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Volumn 6, Issue 4, 2014, Pages 413-427

Fragment-based inhibitor discovery against β-lactamase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BETA LACTAMASE; BETA LACTAMASE CTX M; BETA LACTAMASE CTX M 9; BETA LACTAMASE INHIBITOR; CEFOTAXIME; CEFTAZIDIME; DICARBOXYLIC ACID; EXTENDED SPECTRUM BETA LACTAMASE; HYDROLASE; METALLO BETA LACTAMASE; SERINE BETA LACTAMASE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84896932244     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.14.10     Document Type: Review
Times cited : (17)

References (115)
  • 3
    • 0029019031 scopus 로고
    • Beta-lactamases and bacterial resistance to antibiotics
    • Frere JM. Beta-lactamases and bacterial resistance to antibiotics. Mol. Microbiol. 16(3), 385-395 (1995).
    • (1995) Mol. Microbiol. , vol.16 , Issue.3 , pp. 385-395
    • Frere, J.M.1
  • 4
    • 47749093130 scopus 로고    scopus 로고
    • The bacteria fight back
    • Taubes G. The bacteria fight back. Science 321(5887), 356-361 (2008).
    • (2008) Science , vol.321 , Issue.5887 , pp. 356-361
    • Taubes, G.1
  • 5
    • 0029071785 scopus 로고
    • A functional classification scheme for beta-lactamases and its correlation with molecular structure
    • Bush K, Jacoby GA, Medeiros AA. A functional classification scheme for beta-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39(6), 1211-1233. (1995).
    • (1995) Antimicrob. Agents Chemother. , vol.39 , Issue.6 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 6
    • 0028883511 scopus 로고
    • Beta-lactamases in laboratory and clinical resistance
    • Livermore DM. Beta-lactamases in laboratory and clinical resistance. Clin. Microbiol. Rev. 8(4), 557-584 (1995).
    • (1995) Clin. Microbiol. Rev. , vol.8 , Issue.4 , pp. 557-584
    • Livermore, D.M.1
  • 7
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to beta-lactam antibiotics: Compelling opportunism, compelling opportunity
    • Fisher JF, Meroueh SO, Mobashery S. Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity. Chem. Rev. 105(2), 395-424 (2005).
    • (2005) Chem. Rev. , vol.105 , Issue.2 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 8
    • 0347362476 scopus 로고    scopus 로고
    • Growing group of extended-spectrum beta-lactamases: The CTX-M enzymes
    • Bonnet R. Growing group of extended-spectrum beta-lactamases: the CTX-M enzymes. Antimicrob. Agents Chemother. 48(1), 1-14 (2004).
    • (2004) Antimicrob. Agents Chemother. , vol.48 , Issue.1 , pp. 1-14
    • Bonnet, R.1
  • 9
    • 16244415566 scopus 로고    scopus 로고
    • Atomic resolution structures of CTX-M beta-lactamases: Extended spectrum activities from increased mobility and decreased stability
    • Chen Y, Delmas J, Sirot J, Shoichet B, Bonnet R. Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability. J. Mol. Biol. 348(2), 349-362. (2005).
    • (2005) J. Mol. Biol. , vol.348 , Issue.2 , pp. 349-362
    • Chen, Y.1    Delmas, J.2    Sirot, J.3    Shoichet, B.4    Bonnet, R.5
  • 10
    • 17644390560 scopus 로고    scopus 로고
    • Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases
    • Chen Y, Shoichet B, Bonnet R. Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases. J. Am. Chem. Soc. 127(15), 5423-5434. (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.15 , pp. 5423-5434
    • Chen, Y.1    Shoichet, B.2    Bonnet, R.3
  • 11
    • 0034763241 scopus 로고    scopus 로고
    • Extended-spectrum beta-lactamases in the 21st century: Characterization, epidemiology, and detection of this important resistance threat
    • Bradford PA. Extended-spectrum beta-lactamases in the 21st century: characterization, epidemiology, and detection of this important resistance threat. Clin. Microbiol. Rev. 14(4), 933-951 (2001).
    • (2001) Clin. Microbiol. Rev. , vol.14 , Issue.4 , pp. 933-951
    • Bradford, P.A.1
  • 13
    • 73849149415 scopus 로고    scopus 로고
    • Hydrolysis and inhibition profiles of beta-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem
    • Queenan AM, Shang W, Flamm R, Bush K. Hydrolysis and inhibition profiles of beta-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem. Antimicrob. Agents Chemother. 54(1), 565-569 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.1 , pp. 565-569
    • Queenan, A.M.1    Shang, W.2    Flamm, R.3    Bush, K.4
  • 14
    • 79957581336 scopus 로고    scopus 로고
    • Status report on carbapenemases: Challenges and prospects
    • Patel G, Bonomo RA. Status report on carbapenemases: challenges and prospects. Expert Rev. Anti Infect. Ther. 9(5), 555-570 (2012).
    • (2012) Expert Rev. Anti Infect. Ther. , vol.9 , Issue.5 , pp. 555-570
    • Patel, G.1    Bonomo, R.A.2
  • 15
    • 33747795961 scopus 로고    scopus 로고
    • What's new in antibiotic resistance? Focus on beta-lactamases
    • Babic M, Hujer AM, Bonomo RA. What's new in antibiotic resistance? Focus on beta-lactamases. Drug Resist. Updat. 9(3), 142-156 (2006).
    • (2006) Drug Resist. Updat. , vol.9 , Issue.3 , pp. 142-156
    • Babic, M.1    Hujer, A.M.2    Bonomo, R.A.3
  • 16
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of beta-lactamase inhibitors
    • Drawz SM, Bonomo RA. Three decades of beta-lactamase inhibitors. Clin. Microbiol. Rev. 23(1), 160-201 (2010).
    • (2010) Clin. Microbiol. Rev. , vol.23 , Issue.1 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 17
    • 0027513336 scopus 로고
    • Molecular basis of beta-lactamase induction in bacteria
    • Bennett PM, Chopra I. Molecular basis of beta-lactamase induction in bacteria. Antimicrob. Agents Chemother. 37(2), 153-158 (1993).
