메뉴 건너뛰기




Volumn 55, Issue 11, 2011, Pages 4943-4960

Carbapenems: Past, present, and future

Author keywords

[No Author keywords available]

Indexed keywords

AMIKACIN; AMINOGLYCOSIDE; AZITHROMYCIN; BETA LACTAM; BIAPENEM; CARBAPENEM; CEPHALOSPORIN; CILASTATIN PLUS IMIPENEM; CIPROFLOXACIN; CLAVULANIC ACID; COLISTIN; DORIPENEM; ERTAPENEM; GENTAMICIN; IMIPENEM; LEVOFLOXACIN; LINEZOLID; MEROPENEM; PANIPENEM PLUS BETAMIPRON; PENICILLIN G; POLYMYXIN B; QUINOLINE DERIVED ANTIINFECTIVE AGENT; RIFAMPICIN; SULBACTAM; TACHYPLESIN; TEICOPLANIN; THIENAMYCIN; TIGECYCLINE; UNINDEXED DRUG; VANCOMYCIN;

EID: 80054693925     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00296-11     Document Type: Short Survey
Times cited : (1068)

References (257)
  • 1
    • 54849433348 scopus 로고    scopus 로고
    • New agents in development for the treatment of bacterial infections
    • Abbanat, D., B. Morrow, and K. Bush. 2008. New agents in development for the treatment of bacterial infections. Curr. Opin. Pharmacol. 8:582-592.
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 582-592
    • Abbanat, D.1    Morrow, B.2    Bush, K.3
  • 4
    • 0025870126 scopus 로고
    • A standard numbering scheme for the class A β-lactamases
    • Ambler, R. P., et al. 1991. A standard numbering scheme for the class A β-lactamases. Biochem. J. 276(Pt. 1):269-270.
    • (1991) Biochem. J. , vol.276 , Issue.PART 1 , pp. 269-270
    • Ambler, R.P.1
  • 6
    • 27644534247 scopus 로고    scopus 로고
    • Penicillin-binding proteins of Bacteroides fragilis and their role in the resistance to imipenem of clinical isolates
    • DOI 10.1099/jmm.0.45930-0
    • Ayala, J., A. Quesada, S. Vadillo, J. Criado, and S. Piriz. 2005. Penicillin-binding proteins of Bacteroides fragilis and their role in the resistance to imipenem of clinical isolates. J. Med. Microbiol. 54:1055-1064. (Pubitemid 41566776)
    • (2005) Journal of Medical Microbiology , vol.54 , Issue.11 , pp. 1055-1064
    • Ayala, J.1    Quesada, A.2    Vadillo, S.3    Criado, J.4    Piriz, S.5
  • 9
    • 0019863676 scopus 로고
    • Synthesis of 6-unsubstituted olivanic acid analogues and their antibacterial activities
    • Basker, M. J., et al. 1981. Synthesis of 6-unsubstituted olivanic acid analogues and their antibacterial activities. J. Antibiot. (Tokyo) 34:1224-1226. (Pubitemid 12174625)
    • (1981) Journal of Antibiotics , vol.34 , Issue.9 , pp. 1224-1226
    • Basker, M.J.1    Bateson, J.H.2    Baxter, A.J.G.3
  • 10
    • 0019200570 scopus 로고
    • Comparative antibacterial properties in vitro of seven olivanic acid derivatives: MM 4550, MM 13902, MM 17880, MM 22380, MM 22381, MM 22382 AND MM 22383
    • Basker, M. J., R. J. Boon, and P. A. Hunter. 1980. Comparative antibacterial properties in vitro of seven olivanic acid derivatives: MM 4550, MM 13902, MM 17880, MM 22380, MM 22381, MM 22382 and MM 22383. J. Antibiot. (Tokyo) 33:878-884. (Pubitemid 11231474)
    • (1980) Journal of Antibiotics , vol.33 , Issue.8 , pp. 878-884
    • Basker, M.J.1    Boon, R.J.2    Hunter, P.A.3
  • 13
    • 0036894235 scopus 로고    scopus 로고
    • Structural basis for imipenem inhibition of class C β-lactamases
    • DOI 10.1128/AAC.46.12.3978-3980.2002
    • Beadle, B. M., and B. K. Shoichet. 2002. Structural basis for imipenem inhibition of class C β-lactamases. Antimicrob. Agents Chemother. 46:3978-3980. (Pubitemid 35403277)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.12 , pp. 3978-3980
    • Beadle, B.M.1    Shoichet, B.K.2
  • 14
    • 34948859355 scopus 로고    scopus 로고
    • Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily
    • Bebrone, C. 2007. Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Biochem. Pharmacol. 74:1686-1701.
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 1686-1701
    • Bebrone, C.1
  • 15
    • 49649086489 scopus 로고    scopus 로고
    • Mutational analysis of the zinc- and substrate-binding sites in the CphA metallo-β-lactamase from Aeromonas hydrophila
    • Bebrone, C., et al. 2008. Mutational analysis of the zinc- and substrate-binding sites in the CphA metallo-β-lactamase from Aeromonas hydrophila. Biochem. J. 414:151-159.
    • (2008) Biochem. J. , vol.414 , pp. 151-159
    • Bebrone, C.1
  • 16
    • 70349324693 scopus 로고    scopus 로고
    • The structure of the dizinc subclass B2 metallo-β-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site
    • Bebrone, C., et al. 2009. The structure of the dizinc subclass B2 metallo-β-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site. Antimicrob. Agents Chemother. 53:4464-4471.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 4464-4471
    • Bebrone, C.1
  • 17
    • 0025021475 scopus 로고
    • Novel resistance to imipenem associated with an altered PBP-4 in a Pseudomonas aeruginosa clinical isolate
    • Bellido, F., C. Veuthey, J. Blaser, A. Bauernfeind, and J. C. Pechere. 1990. Novel resistance to imipenem associated with an altered PBP-4 in a Pseudomonas aeruginosa clinical isolate. J. Antimicrob. Chemother. 25:57-68. (Pubitemid 20042490)
    • (1990) Journal of Antimicrobial Chemotherapy , vol.25 , Issue.1 , pp. 57-68
    • Bellido, F.1    Veuthey, C.2    Blaser, J.3    Bauernfeind, A.4    Pechere, J.C.5
  • 18
    • 79959195660 scopus 로고    scopus 로고
    • Exploring the inhibition of CTX-M-9 by β-lactamase inhibitors and carbapenems
    • Bethel, C. R., et al. 2011. Exploring the inhibition of CTX-M-9 by β-lactamase inhibitors and carbapenems. Antimicrob. Agents Chemother. 55:3465-3475.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 3465-3475
    • Bethel, C.R.1
  • 19
    • 0033060964 scopus 로고    scopus 로고
    • Comparative in vitro activities of meropenem, imipenem, temocillin, piperacillin, and ceftazidime in combination with tobramycin, rifampin, or ciprofloxacin against Burkholderia cepacia isolates from patients with cystic fibrosis
    • Bonacorsi, S., F. Fitoussi, S. Lhopital, and E. Bingen. 1999. Comparative in vitro activities of meropenem, imipenem, temocillin, piperacillin, and ceftazidime in combination with tobramycin, rifampin, or ciprofloxacin against Burkholderia cepacia isolates from patients with cystic fibrosis. Antimicrob. Agents Chemother. 43:213-217. (Pubitemid 29079148)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.2 , pp. 213-217
    • Bonacorsi, S.1    Fitoussi, F.2    Lhopital, S.3    Bingen, E.4
  • 21
    • 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., G. Cervero, M. A. Dominguez, C. Quereda, and J. Martinez-Beltran. 2000. 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. 38:3299-3305.
    • (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
  • 22
    • 0031026934 scopus 로고    scopus 로고
    • Imipenem resistance in Klebsiella pneumoniae is associated with the combination of ACT-1, a plasmid-mediated AmpC β-lactamase, and the loss of an outer membrane protein
    • Bradford, P. A., et al. 1997. Imipenem resistance in Klebsiella pneumoniae is associated with the combination of ACT-1, a plasmid-mediated AmpC β-lactamase, and the loss of an outer membrane protein. Antimicrob. Agents Chemother. 41:563-569. (Pubitemid 27098404)
    • (1997) Antimicrobial Agents and Chemotherapy , vol.41 , Issue.3 , pp. 563-569
    • Bradford, P.A.1    Urban, C.2    Mariano, N.3    Projan, S.J.4    Rahal, J.J.5    Bush, K.6
  • 25
    • 0017074284 scopus 로고
    • Naturally-occurring β-lactamase inhibitors with antibacterial activity
    • Tokyo
    • Brown, A. G., et al. 1976. Naturally-occurring β-lactamase inhibitors with antibacterial activity. J. Antibiot. (Tokyo) 29:668-669.
    • (1976) J. Antibiot. , vol.29 , pp. 668-669
    • Brown, A.G.1
  • 26
    • 77149165713 scopus 로고    scopus 로고
    • Updated functional classification of β-lactamases
    • Bush, K., and G. A. Jacoby. 2010. Updated functional classification of β-lactamases. Antimicrob. Agents Chemother. 54:969-976.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 969-976
    • Bush, K.1    Jacoby, G.A.2
  • 27
    • 0018388508 scopus 로고
    • Olivanic acids, a family of β-lactam antibiotics with β-lactamase inhibitory properties produced by Streptomyces species. I. Detection, properties and fermentation studies
    • Butterworth, D., M. Cole, G. Hanscomb, and G. N. Rolinson. 1979. Olivanic acids, a family of β-lactam antibiotics with β-lactamase inhibitory properties produced by Streptomyces species. I. Detection, properties and fermentation studies. J. Antibiot. (Tokyo) 32:287-294. (Pubitemid 9189889)
    • (1979) Journal of Antibiotics , vol.32 , Issue.4 , pp. 287-294
    • Butterworth, D.1    Cole, M.2    Hanscomb, G.3    Rolinson, G.N.4
  • 28
    • 0018257865 scopus 로고
    • Total synthesis of thienamycin analogues. 1. Synthesis of the thienamycin nucleus and dl-descysteaminylthienamycin
    • Cama, L. D., and B. G. Christensen. 1978. Total synthesis of thienamycin analogs. 1. Synthesis of the thienamycin nucleus and dl- decysteaminylthienamycin. J. Am. Chem. Soc. 100:8006-8007. (Pubitemid 9115604)
    • (1978) Journal of the American Chemical Society , vol.100 , Issue.25 , pp. 8006-8007
    • Cama, L.D.1    Christensen, B.G.2
  • 31
    • 35949002763 scopus 로고    scopus 로고
    • First characterization of heterogeneous resistance to imipenem in invasive nontypeable Haemophilus influenzae isolates
    • DOI 10.1128/AAC.00335-07
    • Cerquetti, M., M. Giufre, R. Cardines, and P. Mastrantonio. 2007. First characterization of heterogeneous resistance to imipenem in invasive non-typeable Haemophilus influenzae isolates. Antimicrob. Agents Chemother. 51:3155-3161. (Pubitemid 350067522)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.9 , pp. 3155-3161
    • Cerquetti, M.1    Giufre, M.2    Cardines, R.3    Mastrantonio, P.4
  • 32
    • 40149087719 scopus 로고    scopus 로고
    • In vitro activity of cefepime, imipenem, tigecycline, and gentamicin, alone and in combination, against extended-spectrum β-lactamase-producing Klebsiella pneumoniae and Escherichia coli
    • DOI 10.1592/phco.28.3.295
    • Cha, R. 2008. In vitro activity of cefepime, imipenem, tigecycline, and gentamicin, alone and in combination, against extended-spectrum β-lactamase-producing Klebsiella pneumoniae and Escherichia coli. Pharmacotherapy 28:295-300. (Pubitemid 351328901)
    • (2008) Pharmacotherapy , vol.28 , Issue.3 , pp. 295-300
    • Cha, R.1
  • 33
    • 0025100324 scopus 로고
    • Binding affinity for penicillin-binding protein 2a correlates with in vivo activity of β-lactam antibiotics against methicillin-resistant Staphylococcus aureus
    • Chambers, H. F., M. Sachdeva, and S. Kennedy. 1990. Binding affinity for penicillin-binding protein 2a correlates with in vivo activity of β-lactam antibiotics against methicillin-resistant Staphylococcus aureus. J. Infect. Dis. 162:705-710. (Pubitemid 20266163)
    • (1990) Journal of Infectious Diseases , vol.162 , Issue.3 , pp. 705-710
    • Chambers, H.F.1    Sachdeva, M.2    Kennedy, S.3
  • 34
    • 0019793751 scopus 로고
    • Inhibition of the RTEM β-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid
    • DOI 10.1021/bi00513a005
    • Charnas, R. L., and J. R. Knowles. 1981. Inhibition of the RTEM β-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid. Biochemistry 20:2732-2737. (Pubitemid 11038334)
    • (1981) Biochemistry , vol.20 , Issue.10 , pp. 2732-2737
    • Charnas, R.L.1    Knowles, J.R.2
  • 35
    • 79959700071 scopus 로고    scopus 로고
    • Evolution of β-lactams resistance in Gram-negative bacteria in Tunisia
    • Chouchani, C., R. Marrakchi, and A. El Salabi. 2011. Evolution of β-lactams resistance in Gram-negative bacteria in Tunisia. Crit. Rev. Microbiol. 37:167-177.
    • (2011) Crit. Rev. Microbiol. , vol.37 , pp. 167-177
    • Chouchani, C.1    Marrakchi, R.2    El Salabi, A.3
  • 36
    • 0025943112 scopus 로고
    • Imipenem resistance associated with the loss of a 40 kDa outer membrane protein in Enterobacter aerogenes
    • Chow, J. W., and D. M. Shlaes. 1991. Imipenem resistance associated with the loss of a 40 kDa outer membrane protein in Enterobacter aerogenes. J. Antimicrob. Chemother. 28:499-504.
