메뉴 건너뛰기




Volumn 43, Issue SUPPL. 2, 2006, Pages

Mechanisms of multidrug resistance in Acinetobacter species and Pseudomonas aeruginosa

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; AMOXICILLIN; AZTREONAM; BETA LACTAMASE; CARBAPENEM; CEFALOTIN; CEFOPERAZONE; CEFTAZIDIME; CEFTRIAXONE; CEFUROXIME; CEPHALOSPORINASE; CEPHAMYCIN; DNA TOPOISOMERASE; IMIPENEM; OUTER MEMBRANE PROTEIN; OXACILLIN; PENICILLIN G; POLYMYXIN; PORIN; TICARCILLIN; AMINOGLYCOSIDE; CARRIER PROTEIN; QUINOLONE DERIVATIVE;

EID: 33747625237     PISSN: 10584838     EISSN: None     Source Type: Journal    
DOI: 10.1086/504477     Document Type: Conference Paper
Times cited : (573)

References (131)
  • 1
    • 0000123301 scopus 로고
    • An enzyme from bacteria able to destroy penicillin
    • Abraham EP, Chain E. An enzyme from bacteria able to destroy penicillin. Nature 1940; 146:837.
    • (1940) Nature , vol.146 , pp. 837
    • Abraham, E.P.1    Chain, E.2
  • 2
    • 24644515282 scopus 로고    scopus 로고
    • Overview of nosocomial infections caused by gram-negative bacilli
    • Gaynes R, Edwards JR. Overview of nosocomial infections caused by gram-negative bacilli. Clin Infect Dis 2005; 41:848-54.
    • (2005) Clin Infect Dis , vol.41 , pp. 848-854
    • Gaynes, R.1    Edwards, J.R.2
  • 3
    • 3943093972 scopus 로고    scopus 로고
    • Nosocomial bloodstream infections in US hospitals: Analysis of 24,179 cases from a prospective nationwide surveillance study
    • Wisplinghoff H, Bischoff T, Tallent SM, Seifert H, Wenzel RP, Edmond MB. Nosocomial bloodstream infections in US hospitals: analysis of 24,179 cases from a prospective nationwide surveillance study. Clin Infect Dis 2004; 39:309-17.
    • (2004) Clin Infect Dis , vol.39 , pp. 309-317
    • Wisplinghoff, H.1    Bischoff, T.2    Tallent, S.M.3    Seifert, H.4    Wenzel, R.P.5    Edmond, M.B.6
  • 4
    • 0023816590 scopus 로고
    • Distribution of β-lactamases and phenotype analysis in clinical strains of Acinetobacter calcoaceticus
    • Joly-Guillo ML, Vallee E, Bergogne-Berezin E, Philippon A. Distribution of β-lactamases and phenotype analysis in clinical strains of Acinetobacter calcoaceticus. J Antimicrob Chemother 1988; 22:597-604.
    • (1988) J Antimicrob Chemother , vol.22 , pp. 597-604
    • Joly-Guillo, M.L.1    Vallee, E.2    Bergogne-Berezin, E.3    Philippon, A.4
  • 5
    • 0026695472 scopus 로고
    • Purification and characterization of an extracellular β-lactamase produced by Acinetobacter calcoaceticus
    • Blechschmidt B, Borneleit P, Kleber HP. Purification and characterization of an extracellular β-lactamase produced by Acinetobacter calcoaceticus. J Gen Microbiol 1992; 138:1197-202.
    • (1992) J Gen Microbiol , vol.138 , pp. 1197-1202
    • Blechschmidt, B.1    Borneleit, P.2    Kleber, H.P.3
  • 6
    • 0027446214 scopus 로고
    • In vitro antimicrobial production of β-lactamases, aminoglycoside-modifying enzymes, and chloramphenicol acetyltransferase by and susceptibility of clinical isolates of Acinetobacter baumannii
    • Vila J, Marcos A, Marco F, et al. In vitro antimicrobial production of β-lactamases, aminoglycoside-modifying enzymes, and chloramphenicol acetyltransferase by and susceptibility of clinical isolates of Acinetobacter baumannii. Antimicrob Agents Chemother 1993; 37:138-41.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 138-141
    • Vila, J.1    Marcos, A.2    Marco, F.3
  • 8
    • 0038674216 scopus 로고    scopus 로고
    • Chromosomal integration of a cephalosporinase gene from Acinetobacter baumannii into Oligella urethralis as a source of acquired resistance to β-lactams
    • Mammeri H, Poirel L, Mangeney N, Nordmann P. Chromosomal integration of a cephalosporinase gene from Acinetobacter baumannii into Oligella urethralis as a source of acquired resistance to β-lactams. Antimicrob Agents Chemother 2003; 47:1536-42.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1536-1542
    • Mammeri, H.1    Poirel, L.2    Mangeney, N.3    Nordmann, P.4
  • 9
    • 0035322722 scopus 로고    scopus 로고
    • Biochemical characterization of chromosomal cephalosporinases from isolates belonging to the Acinetobacter baumannii complex
    • Lopez-Hernandez S, Alarcon T, Lopez-Brea M. Biochemical characterization of chromosomal cephalosporinases from isolates belonging to the Acinetobacter baumannii complex. Clin Microbiol Infect 2001; 7: 218-26.
    • (2001) Clin Microbiol Infect , vol.7 , pp. 218-226
    • Lopez-Hernandez, S.1    Alarcon, T.2    Lopez-Brea, M.3
  • 10
    • 1642461345 scopus 로고    scopus 로고
    • Molecular characterization of the gene encoding a new AmpC β-lactamase in a clinical strain of Acinetobacter genomic species 3
    • Beceiro A, Dominguez L, Ribera A, et al. Molecular characterization of the gene encoding a new AmpC β-lactamase in a clinical strain of Acinetobacter genomic species 3. Antimicrob Agents Chemother 2004; 48:1374-8.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 1374-1378
    • Beceiro, A.1    Dominguez, L.2    Ribera, A.3
  • 11
    • 0030030554 scopus 로고    scopus 로고
    • Characterization of the chromosomal cephalosporinases produced by Acinetobacter Iwoffii and Acinetobacter baumannii clinical isolates
    • Perilli M, Felici A, Oratore A, et al. Characterization of the chromosomal cephalosporinases produced by Acinetobacter Iwoffii and Acinetobacter baumannii clinical isolates. Antimicrob Agents Chemother 1996; 40:715-9.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 715-719
    • Perilli, M.1    Felici, A.2    Oratore, A.3
  • 12
    • 0343185958 scopus 로고    scopus 로고
    • Cloning, nucleotide sequencing, and analysis of the gene encoding an AmpC β-lactamase in Acinetobacter baumannii
    • Bou G, Martinez-Beltran J. Cloning, nucleotide sequencing, and analysis of the gene encoding an AmpC β-lactamase in Acinetobacter baumannii. Antimicrob Agents Chemother 2000; 44:428-32.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 428-432
    • Bou, G.1    Martinez-Beltran, J.2
  • 13
    • 21444461393 scopus 로고    scopus 로고
    • Identification of a new allelic variant of the Acinetobacter baumannii cephalosporinase, ADC-7 β-lactamase: Defining a unique family of class C enzymes
    • Hujer KM, Hamza NS, Hujer AM, et al. Identification of a new allelic variant of the Acinetobacter baumannii cephalosporinase, ADC-7 β-lactamase: defining a unique family of class C enzymes. Antimicrob Agents Chemother 2005; 49:2941-8.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2941-2948
    • Hujer, K.M.1    Hamza, N.S.2    Hujer, A.M.3
  • 14
    • 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; 48:612-4.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 612-614
    • Segal, H.1    Nelson, E.C.2    Elisha, B.G.3
  • 15
    • 0037362989 scopus 로고    scopus 로고
    • Characterization of class 1 integron resistance gene cassettes and the identification of a novel IS-like element in Acinetobacter baumannii
    • Segal H, Thomas R, Gay Elisha B. Characterization of class 1 integron resistance gene cassettes and the identification of a novel IS-like element in Acinetobacter baumannii. Plasmid 2003; 49:169-78.
