메뉴 건너뛰기




Volumn 18, Issue 2, 2005, Pages 306-325

Metallo-β-lactamases: The quiet before the storm?

Author keywords

[No Author keywords available]

Indexed keywords

1BETA METHYL CARBAPENEM DERIVATIVE; AMINOGLYCOSIDE ANTIBIOTIC AGENT; AMPICILLIN; AZLOCILLIN; AZTREONAM; BACTERIAL ENZYME; BETA LACTAM; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; BIPHENYL TETRAZOLE; CARBENICILLIN; CEFALOTIN; CEFEPIME; CEFOTAXIME; CEFOXITIN; CEFTAZIDIME; CEFUROXIME; CLAVULANIC ACID; CYSTEINE DERIVATIVE; IMIPENEM; LATAMOXEF; MEROPENEM; METALLO BETA LACTAMASE; METALLO BETA LACTAMASE INHIBITOR; NITROCEFIN; PENICILLIN DERIVATIVE; PENICILLIN G; PIPERACILLIN; SULFONYLHYDRAZONE; TAZOBACTAM; THIOESTER; THIOL DERIVATIVE; THIOXOCEPHALOSPORIN; TICARCILLIN; TRICYCLIC AROMATIC COMPOUND; TRIFLUOROMETHYL ALCOHOL; UNCLASSIFIED DRUG;

EID: 17444363393     PISSN: 08938512     EISSN: None     Source Type: Journal    
DOI: 10.1128/CMR.18.2.306-325.2005     Document Type: Review
Times cited : (1278)

References (203)
  • 1
    • 0035143274 scopus 로고    scopus 로고
    • Characterization of OXA-25, OXA-26, and OXA-27, molecular class D β-lactamases associated with carbapenem resistance in clinical isolates of Acinetobacter baumannii
    • Afzal-Shah, M., N. Woodford, and D. M. Livermore. 2001. Characterization of OXA-25, OXA-26, and OXA-27, molecular class D β-lactamases associated with carbapenem resistance in clinical isolates of Acinetobacter baumannii. Antimicrob. Agents Chemother. 45:583-588.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 583-588
    • Afzal-Shah, M.1    Woodford, N.2    Livermore, D.M.3
  • 3
    • 0038262635 scopus 로고    scopus 로고
    • Increasing prevalence of antimicrobial resistance among Pseudomonas aeruginosa isolates in Latin American medical centres: 5 Year report of the SENTRY Antimicrobial Surveillance Program (1997-2001)
    • Andrade, S. S., R. N. Jones, A. C. Gales, and H. S. Sader. 2003. Increasing prevalence of antimicrobial resistance among Pseudomonas aeruginosa isolates in Latin American medical centres: 5 year report of the SENTRY Antimicrobial Surveillance Program (1997-2001). J. Antimicrob. Chemother. 52:140-U7.
    • (2003) J. Antimicrob. Chemother. , vol.52
    • Andrade, S.S.1    Jones, R.N.2    Gales, A.C.3    Sader, H.S.4
  • 6
    • 0033986661 scopus 로고    scopus 로고
    • Convenient test for screening metallo-β-lactamase-producing gram-negative bacteria by using thiol compounds
    • Arakawa, Y., N. Shibata, K. Shibayama, H. Kurokawa, T. Yagi, H. Fujiwara, and M. Goto. 2000. Convenient test for screening metallo-β-lactamase- producing gram-negative bacteria by using thiol compounds. J. Clin. Microbiol. 38:40-43.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 40-43
    • Arakawa, Y.1    Shibata, N.2    Shibayama, K.3    Kurokawa, H.4    Yagi, T.5    Fujiwara, H.6    Goto, M.7
  • 7
    • 0035144769 scopus 로고    scopus 로고
    • Plasmid location and molecular heterogeneity of the L1 and L2 β-lactamase genes of Stenotrophomonas maltophilia
    • Avison, M. B., C. S. Higgins, C. J. von Heldreich, P. M. Bennett, and T. R. Walsh. 2001. Plasmid location and molecular heterogeneity of the L1 and L2 β-lactamase genes of Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 45:413-419.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 413-419
    • Avison, M.B.1    Higgins, C.S.2    Von Heldreich, C.J.3    Bennett, P.M.4    Walsh, T.R.5
  • 9
    • 0345827436 scopus 로고    scopus 로고
    • SOS response promotes horizontal dissemination of antibiotic resistance genes
    • Beaber, J. W., B. Hochhut, and M. K. Waldor. 2004. SOS response promotes horizontal dissemination of antibiotic resistance genes. Nature 427:72-74.
    • (2004) Nature , vol.427 , pp. 72-74
    • Beaber, J.W.1    Hochhut, B.2    Waldor, M.K.3
  • 10
    • 0345471398 scopus 로고    scopus 로고
    • Molecular characterization of a carbapcnem-hydrolyzing β-lactamase from Chryseobacterium (Flavobacterium) indologenes
    • Bellais, S., S. Leotard, L. Poirel, T. Naas, and P. Nordmann. 1999. Molecular characterization of a carbapcnem-hydrolyzing β-lactamase from Chryseobacterium (Flavobacterium) indologenes. FEMS Microbiol. Lett. 171:127-132.
    • (1999) FEMS Microbiol. Lett. , vol.171 , pp. 127-132
    • Bellais, S.1    Leotard, S.2    Poirel, L.3    Naas, T.4    Nordmann, P.5
  • 11
    • 0036090615 scopus 로고    scopus 로고
    • Efficacy of β-lactams for treating experimentally induced pneumonia due to a carbapenem-hydrolyzing metallo-β-lactamase-producing strain of Pseudomonas aeruginosa
    • Bellais, S., O. Mimoz, S. Leotard, A. Jacolot, O. Petitjean, and P. Nordmann. 2002. Efficacy of β-lactams for treating experimentally induced pneumonia due to a carbapenem-hydrolyzing metallo-β-lactamase-producing strain of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 46: 2032-2034.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2032-2034
    • Bellais, S.1    Mimoz, O.2    Leotard, S.3    Jacolot, A.4    Petitjean, O.5    Nordmann, P.6
  • 12
    • 0036719608 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of CGB-1, an ambler class B earbapenem-hydrolyzing β-lactamase from Chryseobacterium gleum
    • Bellais, S., T. Naas, and P. Nordmann. 2002. Genetic and biochemical characterization of CGB-1, an ambler class B earbapenem-hydrolyzing β-lactamase from Chryseobacterium gleum. Antimicrob. Agents Chemother. 46: 2791-2796.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2791-2796
    • Bellais, S.1    Naas, T.2    Nordmann, P.3
  • 13
    • 0033752410 scopus 로고    scopus 로고
    • Genetic diversity of carbapenem-hydrolyzing metallo-β-lactamases from Chryseobacterium (Fluvobucterium) indologenes
    • Bellais, S., L. Poirel, S. Leotard, T. Naas, and P. Nordmann. 2000. Genetic diversity of carbapenem-hydrolyzing metallo-β-lactamases from Chryseobacterium (Fluvobucterium) indologenes. Antimicrob. Agents Chemother. 44:3028-3034.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3028-3034
    • Bellais, S.1    Poirel, L.2    Leotard, S.3    Naas, T.4    Nordmann, P.5
  • 14
    • 0032925637 scopus 로고    scopus 로고
    • Integrons and gene cassettes: A genetic construction kit for bacteria
    • Bennett, P. M. 1999. Integrons and gene cassettes: a genetic construction kit for bacteria. J. Antimicrob. Chemother. 43:1-4.
