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Volumn 2015, Issue , 2015, Pages

Antibacterial mechanisms of polymyxin and bacterial resistance

Author keywords

[No Author keywords available]

Indexed keywords

POLYMYXIN; POLYMYXIN DERIVATIVE; ANTIINFECTIVE AGENT;

EID: 84947648622     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2015/679109     Document Type: Review
Times cited : (202)

References (83)
  • 1
    • 33144473431 scopus 로고    scopus 로고
    • Bad bugs need drugs: An update on the development pipeline from the antimicrobial availability task force of the infectious diseases society of America
    • G.H. Talbot, J. Bradley, J. E. Edwards Jr., D. Gilbert, M. Scheid, and J. G. Bartlett, "Bad bugs need drugs: an update on the development pipeline from the antimicrobial availability task force of the infectious diseases society of America," Clinical Infectious Diseases, vol. 42, no. 5, pp. 657-668, 2006.
    • (2006) Clinical Infectious Diseases , vol.42 , Issue.5 , pp. 657-668
    • Talbot, G.H.1    Bradley, J.2    Edwards, J.E.3    Gilbert, D.4    Scheid, M.5    Bartlett, J.G.6
  • 2
    • 33747589695 scopus 로고    scopus 로고
    • Challenges in identifying new antimicrobial agents effective for treating infections with Acinetobacter baumannii and Pseudomonas aeruginosa
    • L. B. Rice, "Challenges in identifying new antimicrobial agents effective for treating infections with Acinetobacter baumannii and Pseudomonas aeruginosa," Clinical Infectious Diseases, vol. 43, no. 2, pp. S100-S105, 2006.
    • (2006) Clinical Infectious Diseases , vol.43 , Issue.2 , pp. S100-S105
    • Rice, L.B.1
  • 3
    • 33747603489 scopus 로고    scopus 로고
    • Old polymyxins are back: Is resistance close?
    • J. Li and R. L. Nation, "Old polymyxins are back: is resistance close?" Clinical Infectious Diseases, vol. 43, no. 5, pp. 663-664, 2006.
    • (2006) Clinical Infectious Diseases , vol.43 , Issue.5 , pp. 663-664
    • Li, J.1    Nation, R.L.2
  • 4
    • 34548273967 scopus 로고    scopus 로고
    • Antibiograms ofmultidrug-resistant clinical Acinetobacter baumannii: Promising therapeutic options for treatment of infection with colistin-resistant strains
    • J. Li, R. L. Nation, R. J. Owen, S. Wong, O. Spelman, and C. Franklin, "Antibiograms ofmultidrug-resistant clinical Acinetobacter baumannii: promising therapeutic options for treatment of infection with colistin-resistant strains," Clinical Infectious Diseases, vol. 45, no. 5, pp. 594-598, 2007.
    • (2007) Clinical Infectious Diseases , vol.45 , Issue.5 , pp. 594-598
    • Li, J.1    Nation, R.L.2    Owen, R.J.3    Wong, S.4    Spelman, O.5    Franklin, C.6
  • 6
    • 56649123524 scopus 로고    scopus 로고
    • In vitro pharmacodynamics of colistin againstmultidrug-resistant Klebsiella pneumoniae
    • A. Poudyal, B. P. Howden, J. M. Bell et al., "In vitro pharmacodynamics of colistin againstmultidrug-resistant Klebsiella pneumoniae," Journal of Antimicrobial Chemotherapy, vol. 62, no. 6, pp. 1311-1318, 2008.
    • (2008) Journal of Antimicrobial Chemotherapy , vol.62 , Issue.6 , pp. 1311-1318
    • Poudyal, A.1    Howden, B.P.2    Bell, J.M.3
  • 7
    • 36448983944 scopus 로고    scopus 로고
    • Polymyxin B for the treatment of multidrug-resistant pathogens: A critical review
    • A. P. Zavascki, L. Z. Goldani, J. Li, and R. L. Nation, "Polymyxin B for the treatment of multidrug-resistant pathogens: a critical review," Journal of Antimicrobial Chemotherapy, vol. 60, no. 6, pp. 1206-1215, 2007.
    • (2007) Journal of Antimicrobial Chemotherapy , vol.60 , Issue.6 , pp. 1206-1215
    • Zavascki, A.P.1    Goldani, L.Z.2    Li, J.3    Nation, R.L.4
  • 9
    • 77949346087 scopus 로고    scopus 로고
    • Structureactivity relationships of polymyxin antibiotics
    • T. Velkov, P. E. Thompson, R. L. Nation, and J. Li, "Structureactivity relationships of polymyxin antibiotics," Journal of Medicinal Chemistry, vol. 53, no. 5, pp. 1898-1916, 2010.
    • (2010) Journal of Medicinal Chemistry , vol.53 , Issue.5 , pp. 1898-1916
    • Velkov, T.1    Thompson, P.E.2    Nation, R.L.3    Li, J.4
  • 10
    • 84878293341 scopus 로고    scopus 로고
    • Pharmacology of polymyxins: New insights into an "old" class of antibiotics
    • T. Velkov, K. D. Roberts, R. L. Nation, P. E. Thompson, and J. Li, "Pharmacology of polymyxins: new insights into an "old" class of antibiotics," Future Microbiology, vol. 8, no. 6, pp. 711-724, 2013.
