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Volumn 13, Issue 10, 2004, Pages 1307-1318

β-Lactamase inhibitors: Evolving compounds for evolving resistance targets

Author keywords

lactamase inhibitors; lactamases; Carbapenemases; Cephem sulfones; Clavulanic acid; ESBLs; IMP 1 metallo lactamase; L1 metallo lactamase; OXA lactamase; Oxapenams; Oxapenems; PC1 lactamase; Penam sulfones; SHV lactamse; Sulbactam; Tazobactam; TEM lactamase

Indexed keywords

3 (4 AMINO 1,1 DIMETHYLBUTYL) 6 (1 HYDROXYETHYL)OXAPENEM 3 CARBOXYLIC ACID; 6 (1 METHYL 1,2,3 TRIAZOL 4 YLMETHYLENE)PENEM 3 CARBOXYLIC ACID; AMOXICILLIN; AMOXICILLIN PLUS CLAVULANIC ACID; AMPICILLIN; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; BORONIC ACID DERIVATIVE; CEFEPIME; CEFOPERAZONE; CEFTAZIDIME; CEFTRIAXONE; CEPHEM DERIVATIVE; CLAVULANIC ACID; MONOBACTAM; PENAM DERIVATIVE; PENEM DERIVATIVE; PHOSPHONIC ACID DERIVATIVE; PIPERACILLIN; PIPERACILLIN PLUS TAZOBACTAM; RO 151903; SERINE DERIVATIVE; SULBACTAM; SULPERAZONE; SULTAMICILLIN; TAZOBACTAM; TICARCILLIN; TIMENTIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 5444244484     PISSN: 13543784     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543784.13.10.1307     Document Type: Review
Times cited : (38)

References (128)
  • 2
    • 0022745699 scopus 로고
    • β-Lactam antibiotics: Structural relationships affecting in vitro activity and pharmacologic properties
    • NEU HC: β-Lactam antibiotics: structural relationships affecting in vitro activity and pharmacologic properties. Rev. Infect. Dis. (1986) 8 (Suppl. 3):S237-S259.
    • (1986) Rev. Infect. Dis. , vol.8 , Issue.SUPPL. 3
    • Neu, H.C.1
  • 3
    • 0027381457 scopus 로고
    • Penicillin-binding proteins and bacterial resistance to β-lactams
    • GEORGOPAPADAKOU NH: Penicillin-binding proteins and bacterial resistance to β-lactams. Antimicrob. Agents Chemother. (1993) 37: 2045-2053.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2045-2053
    • Georgopapadakou, N.H.1
  • 4
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs
    • GOFFIN C, GHUYSEN JM: Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. (1998) 62: 1079-1093.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1079-1093
    • Goffin, C.1    Ghuysen, J.M.2
  • 5
    • 0033830225 scopus 로고    scopus 로고
    • The cost of antibiotic resistance from a bacterial perspective
    • BJORKMAN J, ANDERSSON DI: The cost of antibiotic resistance from a bacterial perspective. Drug Resist. Updat. (2000) 3: 237-245.
    • (2000) Drug Resist. Updat. , vol.3 , pp. 237-245
    • Bjorkman, J.1    Andersson, D.I.2
  • 6
    • 0033402097 scopus 로고    scopus 로고
    • Penicillin-binding protein-mediated resistance in pneumococci and staphylococci
    • CHAMBERS HF: Penicillin-binding protein-mediated resistance in pneumococci and staphylococci. J. Infect. Dis. (1999)179 (Suppl. 2):S353-S359.
    • (1999) J. Infect. Dis. , vol.179 , Issue.SUPPL. 2
    • Chambers, H.F.1
  • 7
    • 0035091085 scopus 로고    scopus 로고
    • Recruitment of the mecA gene homologue of Staphylococcus sciuri into a resistance determinant and expression of the resistant phenotype in Staphylococcus aureus
    • WU SW, DE LENCASTRE H, TOMASZ A: Recruitment of the mecA gene homologue of Staphylococcus sciuri into a resistance determinant and expression of the resistant phenotype in Staphylococcus aureus. J. Bacteriol. (2001) 183: 2417-2424.
    • (2001) J. Bacteriol. , vol.183 , pp. 2417-2424
    • Wu, S.W.1    De Lencastre, H.2    Tomasz, A.3
  • 8
    • 0030292866 scopus 로고    scopus 로고
    • Molecular evolution of bacterial β-lactam resistance
    • KNOX JR, MOEWS PC, FRERE JM: Molecular evolution of bacterial β-lactam resistance. Chem. Biol. (1996) 3: 937-947.
    • (1996) Chem. Biol. , vol.3 , pp. 937-947
    • Knox, J.R.1    Moews, P.C.2    Frere, J.M.3
  • 10
    • 0026049801 scopus 로고
    • Serine β-lactamases and penicillin-binding proteins
    • GHUYSEN JM: Serine β-lactamases and penicillin-binding proteins. Ann. Rev. Microbiol. (1991) 45: 37-67.
    • (1991) Ann. Rev. Microbiol. , vol.45 , pp. 37-67
    • Ghuysen, J.M.1
  • 11
    • 0033862706 scopus 로고    scopus 로고
    • β-Lactamases: Which ones are clinically important?
    • RICE LB, BONOMO RA: β-Lactamases: which ones are clinically important? Drug Resist. Updat. (2000) 3: 178-189.
    • (2000) Drug Resist. Updat. , vol.3 , pp. 178-189
    • Rice, L.B.1    Bonomo, R.A.2
  • 12
    • 0033830002 scopus 로고    scopus 로고
    • Version 2000: The new β-lactamases of Gram-negative bacteria at the dawn of the new millennium
    • THOMSON KS, SMITH MOLAND E: Version 2000: the new β-lactamases of Gram-negative bacteria at the dawn of the new millennium. Microbes Infect. (2000) 2: 1225-1235.
    • (2000) Microbes. Infect. , vol.2 , pp. 1225-1235
    • Thomson, K.S.1    Smith Moland, E.2
  • 13
    • 0036771257 scopus 로고    scopus 로고
    • The impact of β-lactamases on the development of novel antimicrobial agents
    • BUSH K: The impact of β-lactamases on the development of novel antimicrobial agents. Curr. Opin. Investig. Drugs (2002) 3 1284-1290.
    • (2002) Curr. Opin. Investig. Drugs , vol.3 , pp. 1284-1290
    • Bush, K.1
  • 17
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • BUSH K, JACOBY GA, MEDEIROS AA: A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. (1995) 39: 1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 18
    • 0023277283 scopus 로고
    • An explicit model for bacterial resistance: Application to β-lactam antibiotics
    • WALEY SG: An explicit model for bacterial resistance: application to β-lactam antibiotics. Microbiol. Sci. (1987) 4 143-146.
    • (1987) Microbiol. Sci. , vol.4 , pp. 143-146
    • Waley, S.G.1
  • 19
    • 0023375673 scopus 로고
    • Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamases: A quantitative predictive treatment
    • NIKAIDO H, NORMARK S. Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamases: a quantitative predictive treatment. Mol. Microbiol. (1987) 1: 29-36.