    • (1991) J. Antimicrob. Chemother. , vol.28 , pp. 499-504
    • Chow, J.W.1    Shlaes, D.M.2
  • 40
    • 33750970568 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-β-lactamase ImiS from Aeromonas veronii bv. sobria
    • DOI 10.1021/bi061547e
    • Costello, A. L., N. P. Sharma, K. W. Yang, M. W. Crowder, and D. L. Tierney. 2006. X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-β-lactamase ImiS from Aeromonas veronii bv. sobria. Biochemistry 45:13650-13658. (Pubitemid 44748511)
    • (2006) Biochemistry , vol.45 , Issue.45 , pp. 13650-13658
    • Costello, A.L.1    Sharma, N.P.2    Yang, K.-W.3    Crowder, M.W.4    Tierney, D.L.5
  • 42
    • 16444387315 scopus 로고    scopus 로고
    • Spectroscopic studies on cobalt(II)-substituted metallo-β-lactamase ImiS from Aeromonas veronii bv. sobria
    • DOI 10.1021/bi047463s
    • Crawford, P. A., K. W. Yang, N. Sharma, B. Bennett, and M. W. Crowder. 2005. Spectroscopic studies on cobalt(II)-substituted metallo-β-lactamase ImiS from Aeromonas veronii bv. sobria. Biochemistry 44:5168-5176. (Pubitemid 40476141)
    • (2005) Biochemistry , vol.44 , Issue.13 , pp. 5168-5176
    • Crawford, P.A.1    Yang, K.-W.2    Sharma, N.3    Bennett, B.4    Crowder, M.W.5
  • 43
    • 0031836428 scopus 로고    scopus 로고
    • Entry of sanfetrinem into human polymorphonuclear granulocytes and its cell-associated activity against intracellular, penicillin-resistant Streptococcus pneumoniae
    • Cuffini, A. M., et al. 1998. Entry of sanfetrinem into human polymorphonuclear granulocytes and its cell-associated activity against intracellular, penicillin-resistant Streptococcus pneumoniae. Antimicrob. Agents Chemother. 42:1745-1750. (Pubitemid 28311573)
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , Issue.7 , pp. 1745-1750
    • Cuffini, A.M.1    Tullio, V.2    Bonino, A.3    Allocco, A.4    Ianni, P.A.5    Carlone, N.A.6
  • 44
    • 0020966463 scopus 로고
    • Investigations on β-lactamase stability of recently developed β-lactam compounds: Study of enzyme kinetics
    • Cullmann, W., and W. Dick. 1983. Investigations on β-lactamase stability of recently developed β-lactam compounds: study of enzyme kinetics. Zentralbl. Bakteriol. Mikrobiol. Hyg. A 254:413-422. (Pubitemid 13025344)
    • (1983) Zentralblatt fur Bakteriologie Mikrobiologie und Hygiene - Abt. 1 Orig. A , vol.254 , Issue.3 , pp. 413-422
    • Cullmann, W.1    Dick, W.2
  • 45
    • 44849098420 scopus 로고    scopus 로고
    • Safety of meropenem in patients reporting penicillin allergy: Lack of allergic cross reactions
    • Cunha, B. A., N. S. Hamid, V. Krol, and L. Eisenstein. 2008. Safety of meropenem in patients reporting penicillin allergy: lack of allergic cross reactions. J. Chemother. 20:233-237. (Pubitemid 351797065)
    • (2008) Journal of Chemotherapy , vol.20 , Issue.2 , pp. 233-237
    • Cunha, B.A.1    Hamid, N.S.2    Krol, V.3    Eisenstein, L.4
  • 47
    • 65749120570 scopus 로고    scopus 로고
    • Crystal structure of the OXA-48 β-lactamase reveals mechanistic diversity among class D carbapenemases
    • Docquier, J. D., et al. 2009. Crystal structure of the OXA-48 β-lactamase reveals mechanistic diversity among class D carbapenemases. Chem. Biol. 16:540-547.
    • (2009) Chem. Biol. , vol.16 , pp. 540-547
    • Docquier, J.D.1
  • 48
    • 75349096353 scopus 로고    scopus 로고
    • Inhibition of the class C β-lactamase from Acinetobacter spp.: Insights into effective inhibitor design
    • Drawz, S. M., et al. 2010. Inhibition of the class C β-lactamase from Acinetobacter spp.: insights into effective inhibitor design. Biochemistry 49:329-340.
    • (2010) Biochemistry , vol.49 , pp. 329-340
    • Drawz, S.M.1
  • 49
    • 67049107918 scopus 로고    scopus 로고
    • Differing effects of combination chemotherapy with meropenem and tobramycin on cell kill and suppression of resistance of wild-type Pseudomonas aeruginosa PAO1 and its isogenic MexAB efflux pump-overexpressed mutant
    • Drusano, G. L., W. Liu, C. Fregeau, R. Kulawy, and A. Louie. 2009. Differing effects of combination chemotherapy with meropenem and tobramycin on cell kill and suppression of resistance of wild-type Pseudomonas aeruginosa PAO1 and its isogenic MexAB efflux pump-overexpressed mutant. Antimicrob. Agents Chemother. 53:2266-2273.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2266-2273
    • Drusano, G.L.1    Liu, W.2    Fregeau, C.3    Kulawy, R.4    Louie, A.5
  • 50
    • 75749107905 scopus 로고    scopus 로고
    • In-vitro efficacy of synergistic antibiotic combinations in multidrug resistant Pseudomonas aeruginosa strains
    • Dundar, D., and M. Otkun. 2010. In-vitro efficacy of synergistic antibiotic combinations in multidrug resistant Pseudomonas aeruginosa strains. Yonsei Med. J. 51:111-116.
    • (2010) Yonsei Med. J. , vol.51 , pp. 111-116
    • Dundar, D.1    Otkun, M.2
  • 51
    • 0020327724 scopus 로고
    • Inhibition of the RTEM β-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acid
    • DOI 10.1021/bi00541a008
    • Easton, C. J., and J. R. Knowles. 1982. Inhibition of the RTEM β-lactamase from Escherichia coli. Interaction of the enzyme with derivatives of olivanic acid. Biochemistry 21:2857-2862. (Pubitemid 12067503)
    • (1982) Biochemistry , vol.21 , Issue.12 , pp. 2857-2862
    • Easton, C.J.1    Knowles, J.R.2
  • 52
    • 75749099741 scopus 로고    scopus 로고
    • Enhancing resistance to cephalosporins in class C β-lactamases: Impact of Gly214Glu in CMY-2
    • Endimiani, A., et al. 2010. Enhancing resistance to cephalosporins in class C β-lactamases: impact of Gly214Glu in CMY-2. Biochemistry 49:1014-1023.
    • (2010) Biochemistry , vol.49 , pp. 1014-1023
    • Endimiani, A.1
  • 53
    • 33646270908 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa bloodstream infections: Risk factors and treatment outcome related to expression of the PER-1 extended-spectrum β-lactamase
    • Endimiani, A., et al. 2006. Pseudomonas aeruginosa bloodstream infections: risk factors and treatment outcome related to expression of the PER-1 extended-spectrum β-lactamase. BMC Infect. Dis. 6:52.
    • (2006) BMC Infect. Dis. , vol.6 , pp. 52
    • Endimiani, A.1
  • 54
    • 0035166539 scopus 로고    scopus 로고
    • Investigation of synergism of meropenem and ciprofloxacin against pseudomonas aeruginosa and acinetobacter strains isolated from intensive care unit infections
    • DOI 10.1080/00365540110027222
    • Ermertcan, S., M. Hosgor, O. Tunger, and G. Cosar. 2001. Investigation of synergism of meropenem and ciprofloxacin against Pseudomonas aeruginosa and Acinetobacter strains isolated from intensive care unit infections. Scand. J. Infect. Dis. 33:818-821. (Pubitemid 33069519)
    • (2001) Scandinavian Journal of Infectious Diseases , vol.33 , Issue.11 , pp. 818-821
    • Ermertcan, S.1    Hosgor, M.2    Tunger, O.3    Cosar, G.4
  • 55
    • 0020070081 scopus 로고
    • A comparative in vitro study of thienamycin
    • Fainstein, V., B. LeBlanc, S. Weaver, and G. P. Bodey. 1982. A comparative in vitro study of thienamycin. Infection 10:50-52. (Pubitemid 12184124)
    • (1982) Infection , vol.10 , Issue.1 , pp. 50-52
    • Fainstein, V.1    LeBlanc, B.2    Weaver, S.3    Bodey, G.P.4
  • 56
    • 41949136273 scopus 로고    scopus 로고
    • Role of outer membrane protein OprD and penicillin-binding proteins in resistance of Pseudomonas aeruginosa to imipenem and meropenem
    • Farra, A., S. Islam, A. Stralfors, M. Sorberg, and B. Wretlind. 2008. Role of outer membrane protein OprD and penicillin-binding proteins in resistance of Pseudomonas aeruginosa to imipenem and meropenem. Int. J. Antimicrob. Agents 31:427-433.
    • (2008) Int. J. Antimicrob. Agents , vol.31 , pp. 427-433
    • Farra, A.1    Islam, S.2    Stralfors, A.3    Sorberg, M.4    Wretlind, B.5
  • 57
    • 0037339172 scopus 로고    scopus 로고
    • Relationship between β-lactamase production, outer membrane protein and penicillin-binding protein profiles on the activity of carbapenems against clinical isolates of Acinetobacter baumannii
    • DOI 10.1093/jac/dkg097
    • Fernandez-Cuenca, F., et al. 2003. Relationship between β-lactamase production, outer membrane protein and penicillin-binding protein profiles on the activity of carbapenems against clinical isolates of Acinetobacter baumannii. J. Antimicrob. Chemother. 51:565-574. (Pubitemid 36336148)
    • (2003) Journal of Antimicrobial Chemotherapy , vol.51 , Issue.3 , pp. 565-574
    • Fernandez-Cuenca, F.1    Martinez-Martinez, L.2    Conejo, M.C.3    Ayala, J.A.4    Perea, E.J.5    Pascual, A.6
  • 58
    • 0037262561 scopus 로고    scopus 로고
    • In vitro activity of azithromycin in combination with amikacin, ceftazidime, ciprofloxacin or imipenem against clinical isolates of Acinetobacter baumannii
    • DOI 10.1159/000069774
    • Fernandez-Cuenca, F., L. Martinez-Martinez, A. Pascual, and E. J. Perea. 2003. In vitro activity of azithromycin in combination with amikacin, ceftazidime, ciprofloxacin or imipenem against clinical isolates of Acinetobacter baumannii. Chemotherapy 49:24-26. (Pubitemid 36469791)
    • (2003) Chemotherapy , vol.49 , Issue.1-2 , pp. 24-26
    • Fernandez-Cuenca, F.1    Martinez-Martinez, L.2    Pascual, A.3    Perea, E.J.4
  • 59
    • 80051672898 scopus 로고    scopus 로고
    • Crystal structure of Serratia fonticola Sfh-I: Activation of the nucleophile in mono-zinc metallo-β-lactamases
    • Fonseca, F., E. H. Bromley, M. J. Saavedra, A. Correia, and J. Spencer. 2011. Crystal structure of Serratia fonticola Sfh-I: activation of the nucleophile in mono-zinc metallo-β-lactamases. J. Mol. Biol. 411:951-959.
    • (2011) J. Mol. Biol. , vol.411 , pp. 951-959
    • Fonseca, F.1    Bromley, E.H.2    Saavedra, M.J.3    Correia, A.4    Spencer, J.5
  • 60
    • 67349253074 scopus 로고    scopus 로고
    • Evaluation of meropenem alone and combined with rifampin in the guinea pig model of pneumococcal meningitis
    • Force, E., et al. 2009. Evaluation of meropenem alone and combined with rifampin in the guinea pig model of pneumococcal meningitis. Eur. J. Clin. Microbiol. Infect. Dis. 28:807-811.
    • (2009) Eur. J. Clin. Microbiol. Infect. Dis. , vol.28 , pp. 807-811
    • Force, E.1
  • 61
    • 70350357203 scopus 로고    scopus 로고
    • Mechanistic basis for the emergence of catalytic competence against carbapenem antibiotics by the GES family of β-lactamases
    • Frase, H., Q. Shi, S. A. Testero, S. Mobashery, and S. B. Vakulenko. 2009. Mechanistic basis for the emergence of catalytic competence against carbapenem antibiotics by the GES family of β-lactamases. J. Biol. Chem. 284:29509-29513.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29509-29513
    • Frase, H.1    Shi, Q.2    Testero, S.A.3    Mobashery, S.4    Vakulenko, S.B.5
  • 62
    • 0026725416 scopus 로고
    • Stability of meropenem and effect of 1 β-methyl substitution on its stability in the presence of renal dehydropeptidase I
    • Fukasawa, M., et al. 1992. Stability of meropenem and effect of 1 β-methyl substitution on its stability in the presence of renal dehydropeptidase I. Antimicrob. Agents Chemother. 36:1577-1579.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 1577-1579
    • Fukasawa, M.1
  • 64
    • 79952255053 scopus 로고    scopus 로고
    • Rapid increase of carbapenemase-producing Klebsiella pneumoniae strains in a large Italian hospital: Surveillance period 1 March-30 September 2010
    • pii=19800
    • Gaibani, P., et al. 2011. Rapid increase of carbapenemase-producing Klebsiella pneumoniae strains in a large Italian hospital: surveillance period 1 March-30 September 2010. Euro Surveill. 16:pii=19800.
    • (2011) Euro Surveill , vol.16
    • Gaibani, P.1
  • 65
    • 0023777977 scopus 로고
    • A survey of the kinetic parameters of class C β-lactamases. Cephalosporins and other β-lactam compounds
    • Galleni, M., G. Amicosante, and J. M. Frere. 1988. A survey of the kinetic parameters of class C β-lactamases. Cephalosporins and other β-lactam compounds. Biochem. J. 255:123-129.
