Gram-positive bacteria do it differently Mol. Microbiol. 62, 320-330
    • (2006) Mol. Microbiol. , vol.62 , pp. 320-330
    • Scott, J.R.1    Zahner, D.2
  • 127
    • 36849072428 scopus 로고    scopus 로고
    • Stabilizing isopeptide bonds revealed in Gram-positive bacterial pilus structure
    • Kang, H. J., Coulibaly, F., Clow, F., Proft, T., and Baker, E. N. (2007) Stabilizing isopeptide bonds revealed in Gram-positive bacterial pilus structure Science 318, 1625-1628
    • (2007) Science , vol.318 , pp. 1625-1628
    • Kang, H.J.1    Coulibaly, F.2    Clow, F.3    Proft, T.4    Baker, E.N.5
  • 128
    • 68949105832 scopus 로고    scopus 로고
    • Intramolecular isopeptide bonds give thermodynamic and proteolytic stability to the major pilin protein of Streptococcus pyogenes
    • Kang, H. J. and Baker, E. N. (2009) Intramolecular isopeptide bonds give thermodynamic and proteolytic stability to the major pilin protein of Streptococcus pyogenes J. Biol. Chem. 284, 20729-20737
    • (2009) J. Biol. Chem. , vol.284 , pp. 20729-20737
    • Kang, H.J.1    Baker, E.N.2
  • 129
    • 77951250536 scopus 로고    scopus 로고
    • Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes
    • Alegre-Cebollada, J., Badilla, C. L., and Fernandez, J. M. (2010) Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes J. Biol. Chem. 285, 11235-11242
    • (2010) J. Biol. Chem. , vol.285 , pp. 11235-11242
    • Alegre-Cebollada, J.1    Badilla, C.L.2    Fernandez, J.M.3
  • 131
    • 79951838791 scopus 로고    scopus 로고
    • Intramolecular isopeptide bonds: Protein crosslinks built for stress?
    • Kang, H. J. and Baker, E. N. (2011) Intramolecular isopeptide bonds: Protein crosslinks built for stress? Trends Biochem. Sci. 36, 229-237
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 229-237
    • Kang, H.J.1    Baker, E.N.2
  • 132
    • 77958613852 scopus 로고    scopus 로고
    • A highly unusual thioester bond in a pilus adhesin is required for efficient host cell interaction
    • Pointon, J. A., Smith, W. D., Saalbach, G., Crow, A., Kehoe, M. A., and Banfield, M. J. (2010) A highly unusual thioester bond in a pilus adhesin is required for efficient host cell interaction J. Biol. Chem. 285, 33858-33866
    • (2010) J. Biol. Chem. , vol.285 , pp. 33858-33866
    • Pointon, J.A.1    Smith, W.D.2    Saalbach, G.3    Crow, A.4    Kehoe, M.A.5    Banfield, M.J.6
  • 133
    • 34547448587 scopus 로고    scopus 로고
    • Dispersing biofilms with engineered enzymatic bacteriophage
    • Lu, T. K. and Collins, J. J. (2007) Dispersing biofilms with engineered enzymatic bacteriophage Proc. Natl. Acad. Sci. U.S.A. 104, 11197-11202
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 11197-11202
    • Lu, T.K.1    Collins, J.J.2
  • 134
    • 11144330206 scopus 로고    scopus 로고
    • Depolymerization of beta-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms
    • Itoh, Y., Wang, X., Hinnebusch, B. J., 3rd, and Romeo, T. (2005) Depolymerization of beta-1,6-N-acetyl-D-glucosamine disrupts the integrity of diverse bacterial biofilms J. Bacteriol. 187, 382-387
    • (2005) J. Bacteriol. , vol.187 , pp. 382-387
    • Itoh, Y.1    Wang, X.2    Hinnebusch, B.J.3    Preston, J.F.4    Romeo, T.5
  • 136
    • 63849290890 scopus 로고    scopus 로고
    • Engineered bacteriophage targeting gene networks as adjuvants for antibiotic therapy
    • Lu, T. K. and Collins, J. J. (2009) Engineered bacteriophage targeting gene networks as adjuvants for antibiotic therapy Proc. Natl. Acad. Sci. U.S.A. 106, 4629-4634
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4629-4634
    • Lu, T.K.1    Collins, J.J.2
  • 137
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski, M. A., Dwyer, D. J., Hayete, B., Lawrence, C. A., and Collins, J. J. (2007) A common mechanism of cellular death induced by bactericidal antibiotics Cell 130, 797-810
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 139
    • 84855894994 scopus 로고    scopus 로고
    • Reversing bacterial resistance to antibiotics by phage-mediated delivery of dominant sensitive genes
    • Edgar, R., Friedman, N., Molshanski-Mor, S., and Qimron, U. (2012) Reversing bacterial resistance to antibiotics by phage-mediated delivery of dominant sensitive genes Appl. Environ. Microbiol. 78, 744-751
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 744-751
    • Edgar, R.1    Friedman, N.2    Molshanski-Mor, S.3    Qimron, U.4
  • 140
    • 78149357025 scopus 로고    scopus 로고
    • Clavulanic acid biosynthesis and genetic manipulation for its overproduction
    • Song, J. Y., Jensen, S. E., and Lee, K. J. (2010) Clavulanic acid biosynthesis and genetic manipulation for its overproduction Appl. Microbiol. Biotechnol. 88, 659-669
