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Volumn 8, Issue 1, 2009, Pages 3-16

Polyfunctional antibiotics affecting bacterial membrane dynamics

Author keywords

[No Author keywords available]

Indexed keywords

AMIKACIN; AMINOGLYCOSIDE ANTIBIOTIC AGENT; AZITHROMYCIN; CECROPIN D; CLARITHROMYCIN; COLISTIN; DAPTOMYCIN; ERYTHROMYCIN; GENTAMICIN; GRAMICIDIN DERIVATIVE; IONOPHORE; LANTIBIOTIC; LASALOCID; LIPOPEPTIDE; MACROLIDE; MONENSIN; NETILMICIN; NISIN; PARDAXIN; POLYAMINE DERIVATIVE; POLYMYXIN B; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN; ROXITHROMYCIN; STREPTOMYCIN; SURFACTIN; TEICOPLANIN DERIVATIVE; TELAVANCIN; UNINDEXED DRUG; VANCOMYCIN;

EID: 67651100935     PISSN: 18715214     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152109787047779     Document Type: Article
Times cited : (20)

References (81)
  • 1
    • 0001634844 scopus 로고
    • Supramolecular transport of metal amine complexes through liquid membranes by the ionophore lasalocid A
    • Chia, P. S. K.; Lindoy, L. F.; Walker, G. W.; Everett, G. W. Supramolecular transport of metal amine complexes through liquid membranes by the ionophore lasalocid A. Pure Appl. Chem. 1993, 65, 521-526.
    • (1993) Pure Appl. Chem , vol.65 , pp. 521-526
    • Chia, P.S.K.1    Lindoy, L.F.2    Walker, G.W.3    Everett, G.W.4
  • 2
    • 0023375673 scopus 로고
    • Sensitivity of Escherichia coli to various b-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic b-lactamases: A quantitative predictive treatment
    • Nikaido, H.; Normark, S. Sensitivity of Escherichia coli to various b-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic b-lactamases: a quantitative predictive treatment. Mol. Microbiol., 1987, 1, 29-36.
    • (1987) Mol. Microbiol , vol.1 , pp. 29-36
    • Nikaido, H.1    Normark, S.2
  • 3
    • 0030542269 scopus 로고    scopus 로고
    • Outer-sphere and inner-sphere complexation of cations by the natural ionophore lasalocid A
    • Lindoy, L. F. Outer-sphere and inner-sphere complexation of cations by the natural ionophore lasalocid A. Coord. Chem. Rev. 1996, 148, 349-368.
    • (1996) Coord. Chem. Rev , vol.148 , pp. 349-368
    • Lindoy, L.F.1
  • 4
    • 0031542249 scopus 로고    scopus 로고
    • Structure, dynamics, and topological orientation of the polyether, ionophore antibiotic monensin, in a micellar environment
    • Mercurio, E.; Pellegrini, M.; Mierke, D. F. Structure, dynamics, and topological orientation of the polyether, ionophore antibiotic monensin, in a micellar environment. Biopolymers 1997, 42, 759-769.
    • (1997) Biopolymers , vol.42 , pp. 759-769
    • Mercurio, E.1    Pellegrini, M.2    Mierke, D.F.3
  • 5
    • 0142176967 scopus 로고    scopus 로고
    • Monovalent cation salts of bacterial ionophore monensin in methanol. Structural aspects from NMR experiments
    • Mimouni, M.; Hebrant, M.; Dauphin, G.; Muillard, J. Monovalent cation salts of bacterial ionophore monensin in methanol. Structural aspects from NMR experiments. J. Chem. Res. Synopsis, 1996, 6, 278-279.
    • (1996) J. Chem. Res. Synopsis , vol.6 , pp. 278-279
    • Mimouni, M.1    Hebrant, M.2    Dauphin, G.3    Muillard, J.4
  • 6
    • 67651131949 scopus 로고    scopus 로고
    • Shimohigashi, Y.; Yoshitomi, H.; Ono, S.; Sakaguchi, K.; Waki, M. Structure function studies of gramicidin S. I. Ornithine side chains are not necessary to the antimicrobial activity. Peptide Chem., 1989, 26, 313-316.
    • Shimohigashi, Y.; Yoshitomi, H.; Ono, S.; Sakaguchi, K.; Waki, M. Structure function studies of gramicidin S. I. Ornithine side chains are not necessary to the antimicrobial activity. Peptide Chem., 1989, 26, 313-316.
