메뉴 건너뛰기




Volumn 15, Issue 4, 2004, Pages 141-152

Class C β-Lactamases: An increasing problem worldwide

Author keywords

AmpC enzymes; Inhibitors; lactamase profile

Indexed keywords

ALEFOTELAN; AMINOGLYCOSIDE ANTIBIOTIC AGENT; ANTIBIOTIC AGENT; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; BETA LACTAMASE AMPC; BETA LACTAMASE INHIBITOR; CARBAPENEM DERIVATIVE; CARBENICILLIN; CEFEPIME; CEFOTAXIME; CEFOXITIN; CEFPIROME; CEFTAZIDIME; CEPHALOSPORIN DERIVATIVE; CEPHAMYCIN DERIVATIVE; CLAVULANIC ACID; COTRIMOXAZOLE; IMIPENEM; LATAMOXEF; MEROPENEM; OXACILLIN; PIPERACILLIN; QUINOLONE DERIVATIVE; RESERPINE; SULBACTAM; TAZOBACTAM; TICARCILLIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 12244307473     PISSN: 0954139X     EISSN: None     Source Type: Journal    
DOI: 10.1097/00013542-200410000-00003     Document Type: Review
Times cited : (27)

References (105)
  • 1
    • 0020972419 scopus 로고
    • Penicillin-binding proteins and the mechanism of action of beta-lactam antibiotics
    • Waxman DJ, Strominger JL. Penicillin-binding proteins and the mechanism of action of beta-lactam antibiotics. Annu Rev Biochem 1983, 52:825-869.
    • (1983) Annu Rev Biochem , vol.52 , pp. 825-869
    • Waxman, D.J.1    Strominger, J.L.2
  • 2
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H, Vaara M. Molecular basis of bacterial outer membrane permeability. Mol Biol Rev 2003, 62:593-656.
    • (2003) Mol Biol Rev , vol.62 , pp. 593-656
    • Nikaido, H.1    Vaara, M.2
  • 3
    • 0031050613 scopus 로고    scopus 로고
    • The bacterial outer membrane as a drug barrier
    • Hancock RE. The bacterial outer membrane as a drug barrier. Trends Microbiol 1997, 5:37-42.
    • (1997) Trends Microbiol , vol.5 , pp. 37-42
    • Hancock, R.E.1
  • 4
    • 0017208308 scopus 로고
    • The beta-lactamases of gram-negative bacteria and their role in resistance to beta-lactam antibiotics
    • Sykes RB, Matthew M. The beta-lactamases of gram-negative bacteria and their role in resistance to beta-lactam antibiotics. J Antimicrob Chemother 1976, 2:115-157.
    • (1976) J Antimicrob Chemother , vol.2 , pp. 115-157
    • Sykes, R.B.1    Matthew, M.2
  • 6
    • 0029071785 scopus 로고
    • A functional classification scheme for beta-lactamases and its correlation with molecular structure
    • Bush K, Jacoby GA, Medeiros AA. A functional classification scheme for beta-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother 1995, 39:1211-1233.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 7
    • 0023461845 scopus 로고
    • Chromosomal cephalosporinases responsible for multiple resistance to newer beta-lactam antibiotics
    • Sanders CC. Chromosomal cephalosporinases responsible for multiple resistance to newer beta-lactam antibiotics. Annu Rev Microbiol 1987, 41:573-593.
    • (1987) Annu Rev Microbiol , vol.41 , pp. 573-593
    • Sanders, C.C.1
  • 8
    • 0004465830 scopus 로고
    • Observations on the nature, distribution, and significance of cephalosporinase
    • Fleming PC, Goldner M, Glass DG. Observations on the nature, distribution, and significance of cephalosporinase. Lancet 1963, 1:1399-1401.
    • (1963) Lancet , vol.1 , pp. 1399-1401
    • Fleming, P.C.1    Goldner, M.2    Glass, D.G.3
  • 9
    • 12244267566 scopus 로고
    • Inhibition of penicillinases from gram-positive and gram-negative bacteria by substrate analogues
    • Hamilton-Miller JM, Smith JT. Inhibition of penicillinases from gram-positive and gram-negative bacteria by substrate analogues. Nature 1964, 201:999-1001.
    • (1964) Nature , vol.201 , pp. 999-1001
    • Hamilton-Miller, J.M.1    Smith, J.T.2
  • 10
    • 0013850075 scopus 로고
    • Interaction of cephaloridine with penicillinase-producing gram-negative bacteria
    • Hamilton-Miller JM, Smith JT, Knox R. Interaction of cephaloridine with penicillinase-producing gram-negative bacteria. Nature 1965, 208:235-237.
    • (1965) Nature , vol.208 , pp. 235-237
    • Hamilton-Miller, J.M.1    Smith, J.T.2    Knox, R.3
  • 11
    • 0013797654 scopus 로고
    • Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea
    • Sabath LD, Jago M, Abraham EP. Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea. Biochem J 1965, 96:739-752.
    • (1965) Biochem J , vol.96 , pp. 739-752
    • Sabath, L.D.1    Jago, M.2    Abraham, E.P.3
  • 12
    • 0021633486 scopus 로고
    • Development of resistance to beta-lactam antibiotics with special reference to third-generation cephalosporins
    • Collatz E, Gutmann L, Williamson R, Acar JF. Development of resistance to beta-lactam antibiotics with special reference to third-generation cephalosporins. J Antimicrob Chemother 1984, 14(Suppl B):13-21.
    • (1984) J Antimicrob Chemother , vol.14 , Issue.SUPPL. B , pp. 13-21
    • Collatz, E.1    Gutmann, L.2    Williamson, R.3    Acar, J.F.4
  • 13
    • 0021966579 scopus 로고
    • Occurrence of cefotaxime-resistant Enterobacter during therapy of cardiac surgery patients
    • Weinstein RA. Occurrence of cefotaxime-resistant Enterobacter during therapy of cardiac surgery patients. Chemioterapia 1985, 4:110-112.