    • (2003) Plasmid , vol.49 , pp. 169-178
    • Segal, H.1    Thomas, R.2    Gay Elisha, B.3
  • 16
    • 0033827703 scopus 로고    scopus 로고
    • Characterization of a nosocomial outbreak caused by a multiresistant Acinetobacter baumannii strain with a carbapenem-hydrolyzing enzyme: High-level carbapenem resistance in A. baumannii is not due solely to the presence of β-lactamases
    • Bou G, Cervero G, Dominguez MA, Quereda C, Martinez-Beltran J. Characterization of a nosocomial outbreak caused by a multiresistant Acinetobacter baumannii strain with a carbapenem-hydrolyzing enzyme: high-level carbapenem resistance in A. baumannii is not due solely to the presence of β-lactamases. J Clin Microbiol 2000; 38:3299-305.
    • (2000) J Clin Microbiol , vol.38 , pp. 3299-3305
    • Bou, G.1    Cervero, G.2    Dominguez, M.A.3    Quereda, C.4    Martinez-Beltran, J.5
  • 17
    • 21644489492 scopus 로고    scopus 로고
    • Study on the molecular epidemiology of SHV type β-lactamase-encoding genes of multipledrug-resistant Acinetobacter baumannii
    • Huang ZM, Mao PH, Chen Y, Wu L, Wu J. Study on the molecular epidemiology of SHV type β-lactamase-encoding genes of multipledrug-resistant Acinetobacter baumannii. Zhonghua Liu Xing Bing Xue Za Zhi 2004; 25:425-7.
    • (2004) Zhonghua Liu Xing Bing Xue Za Zhi , vol.25 , pp. 425-427
    • Huang, Z.M.1    Mao, P.H.2    Chen, Y.3    Wu, L.4    Wu, J.5
  • 18
    • 0029913746 scopus 로고    scopus 로고
    • Acinetobacter spp. as nosocomial pathogens: Microbiological, clinical, and epidemiological features
    • Bergogne-Berezin E, Towner KJ. Acinetobacter spp. as nosocomial pathogens: microbiological, clinical, and epidemiological features. Clin Microbiol Rev 1996; 9:148-65.
    • (1996) Clin Microbiol Rev , vol.9 , pp. 148-165
    • Bergogne-Berezin, E.1    Towner, K.J.2
  • 19
    • 4644315827 scopus 로고    scopus 로고
    • Nosocomial transmission of CTX-M-2 β-lactamase-producing Acinetobacter baumannii in a neurosurgery ward
    • Nagano N, Nagano Y, Cordevant C, Shibata N, Arakawa Y. Nosocomial transmission of CTX-M-2 β-lactamase-producing Acinetobacter baumannii in a neurosurgery ward. J Clin Microbiol 2004; 42: 3978-84.
    • (2004) J Clin Microbiol , vol.42 , pp. 3978-3984
    • Nagano, N.1    Nagano, Y.2    Cordevant, C.3    Shibata, N.4    Arakawa, Y.5
  • 20
    • 0342762055 scopus 로고    scopus 로고
    • Widespread detection of PER-1-type extended-spectrum β-lactamases among nosocomial Acinetobacter and Pseudomonas aeruginosa isolates in Turkey: A nationwide multicenter study
    • Vahaboglu H, Ozturk R, Aygun G, et al. Widespread detection of PER-1-type extended-spectrum β-lactamases among nosocomial Acinetobacter and Pseudomonas aeruginosa isolates in Turkey: a nationwide multicenter study. Antimicrob Agents Chemother 1997; 41:2265-9.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2265-2269
    • Vahaboglu, H.1    Ozturk, R.2    Aygun, G.3
  • 21
    • 0038334864 scopus 로고    scopus 로고
    • High prevalence of PER-1 extended-spectrum β-lactamase-producing Acinetobacter spp. in Korea
    • Yong D, Shin JH, Kim S, et al. High prevalence of PER-1 extended-spectrum β-lactamase-producing Acinetobacter spp. in Korea. Antimicrob Agents Chemother 2003; 47:1749-51.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1749-1751
    • Yong, D.1    Shin, J.H.2    Kim, S.3
  • 22
    • 0032935004 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamase-producing strain of Acinetobacter baumannii isolated from a patient in France
    • Poirel L, Karim A, Mercat A, et al. Extended-spectrum β-lactamase-producing strain of Acinetobacter baumannii isolated from a patient in France. J Antimicrob Chemother 1999; 43:157-8.
    • (1999) J Antimicrob Chemother , vol.43 , pp. 157-158
    • Poirel, L.1    Karim, A.2    Mercat, A.3
  • 23
    • 0043025370 scopus 로고    scopus 로고
    • Outbreak of extended-spectrum β-lactamase VEB-1-producing isolates of Acinetobacter baumannii in a French hospital
    • Poirel L, Menuteau O, Agoli N, Cattoen C, Nordmann P. Outbreak of extended-spectrum β-lactamase VEB-1-producing isolates of Acinetobacter baumannii in a French hospital. J Clin Microbiol 2003; 41: 3542-7.
    • (2003) J Clin Microbiol , vol.41 , pp. 3542-3547
    • Poirel, L.1    Menuteau, O.2    Agoli, N.3    Cattoen, C.4    Nordmann, P.5
  • 24
    • 16844370576 scopus 로고    scopus 로고
    • Investigation of a nosocomial outbreak of extended-spectrum β-lactamase VEB-1-producing isolates of Acinetobacter baumannii in a hospital setting
    • Carbonne A, Naas T, Blanckaert K, et al. Investigation of a nosocomial outbreak of extended-spectrum β-lactamase VEB-1-producing isolates of Acinetobacter baumannii in a hospital setting. J Hosp Infect 2005; 60:14-8.
    • (2005) J Hosp Infect , vol.60 , pp. 14-18
    • Carbonne, A.1    Naas, T.2    Blanckaert, K.3
  • 25
    • 1542513872 scopus 로고    scopus 로고
    • Molecular epidemiology of sequential outbreaks of Acinetobacter baumannii in an intensive care unit shows the emergence of carbapenem resistance
    • Zarrilli R, Crispino M, Bagattini M, et al. Molecular epidemiology of sequential outbreaks of Acinetobacter baumannii in an intensive care unit shows the emergence of carbapenem resistance. J Clin Microbiol 2004; 42:946-53.
    • (2004) J Clin Microbiol , vol.42 , pp. 946-953
    • Zarrilli, R.1    Crispino, M.2    Bagattini, M.3
  • 26
    • 15944385352 scopus 로고    scopus 로고
    • The sequences of seven class D β-lactamases isolated from carbapenem-resistant Acinetobacter baumannii from four continents
    • Brown S, Amyes SG. The sequences of seven class D β-lactamases isolated from carbapenem-resistant Acinetobacter baumannii from four continents. Clin Microbiol Infect 2005; 11:326-9.
    • (2005) Clin Microbiol Infect , vol.11 , pp. 326-329
    • Brown, S.1    Amyes, S.G.2
  • 27
    • 22544477125 scopus 로고    scopus 로고
    • Update on Pseudomonas aeruginosa and Acinetobacter baumannii infections in the healthcare setting
    • Navon-Venezia S, Ben-Ami R, Carmeli Y. Update on Pseudomonas aeruginosa and Acinetobacter baumannii infections in the healthcare setting. Curr Opin Infect Dis 2005; 18:306-13.