  • 8
    • 1842739447 scopus 로고    scopus 로고
    • Synthesis of Gramicidin S and its analogues via an on-resin macrolactamization assisted by a predisposed conformation of linear precursors
    • Bu, X.; Wu, X.; Ng, N. L. J.; Mak, C. K.; Qin, C.; Guo, Z. Synthesis of Gramicidin S and its analogues via an on-resin macrolactamization assisted by a predisposed conformation of linear precursors. J. Org. Chem., 2003, 69, 2681.
    • (2003) J. Org. Chem , vol.69 , pp. 2681
    • Bu, X.1    Wu, X.2    Ng, N.L.J.3    Mak, C.K.4    Qin, C.5    Guo, Z.6
  • 9
    • 19644376403 scopus 로고    scopus 로고
    • Synthesis and properties of gramicidin S analogues with smaller ring size
    • Tamaki, M.; Ishii, R.;, Kikuchi, S.; Watanabe, E. Synthesis and properties of gramicidin S analogues with smaller ring size. J. Antibiotics, 2005, 58, 293-295.
    • (2005) J. Antibiotics , vol.58 , pp. 293-295
    • Tamaki, M.1    Ishii, R.2    Kikuchi, S.3    Watanabe, E.4
  • 10
    • 0022553466 scopus 로고
    • Mode of action of gramicidin S on Escherichia coli membrane
    • Katsu, T.; Kobayashi, H.; Fujita, Y. Mode of action of gramicidin S on Escherichia coli membrane. Biochim. Biophys. Acta Biomem., 1986, 860, 608-619.
    • (1986) Biochim. Biophys. Acta Biomem , vol.860 , pp. 608-619
    • Katsu, T.1    Kobayashi, H.2    Fujita, Y.3
  • 11
    • 0025241061 scopus 로고
    • Heavy metal cation-induced increase in gramicidin activity. Higher sensitivity of metalloresistant mutants of 0Escherichia coli B to the antibiotic
    • Kuzovnikova, T. A.; Fedorov, Y. I. Heavy metal cation-induced increase in gramicidin activity. Higher sensitivity of metalloresistant mutants of 0Escherichia coli B to the antibiotic. Antibiotiki i Khimioterapiya, 1990, 35, 24-27.
    • (1990) Antibiotiki i Khimioterapiya , vol.35 , pp. 24-27
    • Kuzovnikova, T.A.1    Fedorov, Y.I.2
  • 12
    • 0024343845 scopus 로고
    • Cooperative binding of primycin and gramicidin on erythrocyte membranes. A cation transport study
    • Sugar, I. P.; Blasko, K.; Gyorgyi, S.; Shchagina, L. V.; Malev, V. V.; Lev, A. A. Cooperative binding of primycin and gramicidin on erythrocyte membranes. A cation transport study. Membr. Biochem., 1989, 8, 1-10.
    • (1989) Membr. Biochem , vol.8 , pp. 1-10
    • Sugar, I.P.1    Blasko, K.2    Gyorgyi, S.3    Shchagina, L.V.4    Malev, V.V.5    Lev, A.A.6
  • 13
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner, E. J.; Lewis, R. N. A. H.; McElhaney, R. N. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim. Biophys. Acta Biomembr., 1999, 1462, 201-221.
    • (1999) Biochim. Biophys. Acta Biomembr , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 14
    • 0011098761 scopus 로고    scopus 로고
    • NMR elucidation of anesthetic binding sites in transmembrane channels
    • Xu, Y.; Tang, P.; Zubrzycki, I. Z.; Hu, J. NMR elucidation of anesthetic binding sites in transmembrane channels. Prog. Anesthetic Mech., 2000, 6, 306-311.
    • (2000) Prog. Anesthetic Mech , vol.6 , pp. 306-311
    • Xu, Y.1    Tang, P.2    Zubrzycki, I.Z.3    Hu, J.4
  • 15
    • 8944248272 scopus 로고    scopus 로고
    • Polyamines decrease Escherichia coli outer membrane permeability
    • dela Vega, A. L.; Delcour, A. H. Polyamines decrease Escherichia coli outer membrane permeability. J. Bacteriol., 1996, 178, 3715-3721.