    • (1987) Mol. Microbiol. , vol.1 , pp. 29-36
    • Nikaido, H.1    Normark, S.2
  • 20
    • 0030045364 scopus 로고    scopus 로고
    • In vivo selection of porin-deficient mutants of Klebsiella pneumoniae with increased resistance to cefoxitin and expanded-spectrum cephalosporins
    • MARTINEZ-MARTINEZ L, HERNANDEZ-ALLES S, ALBERTI S, JACOBY GA: In vivo selection of porin-deficient mutants of Klebsiella pneumoniae with increased resistance to cefoxitin and expanded-spectrum cephalosporins. Antimicrob. Agents Chemother. (1996) 40: 342-348.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 342-348
    • Martinez-Martinez, L.1    Hernandez-Alles, S.2    Alberti, S.3    Jacoby, G.A.4
  • 21
    • 0031952858 scopus 로고    scopus 로고
    • β-Lactamase inhibitors are substrates for the multidrug efflux pumps of Pseudomonas aeruginosa
    • LI XZ, ZHANG L, SRIKUMAR R, POOLE K: β-Lactamase inhibitors are substrates for the multidrug efflux pumps of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (1998) 42: 399-403.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 399-403
    • Li, X.Z.1    Zhang, L.2    Srikumar, R.3    Poole, K.4
  • 22
    • 0032807154 scopus 로고    scopus 로고
    • Penetration of β-lactamase inhibitors into the periplasm of Gram-negative bacteria
    • FARMER TH, DEGNAN BA, PAYNE DJ: Penetration of β-lactamase inhibitors into the periplasm of Gram-negative bacteria. FEMS Microbiol. Lett. (1999) 176: 11-15.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 11-15
    • Farmer, T.H.1    Degnan, B.A.2    Payne, D.J.3
  • 23
    • 0034763241 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases in the 21st century-characterization, epidemiology, and detection of this important resistance threat
    • BRADFORD PA: Extended-spectrum β-lactamases in the 21st century-characterization, epidemiology, and detection of this important resistance threat. Clin. Microbiol. Rev. (2001) 14: 933-951.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 933-951
    • Bradford, P.A.1
  • 24
    • 0036894253 scopus 로고    scopus 로고
    • Chromosome-encoded Ambler class A β-lactamase of Kluyvera georgiana, a probable progenitor of a subgroup of CTX-M extended-spectrum β-lactamases
    • POIREL L, KAMPFER P, NORDMANN P. Chromosome-encoded Ambler class A β-lactamase of Kluyvera georgiana, a probable progenitor of a subgroup of CTX-M extended-spectrum β-lactamases. Antimicrob. Agents Chemother. (2002) 46: 4038-4040.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 4038-4040
    • Poirel, L.1    Kampfer, P.2    Nordmann, P.3
  • 25
    • 1542286960 scopus 로고    scopus 로고
    • Endemic carbapenem-resistant Pseudomonas aeruginosa with acquired metallo-β-lactamase determinants in European hospital
    • LAGATOLLA C, TONIN EA, MONTI-BRAGADIN C et al.: Endemic carbapenem-resistant Pseudomonas aeruginosa with acquired metallo-β-lactamase determinants in European hospital. Emerg. Infect. Dis. (2004) 10: 535-538.
    • (2004) Emerg. Infect. Dis. , vol.10 , pp. 535-538
    • Lagatolla, C.1    Tonin, E.A.2    Monti-Bragadin, C.3
  • 26
    • 0942301301 scopus 로고    scopus 로고
    • Epidemiology of conjugative plasmid-mediated AmpC β-lactamases in the United States
    • ALVAREZ M, TRAN JH, CHOW N, JACOBY GA: Epidemiology of conjugative plasmid-mediated AmpC β-lactamases in the United States. Antimicrob. Agents Chemother. (2004) 48: 533-537.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 533-537
    • Alvarez, M.1    Tran, J.H.2    Chow, N.3    Jacoby, G.A.4
  • 27
    • 1842862848 scopus 로고    scopus 로고
    • Comparative activity of β-lactam agents (carbapenem excepted) against Pseudomonas aeruginosa strains with CARB or OXA β-lactamases
    • BERT F, BRANGER C, LAMBERT-ZECHOVSKY N: Comparative activity of β-lactam agents (carbapenem excepted) against Pseudomonas aeruginosa strains with CARB or OXA β-lactamases. Chemotherapy (2004) 50: 31-34.
    • (2004) Chemotherapy , vol.50 , pp. 31-34
    • Bert, F.1    Branger, C.2    Lambert-Zechovsky, N.3
  • 28
    • 0026016867 scopus 로고
    • Refined crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution
    • HERZBERG O: Refined crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.0 A resolution. J. Mol. Biol. (1991) 217: 701-719.
    • (1991) J. Mol. Biol. , vol.217 , pp. 701-719
    • Herzberg, O.1
  • 29
    • 0032502332 scopus 로고    scopus 로고
    • Role of the omega-loop in the activity, substrate specificity, and structure of class A β-lactamase
    • BANERJEE S, PIEPER U, KAPADIA G, PANNELL LK, HERZBERG O: Role of the omega-loop in the activity, substrate specificity, and structure of class A β-lactamase. Biochemistry (1998) 37: 3286-3296.
    • (1998) Biochemistry , vol.37 , pp. 3286-3296
    • Banerjee, S.1    Pieper, U.2    Kapadia, G.3    Pannell, L.K.4    Herzberg, O.5
  • 30
    • 0035957080 scopus 로고    scopus 로고
    • Structures of the acyl-enzyme complexes of the Staphylococcus aureus β-lactamase mutant Glu166Asp:Asn170Gln with benzylpenicillin and cephaloridine
    • CHEN CC, HERZBERG O: Structures of the acyl-enzyme complexes of the Staphylococcus aureus β-lactamase mutant Glu166Asp:Asn170Gln with benzylpenicillin and cephaloridine. Biochemistry (2001) 40: 2351-2358.
    • (2001) Biochemistry , vol.40 , pp. 2351-2358
    • Chen, C.C.1    Herzberg, O.2
  • 31
    • 0026801518 scopus 로고
    • Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution
    • STRYNADKA NC, ADACHI H, JENSEN SE et al.: Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution. Nature (1992) 359: 700-705.
    • (1992) Nature , vol.359 , pp. 700-705
    • Strynadka, N.C.1    Adachi, H.2    Jensen, S.E.3
  • 32
    • 0027275788 scopus 로고
    • Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution
    • JELSCH C, MOUREY L, MASSON JM, SAMAMA JP: Crystal structure of Escherichia coli TEM1 β-lactamase at 1.8 Å resolution. Proteins (1993) 16: 364-383.
    • (1993) Proteins , vol.16 , pp. 364-383
    • Jelsch, C.1    Mourey, L.2    Masson, J.M.3    Samama, J.P.4
  • 33
    • 0028821830 scopus 로고
    • Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: Mutations, specificity, and three-dimensional structure
    • KNOX JR. Extended-spectrum and inhibitor-resistant TEM-type β-lactamases: mutations, specificity, and three-dimensional structure. Antimicrob. Agents Chemother. (1995) 39: 2593-2601.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2593-2601
    • Knox, J.R.1
  • 35
    • 0037453313 scopus 로고    scopus 로고
    • Ultrahigh resolution structure of a class A β-lactamase: On the mechanism and specificity of the extended-spectrum SHV-2 enzyme
    • NUKAGA M, MAYAMA K, HUJER AM, BONOMO RA, KNOX JR: Ultrahigh resolution structure of a class A β-lactamase: on the mechanism and specificity of the extended-spectrum SHV-2 enzyme. J. Mol. Biol. (2003) 328: 289-301.