    • (2005) Curr Opin Infect Dis , vol.18 , pp. 306-313
    • Navon-Venezia, S.1    Ben-Ami, R.2    Carmeli, Y.3
  • 28
    • 21244471489 scopus 로고    scopus 로고
    • Hospital outbreak caused by a carbapenem-resistant strain of Acinetobacter baumannii: Patient prognosis and risk-factors for colonization and infection
    • del Mar Tomas M, Cartelle M, Pertega S, et al. Hospital outbreak caused by a carbapenem-resistant strain of Acinetobacter baumannii: patient prognosis and risk-factors for colonization and infection. Clin Microbiol Infect 2005; 11:540-6.
    • (2005) Clin Microbiol Infect , vol.11 , pp. 540-546
    • Mar Tomas, M.1    Cartelle, M.2    Pertega, S.3
  • 29
    • 0033988342 scopus 로고    scopus 로고
    • Sequence analysis of ARI-1, a novel OXA β-lactamase, responsible for imipenem resistance in Acinetobacter baumannii 6B92
    • Donald HM, Scaife W, Amyes SG, Young HK. Sequence analysis of ARI-1, a novel OXA β-lactamase, responsible for imipenem resistance in Acinetobacter baumannii 6B92. Antimicrob Agents Chemother 2000; 44:196-9.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 196-199
    • Donald, H.M.1    Scaife, W.2    Amyes, S.G.3    Young, H.K.4
  • 30
    • 23044458428 scopus 로고    scopus 로고
    • Contribution of acquired carbapenem-hydrolyzing oxacillinases to carbapenem resistance in Acinetobacter baumannii
    • Heritier C, Poirel L, Lambert T, Nordmann P. Contribution of acquired carbapenem-hydrolyzing oxacillinases to carbapenem resistance in Acinetobacter baumannii. Antimicrob Agents Chemother 2005; 49:3198-202.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3198-3202
    • Heritier, C.1    Poirel, L.2    Lambert, T.3    Nordmann, P.4
  • 31
    • 0036929877 scopus 로고    scopus 로고
    • Characterization of an integron carrying a new class D β-lactamase (OXA-37) in Acinetobacter baumannii
    • Navia MM, Ruiz J, Vila J. Characterization of an integron carrying a new class D β-lactamase (OXA-37) in Acinetobacter baumannii. Microb Drug Resist 2002; 8:261-5.
    • (2002) Microb Drug Resist , vol.8 , pp. 261-265
    • Navia, M.M.1    Ruiz, J.2    Vila, J.3
  • 32
    • 0030777048 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence analysis of a gene encoding an OXA-derived β-lactamase in Acinetobacter baumannii
    • Vila J, Navia M, Ruiz J, Casals C. Cloning and nucleotide sequence analysis of a gene encoding an OXA-derived β-lactamase in Acinetobacter baumannii. Antimicrob Agents Chemother 1997; 41:2757-9.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2757-2759
    • Vila, J.1    Navia, M.2    Ruiz, J.3    Casals, C.4
  • 33
    • 0036150052 scopus 로고    scopus 로고
    • Integron-located oxa-32 gene cassette encoding an extended-spectrum variant of OXA-2 β-lactamase from Pseudomonas aeruginosa
    • Poirel L, Gerome P, De Champs C, Stephanazzi J, Naas T, Nordmann P. Integron-located oxa-32 gene cassette encoding an extended-spectrum variant of OXA-2 β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 2002; 46:566-9.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 566-569
    • Poirel, L.1    Gerome, P.2    De Champs, C.3    Stephanazzi, J.4    Naas, T.5    Nordmann, P.6
  • 34
    • 0035144848 scopus 로고    scopus 로고
    • OXA-28, an extended-spectrum variant of OXA-10 β-lactamase from Pseudomonas aeruginosa and its plasmid- and integron-located gene
    • Poirel L, Girlich D, Naas T, Nordmann P. OXA-28, an extended-spectrum variant of OXA-10 β-lactamase from Pseudomonas aeruginosa and its plasmid- and integron-located gene. Antimicrob Agents Chemother 2001; 45:447-53.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 447-453
    • Poirel, L.1    Girlich, D.2    Naas, T.3    Nordmann, P.4
  • 35
    • 0036001185 scopus 로고    scopus 로고
    • Molecular characterization of metallo-β-lactamase-producing Acinetobacter baumannii and Acinetobacter genomospecies 3 from Korea: Identification of two new integrons carrying the bla(VIM-2) gene cassettes
    • Yum JH, Yi K, Lee H, et al. Molecular characterization of metallo-β-lactamase-producing Acinetobacter baumannii and Acinetobacter genomospecies 3 from Korea: identification of two new integrons carrying the bla(VIM-2) gene cassettes. J Antimicrob Chemother 2002; 49: 837-40.
    • (2002) J Antimicrob Chemother , vol.49 , pp. 837-840
    • Yum, J.H.1    Yi, K.2    Lee, H.3
  • 36
    • 5444265955 scopus 로고    scopus 로고
    • Metallo-β-lactamase-producing gram-negative bacilli in Korean Nationwide Surveillance of Antimicrobial Resistance group hospitals in 2003: Continued prevalence of VIM-producing Pseudomonas spp. and increase of IMF-producing Acinetobacter spp
    • Lee K, Ha GY, Shin BM, et al. Metallo-β-lactamase-producing gram-negative bacilli in Korean Nationwide Surveillance of Antimicrobial Resistance group hospitals in 2003: continued prevalence of VIM-producing Pseudomonas spp. and increase of IMF-producing Acinetobacter spp. Diagn Microbiol Infect Dis 2004; 50:51-8.
    • (2004) Diagn Microbiol Infect Dis , vol.50 , pp. 51-58
    • Lee, K.1    Ha, G.Y.2    Shin, B.M.3
  • 38
    • 0037167473 scopus 로고    scopus 로고
    • Molecular characterization of bla(IMP-5), a new integron-borne metallo-β-lactamase gene from an Acinetobacter baumannii nosocomial isolate in Portugal
    • Da Silva GJ, Correia M, Vital C, et al. Molecular characterization of bla(IMP-5), a new integron-borne metallo-β-lactamase gene from an Acinetobacter baumannii nosocomial isolate in Portugal. FEMS Microbiol Lett 2002; 215:33-9.
    • (2002) FEMS Microbiol Lett , vol.215 , pp. 33-39
    • Da Silva, G.J.1    Correia, M.2    Vital, C.3
  • 39
    • 0043269798 scopus 로고    scopus 로고
    • Molecular epidemiology and mechanisms of carbapenem resistance in Acinetobacter baumannii endemic in New York City
    • Quale J, Bratu S, Landman D, Heddurshetti R. Molecular epidemiology and mechanisms of carbapenem resistance in Acinetobacter baumannii endemic in New York City. Clin Infect Dis 2003; 37:214-20.
    • (2003) Clin Infect Dis , vol.37 , pp. 214-220
    • Quale, J.1    Bratu, S.2    Landman, D.3    Heddurshetti, R.4
  • 40
    • 0029763190 scopus 로고    scopus 로고
    • Imipenem resistance among Acinetobacter baumannii: Association with reduced expression of a 33-36 kDa outer membrane protein
    • Clark RB. Imipenem resistance among Acinetobacter baumannii: association with reduced expression of a 33-36 kDa outer membrane protein. J Antimicrob Chemother 1996; 38:245-51.
    • (1996) J Antimicrob Chemother , vol.38 , pp. 245-251
    • Clark, R.B.1
  • 41
    • 0036900235 scopus 로고    scopus 로고
    • Loss of a 29-kilodalton outer membrane protein in Acinetobacter baumannii is associated with imipenem resistance
    • Limansky AS, Mussi MA, Viale AM. Loss of a 29-kilodalton outer membrane protein in Acinetobacter baumannii is associated with imipenem resistance. J Clin Microbiol 2002; 40:4776-8.