    • (1985) Chemioterapia , vol.4 , pp. 110-112
    • Weinstein, R.A.1
  • 14
    • 0022442697 scopus 로고
    • Failure of new beta-lactam antibiotics in the treatment of severe Enterobacter cloacae infections
    • Oct
    • Perronne C, Regnier B, Legrand P, Bure A, Frottier J, Vilde JL, Vachon F. Failure of new beta-lactam antibiotics in the treatment of severe Enterobacter cloacae infections. Presse Med 1986 Oct, 15:1813-1818.
    • (1986) Presse Med , vol.15 , pp. 1813-1818
    • Perronne, C.1    Regnier, B.2    Legrand, P.3    Bure, A.4    Frottier, J.5    Vilde, J.L.6    Vachon, F.7
  • 15
    • 0022576641 scopus 로고
    • An epidemic spread of multiresistant Pseudomonas aeruginosa in a cystic fibrosis centre
    • Pedersen SS, Koch C, Hoiby N, Rosendal K. An epidemic spread of multiresistant Pseudomonas aeruginosa in a cystic fibrosis centre. J Antimicrob Chemother 1986, 17:505-516.
    • (1986) J Antimicrob Chemother , vol.17 , pp. 505-516
    • Pedersen, S.S.1    Koch, C.2    Hoiby, N.3    Rosendal, K.4
  • 16
    • 0022468220 scopus 로고
    • Derepressed beta-lactamase synthesis in strains of Pseudomonas aeruginosa isolated from patients with cystic fibrosis
    • Nichols WW, Milne LM. Derepressed beta-lactamase synthesis in strains of Pseudomonas aeruginosa isolated from patients with cystic fibrosis. J Antimicrob Chemother 1986, 18:549-550.
    • (1986) J Antimicrob Chemother , vol.18 , pp. 549-550
    • Nichols, W.W.1    Milne, L.M.2
  • 17
    • 0021825443 scopus 로고
    • Gram-negative bacilli resistant to third-generation cephalosporins: Beta-lactamase characterization and susceptibility to Sch 34343
    • Medeiros AA, Hare R, Papa E, Adam C, Miller GH. Gram-negative bacilli resistant to third-generation cephalosporins: beta-lactamase characterization and susceptibility to Sch 34343. J Antimicrob Chemother 1985, 15 Suppl C:119-132.
    • (1985) J Antimicrob Chemother , vol.15 , Issue.100 SUPPL. , pp. 119-132
    • Medeiros, A.A.1    Hare, R.2    Papa, E.3    Adam, C.4    Miller, G.H.5
  • 18
    • 0028017953 scopus 로고
    • Origin and impact of plasmid-mediated extended-spectrum beta-lactamases
    • Philippon A, Arlet G, Lagrange PH. Origin and impact of plasmid-mediated extended-spectrum beta-lactamases. Eur J Clin Microbiol Infect Dis 1994, 13 (Suppl 1):S17-S29.
    • (1994) Eur J Clin Microbiol Infect Dis , vol.13 , Issue.1 SUPPL.
    • Philippon, A.1    Arlet, G.2    Lagrange, P.H.3
  • 19
    • 0028883511 scopus 로고
    • Beta-Lactamases in laboratory and clinical resistance
    • Livermore DM. Beta-Lactamases in laboratory and clinical resistance. Clin Microbiol Rev 1995, 8:557-584.
    • (1995) Clin Microbiol Rev , vol.8 , pp. 557-584
    • Livermore, D.M.1
  • 20
    • 0017227763 scopus 로고
    • Plasmid-determined beta-lactamase indistinguishable from the chromosomal beta-lactamase of Escherichia coli
    • Bobrowski MM, Matthew M, Barth PT, Datta N, Grinter NJ, Jacob AE, et al. Plasmid-determined beta-lactamase indistinguishable from the chromosomal beta-lactamase of Escherichia coli. J Bacteriol 1976, 125:149-157.
    • (1976) J Bacteriol , vol.125 , pp. 149-157
    • Bobrowski, M.M.1    Matthew, M.2    Barth, P.T.3    Datta, N.4    Grinter, N.J.5    Jacob, A.E.6
  • 21
    • 0020040508 scopus 로고
    • A plasmid-mediated cephalosporinase from Achromobacter species
    • Levesque R, Roy PH, Letarte R, Pechere JC. A plasmid-mediated cephalosporinase from Achromobacter species. J Infect Dis 1982, 145:753-761.
    • (1982) J Infect Dis , vol.145 , pp. 753-761
    • Levesque, R.1    Roy, P.H.2    Letarte, R.3    Pechere, J.C.4
  • 22
    • 0032450190 scopus 로고    scopus 로고
    • Plasmid-encoded AmpC beta-lactamases: How far have we gone 10 years after the discovery?
    • Bauernfeind A, Chong Y, Lee K. Plasmid-encoded AmpC beta-lactamases: how far have we gone 10 years after the discovery? Yonsei Med J 1998, 39:520-525.
    • (1998) Yonsei Med J , vol.39 , pp. 520-525
    • Bauernfeind, A.1    Chong, Y.2    Lee, K.3
  • 23
    • 0025170055 scopus 로고
    • Novel plasmid-mediated beta-lactamase (MIR-1) conferring resistance to oxyimino- And alpha-methoxy beta-lactams in clinical isolates of Klebsiella pneumomae
    • Papanicolaou GA, Medeiros AA, Jacoby GA. Novel plasmid-mediated beta-lactamase (MIR-1) conferring resistance to oxyimino- and alpha-methoxy beta-lactams in clinical isolates of Klebsiella pneumomae. Antimicrob Agents Chemotner 1990, 34:2200-2209.