    • (1993) Antimicrob. Agents Chemother. , vol.37 , Issue.2 , pp. 153-158
    • Bennett, P.M.1    Chopra, I.2
  • 18
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in gram-negative bacteria
    • Jacobs C, Frere JM, Normark S. Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in gram-negative bacteria. Cell 88, 823-832 (1997).
    • (1997) Cell , vol.88 , pp. 823-832
    • Jacobs, C.1    Frere, J.M.2    Normark, S.3
  • 19
    • 0031670104 scopus 로고    scopus 로고
    • Beta-lactamases: Protein evolution in real time
    • Petrosino J, Cantu C 3rd, Palzkill T. Beta-lactamases: protein evolution in real time. Trends Microbiol. 6(8), 323-327 (1998).
    • (1998) Trends Microbiol. , vol.6 , Issue.8 , pp. 323-327
    • Petrosino, J.1    Cantu III, C.2    Palzkill, T.3
  • 20
    • 62849121696 scopus 로고    scopus 로고
    • Efflux pump, the masked side of beta-lactam resistance in Klebsiella pneumoniae clinical isolates
    • Pages JM, Lavigne JP, Leflon-Guibout V et al. Efflux pump, the masked side of beta-lactam resistance in Klebsiella pneumoniae clinical isolates. PloS ONE 4(3), e4817 (2009).
    • (2009) PloS ONE , vol.4 , Issue.3
    • Pages, J.M.1    Lavigne, J.P.2    Leflon-Guibout, V.3
  • 21
    • 84863905057 scopus 로고    scopus 로고
    • Avibactam is a covalent, reversible, non-beta-lactam beta-lactamase inhibitor
    • Ehmann DE, Jahic H, Ross PL et al. Avibactam is a covalent, reversible, non-beta-lactam beta-lactamase inhibitor. Proc. Natl Acad. Sci. USA 109(29), 11663-11668 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , Issue.29 , pp. 11663-11668
    • De, E.1    Jahic, H.2    Ross, P.L.3
  • 22
    • 84877842576 scopus 로고    scopus 로고
    • Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: Avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC beta-lactamases
    • Lahiri SD, Mangani S, Durand-Reville T et al. Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC beta-lactamases. Antimicrob. Agents Chemother. 57(6), 2496-2505 (2013).
    • (2013) Antimicrob. Agents Chemother. , vol.57 , Issue.6 , pp. 2496-2505
    • Lahiri, S.D.1    Mangani, S.2    Durand-Reville, T.3
  • 23
    • 84884764949 scopus 로고    scopus 로고
    • Kinetics of avibactam inhibition against class A, C, and D beta-lactamases
    • Ehmann DE, Jahic H, Ross PL et al. Kinetics of avibactam inhibition against class A, C, and D beta-lactamases. J. Biol. Chem. 288(39), 27960-27971 (2013).
    • (2013) J. Biol. Chem. , vol.288 , Issue.39 , pp. 27960-27971
    • De, E.1    Jahic, H.2    Ross, P.L.3
  • 24
    • 84877858916 scopus 로고    scopus 로고
    • In vitro activity of Biapenem plus RPX7009, a carbapenem combined with a serine beta-lactamase inhibitor, against anaerobic bacteria
    • Goldstein EJ, Citron DM, Tyrrell KL, Merriam CV. In vitro activity of Biapenem plus RPX7009, a carbapenem combined with a serine beta-lactamase inhibitor, against anaerobic bacteria. Antimicrob. Agents Chemother. 57(6), 2620-2630 (2013).
    • (2013) Antimicrob. Agents Chemother. , vol.57 , Issue.6 , pp. 2620-2630
    • Goldstein, E.J.1    Citron, D.M.2    Tyrrell, K.L.3    Merriam, C.V.4
  • 25
    • 84880714408 scopus 로고    scopus 로고
    • Activity of biapenem (RPX2003) combined with the boronate beta-lactamase inhibitor RPX7009 against carbapenem-resistant Enterobacteriaceae
    • Livermore DM, Mushtaq S. Activity of biapenem (RPX2003) combined with the boronate beta-lactamase inhibitor RPX7009 against carbapenem-resistant Enterobacteriaceae. J. Antimicrob. Chemother. 68(8), 1825-1831 (2013).
    • (2013) J. Antimicrob. Chemother. , vol.68 , Issue.8 , pp. 1825-1831
    • Livermore, D.M.1    Mushtaq, S.2
  • 26
    • 0025849757 scopus 로고
    • Phosphonate monoester inhibitors of class A beta-lactamases
    • Rahil J, Pratt RF. Phosphonate monoester inhibitors of class A beta-lactamases. Biochem. J. 275(Pt 3), 793-795 (1991).
    • (1991) Biochem. J. , vol.275 , Issue.PART 3 , pp. 793-795
    • Rahil, J.1    Pratt, R.F.2
  • 28
    • 84867919842 scopus 로고    scopus 로고
    • Fragment-guided design of subnanomolar beta-lactamase inhibitors active in vivo
    • Eidam O, Romagnoli C, Dalmasso G et al. Fragment-guided design of subnanomolar beta-lactamase inhibitors active in vivo. Proc. Natl. Acad Sci. USA 109(43), 17448-17453 (2012).
    • (2012) Proc. Natl. Acad Sci. USA , vol.109 , Issue.43 , pp. 17448-17453
    • Eidam, O.1    Romagnoli, C.2    Dalmasso, G.3
  • 29
    • 34547780834 scopus 로고    scopus 로고
    • O-aryloxycarbonyl hydroxamates: New beta-lactamase inhibitors that cross-link the active site
    • Wyrembak PN, Babaoglu K, Pelto RB, Shoichet BK, Pratt RF. O-aryloxycarbonyl hydroxamates: new beta-lactamase inhibitors that cross-link the active site. J. Am. Chem. Soc. 129(31), 9548-9549 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.31 , pp. 9548-9549
    • Wyrembak, P.N.1    Babaoglu, K.2    Pelto, R.B.3    Shoichet, B.K.4    Pratt, R.F.5
  • 30
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • Payne DJ, Gwynn MN, Holmes DJ, Pompliano DL. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat. Rev. Drug Discov. 6(1), 29-40 (2007).