    • (1999) J. Antimicrob. Chemother. , vol.43 , pp. 1-4
    • Bennett, P.M.1
  • 15
    • 0034128893 scopus 로고    scopus 로고
    • The Legionella (Fluoribacter) gormanii metallo-β-lactamase: A new member of the highly divergent lineage of molecular-subclass B3 β-lactamases
    • Boschi, L., P. S. Mercuri, M. L. Riccio, G. Amicosante, M. Galleni, J. M. Frere, and G. M. Rossolini. 2000. The Legionella (Fluoribacter) gormanii metallo-β-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 β-lactamases. Antimicrob. Agents Chemother. 44: 1538-1543.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1538-1543
    • Boschi, L.1    Mercuri, P.S.2    Riccio, M.L.3    Amicosante, G.4    Galleni, M.5    Frere, J.M.6    Rossolini, G.M.7
  • 16
    • 0034077976 scopus 로고    scopus 로고
    • OXA-24, a novel class D β-lactamase with carbapenemase activity in an Acinetobacter baumannii clinical strain
    • Bou, G., A. Oliver, and J. Martinez-Beltran. 2000. OXA-24, a novel class D β-lactamase with carbapenemase activity in an Acinetobacter baumannii clinical strain. Antimicrob. Agents Chemother. 44:1556-1561.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1556-1561
    • Bou, G.1    Oliver, A.2    Martinez-Beltran, J.3
  • 17
    • 0035078014 scopus 로고    scopus 로고
    • Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase
    • Bounaga, S., M. Galleni, A. P. Laws, and M. I. Page. 2001. Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase. Bioorg. Med. Chem. 9:503-510.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 503-510
    • Bounaga, S.1    Galleni, M.2    Laws, A.P.3    Page, M.I.4
  • 18
    • 0032080039 scopus 로고    scopus 로고
    • The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent β-lactamase
    • Bounaga, S., A. P. Laws, M. Galleni, and M. I. Page. 1998. The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent β-lactamase. Biochem. J. 331:703-711.
    • (1998) Biochem. J. , vol.331 , pp. 703-711
    • Bounaga, S.1    Laws, A.P.2    Galleni, M.3    Page, M.I.4
  • 19
    • 0034763241 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases in the 21st century: Characterization, epidemiology, and detection of this important resistance threat
    • Bradford, P. A. 2001. Extended-spectrum β-lactamases in the 21st century: characterization, epidemiology, and detection of this important resistance threat. Clin. Microbiol. Rev. 14:933-951.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 933-951
    • Bradford, P.A.1
  • 20
    • 0032743692 scopus 로고    scopus 로고
    • β-lactamases of increasing clinical importance
    • Bush, K. 1999. β-Lactamases of increasing clinical importance. Curr. Pharm. Des. 5:839-845.
    • (1999) Curr. Pharm. Des. , vol.5 , pp. 839-845
    • Bush, K.1
  • 21
    • 0024536258 scopus 로고
    • Classification of β-lactamases-group-2c, group-2d, group-2e, group-3, and group-4
    • Bush, K. 1989. Classification of β-lactamases-group-2c, group-2d, group-2e, group-3, and group-4. Antimicrob. Agents Chemother. 33:271-276.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 271-276
    • Bush, K.1
  • 22
    • 0031927435 scopus 로고    scopus 로고
    • Metallo-β-lactamases: A class apart
    • Bush, K. 1998. Metallo-β-lactamases: a class apart. Clin. Infect. Dis. 27: S48-53.
    • (1998) Clin. Infect. Dis. , vol.27
    • Bush, K.1
  • 23
    • 0035311003 scopus 로고    scopus 로고
    • New β-lactamases in gram-negative bacteria: Diversity and impact on the selection of antimicrobial therapy
    • Bush, K, 2001. New β-lactamases in gram-negative bacteria: diversity and impact on the selection of antimicrobial therapy. Clin. Infect. Dis. 32:1085-1089.
    • (2001) Clin. Infect. Dis. , vol.32 , pp. 1085-1089
    • Bush, K.1
  • 24
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 30
    • 0037310366 scopus 로고    scopus 로고
    • β-lactamase genes of the penicillin-susceptible Bacillus anthracis Sterne strain
    • Chen, Y. H., J. Succi, F. C. Tenover, and T. M. Koehler. 2003. β-Lactamase genes of the penicillin-susceptible Bacillus anthracis Sterne strain. J. Bacteriol. 185:823-830.
    • (2003) J. Bacteriol. , vol.185 , pp. 823-830
    • Chen, Y.H.1    Succi, J.2    Tenover, F.C.3    Koehler, T.M.4
  • 32
    • 0036886073 scopus 로고    scopus 로고
    • Integron-encoded IntI integrases preferentially recognize the adjacent cognate attl site in recombination with a 59-be site
    • Collis, C. M., M. J. Kim, H. W. Stokes, and R. M. Hall. 2002. Integron-encoded IntI integrases preferentially recognize the adjacent cognate attl site in recombination with a 59-be site. Mol. Microbiol. 46:1415-1427.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1415-1427
    • Collis, C.M.1    Kim, M.J.2    Stokes, H.W.3    Hall, R.M.4
  • 33
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor
    • Concha, N. O., C. A. Janson, P. Rowling, S. Pearson, C. A. Cheever, B. P. Clarke, C. Lewis, M. Galleni, J. M. Frere, D. J. Payne, J. H. Bateson, and S. S. Abdel-Meguid. 2000. Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39:4288-4298.
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3    Pearson, S.4    Cheever, C.A.5    Clarke, B.P.6    Lewis, C.7    Galleni, M.8    Frere, J.M.9    Payne, D.J.10    Bateson, J.H.11    Abdel-Meguid, S.S.12
  • 34
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
    • Concha, N. O., B. A. Rasmussen, K. Bush, and O. Herzberg. 1996. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4:823-836.
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 35
    • 0037636470 scopus 로고    scopus 로고
    • Zinc eluted from siliconized latex urinary catheters decreases OprD expression, causing carbapenem resistance in Pseudomonas aeruginosa
    • Conejo, M. C., I. Garcia, L. Martinez-Martinez, L. Picabea, and A. Pascual. 2003. Zinc eluted from siliconized latex urinary catheters decreases OprD expression, causing carbapenem resistance in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 47:2313-2315.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2313-2315
    • Conejo, M.C.1    Garcia, I.2    Martinez-Martinez, L.3    Picabea, L.4    Pascual, A.5
  • 37
    • 0029808391 scopus 로고    scopus 로고
    • Characterization of the metal-binding sites of the β-lactamase from Bacteroides fragilis
    • Crowder, M. W., Z. Wang, S. L. Franklin, E. P. Zovinka, and S. J. Benkovic. 1996. Characterization of the metal-binding sites of the β-lactamase from Bacteroides fragilis. Biochemistry 35:12126-12132.
    • (1996) Biochemistry , vol.35 , pp. 12126-12132
    • Crowder, M.W.1    Wang, Z.2    Franklin, S.L.3    Zovinka, E.P.4    Benkovic, S.J.5
  • 38
    • 0035839131 scopus 로고    scopus 로고
    • Expansion of the zinc metallo-hydrolase family of the β-lactamase fold
    • Daiyasu, H., K. Osaka, Y. Ishino, and H. Toh. 2001. Expansion of the zinc metallo-hydrolase family of the β-lactamase fold. FEBS Lett. 503:1-6.
    • (2001) FEBS Lett. , vol.503 , pp. 1-6
    • Daiyasu, H.1    Osaka, K.2    Ishino, Y.3    Toh, H.4
  • 40
    • 0032958777 scopus 로고    scopus 로고
    • Emergence of carbapenem-hydrolyzing enzymes in Acinetobacter baumannii clinical isolates
    • Da Silva, G. J., R. Leitao, and L. Peixe. 1999. Emergence of carbapenem-hydrolyzing enzymes in Acinetobacter baumannii clinical isolates. J. Clin. Microbiol. 37:2109-2110.
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 2109-2110
    • Da Silva, G.J.1    Leitao, R.2    Peixe, L.3
  • 44
    • 0032510815 scopus 로고    scopus 로고
    • Unanticipated inhibition of the metallo-β-lactamase from Bacteroides fragilis by 4-morpholine-ethanesulfonic acid (MES): A crystallographic study at 1.85-A resolution
    • Fitzgerald, P. M., J. K. Wu, and J. H. Toney. 1998. Unanticipated inhibition of the metallo-β-lactamase from Bacteroides fragilis by 4-morpholine-ethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution. Biochemistry 37:6791-6800.