    • (1996) J. Bacteriol , vol.178 , pp. 3715-3721
    • dela Vega, A.L.1    Delcour, A.H.2
  • 16
    • 0032944380 scopus 로고    scopus 로고
    • Excretion of endogenous cadaverine leads to a decrease in porin-mediated outer membrane permeability
    • Samartzidou, H.; Delcour, A. H. Excretion of endogenous cadaverine leads to a decrease in porin-mediated outer membrane permeability. J. Bacteriol., 1999, 181, 791-798.
    • (1999) J. Bacteriol , vol.181 , pp. 791-798
    • Samartzidou, H.1    Delcour, A.H.2
  • 17
    • 18744428537 scopus 로고    scopus 로고
    • Streptomycin bactericidal action is dependent on polyamine endogenous levels in E. coli
    • Diniello, G. B.; Algranati, I. D.; Goldemberg, S. H. Streptomycin bactericidal action is dependent on polyamine endogenous levels in E. coli. Cell Mol. Biol.(Paris), 1998, 44, 521-526.
    • (1998) Cell Mol. Biol.(Paris) , vol.44 , pp. 521-526
    • Diniello, G.B.1    Algranati, I.D.2    Goldemberg, S.H.3
  • 18
    • 3042644686 scopus 로고    scopus 로고
    • Mode of action of novel polyamines increasing the permeability of bacterial outer membrane
    • Yasuda, K.; Ohmizo, C.; Katsu, T. Mode of action of novel polyamines increasing the permeability of bacterial outer membrane. Int. J. of Antimicrob. Agents, 2004, 24, 67-71.
    • (2004) Int. J. of Antimicrob. Agents , vol.24 , pp. 67-71
    • Yasuda, K.1    Ohmizo, C.2    Katsu, T.3
  • 20
    • 0031933628 scopus 로고    scopus 로고
    • Permeabilizing action of polyethyleneimine on Salmonella typhimurium involves disruption of the outer membrane and interactions with lipopolysaccharide
    • Helander, I. M.; Latva-Kala, K.; Lounatmaa, K. Permeabilizing action of polyethyleneimine on Salmonella typhimurium involves disruption of the outer membrane and interactions with lipopolysaccharide. Microbiology, 1998, 144, 385-390.
    • (1998) Microbiology , vol.144 , pp. 385-390
    • Helander, I.M.1    Latva-Kala, K.2    Lounatmaa, K.3
  • 21
    • 0031217778 scopus 로고    scopus 로고
    • Multiantibiotic resistance caused by active drug extrusion in Pseudomonas aeruginosa and other Gram-negative bacteria
    • Nakae, T. Multiantibiotic resistance caused by active drug extrusion in Pseudomonas aeruginosa and other Gram-negative bacteria. Microbiologia (Madrid), 1997, 13, 273-284.
    • (1997) Microbiologia (Madrid) , vol.13 , pp. 273-284
    • Nakae, T.1
  • 22
    • 0003830516 scopus 로고
    • Misread protein creates membrane channels: An essential step in the bactericidal action of aminoglycosides
    • Davis, B. D.; Chen, L.; Tai, P.C. Misread protein creates membrane channels: an essential step in the bactericidal action of aminoglycosides. Proc. Nat. Acad. Sci. USA, 1986, 83, 6164-6168.
    • (1986) Proc. Nat. Acad. Sci. USA , vol.83 , pp. 6164-6168
    • Davis, B.D.1    Chen, L.2    Tai, P.C.3
  • 23
    • 0023867194 scopus 로고
    • Amikacin disrupts the cell envelope of Pseudomonas aeruginosa ATCC 9027
    • Walker, S. G.; Beveridge, T. J. Amikacin disrupts the cell envelope of Pseudomonas aeruginosa ATCC 9027. Can. J. Microbiol., 1988, 34, 12-18.
    • (1988) Can. J. Microbiol , vol.34 , pp. 12-18
    • Walker, S.G.1    Beveridge, T.J.2
  • 24
    • 0024383106 scopus 로고
    • Influence of aminoglycosides on [14C]benzylpenicillin binding to Escherichia coli penicillin-binding proteins
    • Belyavskaya, I. V.; Gryaznova, N. S.; Subbotina, N. A.; Afonin, V. I. Influence of aminoglycosides on [14C]benzylpenicillin binding to Escherichia coli penicillin-binding proteins. Antibiotiki i Khimioterapiya, 1989, 34, 510.