    • (1988) Biochem. J. , vol.255 , pp. 123-129
    • Galleni, M.1    Amicosante, G.2    Frere, J.M.3
  • 66
    • 61349126689 scopus 로고    scopus 로고
    • Approaches to the simultaneous inactivation of metallo- and serine-β-lactamases
    • Ganta, S. R., et al. 2009. Approaches to the simultaneous inactivation of metallo- and serine-β-lactamases. Bioorg. Med. Chem. Lett. 19:1618-1622.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1618-1622
    • Ganta, S.R.1
  • 67
    • 10044225894 scopus 로고    scopus 로고
    • A metallo-β-lactamase enzyme in action: Crystal structures of the monozinc carbapenemase CphA and its complex with biapenem
    • DOI 10.1016/j.jmb.2004.10.070, PII S0022283604013762
    • Garau, G., et al. 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. (Pubitemid 39600934)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.4 , pp. 785-795
    • Garau, G.1    Bebrone, C.2    Anne, C.3    Galleni, M.4    Frere, J.-M.5    Dideberg, O.6
  • 68
    • 0025992960 scopus 로고
    • Imipenem resistance in Acinetobacter baumannii is due to altered penicillin-binding proteins
    • Gehrlein, M., H. Leying, W. Cullmann, S. Wendt, and W. Opferkuch. 1991. Imipenem resistance in Acinetobacter baumannii is due to altered penicillin-binding proteins. Chemotherapy 37:405-412.
    • (1991) Chemotherapy , vol.37 , pp. 405-412
    • Gehrlein, M.1    Leying, H.2    Cullmann, W.3    Wendt, S.4    Opferkuch, W.5
  • 69
    • 0033031973 scopus 로고    scopus 로고
    • Impaired imipenem uptake associated with alterations in outer membrane proteins and lipopolysaccharides in imipenem-resistant Shigella dysenteriae
    • DOI 10.1093/jac/43.2.195
    • Ghosh, A. S., A. K. Kar, and M. Kundu. 1999. Impaired imipenem uptake associated with alterations in outer membrane proteins and lipopolysaccharides in imipenem-resistant Shigella dysenteriae. J. Antimicrob. Chemother. 43:195-201. (Pubitemid 29082443)
    • (1999) Journal of Antimicrobial Chemotherapy , vol.43 , Issue.2 , pp. 195-201
    • Ghosh, A.S.1    Kar, A.K.2    Kundu, M.3
  • 71
    • 41149095072 scopus 로고    scopus 로고
    • Alterations of porin, pumps, and penicillin-binding proteins in carbapenem resistant clinical isolates of Pseudomonas aeruginosa
    • DOI 10.1089/mdr.2008.0778
    • Giske, C. G., L. Buaro, A. Sundsfjord, and B. Wretlind. 2008. Alterations of porin, pumps, and penicillin-binding proteins in carbapenem resistant clinical isolates of Pseudomonas aeruginosa. Microb. Drug Resist. 14:23-30. (Pubitemid 351441848)
    • (2008) Microbial Drug Resistance , vol.14 , Issue.1 , pp. 23-30
    • Giske, C.G.1    Buaro, L.2    Sundsfjord, A.3    Wretlind, B.4
  • 72
    • 0038754804 scopus 로고    scopus 로고
    • Panipenem/betamipron
    • Goa, K. L., and S. Noble. 2003. Panipenem/betamipron. Drugs 63:913-926.
    • (2003) Drugs , vol.63 , pp. 913-926
    • Goa, K.L.1    Noble, S.2
  • 73
    • 79956202403 scopus 로고    scopus 로고
    • Changing trends in antimicrobial susceptibility and hospital acquired infections over an 8 year period in a tertiary care hospital in relation to introduction of an infection control programme
    • Gopalakrishnan, R., and D. Sureshkumar. 2010. Changing trends in antimicrobial susceptibility and hospital acquired infections over an 8 year period in a tertiary care hospital in relation to introduction of an infection control programme. J. Assoc. Physicians India 58(Suppl.):25-31.
    • (2010) J. Assoc. Physicians India , vol.58 , Issue.SUPPL. , pp. 25-31
    • Gopalakrishnan, R.1    Sureshkumar, D.2
  • 74
    • 0023259926 scopus 로고
    • Inhibition of the mammalian β-lactamase renal dipeptidase (dehydropeptidase-I) by (Z)-2-(acylamino)-3-substituted-propenoic acids
    • Graham, D. W., et al. 1987. Inhibition of the mammalian β-lactamase renal dipeptidase (dehydropeptidase-I) by (Z)-2-(acylamino)-3-substituted- propenoic acids. J. Med. Chem. 30:1074-1090. (Pubitemid 17120791)
    • (1987) Journal of Medicinal Chemistry , vol.30 , Issue.6 , pp. 1074-1090
    • Graham, D.W.1    Ashton, W.T.2    Barash, L.3
  • 75
    • 44849142803 scopus 로고    scopus 로고
    • In vitro evaluation of the antimicrobial activity of meropenem in combination with polymyxin B and gatifloxacin against Pseudomonas aeruginosa and Acinetobacter baumannii
    • Guelfi, K. C., et al. 2008. In vitro evaluation of the antimicrobial activity of meropenem in combination with polymyxin B and gatifloxacin against Pseudomonas aeruginosa and Acinetobacter baumannii. J. Chemother. 20:180-185. (Pubitemid 351797057)
    • (2008) Journal of Chemotherapy , vol.20 , Issue.2 , pp. 180-185
    • Guelfi, K.C.1    Tognim, M.C.B.2    Cardoso, C.L.3    Gales, A.C.4    Carrara-Marrone, F.E.5    Garcia, L.B.6
  • 76
    • 0033203219 scopus 로고    scopus 로고
    • Combination effect of teicoplanin and various antibiotics against hetero-VRSA and VRSA
    • In Japanese
    • Hanaki, H., and K. Hiramatsu. 1999. Combination effect of teicoplanin and various antibiotics against hetero-VRSA and VRSA. Kansenshogaku Zasshi 73:1048-1053. (In Japanese.)
    • (1999) Kansenshogaku Zasshi , vol.73 , pp. 1048-1053
    • Hanaki, H.1    Hiramatsu, K.2
  • 77
    • 0036403720 scopus 로고    scopus 로고
    • Function of Pseudomonas porins in uptake and efflux
    • DOI 10.1146/annurev.micro.56.012302.160310
    • Hancock, R. E., and F. S. Brinkman. 2002. Function of Pseudomonas porins in uptake and efflux. Annu. Rev. Microbiol. 56:17-38. (Pubitemid 35217446)
    • (2002) Annual Review of Microbiology , vol.56 , pp. 17-38
    • Hancock, R.E.W.1    Brinkman, F.S.L.2
  • 80
    • 0036511914 scopus 로고    scopus 로고
    • Synthesis of the side chain of a novel carbapenem via iodine-mediated oxidative cyclization of (1R)-N-(1-aryl-3-butenyl)acetamide
    • DOI 10.1248/cpb.50.423
    • Hashihayata, T., H. Sakoh, Y. Goto, K. Yamada, and H. Morishima. 2002. Synthesis of the side chain of a novel carbapenem via iodine-mediated oxidative cyclization of (1R)-N-(1-aryl-3-butenyl)acetamide. Chem. Pharm. Bull. (Tokyo) 50:423-425. (Pubitemid 41685651)
    • (2002) Chemical and Pharmaceutical Bulletin , vol.50 , Issue.3 , pp. 423-425
    • Hashihayata, T.1    Sakoh, H.2    Goto, Y.3    Yamada, K.4    Morishima, H.5
  • 81
    • 0021139196 scopus 로고
    • Studies on the mechanism of action of imipenem (N-formimidoylthienamycin) in vitro: Binding to the penicillin-binding proteins (PBPs) in Escherichia coli and Pseudomonas aeruginosa and inhibition of enzyme activities due to the PBPs in E. coli
    • Hashizume, T., F. Ishino, J. Nakagawa, S. Tamaki, and M. Matsuhashi. 1984. Studies on the mechanism of action of imipenem (N-formimidoylthienamycin) in vitro: binding to the penicillin-binding proteins (PBPs) in Escherichia coli and Pseudomonas aeruginosa, and inhibition of enzyme activities due to the PBPs in E. coli. J. Antibiot. (Tokyo) 37:394-400. (Pubitemid 14129492)
    • (1984) Journal of Antibiotics , vol.37 , Issue.4 , pp. 394-400
    • Hashizume, T.1    Ishino, F.2    Nakagawa, J.3
  • 82
    • 0032818533 scopus 로고    scopus 로고
    • In vitro antibacterial activity of LJC 11,036, an active metabolite of L-084, a new oral carbapenem antibiotic with potent antipneumococcal activity
    • Hikida, M., K. Itahashi, A. Igarashi, T. Shiba, and M. Kitamura. 1999. In vitro antibacterial activity of LJC 11,036, an active metabolite of L-084, a new oral carbapenem antibiotic with potent antipneumococcal activity. Antimicrob. Agents Chemother. 43:2010-2016. (Pubitemid 29395201)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.8 , pp. 2010-2016
    • Hikida, M.1    Itahashi, K.2    Igarashi, A.3    Shiba, T.4    Kitamura, M.5
  • 83
    • 0026732827 scopus 로고
    • Inactivation of new carbapenem antibiotics by dehydropeptidase-I from porcine and human renal cortex
    • Hikida, M., K. Kawashima, M. Yoshida, and S. Mitsuhashi. 1992. Inactivation of new carbapenem antibiotics by dehydropeptidase-I from porcine and human renal cortex. J. Antimicrob. Chemother. 30:129-134.
    • (1992) J. Antimicrob. Chemother. , vol.30 , pp. 129-134
    • Hikida, M.1    Kawashima, K.2    Yoshida, M.3    Mitsuhashi, S.4
  • 84
    • 68349152498 scopus 로고    scopus 로고
    • Metallo-β-lactamase inhibitory activity of phthalic acid derivatives
    • Hiraiwa, Y., A. Morinaka, T. Fukushima, and T. Kudo. 2009. Metallo-β-lactamase inhibitory activity of phthalic acid derivatives. Bioorg. Med. Chem. Lett. 19:5162-5165.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5162-5165
    • Hiraiwa, Y.1    Morinaka, A.2    Fukushima, T.3    Kudo, T.4
  • 85
    • 67651218771 scopus 로고    scopus 로고
    • Efflux pump inhibitors reduce the invasiveness of Pseudomonas aeruginosa
    • Hirakata, Y., et al. 2009. Efflux pump inhibitors reduce the invasiveness of Pseudomonas aeruginosa. Int. J. Antimicrob. Agents 34:343-346.
    • (2009) Int. J. Antimicrob. Agents , vol.34 , pp. 343-346
    • Hirakata, Y.1
  • 86
    • 0021258806 scopus 로고
    • π-Allyltricarbonyliron lactone complexes in synthesis: Application to the synthesis of the β-lactam antibiotic (+)- thienamycin
    • Hodgson, S. T., D. M. Hollinshead, and S. V. Ley. 1984. π-Allyltricarbonyliron lactone complexes in synthesis: application to the synthesis of the β-lactam antibiotic (+)-thienamycin J. Chem. Soc. Chem. Commun. (Camb.) 1984:494-496. (Pubitemid 14103052)
    • (1984) Journal of the Chemical Society - Series Chemical Communications , vol.NO. 8 , pp. 494-496
    • Hodgson, S.T.1    Hollinshead, D.M.2    Ley, S.V.3
  • 87
    • 0029892737 scopus 로고    scopus 로고
    • The role of specific surface loop regions in determining the function of the imipenem-specific pore protein OprD of Pseudomonas aeruginosa
    • Huang, H., and R. E. Hancock. 1996. The role of specific surface loop regions in determining the function of the imipenem-specific pore protein OprD of Pseudomonas aeruginosa. J. Bacteriol. 178:3085-3090. (Pubitemid 26169348)
    • (1996) Journal of Bacteriology , vol.178 , Issue.11 , pp. 3085-3090
    • Huang, H.1    Hancock, R.E.W.2
  • 88
    • 0029101289 scopus 로고
    • Membrane topology and site-specific mutagenesis of Pseudomonas aeruginosa porin OprD
    • Huang, H., D. Jeanteur, F. Pattus, and R. E. Hancock. 1995. Membrane topology and site-specific mutagenesis of Pseudomonas aeruginosa porin OprD. Mol. Microbiol. 16:931-941.
    • (1995) Mol. Microbiol. , vol.16 , pp. 931-941
    • Huang, H.1    Jeanteur, D.2    Pattus, F.3    Hancock, R.E.4
  • 89
    • 0026739082 scopus 로고
    • Analysis of two gene regions involved in the expression of the imipenem-specific, outer membrane porin protein OprD of Pseudomonas aeruginosa
    • Huang, H., R. J. Siehnel, F. Bellido, E. Rawling, and R. E. Hancock. 1992. Analysis of two gene regions involved in the expression of the imipenem-specific, outer membrane porin protein OprD of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 76:267-273.
    • (1992) FEMS Microbiol. Lett. , vol.76 , pp. 267-273
    • Huang, H.1    Siehnel, R.J.2    Bellido, F.3    Rawling, E.4    Hancock, R.E.5
  • 90
    • 61349183785 scopus 로고    scopus 로고
    • Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis
    • Hugonnet, J. E., L. W. Tremblay, H. I. Boshoff, C. E. Barry, III, and J. S. Blanchard. 2009. Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis. Science 323:1215-1218.
    • (2009) Science , vol.323 , pp. 1215-1218
    • Hugonnet, J.E.1    Tremblay, L.W.2    Boshoff, H.I.3    Barry III, C.E.4    Blanchard, J.S.5
  • 91
    • 70350518310 scopus 로고    scopus 로고
    • Permeability of a novel β-lactamase inhibitor LK-157 and its ester prodrugs across rat jejunum in vitro
    • Iglicar, P., I. Legen, G. Vilfan, L. Selic, and A. Prezelj. 2009. Permeability of a novel β-lactamase inhibitor LK-157 and its ester prodrugs across rat jejunum in vitro. J. Pharm. Pharmacol. 61:1211-1218.
