메뉴 건너뛰기




Volumn 153, Issue 7, 2007, Pages 2093-2103

The β-lactam-resistance modifier (-)-epicatechin gallate alters the architecture of the cell wall of Staphylococcus aureas

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAM ANTIBIOTIC; EPICATECHIN GALLATE; EPIGALLOCATECHIN GALLATE; LIPOTEICHOIC ACID; LYSOSTAPHIN; OXACILLIN; PENICILLIN BINDING PROTEIN 2A; PEPTIDOGLYCAN; TEICHOIC ACID; TRITON X 100;

EID: 34447514359     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.2007/007807-0     Document Type: Article
Times cited : (101)

References (44)
  • 1
    • 33645749939 scopus 로고    scopus 로고
    • The emergence of vancomycin-interinediate and vancomycin-resistant Staphylococcus aureus
    • Suppl. 1, 16-23
    • Appelbaum, P. C. (2006). The emergence of vancomycin-interinediate and vancomycin-resistant Staphylococcus aureus. Clin Microbiol Infect 12 (Suppl. 1), 16-23.
    • (2006) Clin Microbiol Infect , vol.12
    • Appelbaum, P.C.1
  • 2
    • 13444282403 scopus 로고    scopus 로고
    • Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus
    • Bera, A., Herbert, S., Jakob, A., Vollmer, W. & Götz, F. (2005). Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol Microbiol 55, 778-787.
    • (2005) Mol Microbiol , vol.55 , pp. 778-787
    • Bera, A.1    Herbert, S.2    Jakob, A.3    Vollmer, W.4    Götz, F.5
  • 4
    • 0035178825 scopus 로고    scopus 로고
    • Development of vancomycin and lysostaphin resistance in a methicillin-resistant Staphylococcus aureus isolate
    • Boyle-Vavra, S., Carey, R. B. & Daum, R. S. (2001). Development of vancomycin and lysostaphin resistance in a methicillin-resistant Staphylococcus aureus isolate. J Antimicrob Chemother 48, 617-625.
    • (2001) J Antimicrob Chemother , vol.48 , pp. 617-625
    • Boyle-Vavra, S.1    Carey, R.B.2    Daum, R.S.3
  • 5
    • 0037443719 scopus 로고    scopus 로고
    • The relationship between the antioxidant and the antibacterial proper-ties of galloylated catechins and the structure of phospholipid model membranes
    • Caturia, N., Vera-Samper, E., Villallain, J., Mateo, C. R. & Micol, V. (2003). The relationship between the antioxidant and the antibacterial proper-ties of galloylated catechins and the structure of phospholipid model membranes. Free Radic Biol Med 34, 648-662.
    • (2003) Free Radic Biol Med , vol.34 , pp. 648-662
    • Caturia, N.1    Vera-Samper, E.2    Villallain, J.3    Mateo, C.R.4    Micol, V.5
  • 6
    • 0037024849 scopus 로고    scopus 로고
    • Staphylococcus aureus resistant to vancomycin - United States, 2002
    • Centers for Disease Control
    • Centers for Disease Control (2002). Staphylococcus aureus resistant to vancomycin - United States, 2002. MMWR Morbid Mortal Wkly Rep 51, 565-567.