    • (1989) Antibiotiki i Khimioterapiya , vol.34 , pp. 510
    • Belyavskaya, I.V.1    Gryaznova, N.S.2    Subbotina, N.A.3    Afonin, V.I.4
  • 25
    • 0024440040 scopus 로고    scopus 로고
    • Nouhnejad, P.; Salehian, P. Toxicity and mechanism of action of aminoglycoside antibiotics (gentamicin and amikacin) at the level of neural membranes. Asia Pacific J. Pharm., 1989, 4, 227-231.
    • Nouhnejad, P.; Salehian, P. Toxicity and mechanism of action of aminoglycoside antibiotics (gentamicin and amikacin) at the level of neural membranes. Asia Pacific J. Pharm., 1989, 4, 227-231.
  • 26
    • 0026507243 scopus 로고
    • Aminoglycoside antibiotics block voltage-dependent calcium channels in intact vertebrate nerve terminals
    • Parsons, T. D.; Obaid, A. L.; Salzberg, B. M. Aminoglycoside antibiotics block voltage-dependent calcium channels in intact vertebrate nerve terminals. J. Gen. Physiol., 1992, 99, 491-504.
    • (1992) J. Gen. Physiol , vol.99 , pp. 491-504
    • Parsons, T.D.1    Obaid, A.L.2    Salzberg, B.M.3
  • 27
    • 0021239244 scopus 로고
    • The use of redox compounds as potentiators of aminoglycoside sensitivity in highly resistant gram-negative bacteria
    • Pessione, E.; Martinetto, P.; Giunta, C.; Achino, A.; Curino, E. The use of redox compounds as potentiators of aminoglycoside sensitivity in highly resistant gram-negative bacteria. Drugs Exp. Clin. Res., 1984, 10, 303-314.
    • (1984) Drugs Exp. Clin. Res , vol.10 , pp. 303-314
    • Pessione, E.1    Martinetto, P.2    Giunta, C.3    Achino, A.4    Curino, E.5
  • 29
    • 0025340980 scopus 로고
    • Adsorption of gentamicin onto a bilayer lipid membrane
    • Butko, P.; Salamon, Z.; Tien, H. T. Adsorption of gentamicin onto a bilayer lipid membrane. Bioelectrochem. Bioenerg., 1990, 23, 153-160.
    • (1990) Bioelectrochem. Bioenerg , vol.23 , pp. 153-160
    • Butko, P.1    Salamon, Z.2    Tien, H.T.3
  • 30
    • 0022401906 scopus 로고
    • Distribution of gentamicin in the guinea pig inner ear as determined by immunofluorescence
    • Hayashida, T.; Nomura, Y.; Iwamori, M.; Nagai, Y.; Kurata, T. Distribution of gentamicin in the guinea pig inner ear as determined by immunofluorescence. Archives Oto-Rhino-Laryngol., 1985, 242, 257-264.
    • (1985) Archives Oto-Rhino-Laryngol , vol.242 , pp. 257-264
    • Hayashida, T.1    Nomura, Y.2    Iwamori, M.3    Nagai, Y.4    Kurata, T.5
  • 32
    • 0025349707 scopus 로고
    • Effects of production of abnormal proteins on the rate of killing of Escherichia coli by streptomycin
    • Wyka, M. A.; St. John, A. C. Effects of production of abnormal proteins on the rate of killing of Escherichia coli by streptomycin. Antimicrob. Agents Chemother., 1990, 34, 534-538.
    • (1990) Antimicrob. Agents Chemother , vol.34 , pp. 534-538
    • Wyka, M.A.1    St. John, A.C.2
  • 33
    • 15844431142 scopus 로고    scopus 로고
    • Daptomycin: A lipopeptide antibiotic for the treatment of serious Gram-positive infections
    • Steenbergen, J. N.; Alder, J.; Thorne, G. M.; Tally, F. P. Daptomycin: a lipopeptide antibiotic for the treatment of serious Gram-positive infections. J. Antimicrob. Chemother., 2005, 55, 283-288.
    • (2005) J. Antimicrob. Chemother , vol.55 , pp. 283-288
    • Steenbergen, J.N.1    Alder, J.2    Thorne, G.M.3    Tally, F.P.4
  • 34
    • 0026009533 scopus 로고
    • Daptomycin disrupts membrane potential in growing Staphylococcus aureus
    • Alborn, W. E., Jr.; Allen, N. E.; Preston, D. A. Daptomycin disrupts membrane potential in growing Staphylococcus aureus. Antimicrob. Agents Chemother., 1991, 35, 2282-2287.