    • (2009) J. Pharm. Pharmacol. , vol.61 , pp. 1211-1218
    • Iglicar, P.1    Legen, I.2    Vilfan, G.3    Selic, L.4    Prezelj, A.5
  • 92
    • 0019141616 scopus 로고
    • 2, new carbapenem antibiotics. I. Taxonomy of the producing strain, fermentation and antibacterial properties
    • Imada, A., et al. 1980. C-19393 S2 and H2, new carbapenem antibiotics. I. Taxonomy of the producing strain, fermentation and antibacterial properties. J. Antibiot. (Tokyo) 33:1417-1424. (Pubitemid 11186857)
    • (1980) Journal of Antibiotics , vol.33 , Issue.12 , pp. 1417-1424
    • Imada, A.1    Nozaki, Y.2    Kintaka, K.3
  • 95
    • 0018343188 scopus 로고
    • Thienamycin, a new β-lactam antibiotic. I. Discovery, taxonomy, isolation and physical properties
    • Kahan, J. S., et al. 1979. Thienamycin, a new β-lactam antibiotic. I. Discovery, taxonomy, isolation and physical properties. J. Antibiot. (Tokyo) 32:1-12. (Pubitemid 9104065)
    • (1979) Journal of Antibiotics , vol.32 , Issue.1 , pp. 1-12
    • Kahan, J.S.1    Kahan, F.M.2    Goegelman, R.3
  • 96
    • 0027997238 scopus 로고
    • Antibiotic-related nephrotoxicity
    • Kaloyanides, G. J. 1994. Antibiotic-related nephrotoxicity. Nephrol. Dial. Transplant. 9(Suppl. 4):130-134. (Pubitemid 24249487)
    • (1994) Nephrology Dialysis Transplantation , vol.9 , Issue.SUPPL. 4 , pp. 130-134
    • Kaloyanides, G.J.1
  • 97
    • 55849091037 scopus 로고    scopus 로고
    • Carbapenems and SHV-1 β-lactamase form different acyl-enzyme populations in crystals and solution
    • Kalp, M., and P. R. Carey. 2008. Carbapenems and SHV-1 β-lactamase form different acyl-enzyme populations in crystals and solution. Biochemistry 47:11830-11837.
    • (2008) Biochemistry , vol.47 , pp. 11830-11837
    • Kalp, M.1    Carey, P.R.2
  • 100
    • 0942279626 scopus 로고    scopus 로고
    • PBP 2a Mutations Producing Very-High-Level Resistance to Beta-Lactams
    • DOI 10.1128/AAC.48.2.453-459.2004
    • Katayama, Y., H. Z. Zhang, and H. F. Chambers. 2004. PBP 2a mutations producing very-high-level resistance to β-lactams. Antimicrob. Agents Chemother. 48:453-459. (Pubitemid 38141701)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.2 , pp. 453-459
    • Katayama, Y.1    Zhang, H.-Z.2    Chambers, H.F.3
  • 103
    • 34248580602 scopus 로고    scopus 로고
    • Crystal structure of KPC-2: Insights into carbapenemase activity in class A β-lactamases
    • DOI 10.1021/bi700300u
    • Ke, W., C. R. Bethel, J. M. Thomson, R. A. Bonomo, and F. van den Akker. 2007. Crystal structure of KPC-2: insights into carbapenemase activity in class A β-lactamases. Biochemistry 46:5732-5740. (Pubitemid 46764122)
    • (2007) Biochemistry , vol.46 , Issue.19 , pp. 5732-5740
    • Ke, W.1    Bethel, C.R.2    Thomson, J.M.3    Bonomo, R.A.4    Van Den, A.F.5
  • 105
    • 70350718106 scopus 로고    scopus 로고
    • Pharmacokinetics analysis of tebipenem pivoxil in a phase II clinical trial in otolaryngological infections
    • In Japanese
    • Kijima, K., et al. 2009. Pharmacokinetics analysis of tebipenem pivoxil in a phase II clinical trial in otolaryngological infections. Jpn. J. Antibiot. 62:143-154. (In Japanese.)
    • (2009) Jpn. J. Antibiot. , vol.62 , pp. 143-154
    • Kijima, K.1
  • 106
    • 33646436194 scopus 로고    scopus 로고
    • Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C β-lactamase
    • Kim, J. Y., et al. 2006. Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C β-lactamase. Mol. Microbiol. 60:907-916.
    • (2006) Mol. Microbiol. , vol.60 , pp. 907-916
    • Kim, J.Y.1
  • 107
    • 0019966886 scopus 로고
    • Antimicrobial and β-lactamase inhibitory activities of carpetimycins A and B, new carbapenem antibiotics
    • Kobayashi, F., et al. 1982. Antimicrobial and β-lactamase inhibitory activities of carpetimycins A and B, new carbapenem antibiotics. Antimicrob. Agents Chemother. 21:536-544. (Pubitemid 12070517)
    • (1982) Antimicrobial Agents and Chemotherapy , vol.21 , Issue.4 , pp. 536-544
    • Kobayashi, F.1    Saino, Y.2    Koshi, T.3
  • 108
    • 27644484826 scopus 로고    scopus 로고
    • Study of the synergism between carbapenems and vancomycin or teicoplanin against MRSA, focusing on S-4661, a carbapenem newly developed in Japan
    • DOI 10.1007/s10156-005-0402-2
    • Kobayashi, Y. 2005. Study of the synergism between carbapenems and vancomycin or teicoplanin against MRSA, focusing on S-4661, a carbapenem newly developed in Japan. J. Infect. Chemother. 11:259-261. (Pubitemid 41570025)
    • (2005) Journal of Infection and Chemotherapy , vol.11 , Issue.5 , pp. 259-261
    • Kobayashi, Y.1
  • 109
    • 62949244999 scopus 로고    scopus 로고
    • Affinity of tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa
    • Koga, T., et al. 2009. Affinity of tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 53:1238-1241.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1238-1241
    • Koga, T.1
  • 110
    • 0344572646 scopus 로고    scopus 로고
    • Carbapenem activities against Pseudomonas aeruginosa: Respective contributions of OprD and efflux systems
    • Kohler, T., M. Michea-Hamzehpour, S. F. Epp, and J. C. Pechere. 1999. Carbapenem activities against Pseudomonas aeruginosa: respective contributions of OprD and efflux systems. Antimicrob. Agents Chemother. 43:424-427. (Pubitemid 29079192)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.2 , pp. 424-427
    • Kohler, T.1    Michea-Hamzehpour, M.2    Epp, S.F.3    Pechere, J.-C.4
  • 111
    • 78049240384 scopus 로고    scopus 로고
    • Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES β-lactamases
    • Kotsakis, S. D., V. Miriagou, E. Tzelepi, and L. S. Tzouvelekis. 2010. Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES β-lactamases. Antimicrob. Agents Chemother. 54:4864-4871.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4864-4871
    • Kotsakis, S.D.1    Miriagou, V.2    Tzelepi, E.3    Tzouvelekis, L.S.4
  • 114
    • 0019962519 scopus 로고
    • Metabolism of thienamycin and related carbapenem antibiotics by the renal dipeptidase, dehydropeptidase-I
    • Kropp, H., J. G. Sundelof, R. Hajdu, and F. M. Kahan. 1982. Metabolism of thienamycin and related carbapenem antibiotics by the renal dipeptidase, dehydropeptidase. Antimicrob. Agents Chemother. 22:62-70. (Pubitemid 12029995)
    • (1982) Antimicrobial Agents and Chemotherapy , vol.22 , Issue.1 , pp. 62-70
    • Kropp, H.1    Sundelof, J.G.2    Hajdu, R.3    Khan, F.M.4
  • 115
    • 77955660592 scopus 로고    scopus 로고
    • Investigation of pneumonia-causing pathogenic organisms in children and the usefulness of tebipenem pivoxil for their treatment
    • Kuroki, H., N. Tateno, H. Ikeda, and N. Saito. 2010. Investigation of pneumonia-causing pathogenic organisms in children and the usefulness of tebipenem pivoxil for their treatment. J. Infect. Chemother. 16:280-287.
    • (2010) J. Infect. Chemother. , vol.16 , pp. 280-287
    • Kuroki, H.1    Tateno, N.2    Ikeda, H.3    Saito, N.4
  • 116
    • 0032896617 scopus 로고    scopus 로고
    • When drug inactivation renders the target irrelevant to antibiotic resistance: A case story with β-lactams
    • DOI 10.1046/j.1365-2958.1999.01150.x
    • Lakaye, B., A. Dubus, S. Lepage, S. Groslambert, and J. M. Frere. 1999. When drug inactivation renders the target irrelevant to antibiotic resistance: a case story with β-lactams. Mol. Microbiol. 31:89-101. (Pubitemid 29012151)
    • (1999) Molecular Microbiology , vol.31 , Issue.1 , pp. 89-101
    • Lakaye, B.1    Dubus, A.2    Lepage, S.3    Groslambert, S.4    Frere, J.-M.5
  • 119
    • 0346100720 scopus 로고    scopus 로고
    • Risk factors for acquisition of imipenem-resistant Acinetobacter baumannii: A case-control study
    • Lee, S. O., et al. 2004. Risk factors for acquisition of imipenem-resistant Acinetobacter baumannii: a case-control study. Antimicrob. Agents Chemother. 48:224-228.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 224-228
    • Lee, S.O.1
  • 120
    • 71249096041 scopus 로고    scopus 로고
    • Imipenem-resistant Pseudomonas aeruginosa gastrointestinal carriage among hospitalized patients: Risk factors and resistance mechanisms
    • Lepelletier, D., et al. 2010. Imipenem-resistant Pseudomonas aeruginosa gastrointestinal carriage among hospitalized patients: risk factors and resistance mechanisms. Diagn. Microbiol. Infect. Dis. 66:1-6.
    • (2010) Diagn. Microbiol. Infect. Dis. , vol.66 , pp. 1-6
    • Lepelletier, D.1
  • 121
    • 0036900235 scopus 로고    scopus 로고
    • Loss of a 29-kilodalton outer membrane protein in Acinetobacter baumannii is associated with imipenem resistance
    • DOI 10.1128/JCM.40.12.4776-4778.2002
    • Limansky, A. S., M. A. Mussi, and A. M. Viale. 2002. Loss of a 29-kilodalton outer membrane protein in Acinetobacter baumannii is associated with imipenem resistance. J. Clin. Microbiol. 40:4776-4778. (Pubitemid 35434989)
    • (2002) Journal of Clinical Microbiology , vol.40 , Issue.12 , pp. 4776-4778
    • Limansky, A.S.1    Mussi, M.A.2    Viale, A.M.3
  • 122
    • 77951160840 scopus 로고    scopus 로고
    • Catalytic role of the metal ion in the metallo-β-lactamase GOB
    • Lisa, M. N., L. Hemmingsen, and A. J. Vila. 2010. Catalytic role of the metal ion in the metallo-β-lactamase GOB. J. Biol. Chem. 285:4570-4577.
    • (2010) J. Biol. Chem. , vol.285 , pp. 4570-4577
    • Lisa, M.N.1    Hemmingsen, L.2    Vila, A.J.3
  • 123
    • 79953851292 scopus 로고    scopus 로고
    • What remains against carbapenem-resistant Enterobacteriaceae? Evaluation of chloramphenicol, ciprofloxacin, colistin, fosfomycin, minocycline, nitrofurantoin, temocillin and tigecycline
    • Livermore, D. M., et al. 2011. What remains against carbapenem-resistant Enterobacteriaceae? Evaluation of chloramphenicol, ciprofloxacin, colistin, fosfomycin, minocycline, nitrofurantoin, temocillin and tigecycline. Int. J. Antimicrob. Agents 37:415-419.
    • (2011) Int. J. Antimicrob. Agents , vol.37 , pp. 415-419
    • Livermore, D.M.1
  • 124
    • 77952607034 scopus 로고    scopus 로고
    • The combination of meropenem and levofloxacin is synergistic with respect to both Pseudomonas aeruginosa kill rate and resistance suppression
    • Louie, A., et al. 2010. The combination of meropenem and levofloxacin is synergistic with respect to both Pseudomonas aeruginosa kill rate and resistance suppression. Antimicrob. Agents Chemother. 54:2646-2654.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2646-2654
    • Louie, A.1
  • 125
    • 79951487602 scopus 로고    scopus 로고
    • An alkylaminoquinazoline restores antibiotic activity in Gram-negative resistant isolates
    • Mahamoud, A., J. Chevalier, M. Baitiche, E. Adam, and J. M. Pages. 2010. An alkylaminoquinazoline restores antibiotic activity in Gram-negative resistant isolates. Microbiology 157:566-571.