    • (2002) J Clin Microbiol , vol.40 , pp. 4776-4778
    • Limansky, A.S.1    Mussi, M.A.2    Viale, A.M.3
  • 42
    • 0031920489 scopus 로고    scopus 로고
    • Molecular epidemiology of aminoglycoside resistance in Acinetobacter spp
    • Seward RJ, Lambert T, Towner KJ. Molecular epidemiology of aminoglycoside resistance in Acinetobacter spp. J Med Microbiol 1998; 47:455-62.
    • (1998) J Med Microbiol , vol.47 , pp. 455-462
    • Seward, R.J.1    Lambert, T.2    Towner, K.J.3
  • 43
    • 9244250185 scopus 로고    scopus 로고
    • Diversity of aminoglycoside-resistance genes and their association with class I integrons among strains of pan-European Acinetobacter baumannii clones
    • Nemec A, Dolzani L, Brisse S, van den Broek P, Dijkshoorn L. Diversity of aminoglycoside-resistance genes and their association with class I integrons among strains of pan-European Acinetobacter baumannii clones. J Med Microbiol 2004; 53:1233-40.
    • (2004) J Med Microbiol , vol.53 , pp. 1233-1240
    • Nemec, A.1    Dolzani, L.2    Brisse, S.3    Van Den Broek, P.4    Dijkshoorn, L.5
  • 44
    • 0029035984 scopus 로고
    • Mutation in the gyrA gene of quinolone-resistant clinical isolates of Acinetobacter baumannii
    • Vila J, Ruiz J, Goni P, Marcos A, Jimenez de Anta T. Mutation in the gyrA gene of quinolone-resistant clinical isolates of Acinetobacter baumannii. Antimicrob Agents Chemother 1995; 39:1201-3.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1201-1203
    • Vila, J.1    Ruiz, J.2    Goni, P.3    Marcos, A.4    De Jimenez Anta, T.5
  • 45
    • 0030851997 scopus 로고    scopus 로고
    • Quinolone-resistance mutations in the topoisomerase IV parC gene of Acinetobacter baumannii
    • Vila J, Ruiz J, Goni P, Jimenez de Anta T. Quinolone-resistance mutations in the topoisomerase IV parC gene of Acinetobacter baumannii. J Antimicrob Chemother 1997; 39:757-62.
    • (1997) J Antimicrob Chemother , vol.39 , pp. 757-762
    • Vila, J.1    Ruiz, J.2    Goni, P.3    De Jimenez Anta, T.4
  • 47
    • 24644466428 scopus 로고    scopus 로고
    • Emergence of plasmid-mediated resistance to quinolones in Enterobacteriaceae
    • Nordmann P, Poirel L. Emergence of plasmid-mediated resistance to quinolones in Enterobacteriaceae. J Antimicrob Chemother 2005; 56: 463-9.
    • (2005) J Antimicrob Chemother , vol.56 , pp. 463-469
    • Nordmann, P.1    Poirel, L.2
  • 48
    • 0035178557 scopus 로고    scopus 로고
    • Resistance-modulation-cell division-type efflux pump involved in aminoglycoside resistance in Acinetobacter baumannii strain BM4454
    • Magnet S, Courvalin P, Lambert T. Resistance-modulation-cell division-type efflux pump involved in aminoglycoside resistance in Acinetobacter baumannii strain BM4454. Antimicrob Agents Chemother 2001; 45:3375-80.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 3375-3380
    • Magnet, S.1    Courvalin, P.2    Lambert, T.3
  • 49
    • 4344572020 scopus 로고    scopus 로고
    • Expression of the RND-type efflux pump AdeABC in Acinetobacter baumannii is regulated by the AdeRS two-component system
    • Marchand I, Damier-Piolle L, Courvalin P, Lambert T. Expression of the RND-type efflux pump AdeABC in Acinetobacter baumannii is regulated by the AdeRS two-component system. Antimicrob Agents Chemother 2004; 48:3298-304.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3298-3304
    • Marchand, I.1    Damier-Piolle, L.2    Courvalin, P.3    Lambert, T.4
  • 50
    • 0032920406 scopus 로고    scopus 로고
    • Clavulanate induces expression of the Pseudomonas aeruginosa AmpC cephalosporinase at physiologically relevant concentrations and antagonizes the antibacterial activity of ticarcillin
    • Lister PD, Gardner VM, Sanders CC. Clavulanate induces expression of the Pseudomonas aeruginosa AmpC cephalosporinase at physiologically relevant concentrations and antagonizes the antibacterial activity of ticarcillin. Antimicrob Agents Chemother 1999; 43:882-9.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 882-889
    • Lister, P.D.1    Gardner, V.M.2    Sanders, C.C.3
  • 51
    • 0022446748 scopus 로고
    • Effect of clavulanic acid on the activity of ticarcillin against Pseudomonas aeruginosa
    • Tausk F, Stratton CW. Effect of clavulanic acid on the activity of ticarcillin against Pseudomonas aeruginosa. Antimicrob Agents Chemother 1986; 30:584-9.
    • (1986) Antimicrob Agents Chemother , vol.30 , pp. 584-589
    • Tausk, F.1    Stratton, C.W.2
  • 52
    • 0023583815 scopus 로고
    • Clinical significance of β-lactamase induction and stable derepression in gram-negative rods
    • Livermore DM. Clinical significance of β-lactamase induction and stable derepression in gram-negative rods. Eur J Clin Microbiol 1987; 6:439-45.
    • (1987) Eur J Clin Microbiol , vol.6 , pp. 439-445
    • Livermore, D.M.1
  • 53
    • 0025117724 scopus 로고
    • Nucleotide sequence of the PSE-4 carbenicillinase gene and correlations with the Staphylococcus aureus PC1 β-lactamase crystal structure
    • Boissinot M, Levesque RC. Nucleotide sequence of the PSE-4 carbenicillinase gene and correlations with the Staphylococcus aureus PC1 β-lactamase crystal structure. J Biol Chem 1990; 265:1225-30.
    • (1990) J Biol Chem , vol.265 , pp. 1225-1230
    • Boissinot, M.1    Levesque, R.C.2
  • 55
    • 0025923469 scopus 로고
    • Characterization of the blaCARB-3 gene encoding the carbenicillinase-3 β-lactamase of Pseudomonas aeruginosa
    • Lachapelle J, Dufresne J, Levesque RC. Characterization of the blaCARB-3 gene encoding the carbenicillinase-3 β-lactamase of Pseudomonas aeruginosa. Gene 1991; 102:7-12.
    • (1991) Gene , vol.102 , pp. 7-12
    • Lachapelle, J.1    Dufresne, J.2    Levesque, R.C.3
  • 56
    • 0031903175 scopus 로고    scopus 로고
    • Structure of CARB-4 and AER-1 carbenicillin-hydrolyzing β-lactamases
    • Sanschagrin F, Bejaoui N, Levesque RC. Structure of CARB-4 and AER-1 carbenicillin-hydrolyzing β-lactamases. Antimicrob Agents Chemother 1998; 42:1966-72.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 1966-1972
    • Sanschagrin, F.1    Bejaoui, N.2    Levesque, R.C.3
  • 57
    • 0029154451 scopus 로고
    • OXA-14, another extended-spectrum variant of OXA-10 (PSE-2) β-lactamase from Pseudomonas aeruginosa
    • Danel F, Hall LM, Gur D, Livermore DM. OXA-14, another extended-spectrum variant of OXA-10 (PSE-2) β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 1995; 39:1881-4.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1881-1884
    • Danel, F.1    Hall, L.M.2    Gur, D.3    Livermore, D.M.4
  • 58
    • 0030939635 scopus 로고    scopus 로고
    • OXA-15, an extended-spectrum variant of OXA-2 β-lactamase, isolated from a Pseudomonas aeruginosa strain
    • Danel F, Hall LM, Gur D, Livermore DM. OXA-15, an extended-spectrum variant of OXA-2 β-lactamase, isolated from a Pseudomonas aeruginosa strain. Antimicrob Agents Chemother 1997; 41:785-90.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 785-790
    • Danel, F.1    Hall, L.M.2    Gur, D.3    Livermore, D.M.4
  • 59
    • 0033002098 scopus 로고    scopus 로고
    • OXA-17, a further extended-spectrum variant of OXA-10 β-lactamase, isolated from Pseudomonas aeruginosa
    • Danel F, Hall LM, Duke B, Gur D, Livermore DM. OXA-17, a further extended-spectrum variant of OXA-10 β-lactamase, isolated from Pseudomonas aeruginosa. Antimicrob Agents Chemother 1999; 43:1362-6.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1362-1366
    • Danel, F.1    Hall, L.M.2    Duke, B.3    Gur, D.4    Livermore, D.M.5
  • 60
    • 0021907611 scopus 로고
    • β-lactamases of Pseudomonas aeruginosa and susceptibility against β-lactam antibiotics
    • Thabaut A, Philippon A, Meyran M. β-lactamases of Pseudomonas aeruginosa and susceptibility against β-lactam antibiotics. Chemioterapia 1985; 4:36-42.