    • (1991) Antimicrob. Agents Chemother , vol.35 , pp. 2282-2287
    • Alborn Jr., W.E.1    Allen, N.E.2    Preston, D.A.3
  • 35
    • 0041592783 scopus 로고    scopus 로고
    • Correlation of daptomycin bactericidal activity and membrane depolarization in Staphylococcus aureus
    • Silverman, J. A.; Perlmutter, N. G.; Shapiro, H. M. Correlation of daptomycin bactericidal activity and membrane depolarization in Staphylococcus aureus. Antimicrob. Agents Chemother., 2003, 47, 2538-2544.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 2538-2544
    • Silverman, J.A.1    Perlmutter, N.G.2    Shapiro, H.M.3
  • 36
    • 0034223021 scopus 로고    scopus 로고
    • Purification of daptomycin binding proteins (DBPs) from the membrane of Enterococcus hirae
    • Boaretti, M.; Canepari, P. Purification of daptomycin binding proteins (DBPs) from the membrane of Enterococcus hirae. Microbiologica, 2000, 23, 305-317.
    • (2000) Microbiologica , vol.23 , pp. 305-317
    • Boaretti, M.1    Canepari, P.2
  • 37
    • 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, R. E. W. Structural Transitions as determinants of the action of the calcium-dependent antibiotic daptomycin. Chem. Biol., 2004, 11, 949-957.
    • (2004) Chem. Biol , vol.11 , pp. 949-957
    • Jung, D.1    Rozek, A.2    Okon, M.3    Hancock, R.E.W.4
  • 38
    • 20344382979 scopus 로고    scopus 로고
    • A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution
    • Rotondi, K. S.; Gierasch, L. M. A well-defined amphipathic conformation for the calcium-free cyclic lipopeptide antibiotic, daptomycin, in aqueous solution. Biopolymers, 2005, 80, 374-385.
    • (2005) Biopolymers , vol.80 , pp. 374-385
    • Rotondi, K.S.1    Gierasch, L.M.2
  • 39
  • 40
    • 20444384347 scopus 로고    scopus 로고
    • Inhibition of daptomycin by pulmonary surfactant: In vitro modeling and clinical impact
    • i
    • Silverman, J.A.; Mortin, L. I.; VanPraagh, A. D. G.; Tongchuan, L.; Alder, J. Inhibition of daptomycin by pulmonary surfactant: In vitro modeling and clinical impact. J. Infect. Dis., 2005, [i 191, 2149.
    • (2005) J. Infect. Dis , vol.191 , pp. 2149
    • Silverman, J.A.1    Mortin, L.I.2    VanPraagh, A.D.G.3    Tongchuan, L.4    Alder, J.5
  • 41
    • 0038377291 scopus 로고    scopus 로고
    • Influence of polymyxins on the structural dynamics of Escherichia coli lipid membranes
    • Clausell, A.; Pujol, M.; Alsina, M. A.; Cajal, Y. Influence of polymyxins on the structural dynamics of Escherichia coli lipid membranes. Talanta, 2003, 60, 225-234.
    • (2003) Talanta , vol.60 , pp. 225-234
    • Clausell, A.1    Pujol, M.2    Alsina, M.A.3    Cajal, Y.4
  • 42
    • 0032520840 scopus 로고    scopus 로고
    • Molecular mechanisms of polymyxin B-membrane interactions: Direct correlation between surface charge density and self-promoted transport
    • Wiese, A.; Munstermann, M.; Gutsmann, T.; Lindner, B.; Kawahara, K.; Zahringer, U.; Seydel, U. Molecular mechanisms of polymyxin B-membrane interactions: direct correlation between surface charge density and self-promoted transport. J. Mem. Biol., 1998, 162, 127-138.