    • (2002) MMWR Morbid Mortal Wkly Rep , vol.51 , pp. 565-567
  • 7
    • 0035859931 scopus 로고    scopus 로고
    • The evolution of methicillin resistance in Staphylococcus aureus: Similarity of genetic backgrounds in historically early methicillin-susceptible and -resistant isolates and contemporary epidemic clones
    • Crisóstomo, M. I., Westh, H., Tomasz, A., Chung, M., Oliveira, D. C. & de Lencastre, H. (2001). The evolution of methicillin resistance in Staphylococcus aureus: Similarity of genetic backgrounds in historically early methicillin-susceptible and -resistant isolates and contemporary epidemic clones. Proc Natl Acad Sci U S A 98, 9865-9870.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9865-9870
    • Crisóstomo, M.I.1    Westh, H.2    Tomasz, A.3    Chung, M.4    Oliveira, D.C.5    de Lencastre, H.6
  • 8
    • 0027394738 scopus 로고
    • Abnormal peptidoglycan produced in a methicillin-resistant strain of Staphylococcus aureus grown in the presence of methicillin: Functional role for penicillin-binding protein 2A in cell wall synthesis
    • de Jonge, B. L. M. & Tomasz, A. (1993). Abnormal peptidoglycan produced in a methicillin-resistant strain of Staphylococcus aureus grown in the presence of methicillin: Functional role for penicillin-binding protein 2A in cell wall synthesis. Antimicrob Agents Chemother 37, 342-346.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 342-346
    • de Jonge, B.L.M.1    Tomasz, A.2
  • 9
    • 0026088721 scopus 로고
    • Suppression of autolysis and cell wall turnover in heterogeneous Tn551 mutants of a methicillin-resistant Staphylococcus aureus strain
    • de Jonge, B. L. M., de Lancastre, H. & Tomasz, T. (1991). Suppression of autolysis and cell wall turnover in heterogeneous Tn551 mutants of a methicillin-resistant Staphylococcus aureus strain. J Bacteriol 173, 1105-1110.
    • (1991) J Bacteriol , vol.173 , pp. 1105-1110
    • de Jonge, B.L.M.1    de Lancastre, H.2    Tomasz, T.3
  • 10
    • 0034769882 scopus 로고    scopus 로고
    • Role of penicillin-binding protein 4 in expression of vancomycin resistance among clinical isolates of oxacillin-resistant Staphylococcus aureus
    • Finan, J. E., Archer, G. L., Pucci, M. J. & Climo, M. W. (2001). Role of penicillin-binding protein 4 in expression of vancomycin resistance among clinical isolates of oxacillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother 45, 3070-3075.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 3070-3075
    • Finan, J.E.1    Archer, G.L.2    Pucci, M.J.3    Climo, M.W.4
  • 11
    • 0033918491 scopus 로고    scopus 로고
    • A new two-component regulatory system involved in adhesion, autolysis, and extracellular proteolytic activity of Staphylococcus aureus
    • Fournier, B. & Hooper, D. C. (2000). A new two-component regulatory system involved in adhesion, autolysis, and extracellular proteolytic activity of Staphylococcus aureus. J Bacteriol 182, 3955-3964.
    • (2000) J Bacteriol , vol.182 , pp. 3955-3964
    • Fournier, B.1    Hooper, D.C.2
  • 12
    • 0032989614 scopus 로고    scopus 로고
    • Disorganization of cell division of methicillin-resistant Staphylococcus aureus by a component of tea (Camellia sinensis): A study by electron microscopy
    • Hamilton-Miller, J. M. T. & Shah, S. (1999). Disorganization of cell division of methicillin-resistant Staphylococcus aureus by a component of tea (Camellia sinensis): A study by electron microscopy. FEMS Microbiol Lett 176, 463-469.
    • (1999) FEMS Microbiol Lett , vol.176 , pp. 463-469
    • Hamilton-Miller, J.M.T.1    Shah, S.2
  • 13
    • 0021361020 scopus 로고
    • Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus
    • Hartman, B. J. & Tomasz, A. (1984). Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus. J Bacteriol 158, 513-516.
    • (1984) J Bacteriol , vol.158 , pp. 513-516
    • Hartman, B.J.1    Tomasz, A.2
  • 14
    • 0033250139 scopus 로고    scopus 로고
    • Interaction of tea catechins with lipid bilayers investigated with liposome systems
    • Hashimoto, T., Kumazawa, S., Nanjo, F., Hara, Y. & Nakayama, T. (1999). Interaction of tea catechins with lipid bilayers investigated with liposome systems. Biosci Biotechnol Biochem 63, 2252-2255.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 2252-2255
    • Hashimoto, T.1    Kumazawa, S.2    Nanjo, F.3    Hara, Y.4    Nakayama, T.5
  • 15
    • 0030841073 scopus 로고    scopus 로고
    • Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility
    • Hiramatsu, K., Hanaki, H., Ino, T., Yabuta, K., Oguri, T. & Tenover, F. C. (1997). Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility. J Antimicrob Chemother 40, 135-136.