    • (1998) Biochemistry , vol.37 , pp. 6791-6800
    • Fitzgerald, P.M.1    Wu, J.K.2    Toney, J.H.3
  • 45
    • 0029019031 scopus 로고
    • β-lactamases and bacterial resistance to antibiotics
    • Frere, J. M. 1995. β-lactamases and bacterial resistance to antibiotics. Mol. Microbiol. 16:385-395.
    • (1995) Mol. Microbiol. , vol.16 , pp. 385-395
    • Frere, J.M.1
  • 46
    • 0141997696 scopus 로고    scopus 로고
    • Dissemination in distinct Brazilian regions of an epidemic carbapenem-resistant Pseudomonas aeruginosa producing SPM metallo-β- lactamase
    • Gales, A. C., L. C. Menezes, S. Silbert, and H. S. Sader. 2003. Dissemination in distinct Brazilian regions of an epidemic carbapenem-resistant Pseudomonas aeruginosa producing SPM metallo-β-lactamase. J. Antimicrob. Chemother. 52:699-702.
    • (2003) J. Antimicrob. Chemother. , vol.52 , pp. 699-702
    • Gales, A.C.1    Menezes, L.C.2    Silbert, S.3    Sader, H.S.4
  • 47
    • 0037309874 scopus 로고    scopus 로고
    • Emergence of an IMP-like metallo-enzyme in an Acinetobacter baumannii clinical strain from a Brazilian teaching hospital
    • Gales, A. C., M. C. Tognim, A. O. Reis, R. N. Jones, and H. S. Sader. 2003. Emergence of an IMP-like metallo-enzyme in an Acinetobacter baumannii clinical strain from a Brazilian teaching hospital. Diagn. Microbiol. Infect. Dis. 45:77-79.
    • (2003) Diagn. Microbiol. Infect. Dis. , vol.45 , pp. 77-79
    • Gales, A.C.1    Tognim, M.C.2    Reis, A.O.3    Jones, R.N.4    Sader, H.S.5
  • 49
    • 10044225894 scopus 로고    scopus 로고
    • A metallo-β-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem
    • Garau, G., C. Bebrone, C. Anne, M. Galleni, J. M. Frere, and O. Dideberg. 2005. A metallo-β-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem. J. Mol. Biol. 345:785-795.
    • (2005) J. Mol. Biol. , vol.345 , pp. 785-795
    • Garau, G.1    Bebrone, C.2    Anne, C.3    Galleni, M.4    Frere, J.M.5    Dideberg, O.6
  • 52
    • 0037462925 scopus 로고    scopus 로고
    • Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-β-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril
    • Garcia-Saez, I., P. S. Mercuri, C. Papamicael, R. Kahn, J. M. Frere, M. Galleni, G. M. Rossolini, and O. Dideberg. 2003. Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-β-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril. J. Mol. Biol. 325:651-660.
    • (2003) J. Mol. Biol. , vol.325 , pp. 651-660
    • Garcia-Saez, I.1    Mercuri, P.S.2    Papamicael, C.3    Kahn, R.4    Frere, J.M.5    Galleni, M.6    Rossolini, G.M.7    Dideberg, O.8
  • 55
    • 0041922481 scopus 로고    scopus 로고
    • VIM-4 in a carbapenem-resistant strain of Pseudomonas aeruginosa isolated in Sweden
    • Giske, C. G., M. Rylander, and G. Kronvall. 2003. VIM-4 in a carbapenem-resistant strain of Pseudomonas aeruginosa isolated in Sweden. Antimicrob. Agents Chemother. 47:3034-3035.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3034-3035
    • Giske, C.G.1    Rylander, M.2    Kronvall, G.3
  • 56
  • 60
    • 0035170847 scopus 로고    scopus 로고
    • Occurrence of a new metallo-β-lactamase IMP-4 carried on a conjugative plasmid in Citrobacter youngae from the People's Republic of China
    • Hawkey, P. M., J. Xiong, H. Ye, H. Li, and F. H. M'Zali. 2001. Occurrence of a new metallo-β-lactamase IMP-4 carried on a conjugative plasmid in Citrobacter youngae from the People's Republic of China. FEMS Microbiol. Lett. 194:53-57.
    • (2001) FEMS Microbiol. Lett. , vol.194 , pp. 53-57
    • Hawkey, P.M.1    Xiong, J.2    Ye, H.3    Li, H.4    M'Zali, F.H.5
  • 61
    • 0037228293 scopus 로고    scopus 로고
    • Genetic and functional analysis of the chromosome-encoded carbapenem-hydrolyzing oxacillinasc OXA-40 of Acinetobacter baumannii
    • Héritier, C., L. Poirel, D. Aubert, and P. Nordmann. 2003. Genetic and functional analysis of the chromosome-encoded carbapenem-hydrolyzing oxacillinasc OXA-40 of Acinetobacter baumannii. Antimicrob. Agents Chemother. 47:268-273.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 268-273
    • Héritier, C.1    Poirel, L.2    Aubert, D.3    Nordmann, P.4
  • 65
    • 0022374336 scopus 로고
    • Cloning and sequencing of the metallothioprotein β-lactamase II gene of Bacillus cerens 569/H in Escherichia coli
    • Hussain, M., A. Carlino, M. J. Madonna, and J. O. Lampen. 1985. Cloning and sequencing of the metallothioprotein β-lactamase II gene of Bacillus cerens 569/H in Escherichia coli. J. Bacteriol. 164:223-229.
    • (1985) J. Bacteriol. , vol.164 , pp. 223-229
    • Hussain, M.1    Carlino, A.2    Madonna, M.J.3    Lampen, J.O.4
  • 67
    • 3042536353 scopus 로고    scopus 로고
    • Antibiotic resistance conferred by a class I integron and SXT constin in Vibrio cholerae O1 strains isolated in Laos
    • Iwanaga, M., C. Toma, T. Miyazato, S. Insisiengmay, N. Nakasone, and M. Ehara. 2004. Antibiotic resistance conferred by a class I integron and SXT constin in Vibrio cholerae O1 strains isolated in Laos. Antimicrob. Agents Chemother. 48:2364-2369.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 2364-2369
    • Iwanaga, M.1    Toma, C.2    Miyazato, T.3    Insisiengmay, S.4    Nakasone, N.5    Ehara, M.6
  • 69
    • 0036096012 scopus 로고    scopus 로고
    • Detection of a variant metallo-β-lactamase, IMP-10, from two unrelated strains of Pseudomonas aeruginosa and alcaligenes xylosoxidans strain
    • Iyobe, S., H. Kusadokoro, A. Takahashi, S. Yomoda, T. Okubo, A. Nakamura, and K. O'Hara. 2002. Detection of a variant metallo-β-lactamase, IMP-10, from two unrelated strains of Pseudomonas aeruginosa and alcaligenes xylosoxidans strain. Antimicrob. Agents Chemother. 46:2014-2016.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2014-2016
    • Iyobe, S.1    Kusadokoro, H.2    Takahashi, A.3    Yomoda, S.4    Okubo, T.5    Nakamura, A.6    O'Hara, K.7
  • 72
    • 3042787722 scopus 로고    scopus 로고
    • Determination of epidemic clonality among multidrug-resistant strains of Acinetobacter spp. and Pseudomonas aeruginosa in the MYSTIC Programme (UAS 1999-2003)
    • Jones, R. N., L. M. Deshpande, T. R. Fritsche, and H. S. Sader. 2004. Determination of epidemic clonality among multidrug-resistant strains of Acinetobacter spp. and Pseudomonas aeruginosa in the MYSTIC Programme (UAS 1999-2003). Diagn. Microbiol. Infect. Dis. 49:211-216.