    • (2007) Nat. Rev. Drug Discov. , vol.6 , Issue.1 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 31
    • 43049129991 scopus 로고    scopus 로고
    • Comprehensive mechanistic analysis of hits from high-throughput and docking screens against beta-lactamase
    • Babaoglu K, Simeonov A, Irwin JJ et al. Comprehensive mechanistic analysis of hits from high-throughput and docking screens against beta-lactamase. J. Med. Chem. 51(8), 2502-2511. (2008).
    • (2008) J. Med. Chem. , vol.51 , Issue.8 , pp. 2502-2511
    • Babaoglu, K.1    Simeonov, A.2    Irwin, J.J.3
  • 32
    • 77952281288 scopus 로고    scopus 로고
    • Antibacterial oxazolidinones: Emerging structure-toxicity relationships
    • Renslo AR. Antibacterial oxazolidinones: emerging structure-toxicity relationships. Expert Rev. Anti Infect. Ther. 8(5), 565-574 (2010).
    • (2010) Expert Rev. Anti Infect. Ther. , vol.8 , Issue.5 , pp. 565-574
    • Renslo, A.R.1
  • 33
    • 41849111626 scopus 로고    scopus 로고
    • Linezolid (ZYVOX), the first member of a completely new class of antibacterial agents for treatment of serious gram-positive infections
    • Brickner SJ, Barbachyn MR, Hutchinson DK, Manninen PR. Linezolid (ZYVOX), the first member of a completely new class of antibacterial agents for treatment of serious gram-positive infections. J. Med. Chem. 51(7), 1981-1990 (2008).
    • (2008) J. Med. Chem. , vol.51 , Issue.7 , pp. 1981-1990
    • Brickner, S.J.1    Barbachyn, M.R.2    Hutchinson, D.K.3    Manninen, P.R.4
  • 34
    • 43949129098 scopus 로고    scopus 로고
    • Physicochemical properties of antibacterial compounds: Implications for drug discovery
    • O'shea R, Moser HE. Physicochemical properties of antibacterial compounds: implications for drug discovery. J. Med. Chem. 51(10), 2871-2878 (2008).
    • (2008) J. Med. Chem. , vol.51 , Issue.10 , pp. 2871-2878
    • O'Shea, R.1    Moser, H.E.2
  • 36
    • 34247194965 scopus 로고    scopus 로고
    • Virtual exploration of the chemical universe up to 11 atoms of C, N, O, F: Assembly of 26.4 million structures (110.9 million stereoisomers) and analysis for new ring systems, stereochemistry, physicochemical properties, compound classes, and drug discovery
    • Fink T, Reymond JL. Virtual exploration of the chemical universe up to 11 atoms of C, N, O, F: assembly of 26.4 million structures (110.9 million stereoisomers) and analysis for new ring systems, stereochemistry, physicochemical properties, compound classes, and drug discovery. J. Chem. Inf. Model. 47(2), 342-353 (2007).
    • (2007) J. Chem. Inf. Model. , vol.47 , Issue.2 , pp. 342-353
    • Fink, T.1    Reymond, J.L.2
  • 37
    • 0030039619 scopus 로고    scopus 로고
    • The art and practice of structure-based drug design: A molecular modeling perspective
    • Bohacek RS, Mcmartin C, Guida WC. The art and practice of structure-based drug design: a molecular modeling perspective. Med. Res. Rev. 16(1), 3-50 (1996).
    • (1996) Med. Res. Rev. , vol.16 , Issue.1 , pp. 3-50
    • Bohacek, R.S.1    McMartin, C.2    Guida, W.C.3
  • 38
    • 84881315859 scopus 로고    scopus 로고
    • The 'rule of three' for fragment-based drug discovery: Where are we now?
    • Jhoti H, Williams G, Rees DC, Murray CW. The 'rule of three' for fragment-based drug discovery: where are we now? Nat. Rev. Drug Discov. 12(8), 644 (2013).
    • (2013) Nat. Rev. Drug Discov. , vol.12 , Issue.8 , pp. 644
    • Jhoti, H.1    Williams, G.2    Rees, D.C.3    Murray, C.W.4
  • 40
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • Hajduk PJ, Greer J. A decade of fragment-based drug design: strategic advances and lessons learned. Nat. Rev. Drug Discov. 6(3), 211-219 (2007).
    • (2007) Nat. Rev. Drug Discov. , vol.6 , Issue.3 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 41
    • 70349425790 scopus 로고    scopus 로고
    • Recent progress in fragment-based lead discovery
    • Schulz MN, Hubbard RE. Recent progress in fragment-based lead discovery. Curr. Opin. Pharmacol. 9(5), 615-621 (2009).
    • (2009) Curr. Opin. Pharmacol. , vol.9 , Issue.5 , pp. 615-621
    • Schulz, M.N.1    Hubbard, R.E.2
  • 42
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker SB, Hajduk PJ, Meadows RP, Fesik SW. Discovering high-affinity ligands for proteins: SAR by NMR. Science 274, 1531-1534 (1996).
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 43
    • 51249121331 scopus 로고    scopus 로고
    • Perspectives on NMR in drug discovery: A technique comes of age
    • Pellecchia M, Bertini I, Cowburn D et al. Perspectives on NMR in drug discovery: a technique comes of age. Nat. Rev. Drug Discov. 7(9), 738-745. (2008).
    • (2008) Nat. Rev. Drug Discov. , vol.7 , Issue.9 , pp. 738-745
    • Pellecchia, M.1    Bertini, I.2    Cowburn, D.3
  • 45
    • 47749136565 scopus 로고    scopus 로고
    • Discovery of triazolinone non-nucleoside inhibitors of HIV reverse transcriptase
    • Sweeney ZK, Acharya S, Briggs A et al. Discovery of triazolinone non-nucleoside inhibitors of HIV reverse transcriptase. Bioorg. Med. Chem. Lett. 18(15), 4348-4351. (2008).
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.15 , pp. 4348-4351
    • Sweeney, Z.K.1    Acharya, S.2    Briggs, A.3
  • 46
    • 84862869077 scopus 로고    scopus 로고
    • Fragment-based approaches in drug discovery and chemical biology
    • Scott DE, Coyne AG, Hudson SA, Abell C. Fragment-based approaches in drug discovery and chemical biology. Biochemistry 51(25), 4990-5003 (2012).