    • (2013) Future Microbiology , vol.8 , Issue.6 , pp. 711-724
    • Velkov, T.1    Roberts, K.D.2    Nation, R.L.3    Thompson, P.E.4    Li, J.5
  • 11
    • 0037630382 scopus 로고    scopus 로고
    • Isolation, structural characterization, and properties of mattacin (polymyxin M), a cyclic peptide antibiotic produced by Paenibacillus kobensis M
    • N. I. Martin, H. Hu, M. M. Moake et al., "Isolation, structural characterization, and properties of mattacin (polymyxin M), a cyclic peptide antibiotic produced by Paenibacillus kobensis M," The Journal of Biological Chemistry, vol. 278, no. 15, pp. 13124-13132, 2003.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13124-13132
    • Martin, N.I.1    Hu, H.2    Moake, M.M.3
  • 12
    • 34250710858 scopus 로고    scopus 로고
    • Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution
    • C. Rausch, I. Hoof, T. Weber, W. Wohlleben, and D. H. Huson, "Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution," BMC Evolutionary Biology, vol. 7, article 78, 2007.
    • (2007) BMC Evolutionary Biology , vol.7
    • Rausch, C.1    Hoof, I.2    Weber, T.3    Wohlleben, W.4    Huson, D.H.5
  • 13
    • 3442896886 scopus 로고    scopus 로고
    • NRPSPKS: A knowledge-based resource for analysis of NRPS-PKS megasynthases
    • M. Z. Ansari, G. Yadav, R. S. Gokhale, and D. Mohanty, "NRPSPKS: a knowledge-based resource for analysis of NRPS-PKS megasynthases," Nucleic Acids Research, vol. 32, pp. W405-W413, 2004.
    • (2004) Nucleic Acids Research , vol.32 , pp. W405-W413
    • Ansari, M.Z.1    Yadav, G.2    Gokhale, R.S.3    Mohanty, D.4
  • 14
    • 65549086085 scopus 로고    scopus 로고
    • Identification of a polymyxin synthetase gene cluster of Paenibacillus polymyxa and heterologous expression of the gene in Bacillus subtilis
    • S.-K. Choi, S.-Y. Park, R. Kim et al., "Identification of a polymyxin synthetase gene cluster of Paenibacillus polymyxa and heterologous expression of the gene in Bacillus subtilis," Journal of Bacteriology, vol. 191, no. 10, pp. 3350-3358, 2009.
    • (2009) Journal of Bacteriology , vol.191 , Issue.10 , pp. 3350-3358
    • Choi, S.-K.1    Park, S.-Y.2    Kim, R.3
  • 15
    • 23044475550 scopus 로고    scopus 로고
    • Neopeptide antibiotics that function as opsonins and membrane-permeabilizing agents for gram-negative bacteria
    • H. Tsubery, H. Yaakov, S. Cohen et al., "Neopeptide antibiotics that function as opsonins and membrane-permeabilizing agents for gram-negative bacteria," Antimicrobial Agents and Chemotherapy, vol. 49, no. 8, pp. 3122-3128, 2005.
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.8 , pp. 3122-3128
    • Tsubery, H.1    Yaakov, H.2    Cohen, S.3
  • 16
    • 0016262861 scopus 로고
    • Chemical synthesis and characterization of n fattyacyl monoaminoacyl derivatives of colistin nonapeptide
    • S. Chihara, A. Ito, and M. Yahata, "Chemical synthesis and characterization of n fattyacyl monoaminoacyl derivatives of colistin nonapeptide," Agricultural and Biological Chemistry, vol. 38, no. 10, pp. 1767-1777, 1974.
    • (1974) Agricultural and Biological Chemistry , vol.38 , Issue.10 , pp. 1767-1777
    • Chihara, S.1    Ito, A.2    Yahata, M.3
  • 17
    • 0016379789 scopus 로고
    • Chemical synthesis, isolation and characterization of α-N-fattyacyl colistin nonapeptide with special reference to the correlation between antimicrobial activity and carbon number of fattyacyl moiety
    • S. Chihara, A. Ito, andM. Yahata, "Chemical synthesis, isolation and characterization of α-N-fattyacyl colistin nonapeptide with special reference to the correlation between antimicrobial activity and carbon number of fattyacyl moiety," Agricultural and Biological Chemistry, vol. 38, no. 3, pp. 521-529, 1974.
    • (1974) Agricultural and Biological Chemistry , vol.38 , Issue.3 , pp. 521-529
    • Chihara, S.1    Ito, A.2    Yahata, M.3
  • 18
    • 0028864831 scopus 로고
    • Conformation of polymyxin B analogs in DMSO from NMR spectra and molecular modeling
    • S.-Y. Liao, G.-T. Ong, K.-T. Wang, and S.-H. Wu, "Conformation of polymyxin B analogs in DMSO from NMR spectra and molecular modeling," Biochimica et Biophysica Acta (BBA), vol. 1252, no. 2, pp. 312-320, 1995.
