메뉴 건너뛰기




Volumn 17, Issue 9, 2016, Pages 983-1005

Decoding the Structural Basis For Carbapenem Hydrolysis By Class A β-lactamases: Fishing For A Pharmacophore

Author keywords

Carbapenemases; Guyana extended spectrum lactamase (GES); Klebsiella pneumoniae carbapenemase (KPC); Molecular interaction fields (MIFs); Nonmetallo carbapanemase (NMC); Pharmacophore prediction; Serratia fonticola (SFC1); Serratia marcescens (SME)

Indexed keywords

3 NITROPHENYL BORONIC ACID; AMOXICILLIN; AMPICILLIN; AZTREONAM; BETA LACTAMASE; CARBAPENEM; CARBAPENEMASE; CEFOTAXIME; CEFOXITIN; CEFTAZIDIME; CEPHALOSPORIN; CITRIC ACID; CLAVULANIC ACID; DORIPENEM; ERTAPENEM; EXTENDED SPECTRUM BETA LACTAMASE; FOSFOMYCIN; IMIPENEM; MEROPENEM; PENICILLIN DERIVATIVE; PROTEIN GES 5; PROTEIN KPC 2; PROTEIN NMC A; PROTEIN SFC 1; PROTEIN TEM1; SULBACTAM; TAZOBACTAM; TICARCILLIN; TIGECYCLINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARBAPENEM DERIVATIVE;

EID: 84973664420     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/1389450116666151001104448     Document Type: Article
Times cited : (27)

