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Volumn 194, Issue 17, 2012, Pages 4494-4504

Daptomycin-mediated reorganization of membrane architecture causes mislocalization of essential cell division proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DAPTOMYCIN; DIVIVA PROTEIN; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

EID: 84865425113     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00011-12     Document Type: Article
Times cited : (251)

References (60)
  • 1
    • 0037115463 scopus 로고    scopus 로고
    • A cytoskeletonlike role for the bacterial cell wall during engulfment of the Bacillus subtilis forespore
    • Abanes-De Mello A, Sun YL, Aung S, Pogliano K. 2002. A cytoskeletonlike role for the bacterial cell wall during engulfment of the Bacillus subtilis forespore. Genes Dev. 16:3253-3264.
    • (2002) Genes Dev. , vol.16 , pp. 3253-3264
    • Mello, A-D.A.1    Sun, Y.L.2    Aung, S.3    Pogliano, K.4
  • 2
    • 80052576088 scopus 로고    scopus 로고
    • Genetic basis for in vivo daptomycin resistance in enterococci
    • Arias CA, et al. 2011. Genetic basis for in vivo daptomycin resistance in enterococci. N. Engl. J. Med. 365:892-900
    • (2011) N. Engl. J. Med. , vol.365 , pp. 892-900
    • Arias, C.A.1
  • 3
    • 65349126661 scopus 로고    scopus 로고
    • Daptomycin: mechanisms of action and resistance, and biosynthetic engineering
    • Baltz RH. 2009. Daptomycin: mechanisms of action and resistance, and biosynthetic engineering. Curr. Opin. Chem. Biol. 13:144-151.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 144-151
    • Baltz, R.H.1
  • 4
    • 71549130716 scopus 로고    scopus 로고
    • Division site selection in rod-shaped bacteria
    • Bramkamp M, van Baarle S. 2009. Division site selection in rod-shaped bacteria. Curr. Opin. Microbiol. 12:683-688.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 683-688
    • Bramkamp, M.1    Baarle, V.S.2
  • 5
    • 33748201611 scopus 로고    scopus 로고
    • Forespore engulfment mediated by a ratchet-like mechanism
    • Broder DH, Pogliano K. 2006. Forespore engulfment mediated by a ratchet-like mechanism. Cell 126:917-928.
    • (2006) Cell , vol.126 , pp. 917-928
    • Broder, D.H.1    Pogliano, K.2
  • 7
    • 44449115576 scopus 로고    scopus 로고
    • Daptomycin exerts bactericidal activity without lysis of Staphylococcus aureus. Antimicrob
    • Cotroneo N, Harris R, Perlmutter N, Beveridge T, Silverman JA. 2008. Daptomycin exerts bactericidal activity without lysis of Staphylococcus aureus. Antimicrob. Agents Chemother. 52:2223-2225.
    • (2008) Agents Chemother. , vol.52 , pp. 2223-2225
    • Cotroneo, N.1    Harris, R.2    Perlmutter, N.3    Beveridge, T.4    Silverman, J.A.5
  • 8
    • 33644655658 scopus 로고    scopus 로고
    • Correlation between reduced daptomycin susceptibility and vancomycin resistance in vancomycin-intermediate Staphylococcus aureus
    • Cui L, Tominaga E, Neoh HM, Hiramatsu K. 2006. Correlation between reduced daptomycin susceptibility and vancomycin resistance in vancomycin-intermediate Staphylococcus aureus. Antimicrob. Agents Chemother. 50:1079-1082.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1079-1082
    • Cui, L.1    Tominaga, E.2    Neoh, H.M.3    Hiramatsu, K.4
  • 9
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell
    • Daniel RA, Errington J. 2003. Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113:767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 10
    • 75749105024 scopus 로고    scopus 로고
    • Daptomycin: from the mountain to the clinic, with essential help from Francis Tally, MD
    • Eisenstein BI, Oleson FB, Jr, Baltz RH. 2010. Daptomycin: from the mountain to the clinic, with essential help from Francis Tally, MD. Clin. Infect. Dis. 50(Suppl. 1):S10-S15.
