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Volumn 69, Issue 6, 2014, Pages 1715-1716

Avibactam activity against extended-spectrum AmpC β-lactamases

Author keywords

Cephalosporins; Enterobacteria; Inhibitors; Resistance; Variants

Indexed keywords

AVIBACTAM; BETA LACTAMASE AMPC; CEFEPIME; CEFTAZIDIME; IMIPENEM; AMPC BETA-LACTAMASES; ANTIINFECTIVE AGENT; AZABICYCLO DERIVATIVE; BACTERIAL PROTEIN; BETA LACTAMASE;

EID: 84903900875     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dku002     Document Type: Letter
Times cited : (20)

References (10)
  • 1
    • 82955187694 scopus 로고    scopus 로고
    • In vitro activity of avibactam (NXL104) in combination with β-lactams against Gram-negative bacteria, including OXA-48 β-lactamase-producing Klebsiella pneumoniae
    • Aktaş Z, Kayacan C, Oncul O. In vitro activity of avibactam (NXL104) in combination with β-lactams against Gram-negative bacteria, including OXA-48 β-lactamase-producing Klebsiella pneumoniae. Int J Antimicrob Agents 2012; 39: 86-9.
    • (2012) Int J Antimicrob Agents , vol.39 , pp. 86-89
    • Aktaş, Z.1    Kayacan, C.2    Oncul, O.3
  • 2
    • 67650718178 scopus 로고    scopus 로고
    • In vitro activity of the β-lactamase inhibitor NXL104 against KPC-2 carbapenemase and Enterobacteriaceae expressing KPC carbapenemases
    • Stachyra T, Levasseur P, Péchereau MC et al. In vitro activity of the β-lactamase inhibitor NXL104 against KPC-2 carbapenemase and Enterobacteriaceae expressing KPC carbapenemases. J Antimicrob Chemother 2009; 64: 326-9.
    • (2009) J Antimicrob Chemother , vol.64 , pp. 326-329
    • Stachyra, T.1    Levasseur, P.2    Péchereau, M.C.3
  • 3
    • 84861121770 scopus 로고    scopus 로고
    • Characterization of β-lactamase and porin mutants of Enterobacteriaceae selected with ceftaroline+avibactam (NXL104)
    • Livermore DM, Mushtaq S, Barker K et al. Characterization of β-lactamase and porin mutants of Enterobacteriaceae selected with ceftaroline+avibactam (NXL104). J Antimicrob Chemother 2012; 67: 1354-8.
    • (2012) J Antimicrob Chemother , vol.67 , pp. 1354-1358
    • Livermore, D.M.1    Mushtaq, S.2    Barker, K.3
  • 4
    • 0141539215 scopus 로고    scopus 로고
    • Characterization of blaCMY-10 a novel, plasmid-encoded AmpC-type β-lactamase gene in a clinical isolate of Enterobacter aerogenes
    • Lee SH, Jeong SH, Park YM. Characterization of blaCMY-10 a novel, plasmid-encoded AmpC-type β-lactamase gene in a clinical isolate of Enterobacter aerogenes. J Appl Microbiol 2003; 95: 744-52.
    • (2003) J Appl Microbiol , vol.95 , pp. 744-752
    • Lee, S.H.1    Jeong, S.H.2    Park, Y.M.3
  • 5
    • 34547521263 scopus 로고    scopus 로고
    • Extended-spectrum cephalosporinases: structure, detection and epidemiology
    • Nordmann P, Mammeri H. Extended-spectrum cephalosporinases: structure, detection and epidemiology. Future Microbiol 2007; 2: 297-307.
    • (2007) Future Microbiol , vol.2 , pp. 297-307
    • Nordmann, P.1    Mammeri, H.2
  • 6
    • 80051818446 scopus 로고    scopus 로고
    • Emergence of ertapenem resistance in an Escherichia coli clinical isolate producing extended-spectrum β-lactamase AmpC
    • Guillon H, Tande D, Mammeri H. Emergence of ertapenem resistance in an Escherichia coli clinical isolate producing extended-spectrum β-lactamase AmpC. Antimicrob Agents Chemother 2011; 55: 4443-6.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 4443-4446
    • Guillon, H.1    Tande, D.2    Mammeri, H.3
  • 7
    • 33745620492 scopus 로고    scopus 로고
    • Naturally occurring extended-spectrum cephalosporinases in Escherichia coli
    • Mammeri H, Poirel L, Fortineau N et al. Naturally occurring extended-spectrum cephalosporinases in Escherichia coli. Antimicrob Agents Chemother 2006; 50: 2573-6.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2573-2576
    • Mammeri, H.1    Poirel, L.2    Fortineau, N.3
  • 8
    • 34548136190 scopus 로고    scopus 로고
    • Extension of the hydrolysis spectrum of AmpC β-lactamase of Escherichia coli due to amino acid insertion in the H-10 helix
    • Mammeri H, Poirel L, Nordmann P. Extension of the hydrolysis spectrum of AmpC β-lactamase of Escherichia coli due to amino acid insertion in the H-10 helix. J Antimicrob Chemother 2007; 60: 490-4.
    • (2007) J Antimicrob Chemother , vol.60 , pp. 490-494
    • Mammeri, H.1    Poirel, L.2    Nordmann, P.3
  • 10
    • 84877842576 scopus 로고    scopus 로고
    • Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC β-lactamases
    • Lahiri SD, Mangani S, Durand-Reville T et al. Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC β-lactamases. Antimicrob Agents Chemother 2013; 57: 2496-505.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 2496-2505
    • Lahiri, S.D.1    Mangani, S.2    Durand-Reville, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.