    • (1997) J Antimicrob Chemother , vol.40 , pp. 135-136
    • Hiramatsu, K.1    Hanaki, H.2    Ino, T.3    Yabuta, K.4    Oguri, T.5    Tenover, F.C.6
  • 16
    • 0035752067 scopus 로고    scopus 로고
    • Steric effects on interaction of tea catechins with lipid bilayers
    • Kajiya, K., Kumazawa, S. & Nakayama, T. (2001). Steric effects on interaction of tea catechins with lipid bilayers. Biosci Biotechnol Biochem 65, 2638-2643.
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 2638-2643
    • Kajiya, K.1    Kumazawa, S.2    Nakayama, T.3
  • 17
    • 1842831532 scopus 로고    scopus 로고
    • Effects of external factors on the interaction of tea catechins with lipid bilayers
    • Kajiya, K., Kumazawa, S. & Nakayama, T. (2002). Effects of external factors on the interaction of tea catechins with lipid bilayers. Biosci Biotechnol Biochem 66, 2330-2335.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2330-2335
    • Kajiya, K.1    Kumazawa, S.2    Nakayama, T.3
  • 18
    • 4644344349 scopus 로고    scopus 로고
    • Cell wall composition and decreased autolytic activity and lysostaphin susceptibility of glycopeptide-intermediate Staphylococcus aureus
    • Koehl, J. L., Muthaiyan, A., Jayaswal, R. K., Ehlert, K., Labischinski, H. & Wilkinson, B. (2004). Cell wall composition and decreased autolytic activity and lysostaphin susceptibility of glycopeptide-intermediate Staphylococcus aureus. Antimicrob Agents Chemother 48, 3749-3757.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3749-3757
    • Koehl, J.L.1    Muthaiyan, A.2    Jayaswal, R.K.3    Ehlert, K.4    Labischinski, H.5    Wilkinson, B.6
  • 19
    • 77956988838 scopus 로고
    • Characterization of phosphorus compound by acid lability
    • Leloir, L. F. & Cardini, C. E. (1957). Characterization of phosphorus compound by acid lability. Methods Enzymol 3, 840-850.
    • (1957) Methods Enzymol , vol.3 , pp. 840-850
    • Leloir, L.F.1    Cardini, C.E.2
  • 20
    • 14244254169 scopus 로고    scopus 로고
    • Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: Evidence for the cooperative functioning of PBP2, PBP4 and PBP2A
    • Łeski, A. & Tomasz A. (2005). Role of penicillin-binding protein 2 (PBP2) in the antibiotic susceptibility and cell wall cross-linking of Staphylococcus aureus: Evidence for the cooperative functioning of PBP2, PBP4 and PBP2A. J Bacteriol 187, 1815-1824.
    • (2005) J Bacteriol , vol.187 , pp. 1815-1824
    • Łeski, A.1    Tomasz, A.2
  • 21
    • 0035491150 scopus 로고    scopus 로고
    • Beta-lactamase-inhibitor combinations in the 21st century: Current agents and new developments
    • Miller, L. A., Ratnam, K & Payne, D. J. (2001). Beta-lactamase-inhibitor combinations in the 21st century: Current agents and new developments. Curr Opin Pharmacol 1, 451-458.
    • (2001) Curr Opin Pharmacol , vol.1 , pp. 451-458
    • Miller, L.A.1    Ratnam, K.2    Payne, D.J.3
  • 22
    • 0033989880 scopus 로고    scopus 로고
    • Triton X-100-induced lipoteichoic acid release is correlated with the methicillin resistance in Staphylococcus aureus
    • Ohta, K, Komatsuzawa, H., Sugai, M. & Suginaka, H. (2000). Triton X-100-induced lipoteichoic acid release is correlated with the methicillin resistance in Staphylococcus aureus. FEMS Microbiol Lett 182, 77-79.