    • (2010) Clin. Infect. Dis. , vol.50 , Issue.SUPPL. 1
    • Eisenstein, B.I.1    Oleson Jr., F.B.2    Baltz, R.H.3
  • 12
    • 1842613501 scopus 로고    scopus 로고
    • Regulation of endospore formation in Bacillus subtilis
    • Errington J. 2003. Regulation of endospore formation in Bacillus subtilis. Nat. Rev. Microbiol. 1:117-126.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 117-126
    • Errington, J.1
  • 13
    • 84855229532 scopus 로고    scopus 로고
    • Cellular architecture mediates DivIVA ultrastructure and regulates Min activity in Bacillus subtilis
    • doi:10.1128/mBio.00257-11
    • Eswaramoorthy P, et al. 2011. Cellular architecture mediates DivIVA ultrastructure and regulates Min activity in Bacillus subtilis. Mbio 2:e00257-11. doi:10.1128/mBio.00257-11.
    • (2011) Mbio , vol.2
    • Eswaramoorthy, P.1
  • 14
    • 0141789744 scopus 로고    scopus 로고
    • Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2)
    • Flardh K. 2003. Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2). Mol. Microbiol. 49:1523-1536.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1523-1536
    • Flardh, K.1
  • 15
    • 33744485823 scopus 로고    scopus 로고
    • Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus
    • Friedman L, Alder JD, Silverman JA. 2006. Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus. Antimicrob. Agents Chemother. 50:2137-2145.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 2137-2145
    • Friedman, L.1    Alder, J.D.2    Silverman, J.A.3
  • 16
    • 46949100415 scopus 로고    scopus 로고
    • A sensor histidine kinase co-ordinates cell wall architecture with cell division in Bacillus subtilis
    • Fukushima T, Szurmant H, Kim EJ, Perego M, Hoch JA. 2008. A sensor histidine kinase co-ordinates cell wall architecture with cell division in Bacillus subtilis. Mol. Microbiol. 69:621-632.
    • (2008) Mol. Microbiol. , vol.69 , pp. 621-632
    • Fukushima, T.1    Szurmant, H.2    Kim, E.J.3    Perego, M.4    Hoch, J.A.5
  • 17
    • 65649154706 scopus 로고    scopus 로고
    • Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin
    • Hachmann AB, Angert ER, Helmann JD. 2009. Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin. Antimicrob. Agents Chemother. 53:1598-1609.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1598-1609
    • Hachmann, A.B.1    Angert, E.R.2    Helmann, J.D.3
  • 18
    • 80051814122 scopus 로고    scopus 로고
    • Reduction in membrane phosphatidylglycerol content leads to daptomycin resistance in Bacillus subtilis
    • Hachmann AB, et al. 2011. Reduction in membrane phosphatidylglycerol content leads to daptomycin resistance in Bacillus subtilis. Antimicrob. Agents Chemother. 55:4326-4337.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 4326-4337
    • Hachmann, A.B.1
  • 19
    • 79960288307 scopus 로고    scopus 로고
    • Tripropeptin C blocks the lipid cycle of cell wall biosynthesis by complex formation with undecaprenyl pyrophosphate
    • Hashizume H, et al. 2011. Tripropeptin C blocks the lipid cycle of cell wall biosynthesis by complex formation with undecaprenyl pyrophosphate. Antimicrob. Agents Chemother. 55:3821-3828.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 3821-3828
    • Hashizume, H.1
  • 20
    • 55549130778 scopus 로고    scopus 로고
    • Assemblies of DivIVA mark sites for hyphal branching and can establish new zones of cell wall growth in Streptomyces coelicolor
    • Hempel AM, Wang SB, Letek M, Gil JA, Flardh K. 2008. Assemblies of DivIVA mark sites for hyphal branching and can establish new zones of cell wall growth in Streptomyces coelicolor. J. Bacteriol. 190:7579-7583.
    • (2008) J. Bacteriol. , vol.190 , pp. 7579-7583
    • Hempel, A.M.1    Wang, S.B.2    Letek, M.3    Gil, J.A.4    Flardh, K.5
  • 21
    • 33751395400 scopus 로고    scopus 로고
    • A curvaturemediated mechanism for localization of lipids to bacterial poles
    • doi:10.1371/journal.pcbi.0020151
    • Huang KC, Mukhopadhyay R, Wingreen NS. 2006. A curvaturemediated mechanism for localization of lipids to bacterial poles. PloS Comput. Biol. 2:e151. doi:10.1371/journal.pcbi.0020151.