    • (1998) J. Mem. Biol , vol.162 , pp. 127-138
    • Wiese, A.1    Munstermann, M.2    Gutsmann, T.3    Lindner, B.4    Kawahara, K.5    Zahringer, U.6    Seydel, U.7
  • 43
    • 10844275575 scopus 로고    scopus 로고
    • Polymyxin B-lipid interactions in Langmuir-Blodgett monolayers of Escherichia coli lipids: A thermodynamic and atomic force microscopy study
    • Clausell, A.; Busquets, M. A.; Pujol, M.; Alsina, A.; Cajal, Y. Polymyxin B-lipid interactions in Langmuir-Blodgett monolayers of Escherichia coli lipids: A thermodynamic and atomic force microscopy study. Biopolymers, 2004, 75, 480-490.
    • (2004) Biopolymers , vol.75 , pp. 480-490
    • Clausell, A.1    Busquets, M.A.2    Pujol, M.3    Alsina, A.4    Cajal, Y.5
  • 47
    • 14844362397 scopus 로고    scopus 로고
    • Chemical and enzymatic synthesis of lanthionines
    • Paul, M.; van der Donk, W. A. Chemical and enzymatic synthesis of lanthionines. Mini-Rev. Organic Chem., 2005, 2, 23-37.
    • (2005) Mini-Rev. Organic Chem , vol.2 , pp. 23-37
    • Paul, M.1    van der Donk, W.A.2
  • 48
    • 0001879962 scopus 로고    scopus 로고
    • Lanthionine-containing antibiotic peptides (lantibiotics): Features, functions and perspectives
    • Bierbaum, G.; Brotz, H.; Sahl, H.G. Lanthionine-containing antibiotic peptides (lantibiotics): features, functions and perspectives. BIOspektrum, 1997, 3, 51-55.
    • (1997) BIOspektrum , vol.3 , pp. 51-55
    • Bierbaum, G.1    Brotz, H.2    Sahl, H.G.3
  • 49
    • 0036257622 scopus 로고    scopus 로고
    • Multiple activities in lantibiotics - models for the design of novel antibiotics?
    • Pag, U.; Sahl, H. G. Multiple activities in lantibiotics - models for the design of novel antibiotics? Curr. Pharm. Des., 2002, 8, 815-833.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 815-833
    • Pag, U.1    Sahl, H.G.2
  • 50
    • 0021993065 scopus 로고
    • Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles
    • Ruhr, E.; Sahl, H. G. Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrob. Agents Chemother., 1985, 27, 841-845.
    • (1985) Antimicrob. Agents Chemother , vol.27 , pp. 841-845
    • Ruhr, E.1    Sahl, H.G.2
  • 52
    • 0023547233 scopus 로고
    • Autolytic system of Staphylococcus simulans 22: Influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase
    • Bierbaum, G.; Sahl, H. G. Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase. J. Bacteriol., 1987, 169, 5452-5428.
    • (1987) J. Bacteriol , vol.169 , pp. 5452-5428
    • Bierbaum, G.1    Sahl, H.G.2
  • 57
    • 0033519259 scopus 로고    scopus 로고
    • The vancomycin group of antibiotics and the fight against resistant bacteria
    • Williams, D. H.; Bardsley, B. The vancomycin group of antibiotics and the fight against resistant bacteria. Angewandte Chem. Inter. Ed., 1999, 38, 1173-1193.
    • (1999) Angewandte Chem. Inter. Ed , vol.38 , pp. 1173-1193
    • Williams, D.H.1    Bardsley, B.2
  • 59
    • 0030998236 scopus 로고    scopus 로고
    • Glycopeptide resistance in multiple antibiotic-resistant gram-positive bacteria: A current challenge for novel semi-synthetic glycopeptide derivatives
    • Malabarba, A.; Nicas, T.; Ciabatti, R. Glycopeptide resistance in multiple antibiotic-resistant gram-positive bacteria: a current challenge for novel semi-synthetic glycopeptide derivatives. Euro. J. Med. Chem., 1997, 32, 459-478.
    • (1997) Euro. J. Med. Chem , vol.32 , pp. 459-478
    • Malabarba, A.1    Nicas, T.2    Ciabatti, R.3
  • 60
    • 3142743426 scopus 로고    scopus 로고
    • Characterization of an inducible vancomycin resistance system in Streptomyces coelicolor reveals a novel gene (vanK) required for drug resistance
    • Hong, H.J.; Hutchings, M. I.; Neu, J. M.; Wright, G. D.; Paget, M. S. B.; Buttner, M. J. Characterization of an inducible vancomycin resistance system in Streptomyces coelicolor reveals a novel gene (vanK) required for drug resistance. Mol. Microbiol., 2004, 52, 1107-1121.