    • (1995) Biochimica et Biophysica Acta (BBA) , vol.1252 , Issue.2 , pp. 312-320
    • Liao, S.-Y.1    Ong, G.-T.2    Wang, K.-T.3    Wu, S.-H.4
  • 19
    • 0031106743 scopus 로고    scopus 로고
    • Polymyxin B nonapeptide: Conformations in water and in the lipopolysaccharide-bound state determined by twodimensional NMR and molecular dynamics
    • S. Bhattacharjya, S. A. David, V. I. Mathan, and P. Balaram, "Polymyxin B nonapeptide: conformations in water and in the lipopolysaccharide-bound state determined by twodimensional NMR and molecular dynamics," Biopolymers, vol. 41, pp. 251-265, 1997.
    • (1997) Biopolymers , vol.41 , pp. 251-265
    • Bhattacharjya, S.1    David, S.A.2    Mathan, V.I.3    Balaram, P.4
  • 20
    • 66449085268 scopus 로고    scopus 로고
    • Interactions of lipopolysaccharide and polymyxin studied by NMR spectroscopy
    • J. Mares, S. Kumaran, M. Gobbo, and O. Zerbe, "Interactions of lipopolysaccharide and polymyxin studied by NMR spectroscopy," Journal of Biological Chemistry, vol. 284, no. 17, pp. 11498-11506, 2009.
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.17 , pp. 11498-11506
    • Mares, J.1    Kumaran, S.2    Gobbo, M.3    Zerbe, O.4
  • 23
    • 36849073561 scopus 로고    scopus 로고
    • Semi-synthesis of polymyxin B (2-10) and colistin (2-10) analogs employing the trichloroethoxycarbonyl (Troc) group for side chain protection of α, γ-diaminobutyric acid residues
    • K. Okimura, K. Ohki, Y. Sato, K. Ohnishi, and N. Sakura, "Semi-synthesis of polymyxin B (2-10) and colistin (2-10) analogs employing the trichloroethoxycarbonyl (Troc) group for side chain protection of α, γ-diaminobutyric acid residues," Chemical and Pharmaceutical Bulletin, vol. 55, no. 12, pp. 1724-1730, 2007.
    • (2007) Chemical and Pharmaceutical Bulletin , vol.55 , Issue.12 , pp. 1724-1730
    • Okimura, K.1    Ohki, K.2    Sato, Y.3    Ohnishi, K.4    Sakura, N.5
  • 24
    • 0017037922 scopus 로고
    • Broad spectrum derivatives of polymyxin B and colistin
    • N. M. Witzke and H. Heding, "Broad spectrum derivatives of polymyxin B and colistin," The Journal of Antibiotics, vol. 29, no. 12, pp. 1349-1350, 1976.
    • (1976) The Journal of Antibiotics , vol.29 , Issue.12 , pp. 1349-1350
    • Witzke, N.M.1    Heding, H.2
  • 26
    • 62549141514 scopus 로고    scopus 로고
    • Contribution of each amino acid residue in polymyxin b3 to antimicrobial and lipopolysaccharide binding activity
    • K. Kanazawa, Y. Sato, K. Ohki et al., "Contribution of each amino acid residue in polymyxin b3 to antimicrobial and lipopolysaccharide binding activity," Chemical and Pharmaceutical Bulletin, vol. 57, no. 3, pp. 240-244, 2009.
    • (2009) Chemical and Pharmaceutical Bulletin , vol.57 , Issue.3 , pp. 240-244
    • Kanazawa, K.1    Sato, Y.2    Ohki, K.3
  • 27
    • 50949130838 scopus 로고    scopus 로고
    • Novel polymyxin derivatives carrying only three positive charges are effective antibacterial agents
    • M. Vaara, J. Fox, G. Loidl et al., "Novel polymyxin derivatives carrying only three positive charges are effective antibacterial agents," Antimicrobial Agents and Chemotherapy, vol. 52, no. 9, pp. 3229-3236, 2008.
    • (2008) Antimicrobial Agents and Chemotherapy , vol.52 , Issue.9 , pp. 3229-3236
    • Vaara, M.1    Fox, J.2    Loidl, G.3
  • 28
    • 0036840627 scopus 로고    scopus 로고
    • Modulation of the hydrophobic domain of polymyxin B nonapeptide: Effect on outer-membrane permeabilization and lipopolysaccharide neutralization
    • H. Tsubery, I. Ofek, S. Cohen, M. Eisenstein, and M. Fridkin, "Modulation of the hydrophobic domain of polymyxin B nonapeptide: effect on outer-membrane permeabilization and lipopolysaccharide neutralization," Molecular Pharmacology, vol. 62, no. 5, pp. 1036-1042, 2002.
    • (2002) Molecular Pharmacology , vol.62 , Issue.5 , pp. 1036-1042
    • Tsubery, H.1    Ofek, I.2    Cohen, S.3    Eisenstein, M.4    Fridkin, M.5
  • 29
    • 0038664329 scopus 로고    scopus 로고
    • Solidphase synthesis of polymyxin B1 and analogues via a safetycatch approach
    • P.C. DeVisser, N.M. A. J. Kriek, P. A. V. VanHooftet al., "Solidphase synthesis of polymyxin B1 and analogues via a safetycatch approach," The Journal of Peptide Research, vol. 61, no. 6, pp. 298-306, 2003.
