메뉴 건너뛰기




Volumn 71, Issue 7, 2005, Pages 3512-3518

Role of porins in sensitivity of Escherichia coli to antibacterial activity of the lactoperoxidase enzyme system

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; DEGRADATION; ESCHERICHIA COLI; GENES; MUTAGENESIS; POLYSACCHARIDES; SODIUM COMPOUNDS;

EID: 22144462529     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.7.3512-3518.2005     Document Type: Article
Times cited : (25)

References (54)
  • 1
    • 0015973774 scopus 로고
    • Protein composition of outer membrane of Salmonella typhimurium-effect of lipopolysaccharide mutations
    • Ames, G. F., E. N. Spudich, and H. Nikaido. 1974. Protein composition of outer membrane of Salmonella typhimurium-effect of lipopolysaccharide mutations. J. Bacteriol. 117:406-416.
    • (1974) J. Bacteriol. , vol.117 , pp. 406-416
    • Ames, G.F.1    Spudich, E.N.2    Nikaido, H.3
  • 2
    • 0032536195 scopus 로고    scopus 로고
    • Voltage-gating of Escherichia coli porin: A cystine-scanning mutagenesis study of loop 3
    • Bainbridge, G., H. Mobasheri, G. A. Armstrong, E. J. A. Lea, and J. H. Lakey. 1998. Voltage-gating of Escherichia coli porin: a cystine-scanning mutagenesis study of loop 3. J. Mol. Biol. 275:171-176.
    • (1998) J. Mol. Biol. , vol.275 , pp. 171-176
    • Bainbridge, G.1    Mobasheri, H.2    Armstrong, G.A.3    Lea, E.J.A.4    Lakey, J.H.5
  • 3
    • 0026648024 scopus 로고
    • Mutations in a central highly conserved non-DNA-binding region of OmpR, an Escherichia coli transcriptional activator, influence its DNA-binding ability
    • Brissette, R. E., K. Tsung, and M. Inouye. 1992. Mutations in a central highly conserved non-DNA-binding region of OmpR, an Escherichia coli transcriptional activator, influence its DNA-binding ability. J. Bacteriol. 174:4907-4912.
    • (1992) J. Bacteriol. , vol.174 , pp. 4907-4912
    • Brissette, R.E.1    Tsung, K.2    Inouye, M.3
  • 4
    • 2642565930 scopus 로고    scopus 로고
    • Hydroxyl-radical production in physiological reactions-a novel function of peroxidase
    • Chen, S. X., and P. Schopfer. 1999. Hydroxyl-radical production in physiological reactions-a novel function of peroxidase. Eur. J. Biochem. 260:726-735.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 726-735
    • Chen, S.X.1    Schopfer, P.2
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 6
    • 0029885361 scopus 로고    scopus 로고
    • In vitro insertion and assembly of outer membrane protein PhoE of Escherichia coli K-12 into the outer membrane-role of Triton X-100
    • de Cock, H., S. van Blokland, and J. Tommassen. 1996. In vitro insertion and assembly of outer membrane protein PhoE of Escherichia coli K-12 into the outer membrane-role of Triton X-100. J. Biol. Chem. 271:12885-12890.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12885-12890
    • De Cock, H.1    Van Blokland, S.2    Tommassen, J.3
  • 7
    • 0001256839 scopus 로고    scopus 로고
    • Structure, functions and applications of lactoperoxidase in natural antimicrobial systems
    • de Wit, J. N., and A. C. M. van Hooydonk. 1996. Structure, functions and applications of lactoperoxidase in natural antimicrobial systems. Neth. Milk Dairy J. 50:227-244.
    • (1996) Neth. Milk Dairy J. , vol.50 , pp. 227-244
    • Wit, J.N.1    Van Hooydonk, A.C.M.2
  • 8
    • 0002716288 scopus 로고
    • Lactoperoxidase and lactoferrin
    • V. M. Dillon and R. G. Board (ed.). CAB International, Wallingford, United Kingdom
    • Ekstrand, B. 1994. Lactoperoxidase and lactoferrin, p. 15-57. In V. M. Dillon and R. G. Board (ed.). Natural antimicrobial systems and food preservation. CAB International, Wallingford, United Kingdom.