    • (2000) FEMS Microbiol Lett , vol.182 , pp. 77-79
    • Ohta, K.1    Komatsuzawa, H.2    Sugai, M.3    Suginaka, H.4
  • 23
    • 0033806585 scopus 로고    scopus 로고
    • The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolytic enzymes
    • Paschal, A., Vuong, C., Otto, M. & Götz, F. (2000). The D-alanine residues of Staphylococcus aureus teichoic acids alter the susceptibility to vancomycin and the activity of autolytic enzymes. Antimicrob Agents Chemother 44, 2845-2847.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 2845-2847
    • Paschal, A.1    Vuong, C.2    Otto, M.3    Götz, F.4
  • 24
    • 0033959682 scopus 로고    scopus 로고
    • Cloning, characterization, and inactivation of the gene pbpC, encoding penicillin-binding protein 3 of Staphylococcus aureus
    • Pinho, M. G., de Lencastre, H. & Tomasz, A. (2000). Cloning, characterization, and inactivation of the gene pbpC, encoding penicillin-binding protein 3 of Staphylococcus aureus. J Bacteriol 182, 1074-1079.
    • (2000) J Bacteriol , vol.182 , pp. 1074-1079
    • Pinho, M.G.1    de Lencastre, H.2    Tomasz, A.3
  • 25
    • 0022412324 scopus 로고
    • Use of resistant mutants to study the interaction of Triton X-100 with Staphylococcus aureus
    • Raychaudhuri, D. & Chatterjee, A. N. (1985). Use of resistant mutants to study the interaction of Triton X-100 with Staphylococcus aureus. J Bacteriol 164, 1337-1349.
    • (1985) J Bacteriol , vol.164 , pp. 1337-1349
    • Raychaudhuri, D.1    Chatterjee, A.N.2
  • 27
    • 0032512678 scopus 로고    scopus 로고
    • Improved high-performance liquid chromatographic separation of peptidoglycan isolated from various Staphylococcus aureus strains for mass spectrometric characterization
    • Roos, M., Pittenauer, E., Schmid, E., Beyer, M., Reinike, B., Allmaier, G. & Labischinski, H. (1998). Improved high-performance liquid chromatographic separation of peptidoglycan isolated from various Staphylococcus aureus strains for mass spectrometric characterization. J Chromatogr B Biomed Sci Appl 705, 183-192.
    • (1998) J Chromatogr B Biomed Sci Appl , vol.705 , pp. 183-192
    • Roos, M.1    Pittenauer, E.2    Schmid, E.3    Beyer, M.4    Reinike, B.5    Allmaier, G.6    Labischinski, H.7
  • 28
    • 0033387218 scopus 로고    scopus 로고
    • Marked reduction in the minimum inhibitory concentration (MIC) of beta-lactams in methicillin-resistant Staphylococcus aureus produced by epicatechin gallate, an ingredient of green tea (Camellia sinensis)
    • Shiota, S., Shimizu, M., Mizushima, T., Ito, H., Hatano, T., Yoshida, T. & Tsuchiya, T. (1999). Marked reduction in the minimum inhibitory concentration (MIC) of beta-lactams in methicillin-resistant Staphylococcus aureus produced by epicatechin gallate, an ingredient of green tea (Camellia sinensis). Biol Pharm Bull 22, 1388-1390.
    • (1999) Biol Pharm Bull , vol.22 , pp. 1388-1390
    • Shiota, S.1    Shimizu, M.2    Mizushima, T.3    Ito, H.4    Hatano, T.5    Yoshida, T.6    Tsuchiya, T.7
  • 29
    • 0031959963 scopus 로고    scopus 로고
    • A triazine dye, cibacron blue F3GA, decreases oxacillin resistance levels in methicillin-resistant Staphylococcus aureus
    • Shirai, C., Sugal, M., Komatsuzawa, H., Ohta, K., Yamakido, M. & Suginaka, H. (1998). A triazine dye, cibacron blue F3GA, decreases oxacillin resistance levels in methicillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother 42, 1278-1280.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 1278-1280
    • Shirai, C.1    Sugal, M.2    Komatsuzawa, H.3    Ohta, K.4    Yamakido, M.5    Suginaka, H.6
  • 30
    • 0030246884 scopus 로고    scopus 로고
    • A highly vancomycin-resistant laboratory mutant of Staphylococcus aureus
    • Sieradzki, K & Tomasz, A. (1996). A highly vancomycin-resistant laboratory mutant of Staphylococcus aureus. FEMS Microbiol Lett 142, 161-166.