    • (1990) Antimicrob Agents Chemotner , vol.34 , pp. 2200-2209
    • Papanicolaou, G.A.1    Medeiros, A.A.2    Jacoby, G.A.3
  • 25
    • 0000623780 scopus 로고
    • Regulatory components in Citrobacter freundii ampC beta-lactamase induction
    • Lindberg F, Westman L, Normark S. Regulatory components in Citrobacter freundii ampC beta-lactamase induction. Proc Natl Acad Sci USA 1985, 82:4620-4624.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4620-4624
    • Lindberg, F.1    Westman, L.2    Normark, S.3
  • 26
    • 0036784084 scopus 로고    scopus 로고
    • -11 Mutation in the ampC promoter increasing resistance to beta-lactams in a clinical Escherichia coli strain
    • Corvec S, Caroff N, Espaze E, Marraillac J, Reynaud A. -11 Mutation in the ampC promoter increasing resistance to beta-lactams in a clinical Escherichia coli strain. Antimicrob Agents Chemother 2002, 46:3265-3267.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3265-3267
    • Corvec, S.1    Caroff, N.2    Espaze, E.3    Marraillac, J.4    Reynaud, A.5
  • 27
    • 0034129458 scopus 로고    scopus 로고
    • Analysis of the effects of -42 and -32 ampC promoter mutations in clinical isolates of Escherichia coli hyperproducing ampC
    • Caroff N, Espaze E, Gautreau D, Richet H, Reynaud A. Analysis of the effects of -42 and -32 ampC promoter mutations in clinical isolates of Escherichia coli hyperproducing ampC. J Antimicrob Chemother 2000, 45:783-788.
    • (2000) J Antimicrob Chemother , vol.45 , pp. 783-788
    • Caroff, N.1    Espaze, E.2    Gautreau, D.3    Richet, H.4    Reynaud, A.5
  • 28
    • 0019425938 scopus 로고
    • The E. coli beta-lactamase attenuator mediates growth rate-dependent regulation
    • Jaurin B, Grundstrom T, Edlund T, Normark S. The E. coli beta-lactamase attenuator mediates growth rate-dependent regulation. Nature 1981, 290:221-225.
    • (1981) Nature , vol.290 , pp. 221-225
    • Jaurin, B.1    Grundstrom, T.2    Edlund, T.3    Normark, S.4
  • 29
    • 0038338397 scopus 로고    scopus 로고
    • High-level expression of ampC beta-lactamase due to insertion of nucleotides between -10 and -35 promoter sequences in Escherichia coli clinical isolates: Cases not responsive to extended-spectrum-cephalosporin treatment
    • Siu LK, Lu PL, Chen JY, Lin FM, Chang SC. High-level expression of ampC beta-lactamase due to insertion of nucleotides between -10 and -35 promoter sequences in Escherichia coli clinical isolates: cases not responsive to extended-spectrum-cephalosporin treatment. Antimicrob Agents Chemother 2003, 47:2138-2144.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2138-2144
    • Siu, L.K.1    Lu, P.L.2    Chen, J.Y.3    Lin, F.M.4    Chang, S.C.5
  • 31
    • 0942290551 scopus 로고    scopus 로고
    • Genetic environment and transcription of ampC in an Acinetobacter baumannii clinical isolate
    • Segal H, Nelson EC, Elisha BG. Genetic environment and transcription of ampC in an Acinetobacter baumannii clinical isolate. Antimicrob Agents Chemother 2004, 48:612-614.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 612-614
    • Segal, H.1    Nelson, E.C.2    Elisha, B.G.3
  • 32
    • 0021881891 scopus 로고
    • Recycling of murein by Escherichia coli
    • Goodell EW. Recycling of murein by Escherichia coli. J Bacteriol 1985, 163:305-310.
    • (1985) J Bacteriol , vol.163 , pp. 305-310
    • Goodell, E.W.1
  • 33
    • 0032700851 scopus 로고    scopus 로고
    • Regulation of inducible AmpC beta-lactamase expression among Enterobacteriaceae
    • Review
    • Hanson ND, Sanders CC. Regulation of inducible AmpC beta-lactamase expression among Enterobacteriaceae. Curr Pharm Des 1999, 5:881 -894. Review.
    • (1999) Curr Pharm Des , vol.5 , pp. 881-894
    • Hanson, N.D.1    Sanders, C.C.2
  • 34
    • 0024712562 scopus 로고
    • Signalling proteins in enterobacterial AmpC beta-lactamase regulation
    • Lindquist S, Galleni M, Lindberg F, Normark S. Signalling proteins in enterobacterial AmpC beta-lactamase regulation. Mol Microbiol 1989, 3:1091-1102.
    • (1989) Mol Microbiol , vol.3 , pp. 1091-1102
    • Lindquist, S.1    Galleni, M.2    Lindberg, F.3    Normark, S.4
  • 35
    • 0030802782 scopus 로고    scopus 로고
    • The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide
    • Dietz H, Pfeifle D, Wiedemann B. The signal molecule for beta-lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide. Antimicrob Agents Chemother 1997, 41:2113-2120.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2113-2120
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 36
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction
    • Jacobs C, Huang LJ, Bartowsky E, Normark S, Park JT. Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta-lactamase induction. EMBO J 1994, 13:4684-4694.
    • (1994) EMBO J , vol.13 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.J.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 37
    • 0023583815 scopus 로고
    • Clinical significance of beta-lactamase induction and stable derepression in gram-negative rods
    • Livermore DM. Clinical significance of beta-lactamase induction and stable derepression in gram-negative rods. Eur J Clin Microbiol 1987, 6:439-445.
    • (1987) Eur J Clin Microbiol , vol.6 , pp. 439-445
    • Livermore, D.M.1
  • 38
    • 0027513336 scopus 로고
    • Molecular basis of beta-lactamase induction in bacteria
    • Bennett PM, Chopra I. Molecular basis of beta-lactamase induction in bacteria. Antimicrob Agents Chemother 1993, 37:153-158.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 153-158
    • Bennett, P.M.1    Chopra, I.2
  • 39
    • 0023216969 scopus 로고
    • Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii beta-lactamase
    • Lindberg F, Lindquist S, Normark S. Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii beta-lactamase. J Bacteriol 1987, 169:1923-1928.