    • (2003) J. Mol. Biol. , vol.328 , pp. 289-301
    • Nukaga, M.1    Mayama, K.2    Hujer, A.M.3    Bonomo, R.A.4    Knox, J.R.5
  • 36
    • 0026447287 scopus 로고
    • Site-saturation mutagenesis and three-dimensional modeling of ROB-1 define a substrate binding role of Ser130 in class A β -lactamases
    • JUTEAU JM, BILLINGS E, KNOX JR, LEVESQUE RC: Site-saturation mutagenesis and three-dimensional modeling of ROB-1 define a substrate binding role of Ser130 in class A β-lactamases.Protein Eng. (1992) 5: 693-701.
    • (1992) Protein Eng. , vol.5 , pp. 693-701
    • Juteau, J.M.1    Billings, E.2    Knox, J.R.3    Levesque, R.C.4
  • 37
    • 0034623247 scopus 로고    scopus 로고
    • The high resolution crystal structure for class A β-lactamase PER-1 reveals the bases for its increase in breadth of activity
    • TRANIER S, BOUTHORS AT, MAVEYRAUD L, GUILLET V, SOUGAKOFF W, SAMAMA JP: The high resolution crystal structure for class A β -lactamase PER-1 reveals the bases for its increase in breadth of activity. J. Biol. Chem. (2000) 275: 28075-28082.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28075-28082
    • Tranier, S.1    Bouthors, A.T.2    Maveyraud, L.3    Guillet, V.4    Sougakoff, W.5    Samama, J.P.6
  • 38
    • 0036008512 scopus 로고    scopus 로고
    • Structure of the imipenem-hydrolyzing class A β-lactamase SME-1 from Serratia marcescens
    • SOUGAKOFF W, L'HERMITE G, PERNOT L et al.: Structure of the imipenem-hydrolyzing class A β-lactamase SME-1 from Serratia marcescens. Acta Crystallogr. D. Biol. Crystallogr. (2002) 58 (Pt 2): 267-274.
    • (2002) Acta Crystallogr. D. Biol. Crystallogr. , vol.58 , Issue.PART 2 , pp. 267-274
    • Sougakoff, W.1    L'Hermite, G.2    Pernot, L.3
  • 39
    • 15444338960 scopus 로고    scopus 로고
    • X-ray analysis of the NMC-A β-lactamase at 1.64-Å resolution, a class A carbapenemase with broad substrate specificity
    • SWAREN P, MAVEYRAUD L, RAQUET X et al.: X-ray analysis of the NMC-A β-lactamase at 1.64-Å resolution, a class A carbapenemase with broad substrate specificity. J. Biol. Chem. (1998) 273: 26714-26721.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26714-26721
    • Swaren, P.1    Maveyraud, L.2    Raquet, X.3
  • 40
    • 0033520397 scopus 로고    scopus 로고
    • Inhibition of the broad spectrum non-metallo-carbapenamase of class A (NMC-A) β-lactamase from Enterobacter cloacae by monocyclic β-lactams
    • MOUREY L, KOTRA LP, BELLETTINI J et al.: Inhibition of the broad spectrum non-metallo-carbapenamase of class A (NMC-A) β-lactamase from Enterobacter cloacae by monocyclic β -lactams. J. Biol. Chem. (1999) 274: 25260-25265.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25260-25265
    • Mourey, L.1    Kotra, L.P.2    Bellettini, J.3
  • 41
    • 0032542009 scopus 로고    scopus 로고
    • Three-dimensional structure of AmpC β-lactamase from Escherichia coli bound to a transition-state analogue: Possible implications for the oxyanion hypothesis and for inhibitor design
    • USHER KC, BLASZCZAK LC, WESTON GS, SHOICHET BK, REMINGTON SJ: Three-dimensional structure of AmpC β-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design. Biochemistry (1998) 37: 16082-16092.
    • (1998) Biochemistry , vol.37 , pp. 16082-16092
    • Usher, K.C.1    Blaszczak, L.C.2    Weston, G.S.3    Shoichet, B.K.4    Remington, S.J.5
  • 42
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • LOBKOVSKY E, MOEWS PC, LIU H, ZHAO H, FRERE JM, KNOX JR: Evolution of an enzyme activity: crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase.Proc. Natl. Acad. Sci. USA (1993) 90: 11257-11261.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1    Moews, P.C.2    Liu, H.3    Zhao, H.4    Frere, J.M.5    Knox, J.R.6
  • 43
    • 0037130228 scopus 로고    scopus 로고
    • Structure-based approach for binding-site identification on AmpC β-lactamase
    • POWERS RA, SHOICHET BK: Structure-based approach for binding-site identification on AmpC β-lactamase. J. Med. Chem. (2002) 45: 3222-3234.
    • (2002) J. Med. Chem. , vol.45 , pp. 3222-3234
    • Powers, R.A.1    Shoichet, B.K.2
  • 44
    • 0035919770 scopus 로고    scopus 로고
    • Crystal structures of the class D β-lactamase OXA-13 in the native form and in complex with meropenem
    • PERNOT L, FRENOIS F, RYBKINE T et al.: Crystal structures of the class D β-lactamase OXA-13 in the native form and in complex with meropenem. J. Mol. Biol. (2001) 310: 859-874.
    • (2001) J. Mol. Biol. , vol.310 , pp. 859-874
    • Pernot, L.1    Frenois, F.2    Rybkine, T.3
  • 46
    • 0034476988 scopus 로고    scopus 로고
    • Insights into class D β-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa
    • MAVEYRAUD L, GOLEMI D, KOTRA LP et al.: Insights into class D β-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa. Structure Fold Des. (2000) 8 1289-1298.
    • (2000) Structure Fold Des. , vol.8 , pp. 1289-1298
    • Maveyraud, L.1    Golemi, D.2    Kotra, L.P.3
  • 48
    • 0037216363 scopus 로고    scopus 로고
    • Comparison of β-lactamases of classes A and D: 1.5-Å crystallographic structure of the class D OXA-1 oxacillinase
    • SUN T, NUKAGA M, MAYAMA K, BRASWELL EH, KNOX JR: Comparison of β-lactamases of classes A and D: 1.5-Å crystallographic structure of the class D OXA-1 oxacillinase. Protein Sci. (2003) 12: 82-91.
    • (2003) Protein Sci. , vol.12 , pp. 82-91
    • Sun, T.1    Nukaga, M.2    Mayama, K.3    Braswell, E.H.4    Knox, J.R.5
  • 49
  • 50
    • 0035122917 scopus 로고    scopus 로고
    • Predicting the emergence of antibiotic resistance by directed evolution and structural analysis
    • ORENCIA MC, YOON JS, NESS JE, STEMMER WP, STEVENS RC: Predicting the emergence of antibiotic resistance by directed evolution and structural analysis. Nat. Struct. Biol. (2001) 8: 238-242.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 238-242
    • Orencia, M.C.1    Yoon, J.S.2    Ness, J.E.3    Stemmer, W.P.4    Stevens, R.C.5
  • 51
    • 2942562249 scopus 로고    scopus 로고
    • Evolution of the serine β-lactamases: Past, present and future
    • HALL BG, BARLOW M: Evolution of the serine β-lactamases: past, present and future. Drug Resist. Updat. (2004) 7: 111-123.