    • (2003) The Journal of Peptide Research , vol.61 , Issue.6 , pp. 298-306
    • Devisser, P.C.1    Kriek, N.M.A.J.2    Vanhooftet Al, P.A.V.3
  • 30
    • 0034632833 scopus 로고    scopus 로고
    • Structurefunction studies of polymyxin B nonapeptide: Implications to sensitization of Gram-negative bacteria
    • H. Tsubery, I. Ofek, S. Cohen, and M. Fridkin, "Structurefunction studies of polymyxin B nonapeptide: implications to sensitization of Gram-negative bacteria," Journal of Medicinal Chemistry, vol. 43, no. 16, pp. 3085-3092, 2000.
    • (2000) Journal of Medicinal Chemistry , vol.43 , Issue.16 , pp. 3085-3092
    • Tsubery, H.1    Ofek, I.2    Cohen, S.3    Fridkin, M.4
  • 31
    • 23044475550 scopus 로고    scopus 로고
    • Neopeptide antibiotics that function as opsonins and membrane-permeabilizing agents for gram-negative bacteria
    • H. Tsubery, H. Yaakov, S. Cohen et al., "Neopeptide antibiotics that function as opsonins and membrane-permeabilizing agents for gram-negative bacteria," Antimicrobial Agents and Chemotherapy, vol. 49, no. 8, pp. 3122-3128, 2005.
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.8 , pp. 3122-3128
    • Tsubery, H.1    Yaakov, H.2    Cohen, S.3
  • 32
    • 4344638189 scopus 로고    scopus 로고
    • De novo design of potent antimicrobial peptides
    • V. Frecer, B. Ho, and J. L. Ding, "De novo design of potent antimicrobial peptides," Antimicrobial Agents and Chemotherapy, vol. 48, no. 9, pp. 3349-3357, 2004.
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.9 , pp. 3349-3357
    • Frecer, V.1    Ho, B.2    Ding, J.L.3
  • 33
    • 33748294219 scopus 로고    scopus 로고
    • Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)
    • K. Nishino, F.-F. Hsu, J. Turk, M. J. Cromie, M.M. S.M. Wösten, and E. A. Groisman, "Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)," Molecular Microbiology, vol. 61, no. 3, pp. 645-654, 2006.
    • (2006) Molecular Microbiology , vol.61 , Issue.3 , pp. 645-654
    • Nishino, K.1    Hsu, F.-F.2    Turk, J.3    Cromie, M.J.4    Wösten, M.M.S.M.5    Groisman, E.A.6
  • 34
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • H. Nikaido, "Molecular basis of bacterial outer membrane permeability revisited," Microbiology and Molecular Biology Reviews, vol. 67, no. 4, pp. 593-656, 2003.
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.4 , pp. 593-656
    • Nikaido, H.1
  • 37
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • J. P. Powers and R. E. Hancock, "The relationship between peptide structure and antibacterial activity," Peptides, vol. 24, no. 11, pp. 1681-1691, 2003.
    • (2003) Peptides , vol.24 , Issue.11 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 38
    • 3142689915 scopus 로고    scopus 로고
    • The search for molecular determinants of LPS inhibition by proteins and peptides
    • P. Pristovšek and J. Kidrič, "The search for molecular determinants of LPS inhibition by proteins and peptides," Current Topics in Medicinal Chemistry, vol. 4, no. 11, pp. 1185-1201, 2004.
    • (2004) Current Topics in Medicinal Chemistry , vol.4 , Issue.11 , pp. 1185-1201
    • Pristovšek, P.1    Kidrič, J.2
  • 40
    • 0030022871 scopus 로고    scopus 로고
    • Intermembrane molecular contacts by polymyxin B mediate exchange of phospholipids
    • Y. Cajal, J. Rogers, O. G. Berg, andM. K. Jain, "Intermembrane molecular contacts by polymyxin B mediate exchange of phospholipids," Biochemistry, vol. 35, no. 1, pp. 299-308, 1996.
    • (1996) Biochemistry , vol.35 , Issue.1 , pp. 299-308
    • Cajal, Y.1    Rogers, J.2    Berg, O.G.3    Jain, M.K.4
  • 42
    • 33645665230 scopus 로고    scopus 로고
    • Membrane association and contact formation by a synthetic analogue of polymyxin B and its fluorescent derivatives,"The
    • A. Clausell, F. Rabanal, M. Garcia-Subirats, M. A. Alsina, and Y. Cajal, "Membrane association and contact formation by a synthetic analogue of polymyxin B and its fluorescent derivatives,"The Journal of Physical Chemistry B, vol. 110, no. 9, pp. 4465-4471, 2006.
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.9 , pp. 4465-4471
    • Clausell, A.1    Rabanal, F.2    Garcia-Subirats, M.3    Alsina, M.A.4    Cajal, Y.5
  • 43
    • 84879422944 scopus 로고    scopus 로고
    • The molecular mechanisms and physiological consequences of oxidative stress: Lessons from a model bacterium
    • J. A. Imlay, "The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium," Nature Reviews Microbiology, vol. 11, no. 7, pp. 443-454, 2013.