    • (1994) Natural Antimicrobial Systems and Food Preservation , pp. 15-57
    • Ekstrand, B.1
  • 9
    • 0033774732 scopus 로고    scopus 로고
    • Inactivation of Escherichia coli and Listeria innocua in milk by combined treatment with high hydrostatic pressure and the lactoperoxidase system
    • Garcia-Graells, C., C. Valckx, and C. W. Michiels. 2000. Inactivation of Escherichia coli and Listeria innocua in milk by combined treatment with high hydrostatic pressure and the lactoperoxidase system. Appl. Environ. Microbiol. 66:4173-4179.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 4173-4179
    • Garcia-Graells, C.1    Valckx, C.2    Michiels, C.W.3
  • 10
    • 0037465606 scopus 로고    scopus 로고
    • The lactoperoxidase system increases efficacy of high-pressure inactivation of foodborne bacteria
    • Garcia-Graells, C., I. Van Opstal, S. C. M. Vanmuysen, and C. W. Michiels. 2003. The lactoperoxidase system increases efficacy of high-pressure inactivation of foodborne bacteria. Int. J. Food Microbiol. 81:211-221.
    • (2003) Int. J. Food Microbiol. , vol.81 , pp. 211-221
    • Garcia-Graells, C.1    Van Opstal, I.2    Vanmuysen, S.C.M.3    Michiels, C.W.4
  • 11
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton, M. B., A. J. Kettle, and C. C. Winterbourn. 1998. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92:3007-3017.
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 12
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven, J., and R. Dernick. 1985. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6:103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 13
    • 0029398139 scopus 로고
    • Commercial utilization of minor milk components in the health and food industries
    • Horton, B. S. 1995. Commercial utilization of minor milk components in the health and food industries. J. Dairy Sci. 78:2584-2589.
    • (1995) J. Dairy Sci. , vol.78 , pp. 2584-2589
    • Horton, B.S.1
  • 14
    • 0037174983 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12-the effects of leucine-responsive regulatory protein
    • Hung, S. P., P. Baldi, and G. W. Hatfield. 2002. Global gene expression profiling in Escherichia coli K12-the effects of leucine-responsive regulatory protein. J. Biol. Chem. 277:40309-40323.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40309-40323
    • Hung, S.P.1    Baldi, P.2    Hatfield, G.W.3
  • 15
    • 0025841773 scopus 로고
    • Uses of transposons with emphasis on Tn10
    • Kleckner, N., J. Bender, and S. Gottesman. 1991. Uses of transposons with emphasis on Tn10. Methods Enzymol. 204:139-180.
    • (1991) Methods Enzymol. , vol.204 , pp. 139-180
    • Kleckner, N.1    Bender, J.2    Gottesman, S.3
  • 16
    • 0015969864 scopus 로고
    • Alterations in outer membrane of cell-envelope of heptose-deficient mutants of Escherichia coli
    • Koplow, J., and H. Goldfine. 1974. Alterations in outer membrane of cell-envelope of heptose-deficient mutants of Escherichia coli. J. Bacteriol. 117:527-543.
    • (1974) J. Bacteriol. , vol.117 , pp. 527-543
    • Koplow, J.1    Goldfine, H.2
  • 17
    • 0034492989 scopus 로고    scopus 로고
    • Lactoperoxidase: Physico-chemical properties, occurrence, mechanism of action and applications
    • Kussendrager, K. D., and A. C. M. van Hooijdonk. 2000. Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 84:S19-S25.
    • (2000) Br. J. Nutr. , vol.84
    • Kussendrager, K.D.1    Van Hooijdonk, A.C.M.2
  • 18
    • 0028297759 scopus 로고
    • Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12
    • Laird, M. W., A. W. Kloser, and R. Misra. 1994. Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12. J. Bacteriol. 176:2259-2264.
    • (1994) J. Bacteriol. , vol.176 , pp. 2259-2264
    • Laird, M.W.1    Kloser, A.W.2    Misra, R.3
  • 19
    • 0031859738 scopus 로고    scopus 로고
    • Regulation of porin-mediated outer membrane permeability by nutrient limitation in Escherichia coli
    • Liu, X., and T. Ferenci. 1998. Regulation of porin-mediated outer membrane permeability by nutrient limitation in Escherichia coli. J. Bacteriol. 180:3917-3922.
    • (1998) J. Bacteriol. , vol.180 , pp. 3917-3922
    • Liu, X.1    Ferenci, T.2
  • 21
    • 85022982944 scopus 로고
    • In vivo kinetic-studies of clustered enzymes using overexpression of alkaline-phosphatase in Escherichia coli
    • Martinez, M. B., F. J. Schendel, M. C. Flickinger, and G. L. Nelsestuen. 1992. In vivo kinetic-studies of clustered enzymes using overexpression of alkaline-phosphatase in Escherichia coli. FASEB J. 6:A460.