    • (2004) Drug Resist. Updat. , vol.7 , pp. 111-123
    • Hall, B.G.1    Barlow, M.2
  • 53
    • 0032553559 scopus 로고    scopus 로고
    • The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution
    • ULLAH JH, WALSH TR, TAYLOR IA et al.: The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution. J. Mol. Biol. (1998) 284: 125-136.
    • (1998) J. Mol. Biol. , vol.284 , pp. 125-136
    • Ullah, J.H.1    Walsh, T.R.2    Taylor, I.A.3
  • 54
    • 0037025381 scopus 로고    scopus 로고
    • Characterization of monomeric L1 metallo-β-lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis
    • SIMM AM, HIGGINS CS, CARENBAUER AL et al.: Characterization of monomeric L1 metallo-β-lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis. J. Biol. Chem. (2002) 277: 24744-24752.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24744-24752
    • Simm, A.M.1    Higgins, C.S.2    Carenbauer, A.L.3
  • 56
    • 0032698787 scopus 로고    scopus 로고
    • The reactivity of β-lactams, the mechanism of catalysis and the inhibition of β-lactamases
    • PAGE MI: The reactivity of β-lactams, the mechanism of catalysis and the inhibition of β-lactamases. Curr. Pharm. Des. (1999) 5: 895-913.
    • (1999) Curr. Pharm. Des. , vol.5 , pp. 895-913
    • Page, M.I.1
  • 57
    • 0036923291 scopus 로고    scopus 로고
    • Structural determinants and hydrogen-bond network of the mononuclear zinc(Ii)-β-lactamase active site
    • DAL PERARO M, VILA AJ, CARLONI P: Structural determinants and hydrogen-bond network of the mononuclear zinc(Ii)-β-lactamase active site. J. Biol. Inorg. Chem. (2002) 7: 704-712.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 704-712
    • Dal Peraro, M.1    Vila, A.J.2    Carloni, P.3
  • 58
    • 0019171830 scopus 로고
    • Inhibition of Escherichia coli TEM-2 β-lactamase by the sulfated compounds izumenolide, panosialin and sodium dodecyl sulfate
    • BUSH K, FREUDENBERGER J, SYKES RB: Inhibition of Escherichia coli TEM-2 β-lactamase by the sulfated compounds izumenolide, panosialin and sodium dodecyl sulfate. J. Antibiot. (1980) 33: 1560-1562.
    • (1980) J. Antibiot. , vol.33 , pp. 1560-1562
    • Bush, K.1    Freudenberger, J.2    Sykes, R.B.3
  • 59
    • 0242580779 scopus 로고    scopus 로고
    • Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 β-lactamase with β-lactamase inhibitory protein
    • ZHANG Z, PALZKILL T. Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 β-lactamase with β-lactamase inhibitory protein. J. Biol. Chem. (2003) 278: 45706-45712.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45706-45712
    • Zhang, Z.1    Palzkill, T.2
  • 61
    • 0034176494 scopus 로고    scopus 로고
    • β-Lactamase inhibitors
    • PAGE MG: β-Lactamase inhibitors. Drug Resist. Updat. (2000) 3: 109-125.
    • (2000) Drug Resist. Updat. , vol.3 , pp. 109-125
    • Page, M.G.1
  • 62
    • 2142758673 scopus 로고    scopus 로고
    • In vitro activities of the β-lactamase inhibitors clavulanic acid, sulbactam, and tazobactam alone or in combination with β -lactams against epidemiologically characterized multidrug-resistant Acinetobacter baumannii strains
    • HIGGINS PG, WISPLINGHOFF H, STEFANIK D, SEIFERT H: In vitro activities of the β-lactamase inhibitors clavulanic acid, sulbactam, and tazobactam alone or in combination with β-lactams against epidemiologically characterized multidrug-resistant Acinetobacter baumannii strains. Antimicrob. Agents Chemother. (2004) 48 1586-1592.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1586-1592
    • Higgins, P.G.1    Wisplinghoff, H.2    Stefanik, D.3    Seifert, H.4
  • 63
    • 0011854502 scopus 로고
    • 6β-bromopenicillanic acid, a potent β-lactamase inhibitor
    • PRATT RF, LOOSEMORE MJ: 6β-bromopenicillanic acid, a potent β-lactamase inhibitor. Proc. Natl. Acad. Sci. USA (1978) 75: 4145-4149.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4145-4149
    • Pratt, R.F.1    Loosemore, M.J.2
  • 64
    • 0026027626 scopus 로고
    • In vitro evaluation of ampicillin/brobactam and comparison with other β-lactam antibiotics
    • MELCHIOR NH, KEIDING J: In vitro evaluation of ampicillin/brobactam and comparison with other β-lactam antibiotics. J. Antimicrob. Chemother. (1991) 27: 29-40.
    • (1991) J. Antimicrob. Chemother. , vol.27 , pp. 29-40
    • Melchior, N.H.1    Keiding, J.2
  • 65
    • 0019793751 scopus 로고
    • Inhibition of the RTEM β-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid
    • CHARNAS RL, KNOWLES JR: Inhibition of the RTEM β-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid. Biochemistry (1981) 20: 2732-2737.
    • (1981) Biochemistry , vol.20 , pp. 2732-2737
    • Charnas, R.L.1    Knowles, J.R.2
  • 66
    • 0036739966 scopus 로고    scopus 로고
    • Clonal diversity and metallo-β-lactamase production in clinical isolates of Stenotrophomonas maltophilia
    • MERCURI PS, ISHII Y, MA L et al.: Clonal diversity and metallo-β-lactamase production in clinical isolates of Stenotrophomonas maltophilia. Microb. Drug Resist. (2002) 8: 193-200.
    • (2002) Microb. Drug Resist. , vol.8 , pp. 193-200
    • Mercuri, P.S.1    Ishii, Y.2    Ma, L.3
  • 67
    • 0141673604 scopus 로고    scopus 로고
    • Antimicrobial resistance among Gram-negative organisms in the intensive care unit
    • CLARK NM, PATTERSON J, LYNCH JP 3rd: Antimicrobial resistance among Gram-negative organisms in the intensive care unit. Curr. Opin. Crit. Care. (2003) 9: 413-423.
    • (2003) Curr. Opin. Crit. Care , vol.9 , pp. 413-423
    • Clark, N.M.1    Patterson, J.2    Lynch III, J.P.3
  • 68
    • 0043136483 scopus 로고    scopus 로고
    • Treatment of Acinetobacter spp. infections
    • LEVIN AS: Treatment of Acinetobacter spp. infections. Expert Opin. Pharmacother. (2003) 4: 1289-96.
    • (2003) Expert Opin. Pharmacother. , vol.4 , pp. 1289-1296
    • Levin, A.S.1
  • 69
    • 0018151178 scopus 로고
    • Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acid
    • FISHER J, CHARNAS RL, KNOWLES JR: Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acid. Biochemistry (1978) 17: 2180-2184.
    • (1978) Biochemistry , vol.17 , pp. 2180-2184
    • Fisher, J.1    Charnas, R.L.2    Knowles, J.R.3
  • 70
    • 0021767839 scopus 로고
    • 6-(Methoxymethylene)penicillanic acid: Inactivator of RTEM β-lactamase from Escherichia coli
    • BRENNER DG, KNOWLES JR: 6-(Methoxymethylene)penicillanic acid: inactivator of RTEM β-lactamase from Escherichia coli. Biochemistry (1984) 23: 5839-5846.