    • (1987) J Bacteriol , vol.169 , pp. 1923-1928
    • Lindberg, F.1    Lindquist, S.2    Normark, S.3
  • 40
    • 0031800337 scopus 로고    scopus 로고
    • Important and emerging beta-lactamase-mediated resistances in hospital-based pathogens: The Amp C enzymes
    • Jones RN. Important and emerging beta-lactamase-mediated resistances in hospital-based pathogens: the Amp C enzymes. Diagn Microbiol Infect Dis 1998, 31:461-466.
    • (1998) Diagn Microbiol Infect Dis , vol.31 , pp. 461-466
    • Jones, R.N.1
  • 43
    • 25544461564 scopus 로고
    • Trends in antibiotic utilization and bacterial resistance. Report of the National Nosocomial Resistance Surveillance Group
    • Ballow CH, Schentag JJ. Trends in antibiotic utilization and bacterial resistance. Report of the National Nosocomial Resistance Surveillance Group. Diagn Microbiol Infect Dis 1992, 15(2 Suppl):37S-42S.
    • (1992) Diagn Microbiol Infect Dis , vol.15 , Issue.2 SUPPL.
    • Ballow, C.H.1    Schentag, J.J.2
  • 44
    • 0031746493 scopus 로고    scopus 로고
    • Empiric therapy of bacterial infections in patients with severe neutropenia
    • Glauser M. Empiric therapy of bacterial infections in patients with severe neutropenia. Diagn Microbiol Infect Dis 1998, 31:467-472.
    • (1998) Diagn Microbiol Infect Dis , vol.31 , pp. 467-472
    • Glauser, M.1
  • 47
    • 0035032105 scopus 로고    scopus 로고
    • Controversies about extended-spectrum and AmpC beta-lactamases
    • Thomson KS. Controversies about extended-spectrum and AmpC beta-lactamases. Emerg Infect Dis 2001, 7:333-336.
    • (2001) Emerg Infect Dis , vol.7 , pp. 333-336
    • Thomson, K.S.1
  • 48
    • 0345085531 scopus 로고    scopus 로고
    • Rare case of failure by an automated system to detect extended-spectrum beta-lactamase in a cephalosporin-resistant Klebsiella pneumoniae isolate
    • Tzouvelekis LS, Vatopoulos AC, Katsanis G, Tzelepi E. Rare case of failure by an automated system to detect extended-spectrum beta-lactamase in a cephalosporin-resistant Klebsiella pneumoniae isolate. J Clin Microbiol 1999, 37:2388.
    • (1999) J Clin Microbiol , vol.37 , pp. 2388
    • Tzouvelekis, L.S.1    Vatopoulos, A.C.2    Katsanis, G.3    Tzelepi, E.4
  • 49
    • 0033063978 scopus 로고    scopus 로고
    • Use of microdilution panels with and without beta-lactamase inhibitors as a phenotypic test for beta-lactamase production among Escherichia coli. Klebsiella spp., Enterobacter spp., Citrobacter freundii, and Serratia marcescens
    • Thomson KS, Sanders CC, Moland ES. Use of microdilution panels with and without beta-lactamase inhibitors as a phenotypic test for beta-lactamase production among Escherichia coli. Klebsiella spp., Enterobacter spp., Citrobacter freundii, and Serratia marcescens. Antimicrob Agents Chemother 1999, 43:1393-400.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1393-1400
    • Thomson, K.S.1    Sanders, C.C.2    Moland, E.S.3
  • 50
    • 85039475352 scopus 로고    scopus 로고
    • Cefotetan (CTT)-Cloxacillin (CLX) synergy test for differentiation of Klebsiella pneumoniae (Kp) producing plasmid-mediated AmpC-Type β-lactamase(pACBL+) from strains producing extended-spectrum β-lactamases and deficient in porins (ESBL+/POR-)
    • abstr. D-207. Chicago, September, abstracts 168
    • Conejo MC, Van der Hooft M, Fernández-Cuenca F, Pascual A, Martinez-Martinez L. Cefotetan (CTT)-Cloxacillin (CLX) synergy test for differentiation of Klebsiella pneumoniae (Kp) producing plasmid-mediated AmpC-Type β-lactamase(pACBL+) from strains producing extended-spectrum β-lactamases and deficient in porins (ESBL+/POR-), abstr. D-207. 43th Interscience Conference on Antimicrobial Agents and Chemotherapy. Chicago, September 2003 [abstracts 168].
    • (2003) 43th Interscience Conference on Antimicrobial Agents and Chemotherapy
    • Conejo, M.C.1    Van Der Hooft, M.2    Fernández-Cuenca, F.3    Pascual, A.4    Martinez-Martinez, L.5
  • 51
    • 2442532987 scopus 로고    scopus 로고
    • Use of beta-lactamase inhibitors in disk tests to detect plasmid-mediated AmpC beta-lactamases
    • Black JA, Thomson KS, Pitout JD. Use of beta-lactamase inhibitors in disk tests to detect plasmid-mediated AmpC beta-lactamases. J Clin Microbiol 2004, 42:2203-2206.
    • (2004) J Clin Microbiol , vol.42 , pp. 2203-2206
    • Black, J.A.1    Thomson, K.S.2    Pitout, J.D.3
  • 52
    • 0024446886 scopus 로고
    • Interactions of meropenem with class I chromosomal beta-lactamases
    • Yang YJ, Livermore DM. Interactions of meropenem with class I chromosomal beta-lactamases. J Antimicrob Chemother 1989, 24 (Suppl A):207-217.
    • (1989) J Antimicrob Chemother , vol.24 , Issue.SUPPL. A , pp. 207-217
    • Yang, Y.J.1    Livermore, D.M.2
  • 53
  • 54
    • 0025257149 scopus 로고
    • Interactions of tazobactam and clavulanate with inducibly- And constitutively-expressed Class I beta-lactamases
    • Akova M, Yang Y, Livermore DM. Interactions of tazobactam and clavulanate with inducibly- and constitutively-expressed Class I beta-lactamases. J Antimicrob Chemother 1990, 25:199-208.