    • (1992) FASEB J. , vol.6
    • Martinez, M.B.1    Schendel, F.J.2    Flickinger, M.C.3    Nelsestuen, G.L.4
  • 22
    • 0030031594 scopus 로고    scopus 로고
    • Accurate kinetic modeling of alkaline phosphatase in the Escherichia coli periplasm: Implications for enzyme properties and substrate diffusion
    • Martinez, M. B., M. C. Flickinger, and G. L. Nelsestuen. 1996. Accurate kinetic modeling of alkaline phosphatase in the Escherichia coli periplasm: implications for enzyme properties and substrate diffusion. Biochemistry 35:1179-1186.
    • (1996) Biochemistry , vol.35 , pp. 1179-1186
    • Martinez, M.B.1    Flickinger, M.C.2    Nelsestuen, G.L.3
  • 23
    • 0032819028 scopus 로고    scopus 로고
    • Steady-state enzyme kinetics in the Escherichia coli periplasm: A model of a whole cell biocatalyst
    • Martinez, M. B., M. C. Flickinger, and G. L. Nelsestuen. 1999. Steady-state enzyme kinetics in the Escherichia coli periplasm: a model of a whole cell biocatalyst. J. Biotechnol. 71:59-66.
    • (1999) J. Biotechnol. , vol.71 , pp. 59-66
    • Martinez, M.B.1    Flickinger, M.C.2    Nelsestuen, G.L.3
  • 24
    • 0035834043 scopus 로고    scopus 로고
    • Reduced outer membrane permeability of Escherichia coli O157:H7: Suggested role of modified outer membrane porins and theoretical function in resistance to antimicrobial agents
    • Martinez, M. B., M. Flickinger, L. Higgins, T. Krick, and G. L. Nelsestuen. 2001. Reduced outer membrane permeability of Escherichia coli O157:H7: suggested role of modified outer membrane porins and theoretical function in resistance to antimicrobial agents. Biochemistry 40:11965-11974.
    • (2001) Biochemistry , vol.40 , pp. 11965-11974
    • Martinez, M.B.1    Flickinger, M.2    Higgins, L.3    Krick, T.4    Nelsestuen, G.L.5
  • 25
    • 0027787823 scopus 로고
    • The activity of sigma(E), an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • Mecsas, J., P. E. Rouviere, J. W. Erickson, T. J. Donohue, and C. A. Gross. 1993. The activity of sigma(E), an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes Dev. 7:2618-2628.
    • (1993) Genes Dev. , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouviere, P.E.2    Erickson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 27
    • 0036119176 scopus 로고    scopus 로고
    • Mechanisms contributing to hypochlorous acid resistance of a Salmonella isolate from a poultry-processing plant
    • Mokgatla, R. M., P. A. Gouws, and V. S. Brozel. 2002. Mechanisms contributing to hypochlorous acid resistance of a Salmonella isolate from a poultry-processing plant. J. Appl. Microbiol. 92:566-573.
    • (2002) J. Appl. Microbiol. , vol.92 , pp. 566-573
    • Mokgatla, R.M.1    Gouws, P.A.2    Brozel, V.S.3
  • 28
    • 0344837300 scopus 로고    scopus 로고
    • An Escherichia coli MG1655 lipopolysaccharide deep-rough core mutant grows and survives in mouse cecal mucus but fails to colonize the mouse large intestine
    • Moller, A. K., M. P. Leatham, T. Conway, P. J. M. Nuijten, L. A. M. de Haan, K. A. Krogfelt, and P. S. Cohen. 2003. An Escherichia coli MG1655 lipopolysaccharide deep-rough core mutant grows and survives in mouse cecal mucus but fails to colonize the mouse large intestine. Infect. Immun. 71:2142-2152.
    • (2003) Infect. Immun. , vol.71 , pp. 2142-2152
    • Moller, A.K.1    Leatham, M.P.2    Conway, T.3    Nuijten, P.J.M.4    De Haan, L.A.M.5    Krogfelt, K.A.6    Cohen, P.S.7
  • 29
    • 0031924072 scopus 로고    scopus 로고
    • Use of bacteriophage λ recombination functions to promote gene replacement in Escherichia coli
    • Murphy, K. C. 1998. Use of bacteriophage λ recombination functions to promote gene replacement in Escherichia coli. J. Bacteriol. 180:2063-2071.