    • (1984) Biochemistry , vol.23 , pp. 5839-5846
    • Brenner, D.G.1    Knowles, J.R.2
  • 71
    • 0021767820 scopus 로고
    • Penicillanic acid sulfone: Nature of irreversible inactivation of RTEM β-lactamase from Escherichia coli
    • BRENNER DG, KNOWLES JR: Penicillanic acid sulfone: nature of irreversible inactivation of RTEM β-lactamase from Escherichia coli. Biochemistry (1984) 23: 5833-5839.
    • (1984) Biochemistry , vol.23 , pp. 5833-5839
    • Brenner, D.G.1    Knowles, J.R.2
  • 72
    • 0026587983 scopus 로고
    • Inhibition of β-lactamase by clavulanate. Trapped intermediates in cryo-crystallographic studies
    • CHEN CC, HERZBERG O: Inhibition of β-lactamase by clavulanate. Trapped intermediates in cryo-crystallographic studies. J. Mol. Biol. (1992) 224: 1103-1113.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1103-1113
    • Chen, C.C.1    Herzberg, O.2
  • 73
    • 0022820372 scopus 로고
    • Induction/inhibition of chromosomal β-lactamases by β-lactamase inhibitors
    • MOOSDEEN F, KEEBLE J, WILLIAMS JD: Induction/inhibition of chromosomal β-lactamases by β-lactamase inhibitors. Rev. Infect. Dis. (1986) 8 (Suppl. 5):S562-S568.
    • (1986) Rev. Infect. Dis. , vol.8 , Issue.SUPPL. 5
    • Moosdeen, F.1    Keeble, J.2    Williams, J.D.3
  • 74
    • 0343686104 scopus 로고    scopus 로고
    • Inhibitor-resistant TEM β-lactamases: Phenotypic, genetic and biochemical characteristics
    • CHAIBI EB, SIROT D, PAUL G, LABIA R: Inhibitor-resistant TEM β-lactamases: phenotypic, genetic and biochemical characteristics. J. Antimicrob. Chemother. (1999) 43: 447-458.
    • (1999) J. Antimicrob. Chemother. , vol.43 , pp. 447-458
    • Chaibi, E.B.1    Sirot, D.2    Paul, G.3    Labia, R.4
  • 75
    • 0346732273 scopus 로고    scopus 로고
    • Understanding resistance to β-lactams and β-lactamase inhibitors in the SHV β-lactamase: Lessons from the mutagenesis of SER-130
    • HELFAND MS, BETHEL CR, HUJER AM, HUJER KM, ANDERSON VE, BONOMO RA: Understanding resistance to β-lactams and β -lactamase inhibitors in the SHV β-lactamase: lessons from the mutagenesis of SER-130. J. Biol. Chem. (2003) 278: 52724-52729.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52724-52729
    • Helfand, M.S.1    Bethel, C.R.2    Hujer, A.M.3    Hujer, K.M.4    Anderson, V.E.5    Bonomo, R.A.6
  • 76
    • 11144353748 scopus 로고    scopus 로고
    • Variety of β-lactamases produced by amoxicillin-clavulanate-resistant Escherichia coli isolated in the northeastern United States
    • KAYE KS, GOLD HS, SCHWABER MJ et al.: Variety of β-lactamases produced by amoxicillin-clavulanate-resistant Escherichia coli isolated in the northeastern United States. Antimicrob Agents Chemother. (2004) 48: 1520-1525.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1520-1525
    • Kaye, K.S.1    Gold, H.S.2    Schwaber, M.J.3
  • 77
    • 2442520300 scopus 로고    scopus 로고
    • Tazobactam inactivation of SHV-1 and the inhibitor-resistant Ser130 → Gly SHV-1 β-lactamase: Insights into the mechanism of inhibition
    • PAGAN-RODRIGUEZ D, ZHOU X, SIMMONS R et al.: Tazobactam inactivation of SHV-1 and the inhibitor-resistant Ser130 → Gly SHV-1 β-lactamase: insights into the mechanism of inhibition. J. Biol. Chem. (2004) 279: 19494-19501.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19494-19501
    • Pagan-Rodriguez, D.1    Zhou, X.2    Simmons, R.3
  • 78
    • 0033827703 scopus 로고    scopus 로고
    • Characterization of a nosocomial outbreak caused by a multiresistant Acinetobacter baumannii strain with a carbapenem-hydrolyzing enzyme: High-level carbapenem resistance in A. baumannii is not due solely to the presence of β-lactamases
    • BOU G, CERVERO G, DOMINGUEZ MA, QUEREDA C, MARTINEZ-BELTRAN J: Characterization of a nosocomial outbreak caused by a multiresistant Acinetobacter baumannii strain with a carbapenem-hydrolyzing enzyme: high-level carbapenem resistance in A. baumannii is not due solely to the presence of β-lactamases. J. Clin. Microbiol. (2000) 38: 3299-305.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 3299-3305
    • Bou, G.1    Cervero, G.2    Dominguez, M.A.3    Quereda, C.4    Martinez-Beltran, J.5
  • 79
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • NIKAIDO H: Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. (2003) 67: 593-656.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 80
    • 1842637862 scopus 로고    scopus 로고
    • Klebsiella pneumoniae isolate from South Africa with multiple TEM, SHV and AmpC β-lactamases
    • ESSACK SY, HALL LM, LIVERMORE DM: Klebsiella pneumoniae isolate from South Africa with multiple TEM, SHV and AmpC β -lactamases. Int. J. Antimicrob. Agents (2004) 23: 398-400.
    • (2004) Int. J. Antimicrob. Agents , vol.23 , pp. 398-400
    • Essack, S.Y.1    Hall, L.M.2    Livermore, D.M.3
  • 81
    • 0041923557 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of OXA-45, an extended-spectrum class 2d′ β-lactamase in Pseudomonas aeruginosa
    • TOLEMAN MA, ROLSTON K, JONES RN, WALSH TR: Molecular and biochemical characterization of OXA-45, an extended-spectrum class 2d′ β-lactamase in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (2003) 47: 2859-2863.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2859-2863
    • Toleman, M.A.1    Rolston, K.2    Jones, R.N.3    Walsh, T.R.4
  • 82
    • 0025695724 scopus 로고
    • Epidemiological features and chemotherapy of community-acquired respiratory tract infections
    • FINCH RG: Epidemiological features and chemotherapy of community-acquired respiratory tract infections. J. Antimicrob. Chemother. (1990) 26 (Suppl. E):53-61.
    • (1990) J. Antimicrob. Chemother. , vol.26 , Issue.SUPPL. E , pp. 53-61
    • Finch, R.G.1
  • 83
    • 0034097902 scopus 로고    scopus 로고
    • β-Lactamase patterns and β-lactam/clavulanic acid resistance in Escherichia coli isolated from fecal samples from healthy volunteers
    • GULAY Z, BICMEN M, AMYES SG, YULUG N: β-Lactamase patterns and β-lactam/clavulanic acid resistance in Escherichia coli isolated from fecal samples from healthy volunteers. J. Chemother. (2000) 12: 208-215.
    • (2000) J. Chemother. , vol.12 , pp. 208-215
    • Gulay, Z.1    Bicmen, M.2    Amyes, S.G.3    Yulug, N.4
  • 84
    • 0036752271 scopus 로고    scopus 로고
    • Using steric hindrance to design new inhibitors of class C β -lactamases
    • TREHAN I, MORANDI F, BLASZCZAK LC, SHOICHET BK: Using steric hindrance to design new inhibitors of class C β-lactamases. Chem. Biol. (2002) 9: 971-980.