    • (1990) J Antimicrob Chemother , vol.25 , pp. 199-208
    • Akova, M.1    Yang, Y.2    Livermore, D.M.3
  • 55
    • 0035838468 scopus 로고    scopus 로고
    • Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site
    • Trehan I, Beadle BM, Shoichet BK. Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site. Biochemistry 2001, 40:7992-7999.
    • (2001) Biochemistry , vol.40 , pp. 7992-7999
    • Trehan, I.1    Beadle, B.M.2    Shoichet, B.K.3
  • 56
    • 0036894235 scopus 로고    scopus 로고
    • Structural basis for imipenem inhibition of class C beta-lactamases
    • Beadle BM, Shoichet BK. Structural basis for imipenem inhibition of class C beta-lactamases. Antimicrob Agents Chemother 2002, 46:3978-3980.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3978-3980
    • Beadle, B.M.1    Shoichet, B.K.2
  • 57
    • 0025331847 scopus 로고
    • Characteristics of aztreonam as a substrate, inhibitor and inducer for beta-lactamases
    • Sakurai Y, Yoshida Y, Saitoh K, Nemoto M, Yamaguchi A, Sawai T. Characteristics of aztreonam as a substrate, inhibitor and inducer for beta-lactamases. J Antibiot 1990, 43:403-410.
    • (1990) J Antibiot , vol.43 , pp. 403-410
    • Sakurai, Y.1    Yoshida, Y.2    Saitoh, K.3    Nemoto, M.4    Yamaguchi, A.5    Sawai, T.6
  • 58
    • 0031952858 scopus 로고    scopus 로고
    • Beta-lactamase inhibitors are substrates for the multidrug efflux pumps of Pseudomonas aeruginosa
    • Li XZ, Zhang L, Srikumar R, Poole K. Beta-lactamase inhibitors are substrates for the multidrug efflux pumps of Pseudomonas aeruginosa. Antimicrob Agents Chemother 1998, 42:399-403.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 399-403
    • Li, X.Z.1    Zhang, L.2    Srikumar, R.3    Poole, K.4
  • 59
    • 3843112285 scopus 로고    scopus 로고
    • In vivo acquisition of high-level resistance to imipenem in Escherichla coli
    • Poirel L, Heritier C, Spicq C, Nordmann P. In vivo acquisition of high-level resistance to imipenem in Escherichla coli. J Clin Microbiol 2004, 42:3831-3833.
    • (2004) J Clin Microbiol , vol.42 , pp. 3831-3833
    • Poirel, L.1    Heritier, C.2    Spicq, C.3    Nordmann, P.4
  • 61
    • 0030762264 scopus 로고    scopus 로고
    • Potentiation of beta-lactams against Pseudomonas aeruginosa strains by Ro 48-1256, a bridged monobactam inhibitor of AmpC beta-lactamases
    • Livermore DM, Chen HY. Potentiation of beta-lactams against Pseudomonas aeruginosa strains by Ro 48-1256, a bridged monobactam inhibitor of AmpC beta-lactamases. J Antimicrob Chemother 1997, 40:335-343.
    • (1997) J Antimicrob Chemother , vol.40 , pp. 335-343
    • Livermore, D.M.1    Chen, H.Y.2
  • 63
    • 0033983990 scopus 로고    scopus 로고
    • Effect of conalbumin on the activity of Syn 2190, a 1,5 dihydroxy-4-pyridon monobactam inhibitor of AmpC beta-lactamases
    • Babini GS, Livermore DM. Effect of conalbumin on the activity of Syn 2190, a 1,5 dihydroxy-4-pyridon monobactam inhibitor of AmpC beta-lactamases. J Antimicrob Chemother 2000, 45:105-109.
    • (2000) J Antimicrob Chemother , vol.45 , pp. 105-109
    • Babini, G.S.1    Livermore, D.M.2
  • 64
    • 0025219010 scopus 로고
    • Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechols: Study with beta-lactam antibiotics containing catechol and analogous groups
    • Nikaido H, Rosenberg EY. Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechols: study with beta-lactam antibiotics containing catechol and analogous groups. J Bacteriol 1990, 172:1361-1367.
    • (1990) J Bacteriol , vol.172 , pp. 1361-1367
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 65
    • 0036668119 scopus 로고    scopus 로고
    • Distribution of beta-lactamases in Acinetobacter baumannii clinical isolates and the effect of Syn 2190 (AmpC inhibitor) on the MICs of different beta-lactam antibiotics
    • Danes C, Navia MM, Ruiz J, Marco F, Jurado A, Jimenez de Anta MT, et al. Distribution of beta-lactamases in Acinetobacter baumannii clinical isolates and the effect of Syn 2190 (AmpC inhibitor) on the MICs of different beta-lactam antibiotics. J Antimicrob Chemother 2002, 50:261-264.
    • (2002) J Antimicrob Chemother , vol.50 , pp. 261-264
    • Danes, C.1    Navia, M.M.2    Ruiz, J.3    Marco, F.4    Jurado, A.5    Jimenez De Anta, M.T.6
  • 66
    • 0029795726 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of 2 beta-alkenyl penam sulfone acids as inhibitors of beta-lactamases
    • Richter HG, Angehrn P, Hubschwerlen C, Kania M, Page MG, Specklin JL, et al. Design, synthesis, and evaluation of 2 beta-alkenyl penam sulfone acids as inhibitors of beta-lactamases. J Med Chem 1996, 39:3712-3722.