    • (2004) Diagn. Microbiol. Infect. Dis. , vol.49 , pp. 211-216
    • Jones, R.N.1    Deshpande, L.M.2    Fritsche, T.R.3    Sader, H.S.4
  • 74
    • 0034996244 scopus 로고    scopus 로고
    • Carbapenem-resistant Klebsiella pneumoniae in Singapore producing IMP-1 β-lactamase and lacking an outer membrane protein
    • Koh, T. H., L. H. Sng, G. S. Babini, N. Woodford, D. M. Livermore, and L. M. Hall. 2001. Carbapenem-resistant Klebsiella pneumoniae in Singapore producing IMP-1 β-lactamase and lacking an outer membrane protein. Antimicrob. Agents Chemother. 45:1939-1940.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1939-1940
    • Koh, T.H.1    Sng, L.H.2    Babini, G.S.3    Woodford, N.4    Livermore, D.M.5    Hall, L.M.6
  • 75
    • 2542479968 scopus 로고    scopus 로고
    • IMP-1 and a novel metallo-β-lactamase, VIM-6, in fluorescent pseudomonads isolated in Singapore
    • Koh, T. H., G. C. Y. Wang, and L. H. Sng. 2004. IMP-1 and a novel metallo-β-lactamase, VIM-6, in fluorescent pseudomonads isolated in Singapore. Antimicrob. Agents Chemother. 48:2334-2336.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 2334-2336
    • Koh, T.H.1    Wang, G.C.Y.2    Sng, L.H.3
  • 76
    • 0041322837 scopus 로고    scopus 로고
    • Detection of a metallo-β-lactamase (IMP-1) by fluorescent probes having dansyl and thiol groups
    • Kurosaki, H., H. Yasuzawa, Y. Yamaguchi, W. C. Jin, Y. Arakawa, and M. Goto. 2003. Detection of a metallo-β-lactamase (IMP-1) by fluorescent probes having dansyl and thiol groups. Org. Biomol. Chem. 1:17-20.
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 17-20
    • Kurosaki, H.1    Yasuzawa, H.2    Yamaguchi, Y.3    Jin, W.C.4    Arakawa, Y.5    Goto, M.6
  • 80
    • 0038386534 scopus 로고    scopus 로고
    • VIM- and IMF-type metallo-β-lactamase-producing Pseudomonas spp. and Acinetobacter spp. in Korean hospitals
    • Lee, K., W. G. Lee, Y. Uh, G. Y. Ha, J. Cho, and Y. Chong. 2003. VIM- and IMF-type metallo-β-lactamase-producing Pseudomonas spp. and Acinetobacter spp. in Korean hospitals. Emerg. Infect. Dis. 9:868-871.
    • (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
  • 81
    • 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. 46:1053-1058.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1053-1058
    • Lee, K.1    Lim, J.B.2    Yum, J.H.3    Yong, D.4    Chong, Y.5    Kim, J.M.6    Livermore, D.M.7
  • 83
    • 0023947386 scopus 로고
    • Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 β-lactamase II structural gene
    • Lim, H. M., J. J. Pene, and R. W. Shaw. 1988. Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 β-lactamase II structural gene. J. Bacteriol. 170:2873-2878.
    • (1988) J. Bacteriol. , vol.170 , pp. 2873-2878
    • Lim, H.M.1    Pene, J.J.2    Shaw, R.W.3
  • 84
    • 3843109382 scopus 로고    scopus 로고
    • Use of parenteral colistin for the treatment of serious infection due to antimicrobial-resistant Pseudomonas aeruginosa
    • Linden, P. K., S. Kusne, K. Coley, P. Fontes, D. J. Kramer, and D. Paterson. 2003. Use of parenteral colistin for the treatment of serious infection due to antimicrobial-resistant Pseudomonas aeruginosa. Clin. Infect. Dis. 37:E154-E160.
    • (2003) Clin. Infect. Dis. , vol.37
    • Linden, P.K.1    Kusne, S.2    Coley, K.3    Fontes, P.4    Kramer, D.J.5    Paterson, D.6
  • 85
    • 0036229974 scopus 로고    scopus 로고
    • The impact of carbapenemases on antimicrobial development and therapy
    • Livermore, D. M. 2002. The impact of carbapenemases on antimicrobial development and therapy. Curr. Opin. Investig. Drugs 3:218-224.
    • (2002) Curr. Opin. Investig. Drugs , vol.3 , pp. 218-224
    • Livermore, D.M.1
  • 89
    • 0036841355 scopus 로고    scopus 로고
    • Chromosome-encoded β-lactamases TUS-1 and MUS-1 from Myroides odoratus and Myroides odoratimimus (Formerly Flavobacterium odoratum), new members of the lineage of molecular subclass B1 metalloenzymes
    • Mammeri, H., S. Bellais, and P. Nordmann. 2002. Chromosome-encoded β-lactamases TUS-1 and MUS-1 from Myroides odoratus and Myroides odoratimimus (Formerly Flavobacterium odoratum), new members of the lineage of molecular subclass B1 metalloenzymes. Antimicrob. Agents Chemother. 46:3561-3567.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3561-3567
    • Mammeri, H.1    Bellais, S.2    Nordmann, P.3
  • 92
    • 0025875773 scopus 로고
    • The Aeromonas Hydrophila cphA gene: Molecular heterogeneity among class B metallo-β-lactamases
    • Massidda, O., G. M. Rossolini, and G. Satta. 1991. The Aeromonas Hydrophila cphA gene: molecular heterogeneity among class B metallo-β- lactamases. J. Bacteriol. 173:4611-4617.
    • (1991) J. Bacteriol. , vol.173 , pp. 4611-4617
    • Massidda, O.1    Rossolini, G.M.2    Satta, G.3
  • 94
    • 0033514290 scopus 로고    scopus 로고
    • Kinetic mechanism of metallo-β-lactamase L1 from Stenotrophomonas maltophilia
    • McManus-Munoz, S., and M. W. Crowder. 1999. Kinetic mechanism of metallo-β-lactamase L1 from Stenotrophomonas maltophilia. Biochemistry 38:1547-1553.
    • (1999) Biochemistry , vol.38 , pp. 1547-1553
    • McManus-Munoz, S.1    Crowder, M.W.2
  • 95
    • 0031728459 scopus 로고    scopus 로고
    • A zinc-binding motif conserved in glyoxalase 11, β-lactamase and arylsulfatases
    • Melino, S., C. Capo, B. Dragani, A. Aceto, and R. Petruzzelli. 1998. A zinc-binding motif conserved in glyoxalase 11, β-lactamase and arylsulfatases. Trends Biochem. Sci. 23:381-382.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 381-382
    • Melino, S.1    Capo, C.2    Dragani, B.3    Aceto, A.4    Petruzzelli, R.5
  • 100
    • 0035491150 scopus 로고    scopus 로고
    • β-lactamase-inhibitor combinations in the 21st century: Current agents and new developments
    • Miller, L. A., K. Ratnam, and D. J. Payne. 2001. β-lactamase- inhibitor combinations in the 21st century: current agents and new developments, Curr. Opin. Pharm. 1:451-458.
    • (2001) Curr. Opin. Pharm. , vol.1 , pp. 451-458
    • Miller, L.A.1    Ratnam, K.2    Payne, D.J.3
  • 102
    • 0037310952 scopus 로고    scopus 로고
    • Biochemical characterization of the acquired metallo-β-lactamase SPM-1 from Pseudomonas aeruginosa
    • Murphy, T. A., A. M. Simm, M. A. Toleman, R. N. Jones, and T. R. Walsh. 2003. Biochemical characterization of the acquired metallo-β-lactamase SPM-1 from Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 47: 582-587.
    • (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
  • 103
    • 0037323917 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a carbapenem-hydrolysing β-lactamase from Flavobacterium johnsoniae
    • Naas, T., S. Bellais, and P. Nordmann. 2003. Molecular and biochemical characterization of a carbapenem-hydrolysing β-lactamase from Flavobacterium johnsoniae. J. Antimicrob. Chemother. 51:267-273.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 267-273
    • Naas, T.1    Bellais, S.2    Nordmann, P.3
  • 104
    • 0034051621 scopus 로고    scopus 로고
    • In vitro antibacterial activity and mechanism of action of J.-111,225, a novel 1β-methylcarbapenem, against transferable IMP-1 metallo-β- lactamase producers
    • Nagano, R., Y. Adachi, T. Hashizume, and H. Morishima. 2000. In vitro antibacterial activity and mechanism of action of J.-111,225, a novel 1β-methylcarbapenem, against transferable IMP-1 metallo-β-lactamase producers. J. Antimicrob. Chemother. 45:271-276.