    • (2002) Chem. Biol. , vol.9 , pp. 971-980
    • Trehan, I.1    Morandi, F.2    Blaszczak, L.C.3    Shoichet, B.K.4
  • 85
    • 0035822659 scopus 로고    scopus 로고
    • Structures of ceftazidime and its transition-state analogue in complex with AmpC β-lactamase: Implications for resistance mutations and inhibitor design
    • POWERS RA, CASELLI E, FOCIA PJ, PRATI F, SHOICHET BK: Structures of ceftazidime and its transition-state analogue in complex with AmpC β-lactamase: implications for resistance mutations and inhibitor design. Biochemistry (2001) 40: 9207-9214.
    • (2001) Biochemistry , vol.40 , pp. 9207-9214
    • Powers, R.A.1    Caselli, E.2    Focia, P.J.3    Prati, F.4    Shoichet, B.K.5
  • 86
    • 0035838468 scopus 로고    scopus 로고
    • Inhibition of AmpC β-lactamase through a destabilizing interaction in the active site
    • TREHAN I, BEADLE BM, SHOICHET BK: Inhibition of AmpC β-lactamase through a destabilizing interaction in the active site. Biochemistry (2001) 40: 7992-7999.
    • (2001) Biochemistry , vol.40 , pp. 7992-7999
    • Trehan, I.1    Beadle, B.M.2    Shoichet, B.K.3
  • 87
    • 0029795726 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of 2β-alkenyl penam sulfone acids as inhibitors of β-lactamases
    • RICHTER HG, ANGEHRN P, HUBSCHWERLEN C et al.: Design, synthesis, and evaluation of 2β-alkenyl penam sulfone acids as inhibitors of β-lactamases. J. Med. Chem. (1996) 39: 3712-3722.
    • (1996) J. Med. Chem. , vol.39 , pp. 3712-3722
    • Richter, H.G.1    Angehrn, P.2    Hubschwerlen, C.3
  • 88
    • 0037777754 scopus 로고    scopus 로고
    • Spirocyclopropyl β-lactams as mechanism-based inhibitors of serine β-lactamases. Synthesis by rhodium-catalyzed cyclopropanation of 6-diazopenicillanate sulfone
    • SANDANAYAKA VP, PRASHAD AS, YANG Y, WILLIAMSON RT, LIN YI, MANSOUR TS: Spirocyclopropyl β-lactams as mechanism-based inhibitors of serine β-lactamases. Synthesis by rhodium-catalyzed cyclopropanation of 6-diazopenicillanate sulfone. J. Med. Chem. (2003) 46: 2569-2571.
    • (2003) J. Med. Chem. , vol.46 , pp. 2569-2571
    • Sandanayaka, V.P.1    Prashad, A.S.2    Yang, Y.3    Williamson, R.T.4    Lin, Y.I.5    Mansour, T.S.6
  • 89
    • 0034194737 scopus 로고    scopus 로고
    • The synthesis and evaluation of 3-substituted-7-(alkylidene)cephalosporin sulfones as β-lactamase inhibitors
    • BUYNAK JD, DOPPALAPUDI VR, ADAM G: The synthesis and evaluation of 3-substituted-7-(alkylidene)cephalosporin sulfones as β-lactamase inhibitors. Bioorg. Med. Chem. Lett. (2000) 10: 853-857.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 853-857
    • Buynak, J.D.1    Doppalapudi, V.R.2    Adam, G.3
  • 90
    • 0034194737 scopus 로고    scopus 로고
    • The synthesis and evaluation of 2-substituted-7-(alkylidene)cephalosporin sulfories as β-lactamase inhibitors
    • BUYNAK JD, DOPPALAPUDI VR, RAO AS, NIDAMARTHY SD, ADAM G: The synthesis and evaluation of 2-substituted-7-(alkylidene)cephalosporin sulfories as β-lactamase inhibitors. Bioorg. Med. Chem. Lett. (2000) 10: 847-851.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 847-851
    • Buynak, J.D.1    Doppalapudi, V.R.2    Rao, A.S.3    Nidamarthy, S.D.4    Adam, G.5
  • 91
    • 3343024286 scopus 로고    scopus 로고
    • Role of β-lactamases and porins in resistance to ertapenem and other β-lactams in Klebsiella pneumoniae
    • JACOBY GA, MILLS DM, CHOW N: Role of β-lactamases and porins in resistance to ertapenem and other β-lactams in Klebsiella pneumoniae. Antimicrob. Agents Chemother. (2004) 48: 3203-3206.
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 3203-3206
    • Jacoby, G.A.1    Mills, D.M.2    Chow, N.3
  • 92
    • 0035967506 scopus 로고    scopus 로고
    • Inhibition of class C β-lactamases: Structure of a reaction intermediate with a cephem sulfone
    • CRICHLOW GV, NUKAGA M, DOPPALAPUDI VR, BUYNAK JD, KNOX JR: Inhibition of class C β-lactamases: structure of a reaction intermediate with a cephem sulfone. Biochemistry (2001) 40: 6233-6239.
    • (2001) Biochemistry , vol.40 , pp. 6233-6239
    • Crichlow, G.V.1    Nukaga, M.2    Doppalapudi, V.R.3    Buynak, J.D.4    Knox, J.R.5
  • 93
    • 1242316384 scopus 로고    scopus 로고
    • Penicillin-derived inhibitors that simultaneously target both metallo- and serine-β-lactamases
    • BUYNAK JD, CHEN H, VOGETI L et al.: Penicillin-derived inhibitors that simultaneously target both metallo- and serine-β-lactamases. Bioorg. Med. Chem. Lett. (2004) 14: 1299-1304.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 1299-1304
    • Buynak, J.D.1    Chen, H.2    Vogeti, L.3
  • 95
    • 0041767488 scopus 로고    scopus 로고
    • In vitro activities of novel oxapenems, alone and in combination with ceftazidime, against Gram-positive and Gram-negative organisms
    • JAMIESON CE, LAMBERT PA, SIMPSON IN: In vitro activities of novel oxapenems, alone and in combination with ceftazidime, against Gram-positive and Gram-negative organisms. Antimicrob. Agents Chemother. (2003) 47: 2615-2618.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2615-2618
    • Jamieson, C.E.1    Lambert, P.A.2    Simpson, I.N.3
  • 97
    • 0020452803 scopus 로고
    • 6-Acetylmethylenepenicillanic acid (Ro 15-1903), a potent β-lactamase inhibitor. I. Inhibition of chromosomally and R-factor-mediated β-lactamases
    • ARISAWA M, THEN RL: 6-Acetylmethylenepenicillanic acid (Ro 15-1903), a potent β-lactamase inhibitor. I. Inhibition of chromosomally and R-factor-mediated β-lactamases. J. Antibiot. (1982) 35: 1578-1583.
    • (1982) J. Antibiot. , vol.35 , pp. 1578-1583
    • Arisawa, M.1    Then, R.L.2
  • 98
    • 0020408092 scopus 로고
    • 6-Acetylmethylenepenicillanic acid (Ro 15-1903), a potent β-lactamase inhibitor. II. Antibacterial properties
    • ANGEHRN P, ARISAWA M: 6-Acetylmethylenepenicillanic acid (Ro 15-1903), a potent β-lactamase inhibitor. II. Antibacterial properties. J. Antibiot. (1982) 35: 1584-1589.