    • (2006) PloS Comput. Biol. , vol.2
    • Huang, K.C.1    Mukhopadhyay, R.2    Wingreen, N.S.3
  • 22
    • 77952216490 scopus 로고    scopus 로고
    • Macromolecules that prefer their membranes curvy
    • Huang KC, Ramamurthi KS. 2010. Macromolecules that prefer their membranes curvy. Mol. Microbiol. 76:822-832.
    • (2010) Mol. Microbiol. , vol.76 , pp. 822-832
    • Huang, K.C.1    Ramamurthi, K.S.2
  • 23
    • 0019452877 scopus 로고
    • The energized membrane and cellular autolysis in Bacillus subtilis
    • Jolliffe LK, Doyle RJ, Streips UN. 1981. The energized membrane and cellular autolysis in Bacillus subtilis. Cell 25:753-763.
    • (1981) Cell , vol.25 , pp. 753-763
    • Jolliffe, L.K.1    Doyle, R.J.2    Streips, U.N.3
  • 24
    • 46449102872 scopus 로고    scopus 로고
    • Lipid-specific binding of the calcium-dependent antibiotic daptomycin leads to changes in lipid polymorphism of model membranes
    • Jung D, Powers JP, Straus SK, Hancock RE. 2008. Lipid-specific binding of the calcium-dependent antibiotic daptomycin leads to changes in lipid polymorphism of model membranes. Chem. Phys. Lipids 154:120-128.
    • (2008) Chem. Phys. Lipids , vol.154 , pp. 120-128
    • Jung, D.1    Powers, J.P.2    Straus, S.K.3    Hancock, R.E.4
  • 25
    • 3342942636 scopus 로고    scopus 로고
    • Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin
    • Jung D, Rozek A, Okon M, Hancock RE. 2004. Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin. Chem. Biol. 11:949-957.
    • (2004) Chem. Biol. , vol.11 , pp. 949-957
    • Jung, D.1    Rozek, A.2    Okon, M.3    Hancock, R.E.4
  • 26
    • 0022474951 scopus 로고
    • The role of acyl chain character and other determinants on the bilayer activity of A21978C an acidic lipopeptide antibiotic
    • Lakey JH, Lea EJ. 1986. The role of acyl chain character and other determinants on the bilayer activity of A21978C an acidic lipopeptide antibiotic. Biochim. Biophys. Acta 859:219- 226.
    • (1986) Biochim. Biophys. Acta , vol.859 , pp. 219-226
    • Lakey, J.H.1    Lea, E.J.2
  • 27
    • 0023808870 scopus 로고
    • Fluorescence indicates a calcium-dependent interaction between the lipopeptide antibiotic LY146032 and phospholipid membranes
    • Lakey JH, Ptak M. 1988. Fluorescence indicates a calcium-dependent interaction between the lipopeptide antibiotic LY146032 and phospholipid membranes. Biochemistry 27:4639-4645.
    • (1988) Biochemistry , vol.27 , pp. 4639-4645
    • Lakey, J.H.1    Ptak, M.2
  • 28
    • 68249141791 scopus 로고    scopus 로고
    • Localisation of DivIVA by targeting to negatively curved membranes
    • Lenarcic R, et al. 2009. Localisation of DivIVA by targeting to negatively curved membranes. EMBO J. 28:2272-2282.
    • (2009) EMBO J , vol.28 , pp. 2272-2282
    • Lenarcic, R.1
  • 29
    • 0029918758 scopus 로고    scopus 로고
    • Transcription factor SpoOA switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis
    • Levin PA, Losick R. 1996. Transcription factor SpoOA switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis. Genes Dev. 10:478-488.
    • (1996) Genes Dev. , vol.10 , pp. 478-488
    • Levin, P.A.1    Losick, R.2
  • 30
    • 0026500823 scopus 로고
    • Crisscross regulation of cell-type-specific gene expression during development in Bacillus subtilis
    • Losick R, Stragier P. 1992. Crisscross regulation of cell-type-specific gene expression during development in Bacillus subtilis. Nature 355:601-604.