    • (2013) Nature Reviews Microbiology , vol.11 , Issue.7 , pp. 443-454
    • Imlay, J.A.1
  • 44
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • M. A. Kohanski, D. J. Dwyer, B. Hayete, C. A. Lawrence, and J. J. Collins, "A common mechanism of cellular death induced by bactericidal antibiotics," Cell, vol. 130, no. 5, pp. 797-810, 2007.
    • (2007) Cell , vol.130 , Issue.5 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 45
    • 77954609311 scopus 로고    scopus 로고
    • Iron homeostasis affects antibiotic-mediated cell death in Pseudomonas species
    • J. Yeom, J. A. Imlay, and W. Park, "Iron homeostasis affects antibiotic-mediated cell death in Pseudomonas species," The Journal of Biological Chemistry, vol. 285, no. 29, pp. 22689-22695, 2010.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.29 , pp. 22689-22695
    • Yeom, J.1    Imlay, J.A.2    Park, W.3
  • 46
    • 33947247352 scopus 로고    scopus 로고
    • Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli
    • D. J. Dwyer, M.A. Kohanski, B. Hayete, and J. J. Collins, "Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli," Molecular Systems Biology, vol. 3, article 91, 2007.
    • (2007) Molecular Systems Biology , vol.3
    • Dwyer, D.J.1    Kohanski, M.A.2    Hayete, B.3    Collins, J.J.4
  • 47
    • 84868028125 scopus 로고    scopus 로고
    • Rapid killing of Acinetobacter baumannii by polymyxins is mediated by a hydroxyl radical death pathway
    • T. R. Sampson, X. Liu, M. R. Schroeder, C. S. Kraft, E.M. Burd, and D. S. Weiss, "Rapid killing of Acinetobacter baumannii by polymyxins is mediated by a hydroxyl radical death pathway," Antimicrobial Agents and Chemotherapy, vol. 56, no. 11, pp. 5642-5649, 2012.
    • (2012) Antimicrobial Agents and Chemotherapy , vol.56 , Issue.11 , pp. 5642-5649
    • Sampson, T.R.1    Liu, X.2    Schroeder, M.R.3    Kraft, C.S.4    Burd, E.M.5    Weiss, D.S.6
  • 48
    • 84872031103 scopus 로고    scopus 로고
    • Characterization of the polymyxin B resistome of Pseudomonas aeruginosa
    • L. Fernández, C. Àlvarez-Ortega, I. Wiegand et al., "Characterization of the polymyxin B resistome of Pseudomonas aeruginosa," Antimicrobial Agents and Chemotherapy, vol. 57, no. 1, pp. 110-119, 2013.
    • (2013) Antimicrobial Agents and Chemotherapy , vol.57 , Issue.1 , pp. 110-119
    • Fernández, L.1    Àlvarez-Ortega, C.2    Wiegand, I.3
  • 50
    • 84869204668 scopus 로고    scopus 로고
    • The two-component system CprRS senses cationic peptides and triggers adaptive resistance in Pseudomonas aeruginosa independently of ParRS
    • L. Fernández, H. Jenssen, M. Bains, I. Wiegand, W. J. Gooderham, and R. E. W. Hancock, "The two-component system CprRS senses cationic peptides and triggers adaptive resistance in Pseudomonas aeruginosa independently of ParRS," Antimicrobial Agents and Chemotherapy, vol. 56, no. 12, pp. 6212-6222, 2012.
    • (2012) Antimicrobial Agents and Chemotherapy , vol.56 , Issue.12 , pp. 6212-6222
    • Fernández, L.1    Jenssen, H.2    Bains, M.3    Wiegand, I.4    Gooderham, W.J.5    Hancock, R.E.W.6
  • 51
    • 16844384914 scopus 로고    scopus 로고
    • A formyltransferase required for polymyxin resistance in Escherichia coli and themodification of lipidAwith 4-amino- 4-deoxy-L-arabinose: Identification and function of UDP-4- deoxy-4-formamido-L-arabinose
    • S. D. Breazeale, A. A. Ribeiro, A. L. McClerren, and C. R. H. Raetz, "A formyltransferase required for polymyxin resistance in Escherichia coli and themodification of lipidAwith 4-amino- 4-deoxy-L-arabinose: identification and function of UDP-4- deoxy-4-formamido-L-arabinose," Journal of Biological Chemistry, vol. 280, no. 14, pp. 14154-14167, 2005.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 14154-14167
    • Breazeale, S.D.1    Ribeiro, A.A.2    McClerren, A.L.3    Raetz, C.R.H.4
  • 52
    • 0346655236 scopus 로고    scopus 로고
    • PmrAB , a two-component regulatory system of Pseudomonas aeruginosa thatmodulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A
    • S. M. Moskowitz, R. K. Ernst, and S. I. Miller, "PmrAB , a two-component regulatory system of Pseudomonas aeruginosa thatmodulates resistance to cationic antimicrobial peptides and addition of aminoarabinose to lipid A," Journal of Bacteriology, vol. 186, no. 2, pp. 575-579, 2004.