    • (1982) J. Antibiot. , vol.35 , pp. 1584-1589
    • Angehrn, P.1    Arisawa, M.2
  • 100
    • 0025816298 scopus 로고
    • Pharmacokinetic studies and renal dehydropeptidase stability of the new β-lactamase inhibitor BRL 42715 in animals
    • COLEMAN K, GRIFFIN DR, UPSHON PA: Pharmacokinetic studies and renal dehydropeptidase stability of the new β-lactamase inhibitor BRL 42715 in animals. Antimicrob. Agents Chemother. (1991) 35: 1748-1752.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1748-1752
    • Coleman, K.1    Griffin, D.R.2    Upshon, P.A.3
  • 101
    • 0242569199 scopus 로고    scopus 로고
    • Inhibition of class A and class C β-lactamases by penems: Crystallographic structures of a novel 1,4-thiazepine intermediate
    • NUKAGA M, ABE T, VENKATESAN AM, MANSOUR TS, BONOMO RA, KNOX JR. Inhibition of class A and class C β-lactamases by penems: crystallographic structures of a novel 1,4-thiazepine intermediate. Biochemistry (2003) 42: 13152-13159.
    • (2003) Biochemistry , vol.42 , pp. 13152-13159
    • Nukaga, M.1    Abe, T.2    Venkatesan, A.M.3    Mansour, T.S.4    Bonomo, R.A.5    Knox, J.R.6
  • 102
    • 0032497590 scopus 로고    scopus 로고
    • Structure-based design of β-lactamase inhibitors. 2. Synthesis and evaluation of bridged sulfactams and oxamazins
    • HUBSCHWERLEN C, ANGEHRN P, GUBERNATOR K, PAGE MG, SPECKLIN JL: Structure-based design of β-lactamase inhibitors. 2. Synthesis and evaluation of bridged sulfactams and oxamazins. J. Med. Chem. (1998) 41: 3972-3975.
    • (1998) J. Med. Chem. , vol.41 , pp. 3972-3975
    • Hubschwerlen, C.1    Angehrn, P.2    Gubernator, K.3    Page, M.G.4    Specklin, J.L.5
  • 103
    • 0344175930 scopus 로고    scopus 로고
    • Structure-based design of β-lactamase inhibitors. 1. Synthesis and evaluation of bridged monobactams
    • HEINZE-KRAUSS I, ANGEHRN P, CHARNAS RL et al.: Structure-based design of β-lactamase inhibitors. 1. Synthesis and evaluation of bridged monobactams. J. Med. Chem. (1998) 41: 3961-3971.
    • (1998) J. Med. Chem. , vol.41 , pp. 3961-3971
    • Heinze-Krauss, I.1    Angehrn, P.2    Charnas, R.L.3
  • 104
    • 0032858683 scopus 로고    scopus 로고
    • In vitro and in vivo activities of Syn2190, a novel β-lactamase inhibitor
    • NISHIDA K, KUNUGITA C, UJI T et al.: In vitro and in vivo activities of Syn2190, a novel β-lactamase inhibitor. Antimicrob Agents Chemother. (1999) 43: 1895-1900.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1895-1900
    • Nishida, K.1    Kunugita, C.2    Uji, T.3
  • 105
    • 0020684492 scopus 로고
    • The inhibition of class C β-lactamases by boronic acids
    • BEESLEY T, GASCOYNE N, KNOTT-HUNZIKER V et al.: The inhibition of class C β-lactamases by boronic acids. Biochem. J. (1983) 209: 229-233.
    • (1983) Biochem. J. , vol.209 , pp. 229-233
    • Beesley, T.1    Gascoyne, N.2    Knott-Hunziker, V.3
  • 106
    • 0034974174 scopus 로고    scopus 로고
    • Structure-based design and in-parallel synthesis of inhibitors of AmpC β-lactamase
    • TONDI D, POWERS RA, CASELLI E et al.: Structure-based design and in-parallel synthesis of inhibitors of AmpC β-lactamase. Chem. Biol. (2001) 8: 593-611.
    • (2001) Chem. Biol. , vol.8 , pp. 593-611
    • Tondi, D.1    Powers, R.A.2    Caselli, E.3
  • 107
    • 0345102428 scopus 로고    scopus 로고
    • The complexed structure and antimicrobial activity of a non-β-lactam inhibitor of AmpC β-lactamase
    • POWERS RA, BLAZQUEZ J, WESTON GS, MOROSINI MI, BAQUERO F, SHOICHET BK: The complexed structure and antimicrobial activity of a non-β-lactam inhibitor of AmpC β-lactamase. Protein Sci. (1999) 8: 2330-2337.
    • (1999) Protein Sci. , vol.8 , pp. 2330-2337
    • Powers, R.A.1    Blazquez, J.2    Weston, G.S.3    Morosini, M.I.4    Baquero, F.5    Shoichet, B.K.6
  • 108
    • 0034625157 scopus 로고    scopus 로고
    • Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 β -lactamase
    • NESS S, MARTIN R, KINDLER AM et al.: Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 β-lactamase. Biochemistry (2000) 39: 5312-5321.
    • (2000) Biochemistry , vol.39 , pp. 5312-5321
    • Ness, S.1    Martin, R.2    Kindler, A.M.3
  • 109
    • 0026664512 scopus 로고
    • Mechanism of inhibition of the class C β-lactamase of Enterobacter cloacae P99 by phosphonate monoesters
    • RAHIL J, PRATT RF: Mechanism of inhibition of the class C β-lactamase of Enterobacter cloacae P99 by phosphonate monoesters. Biochemistry (1992) 31: 5869-5878.
    • (1992) Biochemistry , vol.31 , pp. 5869-5878
    • Rahil, J.1    Pratt, R.F.2
  • 110
    • 0027451306 scopus 로고
    • Structure of a phosphonate-inhibited β-lactamase. An analog of the tetrahedral transition state/intermediate of β-lactam hydrolysis
    • CHEN CC, RAHIL J, PRATT RF, HERZBERG O: Structure of a phosphonate-inhibited β-lactamase. An analog of the tetrahedral transition state/intermediate of β-lactam hydrolysis. J. Mol. Biol. (1993) 234: 165-178.
    • (1993) J. Mol. Biol. , vol.234 , pp. 165-178
    • Chen, C.C.1    Rahil, J.2    Pratt, R.F.3    Herzberg, O.4
  • 111
    • 0028224698 scopus 로고
    • Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a β-lactamase transition-state analog
    • LOBKOVSKY E, BILLINGS EM, MOEWS PC, RAHIL J, PRATT RF, KNOX JR: Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a β-lactamase transition-state analog. Biochemistry (1994) 33: 6762-6772.
    • (1994) Biochemistry , vol.33 , pp. 6762-6772
    • Lobkovsky, E.1    Billings, E.M.2    Moews, P.C.3    Rahil, J.4    Pratt, R.F.5    Knox, J.R.6
  • 112
    • 0037452523 scopus 로고    scopus 로고
    • Inhibition of β-lactamases by monocyclic acyl phosph(on)ates
    • KAUR K, ADEDIRAN SA, LAN MJ, PRATT RF: Inhibition of β-lactamases by monocyclic acyl phosph(on)ates. Biochemistry (2003) 42: 1529-1536.