    • (2010) Appl. Microbiol. Biotechnol. , vol.88 , pp. 659-669
    • Song, J.Y.1    Jensen, S.E.2    Lee, K.J.3
  • 141
    • 55049135817 scopus 로고    scopus 로고
    • Bacteriophage lysins as effective antibacterials
    • Fischetti, V. A. (2008) Bacteriophage lysins as effective antibacterials Curr. Opin. Microbiol. 11, 393-400
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 393-400
    • Fischetti, V.A.1
  • 143
    • 77950126213 scopus 로고    scopus 로고
    • Synergism between a novel chimeric lysin and oxacillin protects against infection by methicillin-resistant Staphylococcus aureus
    • Daniel, A., Euler, C., Collin, M., Chahales, P., Gorelick, K. J., and Fischetti, V. A. (2010) Synergism between a novel chimeric lysin and oxacillin protects against infection by methicillin-resistant Staphylococcus aureus Antimicrob. Agents Chemother. 54, 1603-1612
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 1603-1612
    • Daniel, A.1    Euler, C.2    Collin, M.3    Chahales, P.4    Gorelick, K.J.5    Fischetti, V.A.6
  • 144
    • 78751697614 scopus 로고    scopus 로고
    • A novel chimeric lysin shows superiority to mupirocin for skin decolonization of methicillin-resistant and -sensitive Staphylococcus aureus strains
    • Pastagia, M., Euler, C., Chahales, P., Fuentes-Duculan, J., Krueger, J. G., and Fischetti, V. A. (2011) A novel chimeric lysin shows superiority to mupirocin for skin decolonization of methicillin-resistant and -sensitive Staphylococcus aureus strains Antimicrob. Agents Chemother. 55, 738-744
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 738-744
    • Pastagia, M.1    Euler, C.2    Chahales, P.3    Fuentes-Duculan, J.4    Krueger, J.G.5    Fischetti, V.A.6
  • 145
    • 0036589162 scopus 로고    scopus 로고
    • The pyocins of Pseudomonas aeruginosa
    • Michel-Briand, Y. and Baysse, C. (2002) The pyocins of Pseudomonas aeruginosa Biochimie 84, 499-510
    • (2002) Biochimie , vol.84 , pp. 499-510
    • Michel-Briand, Y.1    Baysse, C.2
  • 146
    • 45749147914 scopus 로고    scopus 로고
    • Retargeting R-type pyocins to generate novel bactericidal protein complexes
    • Williams, S. R., Gebhart, D., Martin, D. W., and Scholl, D. (2008) Retargeting R-type pyocins to generate novel bactericidal protein complexes Appl. Environ. Microbiol. 74, 3868-3876
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 3868-3876
    • Williams, S.R.1    Gebhart, D.2    Martin, D.W.3    Scholl, D.4
  • 147
    • 67650072870 scopus 로고    scopus 로고
    • An engineered R-type pyocin is a highly specific and sensitive bactericidal agent for the food-borne pathogen Escherichia coli O157:H7
    • Scholl, D., Cooley, M., Williams, S. R., Gebhart, D., Martin, D., Bates, A., and Mandrell, R. (2009) An engineered R-type pyocin is a highly specific and sensitive bactericidal agent for the food-borne pathogen Escherichia coli O157:H7 Antimicrob. Agents Chemother. 53, 3074-3080
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 3074-3080
    • Scholl, D.1    Cooley, M.2    Williams, S.R.3    Gebhart, D.4    Martin, D.5    Bates, A.6    Mandrell, R.7
  • 149
  • 152
    • 84859270554 scopus 로고    scopus 로고
    • Antibiotic resistance is ancient: Implications for drug discovery
    • Wright, G. D. and Poinar, H. (2012) Antibiotic resistance is ancient: Implications for drug discovery Trends Microbiol. 20, 157-159
    • (2012) Trends Microbiol. , vol.20 , pp. 157-159
    • Wright, G.D.1    Poinar, H.2
  • 153
    • 80051585072 scopus 로고    scopus 로고
    • The future of industrial antibiotic production: From random mutagenesis to synthetic biology
    • Medema, M. H., Alam, M. T., Breitling, R., and Takano, E. (2011) The future of industrial antibiotic production: From random mutagenesis to synthetic biology Bioeng. Bugs 2, 230-233
    • (2011) Bioeng. Bugs , vol.2 , pp. 230-233
    • Medema, M.H.1    Alam, M.T.2    Breitling, R.3    Takano, E.4
  • 154
    • 80052484996 scopus 로고    scopus 로고
    • Synthetic biology moving into the clinic
    • Ruder, W. C., Lu, T., and Collins, J. J. (2011) Synthetic biology moving into the clinic Science 333, 1248-1252
    • (2011) Science , vol.333 , pp. 1248-1252
    • Ruder, W.C.1    Lu, T.2    Collins, J.J.3
  • 155
    • 84864258391 scopus 로고    scopus 로고
    • Synthetic biology: An emerging engineering discipline
    • Cheng, A. A. and Lu, T. K. (2012) Synthetic biology: An emerging engineering discipline Annu. Rev. Biomed. Eng. 14, 155-178
    • (2012) Annu. Rev. Biomed. Eng. , vol.14 , pp. 155
    • Cheng, A.A.1    Lu, T.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.