    • (2000) J. Antimicrob. Chemother. , vol.45 , pp. 271-276
    • Nagano, R.1    Adachi, Y.2    Hashizume, T.3    Morishima, H.4
  • 105
    • 0032879868 scopus 로고    scopus 로고
    • Carbapenem derivatives as potential inhibitors of various β-lactamases, including class B metallo-β-lactamases
    • Nagano, R., Y. Adachi, H. Imamura, K. Yamada, T. Hashizume, and H. Morishima. 1999. Carbapenem derivatives as potential inhibitors of various β-lactamases, including class B metallo-β-lactamases. Antimicrob. Agents Chemother. 43:2497-2503.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2497-2503
    • Nagano, R.1    Adachi, Y.2    Imamura, H.3    Yamada, K.4    Hashizume, T.5    Morishima, H.6
  • 106
    • 0037453976 scopus 로고    scopus 로고
    • Antibiotic resistance among gram-negative bacilli in US intensive care units-implications for fluoroquinolone use
    • Neuhauser, M. M., R. A. Weinstein, R. Rydman, L. H. Danziger, G. Karam, and J. P. Quinn. 2003. Antibiotic resistance among gram-negative bacilli in US intensive care units-implications for fluoroquinolone use. JAMA 289: 885-888.
    • (2003) JAMA , vol.289 , pp. 885-888
    • Neuhauser, M.M.1    Weinstein, R.A.2    Rydman, R.3    Danziger, L.H.4    Karam, G.5    Quinn, J.P.6
  • 107
    • 0027193696 scopus 로고
    • Biochemical properties of a carbapenem-hydrolyzing β-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli
    • Nordmann, P., S. Mariotte, T. Naas, R. Labia, and M. H. Nicolas. 1993. Biochemical properties of a carbapenem-hydrolyzing β-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli. Antimicrob. Agents Chemother. 37:939-946.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 939-946
    • Nordmann, P.1    Mariotte, S.2    Naas, T.3    Labia, R.4    Nicolas, M.H.5
  • 108
    • 0036592476 scopus 로고    scopus 로고
    • Emerging carbapenemases in Gram-negative aerobes
    • Nordmann, P., and L. Poirel. 2002. Emerging carbapenemases in Gram-negative aerobes. Clin. Microbiol. Infect. 8:321-331.
    • (2002) Clin. Microbiol. Infect. , vol.8 , pp. 321-331
    • Nordmann, P.1    Poirel, L.2
  • 109
    • 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, E. J., S. Lee, Y. J. Park, J. J. Park, K. Park, S. I. Kim, M. W. Kang, and B. K. Kim. 2003. 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 54:411-418.
    • (2003) J. Microbiol. Methods , vol.54 , pp. 411-418
    • Oh, E.J.1    Lee, S.2    Park, Y.J.3    Park, J.J.4    Park, K.5    Kim, S.I.6    Kang, M.W.7    Kim, B.K.8
  • 110
    • 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., Y. Arakawa, R. Wacharotayankun, M. Ohta, T. Horii, H. Ito, F. Yoshimura, and N. Kato. 1994. Molecular characterization of an enterobacterial metallo-β-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob. Agents Chemother. 38:71-78.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 71-78
    • Osano, E.1    Arakawa, Y.2    Wacharotayankun, R.3    Ohta, M.4    Horii, T.5    Ito, H.6    Yoshimura, F.7    Kato, N.8
  • 111
    • 0032698787 scopus 로고    scopus 로고
    • The reactivity of β-lactams, the mechanism of catalysis and the inhibition of β-lactamases
    • Page, M. I. 1999. The reactivity of β-lactams, the mechanism of catalysis and the inhibition of β-lactamases. Curr. Pharm. Des. 5:895-913.
    • (1999) Curr. Pharm. Des. , vol.5 , pp. 895-913
    • Page, M.I.1
  • 112
    • 0000716627 scopus 로고    scopus 로고
    • Understanding metallo-β-lactamases
    • Page, M. I. 2002. Understanding metallo-β-lactamases. ASM News 68: 217-221.
    • (2002) ASM News , vol.68 , pp. 217-221
    • Page, M.I.1
  • 115
    • 0142245620 scopus 로고    scopus 로고
    • The IS1111 family members IS4321 and 1S5075 have subterminal inverted repeats and target the terminal inverted repeats of Tn21 family transposons
    • Partridge, S. R., and R. M. Hall. 2003. The IS1111 family members IS4321 and 1S5075 have subterminal inverted repeats and target the terminal inverted repeats of Tn21 family transposons. J. Bacteriol. 185:6371-6384.
    • (2003) J. Bacteriol. , vol.185 , pp. 6371-6384
    • Partridge, S.R.1    Hall, R.M.2
  • 117
    • 0027284501 scopus 로고
    • Metallo-β-lactamases - A new therapeutic challenge
    • Payne, D. J. 1993. Metallo-β-lactamases - a new therapeutic challenge. J. Med. Microbiol. 39:93-99.
    • (1993) J. Med. Microbiol. , vol.39 , pp. 93-99
    • Payne, D.J.1
  • 118
  • 121
    • 0033963352 scopus 로고    scopus 로고
    • β-lactamase epidemiology and the utility of established and novel β-lactamase inhibitors
    • Payne, D. J., W. Du, and J. H. Bateson. 2000. β-Lactamase epidemiology and the utility of established and novel β-lactamase inhibitors. Expert Opin. Investig. Drugs 9:247-261.
    • (2000) Expert Opin. Investig. Drugs , vol.9 , pp. 247-261
    • Payne, D.J.1    Du, W.2    Bateson, J.H.3
  • 123
    • 4644356593 scopus 로고    scopus 로고
    • Emergence of IMP-4 metallo-β-lactamase in a clinical isolate from Australia
    • Peleg, A. Y., C. Franklin, J. Bell, and D. W. Spelman. 2004. Emergence of IMP-4 metallo-β-lactamase in a clinical isolate from Australia. J. Antimicrob. Chemother. 54:699-700.
    • (2004) J. Antimicrob. Chemother. , vol.54 , pp. 699-700
    • Peleg, A.Y.1    Franklin, C.2    Bell, J.3    Spelman, D.W.4
  • 124
    • 1542335656 scopus 로고    scopus 로고
    • CzcR-CzcS, a two-component system involved in heavy metal and carbapenem resistance in Pseudomonas aeruginosa. 3
    • Perron, K., O. Caille, C. Rossier, C. van Delden, J. L. Dumas, and T. Kohler. 2004. CzcR-CzcS, a two-component system involved in heavy metal and carbapenem resistance in Pseudomonas aeruginosa. 3. Biol. Chem. 279:8761-8768.
    • (2004) Biol. Chem. , vol.279 , pp. 8761-8768
    • Perron, K.1    Caille, O.2    Rossier, C.3    Van Delden, C.4    Dumas, J.L.5    Kohler, T.6
  • 125
    • 0029125391 scopus 로고
    • Genotypic identification of two groups within the species Bacteroides fragilis by ribotyping and by analysis of PCR-generated fragment patterns and insertion sequence content
    • Podglajen, I, J. Breuil, I. Casin, and E. Collatz. 1995. Genotypic identification of two groups within the species Bacteroides fragilis by ribotyping and by analysis of PCR-generated fragment patterns and insertion sequence content. J. Bacteriol. 177:5270-5275.