    • (1996) J Med Chem , vol.39 , pp. 3712-3722
    • Richter, H.G.1    Angehrn, P.2    Hubschwerlen, C.3    Kania, M.4    Page, M.G.5    Specklin, J.L.6
  • 67
    • 0034194737 scopus 로고    scopus 로고
    • The synthesis and evaluation of 2-substituted-7-(alkylidene)cephalosporin sulfones as beta-lactamase inhibitors
    • Buynak JD, Doppalapudi VR, Rao AS, Nidamarthy SD, Adam G. The synthesis and evaluation of 2-substituted-7-(alkylidene)cephalosporin sulfones as beta-lactamase inhibitors. Bioorg Med Chem Lett 2000, 10:847-851.
    • (2000) Bioorg Med Chem Lett , vol.10 , pp. 847-851
    • Buynak, J.D.1    Doppalapudi, V.R.2    Rao, A.S.3    Nidamarthy, S.D.4    Adam, G.5
  • 70
    • 0033526062 scopus 로고    scopus 로고
    • 6-(1-Hydroxyalkyl)penam sulfone derivatives as inhibitors of class a and class C beta-lactamases I
    • Bitha P, Li Z, Francisco GD, Rasmussen BA, Lin YI. 6-(1-Hydroxyalkyl) penam sulfone derivatives as inhibitors of class A and class C beta-lactamases I. Bioorg Med Chem Lett 1999, 9:991-996.
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 991-996
    • Bitha, P.1    Li, Z.2    Francisco, G.D.3    Rasmussen, B.A.4    Lin, Y.I.5
  • 71
    • 0027246168 scopus 로고
    • Activity of the beta-lactamase inhibitor BRL 42715 against cephalosporinases produced by Enterobacteriaceae
    • Zhou XY, Kitzis MD, Acar JF, Gutmann L. Activity of the beta-lactamase inhibitor BRL 42715 against cephalosporinases produced by Enterobacteriaceae. J Antimicrob Chemother 1993, 31:473-480.
    • (1993) J Antimicrob Chemother , vol.31 , pp. 473-480
    • Zhou, X.Y.1    Kitzis, M.D.2    Acar, J.F.3    Gutmann, L.4
  • 72
    • 0027515337 scopus 로고
    • In-vitro evaluation of the four beta-lactamase inhibitors: BRL42715, clavulanic acid, sulbactam, and tazobactam
    • Muratani T, Yokota E, Nakane T, Inoue E, Mitsuhashi S. In-vitro evaluation of the four beta-lactamase inhibitors: BRL42715, clavulanic acid, sulbactam, and tazobactam. J Antimicrob Chemother 1993, 32:421-429.
    • (1993) J Antimicrob Chemother , vol.32 , pp. 421-429
    • Muratani, T.1    Yokota, E.2    Nakane, T.3    Inoue, E.4    Mitsuhashi, S.5
  • 73
    • 0027196080 scopus 로고
    • Role of cephalosporinase in carbapenem resistance of clinical isolates of Pseudomonas aeruginosa
    • Zhou XY, Kitzis MD, Gutmann L. Role of cephalosporinase in carbapenem resistance of clinical isolates of Pseudomonas aeruginosa. Antimicrob Agents Chemother 1993, 37:1387-1389.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 1387-1389
    • Zhou, X.Y.1    Kitzis, M.D.2    Gutmann, L.3
  • 74
    • 0029022565 scopus 로고
    • Outer membrane permeability of beta-lactamase inhibitors in Pseudomonas aeruginosa
    • Satake S, Nakae T. Outer membrane permeability of beta-lactamase inhibitors in Pseudomonas aeruginosa. FEMS Microbiol Lett 1995, 129:251-254.
    • (1995) FEMS Microbiol Lett , vol.129 , pp. 251-254
    • Satake, S.1    Nakae, T.2
  • 75
    • 0031952858 scopus 로고    scopus 로고
    • Beta-lactamase inhibitors are substrates for the multidrug efflux pumps of Pseudomonas aeruginosa
    • Li XZ, Zhang L, Srikumar R, Poole K. Beta-lactamase inhibitors are substrates for the multidrug efflux pumps of Pseudomonas aeruginosa. Antimicrob Agents Chemother 1998, 42:399-403.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 399-403
    • Li, X.Z.1    Zhang, L.2    Srikumar, R.3    Poole, K.4
  • 76
    • 0345102428 scopus 로고    scopus 로고
    • The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase
    • Powers RA, Blazquez J, Weston GS, Morosini MI, Baquero F, Shoichet BK. The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase. Protein Sci 1999, 8:2330-2337.
    • (1999) Protein Sci , vol.8 , pp. 2330-2337
    • Powers, R.A.1    Blazquez, J.2    Weston, G.S.3    Morosini, M.I.4    Baquero, F.5    Shoichet, B.K.6
  • 77
    • 0032487847 scopus 로고    scopus 로고
    • Structure-based enhancement of boronic acid-based inhibitors of AmpC beta-lactamase
    • Weston GS, Blazquez J, Baquero F, Shoichet BK. Structure-based enhancement of boronic acid-based inhibitors of AmpC beta-lactamase. J Med Chem 1998, 41:4577-86.
    • (1998) J Med Chem , vol.41 , pp. 4577-4586
    • Weston, G.S.1    Blazquez, J.2    Baquero, F.3    Shoichet, B.K.4
  • 80
    • 12244302743 scopus 로고    scopus 로고
    • Bacterial resistance to β-lactam antibiotics and β-lactam inhibitors of β-lactamases
    • Oreste A. Mascaretti (ed). Washington DC: ASM Press
    • Mascaretti, AO. Bacterial resistance to β-lactam antibiotics and β-lactam inhibitors of β-lactamases, p. 171-198. In Oreste A. Mascaretti (ed). Bacterial Versus Antibacterial Agents. An Integrated Approach. Washington DC: ASM Press, 2003.
    • (2003) Bacterial Versus Antibacterial Agents. An Integrated Approach , pp. 171-198
    • Mascaretti, A.O.1
  • 81
    • 0035180098 scopus 로고    scopus 로고
    • Binding properties of a peptide derived from beta-lactamase inhibitory protein
    • Rudgers GW, Huang W, Palzkill T. Binding properties of a peptide derived from beta-lactamase inhibitory protein. Antimicrob Agents Chemother 2001, 45:3279-3286.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 3279-3286
    • Rudgers, G.W.1    Huang, W.2    Palzkill, T.3
  • 82
    • 0034974174 scopus 로고    scopus 로고
    • Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase
    • Tondi D, Powers RA, Caselli E, Negri MC, Blazquez J, Costi MP, et al. Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase. Chem Biol 2001, 8:593-611.
