메뉴 건너뛰기




Volumn 18, Issue 1, 2013, Pages 204-224

Anti-infectious agents against MRSA

Author keywords

Anti infectious agents; MRSA; Peptidoglycan; Teichoic acid; Virulence factors

Indexed keywords


EID: 84872865982     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules18010204     Document Type: Review
Times cited : (52)

References (51)
  • 1
    • 79952701515 scopus 로고    scopus 로고
    • Bacterial cell wall assembly: Still an attractive antibacterial target
    • Bugg, T.D.; Braddick, D.; Dowson, C.G.; Roper, D.I. Bacterial cell wall assembly: Still an attractive antibacterial target. Trends. Biotechnol. 2011, 29, 167-173.
    • (2011) Trends. Biotechnol. , vol.29 , pp. 167-173
    • Bugg, T.D.1    Braddick, D.2    Dowson, C.G.3    Roper, D.I.4
  • 2
    • 0031767816 scopus 로고    scopus 로고
    • Staphylococcal cell wall: Morphogenesis and fatal variations in the presence of penicillin
    • Giesbrecht, P.; Kersten, T.; Maidhof, H.; Wecke, J. Staphylococcal cell wall: Morphogenesis and fatal variations in the presence of penicillin. Microbiol. Mol. Biol. Rev. 2007, 62, 1371-1414.
    • (2007) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1371-1414
    • Giesbrecht, P.1    Kersten, T.2    Maidhof, H.3    Wecke, J.4
  • 3
    • 0022742030 scopus 로고
    • Penicillin-binding proteins and the antibacterial effectiveness of beta-lactam antibiotics
    • Tomasz, A. Penicillin-binding proteins and the antibacterial effectiveness of beta-lactam antibiotics. Rev. Infect. Dis. 1986, 8, S260-S278.
    • (1986) Rev. Infect. Dis. , vol.8
    • Tomasz, A.1
  • 4
    • 0016144780 scopus 로고
    • On the mechanism of action of vancomycin: Inhibition of peptidoglycan synthesis in gaffkya homari
    • Hammes, W.P.; Neuhaus, F.C. On the mechanism of action of vancomycin: Inhibition of peptidoglycan synthesis in Gaffkya homari. Antimicrob. Agents Chemother. 1974, 6, 722-728.
    • (1974) Antimicrob. Agents Chemother. , vol.6 , pp. 722-728
    • Hammes, W.P.1    Neuhaus, F.C.2
  • 5
    • 78049285348 scopus 로고    scopus 로고
    • Moenomycin family antibiotics: Chemical synthesis, biosynthesis, and biological activity
    • Ostash, B.; Walker, S. Moenomycin family antibiotics: Chemical synthesis, biosynthesis, and biological activity. Nat. Prod. Rep. 2010, 27, 1595-1617.
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 1595-1617
    • Ostash, B.1    Walker, S.2
  • 6
    • 0015168380 scopus 로고
    • Mechanism of action of bacitracin: Complexation with metal ion and c55-isoprenyl pyrophosphate
    • Stone, K.J.; Strominger, J.L. Mechanism of action of bacitracin: Complexation with metal ion and C55-isoprenyl pyrophosphate. Proc. Natl. Acad. Sci. USA 1971, 68, 3223-3227.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 3223-3227
    • Stone, K.J.1    Strominger, J.L.2
  • 7
    • 0028267688 scopus 로고
    • Multiple-Antibiotic resistant pathogenic bacteria
    • Tomasz, A. Multiple-Antibiotic resistant pathogenic bacteria. N. Engl. J. Med. 1994, 330, 1247-1251.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 1247-1251
    • Tomasz, A.1
  • 9
    • 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. Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility. J. Antimicrob. Chemother. 1997, 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
  • 10
    • 0031583382 scopus 로고    scopus 로고
    • Staphylococcus aureus with reduced susceptibility to vancomycin-united states, 1997
    • Centers for Disease Control and Prevention
    • Centers for Disease Control and Prevention. Staphylococcus aureus with reduced susceptibility to vancomycin-United States, 1997. MMWR Morb. Mortal. Wkly. Rep. 1997, 46, 765-766.