    • (2003) Biochemistry , vol.42 , pp. 1529-1536
    • Kaur, K.1    Adediran, S.A.2    Lan, M.J.3    Pratt, R.F.4
  • 114
    • 0025186624 scopus 로고
    • Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa
    • TRIAS J, NIKAIDO H: Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (1990) 34: 52-57.
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 52-57
    • Trias, J.1    Nikaido, H.2
  • 115
    • 0025799683 scopus 로고
    • Role of OmpD2 and chromosomal β-lactamase in carbapenem resistance in clinical isolates of Pseudomonas aeruginosa
    • SATAKE S, YONEYAMA H, NAKAE T: Role of OmpD2 and chromosomal β-lactamase in carbapenem resistance in clinical isolates of Pseudomonas aeruginosa. J. Antimicrob. Chemother. (1991) 28: 199-207.
    • (1991) J. Antimicrob. Chemother. , vol.28 , pp. 199-207
    • Satake, S.1    Yoneyama, H.2    Nakae, T.3
  • 116
    • 0026730399 scopus 로고
    • Interplay of impermeability and chromosomal β-lactamase activity in imipenem-resistant Pseudomonas aeruginosa
    • LIVERMORE DM: Interplay of impermeability and chromosomal β-lactamase activity in imipenem-resistant Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (1992) 36: 2046-2048.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 2046-2048
    • Livermore, D.M.1
  • 117
    • 0027488699 scopus 로고
    • Mechanism of efficient elimination of protein D2 in outer membrane of imipenem-resistant Pseudomonas aeruginosa
    • YONEYAMA H, NAKAE T: Mechanism of efficient elimination of protein D2 in outer membrane of imipenem-resistant Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (1993) 37: 2385-2390.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2385-2390
    • Yoneyama, H.1    Nakae, T.2
  • 118
    • 0036934494 scopus 로고    scopus 로고
    • Alterations of susceptibility of Pseudamonas aeruginosa by overproduction of multidrug efflux systems, MexAB-OprM, MexCD-OprJ, and MexXY/OprM to carbapenems: Substrate specificities of the efflux systems
    • OKAMOTO K, GOTOH N, NISHINO T: Alterations of susceptibility of Pseudamonas aeruginosa by overproduction of multidrug efflux systems, MexAB-OprM, MexCD-OprJ, and MexXY/OprM to carbapenems: substrate specificities of the efflux systems. J. Infect. Chemother. (2002) 8: 371-373.
    • (2002) J. Infect. Chemother. , vol.8 , pp. 371-373
    • Okamoto, K.1    Gotoh, N.2    Nishino, T.3
  • 119
    • 0035992009 scopus 로고    scopus 로고
    • Extrusion of penem antibiotics by multicomponent efflux systems MexAB-OprM, MexCD-OprJ, and MexXY-OprM of Pseudomonas aeruginosa
    • OKAMOTO K, GOTOH N, NISHINO T: Extrusion of penem antibiotics by multicomponent efflux systems MexAB-OprM, MexCD-OprJ, and MexXY-OprM of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (2002) 46: 2696-2699.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2696-2699
    • Okamoto, K.1    Gotoh, N.2    Nishino, T.3
  • 120
    • 0034426126 scopus 로고    scopus 로고
    • Substrate specificities of MexAB-OprM, MexCD-OprJ, and MexXY-oprM efflux pumps in Pseudomonas aeruginosa
    • MASUDA N, SAKAGAWA E, OHYA S, GOTOH N, TSUJIMOTO H, NISHINO T: Substrate specificities of MexAB-OprM, MexCD-OprJ, and MexXY-oprM efflux pumps in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. (2000) 44: 3322-3327.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3322-3327
    • Masuda, N.1    Sakagawa, E.2    Ohya, S.3    Gotoh, N.4    Tsujimoto, H.5    Nishino, T.6
  • 121
    • 0034117784 scopus 로고    scopus 로고
    • Interplay between the MexA-MexB-OprM multidrug efflux system and the outer membrane barrier in the multiple antibiotic resistance of Pseudomonas aeruginosa
    • LI XZ, ZHANG L, POOLE K: Interplay between the MexA-MexB-OprM multidrug efflux system and the outer membrane barrier in the multiple antibiotic resistance of Pseudomonas aeruginosa. J. Antimicrob. Chemother. (2000) 45: 433-436.
    • (2000) J. Antimicrob. Chemother. , vol.45 , pp. 433-436
    • Li, X.Z.1    Zhang, L.2    Poole, K.3
  • 122
    • 1542335656 scopus 로고    scopus 로고
    • CzcR-CzcS, a two-component system involved in heavy metal and carbapenem resistance in Pseudomonas aeruginosa
    • PERRON K, CAILLE O, ROSSIER C, VAN DELDEN C, DUMAS JL, KOHLER T: CzcR-CzcS, a two-component system involved in heavy metal and carbapenem resistance in Pseudomonas aeruginosa. J. Biol. Chem. (2004) 279: 8761-8768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8761-8768
    • Perron, K.1    Caille, O.2    Rossier, C.3    Van Delden, C.4    Dumas, J.L.5    Kohler, T.6
  • 123
    • 0343621539 scopus 로고    scopus 로고
    • Multiple antibiotic resistance in Stenotrophomonas maltophilia: Involvement of a multidrug efflux system
    • ZHANG L, LI XZ, POOLE K: Multiple antibiotic resistance in Stenotrophomonas maltophilia: involvement of a multidrug efflux system. Antimicrob. Agents Chemother. (2000) 44: 287-293.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 287-293
    • Zhang, L.1    Li, X.Z.2    Poole, K.3
  • 124
    • 0035087832 scopus 로고    scopus 로고
    • Multidrug efflux pumps and antimicrobial resistance in Pseudomonas aeruginosa and related organisms
    • POOLE K: Multidrug efflux pumps and antimicrobial resistance in Pseudomonas aeruginosa and related organisms. J. Mol. Microbiol. Biotechnol. (2001) 3: 255-264.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 255-264
    • Poole, K.1
  • 126
  • 127
    • 12244283750 scopus 로고    scopus 로고
    • Integration of a transposon Tn1-encoded inhibitor-resistant β-lactamase gene, bla(TEM-67) from Proteus mirabilis, into the Escherichia coli chromosome
    • NAAS T, ZERBIB M, GIRLICH D, NORDMANN P: Integration of a transposon Tn1-encoded inhibitor-resistant β-lactamase gene, bla(TEM-67) from Proteus mirabilis, into the Escherichia coli chromosome. Antimicrob. Agents Chemother. (2003) 47: 19-26.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 19-26
    • Naas, T.1    Zerbib, M.2    Girlich, D.3    Nordmann, P.4
  • 128
    • 4444347175 scopus 로고    scopus 로고
    • In vitro activity of AVE1330A, an innovative broad-spectrum non-β-lactam β-lactamase inhibitor
    • BONNEFOY A, DUPUIS-HAMELIN C, STEIER V et al.: In vitro activity of AVE1330A, an innovative broad-spectrum non-β -lactam β-lactamase inhibitor. J. Antimicrob. Chemother. (2004) 54: 410-417.
    • (2004) J. Antimicrob. Chemother. , vol.54 , pp. 410-417
    • Bonnefoy, A.1    Dupuis-Hamelin, C.2    Steier, V.3


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