    • (2010) Microbiology , vol.157 , pp. 566-571
    • Mahamoud, A.1    Chevalier, J.2    Baitiche, M.3    Adam, E.4    Pages, J.M.5
  • 126
    • 0030699988 scopus 로고    scopus 로고
    • Carbapenem resistance in a clinical isolate of Citrobacter freundii
    • Mainardi, J. L., et al. 1997. Carbapenem resistance in a clinical isolate of Citrobacter freundii. Antimicrob. Agents Chemother. 41:2352-2354.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 2352-2354
    • Mainardi, J.L.1
  • 127
    • 23044482926 scopus 로고    scopus 로고
    • Amino acid residues that contribute to substrate specificity of class a β-lactamase SME-1
    • DOI 10.1128/AAC.49.8.3421-3427.2005
    • Majiduddin, F. K., and T. Palzkill. 2005. Amino acid residues that contribute to substrate specificity of class A β-lactamase SME-1. Antimicrob. Agents Chemother. 49:3421-3427. (Pubitemid 41060591)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.8 , pp. 3421-3427
    • Majiduddin, F.K.1    Palzkill, T.2
  • 128
    • 78049319835 scopus 로고    scopus 로고
    • Phenotypic and biochemical comparison of the carbapenem hydrolyzing activity of five plasmid-borne AmpC β-lactamases
    • Mammeri, H., H. Guillon, F. Eb, and P. Nordmann. 2010. Phenotypic and biochemical comparison of the carbapenem hydrolyzing activity of five plasmid-borne AmpC β-lactamases. Antimicrob. Agents Chemother. 54:4556-4560.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4556-4560
    • Mammeri, H.1    Guillon, H.2    Eb, F.3    Nordmann, P.4
  • 129
    • 42449132083 scopus 로고    scopus 로고
    • Contribution of extended-spectrum AmpC (ESAC) β-lactamases to carbapenem resistance in Escherichia coli
    • DOI 10.1111/j.1574-6968.2008.01126.x
    • Mammeri, H., P. Nordmann, A. Berkani, and F. Eb. 2008. Contribution of extended-spectrum AmpC (ESAC) β-lactamases to carbapenem resistance in Escherichia coli. FEMS Microbiol. Lett. 282:238-240. (Pubitemid 351569457)
    • (2008) FEMS Microbiology Letters , vol.282 , Issue.2 , pp. 238-240
    • Mammeri, H.1    Nordmann, P.2    Berkani, A.3    Eb, F.4
  • 130
    • 67749101888 scopus 로고    scopus 로고
    • Doripenem: A new carbapenem in the treatment of nosocomial infection
    • Mandell, L. 2009. Doripenem: a new carbapenem in the treatment of nosocomial infection. Clin. Infect. Dis. 49(Suppl. 1):S1-S3.
    • (2009) Clin. Infect. Dis. , vol.49 , Issue.SUPPL. 1
    • Mandell, L.1
  • 131
    • 37249041424 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases and the permeability barrier
    • Martinez-Martinez, L. 2008. Extended-spectrum β-lactamases and the permeability barrier. Clin. Microbiol. Infect. 14(Suppl. 1):82-89.
    • (2008) Clin. Microbiol. Infect. , vol.14 , Issue.SUPPL. 1 , pp. 82-89
    • Martinez-Martinez, L.1
  • 132
    • 0030180057 scopus 로고    scopus 로고
    • Evaluation of high-level carbapenem resistance in atypical Serratia marcescens by a comparison with its revertants
    • Marumo, K., T. Nagaki, and Y. Nakamura. 1996. Evaluation of high-level carbapenem resistance in atypical Serratia marcescens by a comparison with its revertants. J. Antimicrob. Chemother. 38:47-58. (Pubitemid 126449208)
    • (1996) Journal of Antimicrobial Chemotherapy , vol.38 , Issue.1 , pp. 47-58
    • Marumo, K.1    Nagaki, T.2    Nakamura, Y.3
  • 133
    • 0026566526 scopus 로고
    • Synthesis and antibacterial activity of some novel 6-methyl- and 6-propenyl-substituted carbapenems
    • Mastalerz, H., M. Menard, E. Ruediger, and J. Fung-Tomc. 1992. Synthesis and antibacterial activity of some novel 6-methyl- and 6-propenyl-substituted carbapenems. J. Med. Chem. 35:953-958.
    • (1992) J. Med. Chem. , vol.35 , pp. 953-958
    • Mastalerz, H.1    Menard, M.2    Ruediger, E.3    Fung-Tomc, J.4
  • 134
  • 135
  • 137
    • 33645240931 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial cell wall peptidoglycan
    • Meroueh, S. O., et al. 2006. Three-dimensional structure of the bacterial cell wall peptidoglycan. Proc. Natl. Acad. Sci. U. S. A. 103:4404-4409.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4404-4409
    • Meroueh, S.O.1
  • 138
    • 67650227781 scopus 로고    scopus 로고
    • Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries
    • Minond, D., et al. 2009. Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries. Bioorg. Med. Chem. 17:5027-5037.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 5027-5037
    • Minond, D.1
  • 139
    • 33750300138 scopus 로고    scopus 로고
    • In vitro activity effects of combinations of cephalothin, dicloxacillin, imipenem, vancomycin and amikacin against methicillin-resistant Staphylococcus spp. strains
    • Miranda-Novales, G., B. E. Leanos-Miranda, M. Vilchis-Perez, and F. Solorzano-Santos. 2006. In vitro activity effects of combinations of cephalothin, dicloxacillin, imipenem, vancomycin and amikacin against methicillin-resistant Staphylococcus spp. strains. Ann. Clin. Microbiol. Antimicrob. 5:25.
    • (2006) Ann. Clin. Microbiol. Antimicrob. , vol.5 , pp. 25
    • Miranda-Novales, G.1    Leanos-Miranda, B.E.2    Vilchis-Perez, M.3    Solorzano-Santos, F.4
  • 140
    • 64649089196 scopus 로고    scopus 로고
    • Assembly and transport mechanism of tripartite drug efflux systems
    • Misra, R., and V. N. Bavro. 2009. Assembly and transport mechanism of tripartite drug efflux systems. Biochim. Biophys. Acta 1794:817-825.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 817-825
    • Misra, R.1    Bavro, V.N.2
  • 141
    • 0020594264 scopus 로고
    • Synthesis and in vitro activity of a new carbapenem, RS-533
    • Miyadera, T., et al. 1983. Synthesis and in vitro activity of a new carbapenem, RS-533. J. Antibiot. (Tokyo) 36:1034-1039. (Pubitemid 13046928)
    • (1983) Journal of Antibiotics , vol.36 , Issue.8 , pp. 1034-1039
    • Miyadera, T.1    Sugimura, Y.2    Hashimoto, T.3
  • 145
    • 0023765072 scopus 로고
    • Imipenem as substrate and inhibitor of β-lactamases
    • Monks, J., and S. G. Waley. 1988. Imipenem as substrate and inhibitor of β-lactamases. Biochem. J. 253:323-328.
    • (1988) Biochem. J. , vol.253 , pp. 323-328
    • Monks, J.1    Waley, S.G.2
  • 146
    • 0028274174 scopus 로고
    • Investigation of the potential role of Enterococcus faecalis in the pathophysiology of experimental peritonitis
    • Montravers, P., A. Andremont, L. Massias, and C. Carbon. 1994. Investigation of the potential role of Enterococcus faecalis in the pathophysiology of experimental peritonitis. J. Infect. Dis. 169:821-830. (Pubitemid 24102116)
    • (1994) Journal of Infectious Diseases , vol.169 , Issue.4 , pp. 821-830
    • Montravers, P.1    Andremont, A.2    Massias, L.3    Carbon, C.4
  • 147
    • 0020325838 scopus 로고
    • Asparenomycins A, B and C, new carbapenem antibiotics. V. Inhibition of β-lactamases
    • Murakami, K., M. Doi, and T. Yoshida. 1982. Asparenomycins A, B and C, new carbapenem antibiotics. V. Inhibition of β-lactamases. J. Antibiot. (Tokyo) 35:39-45. (Pubitemid 12069738)
    • (1982) Journal of Antibiotics , vol.35 , Issue.1 , pp. 39-45
    • Murakami, K.1    Dor, M.2    Yoshida, T.3
  • 148
    • 70350717082 scopus 로고    scopus 로고
    • Antimicrobial activity of tebipenem against various clinical isolates from various specimen, mainly urinary tract
    • In Japanese
    • Muratani, T., K. Doi, T. Kobayashi, T. Nakamura, and T. Matsumoto. 2009. Antimicrobial activity of tebipenem against various clinical isolates from various specimen, mainly urinary tract. Jpn. J. Antibiot. 62:116-126. (In Japanese.)
    • (2009) Jpn. J. Antibiot. , vol.62 , pp. 116-126
    • Muratani, T.1    Doi, K.2    Kobayashi, T.3    Nakamura, T.4    Matsumoto, T.5
  • 149
    • 0019252542 scopus 로고
    • Carpetimycins A and B, new β-lactam antibiotics
    • Tokyo
    • Nakayama, M., et al. 1980. Carpetimycins A and B, new β-lactam antibiotics. J. Antibiot. (Tokyo) 33:1388-1390.
    • (1980) J. Antibiot. , vol.33 , pp. 1388-1390
    • Nakayama, M.1
  • 150
    • 0029050279 scopus 로고
    • Imipenem resistance in clinical isolates of Proteus mirabilis associated with alterations in penicillin-binding proteins
    • Neuwirth, C., E. Siebor, J. M. Duez, A. Pechinot, and A. Kazmierczak. 1995. Imipenem resistance in clinical isolates of Proteus mirabilis associated with alterations in penicillin-binding proteins. J. Antimicrob. Chemother. 36:335-342.
    • (1995) J. Antimicrob. Chemother. , vol.36 , pp. 335-342
    • Neuwirth, C.1    Siebor, E.2    Duez, J.M.3    Pechinot, A.4    Kazmierczak, A.5
  • 151
    • 38849186031 scopus 로고    scopus 로고
    • The current state of multidrug-resistant gram-negative bacilli in North America
    • Nicasio, A. M., J. L. Kuti, and D. P. Nicolau. 2008. The current state of multidrug-resistant gram-negative bacilli in North America. Pharmacotherapy 28:235-249.
    • (2008) Pharmacotherapy , vol.28 , pp. 235-249
    • Nicasio, A.M.1    Kuti, J.L.2    Nicolau, D.P.3
  • 152
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of gram-negative bacteria
    • Nikaido, H. 1996. Multidrug efflux pumps of gram-negative bacteria. J. Bacteriol. 178:5853-5859. (Pubitemid 26337766)
    • (1996) Journal of Bacteriology , vol.178 , Issue.20 , pp. 5853-5859
    • Nikaido, H.1
  • 153
    • 3042637085 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of ertapenem: An overview for clinicians
    • Nix, D. E., A. K. Majumdar, and M. J. DiNubile. 2004. Pharmacokinetics and pharmacodynamics of ertapenem: an overview for clinicians. J. Antimicrob. Chemother. 53(Suppl. 2):ii23-ii28.
    • (2004) J. Antimicrob. Chemother. , vol.53 , Issue.SUPPL. 2
    • Nix, D.E.1    Majumdar, A.K.2    DiNubile, M.J.3
  • 154
    • 0027180832 scopus 로고
    • Penicillin-binding proteins of Rhodococcus equi: Potential role in resistance to imipenem
    • Nordmann, P., M. H. Nicolas, and L. Gutmann. 1993. Penicillin-binding proteins of Rhodococcus equi: potential role in resistance to imipenem. Antimicrob. Agents Chemother. 37:1406-1409. (Pubitemid 23202361)
    • (1993) Antimicrobial Agents and Chemotherapy , vol.37 , Issue.7 , pp. 1406-1409
    • Nordmann, P.1    Nicolas, M.H.2    Gutmann, L.3
  • 155
    • 79954606179 scopus 로고    scopus 로고
    • Comparative activity of carbapenem testing: The COMPACT study
    • Nordmann, P., et al. 2011. Comparative activity of carbapenem testing: the COMPACT study. J. Antimicrob. Chemother. 66:1070-1078.