    • (2001) Chem Biol , vol.8 , pp. 593-611
    • Tondi, D.1    Powers, R.A.2    Caselli, E.3    Negri, M.C.4    Blazquez, J.5    Costi, M.P.6
  • 83
    • 0031973490 scopus 로고    scopus 로고
    • Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases
    • Massova I, Mobashery S. Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases. Antimicrob Agents Chemother 1998, 42:1-17.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 1-17
    • Massova, I.1    Mobashery, S.2
  • 84
    • 0029019031 scopus 로고
    • Beta-lactamases and bacterial resistance to antibiotics
    • Frere JM. Beta-lactamases and bacterial resistance to antibiotics. Mol Microbiol 1995, 16:385-395.
    • (1995) Mol Microbiol , vol.16 , pp. 385-395
    • Frere, J.M.1
  • 85
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • Lobkovsky E, Moews PC, Liu H, Zhao H, Frere JM, Knox JR. Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc Natl Acad Sci USA 1993, 90:11257-11261.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1    Moews, P.C.2    Liu, H.3    Zhao, H.4    Frere, J.M.5    Knox, J.R.6
  • 86
    • 0029817551 scopus 로고    scopus 로고
    • The roles of residues Tyr150, Glu272, and His314 in class C beta-lactamases
    • Dubus A, Ledent P, Lamotte-Brasseur J, Frere JM. The roles of residues Tyr150, Glu272, and His314 in class C beta-lactamases. Proteins 1996, 25:473-485.
    • (1996) Proteins , vol.25 , pp. 473-485
    • Dubus, A.1    Ledent, P.2    Lamotte-Brasseur, J.3    Frere, J.M.4
  • 87
    • 0025022490 scopus 로고
    • Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis
    • Oefner C, D'Arcy A, Daly JJ, Gubernator K, Charnas RL, Heinze I, et al. Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis. Nature 1990, 18:284-288.
    • (1990) Nature , vol.18 , pp. 284-288
    • Oefner, C.1    D'Arcy, A.2    Daly, J.J.3    Gubernator, K.4    Charnas, R.L.5    Heinze, I.6
  • 88
    • 0027978868 scopus 로고
    • The role of tyrosine 150 in catalysis of beta-lactam hydrolysis by AmpC beta-lactamase from Escherichia coli investigated by site-directed mutagenesis
    • Dubus A, Normark S, Kania M, Page MG. The role of tyrosine 150 in catalysis of beta-lactam hydrolysis by AmpC beta-lactamase from Escherichia coli investigated by site-directed mutagenesis. Biochemistry 1994, 33:8577-8586.
    • (1994) Biochemistry , vol.33 , pp. 8577-8586
    • Dubus, A.1    Normark, S.2    Kania, M.3    Page, M.G.4
  • 89
    • 0025027315 scopus 로고
    • Function of the conserved triad residues in the class C beta-lactamase from Citrobacter freundii GN346
    • Tsukamoto K, Nishida N, Tsuruoka M, Sawai T. Function of the conserved triad residues in the class C beta-lactamase from Citrobacter freundii GN346. FEBS Lett 1990, 271:243-246.
    • (1990) FEBS Lett , vol.271 , pp. 243-246
    • Tsukamoto, K.1    Nishida, N.2    Tsuruoka, M.3    Sawai, T.4
  • 90
    • 0037094114 scopus 로고    scopus 로고
    • An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation
    • Minasov G, Wang X, Shoichet BK. An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation. J Am Chem Soc 2002, 124:5333-5340.
    • (2002) J Am Chem Soc , vol.124 , pp. 5333-5340
    • Minasov, G.1    Wang, X.2    Shoichet, B.K.3
  • 91
    • 0027429923 scopus 로고
    • A survey of a functional amino acid of class C beta-lactamase corresponding to Glu166 of class A beta-lactamases
    • Nukaga M, Tanimoto K, Tsukamoto K, Imajo S, Ishiguro M, Sawai T. A survey of a functional amino acid of class C beta-lactamase corresponding to Glu166 of class A beta-lactamases. FEBS Lett 1993, 332:93-98.
    • (1993) FEBS Lett , vol.332 , pp. 93-98
    • Nukaga, M.1    Tanimoto, K.2    Tsukamoto, K.3    Imajo, S.4    Ishiguro, M.5    Sawai, T.6
  • 93
    • 0035824615 scopus 로고    scopus 로고
    • Amino acid sequence determinants of extended spectrum cephalosporin hydrolysis by the class C P99 beta-lactamase
    • Zhang Z, Yu Y, Musser JM, Palzkill T. Amino acid sequence determinants of extended spectrum cephalosporin hydrolysis by the class C P99 beta-lactamase. J Biol Chem 2001, 276:46568-46574.
    • (2001) J Biol Chem , vol.276 , pp. 46568-46574
    • Zhang, Z.1    Yu, Y.2    Musser, J.M.3    Palzkill, T.4
  • 94
    • 0034927827 scopus 로고    scopus 로고
    • Mutation in Serratia marcescens AmpC beta-lactamase producing high-level resistance to ceftazidime and cefpirome
    • Raimondi A, Sisto F, Nikaido H. Mutation in Serratia marcescens AmpC beta-lactamase producing high-level resistance to ceftazidime and cefpirome. Antimicrob Agents Chemother 2001, 45:2331-2339.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 2331-2339
    • Raimondi, A.1    Sisto, F.2    Nikaido, H.3
  • 95
    • 0035916405 scopus 로고    scopus 로고
    • Extension of resistance to cefepime and cefpirome associated to a six amino acid deletion in the H-10 helix of the cephalosporinase of an Enterobacter cloacae clinical isolate
    • Barnaud G, Labia R, Raskine L, Sanson-Le Pors MJ, Philippon A, Arlet G. Extension of resistance to cefepime and cefpirome associated to a six amino acid deletion in the H-10 helix of the cephalosporinase of an Enterobacter cloacae clinical isolate. FEMS Microbiol Lett 2001, 20:185-190.