    • (2012) Biochemistry , vol.51 , Issue.25 , pp. 4990-5003
    • De, S.1    Coyne, A.G.2    Hudson, S.A.3    Abell, C.4
  • 47
    • 84874414338 scopus 로고    scopus 로고
    • Fragment-based lead discovery grows up
    • Baker M. Fragment-based lead discovery grows up. Nat. Rev. Drug Discov. 12(1), 5-7 (2013).
    • (2013) Nat. Rev. Drug Discov. , vol.12 , Issue.1 , pp. 5-7
    • Baker, M.1
  • 48
    • 0036076470 scopus 로고    scopus 로고
    • Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase
    • Powers RA, Morandi F, Shoichet BK. Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase. Structure 10(7), 1013-1023 (2002).
    • (2002) Structure , vol.10 , Issue.7 , pp. 1013-1023
    • Powers, R.A.1    Morandi, F.2    Shoichet, B.K.3
  • 49
    • 1242294467 scopus 로고    scopus 로고
    • Allosteric inhibition through core disruption
    • Horn JR, Shoichet BK. Allosteric inhibition through core disruption. J. Mol. Biol. 336(5), 1283-1291 (2004).
    • (2004) J. Mol. Biol. , vol.336 , Issue.5 , pp. 1283-1291
    • Horn, J.R.1    Shoichet, B.K.2
  • 50
    • 0035943678 scopus 로고    scopus 로고
    • Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase
    • Toney JH, Hammond GG, Fitzgerald PM et al. Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase. J. Biol. Chem. 276(34), 31913-31918 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.34 , pp. 31913-31918
    • Toney, J.H.1    Hammond, G.G.2    Fitzgerald, P.M.3
  • 51
    • 13144295022 scopus 로고    scopus 로고
    • Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase
    • Toney JH, Fitzgerald PM, Grover-Sharma N et al. Antibiotic sensitization using biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis metallo-beta-lactamase. Chem. Biol. 5(4), 185-196 (1998).
    • (1998) Chem. Biol. , vol.5 , Issue.4 , pp. 185-196
    • Toney, J.H.1    Fitzgerald, P.M.2    Grover-Sharma, N.3
  • 52
    • 68349152498 scopus 로고    scopus 로고
    • Metallo-beta-lactamase inhibitory activity of phthalic acid derivatives
    • Hiraiwa Y, Morinaka A, Fukushima T, Kudo T. Metallo-beta-lactamase inhibitory activity of phthalic acid derivatives. Bioorg. Med. Chem. Lett. 19(17), 5162-5165 (2009).
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , Issue.17 , pp. 5162-5165
    • Hiraiwa, Y.1    Morinaka, A.2    Fukushima, T.3    Kudo, T.4
  • 53
    • 12844264250 scopus 로고    scopus 로고
    • Novel IMP-1 metallo-beta-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1
    • Moloughney JG, D Thomas J, Toney JH. Novel IMP-1 metallo-beta-lactamase inhibitors can reverse meropenem resistance in Escherichia coli expressing IMP-1. FEMS Microbiol. Lett. 243(1), 65-71 (2005).
    • (2005) FEMS Microbiol. Lett. , vol.243 , Issue.1 , pp. 65-71
    • Moloughney, J.G.1    Thomas, J.D.2    Toney, J.H.3
  • 55
    • 33747348451 scopus 로고    scopus 로고
    • Homo-cysteinyl peptide inhibitors of the L1 metallo-beta-lactamase, and SAR as determined by combinatorial library synthesis
    • Sun Q, Law A, Crowder MW, Geysen HM. Homo-cysteinyl peptide inhibitors of the L1 metallo-beta-lactamase, and SAR as determined by combinatorial library synthesis. Bioorg. Med. Chem. Lett. 16(19), 5169-5175 (2006).
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , Issue.19 , pp. 5169-5175
    • Sun, Q.1    Law, A.2    Crowder, M.W.3    Geysen, H.M.4
  • 57
    • 67650227781 scopus 로고    scopus 로고
    • Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries
    • Minond D, Saldanha SA, Subramaniam P et al. Inhibitors of VIM-2 by screening pharmacologically active and click-chemistry compound libraries. Bioorg. Med. Chem. 17(14), 5027-5037 (2009).
    • (2009) Bioorg. Med. Chem. , vol.17 , Issue.14 , pp. 5027-5037
    • Minond, D.1    Saldanha, S.A.2    Subramaniam, P.3
  • 58
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor
    • Concha NO, Janson CA, Rowling P et al. Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39(15), 4288-4298 (2000).
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3
  • 59
    • 79957618735 scopus 로고    scopus 로고
    • Crystal structure of NDM-1 reveals a common beta-lactam hydrolysis mechanism
    • Zhang H, Hao Q. Crystal structure of NDM-1 reveals a common beta-lactam hydrolysis mechanism. FASEB J. 25(8), 2574-2582 (2011).
    • (2011) FASEB J. , vol.25 , Issue.8 , pp. 2574-2582
    • Zhang, H.1    Hao, Q.2
  • 60
    • 84863976350 scopus 로고    scopus 로고
    • New Delhi metallo-beta-lactamase: Structural insights into beta-lactam recognition and inhibition
    • King DT, Worrall LJ, Gruninger R, Strynadka NC. New Delhi metallo-beta-lactamase: structural insights into beta-lactam recognition and inhibition. J. Am. Chem. Soc. 134(28), 11362-11365 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.28 , pp. 11362-11365
    • King, D.T.1    Worrall, L.J.2    Gruninger, R.3    Strynadka, N.C.4
  • 61
    • 65349195698 scopus 로고    scopus 로고
    • Molecular docking and ligand specificity in fragment-based inhibitor discovery
    • Chen Y, Shoichet BK. Molecular docking and ligand specificity in fragment-based inhibitor discovery. Nat. Chem. Biol. 5(5), 358-364 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , Issue.5 , pp. 358-364
    • Chen, Y.1    Shoichet, B.K.2
  • 62
    • 84863274415 scopus 로고    scopus 로고
    • Structure-based design of potent and ligand-efficient inhibitors of CTX-M Class A beta-lactamase
    • Nichols DA, Jaishankar P, Larson W et al. Structure-based design of potent and ligand-efficient inhibitors of CTX-M Class A beta-lactamase. J. Med. Chem. 55(5), 2163-2172 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.5 , pp. 2163-2172
    • Nichols, D.A.1    Jaishankar, P.2    Larson, W.3
  • 64
    • 79956140677 scopus 로고    scopus 로고
    • The identification of new metallo-beta-lactamase inhibitor leads from fragment-based screening
    • Vella P, Hussein WM, Leung EW et al. The identification of new metallo-beta-lactamase inhibitor leads from fragment-based screening. Bioorg. Med. Chem. Lett. 21(11), 3282-3285 (2011).