    • (1998) J. Bacteriol. , vol.180 , pp. 2063-2071
    • Murphy, K.C.1
  • 30
    • 0037162486 scopus 로고    scopus 로고
    • Designed to penetrate: Time-resolved interaction of single antibiotic molecules with bacterial pores
    • Nestorovich, E. M., C. Danelon, M, Winterhalter, and S. M. Bezrukov. 2002. Designed to penetrate: time-resolved interaction of single antibiotic molecules with bacterial pores. Proc. Natl. Acad. Sci. USA 99:9789-9794.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9789-9794
    • Nestorovich, E.M.1    Danelon, C.2    Winterhalter, M.3    Bezrukov, S.M.4
  • 31
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 32
    • 0031886481 scopus 로고    scopus 로고
    • MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate
    • Park, J. T., D. Raychaudhuri, H. S. Li, S. Normark, and D. Mengin-Lecreulx. 1998. MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-gamma-D-glutamyl-meso- diaminopimelate. J. Bacteriol. 180:1215-1223.
    • (1998) J. Bacteriol. , vol.180 , pp. 1215-1223
    • Park, J.T.1    Raychaudhuri, D.2    Li, H.S.3    Normark, S.4    Mengin-Lecreulx, D.5
  • 33
    • 0026056527 scopus 로고
    • Effect of RfaH (SfrB) and temperature on expression of rfa genes of Escherichia coli K-12
    • Pradel, E., and C. A. Schnaitman. 1991. Effect of RfaH (SfrB) and temperature on expression of rfa genes of Escherichia coli K-12. J. Bacteriol. 173:6428-6431.
    • (1991) J. Bacteriol. , vol.173 , pp. 6428-6431
    • Pradel, E.1    Schnaitman, C.A.2
  • 35
    • 0000877556 scopus 로고
    • Lactoperoxidase antibacterial system-natural occurrence, biological functions and practical applications
    • Reiter, B., and G. Harnulv. 1984. Lactoperoxidase antibacterial system-natural occurrence, biological functions and practical applications. J. Food Prot. 47:724-732.
    • (1984) J. Food Prot. , vol.47 , pp. 724-732
    • Reiter, B.1    Harnulv, G.2
  • 36
    • 0017610169 scopus 로고
    • Effect of defined lipopolysaccharide core defects upon antibiotic resistances of Salmonella typhimurium
    • Roantree, R. J., T. T. Kuo, and D. G. Macphee. 1977. Effect of defined lipopolysaccharide core defects upon antibiotic resistances of Salmonella typhimurium. J. Gen. Microbiol. 103:223-234.
    • (1977) J. Gen. Microbiol. , vol.103 , pp. 223-234
    • Roantree, R.J.1    Kuo, T.T.2    Macphee, D.G.3
  • 38
    • 0016139595 scopus 로고
    • Permeability of lipopolysaccharide-deficient (rough) mutants of Salmonella typhimuriurn to antibiotics, lysozyme, and other agents
    • Sanderson, K. E., T. MacAlistor, J. W. Costerton, and K. J. Cheng. 1974. Permeability of lipopolysaccharide-deficient (rough) mutants of Salmonella typhimuriurn to antibiotics, lysozyme, and other agents. Can. J. Microbiol. 20:1135-1145.
    • (1974) Can. J. Microbiol. , vol.20 , pp. 1135-1145
    • Sanderson, K.E.1    MacAlistor, T.2    Costerton, J.W.3    Cheng, K.J.4
  • 39
    • 2642554139 scopus 로고    scopus 로고
    • Quality aspects of Gouda cheese made from goat milk preserved by the lactoperoxidase system
    • Seifu, E., E. M. Buys, and E. F. Donkin. 2004. Quality aspects of Gouda cheese made from goat milk preserved by the lactoperoxidase system. Int. Dairy J. 14:581-589.
    • (2004) Int. Dairy J. , vol.14 , pp. 581-589
    • Seifu, E.1    Buys, E.M.2    Donkin, E.F.3
  • 41
    • 0035072117 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli respiratory enzymes by the lactoperoxidase-hydrogen peroxide-thiocyanate antimicrobial system
    • Shin, K., H. Hayasawa, and B. Lonnerdal. 2001. Inhibition of Escherichia coli respiratory enzymes by the lactoperoxidase-hydrogen peroxide-thiocyanate antimicrobial system. J. Appl. Microbiol. 90:489-493.
    • (2001) J. Appl. Microbiol. , vol.90 , pp. 489-493
    • Shin, K.1    Hayasawa, H.2    Lonnerdal, B.3
  • 43
    • 0036120646 scopus 로고    scopus 로고
    • Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: Efficacy and safety
    • Tenovuo, J. 2002. Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety. Oral Dis. 8:23-29.