    • (2011) J. Antimicrob. Chemother. , vol.66 , pp. 1070-1078
    • Nordmann, P.1
  • 156
    • 0029823378 scopus 로고    scopus 로고
    • Neurotoxicity of carbapenem antibacterials
    • Norrby, S. R. 1996. Neurotoxicity of carbapenem antibacterials. Drug Saf. 15:87-90. (Pubitemid 26288228)
    • (1996) Drug Safety , vol.15 , Issue.2 , pp. 87-90
    • Norrby, S.R.1
  • 157
    • 0020693414 scopus 로고
    • Urinary recovery of N-formimidoyl thienamycin (MK0787) as affected by coadministration of N-formimidoyl thienamycin dehydropeptidase inhibitors
    • Norrby, S. R., et al. 1983. Urinary recovery of N-formimidoyl thienamycin (MK0787) as affected by coadministration of N-formimidoyl thienamycin dehydropeptidase inhibitors. Antimicrob. Agents Chemother. 23:300-307. (Pubitemid 13137542)
    • (1983) Antimicrobial Agents and Chemotherapy , vol.23 , Issue.2 , pp. 300-307
    • Norrby, S.R.1    Alestig, K.2    Bjornegard, B.3
  • 158
    • 0021320174 scopus 로고
    • Structure-activity relations of 5,6-cis carbapenem antibiotics and role of factors determining susceptibility of Escherichia coli to β-lactam antibiotics
    • Nozaki, Y., S. Harada, K. Kitano, and A. Imada. 1984. Structure-activity relations of 5,6-cis carbapenem antibiotics and role of factors determining susceptibility of Escherichia coli to β-lactam antibiotics. J. Antibiot. (Tokyo) 37:218-226. (Pubitemid 14172309)
    • (1984) Journal of Antibiotics , vol.37 , Issue.3 , pp. 218-226
    • Nozaki, Y.1    Harada, S.2    Kitano, K.3    Imada, A.4
  • 159
    • 52449111304 scopus 로고    scopus 로고
    • Inhibition of class A β-lactamases by carbapenems: Crystallographic observation of two conformations of meropenem in SHV-1
    • Nukaga, M., et al. 2008. Inhibition of class A β-lactamases by carbapenems: crystallographic observation of two conformations of meropenem in SHV-1. J. Am. Chem. Soc. 130:12656-12662.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12656-12662
    • Nukaga, M.1
  • 160
    • 0037398367 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the β-lactam carbapenem thienamycin in Streptomyces cattleya
    • DOI 10.1016/S1074-5521(03)00069-3
    • Nunez, L. E., C. Mendez, A. F. Brana, G. Blanco, and J. A. Salas. 2003. The biosynthetic gene cluster for the β-lactam carbapenem thienamycin in Streptomyces cattleya. Chem. Biol. 10:301-311. (Pubitemid 36516648)
    • (2003) Chemistry and Biology , vol.10 , Issue.4 , pp. 301-311
    • Nunez, L.E.1    Mendez, C.2    Brana, A.F.3    Blanco, G.4    Salas, J.A.5
  • 161
    • 0032959773 scopus 로고    scopus 로고
    • Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids
    • Ochs, M. M., M. P. McCusker, M. Bains, and R. E. Hancock. 1999. Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids. Antimicrob. Agents Chemother. 43:1085-1090. (Pubitemid 29214729)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.5 , pp. 1085-1090
    • Ochs, M.M.1    McCusker, M.P.2    Bains, M.3    Hancock, R.E.W.4
  • 162
    • 0020413258 scopus 로고
    • Studies on the OA-6129 group of antibiotics, new carbapenem compounds. I. Taxonomy, isolation and physical properties
    • Okabe, M., et al. 1982. Studies on the OA-6129 group of antibiotics, new carbapenem compounds. I. Taxonomy, isolation and physical properties. J. Antibiot. (Tokyo) 35:1255-1263. (Pubitemid 13212101)
    • (1982) Journal of Antibiotics , vol.35 , Issue.10 , pp. 1255-1263
    • Okabe, M.1    Azuma, S.2    Kojima, I.3
  • 163
    • 0017816929 scopus 로고
    • PS-5, a new β-lactam antibiotic from streptomyces
    • Okamura, K., et al. 1978. PS-5, a new β-lactam antibiotic from Streptomyces. J. Antibiot. (Tokyo) 31:480-482. (Pubitemid 8359947)
    • (1978) Journal of Antibiotics , vol.31 , Issue.5 , pp. 480-482
    • Okamura, K.1    Hirata, S.2    Okumura, Y.3
  • 164
    • 7244240733 scopus 로고    scopus 로고
    • Hypermutation and the preexistence of antibiotic-resistant Pseudomonas aeruginosa mutants: Implications for susceptibility testing and treatment of chronic infections
    • DOI 10.1128/AAC.48.11.4226-4233.2004
    • Oliver, A., B. R. Levin, C. Juan, F. Baquero, and J. Blazquez. 2004. Hypermutation and the preexistence of antibiotic-resistant Pseudomonas aeruginosa mutants: implications for susceptibility testing and treatment of chronic infections. Antimicrob. Agents Chemother. 48:4226-4233. (Pubitemid 39434879)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.11 , pp. 4226-4233
    • Oliver, A.1    Levin, B.R.2    Juan, C.3    Baquero, F.4    Blazquez, J.5
  • 165
    • 21444442865 scopus 로고    scopus 로고
    • Genetic approach to study the relationship between penicillin-binding protein 3 mutations and Haemophilus influenzae β-lactam resistance by using site-directed mutagenesis and gene recombinants
    • DOI 10.1128/AAC.49.7.2834-2839.2005
    • Osaki, Y., et al. 2005. Genetic approach to study the relationship between penicillin-binding protein 3 mutations and Haemophilus influenzae β-lactam resistance by using site-directed mutagenesis and gene recombinants. Antimicrob. Agents Chemother. 49:2834-2839. (Pubitemid 40917599)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.7 , pp. 2834-2839
    • Osaki, Y.1    Sanbongi, Y.2    Ishikawa, M.3    Kataoka, H.4    Suzuki, T.5    Maeda, K.6    Ida, T.7
  • 166
    • 55549116670 scopus 로고    scopus 로고
    • Emergence of imipenem resistance in clinical Escherichia coli during therapy
    • Oteo, J., et al. 2008. Emergence of imipenem resistance in clinical Escherichia coli during therapy. Int. J. Antimicrob. Agents 32:534-537.
    • (2008) Int. J. Antimicrob. Agents , vol.32 , pp. 534-537
    • Oteo, J.1
  • 167
    • 0033793334 scopus 로고    scopus 로고
    • Crystal structure of the class D β-lactamase OXA-10
    • Paetzel, M., et al. 2000. Crystal structure of the class D β-lactamase OXA-10. Nat. Struct. Biol. 7:918-925.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 918-925
    • Paetzel, M.1
  • 169
    • 37849040424 scopus 로고    scopus 로고
    • Activity of meropenem with and without ciprofloxacin and colistin against Pseudomonas aeruginosa and Acinetobacter baumannii
    • Pankuch, G. A., G. Lin, H. Seifert, and P. C. Appelbaum. 2008. Activity of meropenem with and without ciprofloxacin and colistin against Pseudomonas aeruginosa and Acinetobacter baumannii. Antimicrob. Agents Chemother. 52:333-336.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 333-336
    • Pankuch, G.A.1    Lin, G.2    Seifert, H.3    Appelbaum, P.C.4
  • 170
    • 77953764780 scopus 로고    scopus 로고
    • Substrate selectivity and a novel role in inhibitor discrimination by position 237 in the KPC-2 β-lactamase
    • Papp-Wallace, K. M., et al. 2010. Substrate selectivity and a novel role in inhibitor discrimination by position 237 in the KPC-2 β-lactamase. Antimicrob. Agents Chemother. 54:2867-2877.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2867-2877
    • Papp-Wallace, K.M.1
  • 171
    • 77956370566 scopus 로고    scopus 로고
    • Elucidating the role of Trp105 in the KPC-2 β-lactamase
    • Papp-Wallace, K. M., et al. 2010. Elucidating the role of Trp105 in the KPC-2 β-lactamase. Protein Sci. 19:1714-1727.
    • (2010) Protein Sci. , vol.19 , pp. 1714-1727
    • Papp-Wallace, K.M.1
  • 172
    • 0020461155 scopus 로고
    • SQ 27,860, a simple carbapenem produced by species of Serratia and Erwinia
    • Parker, W. L., et al. 1982. SQ 27,860, a simple carbapenem produced by species of Serratia and Erwinia. J. Antibiot. (Tokyo) 35:653-660. (Pubitemid 13221967)
    • (1982) Journal of Antibiotics , vol.35 , Issue.6 , pp. 653-660
    • Parker, W.L.1    Rathnum, M.L.2    Wells Jr., J.S.3
  • 173
    • 79957581336 scopus 로고    scopus 로고
    • Status report on carbapenemases: Challenges and prospects
    • Patel, G., and R. A. Bonomo. 2011. Status report on carbapenemases: challenges and prospects. Expert Rev. Anti Infect. Ther. 9:555-570.
    • (2011) Expert Rev. Anti Infect. Ther. , vol.9 , pp. 555-570
    • Patel, G.1    Bonomo, R.A.2
  • 174
    • 0034285477 scopus 로고    scopus 로고
    • Recommendation for treatment of severe infections caused by Enterobacteriaceae producing extended-spectrum β-lactamases (ESBLs)
    • DOI 10.1046/j.1469-0691.2000.00107.x
    • Paterson, D. L. 2000. Recommendation for treatment of severe infections caused by Enterobacteriaceae producing extended-spectrum β-lactamases (ESBLs). Clin. Microbiol. Infect. 6:460-463. (Pubitemid 34966064)
    • (2000) Clinical Microbiology and Infection , vol.6 , Issue.9 , pp. 460-463
    • Paterson, D.L.1
  • 175
    • 0036898574 scopus 로고    scopus 로고
    • Serious infections caused by enteric gram-negative bacilli - Mechanisms of antibiotic resistance and implications for therapy of gram-negative sepsis in the transplanted patient
    • DOI 10.1053/srin.2002.36446
    • Paterson, D. L. 2002. Serious infections caused by enteric gram-negative bacilli - mechanisms of antibiotic resistance and implications for therapy of gram-negative sepsis in the transplanted patient. Semin. Respir. Infect. 17:260-264. (Pubitemid 35453642)
    • (2002) Seminars in Respiratory Infections , vol.17 , Issue.4 , pp. 260-264
    • Paterson, D.L.1
  • 176
    • 27144490073 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases: A clinical update
    • Paterson, D. L., and R. A. Bonomo. 2005. Extended-spectrum β-lactamases: a clinical update. Clin. Microbiol. Rev. 18:657-686.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 657-686
    • Paterson, D.L.1    Bonomo, R.A.2
  • 177
    • 59749085456 scopus 로고    scopus 로고
    • In vitro activity of LK-157, a novel tricyclic carbapenem as broad-spectrum β-lactamase inhibitor
    • Paukner, S., L. Hesse, A. Prezelj, T. Solmajer, and U. Urleb. 2009. In vitro activity of LK-157, a novel tricyclic carbapenem as broad-spectrum β-lactamase inhibitor. Antimicrob. Agents Chemother. 53:505-511.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 505-511
    • Paukner, S.1    Hesse, L.2    Prezelj, A.3    Solmajer, T.4    Urleb, U.5
  • 178
    • 0032989877 scopus 로고    scopus 로고
    • Active efflux and diffusion are involved in transport of Pseudomonas aeruginosa cell-to-cell signals
    • Pearson, J. P., C. Van Delden, and B. H. Iglewski. 1999. Active efflux and diffusion are involved in transport of Pseudomonas aeruginosa cell-to-cell signals. J. Bacteriol. 181:1203-1210. (Pubitemid 29119559)
    • (1999) Journal of Bacteriology , vol.181 , Issue.4 , pp. 1203-1210
    • Pearson, J.P.1    Van Delden, C.2    Iglewski, B.H.3
  • 181
    • 0036032533 scopus 로고    scopus 로고
    • Biapenem
    • Perry, C. M., and T. Ibbotson. 2002. Biapenem. Drugs 62:2221-2235.
    • (2002) Drugs , vol.62 , pp. 2221-2235
    • Perry, C.M.1    Ibbotson, T.2
  • 182
    • 54049149405 scopus 로고    scopus 로고
    • Genetic and structural insights into the dissemination potential of the extremely broad-spectrum class A β-lactamase KPC-2 identified in an Escherichia coli strain and an Enterobacter cloacae strain isolated from the same patient in France
    • Petrella, S., et al. 2008. Genetic and structural insights into the dissemination potential of the extremely broad-spectrum class A β-lactamase KPC-2 identified in an Escherichia coli strain and an Enterobacter cloacae strain isolated from the same patient in France. Antimicrob. Agents Chemother. 52:3725-3736.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3725-3736
    • Petrella, S.1
  • 183
    • 0019443222 scopus 로고
    • Structure, reactivity, and biological activity of strained bicyclic β-lactams
    • DOI 10.1021/ja00405a039
    • Pfaendler, H. R., J. R. Gostel, R. B. Woodward, and G. Rihs. 1981. Structure, reactivity, and biological activity of strained bicyclic β-lactams. J. Am. Chem. Soc. 103:4526-4531. (Pubitemid 11028843)
    • (1981) Journal of the American Chemical Society , vol.103 , Issue.15 , pp. 4526-4531
    • Pfaendler, H.R.1    Gosteli, J.2    Woodward, R.B.3    Rihs, G.4
  • 184
    • 0029399368 scopus 로고
    • Activity of biapenem (LJC 10627) against 51 imipenem-resistant bacteria and selection and characterisation of biapenem-resistant mutants
    • Piddock, L. J., and Y. F. Jin. 1995. Activity of biapenem (LJC 10627) against 51 imipenem-resistant bacteria and selection and characterisation of biapenem-resistant mutants. J. Antimicrob. Chemother. 36:845-850.
    • (1995) J. Antimicrob. Chemother. , vol.36 , pp. 845-850
    • Piddock, L.J.1    Jin, Y.F.2
  • 185
    • 0025126447 scopus 로고
    • Alteration of PBP 3 entails resistance to imipenem in Listeria monocytogenes
    • Pierre, J., A. Boisivon, and L. Gutmann. 1990. Alteration of PBP 3 entails resistance to imipenem in Listeria monocytogenes. Antimicrob. Agents Chemother. 34:1695-1698. (Pubitemid 20259495)
    • (1990) Antimicrobial Agents and Chemotherapy , vol.34 , Issue.9 , pp. 1695-1698
    • Pierre, J.1    Boisivon, A.2    Gutmann, L.3
  • 187
    • 35348905611 scopus 로고    scopus 로고
    • Carbapenemases: Molecular diversity and clinical consequences
    • DOI 10.2217/17460913.2.5.501
    • Poirel, L., J. D. Pitout, and P. Nordmann. 2007. Carbapenemases: molecular diversity and clinical consequences. Future Microbiol. 2:501-512. (Pubitemid 47578214)
    • (2007) Future Microbiology , vol.2 , Issue.5 , pp. 501-512
    • Poirel, L.1    Pitout, J.D.2    Nordmann, P.3
  • 188
    • 77949700523 scopus 로고    scopus 로고
    • Antibacterial activity of carbapenem-based combinations against multidrug-resistant Acinetobacter baumannii
    • Pongpech, P., et al. 2010. Antibacterial activity of carbapenem-based combinations against multidrug-resistant Acinetobacter baumannii. J. Med. Assoc. Thai. 93:161-171.
    • (2010) J. Med. Assoc. Thai. , vol.93 , pp. 161-171
    • Pongpech, P.1
  • 189
    • 34547422759 scopus 로고    scopus 로고
    • Carbapenemases: The versatile β-lactamases
    • table of contents
    • Queenan, A. M., and K. Bush. 2007. Carbapenemases: the versatile β-lactamases. Clin. Microbiol. Rev. 20:440-458, table of contents.
    • (2007) Clin. Microbiol. Rev. , vol.20 , pp. 440-458
    • Queenan, A.M.1    Bush, K.2
  • 190
    • 73849149415 scopus 로고    scopus 로고
    • Hydrolysis and inhibition profiles of β-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem
    • Queenan, A. M., W. Shang, R. Flamm, and K. Bush. 2010. Hydrolysis and inhibition profiles of β-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem. Antimicrob. Agents Chemother. 54:565-569.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 565-569
    • Queenan, A.M.1    Shang, W.2    Flamm, R.3    Bush, K.4
  • 191
    • 0025891515 scopus 로고
    • Imipenem- and meropenem-resistant mutants of Enterobacter cloacae and Proteus rettgeri lack porins
    • Raimondi, A., A. Traverso, and H. Nikaido. 1991. Imipenem- and meropenem-resistant mutants of Enterobacter cloacae and Proteus rettgeri lack porins. Antimicrob. Agents Chemother. 35:1174-1180.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1174-1180
    • Raimondi, A.1    Traverso, A.2    Nikaido, H.3
  • 193
    • 79960943589 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa carbapenem resistance mechanisms in Spain: Impact on the activity of imipenem, meropenem and doripenem
    • 8 June doi:10.1093/jac/dkr232
    • Riera, E., et al. 8 June 2011. Pseudomonas aeruginosa carbapenem resistance mechanisms in Spain: impact on the activity of imipenem, meropenem and doripenem. J. Antimicrob. Chemother. doi:10.1093/jac/dkr232.