    • (1997) MMWR Morb. Mortal. Wkly. Rep. , vol.46 , pp. 765-766
  • 12
    • 0032584588 scopus 로고    scopus 로고
    • Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between e- and z-prenyl diphosphate synthases
    • Shimizu, N.; Koyama, T.; Ogura, K. Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases. J. Biol. Chem. 1998, 273, 19476-19481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19476-19481
    • Shimizu, N.1    Koyama, T.2    Ogura, K.3
  • 13
    • 3242701485 scopus 로고    scopus 로고
    • The effect of triton concentration on the activity of undecaprenyl pyrophosphate synthase inhibitors
    • Li, H.; Huang, J.; Jiang, X.; Seefeld, M.; McQueney, M.; Macarron, R. The effect of triton concentration on the activity of undecaprenyl pyrophosphate synthase inhibitors. J. Biomol. Screen. 2003, 8, 712-715.
    • (2003) J. Biomol. Screen. , vol.8 , pp. 712-715
    • Li, H.1    Huang, J.2    Jiang, X.3    Seefeld, M.4    McQueney, M.5    Macarron, R.6
  • 14
    • 40749124827 scopus 로고    scopus 로고
    • Design And Structure-Activity Relationships Of Potent And Selective Inhibitors Of Undecaprenyl Pyrophosphate Synthase (UPPS): Tetramic Tetronic Acids And Dihydropyridin-2-ones
    • Peukert, S.; Sun, Y.; Zhang, R.; Hurley, B.; Sabio, M.; Shen, X.; Gray, C.; Dzink-Fox, J.; Tao, J.; Cebula, R.; Wattanasin, S. Design and structure-Activity relationships of potent and selective inhibitors of undecaprenyl pyrophosphate synthase (UPPS): Tetramic, tetronic acids and dihydropyridin-2-ones. Bioorg. Med. Chem. Lett. 2008, 18, 1840-1844.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 1840-1844
    • Peukert, S.1    Sun, Y.2    Zhang, R.3    Hurley, B.4    Sabio, M.5    Shen, X.6    Gray, C.7    Dzink-Fox, J.8    Tao, J.9    Cebula, R.10    Wattanasin, S.11
  • 15
    • 42949132874 scopus 로고    scopus 로고
    • Structurebased inhibitors exhibit differential activities against helicobacter pylori and escherichia coli undecaprenyl pyrophosphate synthases
    • Kuo, C.J.; Guo, R.T.; Lu, I.L.; Liu, H.G.; Wu, S.Y.; Ko, T.P.; Wang, A.H.; Liang, P.H. Structurebased inhibitors exhibit differential activities against Helicobacter pylori and Escherichia coli undecaprenyl pyrophosphate synthases. J. Biomed. Biotechnol. 2008, 2008, 1-6.
    • (2008) J. Biomed. Biotechnol. , vol.2008 , pp. 1-6
    • Kuo, C.J.1    Guo, R.T.2    Lu, I.L.3    Liu, H.G.4    Wu, S.Y.5    Ko, T.P.6    Wang, A.H.7    Liang, P.H.8
  • 17
    • 84872839728 scopus 로고    scopus 로고
    • Spirohexalines New inhibitors of bacterial undecaprenyl pyrophosphate synthase, produced by penicillium brasilianum fki-3368
    • doi:10.1038/ja.2012.83
    • Inokoshi, J.; Nakamura, Y.; Hongbin, Z.; Uchida, R.; Nonaka, K.; Masuma, R.; Tomoda, H. Spirohexalines, New Inhibitors of Bacterial Undecaprenyl Pyrophosphate Synthase, produced by Penicillium brasilianum FKI-3368. J. Antibiot. 2012, doi:10.1038/ja.2012.83.
    • (2012) J. Antibiot.