    • (1995) J. Bacteriol. , vol.177 , pp. 5270-5275
    • Podglajen, I.1    Breuil, J.2    Casin, I.3    Collatz, E.4
  • 126
    • 0028304807 scopus 로고
    • Insertion of a novel DNA sequence, IS1186, upstream of the silent carbapcnemase gene cfiA, promotes expression of carbapenem resistance in clinical isolates of Bacteroides fragilis
    • Podglajen, I., J. Breuil, and E. Collatz. 1994. Insertion of a novel DNA sequence, IS1186, upstream of the silent carbapcnemase gene cfiA, promotes expression of carbapenem resistance in clinical isolates of Bacteroides fragilis. Mol. Microbiol. 12:105-114.
    • (1994) Mol. Microbiol. , vol.12 , pp. 105-114
    • Podglajen, I.1    Breuil, J.2    Collatz, E.3
  • 127
    • 0034004571 scopus 로고    scopus 로고
    • Carbapenem-hydrolyzing metallo-β-lactamase from a nosocomial isolate of Pseudomonas aeruginosa in France
    • Poirel, L., L. Collet, and P. Nordmann. 2000. Carbapenem-hydrolyzing metallo-β-lactamase from a nosocomial isolate of Pseudomonas aeruginosa in France. Emerg. Infect. Dis. 6:84-85.
    • (2000) Emerg. Infect. Dis. , vol.6 , pp. 84-85
    • Poirel, L.1    Collet, L.2    Nordmann, P.3
  • 128
    • 0347992026 scopus 로고    scopus 로고
    • Chromosome-encoded ambler class D β-lactamase of Shewanella oneidensis as a progenitor of carbapenem-hydrolyzing oxacillinase
    • Poirel, L., C. Heritier, and P. Nordmann. 2004. Chromosome-encoded ambler class D β-lactamase of Shewanella oneidensis as a progenitor of carbapenem-hydrolyzing oxacillinase. Antimicrob. Agents Chemother. 48:348-351.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 348-351
    • Poirel, L.1    Heritier, C.2    Nordmann, P.3
  • 131
    • 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., T. Naas, D. Nicolas, L. Collet, S. Bellais, J. D. Cavallo, and P. Nordmann. 2000. 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. 44:891-897.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 891-897
    • Poirel, L.1    Naas, T.2    Nicolas, D.3    Collet, L.4    Bellais, S.5    Cavallo, J.D.6    Nordmann, P.7
  • 132
    • 4444360483 scopus 로고    scopus 로고
    • Carbapenem-hydrolysing metallo-β-lactamases from Klebsiella pneumoniae and Escherichia coli isolated in Australia
    • Poirel, L., J. N. Pham, L. Cabanne, B. J. Gatus, S. M. Bell, and P. Nordmann. 2004. Carbapenem-hydrolysing metallo-β-lactamases from Klebsiella pneumoniae and Escherichia coli isolated in Australia. Pathology (Philadelphia) 36:366-367.
    • (2004) Pathology (Philadelphia) , vol.36 , pp. 366-367
    • Poirel, L.1    Pham, J.N.2    Cabanne, L.3    Gatus, B.J.4    Bell, S.M.5    Nordmann, P.6
  • 134
    • 0037301934 scopus 로고    scopus 로고
    • Overcoming multidrug resistance in gram-negative bacteria
    • Poole, K. 2003. Overcoming multidrug resistance in gram-negative bacteria. Curr. Opin. Investig. Drugs 4:128-139.
    • (2003) Curr. Opin. Investig. Drugs , vol.4 , pp. 128-139
    • Poole, K.1
  • 138
    • 0242291985 scopus 로고    scopus 로고
    • Why is big Pharma getting out of antibacterial drug discovery?
    • Projan, S. J. 2003. Why is big Pharma getting out of antibacterial drug discovery? Curr. Opin. Microbiol. 6:427-430.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 427-430
    • Projan, S.J.1
  • 139
    • 0033734984 scopus 로고    scopus 로고
    • SME-type carbapenem-hydrolyzing class A β-lactamases from geographically diverse Serratia marcescens strains
    • Queenan, A. M., C. Torres-Viera, H. S. Gold, Y. Carmeli, G. M. Eliopoulos, R. C. Moellering, J. P. Quinn, J. Hindler, A. A. Medeiros, and K. Bush. 2000. SME-type carbapenem-hydrolyzing class A β-lactamases from geographically diverse Serratia marcescens strains. Antimicrob. Agents Chemother. 44:3035-3039.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3035-3039
    • Queenan, A.M.1    Torres-Viera, C.2    Gold, H.S.3    Carmeli, Y.4    Eliopoulos, G.M.5
  • 143
    • 0025855413 scopus 로고
    • Identification and DNA sequence of a new Bacteroides fragilis insertion sequence-like clement
    • Rasmussen, B. A., and E. Kovacs. 1991. Identification and DNA sequence of a new Bacteroides fragilis insertion sequence-like clement. Plasmid 25: 141-144.
    • (1991) Plasmid , vol.25 , pp. 141-144
    • Rasmussen, B.A.1    Kovacs, E.2
  • 148
    • 0032524824 scopus 로고    scopus 로고
    • Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: A new molecular class B β-lactamase showing a broad substrate profile
    • Rossolini, G. M., N. Franceschini, M. L. Riccio, P. S. Mercuri, M. Perilli, M. Galleni, J. M. Frere, and G. Amicosante. 1998. Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B β-lactamase showing a broad substrate profile. Biochem. J. 332:145-152.
    • (1998) Biochem. J. , vol.332 , pp. 145-152
    • Rossolini, G.M.1    Franceschini, N.2    Riccio, M.L.3    Mercuri, P.S.4    Perilli, M.5    Galleni, M.6    Frere, J.M.7    Amicosante, G.8
  • 151
    • 0031971097 scopus 로고    scopus 로고
    • Molecular heterogeneity of the L-1 metallo-β-lactamase family from Stenotrophomonas maltophilia
    • Sanschagrin, F., J. Dufresne, and R. C. Levesque. 1998. Molecular heterogeneity of the L-1 metallo-β-lactamase family from Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 42:1245-1248.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1245-1248
    • Sanschagrin, F.1    Dufresne, J.2    Levesque, R.C.3
  • 152
    • 0042626513 scopus 로고    scopus 로고
    • Carbapenem-resistant Pseudomonas aeruginosa-carrying VIM-2 metallo-β-lactamase determinants, Croatia
    • Sardelic, S., L. Pallecchi, V. Punda-Polic, and G. M. Rossolini. 2003. Carbapenem-resistant Pseudomonas aeruginosa-carrying VIM-2 metallo-β- lactamase determinants, Croatia. Emerg. Infect. Dis. 9:1022-1023.
    • (2003) Emerg. Infect. Dis. , vol.9 , pp. 1022-1023
    • Sardelic, S.1    Pallecchi, L.2    Punda-Polic, V.3    Rossolini, G.M.4
  • 153
    • 0141928715 scopus 로고    scopus 로고
    • Flexible metal binding of the metallo-β-lactamase domain: Glyoxalase II incorporates iron, manganese, and zinc in vivo
    • Schilling, O., N. Wenzel, M. Naylor, A. Vogel, M. Crowder, C. Makaroff, and W. Meyer-Klaucke. 2003. Flexible metal binding of the metallo-β- lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo. Biochemistry 42:11777-11786.
    • (2003) Biochemistry , vol.42 , pp. 11777-11786
    • Schilling, O.1    Wenzel, N.2    Naylor, M.3    Vogel, A.4    Crowder, M.5    Makaroff, C.6    Meyer-Klaucke, W.7
  • 155
    • 0033517787 scopus 로고    scopus 로고
    • NMR characterization of the metallo-β-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: Role of an active-site loop
    • Scrofani, S. D., J. Chung, J. J. Huntley, S. J. Benkovic, P. E. Wright, and H. J. Dyson. 1999. NMR characterization of the metallo-β-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop. Biochemistry 38:14507-14514.