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , Issue.11 , pp. 3282-3285
    • Vella, P.1    Hussein, W.M.2    Leung, E.W.3
  • 65
    • 84655167173 scopus 로고    scopus 로고
    • 3-mercapto-1,2,4-triazoles and N-acylated thiosemicarbazides as metallo-beta-lactamase inhibitors
    • Faridoon, Hussein WM, Vella P et al. 3-mercapto-1,2,4-triazoles and N-acylated thiosemicarbazides as metallo-beta-lactamase inhibitors. Bioorg. Med. Chem. Lett. 22(1), 380-386 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , Issue.1 , pp. 380-386
    • Faridoon, W.1    Hussein, W.M.2    Vella, P.3
  • 66
    • 77955982439 scopus 로고    scopus 로고
    • Structural biology in fragment-based drug design
    • Murray CW, Blundell TL. Structural biology in fragment-based drug design. Curr. Opin. Struct. Biol. 20(4), 497-507 (2010).
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , Issue.4 , pp. 497-507
    • Murray, C.W.1    Blundell, T.L.2
  • 67
    • 0037094114 scopus 로고    scopus 로고
    • An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation
    • Minasov G, Wang X, Shoichet BK. An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation. J. Am. Chem. Soc. 124(19), 5333-5340 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , Issue.19 , pp. 5333-5340
    • Minasov, G.1    Wang, X.2    Shoichet, B.K.3
  • 68
    • 34247857459 scopus 로고    scopus 로고
    • The acylation mechanism of CTX-M beta-lactamase at 0.88 Angstrom resolution
    • Chen Y, Bonnet R, Shoichet BK. The acylation mechanism of CTX-M beta-lactamase at 0.88 Angstrom resolution. J. Am. Chem. Soc. 129(17), 5378-5380. (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.17 , pp. 5378-5380
    • Chen, Y.1    Bonnet, R.2    Shoichet, B.K.3
  • 69
    • 0037453313 scopus 로고    scopus 로고
    • Ultrahigh resolution structure of a class A beta-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 beta-lactamase: on the mechanism and specificity of the extended-spectrum SHV-2 enzyme. J. Mol. Biol. 328(1), 289-301 (2003).
    • (2003) J. Mol. Biol. , vol.328 , Issue.1 , pp. 289-301
    • Nukaga, M.1    Mayama, K.2    Hujer, A.M.3    Bonomo, R.A.4    Knox, J.R.5
  • 70
    • 54049149405 scopus 로고    scopus 로고
    • Genetic and structural insights into the dissemination potential of the extremely broad-spectrum class A beta-lactamase KPC-2 identified in an Escherichia coli strain and an Enterobacter cloacae strain isolated from the same patient in France
    • Petrella S, Ziental-Gelus N, Mayer C, Renard M, Jarlier V, Sougakoff W. Genetic and structural insights into the dissemination potential of the extremely broad-spectrum class A beta-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(10), 3725-3736 (2008).
    • (2008) Antimicrob. Agents Chemother. , vol.52 , Issue.10 , pp. 3725-3736
    • Petrella, S.1    Ziental-Gelus, N.2    Mayer, C.3    Renard, M.4    Jarlier, V.5    Sougakoff, W.6
  • 71
    • 33644955487 scopus 로고    scopus 로고
    • The deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution
    • Chen Y, Minasov G, Roth TA, Prati F, Shoichet BK. The deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution. J. Am. Chem. Soc. 128(9), 2970-2976. (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.9 , pp. 2970-2976
    • Chen, Y.1    Minasov, G.2    Roth, T.A.3    Prati, F.4    Shoichet, B.K.5
  • 72
    • 78650717723 scopus 로고    scopus 로고
    • In silico docking and scoring of fragments
    • Chen Y, Pohlhaus DT. In silico docking and scoring of fragments. Drug Discov. Today Technol. 7(3), 149-156 (2010).
    • (2010) Drug Discov. Today Technol. , vol.7 , Issue.3 , pp. 149-156
    • Chen, Y.1    Pohlhaus, D.T.2
  • 73
    • 79952374737 scopus 로고    scopus 로고
    • Using computational techniques in fragment-based drug discovery
    • Desjarlais RL. Using computational techniques in fragment-based drug discovery. Methods Enzymol. 493, 137-155 (2011).
    • (2011) Methods Enzymol. , vol.493 , pp. 137-155
    • Desjarlais, R.L.1
  • 75
    • 79952383501 scopus 로고    scopus 로고
    • From experimental design to validated hits a comprehensive walk-through of fragment lead identification using surface plasmon resonance
    • Giannetti AM. From experimental design to validated hits a comprehensive walk-through of fragment lead identification using surface plasmon resonance. Methods Enzymol. 493, 169-218 (2011).
    • (2011) Methods Enzymol. , vol.493 , pp. 169-218
    • Giannetti, A.M.1
  • 76
    • 79952428086 scopus 로고    scopus 로고
    • Practical aspects of NMR-based fragment screening
    • Lepre CA. Practical aspects of NMR-based fragment screening. Methods Enzymol. 493, 219-239 (2011).
    • (2011) Methods Enzymol. , vol.493 , pp. 219-239
    • Lepre, C.A.1
  • 77
    • 13844312649 scopus 로고    scopus 로고
    • ZINC -A free database of commercially available compounds for virtual screening
    • Irwin JJ, Shoichet BK. ZINC -a free database of commercially available compounds for virtual screening. J. Chem. Inf. Model. 45(1), 177-182. (2005).