    • Inokoshi, J.1    Nakamura, Y.2    Hongbin, Z.3    Uchida, R.4    Nonaka, K.5    Masuma, R.6    Tomoda, H.7
  • 18
    • 0035700551 scopus 로고    scopus 로고
    • Tripropeptins novel antimicrobial agents produced by lysobacter sp. I. Taxonomy, isolation and biological activities
    • Hashizume, H.; Igarashi, M.; Hattori, S.; Hori, M.; Hamada, M.; Takeuchi, T. Tripropeptins, novel antimicrobial agents produced by Lysobacter sp. I. Taxonomy, isolation and biological activities. J. Antibiot. 2001, 54, 1054-1059.
    • (2001) J. Antibiot. , vol.54 , pp. 1054-1059
    • Hashizume, H.1    Igarashi, M.2    Hattori, S.3    Hori, M.4    Hamada, M.5    Takeuchi, T.6
  • 20
    • 79960288307 scopus 로고    scopus 로고
    • Tripropeptin c blocks the lipid cycle of cell wall biosynthesis by complex formation with undecaprenyl pyrophosphate
    • Hashizume, H.; Sawa, R.; Harada, S.; Igarashi, M.; Adachi, H.; Nishimura, Y.; Nomoto, A. Tripropeptin C blocks the lipid cycle of cell wall biosynthesis by complex formation with undecaprenyl pyrophosphate. Antimicrob. Agents Chemother. 2011, 55, 3821-3828.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 3821-3828
    • Hashizume, H.1    Sawa, R.2    Harada, S.3    Igarashi, M.4    Adachi, H.5    Nishimura, Y.6    Nomoto, A.7
  • 21
    • 33846018033 scopus 로고    scopus 로고
    • Ramoplanin A topical lipoglycodepsipeptide antibacterial agent
    • Fulco, P.; Wenzel, R.P. Ramoplanin: A topical lipoglycodepsipeptide antibacterial agent. Expert. Rev. Anti Infect. Ther. 2006, 4, 939-945.
    • (2006) Expert. Rev. Anti Infect. Ther. , vol.4 , pp. 939-945
    • Fulco, P.1    Wenzel, R.P.2
  • 22
    • 14844340653 scopus 로고    scopus 로고
    • Chemistry and biology of ramoplanin: A lipoglycodepsipeptide with potent antibiotic activity
    • Walker, S.; Chen, L.; Hu, Y.; Rew, Y.; Shin, D.; Boger, D.L. Chemistry and biology of ramoplanin: A lipoglycodepsipeptide with potent antibiotic activity. Chem. Rev. 2005, 105, 449-476.
    • (2005) Chem. Rev. , vol.105 , pp. 449-476
    • Walker, S.1    Chen, L.2    Hu, Y.3    Rew, Y.4    Shin, D.5    Boger, D.L.6
  • 23
    • 0033856211 scopus 로고    scopus 로고
    • Friulimicins Novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from actinoplanes friuliensis sp. Nov. Ii. Isolation and structural characterization
    • Vértesy, L.; Ehlers, E.; Kogler, H.; Kurz, M.; Meiwes, J.; Seibert, G.; Vogel, M.; Hammann, P. Friulimicins: Novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from Actinoplanes friuliensis sp. nov. II. Isolation and structural characterization. J. Antibiot. 2000, 53, 816-827.