    • (1985) Chemioterapia , vol.4 , pp. 36-42
    • Thabaut, A.1    Philippon, A.2    Meyran, M.3
  • 61
    • 0022618147 scopus 로고
    • New plasmid-mediated oxacillin-hydrolyzing β-lactamase in Pseudomonas aeruginosa
    • Philippon AM, Paul GC, Jacoby GA. New plasmid-mediated oxacillin-hydrolyzing β-lactamase in Pseudomonas aeruginosa. J Antimicrob Chemother 1986; 17:415-22.
    • (1986) J Antimicrob Chemother , vol.17 , pp. 415-422
    • Philippon, A.M.1    Paul, G.C.2    Jacoby, G.A.3
  • 63
    • 0028883511 scopus 로고
    • β-lactamases in laboratory and clinical resistance
    • Livermore DM. β-lactamases in laboratory and clinical resistance. Clin Microbiol Rev 1995; 8:557-84.
    • (1995) Clin Microbiol Rev , vol.8 , pp. 557-584
    • Livermore, D.M.1
  • 64
  • 65
    • 0027313340 scopus 로고
    • OXA-11, an extended-spectrum variant of OXA-10 (PSE-2) β-lactamase from Pseudomonas aeruginosa
    • Hall LM, Livermore DM, Gur D, Akova M, Akalin HE. OXA-11, an extended-spectrum variant of OXA-10 (PSE-2) β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 1993; 37:1637-44.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 1637-1644
    • Hall, L.M.1    Livermore, D.M.2    Gur, D.3    Akova, M.4    Akalin, H.E.5
  • 66
    • 0031728937 scopus 로고    scopus 로고
    • OXA-16, a further extended-spectrum variant of OXA-10 β-lactamase, from two Pseudomonas aeruginosa isolates
    • Danel F, Hall LM, Gur D, Livermore DM. OXA-16, a further extended-spectrum variant of OXA-10 β-lactamase, from two Pseudomonas aeruginosa isolates. Antimicrob Agents Chemother 1998; 42: 3117-22.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 3117-3122
    • Danel, F.1    Hall, L.M.2    Gur, D.3    Livermore, D.M.4
  • 67
    • 0031787913 scopus 로고    scopus 로고
    • Novel OXA-10-derived extended-spectrum β-lactamases selected in vivo or in vitro
    • Mugnier P, Casin I, Bouthors AT, Collatz E. Novel OXA-10-derived extended-spectrum β-lactamases selected in vivo or in vitro. Antimicrob Agents Chemother 1998; 42:3113-6.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 3113-3116
    • Mugnier, P.1    Casin, I.2    Bouthors, A.T.3    Collatz, E.4
  • 68
    • 0031977178 scopus 로고    scopus 로고
    • Carbapenems as inhibitors of OXA-13, a novel, integron-encoded β-lactamase in Pseudomonas aeruginosa
    • Mugnier P, Podglajen I, Goldstein FW, Collatz E. Carbapenems as inhibitors of OXA-13, a novel, integron-encoded β-lactamase in Pseudomonas aeruginosa. Microbiology 1998; 144:1021-31.
    • (1998) Microbiology , vol.144 , pp. 1021-1031
    • Mugnier, P.1    Podglajen, I.2    Goldstein, F.W.3    Collatz, E.4
  • 69
    • 0030815586 scopus 로고    scopus 로고
    • OXA-18, a class D clavulanic acid-inhibited extended-spectrum β-lactamase from Pseudomonas aeruginosa
    • Philippon LN, Naas T, Bouthors AT, Barakett V, Nordmann P. OXA-18, a class D clavulanic acid-inhibited extended-spectrum β-lactamase from Pseudomonas aeruginosa. Antimicrob Agents Chemother 1997; 41:2188-95.
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 2188-2195
    • Philippon, L.N.1    Naas, T.2    Bouthors, A.T.3    Barakett, V.4    Nordmann, P.5
  • 73
    • 0032756334 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamase TEM-4 in Pseudomonas aeruginosa
    • Poirel L, Ronco E, Naas T, Nordmann P. Extended-spectrum β-lactamase TEM-4 in Pseudomonas aeruginosa. Clin Microbiol Infect 1999; 5:651-2.
    • (1999) Clin Microbiol Infect , vol.5 , pp. 651-652
    • Poirel, L.1    Ronco, E.2    Naas, T.3    Nordmann, P.4
  • 74
    • 0036840608 scopus 로고    scopus 로고
    • Clinical strain of Pseudomonas aeruginosa carrying a blaTEM-21 gene located on a chromosomal interrupted TnA type transposon
    • Dubois V, Arpin C, Noury P, Quentin C. Clinical strain of Pseudomonas aeruginosa carrying a blaTEM-21 gene located on a chromosomal interrupted TnA type transposon. Antimicrob Agents Chemother 2002; 46:3624-6.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3624-3626
    • Dubois, V.1    Arpin, C.2    Noury, P.3    Quentin, C.4
  • 75
    • 0033987114 scopus 로고    scopus 로고
    • Production of a TEM-24 plasmid-mediated extended-spectrum β-lactamase by a clinical isolate of Pseudomonas aeruginosa
    • Marchandin H, Jean-Pierre H, De Champs C, et al. Production of a TEM-24 plasmid-mediated extended-spectrum β-lactamase by a clinical isolate of Pseudomonas aeruginosa. Antimicrob Agents Chemother 2000; 44:213-6.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 213-216
    • Marchandin, H.1    Jean-Pierre, H.2    De Champs, C.3
  • 77
    • 0035655141 scopus 로고    scopus 로고
    • SHV-12, SHV-5, SHV-2a, and VEB-1 extended-spectrum β-lactamases in gram-negative bacteria isolated in a university hospital in Thailand
    • Chanawong A, M'Zali FH, Heritage J, Lulitanond A, Hawkey PM. SHV-12, SHV-5, SHV-2a, and VEB-1 extended-spectrum β-lactamases in gram-negative bacteria isolated in a university hospital in Thailand. J Antimicrob Chemother 2001; 48:839-52.