    • (2011) J. Antimicrob. Chemother.
    • Riera, E.1
  • 195
    • 0343091451 scopus 로고    scopus 로고
    • Imipenem, doxycycline and amikacin in monotherapy and in combination in Acinetobacter baumannii experimental pneumonia
    • Rodriguez-Hernandez, M. J., et al. 2000. Imipenem, doxycycline and amikacin in monotherapy and in combination in Acinetobacter baumannii experimental pneumonia. J. Antimicrob. Chemother. 45:493-501.
    • (2000) J. Antimicrob. Chemother. , vol.45 , pp. 493-501
    • Rodriguez-Hernandez, M.J.1
  • 197
    • 70350313477 scopus 로고    scopus 로고
    • Molecular epidemiology and mechanisms of carbapenem resistance in Pseudomonas aeruginosa
    • Rodriguez-Martinez, J. M., L. Poirel, and P. Nordmann. 2009. Molecular epidemiology and mechanisms of carbapenem resistance in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 53:4783-4788.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 4783-4788
    • Rodriguez-Martinez, J.M.1    Poirel, L.2    Nordmann, P.3
  • 198
    • 77951175059 scopus 로고    scopus 로고
    • In vitro antimicrobials activity against endemic Acinetobacter baumannii multiresistant clones
    • Rodriguez, C. H., et al. 2010. In vitro antimicrobials activity against endemic Acinetobacter baumannii multiresistant clones. J. Infect. Dev. Ctries. 4:164-167.
    • (2010) J. Infect. Dev. Ctries. , vol.4 , pp. 164-167
    • Rodriguez, C.H.1
  • 199
    • 0025761016 scopus 로고
    • Evolution of β-lactamase inhibitors
    • Rolinson, G. N. 1991. Evolution of β-lactamase inhibitors. Rev. Infect. Dis. 13(Suppl. 9):S727-S732.
    • (1991) Rev. Infect. Dis. , vol.13 , Issue.SUPPL. 9
    • Rolinson, G.N.1
  • 200
    • 79953875949 scopus 로고    scopus 로고
    • The challenges of antimicrobial resistance in Brazil
    • Rossi, F. 2011. The challenges of antimicrobial resistance in Brazil. Clin. Infect. Dis. 52:1138-1143.
    • (2011) Clin. Infect. Dis. , vol.52 , pp. 1138-1143
    • Rossi, F.1
  • 202
    • 67651177534 scopus 로고    scopus 로고
    • A sensitive coupled HPLC/electrospray mass spectrometry assay for SPM-1 metallo-β-lactamase inhibitors
    • Sanchez, P. A., J. H. Toney, J. D. Thomas, and J. M. Berger. 2009. A sensitive coupled HPLC/electrospray mass spectrometry assay for SPM-1 metallo-β-lactamase inhibitors. Assay Drug Dev. Technol. 7:170-179.
    • (2009) Assay Drug Dev. Technol. , vol.7 , pp. 170-179
    • Sanchez, P.A.1    Toney, J.H.2    Thomas, J.D.3    Berger, J.M.4
  • 204
    • 72449185587 scopus 로고    scopus 로고
    • The 1.4 A crystal structure of the class D β-lactamase OXA-1 complexed with doripenem
    • Schneider, K. D., M. E. Karpen, R. A. Bonomo, D. A. Leonard, and R. A. Powers. 2009. The 1.4 A crystal structure of the class D β-lactamase OXA-1 complexed with doripenem. Biochemistry 48:11840-11847.
    • (2009) Biochemistry , vol.48 , pp. 11840-11847
    • Schneider, K.D.1    Karpen, M.E.2    Bonomo, R.A.3    Leonard, D.A.4    Powers, R.A.5
  • 205
    • 79951679429 scopus 로고    scopus 로고
    • Structures of the class D carbapenemase OXA-24 from Acinetobacter baumannii in complex with doripenem
    • Schneider, K. D., et al. 2011. Structures of the class D carbapenemase OXA-24 from Acinetobacter baumannii in complex with doripenem. J. Mol. Biol. 406:583-594.
    • (2011) J. Mol. Biol. , vol.406 , pp. 583-594
    • Schneider, K.D.1
  • 206
    • 67651180741 scopus 로고    scopus 로고
    • β-lactams and β-lactamase-inhibitors in current- or potential-clinical practice: A comprehensive update
    • Shahid, M., et al. 2009. β-lactams and β-lactamase-inhibitors in current- or potential-clinical practice: a comprehensive update. Crit. Rev. Microbiol. 35:81-108.
    • (2009) Crit. Rev. Microbiol. , vol.35 , pp. 81-108
    • Shahid, M.1
  • 208
    • 70350500104 scopus 로고    scopus 로고
    • Common mechanistic features among metallo-β-lactamases: A computational study of Aeromonas hydrophila CphA enzyme
    • Simona, F., et al. 2009. Common mechanistic features among metallo-β-lactamases: a computational study of Aeromonas hydrophila CphA enzyme. J. Biol. Chem. 284:28164-28171.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28164-28171
    • Simona, F.1
  • 211
    • 34548336958 scopus 로고    scopus 로고
    • Structure of GES-1 at atomic resolution: Insights into the evolution of carbapenamase activity in the class A extended-spectrum β-lactamases
    • DOI 10.1107/S0907444907036955, PII S0907444907036955
    • Smith, C. A., M. Caccamo, K. A. Kantardjieff, and S. Vakulenko. 2007. Structure of GES-1 at atomic resolution: insights into the evolution of carbapenamase activity in the class A extended-spectrum β-lactamases. Acta Crystallogr. D Biol. Crystallogr. 63:982-992. (Pubitemid 47346824)
    • (2007) Acta Crystallographica Section D: Biological Crystallography , vol.63 , Issue.9 , pp. 982-992
    • Smith, C.A.1    Caccamo, M.2    Kantardjieff, K.A.3    Vakulenko, S.4
  • 212
    • 12344287043 scopus 로고    scopus 로고
    • Is it safe to use carbapenems in patients with a history of allergy to penicillin?
    • DOI 10.1093/jac/dkh454
    • Sodhi, M., S. S. Axtell, J. Callahan, and R. Shekar. 2004. Is it safe to use carbapenems in patients with a history of allergy to penicillin? J. Antimicrob. Chemother. 54:1155-1157. (Pubitemid 40136760)
    • (2004) Journal of Antimicrobial Chemotherapy , vol.54 , Issue.6 , pp. 1155-1157
    • Sodhi, M.1    Axtell, S.S.2    Callahan, J.3    Shekar, R.4
  • 213
    • 59349103552 scopus 로고    scopus 로고
    • Efficacy of monotherapy and combined antibiotic therapy for carbapenem-resistant Acinetobacter baumannii pneumonia in an immunosuppressed mouse model
    • Song, J. Y., H. J. Cheong, J. Lee, A. K. Sung, and W. J. Kim. 2009. Efficacy of monotherapy and combined antibiotic therapy for carbapenem-resistant Acinetobacter baumannii pneumonia in an immunosuppressed mouse model. Int. J. Antimicrob. Agents 33:33-39.
    • (2009) Int. J. Antimicrob. Agents , vol.33 , pp. 33-39
    • Song, J.Y.1    Cheong, H.J.2    Lee, J.3    Sung, A.K.4    Kim, W.J.5
  • 215
    • 66149109159 scopus 로고    scopus 로고
    • Does the activity of the combination of imipenem and colistin in vitro exceed the problem of resistance in metallo-β-lactamase-producing Klebsiella pneumoniae isolates?
    • Souli, M., et al. 2009. Does the activity of the combination of imipenem and colistin in vitro exceed the problem of resistance in metallo-β- lactamase-producing Klebsiella pneumoniae isolates? Antimicrob. Agents Chemother. 53:2133-2135.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2133-2135
    • Souli, M.1
  • 216
    • 0017396035 scopus 로고
    • Binding of thienamycin and clavulanic acid to the penicillin binding proteins of Escherichia coli K 12
    • Spratt, B. G., V. Jobanputra, and W. Zimmermann. 1977. Binding of thienamycin and clavulanic acid to the penicillin-binding proteins of Escherichia coli K-12. Antimicrob. Agents Chemother. 12:406-409. (Pubitemid 8170520)
    • (1977) Antimicrobial Agents and Chemotherapy , vol.12 , Issue.3 , pp. 406-409
    • Spratt, B.G.1    Jobanputra, V.2    Zimmermann, W.3
  • 217
    • 0032926983 scopus 로고    scopus 로고
    • Carbapenem resistance in Escherichia coli associated with plasmid- determined CMY-4 β-lactamase production and loss of an outer membrane protein
    • Stapleton, P. D., K. P. Shannon, and G. L. French. 1999. Carbapenem resistance in Escherichia coli associated with plasmid-determined CMY-4 β-lactamase production and loss of an outer membrane protein. Antimicrob. Agents Chemother. 43:1206-1210. (Pubitemid 29214748)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.5 , pp. 1206-1210
    • Stapleton, P.D.1    Shannon, K.P.2    French, G.L.3
  • 218
    • 0029165050 scopus 로고
    • Potent activity of meropenem against Escherichia coli arising from its simultaneous binding to penicillin-binding proteins 2 and 3
    • Sumita, Y., and M. Fukasawa. 1995. Potent activity of meropenem against Escherichia coli arising from its simultaneous binding to penicillin-binding proteins 2 and 3. J. Antimicrob. Chemother. 36:53-64.
    • (1995) J. Antimicrob. Chemother. , vol.36 , pp. 53-64
    • Sumita, Y.1    Fukasawa, M.2
  • 219
    • 0025279314 scopus 로고
    • A novel carbapenem antibiotic, SM-7338 structure-activity relationships
    • Sunagawa, M., H. Matsumura, T. Inoue, M. Fukasawa, and M. Kato. 1990. A novel carbapenem antibiotic, SM-7338 structure-activity relationships. J. Antibiot. (Tokyo) 43:519-532. (Pubitemid 20165229)
    • (1990) Journal of Antibiotics , vol.43 , Issue.5 , pp. 519-532
    • Sunagawa, M.1    Matsumura, H.2    Inoue, T.3    Fukasawa, M.4    Kato, M.5
  • 220
    • 0029046103 scopus 로고
    • Structural features resulting in convulsive activity of carbapenem compounds: Effect of C-2 side chain
    • Tokyo
    • Sunagawa, M., H. Matsumura, Y. Sumita, and H. Nouda. 1995. Structural features resulting in convulsive activity of carbapenem compounds: effect of C-2 side chain. J. Antibiot. (Tokyo) 48:408-416.
    • (1995) J. Antibiot. , vol.48 , pp. 408-416
    • Sunagawa, M.1    Matsumura, H.2    Sumita, Y.3    Nouda, H.4
  • 221
  • 224
    • 0029116982 scopus 로고
    • Mechanism of turnover of imipenem by the TEM β-lactamase revisited
    • Taibi, P., and S. Mobashery. 1995. Mechanism of turnover of imipenem by the TEM β-lactamase revisited. J. Am. Chem. Soc. 117:7600-7605.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7600-7605
    • Taibi, P.1    Mobashery, S.2
  • 226
    • 7244251629 scopus 로고    scopus 로고
    • Novel approach to characterization of combined pharmacodynamic effects of antimicrobial agents
    • DOI 10.1128/AAC.48.11.4315-4321.2004
    • Tam, V. H., A. N. Schilling, R. E. Lewis, D. A. Melnick, and A. N. Boucher. 2004. Novel approach to characterization of combined pharmacodynamic effects of antimicrobial agents. Antimicrob. Agents Chemother. 48:4315-4321. (Pubitemid 39434892)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.11 , pp. 4315-4321
    • Tam, V.H.1    Schilling, A.N.2    Lewis, R.E.3    Melnick, D.A.4    Boucher, A.N.5
  • 227
    • 33745077917 scopus 로고    scopus 로고
    • Involvement of two related porins, OprD and OpdP, in the uptake of arginine by Pseudomonas aeruginosa
    • DOI 10.1111/j.1574-6968.2006.00293.x
    • Tamber, S., and R. E. Hancock. 2006. Involvement of two related porins, OprD and OpdP, in the uptake of arginine by Pseudomonas aeruginosa. FEMS Microbiol. Lett. 260:23-29. (Pubitemid 43879760)
    • (2006) FEMS Microbiology Letters , vol.260 , Issue.1 , pp. 23-29
    • Tamber, S.1    Hancock, R.E.W.2
  • 228
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper, D. J., and J. L. Strominger. 1965. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. U. S. A. 54:1133-1141.
    • (1965) Proc. Natl. Acad. Sci. U. S. A. , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 229
    • 35348982873 scopus 로고    scopus 로고
    • Current concepts in antibiotic-resistant Gram-negative bacteria
    • DOI 10.1586/14787210.5.5.833
    • Torres, J. A., M. V. Villegas, and J. P. Quinn. 2007. Current concepts in antibiotic-resistant gram-negative bacteria. Expert Rev. Anti Infect. Ther. 5:833-843. (Pubitemid 47610946)
    • (2007) Expert Review of Anti-Infective Therapy , vol.5 , Issue.5 , pp. 833-843
    • Torres, J.A.1    Villegas, M.V.2    Quinn, J.P.3
  • 230
    • 77951676093 scopus 로고    scopus 로고
    • Biochemical and structural characterization of Mycobacterium tuberculosis β-lactamase with the carbapenems ertapenem and doripenem
    • Tremblay, L. W., F. Fan, and J. S. Blanchard. 2010. Biochemical and structural characterization of Mycobacterium tuberculosis β-lactamase with the carbapenems ertapenem and doripenem. Biochemistry 49:3766-3773.