    • (2000) J. Antibiot. , vol.53 , pp. 816-827
    • Vértesy, L.1    Ehlers, E.2    Kogler, H.3    Kurz, M.4    Meiwes, J.5    Seibert, G.6    Vogel, M.7    Hammann, P.8
  • 24
    • 65749087124 scopus 로고    scopus 로고
    • The lipopeptide antibiotic friulimicin b inhibits cell wall biosynthesis through complex formation with bactoprenol phosphate
    • Schneider, T.; Gries, K.; Josten, M.; Wiedemann, I.; Pelzer, S.; Labischinski, H.; Sahl, H.G. The lipopeptide antibiotic Friulimicin B inhibits cell wall biosynthesis through complex formation with bactoprenol phosphate. Antimicrob. Agents Chemother. 2009, 53, 1610-1618.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1610-1618
    • Schneider, T.1    Gries, K.2    Josten, M.3    Wiedemann, I.4    Pelzer, S.5    Labischinski, H.6    Sahl, H.G.7
  • 26
    • 0032820601 scopus 로고    scopus 로고
    • Potentiation of methicillin activity against methicillinresistant staphylococcus aureus by diterpenes
    • Nicolson, K.; Evans, G.; O'Toole, P.W. Potentiation of methicillin activity against methicillinresistant Staphylococcus aureus by diterpenes. FEMS Microbiol. Lett. 1999, 179, 233-239.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 233-239
    • Nicolson, K.1    Evans, G.2    O'Toole, P.W.3
  • 27
    • 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. Mechanism of synergy between epigallocatechin gallate and beta-lactams against methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 2001, 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
  • 28
    • 0034780297 scopus 로고    scopus 로고
    • Marked potentiation of activity of beta-lactams against methicillin-resistant staphylococcus aureus by corilagin
    • Shimizu, M.; Shiota, S.; Mizushima, T.; Ito, H.; Hatano, T.; Yoshida, T.; Tsuchiya, T. Marked potentiation of activity of beta-lactams against methicillin-resistant Staphylococcus aureus by corilagin. Antimicrob. Agents Chemother. 2001, 45, 3198-3201.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 3198-3201
    • Shimizu, M.1    Shiota, S.2    Mizushima, T.3    Ito, H.4    Hatano, T.5    Yoshida, T.6    Tsuchiya, T.7
  • 29
    • 0034656247 scopus 로고    scopus 로고
    • Restoration of effectiveness of beta-lactams on methicillin-resistant staphylococcus aureus by tellimagrandin i from rose red
    • Shiota, S.; Shimizu, M.; Mizushima, T.; Ito, H.; Hatano, T.; Yoshida, T.; Tsuchiya, T. Restoration of effectiveness of beta-lactams on methicillin-resistant Staphylococcus aureus by tellimagrandin I from rose red. FEMS Microbiol. Lett. 2000, 185, 135-138.
    • (2000) FEMS Microbiol. Lett. , vol.185 , pp. 135-138
    • Shiota, S.1    Shimizu, M.2    Mizushima, T.3    Ito, H.4    Hatano, T.5    Yoshida, T.6    Tsuchiya, T.7
  • 30
    • 29344449420 scopus 로고    scopus 로고
    • Stemphones novel potentiators of imipenem activity against methicillin-resistant staphylococcus aureus, produced by aspergillus sp. Fki-2136
    • Koyama, N.; Nagahiro, T.; Yamaguchi, Y.; Masuma, R.; Tomoda, H.; Omura, S. Stemphones, novel potentiators of imipenem activity against methicillin-resistant Staphylococcus aureus, produced by Aspergillus sp. FKI-2136. J. Antibiot. 2005, 58, 695-703.
    • (2005) J. Antibiot. , vol.58 , pp. 695-703
    • Koyama, N.1    Nagahiro, T.2    Yamaguchi, Y.3    Masuma, R.4    Tomoda, H.5    Omura, S.6
  • 31
    • 55449128704 scopus 로고    scopus 로고
    • Structure-Activity relationships of stemphones, potentiators of imipenem activity against methicillin-resistant staphylococcus aureus
    • Yamazaki, H.; Koyama, N.; Omura, S.; Tomoda, H. Structure-Activity relationships of stemphones, potentiators of imipenem activity against methicillin-resistant Staphylococcus aureus. J. Antibiot. 2008, 61, 426-441.