    • (2001) J Antimicrob Chemother , vol.48 , pp. 839-852
    • Chanawong, A.1    M'Zali, F.H.2    Heritage, J.3    Lulitanond, A.4    Hawkey, P.M.5
  • 78
    • 0242322614 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases in Klebsiella pneumoniae bloodstream isolates from seven countries: Dominance and widespread prevalence of SHV- and CTX-M-type β-lactamases
    • Paterson DL, Hujer KM, Hujer AM, et al. Extended-spectrum β-lactamases in Klebsiella pneumoniae bloodstream isolates from seven countries: dominance and widespread prevalence of SHV- and CTX-M-type β-lactamases. Antimicrob Agents Chemother 2003; 47:3554-60.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3554-3560
    • Paterson, D.L.1    Hujer, K.M.2    Hujer, A.M.3
  • 80
    • 0028032168 scopus 로고
    • Sequence analysis of PER-1 extended-spectrum β-lactamase from Pseudomonas aeruginosa and comparison with class a β-lactamases
    • Nordmann P, Naas T. Sequence analysis of PER-1 extended-spectrum β-lactamase from Pseudomonas aeruginosa and comparison with class A β-lactamases. Antimicrob Agents Chemother 1994; 38:104-14.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 104-114
    • Nordmann, P.1    Naas, T.2
  • 82
    • 0036720785 scopus 로고    scopus 로고
    • Prospective survey of β-lactamases produced by ceftazidime-resistant Pseudomonas aeruginosa isolated in a French hospital in 2000
    • De Champs C, Poirel L, Bonnet R, et al. Prospective survey of β-lactamases produced by ceftazidime-resistant Pseudomonas aeruginosa isolated in a French hospital in 2000. Antimicrob Agents Chemother 2002; 46:3031-4.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3031-3034
    • De Champs, C.1    Poirel, L.2    Bonnet, R.3
  • 83
    • 0035015071 scopus 로고    scopus 로고
    • Dynamics of a nosocomial outbreak of multidrug-resistant Pseudomonas aeruginosa producing the PER-1 extended-spectrum β-lactamase
    • Luzzaro F, Mantengoli E, Perilli M, et al. Dynamics of a nosocomial outbreak of multidrug-resistant Pseudomonas aeruginosa producing the PER-1 extended-spectrum β-lactamase. J Clin Microbiol 2001; 39:1865-70.
    • (2001) J Clin Microbiol , vol.39 , pp. 1865-1870
    • Luzzaro, F.1    Mantengoli, E.2    Perilli, M.3
  • 84
    • 0035205213 scopus 로고    scopus 로고
    • Multidrug-resistant Pseudomonas aeruginosa producing PER-1 extended-spectrum serine-β-lactamase and VIM-2 metallo-β-lactamase
    • Docquier JD, Luzzaro F, Amicosante G, Toniolo A, Rossolini GM. Multidrug-resistant Pseudomonas aeruginosa producing PER-1 extended-spectrum serine-β-lactamase and VIM-2 metallo-β-lactamase. Emerg Infect Dis 2001; 7:910-1.
    • (2001) Emerg Infect Dis , vol.7 , pp. 910-911
    • Docquier, J.D.1    Luzzaro, F.2    Amicosante, G.3    Toniolo, A.4    Rossolini, G.M.5
  • 85
    • 33646270908 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa bloodstream infections: Risk factors and treatment outcome related to expression of the PER-1 extended-spectrum beta-lactamase
    • Endimiani A, Luzzaro F, Pini B, Amicosante G, Rossolini GM, Toniolo AQ. Pseudomonas aeruginosa bloodstream infections: risk factors and treatment outcome related to expression of the PER-1 extended-spectrum beta-lactamase. BMC Infect Dis 2006; 6:52.
    • (2006) BMC Infect Dis , vol.6 , pp. 52
    • Endimiani, A.1    Luzzaro, F.2    Pini, B.3    Amicosante, G.4    Rossolini, G.M.5    Toniolo, A.Q.6
  • 86
    • 0032738553 scopus 로고    scopus 로고
    • Molecular characterisation of In51, a class 1 integron containing a novel aminoglycoside adenylyltransferase gene cassette, aadA6, in Pseudomonas aeruginosa
    • Naas T, Poirel L, Nordmann P. Molecular characterisation of In51, a class 1 integron containing a novel aminoglycoside adenylyltransferase gene cassette, aadA6, in Pseudomonas aeruginosa. Biochim Biophys Acta 1999; 1489:445-51.
    • (1999) Biochim Biophys Acta , vol.1489 , pp. 445-451
    • Naas, T.1    Poirel, L.2    Nordmann, P.3
  • 87
    • 0036498815 scopus 로고    scopus 로고
    • Nosocomial spread of the integron-located VEB-1-like cassette encoding an extended-spectrum β-lactamase in Pseudomonas aeruginosa in Thailand
    • Girlich D, Naas T, Leelaporn A, Poirel L, Fennewald M, Nordmann P. Nosocomial spread of the integron-located VEB-1-like cassette encoding an extended-spectrum β-lactamase in Pseudomonas aeruginosa in Thailand. Clin Infect Dis 2002; 34:603-11.
    • (2002) Clin Infect Dis , vol.34 , pp. 603-611
    • Girlich, D.1    Naas, T.2    Leelaporn, A.3    Poirel, L.4    Fennewald, M.5    Nordmann, P.6
  • 91
    • 0036125248 scopus 로고    scopus 로고
    • A nosocomial outbreak of Pseudomonas aeruginosa isolates expressing the extended-spectrum β-lactamase GES-2 in South Africa
    • Poirel L, Weldhagen GF, De Champs C, Nordmann P. A nosocomial outbreak of Pseudomonas aeruginosa isolates expressing the extended-spectrum β-lactamase GES-2 in South Africa. J Antimicrob Chemother 2002; 49:561-5.
    • (2002) J Antimicrob Chemother , vol.49 , pp. 561-565
    • Poirel, L.1    Weldhagen, G.F.2    De Champs, C.3    Nordmann, P.4
  • 92
    • 0035178826 scopus 로고    scopus 로고
    • An integron-assodated β-lactamase (IBC-2) from Pseudomonas aeruginosa is a variant of the extended-spectrum β-lactamase IBC-1
    • Mavroidi A, Tzelepi E, Tsakris A, Miriagou V, Sofianou D, Tzouvelekis LS. An integron-assodated β-lactamase (IBC-2) from Pseudomonas aeruginosa is a variant of the extended-spectrum β-lactamase IBC-1. J Antimicrob Chemother 2001; 48:627-30.
    • (2001) J Antimicrob Chemother , vol.48 , pp. 627-630
    • Mavroidi, A.1    Tzelepi, E.2    Tsakris, A.3    Miriagou, V.4    Sofianou, D.5    Tzouvelekis, L.S.6
  • 93
    • 0036592476 scopus 로고    scopus 로고
    • Emerging carbapenemases in gram-negative aerobes
    • Nordmann P, Poirel L. Emerging carbapenemases in gram-negative aerobes. Clin Microbiol Infect 2002; 8:321-31.
    • (2002) Clin Microbiol Infect , vol.8 , pp. 321-331
    • Nordmann, P.1    Poirel, L.2
  • 94
    • 0036848246 scopus 로고    scopus 로고
    • Molecular characterization of SPM-1, a novel metallo-β-lactamase isolated in Latin America: Report from the SENTRY antimicrobial surveillance programme
    • Toleman MA, Simm AM, Murphy TA, et al. Molecular characterization of SPM-1, a novel metallo-β-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme. J Antimicrob Chemother 2002; 50:673-9.
    • (2002) J Antimicrob Chemother , vol.50 , pp. 673-679
    • Toleman, M.A.1    Simm, A.M.2    Murphy, T.A.3
  • 95
    • 0037310952 scopus 로고    scopus 로고
    • Biochemical characterization of the acquired metallo-β-lactamase SPM-1 from Pseudomonas aeruginosa
    • Murphy TA, Simm AM, Toleman MA, Jones RN, Walsh TR. Biochemical characterization of the acquired metallo-β-lactamase SPM-1 from Pseudomonas aeruginosa. Antimicrob Agents Chemother 2003; 47:582-7.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 582-587
    • Murphy, T.A.1    Simm, A.M.2    Toleman, M.A.3    Jones, R.N.4    Walsh, T.R.5
  • 96
    • 0027957461 scopus 로고
    • Molecular characterization of an enterobacterial metallo β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance
    • Osano E, Arakawa Y, Wacharotayankun R, et al. Molecular characterization of an enterobacterial metallo β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob Agents Chemother 1994; 38:71-8.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 71-78
    • Osano, E.1    Arakawa, Y.2    Wacharotayankun, R.3
  • 97
    • 0030071472 scopus 로고    scopus 로고
    • Multifocal outbreaks of metallo-β-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum β-lactams, including carbapenems
    • Senda K, Arakawa Y, Nakashima K, et al. Multifocal outbreaks of metallo-β-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum β-lactams, including carbapenems. Antimicrob Agents Chemother 1996; 40:349-53.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 349-353
    • Senda, K.1    Arakawa, Y.2    Nakashima, K.3
  • 98
    • 0038234897 scopus 로고    scopus 로고
    • Clinical and bacteriological characteristics of IMF-type metallo-β-lactamase-producing Pseudomonas aeruginosa
    • Hirakata Y, Yamaguchi T, Nakano M, et al. Clinical and bacteriological characteristics of IMF-type metallo-β-lactamase-producing Pseudomonas aeruginosa. Clin Infect Dis 2003; 37:26-32.