    • (1996) FEMS Microbiol Lett , vol.142 , pp. 161-166
    • Sieradzki, K.1    Tomasz, A.2
  • 31
    • 0345097579 scopus 로고    scopus 로고
    • Alterations of cell wall structure and metabolism accompany reduced susceptibility to vancomycin in an isogenic series of clinical isolates of Staphylococcus aureus
    • Sieradzki, K. & Tomasz, A. (2003). Alterations of cell wall structure and metabolism accompany reduced susceptibility to vancomycin in an isogenic series of clinical isolates of Staphylococcus aureus. J Bacteriol 185, 7103-7110.
    • (2003) J Bacteriol , vol.185 , pp. 7103-7110
    • Sieradzki, K.1    Tomasz, A.2
  • 32
    • 0033516654 scopus 로고    scopus 로고
    • Inactivated pbp4 in highly glycopeptide-resistant laboratory mutants of Staphylococcus aureus
    • Sieradzki, K., Pinho, M. G. & Tomasz, A. (1999). Inactivated pbp4 in highly glycopeptide-resistant laboratory mutants of Staphylococcus aureus. J Biol Chem 274, 18942-18946.
    • (1999) J Biol Chem , vol.274 , pp. 18942-18946
    • Sieradzki, K.1    Pinho, M.G.2    Tomasz, A.3
  • 33
    • 0036359208 scopus 로고    scopus 로고
    • Methicillin resistance in Staphylococcus aureus: Mechanisms and modulation
    • Stapleton, P. D. & Taylor, P. W. (2002). Methicillin resistance in Staphylococcus aureus: Mechanisms and modulation. Sci Prog 85, 57-72.
    • (2002) Sci Prog , vol.85 , pp. 57-72
    • Stapleton, P.D.1    Taylor, P.W.2
  • 35
    • 31944435625 scopus 로고    scopus 로고
    • Potentiation of catechin gallate-mediated sensitization of Staphylococcus aureus to oxacillin by nongalloylated catechins
    • Stapleton, P. D., Shah, S., Here, Y. & Taylor, P. W. (2006). Potentiation of catechin gallate-mediated sensitization of Staphylococcus aureus to oxacillin by nongalloylated catechins. Antimicrob Agents Chemother 50, 752-755.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 752-755
    • Stapleton, P.D.1    Shah, S.2    Here, Y.3    Taylor, P.W.4
  • 36
    • 0031019864 scopus 로고    scopus 로고
    • Cell wall monoglycine cross-bridges and methicillin, hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus
    • Stranden, A. M., Ehlert, K, Labischinski, H. & Berger-Bächi, B. (1997). Cell wall monoglycine cross-bridges and methicillin, hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus. J Bacteriol 179, 9-16.
    • (1997) J Bacteriol , vol.179 , pp. 9-16
    • Stranden, A.M.1    Ehlert, K.2    Labischinski, H.3    Berger-Bächi, B.4
  • 37
    • 0025015465 scopus 로고
    • Characterization of sodium dodecyl sulfate-stable Staphylococcus aureus bacteriolytic enzymes by polyacrylamide gel electrophoresis
    • Sugai, M., Akiyama, T., Komatsuzawa, H., Miyake, Y. & Suginaka, H. (1990). Characterization of sodium dodecyl sulfate-stable Staphylococcus aureus bacteriolytic enzymes by polyacrylamide gel electrophoresis. J Bacteriol 172, 6494-6498.
    • (1990) J Bacteriol , vol.172 , pp. 6494-6498
    • Sugai, M.1    Akiyama, T.2    Komatsuzawa, H.3    Miyake, Y.4    Suginaka, H.5
  • 38
    • 0028986933 scopus 로고
    • Identification of endo-β-N-acetylglucosaminidase and N-acetylmuramyl-L -alanine amidase as duster-dispersing enzymes in Staphylococcus aureus
    • Sugai, M., Komatsuzawa, H., Akiyama, T., Hong, Y.-M., Oshida, T., Miyake, Y., Yamaguchi, T. & Suginaka, H. (1995). Identification of endo-β-N-acetylglucosaminidase and N-acetylmuramyl-L -alanine amidase as duster-dispersing enzymes in Staphylococcus aureus. J Bacteriol 177, 1491-1496.