    • (2004) Journal of Bacteriology , vol.186 , Issue.2 , pp. 575-579
    • Moskowitz, S.M.1    Ernst, R.K.2    Miller, S.I.3
  • 53
    • 0035900684 scopus 로고    scopus 로고
    • Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PmrA-dependent 4-amino-4-deoxy- L-arabinose, and phosphoethanolamine incorporation
    • Z. Zhou, A. A. Ribeiro, S. Lin, R. J. Cotter, S. I. Miller, and C. R. H. Raetz, "Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PmrA-dependent 4-amino-4-deoxy- L-arabinose, and phosphoethanolamine incorporation," The Journal of Biological Chemistry, vol. 276, no. 46, pp. 43111-43121, 2001.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.46 , pp. 43111-43121
    • Zhou, Z.1    Ribeiro, A.A.2    Lin, S.3    Cotter, R.J.4    Miller, S.I.5    Raetz, C.R.H.6
  • 54
    • 84866872924 scopus 로고    scopus 로고
    • Reciprocal control between a bacterium's regulatory system and the modification status of its lipopolysaccharide
    • A. Kato, H. D. Chen, T. Latifi, and E. A. Groisman, "Reciprocal control between a bacterium's regulatory system and the modification status of its lipopolysaccharide," Molecular Cell, vol. 47, no. 6, pp. 897-908, 2012.
    • (2012) Molecular Cell , vol.47 , Issue.6 , pp. 897-908
    • Kato, A.1    Chen, H.D.2    Latifi, T.3    Groisman, E.A.4
  • 55
    • 3042513872 scopus 로고    scopus 로고
    • The PmrAregulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica
    • H. Lee, F.-F. Hsu, J. Turk, and E. A. Groisman, "The PmrAregulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica," Journal of Bacteriology, vol. 186, no. 13, pp. 4124-4133, 2004.
    • (2004) Journal of Bacteriology , vol.186 , Issue.13 , pp. 4124-4133
    • Lee, H.1    Hsu, F.-F.2    Turk, J.3    Groisman, E.A.4
  • 56
    • 18244379035 scopus 로고    scopus 로고
    • Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core
    • R. Tamayo, B. Choudhury, A. Septer, M. Merighi, R. Carlson, and J. S. Gunn, "Identification of cptA, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core," Journal of Bacteriology, vol. 187, no. 10, pp. 3391-3399, 2005.
    • (2005) Journal of Bacteriology , vol.187 , Issue.10 , pp. 3391-3399
    • Tamayo, R.1    Choudhury, B.2    Septer, A.3    Merighi R Carlson, M.4    Gunn, J.S.5
  • 57
    • 33644833912 scopus 로고    scopus 로고
    • The PmrA/PmrB and RcsC/YojN/RcsB systems control expression of the Salmonella O-antigen chain length determinant
    • M. A. Delgado, C. Mouslim, and E. A. Groisman, "The PmrA/PmrB and RcsC/YojN/RcsB systems control expression of the Salmonella O-antigen chain length determinant," Molecular Microbiology, vol. 60, no. 1, pp. 39-50, 2006.
    • (2006) Molecular Microbiology , vol.60 , Issue.1 , pp. 39-50
    • Delgado, M.A.1    Mouslim, C.2    Groisman, E.A.3
  • 58
    • 80052345809 scopus 로고    scopus 로고
    • The PmrA/PmrB regulatory system controls the expression of the wzzfepE gene involved in the O-antigen synthesis of Salmonella enterica serovar Typhimurium
    • M. M. Pescaretti, F. E. López, R. D. Morero, andM. A. Delgado, "The PmrA/PmrB regulatory system controls the expression of the wzzfepE gene involved in the O-antigen synthesis of Salmonella enterica serovar Typhimurium," Microbiology, vol. 157, no. 9, pp. 2515-2521, 2011.
    • (2011) Microbiology , vol.157 , Issue.9 , pp. 2515-2521
    • Pescaretti, M.M.1    López, F.E.2    Morero, R.D.3    Delgado, M.A.4
  • 60
    • 0029828327 scopus 로고    scopus 로고
    • Two-component regulatory systems can interact to processmultiple environmental signals
    • F. C. Soncini and E. A. Groisman, "Two-component regulatory systems can interact to processmultiple environmental signals," Journal of Bacteriology, vol. 178, no. 23, pp. 6796-6801, 1996.
    • (1996) Journal of Bacteriology , vol.178 , Issue.23 , pp. 6796-6801
    • Soncini, F.C.1    Groisman, E.A.2
  • 61
    • 14244270197 scopus 로고    scopus 로고
    • Signal-dependent binding of the response regulators PhoP and PmrA to their target promoters in vivo,"The
    • D. Shin and E. A. Groisman, "Signal-dependent binding of the response regulators PhoP and PmrA to their target promoters in vivo,"The Journal of Biological Chemistry, vol. 280, no. 6, pp. 4089-4094, 2005.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4089-4094
    • Shin, D.1    Groisman, E.A.2
  • 62
    • 0029671310 scopus 로고    scopus 로고
    • Mg2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • E. García Véscovi, F. C. Soncini, and E. A. Groisman, "Mg2+ as an extracellular signal: environmental regulation of Salmonella virulence," Cell, vol. 84, no. 1, pp. 165-174, 1996.
    • (1996) Cell , vol.84 , Issue.1 , pp. 165-174
    • García Véscovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 63
    • 4444240880 scopus 로고    scopus 로고
    • Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor
    • A. Kato and E. A. Groisman, "Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor," Genes and Development, vol. 18, no. 18, pp. 2302-2313, 2004.