    • (2004) Mol. Microbiol , vol.52 , pp. 1107-1121
    • Hong, H.J.1    Hutchings, M.I.2    Neu, J.M.3    Wright, G.D.4    Paget, M.S.B.5    Buttner, M.J.6
  • 62
    • 0031038392 scopus 로고    scopus 로고
    • Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-Dalanine and D-alanyl-D-lactate residues
    • Allen, N. E.; LeTourneau, D. L.; Hobbs, J. J. N. Molecular interactions of a semisynthetic glycopeptide antibiotic with D-alanyl-Dalanine and D-alanyl-D-lactate residues. Antimicrob. Agents Chemother., 1997, 41, 66-71.
    • (1997) Antimicrob. Agents Chemother , vol.41 , pp. 66-71
    • Allen, N.E.1    LeTourneau, D.L.2    Hobbs, J.J.N.3
  • 63
    • 0037468882 scopus 로고    scopus 로고
    • Role of the glycopeptide framework in the antibacterial activity of hydrophobic derivatives of glycopeptide antibiotics
    • Printsevskaya, S. S.; Pavlov, A. Y.; Olsufyeva, E. N.; Mirchink, E. P.; Preobrazhenskaya, M. N. Role of the glycopeptide framework in the antibacterial activity of hydrophobic derivatives of glycopeptide antibiotics. J. Med. Chem., 2003, 46, 1204-1209.
    • (2003) J. Med. Chem , vol.46 , pp. 1204-1209
    • Printsevskaya, S.S.1    Pavlov, A.Y.2    Olsufyeva, E.N.3    Mirchink, E.P.4    Preobrazhenskaya, M.N.5
  • 64
    • 13544267650 scopus 로고    scopus 로고
    • Sorbera, L. A.; Castaner, J. Telavancin hydrochloride. Drugs Future, 2004, 29, 1211-1219.
    • Sorbera, L. A.; Castaner, J. Telavancin hydrochloride. Drugs Future, 2004, 29, 1211-1219.
  • 65
    • 2542485522 scopus 로고    scopus 로고
    • In vitro activities of the new semisynthetic glycopeptide telavancin (TD-6424), vancomycin, daptomycin, linezolid, and four comparator agents against anaerobic Gram-positive species and Corynebacterium spp
    • Goldstein, E. J. C.; Citron, D. M.; Merriam, C. V.; Warren, Y. A.; Tyrrell, K. L.; Fernandez, H. T. In vitro activities of the new semisynthetic glycopeptide telavancin (TD-6424), vancomycin, daptomycin, linezolid, and four comparator agents against anaerobic Gram-positive species and Corynebacterium spp. Antimicrob. Agents Chemother., 2004, 48, 2149-2152.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 2149-2152
    • Goldstein, E.J.C.1    Citron, D.M.2    Merriam, C.V.3    Warren, Y.A.4    Tyrrell, K.L.5    Fernandez, H.T.6
  • 66
    • 0032004829 scopus 로고    scopus 로고
    • Permeation and concentration of erythromycin by supported and emulsion liquid membranes
    • Habaki, H., Isobe, S., Egashirea, R., Kawasaki, J. Permeation and concentration of erythromycin by supported and emulsion liquid membranes. J. Chem. Eng., 1998, 31, 47.
    • (1998) J. Chem. Eng , vol.31 , pp. 47
    • Habaki, H.1    Isobe, S.2    Egashirea, R.3    Kawasaki, J.4
  • 70
    • 67651133743 scopus 로고
    • Interaction of lipid bilayer membranes with amphiphilic helical peptides
    • Huang, H. W.; He, K.; Heller, W.; Ludtke, S. J. Interaction of lipid bilayer membranes with amphiphilic helical peptides. Proc. Rencontre de Moriond, 1995, 30th, 339-344.
    • (1995) Proc. Rencontre de Moriond , vol.30 th , pp. 339-344
    • Huang, H.W.1    He, K.2    Heller, W.3    Ludtke, S.J.4
  • 71
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M. R.; Yount, N. Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev., 2003, 55, 27-55.
    • (2003) Pharmacol. Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 72
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • Andreu, D.; Rivas, L. Animal antimicrobial peptides: an overview. Biopolymers, 1999, 47, 415.