    • (2005) J. Chem. Inf. Model. , vol.45 , Issue.1 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 78
    • 84879067434 scopus 로고    scopus 로고
    • Metallo-beta-lactamase: Inhibitors and reporter substrates
    • Fast W, Sutton LD. Metallo-beta-lactamase: inhibitors and reporter substrates. Biochim. Biophys. Acta 1834(8), 1648-1659 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1834 , Issue.8 , pp. 1648-1659
    • Fast, W.1    Sutton, L.D.2
  • 79
    • 84884245033 scopus 로고    scopus 로고
    • Assay platform for clinically relevant metallo-beta-lactamases
    • Van Berkel SS, Brem J, Rydzik AM et al. Assay platform for clinically relevant metallo-beta-lactamases. J. Med. Chem. 56(17), 6945-6953 (2013).
    • (2013) J. Med. Chem. , vol.56 , Issue.17 , pp. 6945-6953
    • Van Berkel, S.S.1    Brem, J.2    Rydzik, A.M.3
  • 80
    • 84986432941 scopus 로고
    • Automated docking with grid-based energy evaluation
    • Meng E, Shoichet Bk, Kuntz ID. Automated docking with grid-based energy evaluation. J. Comput. Chem. 13, 505-524 (1992).
    • (1992) J. Comput. Chem. , vol.13 , pp. 505-524
    • Meng, E.1    Bk, S.2    Kuntz, I.D.3
  • 81
    • 0036108486 scopus 로고    scopus 로고
    • Protein-protein docking with multiple ligand residue conformations and multiple residue identities
    • Lorber DM, Udo MK, Shoichet BK. Protein-protein docking with multiple ligand residue conformations and multiple residue identities. Protein Sci. 11, 1393-1408 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 1393-1408
    • Lorber, D.M.1    Udo, M.K.2    Shoichet, B.K.3
  • 82
    • 59649115459 scopus 로고    scopus 로고
    • AmpC beta-lactamases
    • Jacoby GA. AmpC beta-lactamases. Clin. Microbiol. Rev. 22(1), 161-182, (2009).
    • (2009) Clin. Microbiol. Rev. , vol.22 , Issue.1 , pp. 161-182
    • Jacoby, G.A.1
  • 83
    • 4644359239 scopus 로고    scopus 로고
    • Epidemiology and clinical features of bloodstream infections caused by AmpC-type-beta-lactamase-producing Klebsiella pneumoniae
    • Pai H, Kang CI, Byeon JH et al. Epidemiology and clinical features of bloodstream infections caused by AmpC-type-beta-lactamase-producing Klebsiella pneumoniae. Antimicrob. Agents Chemother. 48(10), 3720-3728 (2004).
    • (2004) Antimicrob. Agents Chemother. , vol.48 , Issue.10 , pp. 3720-3728
    • Pai, H.1    Kang, C.I.2    Byeon, J.H.3
  • 84
    • 0035113737 scopus 로고    scopus 로고
    • Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases
    • Caselli E, Powers RA, Blasczcak LC, Wu CY, Prati F, Shoichet BK. Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases. Chem. Biol. 8(1), 17-31. (2001).
    • (2001) Chem. Biol. , vol.8 , Issue.1 , pp. 17-31
    • Caselli, E.1    Powers, R.A.2    Blasczcak, L.C.3    Wu, C.Y.4    Prati, F.5    Shoichet, B.K.6
  • 85
    • 0035822659 scopus 로고    scopus 로고
    • Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-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 beta-lactamase: implications for resistance mutations and inhibitor design. Biochemistry 40(31), 9207-9214. (2001).
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9207-9214
    • Powers, R.A.1    Caselli, E.2    Focia, P.J.3    Prati, F.4    Shoichet, B.K.5
  • 86
    • 0037460187 scopus 로고    scopus 로고
    • Nanomolar inhibitors of AmpC beta-lactamase
    • Morandi F, Caselli E, Morandi S et al. Nanomolar inhibitors of AmpC beta-lactamase. J. Am. Chem. Soc. 125(3), 685-695 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.3 , pp. 685-695
    • Morandi, F.1    Caselli, E.2    Morandi, S.3
  • 87
    • 38849163614 scopus 로고    scopus 로고
    • Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors
    • Morandi S, Morandi F, Caselli E, Shoichet BK, Prati F. Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors. Bioorg. Med. Chem. 16(3), 1195-1205 (2008).
    • (2008) Bioorg. Med. Chem. , vol.16 , Issue.3 , pp. 1195-1205
    • Morandi, S.1    Morandi, F.2    Caselli, E.3    Shoichet, B.K.4    Prati, F.5
  • 88
    • 33751076241 scopus 로고    scopus 로고
    • Deconstructing fragment-based inhibitor discovery
    • Babaoglu K, Shoichet BK. Deconstructing fragment-based inhibitor discovery. Nat. Chem. Biol. 2(12), 720-723 (2006).
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.12 , pp. 720-723
    • Babaoglu, K.1    Shoichet, B.K.2
  • 89
    • 84888615316 scopus 로고    scopus 로고
    • Class D beta-lactamases: A reappraisal after five decades
    • Leonard DA, Bonomo RA, Powers RA. Class D beta-lactamases: a reappraisal after five decades. Acc. Chem. Res. 46(11), 2407-2415 (2013).
    • (2013) Acc. Chem. Res. , vol.46 , Issue.11 , pp. 2407-2415
    • Leonard, D.A.1    Bonomo, R.A.2    Powers, R.A.3
  • 90
    • 66749100727 scopus 로고    scopus 로고
    • Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D beta-lactamase) by screening amino analogs and homologs of citrate and isocitrate
    • Beck J, Vercheval L, Bebrone C, Herteg-Fernea A, Lassaux P, Marchand-Brynaert J. Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D beta-lactamase) by screening amino analogs and homologs of citrate and isocitrate. Bioorg. Med. Chem. Lett. 19(13), 3593-3597 (2009).