    • (2004) Genes and Development , vol.18 , Issue.18 , pp. 2302-2313
    • Kato, A.1    Groisman, E.A.2
  • 64
    • 0034730333 scopus 로고    scopus 로고
    • A signal transduction systemthat responds to extracellular iron
    • M. M. S. M. Wösten, L. F. F. Kox, S. Chamnongpol, F. C. Soncini, and E. A. Groisman, "A signal transduction systemthat responds to extracellular iron," Cell, vol. 103, no. 1, pp. 113-125, 2000.
    • (2000) Cell , vol.103 , Issue.1 , pp. 113-125
    • Wösten, M.M.S.M.1    Kox, L.F.F.2    Chamnongpol, S.3    Soncini, F.C.4    Groisman, E.A.5
  • 65
    • 33845715155 scopus 로고    scopus 로고
    • Acid pH activation of the PmrA/PmrB two-component regulatory system of Salmonella enterica
    • J. C. Perez and E. A. Groisman, "Acid pH activation of the PmrA/PmrB two-component regulatory system of Salmonella enterica," Molecular Microbiology, vol. 63, no. 1, pp. 283-293, 2007.
    • (2007) Molecular Microbiology , vol.63 , Issue.1 , pp. 283-293
    • Perez, J.C.1    Groisman, E.A.2
  • 66
    • 33845458915 scopus 로고    scopus 로고
    • A positive feedback loop promotes transcription surge that jump-starts Salmonella virulence circuit
    • D. Shin, E.-J. Lee, H. Huang, and E. A. Groisman, "A positive feedback loop promotes transcription surge that jump-starts Salmonella virulence circuit," Science, vol. 314, no. 5805, pp. 1607-1609, 2006.
    • (2006) Science , vol.314 , Issue.5805 , pp. 1607-1609
    • Shin, D.1    Lee, E.-J.2    Huang, H.3    Groisman, E.A.4
  • 67
    • 84863058834 scopus 로고    scopus 로고
    • Intrinsic negative feedback governs activation surge in two-component regulatory systems
    • W.-S. Yeo, I. Zwir, H. V. Huang, D. Shin, A. Kato, and E. A. Groisman, "Intrinsic negative feedback governs activation surge in two-component regulatory systems," Molecular Cell, vol. 45, no. 3, pp. 409-421, 2012.
    • (2012) Molecular Cell , vol.45 , Issue.3 , pp. 409-421
    • Yeo, W.-S.1    Zwir, I.2    Huang, H.V.3    Shin, D.4    Kato, A.5    Groisman, E.A.6
  • 68
    • 79960309927 scopus 로고    scopus 로고
    • The pmrCAB operon mediates polymyxin resistance in Acinetobacter baumannii ATCC 17978 and clinical isolates through phosphoethanolamine modification of lipid A
    • L. A. Arroyo, C. M. Herrera, L. Fernandez, J. V. Hankins, M. S. Trent, and R. E. W. Hancock, "The pmrCAB operon mediates polymyxin resistance in Acinetobacter baumannii ATCC 17978 and clinical isolates through phosphoethanolamine modification of lipid A," Antimicrobial Agents and Chemotherapy, vol. 55, no. 8, pp. 3743-3751, 2011.
    • (2011) Antimicrobial Agents and Chemotherapy , vol.55 , Issue.8 , pp. 3743-3751
    • Arroyo, L.A.1    Herrera, C.M.2    Fernandez, L.3    Hankins, J.V.4    Trent, M.S.5    Hancock, R.E.W.6
  • 69
    • 77953523940 scopus 로고    scopus 로고
    • Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides
    • C. M. Herrera, J. V. Hankins, and M. S. Trent, "Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides," Molecular Microbiology, vol. 76, no. 6, pp. 1444-1460, 2010.
    • (2010) Molecular Microbiology , vol.76 , Issue.6 , pp. 1444-1460
    • Herrera, C.M.1    Hankins, J.V.2    Trent, M.S.3
  • 70
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • J. S. Gunn and S. I. Miller, "PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance," Journal of Bacteriology, vol. 178, no. 23, pp. 6857-6864, 1996.
    • (1996) Journal of Bacteriology , vol.178 , Issue.23 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 71
    • 0037447083 scopus 로고    scopus 로고
    • Closing the loop: The PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD
    • A. Kato, T. Latifi, and E. A. Groisman, "Closing the loop: the PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD," Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 8, pp. 4706-4711, 2003.
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.8 , pp. 4706-4711
    • Kato, A.1    Latifi, T.2    Groisman, E.A.3
  • 72
    • 0346694551 scopus 로고    scopus 로고
    • Efflux as a mechanism of resistance to antimicrobials in Pseudomonas aeruginosa and related bacteria: Unanswered questions
    • H. P. Schweizer, "Efflux as a mechanism of resistance to antimicrobials in Pseudomonas aeruginosa and related bacteria: Unanswered questions," Genetics andMolecular Research, vol. 2, no. 1, pp. 48-62, 2003.