    • (1992) Nature , vol.355 , pp. 601-604
    • Losick, R.1    Stragier, P.2
  • 31
    • 77951224520 scopus 로고    scopus 로고
    • Fluorescence microscopy demonstrates enhanced targeting of telavancin to the division septum of Staphylococcus aureus
    • Lunde CS, Rexer CH, Hartouni SR, Axt S, Benton BM. 2010. Fluorescence microscopy demonstrates enhanced targeting of telavancin to the division septum of Staphylococcus aureus. Antimicrob. Agents Chemother. 54:2198-2200.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2198-2200
    • Lunde, C.S.1    Rexer, C.H.2    Hartouni, S.R.3    Axt S.Benton, B.M.4
  • 32
    • 36749053991 scopus 로고    scopus 로고
    • Bactericidal action of daptomycin against stationary-phase and nondividing Staphylococcus aureus cells
    • Mascio CT, Alder JD, Silverman JA. 2007. Bactericidal action of daptomycin against stationary-phase and nondividing Staphylococcus aureus cells. Antimicrob. Agents Chemother. 51:4255-4260.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 4255-4260
    • Mascio, C.T.1    Alder, J.D.2    Silverman, J.A.3
  • 33
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon HT, Gallop JL. 2005. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438:590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • Mcmahon, H.T.1    Gallop, J.L.2
  • 34
    • 77952161340 scopus 로고    scopus 로고
    • Cell wall synthesis is necessary for membrane dynamics during sporulation of Bacillus subtilis
    • Meyer P, Gutierrez J, Pogliano K, Dworkin J. 2010. Cell wall synthesis is necessary for membrane dynamics during sporulation of Bacillus subtilis. Mol. Microbiol. 76:956-970.
    • (2010) Mol. Microbiol. , vol.76 , pp. 956-970
    • Meyer, P.1    Gutierrez, J.2    Pogliano, K.3    Dworkin, J.4
  • 35
    • 77952578858 scopus 로고    scopus 로고
    • Binding of ceftaroline to penicillin-binding proteins of Staphylococcus aureus and Streptococcus pneumoniae
    • Moisan H, Pruneau M, Malouin F. 2010. Binding of ceftaroline to penicillin-binding proteins of Staphylococcus aureus and Streptococcus pneumoniae. J. Antimicrob. Chemother. 65:713-716.
    • (2010) J. Antimicrob. Chemother. , vol.65 , pp. 713-716
    • Moisan, H.1    Pruneau, M.2    Malouin, F.3
  • 37
    • 40549087912 scopus 로고    scopus 로고
    • Transcriptional profiling reveals that daptomycin induces th Staphylococcus aureus cell wall stress stimulon and genes responsive to membrane depolarization
    • Muthaiyan A, Silverman JA, Jayaswal RK, Wilkinson BJ. 2008. Transcriptional profiling reveals that daptomycin induces the Staphylococcus aureus cell wall stress stimulon and genes responsive to membrane depolarization. Antimicrob. Agents Chemother. 52:980-990.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 980-990
    • Muthaiyan, A.1    Silverman, J.A.2    Jayaswal, R.K.3    Wilkinson, B.J.4
  • 39
    • 34948911419 scopus 로고    scopus 로고
    • Fluorescence ratio imaging microscopy shows decreased access of vancomycin to cell wall synthetic sites in vancomycin-resistant Staphylococcus aureus
    • Pereira PM, Filipe SR, Tomasz A, Pinho MG. 2007. Fluorescence ratio imaging microscopy shows decreased access of vancomycin to cell wall synthetic sites in vancomycin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 51:3627-3633.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 3627-3633
    • Pereira, P.M.1    Filipe, S.R.2    Tomasz, A.3    Pinho, M.G.4
  • 40
    • 0033000497 scopus 로고    scopus 로고
    • A vital stain for studying membrane dynamics in bacteria: a novel mechanism controlling septation during Bacillus subtilis sporulation
    • Pogliano J, et al. 1999. A vital stain for studying membrane dynamics in bacteria: a novel mechanism controlling septation during Bacillus subtilis sporulation. Mol. Microbiol. 31:1149 -1159.