    • (2001) FEMS Microbiol Lett , vol.20 , pp. 185-190
    • Barnaud, G.1    Labia, R.2    Raskine, L.3    Sanson-Le Pors, M.J.4    Philippon, A.5    Arlet, G.6
  • 96
    • 0038192438 scopus 로고    scopus 로고
    • Experimental prediction of the evolution of cefepime resistance from the CMY-2 AmpC beta-lactamase
    • Barlow M, Hall BG. Experimental prediction of the evolution of cefepime resistance from the CMY-2 AmpC beta-lactamase. Genetics 2003, 164:23-29.
    • (2003) Genetics , vol.164 , pp. 23-29
    • Barlow, M.1    Hall, B.G.2
  • 97
    • 1442275596 scopus 로고    scopus 로고
    • Selection during cefepime treatment of a new cephalosporinase variant with extended-spectrum resistance to cefepime in an Enterobacter aerogenes clinical isolate
    • Barnaud G, Benzerara Y, Gravisse J, Raskine L, Sanson-Le Pors MJ, Labia R, et al. Selection during cefepime treatment of a new cephalosporinase variant with extended-spectrum resistance to cefepime in an Enterobacter aerogenes clinical isolate. Antimicrob Agents Chemother 2004, 48:1040-1042.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 1040-1042
    • Barnaud, G.1    Benzerara, Y.2    Gravisse, J.3    Raskine, L.4    Sanson-Le Pors, M.J.5    Labia, R.6
  • 99
    • 1442275742 scopus 로고    scopus 로고
    • Resistance to cefepime and cefpirome due to a 4-amino-acid deletion in the chromosome-encoded AmpC beta-lactamase of a Serratia marcescens clinical isolate
    • Mammeri H, Poirel L, Bemer P, Drugeon H, Nordmann P. Resistance to cefepime and cefpirome due to a 4-amino-acid deletion in the chromosome-encoded AmpC beta-lactamase of a Serratia marcescens clinical isolate. Antimicrob Agents Chemother 2004, 48:716-720.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 716-720
    • Mammeri, H.1    Poirel, L.2    Bemer, P.3    Drugeon, H.4    Nordmann, P.5
  • 100
    • 3042677882 scopus 로고    scopus 로고
    • Inhibitor-sensitive AmpC beta-lactamase variant produced by an Escherichia coli clinical isolate resistant to oxyiminocephalosporins and cephamycins
    • Doi Y, Wachino J, Ishiguro M, Kurokawa H, Yamane K, Shibata N, et al. Inhibitor-sensitive AmpC beta-lactamase variant produced by an Escherichia coli clinical isolate resistant to oxyiminocephalosporins and cephamycins. Antimicrob Agents Chemother 2004, 48:2652-2658.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 2652-2658
    • Doi, Y.1    Wachino, J.2    Ishiguro, M.3    Kurokawa, H.4    Yamane, K.5    Shibata, N.6
  • 101
    • 0027966926 scopus 로고
    • Gene sequence and biochemical characterization of FOX-1 from Klebsiella pneumoniae, a new AmpC-type plasmid-mediated beta-lactamase with two molecular variants
    • Gonzalez Leiza M, Perez-Diaz JC, Ayala J, Casellas JM, Martinez-Beltran J, Bush K, et al. Gene sequence and biochemical characterization of FOX-1 from Klebsiella pneumoniae, a new AmpC-type plasmid-mediated beta-lactamase with two molecular variants. Antimicrob Agents Chemother 1994, 38:2150-2157.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 2150-2157
    • Gonzalez Leiza, M.1    Perez-Diaz, J.C.2    Ayala, J.3    Casellas, J.M.4    Martinez-Beltran, J.5    Bush, K.6
  • 102
  • 103
    • 0031941930 scopus 로고    scopus 로고
    • Characterization of FOX-3, an AmpC-type plasmid-mediated beta-lactamase from an Italian isolate of Klebsiella oxytoca
    • Marchese A, Arlet G, Schito GC, Lagrange PH, Philippon A. Characterization of FOX-3, an AmpC-type plasmid-mediated beta-lactamase from an Italian isolate of Klebsiella oxytoca. Antimicrob Agents Chemother 1998, 42:464-467.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 464-467
    • Marchese, A.1    Arlet, G.2    Schito, G.C.3    Lagrange, P.H.4    Philippon, A.5
  • 104
    • 0033840869 scopus 로고    scopus 로고
    • Molecular characterization of FOX-4, a new AmpC-type plasmid-mediated beta-lactamase from an Escherichia coli strain isolated in Spain
    • Bou G, Oliver A, Ojeda M, Monzon C, Martinez-Beltran J. Molecular characterization of FOX-4, a new AmpC-type plasmid-mediated beta-lactamase from an Escherichia coli strain isolated in Spain. Antimicrob Agents Chemother 2000, 44:2549-2553.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 2549-2553
    • Bou, G.1    Oliver, A.2    Ojeda, M.3    Monzon, C.4    Martinez-Beltran, J.5
  • 105
    • 0034769860 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of FOX-5, an AmpC-type plasmid-encoded beta-lactamase from a New York City Klebsiella pneumoniae clinical isolate
    • Queenan AM, Jenkins S, Bush K. Cloning and biochemical characterization of FOX-5, an AmpC-type plasmid-encoded beta-lactamase from a New York City Klebsiella pneumoniae clinical isolate. Antimicrob Agents Chemother 2001, 45:3189-3194.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 3189-3194
    • Queenan, A.M.1    Jenkins, S.2    Bush, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.