    • (1999) Biochemistry , vol.38 , pp. 14507-14514
    • Scrofani, S.D.1    Chung, J.2    Huntley, J.J.3    Benkovic, S.J.4    Wright, P.E.5    Dyson, H.J.6
  • 157
    • 0030071472 scopus 로고    scopus 로고
    • Multifocal outbreaks of metallo-β-lactamase-producing Pseudomonas aeruginosa resistant to broad-spectrum β-lactams, including carbapenems
    • Senda, K., Y. Arakawa, K. Nakashima, H. Ito, S. Ichiyama, K. Shimokata, N. Kato, and M. Ohta. 1996. Multifocal outbreaks of metallo-β-lactamase- producing Pseudomonas aeruginosa resistant to broad-spectrum β-lactams, including carbapenems. Antimicrob. Agents Chemother. 40:349-353.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 349-353
    • Senda, K.1    Arakawa, Y.2    Nakashima, K.3    Ito, H.4    Ichiyama, S.5    Shimokata, K.6    Kato, N.7    Ohta, M.8
  • 158
    • 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., Y. Doi, K. Yamane, T. Yagi, H. Kurokawa, K. Shibayama, H. Kato, K. Kai, and Y. Arakawa. 2003. 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. 41: 5407-5413.
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 5407-5413
    • Shibata, N.1    Doi, Y.2    Yamane, K.3    Yagi, T.4    Kurokawa, H.5    Shibayama, K.6    Kato, H.7    Kai, K.8    Arakawa, Y.9
  • 159
    • 12244297122 scopus 로고    scopus 로고
    • Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-β-lactamases
    • Siemann, S., A. J. Clarke, T. Viswanatha, and G. I. Dmitrienko. 2003. Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-β-lactamases. Biochemistry 42:1673-1683.
    • (2003) Biochemistry , vol.42 , pp. 1673-1683
    • Siemann, S.1    Clarke, A.J.2    Viswanatha, T.3    Dmitrienko, G.I.4
  • 162
    • 0035823527 scopus 로고    scopus 로고
    • Novel mechanism of hydrolysis of therapeutic β-lactams by Stenotrophomonas multophilia L1 metallo-β-lactamase
    • Spencer, J., A. R. Clarke, and T. R. Walsh. 2001. Novel mechanism of hydrolysis of therapeutic β-lactams by Stenotrophomonas multophilia L1 metallo-β-lactamase. J. Biol. Chem. 276:33638-33644.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33638-33644
    • Spencer, J.1    Clarke, A.R.2    Walsh, T.R.3
  • 164
    • 0025305139 scopus 로고
    • Sequencing of the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus β-lactamase BCI1
    • Thompson, J. S., and M. H. Malamy. 1990. Sequencing of the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus β-lactamase BCI1. J. Bacteriol. 172:2584-2593.
    • (1990) J. Bacteriol. , vol.172 , pp. 2584-2593
    • Thompson, J.S.1    Malamy, M.H.2
  • 165
    • 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. 52:583-590.
    • (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
  • 166
    • 0347992025 scopus 로고    scopus 로고
    • VIM-7, an evolutionary distinct metallo-β-lactamase gene in a Pseudomonas aeruginosa isolate from the United States
    • VIM-7, an evolutionary distinct metallo-β-lactamase gene in a Pseudomonas aeruginosa isolate from the United States. Antimicrob. Agents Chemother. 48: 329-332.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 329-332
    • Toleman, M.A.1    Rolston, K.2    Jones, R.N.3    Walsh, T.R.4
  • 167
    • 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, M. A., A. M. Simm, T. A. Murphy, A. C. Gales, D. J. Biedenbach, R. N. Jones, and T. R. Walsh. 2002. Molecular characterization of SPM-1, a novel metallo-β-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme. J. Antimicrob. Chemother. 50:673-679.
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 673-679
    • Toleman, M.A.1    Simm, A.M.2    Murphy, T.A.3    Gales, A.C.4    Biedenbach, D.J.5    Jones, R.N.6    Walsh, T.R.7
  • 168
    • 0037301438 scopus 로고    scopus 로고
    • Metallo-β-lactamase inhibitors: Could they give old antibacterials new life?
    • Toney, J. H. 2003. Metallo-β-lactamase inhibitors: could they give old antibacterials new life? Curr. Opin. Investig. Drugs 4:115-116.
    • (2003) Curr. Opin. Investig. Drugs , vol.4 , pp. 115-116
    • Toney, J.H.1
  • 172
    • 0036924330 scopus 로고    scopus 로고
    • An unwanted import to the UK: A carbapenem-resistant clinical isolate of Acinetobacter baumannii producing metallo-β-lactamase
    • Towner, K. J., T. Gee, and T. Boswell. 2002. An unwanted import to the UK: a carbapenem-resistant clinical isolate of Acinetobacter baumannii producing metallo-β-lactamase. J. Antimicrob. Chemother. 50:1092-1093.
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 1092-1093
    • Towner, K.J.1    Gee, T.2    Boswell, T.3
  • 175
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution
    • Ullah, J. H., T. R. Walsh, I. A. Taylor, D. C. Emery, C. S. Verma, S. J. Gamblin, and J. Spencer. 1998. The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution. J. Mol. Biol. 284:125-136.
    • (1998) J. Mol. Biol. , vol.284 , pp. 125-136
    • Ullah, J.H.1    Walsh, T.R.2    Taylor, I.A.3    Emery, D.C.4    Verma, C.S.5    Gamblin, S.J.6    Spencer, J.7
  • 176
    • 0037508519 scopus 로고    scopus 로고
    • Considerations in control and treatment of nosocomial infections due to multidrug-resistant Acinetobacter baumannii
    • Urban, C., S. Segal-Maurer, and J. J. Rahal. 2003. Considerations in control and treatment of nosocomial infections due to multidrug-resistant Acinetobacter baumannii. Clin. Infect. Dis. 36:1268-1274.
    • (2003) Clin. Infect. Dis. , vol.36 , pp. 1268-1274
    • Urban, C.1    Segal-Maurer, S.2    Rahal, J.J.3
  • 177
    • 0036701621 scopus 로고    scopus 로고
    • Evaluation of a new Etest for detecting metallo-β-lactamases in routine clinical testing
    • Walsh, T. R., A. Bolmstrom, A. Qwarnstrom, and A. Gales. 2002. Evaluation of a new Etest for detecting metallo-β-lactamases in routine clinical testing. J. Clin. Microbiol. 40:2755-2759.
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 2755-2759
    • Walsh, T.R.1    Bolmstrom, A.2    Qwarnstrom, A.3    Gales, A.4
  • 179
    • 0030836575 scopus 로고    scopus 로고
    • Sequence analysis and enzyme kinetics of the L2 serine β-lactamase from Stenotrophomonas maltophilia
    • Walsh, T. R., A. P. MacGowan, and P. M. Bennett. 1997. Sequence analysis and enzyme kinetics of the L2 serine β-lactamase from Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 41:1460-1464.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1460-1464
    • Walsh, T.R.1    MacGowan, A.P.2    Bennett, P.M.3
  • 183
    • 0032575621 scopus 로고    scopus 로고
    • Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-β-lactamase that provides multiple antibiotic resistance
    • Wang, Z., and S. J. Benkovic. 1998. Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-β-lactamase that provides multiple antibiotic resistance. J. Biol. Chem. 273:22402-22408.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22402-22408
    • Wang, Z.1    Benkovic, S.J.2
  • 184
    • 0032556222 scopus 로고    scopus 로고
    • Direct observation of an enzyme-bound intermediate in the catalytic cycle of the metallo-β-lactamase from Bacteroides fragilis
    • Wang, Z., W. Fast, and S. J. Benkovic. 1998. Direct observation of an enzyme-bound intermediate in the catalytic cycle of the metallo-β-lactamase from Bacteroides fragilis. J. Am. Chem. Soc. 120:10788-10789.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10788-10789
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 185
    • 0033520073 scopus 로고    scopus 로고
    • On the mechanism of the metallo-β-lactamase from Bacteroides fragilis
    • Wang, Z., W. Fast, and S. J. Benkovic. 1999. On the mechanism of the metallo-β-lactamase from Bacteroides fragilis. Biochemistry 38:10013-10023.