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , Issue.13 , pp. 3593-3597
    • Beck, J.1    Vercheval, L.2    Bebrone, C.3    Herteg-Fernea, A.4    Lassaux, P.5    Marchand-Brynaert, J.6
  • 91
    • 77951249585 scopus 로고    scopus 로고
    • Crystal structure of the narrow-spectrum OXA-46 class D beta-lactamase: Relationship between active-site lysine carbamylation and inhibition by polycarboxylates
    • Docquier JD, Benvenuti M, Calderone V et al. Crystal structure of the narrow-spectrum OXA-46 class D beta-lactamase: relationship between active-site lysine carbamylation and inhibition by polycarboxylates. Antimicrob. Agents Chemother. 54(5), 2167-2174 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.5 , pp. 2167-2174
    • Docquier, J.D.1    Benvenuti, M.2    Calderone, V.3
  • 92
    • 44949106232 scopus 로고    scopus 로고
    • 2-aminopropane-1,2,3-tricarboxylic acid: Synthesis and co-crystallization with the class A beta-lactamase BS3 of Bacillus licheniformis
    • Beck J, Sauvage E, Charlier P, Marchand-Brynaert J. 2-aminopropane-1,2,3- tricarboxylic acid: synthesis and co-crystallization with the class A beta-lactamase BS3 of Bacillus licheniformis. Bioorg. Med. Chem. Lett. 18(13), 3764-3768 (2008).
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.13 , pp. 3764-3768
    • Beck, J.1    Sauvage, E.2    Charlier, P.3    Marchand-Brynaert, J.4
  • 93
    • 84872871981 scopus 로고    scopus 로고
    • Metallo-beta-lactamase structure and function
    • Palzkill T. Metallo-beta-lactamase structure and function. Ann. NY Acad. Sci. 1277, 91-104 (2013).
    • (2013) Ann. NY Acad. Sci. , vol.1277 , pp. 91-104
    • Palzkill, T.1
  • 94
    • 84893391938 scopus 로고    scopus 로고
    • Targeting metallo-beta-lactamase enzymes in antibiotic resistance
    • King DT, Strynadka NC. Targeting metallo-beta-lactamase enzymes in antibiotic resistance. Future Med. Chem. 5(11), 1243-1263 (2013).
    • (2013) Future Med. Chem. , vol.5 , Issue.11 , pp. 1243-1263
    • King, D.T.1    Strynadka, N.C.2
  • 95
    • 24944529911 scopus 로고    scopus 로고
    • Virtual screening against metalloenzymes for inhibitors and substrates
    • Irwin JJ, Raushel FM, Shoichet BK. Virtual screening against metalloenzymes for inhibitors and substrates. Biochemistry 44(37), 12316-12328 (2005).
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12316-12328
    • Irwin, J.J.1    Raushel, F.M.2    Shoichet, B.K.3
  • 96
    • 84872032680 scopus 로고    scopus 로고
    • Structural insights into the subclass B3 metallo-beta-lactamase SMB-1 and the mode of inhibition by the common metallo-beta-lactamase inhibitor mercaptoacetate
    • Wachino J, Yamaguchi Y, Mori S, Kurosaki H, Arakawa Y, Shibayama K. Structural insights into the subclass B3 metallo-beta-lactamase SMB-1 and the mode of inhibition by the common metallo-beta-lactamase inhibitor mercaptoacetate. Antimicrob. Agents Chemother. 57(1), 101-109 (2013).
    • (2013) Antimicrob. Agents Chemother. , vol.57 , Issue.1 , pp. 101-109
    • Wachino, J.1    Yamaguchi, Y.2    Mori, S.3    Kurosaki, H.4    Arakawa, Y.5    Shibayama, K.6
  • 97
    • 0037592222 scopus 로고    scopus 로고
    • The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, d-captopril
    • Garcia-Saez I, Hopkins J, Papamicael C et al. The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, d-captopril. J. Biol. Chem. 278(26), 23868-23873 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.26 , pp. 23868-23873
    • Garcia-Saez, I.1    Hopkins, J.2    Papamicael, C.3
  • 98
    • 0035976960 scopus 로고    scopus 로고
    • Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: Kinetic and spectroscopic studies
    • Mollard C, Moali C, Papamicael C et al. Thiomandelic acid, a broad spectrum inhibitor of zinc beta-lactamases: kinetic and spectroscopic studies. J. Biol. Chem. 276(48), 45015-45023 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.48 , pp. 45015-45023
    • Mollard, C.1    Moali, C.2    Papamicael, C.3
  • 99
    • 45449088355 scopus 로고    scopus 로고
    • Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols
    • Lienard BM, Garau G, Horsfall L et al. Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols. Org. Biomol. Chem. 6(13), 2282-2294 (2008).
    • (2008) Org. Biomol. Chem. , vol.6 , Issue.13 , pp. 2282-2294
    • Lienard, B.M.1    Garau, G.2    Horsfall, L.3
  • 100
    • 33749030701 scopus 로고    scopus 로고
    • Probing, inhibition, and crystallographic characterization of metallo-beta-lactamase (IMP-1) with fluorescent agents containing dansyl and thiol groups
    • Kurosaki H, Yamaguchi Y, Yasuzawa H, Jin W, Yamagata Y, Arakawa Y. Probing, inhibition, and crystallographic characterization of metallo-beta-lactamase (IMP-1) with fluorescent agents containing dansyl and thiol groups. ChemMedChem 1(9), 969-972 (2006).
    • (2006) ChemMedChem , vol.1 , Issue.9 , pp. 969-972
    • Kurosaki, H.1    Yamaguchi, Y.2    Yasuzawa, H.3    Jin, W.4    Yamagata, Y.5    Arakawa, Y.6
  • 101
    • 84866631880 scopus 로고    scopus 로고
    • Synthesis and kinetic testing of tetrahydropyrimidine-2-thione and pyrrole derivatives as inhibitors of the metallo-beta-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa
    • Hussein WM, Fatahala SS, Mohamed ZM et al. Synthesis and kinetic testing of tetrahydropyrimidine-2-thione and pyrrole derivatives as inhibitors of the metallo-beta-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa. Chem. Biol. Drug Des. 80(4), 500-515 (2012).