    • (1999) Mol. Microbiol. , vol.31
    • Pogliano, J.1
  • 41
    • 43249117738 scopus 로고    scopus 로고
    • Sequence-directed DNA export guides chromosome translocation during sporulation in Bacillus subtilis
    • Ptacin JL, et al. 2008. Sequence-directed DNA export guides chromosome translocation during sporulation in Bacillus subtilis. Nat. Struct. Mol. Biol. 15:485-493.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 485-493
    • Ptacin, J.L.1
  • 42
    • 78649670793 scopus 로고    scopus 로고
    • Protein localization by recognition of membrane curvature
    • Ramamurthi KS. 2010. Protein localization by recognition of membrane curvature. Curr. Opin. Microbiol. 13:753-757.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 753-757
    • Ramamurthi, K.S.1
  • 43
    • 62149141206 scopus 로고    scopus 로고
    • Geometric cue for protein localization in a bacterium
    • Ramamurthi KS, Lecuyer S, Stone HA, Losick R. 2009. Geometric cue for protein localization in a bacterium. Science 323:1354-1357.
    • (2009) Science , vol.323 , pp. 1354-1357
    • Ramamurthi, K.S.1    Lecuyer, S.2    Stone, H.A.3    Losick, R.4
  • 44
    • 69449106111 scopus 로고    scopus 로고
    • Negative membrane curvature as a cue for subcellular localization of a bacterial protein
    • Ramamurthi KS, Losick R. 2009. Negative membrane curvature as a cue for subcellular localization of a bacterial protein. Proc. Natl. Acad. Sci. U. S. A. 106:13541-13545.
    • (2009) Proc. Natl. Acad. Sci. U.S.A , Issue.106 , pp. 13541-13545
    • Ramamurthi, K.S.1    Losick, R.2
  • 45
    • 0030958619 scopus 로고    scopus 로고
    • Bacterial viability and antibiotic susceptibility testing with SYTOX green nucleic acid stain
    • Roth BL, Poot M, Yue ST, Millard PJ. 1997. Bacterial viability and antibiotic susceptibility testing with SYTOX green nucleic acid stain. Appl. Environ. Microbiol. 63:2421-2431.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2421-2431
    • Roth, B.L.1    Poot, M.2    Yue, S.T.3    Millard, P.J.4
  • 46
    • 79956328681 scopus 로고    scopus 로고
    • Mechanism of action and limited crossresistance of new lipopeptide MX-2401
    • Rubinchik E, et al. 2011. Mechanism of action and limited crossresistance of new lipopeptide MX-2401. Antimicrob. Agents Chemother. 55:2743-2754.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 2743-2754
    • Rubinchik, E.1
  • 47
    • 78650634123 scopus 로고    scopus 로고
    • Regulation of mprF by antisense RNA restores daptomycin susceptibility to daptomycin-resistant isolates of Staphylococcus aureus
    • Rubio A, et al. 2011. Regulation of mprF by antisense RNA restores daptomycin susceptibility to daptomycin-resistant isolates of Staphylococcus aureus. Antimicrob. Agents Chemother. 55:364-367.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 364-367
    • Rubio, A.1
  • 48
    • 0001925081 scopus 로고
    • Etude morphologie de la sporulation de Bacillus subtilis
    • Ryter A. 1965. Etude morphologie de la sporulation de Bacillus subtilis. Ann. Inst. Pasteur (Paris) 108:40-60.
    • (1965) Ann. Inst. Pasteur Paris , vol.108 , pp. 40-60
    • Ryter, A.1
  • 49
    • 65749087124 scopus 로고    scopus 로고
    • The lipopeptide antibiotic Friulimicin B inhibits cell wall biosynthesis through complex formation with bactoprenol phosphate
    • Schneider T, et al. 2009. The lipopeptide antibiotic Friulimicin B inhibits cell wall biosynthesis through complex formation with bactoprenol phosphate. Antimicrob. Agents Chemother. 53:1610-1618.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1610-1618
    • Schneider, T.1
  • 50
    • 0041592783 scopus 로고    scopus 로고
    • Correlation of daptomycin bactericidal activity and membrane depolarization in Staphylococcus aureus
    • Silverman JA, Perlmutter NG, Shapiro HM. 2003. Correlation of daptomycin bactericidal activity and membrane depolarization in Staphylococcus aureus. Antimicrob. Agents Chemother. 47:2538-2544.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2538-2544
    • Silverman, J.A.1    Perlmutter, N.G.2    Shapiro, H.M.3
  • 51
    • 0014533169 scopus 로고
    • Commitment to sporulation in Bacillus subtilis and its relationship to development of actinomycin resistance
    • Sterlini JM, Mandelstam J. 1969. Commitment to sporulation in Bacillus subtilis and its relationship to development of actinomycin resistance. Biochem. J. 113:29 -37.