    • (2008) J. Antibiot. , vol.61 , pp. 426-441
    • Yamazaki, H.1    Koyama, N.2    Omura, S.3    Tomoda, H.4
  • 32
    • 44649111844 scopus 로고    scopus 로고
    • Cyslabdan a new potentiator of imipenem activity against methicillin-resistant staphylococcus aureus, produced by streptomyces sp. K04-0144. I. Taxonomy, fermentation, isolation and structural elucidation
    • Fukumoto, A.; Kim, Y.P.; Matsumoto, A.; Takahashi, Y.; Shiomi, K.; Tomoda, H.; Omura, S. Cyslabdan, a new potentiator of imipenem activity against methicillin-resistant Staphylococcus aureus, produced by Streptomyces sp. K04-0144. I. Taxonomy, fermentation, isolation and structural elucidation. J. Antibiot. 2008, 61, 1-6.
    • (2008) J. Antibiot. , vol.61 , pp. 1-6
    • Fukumoto, A.1    Kim, Y.P.2    Matsumoto, A.3    Takahashi, Y.4    Shiomi, K.5    Tomoda, H.6    Omura, S.7
  • 33
    • 44649122131 scopus 로고    scopus 로고
    • Cyslabdan a new potentiator of imipenem activity against methicillin-resistant staphylococcus aureus, produced by streptomyces sp. K04-0144. Ii. Biological activities
    • Fukumoto, A.; Kim, Y.P.; Hanaki, H.; Shiomi, K.; Tomoda, H.; Omura, S. Cyslabdan, a new potentiator of imipenem activity against methicillin-resistant Staphylococcus aureus, produced by Streptomyces sp. K04-0144. II. Biological activities. J. Antibiot. 2008, 61, 7-10.
    • (2008) J. Antibiot. , vol.61 , pp. 7-10
    • Fukumoto, A.1    Kim, Y.P.2    Hanaki, H.3    Shiomi, K.4    Tomoda, H.5    Omura, S.6
  • 34
    • 84872857682 scopus 로고    scopus 로고
    • New cyslabdans b and c, potentiators of imipenem activity against methicillin-resistant staphylococcus aureus produced by streptomyces sp. K04-0144
    • Koyama, N.; Tokura, Y.; Takahashi, Y.; Tomoda, H. New cyslabdans B and C, potentiators of imipenem activity against methicillin-resistant Staphylococcus aureus produced by Streptomyces sp. K04-0144. Acta. Pharm. Sin. B 2011, 1, 236-239.
    • (2011) Acta. Pharm. Sin. B , vol.1 , pp. 236-239
    • Koyama, N.1    Tokura, Y.2    Takahashi, Y.3    Tomoda, H.4
  • 35
    • 70249137994 scopus 로고    scopus 로고
    • Xanthoradones new potentiators of imipenem activity against methicillin-resistant staphylococcus aureus, produced by penicillium radicum fki-3765-2: I. Taxonomy, fermentation, isolation and biological properties
    • Yamazaki, H.; Nonaka, K.; Masuma, R.; Omura, S.; Tomoda, H. Xanthoradones, new potentiators of imipenem activity against methicillin-resistant Staphylococcus aureus, produced by Penicillium radicum FKI-3765-2: I. Taxonomy, fermentation, isolation and biological properties. J. Antibiot. 2009, 62, 431-434.
    • (2009) J. Antibiot. , vol.62 , pp. 431-434
    • Yamazaki, H.1    Nonaka, K.2    Masuma, R.3    Omura, S.4    Tomoda, H.5
  • 36
    • 70249105402 scopus 로고    scopus 로고
    • Xanthoradones new potentiators of imipenem activity against methicillin-resistant staphylococcus aureus, produced by penicillium radicum fki-3765-2 ii. Structure elucidation
    • Yamazaki, H.; Omura, S.; Tomoda, H. Xanthoradones, new potentiators of imipenem activity against methicillin-resistant Staphylococcus aureus, produced by Penicillium radicum FKI-3765-2 II. Structure elucidation. J. Antibiot. 2009, 62, 435-437.