    • (2012) Chem. Biol. Drug Des. , vol.80 , Issue.4 , pp. 500-515
    • Hussein, W.M.1    Fatahala, S.S.2    Mohamed, Z.M.3
  • 102
  • 103
    • 77954347954 scopus 로고    scopus 로고
    • Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases
    • Lassaux P, Hamel M, Gulea M et al. Mercaptophosphonate compounds as broad-spectrum inhibitors of the metallo-beta-lactamases. J. Med. Chem. 53(13), 4862-4876 (2010).
    • (2010) J. Med. Chem. , vol.53 , Issue.13 , pp. 4862-4876
    • Lassaux, P.1    Hamel, M.2    Gulea, M.3
  • 104
    • 34250214527 scopus 로고    scopus 로고
    • Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila
    • Horsfall LE, Garau G, Lienard BM et al. Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila. Antimicrob. Agents Chemother. 51(6), 2136-2142 (2007).
    • (2007) Antimicrob. Agents Chemother. , vol.51 , Issue.6 , pp. 2136-2142
    • Horsfall, L.E.1    Garau, G.2    Lienard, B.M.3
  • 105
    • 77956116298 scopus 로고    scopus 로고
    • In vitro potentiation of carbapenems with ME1071, a novel metallo-beta-lactamase inhibitor, against metallo-beta-lactamase-producing Pseudomonas aeruginosa clinical isolates
    • Ishii Y, Eto M, Mano Y, Tateda K, Yamaguchi K. In vitro potentiation of carbapenems with ME1071, a novel metallo-beta-lactamase inhibitor, against metallo-beta-lactamase-producing Pseudomonas aeruginosa clinical isolates. Antimicrob. Agents Chemother. 54(9), 3625-3629 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.9 , pp. 3625-3629
    • Ishii, Y.1    Eto, M.2    Mano, Y.3    Tateda, K.4    Yamaguchi, K.5
  • 107
    • 84864417937 scopus 로고    scopus 로고
    • N-heterocyclic dicarboxylic acids: Broad-spectrum inhibitors of metallo-beta-lactamases with co-antibacterial effect against antibiotic-resistant bacteria
    • Feng L, Yang KW, Zhou LS et al. N-heterocyclic dicarboxylic acids: broad-spectrum inhibitors of metallo-beta-lactamases with co-antibacterial effect against antibiotic-resistant bacteria. Bioorg. Med. Chem. Lett. 22(16), 5185-5189 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , Issue.16 , pp. 5185-5189
    • Feng, L.1    Yang, K.W.2    Zhou, L.S.3
  • 108
    • 0030598201 scopus 로고    scopus 로고
    • Trifluoromethyl alcohol and ketone inhibitors of metallo-beta-lactamases
    • Walter MW, Felici A, Galleni M et al. Trifluoromethyl alcohol and ketone inhibitors of metallo-beta-lactamases. Bioorg. Med. Chem. Lett. 6, 2455-2458 (1996).
    • (1996) Bioorg. Med. Chem. Lett. , vol.6 , pp. 2455-2458
    • Walter, M.W.1    Felici, A.2    Galleni, M.3
  • 110
    • 77957342399 scopus 로고    scopus 로고
    • High-resolution crystal structure of the subclass B3 metallo-beta- lactamase BJP-1: Rational basis for substrate specificity and interaction with sulfonamides
    • Docquier JD, Benvenuti M, Calderone V et al. High-resolution crystal structure of the subclass B3 metallo-beta-lactamase BJP-1: rational basis for substrate specificity and interaction with sulfonamides. Antimicrob. Agents Chemother. 54(10), 4343-4351 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.10 , pp. 4343-4351
    • Docquier, J.D.1    Benvenuti, M.2    Calderone, V.3
  • 111
    • 0032510815 scopus 로고    scopus 로고
    • Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): A crystallographic study at 1.85-A resolution
    • Fitzgerald PM, Wu JK, Toney JH. Unanticipated inhibition of the metallo-beta-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): a crystallographic study at 1.85-A resolution. Biochemistry 37(19), 6791-6800 (1998).
    • (1998) Biochemistry , vol.37 , Issue.19 , pp. 6791-6800
    • Fitzgerald, P.M.1    Wu, J.K.2    Toney, J.H.3
  • 112
    • 84866426322 scopus 로고    scopus 로고
    • 2-substituted 4,5-dihydrothiazole-4-carboxylic acids are novel inhibitors of metallo-beta-lactamases
    • Chen P, Horton LB, Mikulski RL et al. 2-substituted 4,5-dihydrothiazole- 4-carboxylic acids are novel inhibitors of metallo-beta-lactamases. Bioorg. Med. Chem. Lett. 22(19), 6229-6232 (2012).
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , Issue.19 , pp. 6229-6232
    • Chen, P.1    Horton, L.B.2    Mikulski, R.L.3
  • 113
    • 0032842513 scopus 로고    scopus 로고
    • Inhibition of IMP-1 metallo-beta-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives
    • Hammond GG, Huber JL, Greenlee ML et al. Inhibition of IMP-1 metallo-beta-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives. FEMS Microbiol. Lett. 179(2), 289-296 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.179 , Issue.2 , pp. 289-296
    • Hammond, G.G.1    Huber, J.L.2    Greenlee, M.L.3
  • 114
    • 0037462925 scopus 로고    scopus 로고
    • Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with d-captopril
    • Garcia-Saez I, Mercuri PS, Papamicael C et al. Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with d-captopril. J. Mol. Biol. 325(4), 651-660 (2003).
    • (2003) J. Mol. Biol. , vol.325 , Issue.4 , pp. 651-660
    • Garcia-Saez, I.1    Mercuri, P.S.2    Papamicael, C.3
  • 115
    • 0038419647 scopus 로고    scopus 로고
    • Coordination geometries of metal ions in d-or l-captopril-inhibited metallo-beta-lactamases
    • Heinz U, Bauer R, Wommer S et al. Coordination geometries of metal ions in d-or l-captopril-inhibited metallo-beta-lactamases. J. Biol. Chem. 278(23), 20659-20666 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.23 , pp. 20659-20666
    • Heinz, U.1    Bauer, R.2    Wommer, S.3


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