    • (1969) Biochem. J. , vol.113 , pp. 29-37
    • Sterlini, J.M.1    Mandelstam, J.2
  • 52
    • 77955449195 scopus 로고    scopus 로고
    • Membrane potential is important for bacterial cell division
    • U. S. A
    • Strahl H, Hamoen LW. 2010. Membrane potential is important for bacterial cell division. Proc. Natl. Acad. Sci. U. S. A. 107:12281-12286.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 12281-12286
    • Strahl, H.1    Hamoen, L.W.2
  • 53
    • 33748946749 scopus 로고    scopus 로고
    • Mode of action of the new antibiotic for Gram-positive pathogens daptomycin: comparison with cationic antimicrobial peptides and lipopeptides
    • Straus SK, Hancock RE. 2006. Mode of action of the new antibiotic for Gram-positive pathogens daptomycin: comparison with cationic antimicrobial peptides and lipopeptides. Biochim. Biophys. Acta 1758:1215-1223.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1215-1223
    • Straus, S.K.1    Hancock, R.E.2
  • 54
    • 33746639594 scopus 로고    scopus 로고
    • Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics
    • U. S. A.
    • Tiyanont K, et al. 2006. Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics. Proc. Natl. Acad. Sci. U. S. A. 103: 11033-11038.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 11033-11038
    • Tiyanont, K.1
  • 55
    • 0024447804 scopus 로고
    • Scanning electronmicroscopy of Staphylococcus aureus and Enterococcus faecalis exposed to daptomycin
    • Wale LJ, Shelton AP, Greenwood D. 1989. Scanning electronmicroscopy of Staphylococcus aureus and Enterococcus faecalis exposed to daptomycin. J. Med. Microbiol. 30:45-49.
    • (1989) J. Med. Microbiol. , vol.30 , pp. 45-49
    • Wale, L.J.1    Shelton, A.P.2    Greenwood, D.3
  • 56
    • 0024447804 scopus 로고
    • Scanning electronmicroscopy of Staphylococcus aureus and Enterococcus faecalis exposed to daptomycin
    • Wale LJ, Shelton AP, Greenwood D. 1989. Scanning electronmicroscopy of Staphylococcus aureus and Enterococcus faecalis exposed to daptomycin. J. Med. Microbiol. 30:45-49.
    • (1989) J. Med. Microbiol. , vol.30 , pp. 45-49
    • Wale, L.J.1    Shelton, A.P.2    Greenwood, D.3
  • 57
    • 77955352834 scopus 로고    scopus 로고
    • Cell wall thickening is not a universal accompaniment of the daptomycin nonsusceptibility phenotype in Staphylococcus aureus: evidence for multiple resistance mechanisms. Antimicrob
    • Yang SJ, et al. 2010. Cell wall thickening is not a universal accompaniment of the daptomycin nonsusceptibility phenotype in Staphylococcus aureus: evidence for multiple resistance mechanisms. Antimicrob. Agents Chemother. 54:3079-3085.
    • (2010) Agents Chemother. , vol.54 , pp. 3079-3085
    • Yang, S.J.1
  • 58
    • 67049086887 scopus 로고    scopus 로고
    • Regulation of mprF in daptomycin-nonsusceptible Staphylococcus aureus strains
    • Yang SJ, et al. 2009. Regulation of mprF in daptomycin-nonsusceptible Staphylococcus aureus strains. Antimicrob. Agents Chemother. 53:2636-2637.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2636-2637
    • Yang, S.J.1
  • 60
    • 0032908481 scopus 로고    scopus 로고
    • A sensitive and commercially available reagent for detection of penicillinbinding proteins-Antimicrob
    • Zhao G, Meier TI, Kahl SD, Gee KR, Blaszczak LC. 1999. BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillinbinding proteins-Antimicrob. Agents Chemother. 43:1124-1128.
    • (1999) Agents Chemother , vol.43 , pp. 1124-1128
    • Zhao, G.1    Meier, T.I.2    Kahl, S.D.3    Gee K.R.Blaszczak, L.C.4    Bocillin, F.L.5


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