    • (2010) Biochemistry , vol.49 , pp. 3766-3773
    • Tremblay, L.W.1    Fan, F.2    Blanchard, J.S.3
  • 231
    • 0025186624 scopus 로고
    • Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa
    • Trias, J., and H. Nikaido. 1990. Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 34:52-57. (Pubitemid 20019963)
    • (1990) Antimicrobial Agents and Chemotherapy , vol.34 , Issue.1 , pp. 52-57
    • Trias, J.1    Nikaido, H.2
  • 232
    • 53949085115 scopus 로고    scopus 로고
    • Association between antibiotic usage and subsequent colonization or infection of extensive drug-resistant Acinetobacter baumannii: A matched case-control study in intensive care units
    • Tsai, H. T., J. T. Wang, C. J. Chen, and S. C. Chang. 2008. Association between antibiotic usage and subsequent colonization or infection of extensive drug-resistant Acinetobacter baumannii: a matched case-control study in intensive care units. Diagn. Microbiol. Infect. Dis. 62:298-305.
    • (2008) Diagn. Microbiol. Infect. Dis. , vol.62 , pp. 298-305
    • Tsai, H.T.1    Wang, J.T.2    Chen, C.J.3    Chang, S.C.4
  • 233
    • 0019957934 scopus 로고
    • The structures of pluracidomycins, new carbapenem antibiotics
    • Tsuji, N., et al. 1982. The structures of pluracidomycins, new carbapenem antibiotics. J. Antibiot. (Tokyo) 35:536-540. (Pubitemid 12046414)
    • (1982) Journal of Antibiotics , vol.35 , Issue.4 , pp. 536-540
    • Tsuji, N.1    Nagashima, K.2    Kobayashi, M.3
  • 234
    • 0028173264 scopus 로고
    • Renal tabular transport and nephrotoxicity of beta lactam antibiotics: Structure-activity relationships
    • Tune, B. M. 1994. Renal tubular transport and nephrotoxicity of beta lactam antibiotics: structure-activity relationships. Miner Electrolyte Metab. 20:221-231. (Pubitemid 24320006)
    • (1994) Mineral and Electrolyte Metabolism , vol.20 , Issue.4 , pp. 221-231
    • Tune, B.M.1
  • 235
    • 0024440759 scopus 로고
    • Thienamycin nephrotoxicity. Mitochondrial injury and oxidative effects of imipenem in the rabbit kidney
    • DOI 10.1016/0006-2952(89)90585-6
    • Tune, B. M., D. Fravert, and C. Y. Hsu. 1989. Thienamycin nephrotoxicity. Mitochondrial injury and oxidative effects of imipenem in the rabbit kidney. Biochem. Pharmacol. 38:3779-3783. (Pubitemid 19284027)
    • (1989) Biochemical Pharmacology , vol.38 , Issue.21 , pp. 3779-3783
    • Tune, B.M.1    Fravert, D.2    Hsu, C.-Y.3
  • 236
    • 0026742216 scopus 로고
    • Synthesis and in vitro activity of novel quaternary ammonium carbapenems: 2-pyridiniopropyl and 1-pyridinioethyl carbapenems
    • Tokyo
    • Ueda, Y., and V. Vinet. 1992. Synthesis and in vitro activity of novel quaternary ammonium carbapenems: 2-pyridiniopropyl and 1-pyridinioethyl carbapenems. J. Antibiot. (Tokyo) 45:940-953.
    • (1992) J. Antibiot. , vol.45 , pp. 940-953
    • Ueda, Y.1    Vinet, V.2
  • 237
    • 65549153535 scopus 로고    scopus 로고
    • Specific labeling of peptidoglycan precursors as a tool for bacterial cell wall studies
    • van Dam, V., N. Olrichs, and E. Breukink. 2009. Specific labeling of peptidoglycan precursors as a tool for bacterial cell wall studies. Chembiochem 10:617-624.
    • (2009) Chembiochem , vol.10 , pp. 617-624
    • Van Dam, V.1    Olrichs, N.2    Breukink, E.3
  • 238
    • 77951215313 scopus 로고    scopus 로고
    • In vitro activity of ACH-702, a new isothiazoloquinolone, against Nocardia brasiliensis compared with econazole and the carbapenems imipenem and meropenem alone or in combination with clavulanic acid
    • Vera-Cabrera, L., et al. 2010. In vitro activity of ACH-702, a new isothiazoloquinolone, against Nocardia brasiliensis compared with econazole and the carbapenems imipenem and meropenem alone or in combination with clavulanic acid. Antimicrob. Agents Chemother. 54:2191-2193.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2191-2193
    • Vera-Cabrera, L.1
  • 239
    • 0034913329 scopus 로고    scopus 로고
    • Kinetic study of two novel enantiomeric tricyclic β-lactams which efficiently inactivate class C β-lactamases
    • DOI 10.1128/AAC.45.8.2215-2223.2001
    • Vilar, M., et al. 2001. Kinetic study of two novel enantiomeric tricyclic β-lactams which efficiently inactivate class C β-lactamases. Antimicrob. Agents Chemother. 45:2215-2223. (Pubitemid 32664459)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.8 , pp. 2215-2223
    • Vilar, M.1    Galleni, M.2    Solmajer, T.3    Turk, B.4    Frere, J.-M.5    Matagne, A.6
  • 240
    • 0030759065 scopus 로고    scopus 로고
    • Permeability to carbapenems of Proteus mirabilis mutants selected for resistance to imipenem or other β-lactams
    • DOI 10.1093/jac/40.3.365
    • Villar, H. E., F. Danel, and D. M. Livermore. 1997. Permeability to carbapenems of Proteus mirabilis mutants selected for resistance to imipenem or other β-lactams. J. Antimicrob. Chemother. 40:365-370. (Pubitemid 27437955)
    • (1997) Journal of Antimicrobial Chemotherapy , vol.40 , Issue.3 , pp. 365-370
    • Villar, H.E.1    Danel, F.2    Livermore, D.M.3
  • 241
    • 0031967431 scopus 로고    scopus 로고
    • Determination of activities of levofloxacin, alone and combined with gentamicin, ceftazidime, cefpirome, and meropenem, against 124 strains of Pseudomonas aeruginosa by checkerboard and time-kill methodology
    • Visalli, M. A., M. R. Jacobs, and P. C. Appelbaum. 1998. Determination of activities of levofloxacin, alone and combined with gentamicin, ceftazidime, cefpirome, and meropenem, against 124 strains of Pseudomonas aeruginosa by checkerboard and time-kill methodology. Antimicrob. Agents Chemother. 42:953-955. (Pubitemid 28216390)
    • (1998) Antimicrobial Agents and Chemotherapy , vol.42 , Issue.4 , pp. 953-955
    • Visalli, M.A.1    Jacobs, M.R.2    Appelbaum, P.C.3
  • 242
    • 49049090630 scopus 로고    scopus 로고
    • Clinically significant carbapenemases: An update
    • Walsh, T. R. 2008. Clinically significant carbapenemases: an update. Curr. Opin. Infect. Dis. 21:367-371.
    • (2008) Curr. Opin. Infect. Dis. , vol.21 , pp. 367-371
    • Walsh, T.R.1
  • 243
    • 78649697323 scopus 로고    scopus 로고
    • Emerging carbapenemases: A global perspective
    • Walsh, T. R. 2010. Emerging carbapenemases: a global perspective. Int. J. Antimicrob. Agents 36(Suppl. 3):S8-S14.
    • (2010) Int. J. Antimicrob. Agents , vol.36 , Issue.SUPPL. 3
    • Walsh, T.R.1
  • 244
    • 0036533471 scopus 로고    scopus 로고
    • Noncovalent interaction energies in covalent complexes: Tem-1 β-lactamase and β-lactams
    • DOI 10.1002/prot.10058
    • Wang, X., G. Minasov, and B. K. Shoichet. 2002. Noncovalent interaction energies in covalent complexes: TEM-1 β-lactamase and β-lactams. Proteins 47:86-96. (Pubitemid 34195257)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.1 , pp. 86-96
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 245
    • 33745610747 scopus 로고    scopus 로고
    • In-vitro activity of polymyxin B in combination with imipenem, rifampicin and azithromycin versus multidrug resistant strains of Acinetobacter baumannii producing OXA-23 carbapenemases
    • Wareham, D. W., and D. C. Bean. 2006. In-vitro activity of polymyxin B in combination with imipenem, rifampicin and azithromycin versus multidrug resistant strains of Acinetobacter baumannii producing OXA-23 carbapenemases. Ann. Clin. Microbiol. Antimicrob. 5:10.
    • (2006) Ann. Clin. Microbiol. Antimicrob. , vol.5 , pp. 10
    • Wareham, D.W.1    Bean, D.C.2
  • 246
    • 0018378327 scopus 로고
    • Thienamycin: New beta-lactam antibiotic with potent broad-spectrum activity
    • Weaver, S. S., G. P. Bodey, and B. M. LeBlanc. 1979. Thienamycin: new β-lactam antibiotic with potent broad-spectrum activity. Antimicrob. Agents Chemother. 15:518-521. (Pubitemid 9152428)
    • (1979) Antimicrobial Agents and Chemotherapy , vol.15 , Issue.4 , pp. 518-521
    • Weaver, S.S.1    Bodey, G.P.2    LeBlanc, B.M.3
  • 247
    • 78249260635 scopus 로고    scopus 로고
    • Emergence of carbapenem resistance due to porin loss in an extended-spectrum β-lactamase (ESBL)-producing Klebsiella pneumoniae strain during meropenem therapy
    • Webster, D. P., et al. 2010. Emergence of carbapenem resistance due to porin loss in an extended-spectrum β-lactamase (ESBL)-producing Klebsiella pneumoniae strain during meropenem therapy. Int. J. Antimicrob. Agents 36:575-576.
    • (2010) Int. J. Antimicrob. Agents , vol.36 , pp. 575-576
    • Webster, D.P.1
  • 248
    • 77955915532 scopus 로고    scopus 로고
    • NH-1,2,3-triazole-based inhibitors of the VIM-2 metallo-β-lactamase: Synthesis and structure-activity studies
    • Weide, T., et al. 2010. NH-1,2,3-triazole-based inhibitors of the VIM-2 metallo-β-lactamase: synthesis and structure-activity studies. ACS Med. Chem. Lett. 1:150-154.
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 150-154
    • Weide, T.1
  • 250
    • 78650620354 scopus 로고    scopus 로고
    • QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway
    • Wu, S., D. Xu, and H. Guo. 2010. QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway. J. Am. Chem. Soc. 132:17986-17988.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 17986-17988
    • Wu, S.1    Xu, D.2    Guo, H.3
  • 251
    • 33646855255 scopus 로고    scopus 로고
    • Catalytic mechanism of class B2 metallo-β-lactamase
    • Xu, D., D. Xie, and H. Guo. 2006. Catalytic mechanism of class B2 metallo-β-lactamase. J. Biol. Chem. 281:8740-8747.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8740-8747
    • Xu, D.1    Xie, D.2    Guo, H.3
  • 252
    • 27144445025 scopus 로고    scopus 로고
    • Antibiotic binding to monozinc CphA β-lactamase from Aeromonas hydropila: Quantum mechanical/molecular mechanical and density functional theory studies
    • DOI 10.1021/jm0505112
    • Xu, D., Y. Zhou, D. Xie, and H. Guo. 2005. Antibiotic binding to monozinc CphA β-lactamase from Aeromonas hydropila: quantum mechanical/molecular mechanical and density functional theory studies. J. Med. Chem. 48:6679-6689. (Pubitemid 41504724)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.21 , pp. 6679-6689
    • Xu, D.1    Zhou, Y.2    Xie, D.3    Guo, H.4
  • 253
    • 71249134038 scopus 로고    scopus 로고
    • Characterization of a new metallo-β-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India
    • Yong, D., et al. 2009. Characterization of a new metallo-β-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India. Antimicrob. Agents Chemother. 53:5046-5054.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 5046-5054
    • Yong, D.1
  • 254
    • 0026525195 scopus 로고
    • Facilitation of the delta2 to delta1 pyrroline tautomerization of carbapenem antibiotics by the highly conserved arginine-244 of class A beta-lactamases during the course of turnover
    • Zafaralla, G., and S. Mobashery. 1992. Facilitation of the delta2 to delta1 pyrroline tautomerization of carbapenem antibiotics by the highly conserved arginine-244 of class A beta-lactamases during the course of turnover. J. Am. Chem. Soc. 114:1506-1507.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 1506-1507
    • Zafaralla, G.1    Mobashery, S.2
  • 256
    • 77953100456 scopus 로고    scopus 로고
    • Efflux pump inhibitors: A strategy to combat P-glycoprotein and the NorA multidrug resistance pump
    • Zhang, L., and S. Ma. 2010. Efflux pump inhibitors: a strategy to combat P-glycoprotein and the NorA multidrug resistance pump. ChemMedChem 5:811-822.
    • (2010) ChemMedChem , vol.5 , pp. 811-822
    • Zhang, L.1    Ma, S.2
  • 257
    • 0033039934 scopus 로고    scopus 로고
    • In vivo emergence of multidrug-resistant mutants of Pseudomonas aeruginosa overexpressing the active efflux system mexA-mexB-OprM
    • Ziha-Zarifi, I., C. Llanes, T. Kohler, J. C. Pechere, and P. Plesiat. 1999. In vivo emergence of multidrug-resistant mutants of Pseudomonas aeruginosa overexpressing the active efflux system MexA-MexB-OprM. Antimicrob. Agents Chemother. 43:287-291. (Pubitemid 29079160)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.2 , pp. 287-291
    • Ziha-Zarifi, I.1    Llanes, C.2    Kohler, T.3    Pechere, J.-C.4    Plesiat, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.