    • (2003) Clin Infect Dis , vol.37 , pp. 26-32
    • Hirakata, Y.1    Yamaguchi, T.2    Nakano, M.3
  • 101
    • 0141997753 scopus 로고    scopus 로고
    • IMP-13, harboured by a novel Tn5051-type transposon disseminating carbapenemase genes in Europe: Report from the SENTRY worldwide antimicrobial surveillance programme
    • IMP-13, harboured by a novel Tn5051-type transposon disseminating carbapenemase genes in Europe: report from the SENTRY worldwide antimicrobial surveillance programme. J Antimicrob Chemother 2003; 52:583-90.
    • (2003) J Antimicrob Chemother , vol.52 , pp. 583-590
    • Toleman, M.A.1    Biedenbach, D.2    Bennett, D.3    Jones, R.N.4    Walsh, T.R.5
  • 102
    • 0034458398 scopus 로고    scopus 로고
    • Hospital outbreak of carbapenem-resistant Pseudomonas aeruginosa producing VIM-1, a novel transferable metallo-β-lactamase
    • Cornaglia G, Mazzariol A, Lauretti L, Rossolini GM, Fontana R. Hospital outbreak of carbapenem-resistant Pseudomonas aeruginosa producing VIM-1, a novel transferable metallo-β-lactamase. Clin Infect Dis 2000; 31:1119-25.
    • (2000) Clin Infect Dis , vol.31 , pp. 1119-1125
    • Cornaglia, G.1    Mazzariol, A.2    Lauretti, L.3    Rossolini, G.M.4    Fontana, R.5
  • 103
    • 0034088144 scopus 로고    scopus 로고
    • Outbreak of infections caused by Pseudomonas aeruginosa producing VIM-1 carbapenemase in Greece
    • Tsakris A, Pournaras S, Woodford N, et al. Outbreak of infections caused by Pseudomonas aeruginosa producing VIM-1 carbapenemase in Greece. J Clin Microbiol 2000; 38:1290-2.
    • (2000) J Clin Microbiol , vol.38 , pp. 1290-1292
    • Tsakris, A.1    Pournaras, S.2    Woodford, N.3
  • 104
    • 0034023159 scopus 로고    scopus 로고
    • Characterization of VIM-2, a carbapenem-hydrolyzing metallo-β- lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France
    • Poirel L, Naas T, Nicolas D, et al. Characterization of VIM-2, a carbapenem-hydrolyzing metallo-β-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France. Antimicrob Agents Chemother 2000; 44:891-7.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 891-897
    • Poirel, L.1    Naas, T.2    Nicolas, D.3
  • 107
    • 12244256773 scopus 로고    scopus 로고
    • Spread of integron-associated VIM-type metallo-β-lactamase genes among imipenem-nonsusceptible Pseudomonas aeruginosa strains in Greek hospitals
    • Giakkoupi P, Petrikkos G, Tzouvelekis LS, Tsonas S, Legakis NJ, Vatopoulos AC. Spread of integron-associated VIM-type metallo-β-lactamase genes among imipenem-nonsusceptible Pseudomonas aeruginosa strains in Greek hospitals. J Clin Microbiol 2003; 41:822-5.
    • (2003) J Clin Microbiol , vol.41 , pp. 822-825
    • Giakkoupi, P.1    Petrikkos, G.2    Tzouvelekis, L.S.3    Tsonas, S.4    Legakis, N.J.5    Vatopoulos, A.C.6
  • 109
    • 0042626513 scopus 로고    scopus 로고
    • Carbapenem-resistant Pseudomonas aeruginosa carrying VIM-2 metallo-β-lactamase determinants, Croatia
    • Sardelic S, Pallecchi L, Punda-Polic V, Rossolini GM. Carbapenem-resistant Pseudomonas aeruginosa carrying VIM-2 metallo-β- lactamase determinants, Croatia. Emerg Infect Dis 2003; 9:1022-3.
    • (2003) Emerg Infect Dis , vol.9 , pp. 1022-1023
    • Sardelic, S.1    Pallecchi, L.2    Punda-Polic, V.3    Rossolini, G.M.4
  • 110
    • 0038798564 scopus 로고    scopus 로고
    • Prevalence of metallo-β-lactamase among Pseudomonas aeruginosa and Acinetobacter baumannii in a Korean university hospital and comparison of screening methods for detecting metallo-β-lactamase
    • Oh EJ, Lee S, Park YJ, et al. Prevalence of metallo-β-lactamase among Pseudomonas aeruginosa and Acinetobacter baumannii in a Korean university hospital and comparison of screening methods for detecting metallo-β- lactamase. J Microbiol Methods 2003; 54:411-8.
    • (2003) J Microbiol Methods , vol.54 , pp. 411-418
    • Oh, E.J.1    Lee, S.2    Park, Y.J.3
  • 111
    • 0036211721 scopus 로고    scopus 로고
    • VIM-2 cassette-containing novel integrons in metallo-β-lactamase-producing Pseudomonas aeruginosa and Pseudomonas putida isolates disseminated in a Korean hospital
    • VIM-2 cassette-containing novel integrons in metallo-β-lactamase-producing Pseudomonas aeruginosa and Pseudomonas putida isolates disseminated in a Korean hospital. Antimicrob Agents Chemother 2002; 46:1053-8.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1053-1058
    • Lee, K.1    Lim, J.B.2    Yum, J.H.3
  • 112
    • 0038386534 scopus 로고    scopus 로고
    • VIM- and IMF-type metallo-β-lactamase-producing Pseudomonas spp. and Acinetobacter spp. in Korean hospitals
    • Lee K, Lee WG, Uh Y, Ha GY, Cho J, Chong Y. VIM- and IMF-type metallo-β-lactamase-producing Pseudomonas spp. and Acinetobacter spp. in Korean hospitals. Emerg Infect Dis 2003; 9:868-71.
    • (2003) Emerg Infect Dis , vol.9 , pp. 868-871
    • Lee, K.1    Lee, W.G.2    Uh, Y.3    Ha, G.Y.4    Cho, J.5    Chong, Y.6
  • 113
    • 0034913590 scopus 로고    scopus 로고
    • Metallo-β-lactamases in clinical Pseudomonas isolates in Taiwan and identification of VIM-3, a novel variant of the VIM-2 enzyme
    • Yan JJ, Hsueh PR, Ko WC, et al. Metallo-β-lactamases in clinical Pseudomonas isolates in Taiwan and identification of VIM-3, a novel variant of the VIM-2 enzyme. Antimicrob Agents Chemother 2001; 45:2224-8.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 2224-2228
    • Yan, J.J.1    Hsueh, P.R.2    Ko, W.C.3
  • 114
    • 0347480118 scopus 로고    scopus 로고
    • PCR typing of genetic determinants for metallo-β-lactamases and integrases carried by gram-negative bacteria isolated in Japan, with focus on the class 3 integron
    • Shibata N, Doi Y, Yamane K, et al. PCR typing of genetic determinants for metallo-β-lactamases and integrases carried by gram-negative bacteria isolated in Japan, with focus on the class 3 integron. J Clin Microbiol 2003; 41:5407-13.