    • (2009) J. Antibiot. , vol.62 , pp. 435-437
    • Yamazaki, H.1    Omura, S.2    Tomoda, H.3
  • 37
    • 69049091879 scopus 로고    scopus 로고
    • Chemical genetic identification of peptidoglycan inhibitors potentiating carbapenem activity against methicillin-resistant staphylococcus aureus
    • Huber, J.; Donald, R.G.; Lee, S.H.; Jarantow, L.W.; Salvatore, M.J.; Meng, X.; Painter, R.; Onishi, R.H.; Occi, J.; Dorso, K.; et al. Chemical genetic identification of peptidoglycan inhibitors potentiating carbapenem activity against methicillin-resistant Staphylococcus aureus. Chem. Biol. 2009, 16, 837-848.
    • (2009) Chem. Biol. , vol.16 , pp. 837-848
    • Huber, J.1    Donald, R.G.2    Lee, S.H.3    Jarantow, L.W.4    Salvatore, M.J.5    Meng, X.6    Painter, R.7    Onishi, R.H.8    Occi, J.9    Dorso, K.10
  • 38
    • 0942297805 scopus 로고    scopus 로고
    • Mechanisms of action of corilagin and tellimagrandin i that remarkably potentiate the activity of ß-lactams against methicillin-resistant staphylococcus aureus
    • Shiota, S.; Shimizu, M.; Sugiyama, J.; Morita, Y.; Mizushima, T.; Tsuchiya, T. Mechanisms of action of corilagin and tellimagrandin I that remarkably potentiate the activity of ß-lactams against methicillin-resistant Staphylococcus aureus. Microbiol. Immunol. 2004, 48, 67-73.
    • (2004) Microbiol. Immunol. , vol.48 , pp. 67-73
    • Shiota, S.1    Shimizu, M.2    Sugiyama, J.3    Morita, Y.4    Mizushima, T.5    Tsuchiya, T.6
  • 39
    • 84872844174 scopus 로고    scopus 로고
    • The nonantibiotic small molecule cyslabdan enhances the potency of ß-lactams against mrsa by inhibiting pentaglycine interpeptide bridge synthesis
    • Koyama, N.; Tokura, Y.; Münch, D.; Sahl, H.-G.; Schneider, T.; Shibagaki, Y.; Ikeda, H.; Tomoda, H. The nonantibiotic small molecule cyslabdan enhances the potency of ß-lactams against MRSA by inhibiting pentaglycine interpeptide bridge synthesis. PLoS One 2012, 7, e48981.
    • (2012) PLoS One , vol.7
    • Koyama, N.1    Tokura, Y.2    Münch, D.3    Sahl, H.-G.4    Schneider, T.5    Shibagaki, Y.6    Ikeda, H.7    Tomoda, H.8
  • 40
    • 0024460146 scopus 로고
    • Fema a host-mediated factor essential for methicillin resistance in staphylococcus aureus. Molecular cloning and characterization
    • Berger-Bächi, B.; Barberis-Maino, L.; Strässle, A.; Kayser, F.H. FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus. Molecular cloning and characterization. Mol. Gen. Genet. 1989, 219, 263-269.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 263-269
    • Berger-Bächi, B.1    Barberis-Maino, L.2    Strässle, A.3    Kayser, F.H.4
  • 41
    • 0025822537 scopus 로고
    • Fema, which encodes a factor essential for expression of methicillin resistance, affects glycine content of peptidoglycan in methicillin-resistant and methicillin-susceptible staphylococcus aureus strains
    • Maidhof, H.; Reinicke, B.; Blümel, P.; Berger-Bächi, B.; Labischinski, H. femA, which encodes a factor essential for expression of methicillin resistance, affects glycine content of peptidoglycan in methicillin-resistant and methicillin-susceptible Staphylococcus aureus strains. J. Bacteriol. 1991, 173, 3507-3513.
    • (1991) J. Bacteriol. , vol.173 , pp. 3507-3513
    • Maidhof, H.1    Reinicke, B.2    Blümel, P.3    Berger-Bächi, B.4    Labischinski, H.5
  • 42
    • 0031019864 scopus 로고    scopus 로고
    • Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femab null mutant of methicillin-resistant staphylococcus aureus
    • Strandén, A.M.; Ehlert, K.; Labischinski, H.; Berger-Bächi, B. Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus. J. Bacteriol. 1997, 179, 9-16.