    • (2002) Oral Dis. , vol.8 , pp. 23-29
    • Tenovuo, J.1
  • 44
    • 1842740107 scopus 로고    scopus 로고
    • Resistance to imipenem, cefepime, and cefpirome associated with mutation in Omp36 osmoporin of Enterobacter aerogenes
    • Thiolas, A., C. Bornet, A. vin-Regli, J. M. Pages, and C. Bollet. 2004. Resistance to imipenem, cefepime, and cefpirome associated with mutation in Omp36 osmoporin of Enterobacter aerogenes. Biochem. Biophys. Res. Commun. 317:851-856.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 851-856
    • Thiolas, A.1    Bornet, C.2    Vin-Regli, A.3    Pages, J.M.4    Bollet, C.5
  • 45
    • 0016709298 scopus 로고
    • Isolation of outer membrane proteins of Escherichia coli and their characterization on polyacrylamide-gel
    • Uemura, J., and S. Mizushima. 1975. Isolation of outer membrane proteins of Escherichia coli and their characterization on polyacrylamide-gel. Biochim. Biophys. Acta 413:163-176.
    • (1975) Biochim. Biophys. Acta , vol.413 , pp. 163-176
    • Uemura, J.1    Mizushima, S.2
  • 46
    • 0034490329 scopus 로고    scopus 로고
    • In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defense
    • van Hooijdonk, A. C. M., K. D. Kussendrager, and J. M. Steijns. 2000. In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defense. Br. J. Nutr. 84:8127-8134.
    • (2000) Br. J. Nutr. , vol.84 , pp. 8127-8134
    • Van Hooijdonk, A.C.M.1    Kussendrager, K.D.2    Steijns, J.M.3
  • 47
    • 0037229793 scopus 로고    scopus 로고
    • Regulation of membrane permeability by a two-component regulatory system in Pseudomonas aeruginosa
    • Wang, Y. P., U. Ha, L. Zeng, and S. G. Jin. 2003. Regulation of membrane permeability by a two-component regulatory system in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 47:95-101.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 95-101
    • Wang, Y.P.1    Ha, U.2    Zeng, L.3    Jin, S.G.4
  • 48
    • 0028137389 scopus 로고
    • Antibacterial activity of the lactoperoxidase system against Salmonella typhimurium in Trypticase soy broth in the presence and absence of a heat-treatment
    • Wolfson, L. M., and S. S. Sumner. 1994. Antibacterial activity of the lactoperoxidase system against Salmonella typhimurium in Trypticase soy broth in the presence and absence of a heat-treatment. J. Food Prot. 57:365-368.
    • (1994) J. Food Prot. , vol.57 , pp. 365-368
    • Wolfson, L.M.1    Sumner, S.S.2
  • 49
    • 0032500578 scopus 로고    scopus 로고
    • Involvement of waaY, waaQ, and waaP in the modification of Escherichia coli lipopolysaccharide and their role in the formation of a stable outer membrane
    • Yethon, J. A., D. E. Heinrichs, M. A. Monteiro, M. B. Perry, and C. Whitfield. 1998. Involvement of waaY, waaQ, and waaP in the modification of Escherichia coli lipopolysaccharide and their role in the formation of a stable outer membrane. J. Biol. Chem. 273:26310-26316.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26310-26316
    • Yethon, J.A.1    Heinrichs, D.E.2    Monteiro, M.A.3    Perry, M.B.4    Whitfield, C.5
  • 50
    • 0036136174 scopus 로고    scopus 로고
    • Utilization of L-ascorbate by Escherichia coli K-12: Assignments of functions to products of the yjf-sga and yia-sgb operons
    • Yew, W. S., and J. A. Gerlt. 2002. Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J. Bacteriol. 184:302-306.
    • (2002) J. Bacteriol. , vol.184 , pp. 302-306
    • Yew, W.S.1    Gerlt, J.A.2
  • 53
    • 0017662421 scopus 로고
    • Function of outer membrane of Escherichia coli as a permeability barrier to beta-lactam antibiotics
    • Zimmermann, W., and A. Rosselet. 1977. Function of outer membrane of Escherichia coli as a permeability barrier to beta-lactam antibiotics. Antimicrob. Agents Chemother. 12:368-372.
    • (1977) Antimicrob. Agents Chemother. , vol.12 , pp. 368-372
    • Zimmermann, W.1    Rosselet, A.2
  • 54
    • 0033912882 scopus 로고    scopus 로고
    • Prolonged stationary-phase incubation selects for lrp mutations in Escherichia coli K-12
    • Zinser, E. R., and R. Kolter. 2000. Prolonged stationary-phase incubation selects for lrp mutations in Escherichia coli K-12. J. Bacteriol. 182:4361-4365.
    • (2000) J. Bacteriol. , vol.182 , pp. 4361-4365
    • Zinser, E.R.1    Kolter, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.