    • (1999) Biochemistry , vol.38 , pp. 10013-10023
    • Wang, Z.1    Fast, W.2    Benkovic, S.J.3
  • 188
    • 0034128891 scopus 로고    scopus 로고
    • Carbapenemases of Chryscobacterium (Flavobacterium) meningosepticum: Distribution of blaB and characterization of a novel metallo-β-lactamase gene, blaB3, in the type strain, NCTC 10016
    • Woodford, N., M. F. Palepou, G. S. Babini, B. Holmes, and D. M. Livermore. 2000. Carbapenemases of Chryscobacterium (Flavobacterium) meningosepticum: distribution of blaB and characterization of a novel metallo-β-lactamase gene, blaB3, in the type strain, NCTC 10016. Antimicrob. Agents Chemother. 44:1448-1452.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 1448-1452
    • Woodford, N.1    Palepou, M.F.2    Babini, G.S.3    Holmes, B.4    Livermore, D.M.5
  • 189
    • 0035861974 scopus 로고    scopus 로고
    • Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily
    • Wouters, M. A., and A. Husain. 2001. Changes in zinc ligation promote remodeling of the active site in the zinc hydrolase superfamily. J. Mol. Biol. 314:1191-1207.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1191-1207
    • Wouters, M.A.1    Husain, A.2
  • 190
    • 0037342876 scopus 로고    scopus 로고
    • Production of CTX-M-3 extended-spectrum β-lactamase and IMP-1 metallo β-lactamase by five Gram-negative bacilli: Survey of clinical isolates from seven laboratories collected in 1998 und 2000, in the Kinki region of Japan
    • Yamasaki, K., M. Komatsu, T. Yamashita, K. Shimakawa, T. Ura, H. Nishio, K. Satoh, R. Washidu, S. Kinoshita, and M. Aihara. 2003. Production of CTX-M-3 extended-spectrum β-lactamase and IMP-1 metallo β-lactamase by five Gram-negative bacilli: survey of clinical isolates from seven laboratories collected in 1998 und 2000, in the Kinki region of Japan. J. Antimicrob. Chemother. 51:631-638.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 631-638
    • Yamasaki, K.1    Komatsu, M.2    Yamashita, T.3    Shimakawa, K.4    Ura, T.5    Nishio, H.6    Satoh, K.7    Washidu, R.8    Kinoshita, S.9    Aihara, M.10
  • 191
    • 0032758090 scopus 로고    scopus 로고
    • Distribution of the cfiA gene among Bacteroides fragilis strains in Japan and relatedness of cfiA to imipenem resistance
    • Yamazoe, K., N. Kato, H. Kato, K. Tanaka, Y. Katagiri, and K. Watanabe. 1999. Distribution of the cfiA gene among Bacteroides fragilis strains in Japan and relatedness of cfiA to imipenem resistance. Antimicrob. Agents Chemother. 43:2808-2810.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2808-2810
    • Yamazoe, K.1    Kato, N.2    Kato, H.3    Tanaka, K.4    Katagiri, Y.5    Watanabe, K.6
  • 192
    • 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
    • Van, J. J., P. R. Hsueh, W. C. Ko, K. T. Luh, S. H. Tsai, H. M. Wu, and J. J. Wu. 2001. 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. 45:2224-2228.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 2224-2228
    • Van, J.J.1    Hsueh, P.R.2    Ko, W.C.3    Luh, K.T.4    Tsai, S.H.5    Wu, H.M.6    Wu, J.J.7
  • 193
    • 0036798669 scopus 로고    scopus 로고
    • Metallo-β-lactamase-producing Enterobacteriaceae isolates in a university hospital in Taiwan: Prevalence of IMP-8 in Enterobacter cloacae and first identification of VIM-2 in Citrobacter freundii
    • Yan, J. J., W. C. Ko, C. L. Chuang, and J. J. Wu. 2002. Metallo-β-lactamase-producing Enterobacteriaceae isolates in a university hospital in Taiwan: prevalence of IMP-8 in Enterobacter cloacae and first identification of VIM-2 in Citrobacter freundii. J. Antimicrob. Chemother. 50:503-511.
    • (2002) J. Antimicrob. Chemother. , vol.50 , pp. 503-511
    • Yan, J.J.1    Ko, W.C.2    Chuang, C.L.3    Wu, J.J.4
  • 195
    • 2342462126 scopus 로고    scopus 로고
    • Comparison of the double-disk, combined disk, and Etest methods for detecting metallo-β-lactamases in gram-negative hacilli
    • Yan, J. J., J. J. Wu, S. H. Tsai, and C. L. Chuang. 2004. Comparison of the double-disk, combined disk, and Etest methods for detecting metallo-β-lactamases in gram-negative hacilli, Diagn. Microbiol. Infect. Dis. 49:5-11.
    • (2004) Diagn. Microbiol. Infect. Dis. , vol.49 , pp. 5-11
    • Yan, J.J.1    Wu, J.J.2    Tsai, S.H.3    Chuang, C.L.4
  • 196
    • 0029935951 scopus 로고    scopus 로고
    • Biochemical characterization of the carbapenem-hydrolyzing β-lactamase AsbM1 from Aeromonas sobria AER 14M: A member of a novel subgroup of metallo-β-lactamases
    • Yang, Y., and K. Bush. 1996. Biochemical characterization of the carbapenem-hydrolyzing β-lactamase AsbM1 from Aeromonas sobria AER 14M: a member of a novel subgroup of metallo-β-lactamases. FEMS Microbiol. Lett. 137:193-200.
    • (1996) FEMS Microbiol. Lett. , vol.137 , pp. 193-200
    • Yang, Y.1    Bush, K.2
  • 197
    • 0025366291 scopus 로고
    • Biochemical characterization of a β-lactamase that hydrolyzes penems and carbapenems from two Serratia marcescens isolates
    • Yang, Y. J., P. J. Wu, and D. M. Livermore. 1990. Biochemical characterization of a β-lactamase that hydrolyzes penems and carbapenems from two Serratia marcescens isolates. Antimicrob. Agents Chemother. 34:755-758.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 755-758
    • Yang, Y.J.1    Wu, P.J.2    Livermore, D.M.3
  • 198
    • 0035042388 scopus 로고    scopus 로고
    • Plasmid-encoded metallo-β-lactamase (IMP-6) conferring resistance to carbapenems, especially meropenem
    • Yano, H., A. Kuga, R. Okamoto, H. Kitasato, T. Kobayashi, and M. Inoue. 2001. Plasmid-encoded metallo-β-lactamase (IMP-6) conferring resistance to carbapenems, especially meropenem. Antimicrob. Agents Chemother. 45:1343-1348.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1343-1348
    • Yano, H.1    Kuga, A.2    Okamoto, R.3    Kitasato, H.4    Kobayashi, T.5    Inoue, M.6
  • 202
    • 0036791235 scopus 로고    scopus 로고
    • Imipenem-EDTA disk method for differentiation of metallo-β- lactamase-producing clinical isolates of Pseudomonas spp. and Acinetobacter spp
    • Yong, D., K. Lee, J. H. Yum, H. B. Shin, G. M. Rossolini, and Y. Chong. 2002. Imipenem-EDTA disk method for differentiation of metallo-β-lactamase- producing clinical isolates of Pseudomonas spp. and Acinetobacter spp. J. Clin. Microbiol. 40:3798-3801.
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 3798-3801
    • Yong, D.1    Lee, K.2    Yum, J.H.3    Shin, H.B.4    Rossolini, G.M.5    Chong, Y.6
  • 203
    • 0036201204 scopus 로고    scopus 로고
    • A new integron carrying VIM-2 metallo-β-lactamasc gene cassette in a Serratia marcescens isolate
    • Yum, J. H., D. Yong, K. Lee, H. S. Kim, and Y. Chong. 2002. A new integron carrying VIM-2 metallo-β-lactamasc gene cassette in a Serratia marcescens isolate. Diagn. Microbiol. Infect. Dis. 42:217-219.
    • (2002) Diagn. Microbiol. Infect. Dis. , vol.42 , pp. 217-219
    • Yum, J.H.1    Yong, D.2    Lee, K.3    Kim, H.S.4    Chong, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.