    • (1997) J. Bacteriol. , vol.179 , pp. 9-16
    • Strandén, A.M.1    Ehlert, K.2    Labischinski, H.3    Berger-Bächi, B.4
  • 43
    • 78049405519 scopus 로고    scopus 로고
    • Staphylococcus aureus and bacillus subtilis w23 make polyribitol wall teichoic acids using different enzymatic pathways
    • Brown, S.; Meredith, T.; Swoboda, J.; Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 2010, 17, 1101-1110.
    • (2010) Chem. Biol. , vol.17 , pp. 1101-1110
    • Brown, S.1    Meredith, T.2    Swoboda, J.3    Walker, S.4
  • 44
    • 75649132267 scopus 로고    scopus 로고
    • Wall teichoic acid function biosynthesis, and inhibition
    • Swoboda, J.G.; Campbell, J.; Meredith, T.C.; Walker, S. Wall teichoic acid function, biosynthesis, and inhibition. Chembiochem 2010, 11, 35-45.
    • (2010) Chembiochem , vol.11 , pp. 35-45
    • Swoboda, J.G.1    Campbell, J.2    Meredith, T.C.3    Walker, S.4
  • 46
    • 79957525416 scopus 로고    scopus 로고
    • Abc transporters required for export of wall teichoic acids do not discriminate between different main chain polymers
    • Schirner, K.; Stone, L.K.; Walker, S. ABC transporters required for export of wall teichoic acids do not discriminate between different main chain polymers. ACS Chem. Biol. 2011, 6, 407-412.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 407-412
    • Schirner, K.1    Stone, L.K.2    Walker, S.3
  • 47
    • 76649129529 scopus 로고    scopus 로고
    • Development of improved inhibitors of wall teichoic acid biosynthesis with potent activity against staphylococcus aureus
    • Lee, K.; Campbell, J.; Swoboda, J.G.; Cuny, G.D.; Walker, S. Development of improved inhibitors of wall teichoic acid biosynthesis with potent activity against Staphylococcus aureus. Bioorg. Med. Chem. Lett. 2010, 20, 1767-1770.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 1767-1770
    • Lee, K.1    Campbell, J.2    Swoboda, J.G.3    Cuny, G.D.4    Walker, S.5
  • 48
  • 49
    • 22944462082 scopus 로고    scopus 로고
    • Staphylococcus aureus golden pigment impairs neutrophil killing and promotes virulence through its antioxidant activity
    • Liu, G.Y.; Essex, A.; Buchanan, J.T.; Datta, V.; Hoffman, H.M.; Bastian, J.F.; Fierer, J.; Nizet, V. Staphylococcus aureus golden pigment impairs neutrophil killing and promotes virulence through its antioxidant activity. J. Exp. Med. 2005, 202, 209-215.
    • (2005) J. Exp. Med. , vol.202 , pp. 209-215
    • Liu, G.Y.1    Essex, A.2    Buchanan, J.T.3    Datta, V.4    Hoffman, H.M.5    Bastian, J.F.6    Fierer, J.7    Nizet, V.8
  • 51
    • 84855666970 scopus 로고    scopus 로고
    • Search method for inhibitors of staphyloxanthin production by methicillin-resistant staphylococcus aureus
    • Sakai, K.; Koyama, N.; Fukuda, T.; Mori, Y.; Onaka, H.; Tomoda, H. Search method for inhibitors of Staphyloxanthin production by methicillin-resistant Staphylococcus aureus. Biol. Pharm. Bull. 2012, 35, 48-53.
    • (2012) Biol. Pharm. Bull. , vol.35 , pp. 48-53
    • Sakai, K.1    Koyama, N.2    Fukuda, T.3    Mori, Y.4    Onaka, H.5    Tomoda, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.