    • (2003) J Clin Microbiol , vol.41 , pp. 5407-5413
    • Shibata, N.1    Doi, Y.2    Yamane, K.3
  • 115
    • 23044462515 scopus 로고    scopus 로고
    • First nosocomial outbreak of Pseudomonas aeruginosa producing an integron-borne metallo-β-lactamase (VIM-2) in the United States
    • Lolans K, Queenan AM, Bush K, Sahud A, Quinn JP. First nosocomial outbreak of Pseudomonas aeruginosa producing an integron-borne metallo-β-lactamase (VIM-2) in the United States. Antimicrob Agents Chemother 2005; 49:3538-40.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3538-3540
    • Lolans, K.1    Queenan, A.M.2    Bush, K.3    Sahud, A.4    Quinn, J.P.5
  • 116
    • 0026730399 scopus 로고
    • Interplay of impermeability and chromosomal β-lactamase activity in imipenem-resistant Pseudomonas aeruginosa
    • Livermore DM. Interplay of impermeability and chromosomal β-lactamase activity in imipenem-resistant Pseudomonas aeruginosa. Antimicrob Agents Chemother 1992; 36:2046-8.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 2046-2048
    • Livermore, D.M.1
  • 117
    • 0037599294 scopus 로고    scopus 로고
    • Characterization of Pseudomonas aeruginosa isolates from patients with urinary tract infections during antibiotic therapy
    • Horii T, Muramatsu H, Morita M, Maekawa M. Characterization of Pseudomonas aeruginosa isolates from patients with urinary tract infections during antibiotic therapy. Microb Drug Resist 2003; 9:223-9.
    • (2003) Microb Drug Resist , vol.9 , pp. 223-229
    • Horii, T.1    Muramatsu, H.2    Morita, M.3    Maekawa, M.4
  • 118
    • 10744230588 scopus 로고    scopus 로고
    • Cefepime versus imipenem-cilastatin for treatment of nosocomial pneumonia in intensive care unit patients: A multicenter, evaluator-blind, prospective, randomized study
    • Zanetti G, Bally F, Greub G, et al. Cefepime versus imipenem-cilastatin for treatment of nosocomial pneumonia in intensive care unit patients: a multicenter, evaluator-blind, prospective, randomized study. Antimicrob Agents Chemother 2003; 47:3442-7.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3442-3447
    • Zanetti, G.1    Bally, F.2    Greub, G.3
  • 119
    • 0033059706 scopus 로고    scopus 로고
    • Emergence of antibiotic-resistant Pseudomonas aeruginosa: Comparison of risks associated with different antipseudomonal agents
    • Carmeli Y, Troillet N, Eliopoulos GM, Samore MH. Emergence of antibiotic-resistant Pseudomonas aeruginosa: comparison of risks associated with different antipseudomonal agents. Antimicrob Agents Chemother 1999; 43:1379-82.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1379-1382
    • Carmeli, Y.1    Troillet, N.2    Eliopoulos, G.M.3    Samore, M.H.4
  • 120
    • 0031724015 scopus 로고    scopus 로고
    • Prospective randomized com-parison of imipenem-cilastatin and piperacillin-tazobactam in nosocomial pneumonia or peritonitis
    • Jaccard C, Troillet N, Harbarth S, et al. Prospective randomized com-parison of imipenem-cilastatin and piperacillin-tazobactam in nosocomial pneumonia or peritonitis. Antimicrob Agents Chemother 1998; 42:2966-72.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 2966-2972
    • Jaccard, C.1    Troillet, N.2    Harbarth, S.3
  • 121
    • 0028287227 scopus 로고
    • Prospective randomized comparison of imipenem monotherapy with imipenem plus netilmicin for treatment of severe infections in nonneutropenic patients
    • Cometta A, Baumgartner JD, Lew D, et al. Prospective randomized comparison of imipenem monotherapy with imipenem plus netilmicin for treatment of severe infections in nonneutropenic patients. Antimicrob Agents Chemother 1994; 38:1309-13.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 1309-1313
    • Cometta, A.1    Baumgartner, J.D.2    Lew, D.3
  • 122
    • 0031021201 scopus 로고    scopus 로고
    • The most frequent amino-glycoside resistance mechanisms-changes with time and geographic area: A reflection of aminoglycoside usage patterns?
    • Aminoglycoside Resistance Study Groups
    • Miller GH, Sabatelli FJ, Hare RS, et al. The most frequent amino-glycoside resistance mechanisms-changes with time and geographic area: a reflection of aminoglycoside usage patterns? Aminoglycoside Resistance Study Groups. Clin Infect Dis 1997; 24(Suppl 1):S46-62.
    • (1997) Clin Infect Dis , vol.24 , Issue.SUPPL. 1
    • Miller, G.H.1    Sabatelli, F.J.2    Hare, R.S.3
  • 123
  • 124
    • 0027290638 scopus 로고
    • Serotypes and extended spectrum β-lactam resistance in aminoglycoside resistant Pseudomonas aeruginosa isolates from two Belgian general hospitals: A seven year study
    • Vanhoof R, Godard C, Nulens E, et al. Serotypes and extended spectrum β-lactam resistance in aminoglycoside resistant Pseudomonas aeruginosa isolates from two Belgian general hospitals: a seven year study. J Hosp Infect 1993; 24:129-38.
    • (1993) J Hosp Infect , vol.24 , pp. 129-138
    • Vanhoof, R.1    Godard, C.2    Nulens, E.3
  • 126
    • 0036498656 scopus 로고    scopus 로고
    • Multiple mechanisms of antimicrobial resistance in Pseudomonas aeruginosa: Our worst nightmare?
    • Livermore DM. Multiple mechanisms of antimicrobial resistance in Pseudomonas aeruginosa: our worst nightmare? Clin Infect Dis 2002; 34:634-40.
    • (2002) Clin Infect Dis , vol.34 , pp. 634-640
    • Livermore, D.M.1
  • 127
    • 0032959773 scopus 로고    scopus 로고
    • Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids
    • Ochs MM, McCusker MP, Bains M, Hancock RE. Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids. Antimicrob Agents Chemother 1999; 43:1085-90.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1085-1090
    • Ochs, M.M.1    McCusker, M.P.2    Bains, M.3    Hancock, R.E.4
  • 128
    • 0036785981 scopus 로고    scopus 로고
    • Transmission of colistin-resistant Pseudomonas aeruginosa between patients attending a pediatric cystic fibrosis center
    • Denton M, Kerr K, Mooney L, et al. Transmission of colistin-resistant Pseudomonas aeruginosa between patients attending a pediatric cystic fibrosis center. Pediatr Pulmonol 2002; 34:257-61.
    • (2002) Pediatr Pulmonol , vol.34 , pp. 257-261
    • Denton, M.1    Kerr, K.2    Mooney, L.3
  • 129
    • 14944344361 scopus 로고    scopus 로고
    • Molecular characterization of an epidemic clone of panantibiotic- resistant Pseudomonas aeruginosa
    • Deplano A, Denis O, Poirel L, et al. Molecular characterization of an epidemic clone of panantibiotic-resistant Pseudomonas aeruginosa. J Clin Microbiol 2005; 43:1198-204.
    • (2005) J Clin Microbiol , vol.43 , pp. 1198-1204
    • Deplano, A.1    Denis, O.2    Poirel, L.3
  • 131
    • 0026347455 scopus 로고
    • Mechanisms of resistance to β-lactam antibiotics in Acinetobacter calcoaceticus
    • Obara M, Nakae T. Mechanisms of resistance to β-lactam antibiotics in Acinetobacter calcoaceticus. J Antimicrob Chemother 1991; 28: 791-800.
    • (1991) J Antimicrob Chemother , vol.28 , pp. 791-800
    • Obara, M.1    Nakae, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.