    • (1999) Biopolymers , vol.47 , pp. 415
    • Andreu, D.1    Rivas, L.2
  • 73
    • 0029947232 scopus 로고    scopus 로고
    • A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from Moses sole fish Pardachirus marmoratus
    • Oren, Z.; Shai, Y. A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from Moses sole fish Pardachirus marmoratus. Eur. J. Biochem., 1996, 237, 303-310.
    • (1996) Eur. J. Biochem , vol.237 , pp. 303-310
    • Oren, Z.1    Shai, Y.2
  • 74
    • 0031015251 scopus 로고    scopus 로고
    • Antimycoplasma properties and application in cell culture of surfactin, a lipopeptide antibiotic from Bacillus subtilin
    • Vollenbroich, D; Pauli, G.;Oezel, M.;Vater, J. Antimycoplasma properties and application in cell culture of surfactin, a lipopeptide antibiotic from Bacillus subtilin. Appl. Envir. Microbiol., 1997, 63, 44-49.
    • (1997) Appl. Envir. Microbiol , vol.63 , pp. 44-49
    • Vollenbroich, D.1    Pauli, G.2    Oezel, M.3    Vater, J.4
  • 75
    • 0025081012 scopus 로고
    • Bacternecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in large storage granules
    • Zanetti, M.; Litteri, L.; Gennaro, R.; Horstmann H.;Romeo, D. Bacternecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in large storage granules. J. Cell Biol., 1990, 111, 1363-1371.
    • (1990) J. Cell Biol , vol.111 , pp. 1363-1371
    • Zanetti, M.1    Litteri, L.2    Gennaro, R.3    Horstmann, H.4    Romeo, D.5
  • 76
    • 0025107597 scopus 로고
    • Antibiotic proteins of human neutrophils
    • Spitznagel, J.K. Antibiotic proteins of human neutrophils. J. Clin. Investig., 1990, 86, 1381-1386.
    • (1990) J. Clin. Investig , vol.86 , pp. 1381-1386
    • Spitznagel, J.K.1
  • 77
    • 0036607940 scopus 로고    scopus 로고
    • Antimicrobial peptides are signalling molecules
    • Salzet, M. Antimicrobial peptides are signalling molecules. Trends Immunol., 2002, 23, 283-284.
    • (2002) Trends Immunol , vol.23 , pp. 283-284
    • Salzet, M.1
  • 78
    • 0006422025 scopus 로고    scopus 로고
    • The innate immune response of the respiratory epithelium
    • Diamond, G.; Legarda, D.; Ryan, L.K. The innate immune response of the respiratory epithelium. Immunol. Rev., 2000, 173, 27-38.
    • (2000) Immunol. Rev , vol.173 , pp. 27-38
    • Diamond, G.1    Legarda, D.2    Ryan, L.K.3
  • 79
    • 0033664277 scopus 로고    scopus 로고
    • Leukocyte antimicrobial peptides: Multifunctional effector molecules of innate immunity
    • Risso, A. Leukocyte antimicrobial peptides: multifunctional effector molecules of innate immunity. J. Leukocyte Biol., 2000, 68, 785-792.
    • (2000) J. Leukocyte Biol , vol.68 , pp. 785-792
    • Risso, A.1
  • 80
    • 0031762638 scopus 로고    scopus 로고
    • Kato, A.; Nakaya, S.; Kokubo, A.; Aiba, Y.; Ohashi, Y; Hirata, H.; Fujii, K.; Harada, K. A new anti-MRSA antibiotic complex, WAP-8294A. I. Taxonomy, isolation and biological activities. J. Antibiot., 1998, 51, 929-935.
    • Kato, A.; Nakaya, S.; Kokubo, A.; Aiba, Y.; Ohashi, Y; Hirata, H.; Fujii, K.; Harada, K. A new anti-MRSA antibiotic complex, WAP-8294A. I. Taxonomy, isolation and biological activities. J. Antibiot., 1998, 51, 929-935.
  • 81
    • 0032007337 scopus 로고    scopus 로고
    • Role of the bactericidal/permeability-increasing protein in host defence
    • Elsbach, P.; Weiss, J. Role of the bactericidal/permeability-increasing protein in host defence. Curr. Opin. Immunol., 1998, 10, 45-49.
    • (1998) Curr. Opin. Immunol , vol.10 , pp. 45-49
    • Elsbach, P.1    Weiss, J.2


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