    • (1995) J Bacteriol , vol.177 , pp. 1491-1496
    • Sugai, M.1    Komatsuzawa, H.2    Akiyama, T.3    Hong, Y.-M.4    Oshida, T.5    Miyake, Y.6    Yamaguchi, T.7    Suginaka, H.8
  • 39
    • 0030798089 scopus 로고    scopus 로고
    • Effects of various types of triton X on the susceptibilities of methicillin-resistant staphylococci to oxacillin
    • Suzuki, J., Komatsuzawa, H., Sugai, M., Ohta, K, Kozai, K., Nagasaka, N. & Suginaka, H. (1997). Effects of various types of triton X on the susceptibilities of methicillin-resistant staphylococci to oxacillin. FEMS Microbiol Lett 153, 327-331.
    • (1997) FEMS Microbiol Lett , vol.153 , pp. 327-331
    • Suzuki, J.1    Komatsuzawa, H.2    Sugai, M.3    Ohta, K.4    Kozai, K.5    Nagasaka, N.6    Suginaka, H.7
  • 41
    • 0031728726 scopus 로고    scopus 로고
    • Antibiotic-induced release of lipoteichoic acid and peptidoglycan from Staphylococcus aureus: Quantitative measurements and biological reactivities
    • van Langevelde, P., van Dissel, J. T., Ravensbergen, E, Applemelk, B. J., Schrijver, I. A. & Groeneveld, P. H. P. (1998). Antibiotic-induced release of lipoteichoic acid and peptidoglycan from Staphylococcus aureus: Quantitative measurements and biological reactivities. Antimicrob Agents Chemother 42, 3073-3078.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 3073-3078
    • van Langevelde, P.1    van Dissel, J.T.2    Ravensbergen, E.3    Applemelk, B.J.4    Schrijver, I.A.5    Groeneveld, P.H.P.6
  • 42
    • 27744482600 scopus 로고    scopus 로고
    • Reduced expression of the ad autolysin gene and susceptibility to autolysis in clinical heterogeneous glycopeptide-intermediate Staphylococcus aureus (hGISA) and GISA strains
    • Wootton, M., Bennett, P. M., MacGowan, A. P. & Walsh, T. R. (2005). Reduced expression of the ad autolysin gene and susceptibility to autolysis in clinical heterogeneous glycopeptide-intermediate Staphylococcus aureus (hGISA) and GISA strains. J Antimicrob Chemother 56, 944-947.
    • (2005) J Antimicrob Chemother , vol.56 , pp. 944-947
    • Wootton, M.1    Bennett, P.M.2    MacGowan, A.P.3    Walsh, T.R.4
  • 43
    • 0031872250 scopus 로고    scopus 로고
    • The effect of a component of tea (Camellia sinensis) on methicillin resistance, PBP2′ synthesis, and β-lactamase production in Staphylococcus aureus
    • Yam, T. S., Hamilton-Miller, J. M. T. & Shah, S. (1998). The effect of a component of tea (Camellia sinensis) on methicillin resistance, PBP2′ synthesis, and β-lactamase production in Staphylococcus aureus. J Antimicrob Chemother 42, 211-216.
    • (1998) J Antimicrob Chemother , vol.42 , pp. 211-216
    • Yam, T.S.1    Hamilton-Miller, J.M.T.2    Shah, S.3
  • 44
    • 0035018491 scopus 로고    scopus 로고
    • Mechanism of synergy between epigallocatechin gallate and beta-lactams against methicillin-resistant Staphylococcus aureus
    • Zhao, W.-H., Hu, Z.-Q, Okubo, S., Hara, Y. & Shimamura, T. (2001). Mechanism of synergy between epigallocatechin gallate and beta-lactams against methicillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother 45, 1737-1742.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1737-1742
    • Zhao, W.-H.1    Hu, Z.-Q.2    Okubo, S.3    Hara, Y.4    Shimamura, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.