    • (2003) Genetics AndMolecular Research , vol.2 , Issue.1 , pp. 48-62
    • Schweizer, H.P.1
  • 73
    • 40549126258 scopus 로고    scopus 로고
    • Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes
    • S. J. Pamp, M. Gjermansen, H. K. Johansen, and T. Tolker- Nielsen, "Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes," Molecular Microbiology, vol. 68, no. 1, pp. 223-240, 2008.
    • (2008) Molecular Microbiology , vol.68 , Issue.1 , pp. 223-240
    • Pamp, S.J.1    Gjermansen, M.2    Johansen, H.K.3    Tolker- Nielsen, T.4
  • 75
    • 76449106786 scopus 로고    scopus 로고
    • Different effects of transcriptional regulators MarA, SoxS and Rob on susceptibility of Escherichia coli to cationic antimicrobial peptides (CAMPs): Rob-dependent CAMP induction of the marRAB operon
    • D. M. Warner and S. B. Levy, "Different effects of transcriptional regulators MarA, SoxS and Rob on susceptibility of Escherichia coli to cationic antimicrobial peptides (CAMPs): rob-dependent CAMP induction of the marRAB operon," Microbiology, vol. 156, no. 2, pp. 570-578, 2010.
    • (2010) Microbiology , vol.156 , Issue.2 , pp. 570-578
    • Warner, D.M.1    Levy, S.B.2
  • 76
    • 0037044477 scopus 로고    scopus 로고
    • Cloning and characterization of the Burkholderia vietnamiensis norM gene encoding a multi-drug efflux protein
    • C. C. Fehlner-Gardiner and M. A. Valvano, "Cloning and characterization of the Burkholderia vietnamiensis norM gene encoding a multi-drug efflux protein," FEMS Microbiology Letters, vol. 215, no. 2, pp. 279-283, 2002.
    • (2002) FEMS Microbiology Letters , vol.215 , Issue.2 , pp. 279-283
    • Fehlner-Gardiner, C.C.1    Valvano, M.A.2
  • 77
    • 0032850479 scopus 로고    scopus 로고
    • PhoP-PhoQ homologues in Pseudomonas aeruginosa regulate expression of the outer-membrane protein OprH and polymyxin B resistance
    • E. L. A. Macfarlane, A. Kwasnicka, M. M. Ochs, and R. E. W. Hancock, "PhoP-PhoQ homologues in Pseudomonas aeruginosa regulate expression of the outer-membrane protein OprH and polymyxin B resistance,"MolecularMicrobiology, vol. 34, no. 2, pp. 305-316, 1999.
    • (1999) MolecularMicrobiology , vol.34 , Issue.2 , pp. 305-316
    • Macfarlane, E.L.A.1    Kwasnicka, A.2    Ochs, M.M.3    Hancock, R.E.W.4
  • 78
    • 0037137566 scopus 로고    scopus 로고
    • Outer membrane protein A ( OmpA ): A new pathogen-associated molecular pattern that interacts with antigen presenting cells-impact on vaccine strategies
    • P. Jeannin, G. Magistrelli, L. Goetsch et al., "Outer membrane protein A ( OmpA ): a new pathogen-associated molecular pattern that interacts with antigen presenting cells-impact on vaccine strategies," Vaccine, vol. 20, no. 4, pp.A23-A27, 2002.
    • (2002) Vaccine , vol.20 , Issue.4 , pp. A23-A27
    • Jeannin, P.1    Magistrelli, G.2    Goetsch, L.3
  • 81
    • 58949097012 scopus 로고    scopus 로고
    • Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
    • E. Llobet, J. M. Tomás, and J. A. Bengoechea, "Capsule polysaccharide is a bacterial decoy for antimicrobial peptides," Microbiology, vol. 154, no. 12, pp. 3877-3886, 2008.
    • (2008) Microbiology , vol.154 , Issue.12 , pp. 3877-3886
    • Llobet, E.1    Tomás, J.M.2    Bengoechea, J.A.3
  • 82
    • 78649650250 scopus 로고    scopus 로고
    • Colistin resistance in Acinetobacter baumannii is mediated by complete loss of lipopolysaccharide production
    • J. H. Moffatt, M. Harper, P. Harrison et al., "Colistin resistance in Acinetobacter baumannii is mediated by complete loss of lipopolysaccharide production," Antimicrobial Agents and Chemotherapy, vol. 54, no. 12, pp. 4971-4977, 2010.
    • (2010) Antimicrobial Agents and Chemotherapy , vol.54 , Issue.12 , pp. 4971-4977
    • Moffatt, J.H.1    Harper, M.2    Harrison, P.3
  • 83
    • 79956334183 scopus 로고    scopus 로고
    • Insertion sequence is Aba11 is involved in colistin resistance and loss of lipopolysaccharide in Acinetobacter baumannii
    • J. H. Moffatt, M. Harper, B. Adler, R. L. Nation, J. Li, and J. D. Boyce, "Insertion sequence IS Aba11 is involved in colistin resistance and loss of lipopolysaccharide in Acinetobacter baumannii," Antimicrobial Agents and Chemotherapy, vol. 55, no. 6, pp. 3022-3024, 2011.
    • (2011) Antimicrobial Agents and Chemotherapy , vol.55 , Issue.6 , pp. 3022-3024
    • Moffatt, J.H.1    Harper, M.2    Adler, B.3    Nation, R.L.4    Li, J.5    Boyce, J.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.