References (136)
  • 1
    • 39049128343 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamaseproducing Enterobacteriaceae: An emerging public-health concern
    • Pitout JD, Laupland KB. Extended-spectrum β-lactamaseproducing Enterobacteriaceae: an emerging public-health concern. Lancet Infect Dis 2008; 8: 159-66.
    • (2008) Lancet Infect Dis , vol.8 , pp. 159-166
    • Pitout, J.D.1    Laupland, K.B.2
  • 2
    • 55249101755 scopus 로고    scopus 로고
    • Multiresistant Enterobacteriaceae: New threat of an old problem
    • Pitout JD. Multiresistant Enterobacteriaceae: new threat of an old problem. Expert Rev Anti Infect Ther 2008; 6: 657-69.
    • (2008) Expert Rev Anti Infect Ther , vol.6 , pp. 657-669
    • Pitout, J.D.1
  • 3
    • 33747795961 scopus 로고    scopus 로고
    • What's new in antibiotic resistance? Focus on F-lactamases
    • Babic M, Hujer AM, Bonomo RA. What's new in antibiotic resistance? Focus on F-lactamases. Drug Resist Updat 2006; 9: 142-56.
    • (2006) Drug Resist Updat , vol.9 , pp. 142-156
    • Babic, M.1    Hujer, A.M.2    Bonomo, R.A.3
  • 5
    • 38849186031 scopus 로고    scopus 로고
    • The current state of multidrugresistant gram-negative bacilli in North America
    • Nicasio AM, Kuti JL, Nicolau DP. The current state of multidrugresistant gram-negative bacilli in North America. Pharmacotherapy 2008; 28: 235-49.
    • (2008) Pharmacotherapy , vol.28 , pp. 235-249
    • Nicasio, A.M.1    Kuti, J.L.2    Nicolau, D.P.3
  • 6
    • 35348821803 scopus 로고    scopus 로고
    • A step closer to extreme drug resistance (XDR) in gram-negative bacilli
    • Paterson DL, Doi Y. A step closer to extreme drug resistance (XDR) in gram-negative bacilli. Clin Infect Dis 2007; 45: 1179-81.
    • (2007) Clin Infect Dis , vol.45 , pp. 1179-1181
    • Paterson, D.L.1    Doi, Y.2
  • 7
    • 84875923394 scopus 로고    scopus 로고
    • "Stormy waters ahead": Global emergence of carbapenemases
    • Patel G, Bonomo RA. "Stormy waters ahead": global emergence of carbapenemases. Front Microbiol 2013; 4: 48.
    • (2013) Front Microbiol , vol.4 , pp. 48
    • Patel, G.1    Bonomo, R.A.2
  • 8
    • 0036008512 scopus 로고    scopus 로고
    • Structure of the imipenem-hydrolyzing class A i-lactamase SME-1 from Serratia marcescens
    • Sougakoff W, L'Hermite G, Pernot L, et al. Structure of the imipenem-hydrolyzing class A i-lactamase SME-1 from Serratia marcescens. Acta Crystallogr D Biol Crystallogr 2002; 58: 267-74.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 267-274
    • Sougakoff, W.1    L'Hermite, G.2    Pernot, L.3
  • 9
    • 84860516573 scopus 로고    scopus 로고
    • Carbapenem resistance in Enterobacteriaceae: Here is the storm!
    • Nordmann P, Dortet L, Poirel L. Carbapenem resistance in Enterobacteriaceae: here is the storm! Trends Mol Med 2012; 18: 263-72.
    • (2012) Trends Mol Med , vol.18 , pp. 263-272
    • Nordmann, P.1    Dortet, L.2    Poirel, L.3
  • 10
    • 15944426814 scopus 로고    scopus 로고
    • Regulation and biosynthesis of carbapenem antibiotics in bacteria
    • Coulthurst SJ, Barnard AM. Salmond GP. Regulation and biosynthesis of carbapenem antibiotics in bacteria. Nat Rev Microbiol 2005; 3: 295-306.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 295-306
    • Coulthurst, S.J.1    Barnard, A.M.2    Salmond, G.P.3
  • 11
    • 78649946454 scopus 로고    scopus 로고
    • Current status of carbapenem antibiotics
    • El-Gamal MI, Oh CH. Current status of carbapenem antibiotics. Curr Top Med Chem 2010; 10: 1882-97.
    • (2010) Curr Top Med Chem , vol.10 , pp. 1882-1897
    • El-Gamal, M.I.1    Oh, C.H.2
  • 12
    • 39049121612 scopus 로고    scopus 로고
    • Carbapenems: A potent class of antibiotics
    • Nicolau DP. Carbapenems: a potent class of antibiotics. Expert Opin Pharmacother 2008; 9: 23-37.
    • (2008) Expert Opin Pharmacother , vol.9 , pp. 23-37
    • Nicolau, D.P.1
  • 16
    • 84895782393 scopus 로고    scopus 로고
    • Challenges in the management of infections due to carbapenem-resistant Enterobacteriaceae
    • Drekonja DM, Beekmann SE, Elliott S, et al. Challenges in the management of infections due to carbapenem-resistant Enterobacteriaceae. Infect Control Hosp Epidemiol 2014; 35: 437-9.
    • (2014) Infect Control Hosp Epidemiol , vol.35 , pp. 437-439
    • Drekonja, D.M.1    Beekmann, S.E.2    Elliott, S.3
  • 17
    • 34547422759 scopus 로고    scopus 로고
    • Carbapenemases: The versatile β-lactamases
    • Queenan AM, Bush K. Carbapenemases: the versatile β-lactamases. Clin Microbiol Rev 2007; 20: 440-58.
    • (2007) Clin Microbiol Rev , vol.20 , pp. 440-458
    • Queenan, A.M.1    Bush, K.2
  • 18
    • 33747179934 scopus 로고    scopus 로고
    • The o-lactamase threat in Enterobacteriaceae, Pseudomonas and Acinetobacter
    • Livermore DM, Woodford N. The o-lactamase threat in Enterobacteriaceae, Pseudomonas and Acinetobacter. Trends Microbiol 2006; 14: 413-20.
    • (2006) Trends Microbiol , vol.14 , pp. 413-420
    • Livermore, D.M.1    Woodford, N.2
  • 19
    • 33745234828 scopus 로고    scopus 로고
    • Resistance in gram-negative bacteria: Enterobacteriaceae
    • discussion S64-73
    • Paterson DL. Resistance in gram-negative bacteria: Enterobacteriaceae. Am J Infect Control 2006; 34: S20-8; discussion S64-73.
    • (2006) Am J Infect Control , vol.34 , pp. S20-S28
    • Paterson, D.L.1
  • 20
    • 77149165713 scopus 로고    scopus 로고
    • Updated functional classification of β-lactamases
    • Bush K, Jacoby GA. Updated functional classification of β-lactamases. Antimicrob Agents Chemother 2010; 54: 969-76.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 969-976
    • Bush, K.1    Jacoby, G.A.2
  • 21
    • 84896724608 scopus 로고    scopus 로고
    • Carbapenemase-producing Enterobacteriaceae: Overview of a major public health challenge
    • Nordmann P. Carbapenemase-producing Enterobacteriaceae: overview of a major public health challenge. Med Mal Infect 2013; 44: 51-6.
    • (2013) Med Mal Infect , vol.44 , pp. 51-56
    • Nordmann, P.1
  • 22
    • 80052227440 scopus 로고    scopus 로고
    • Revisiting "older" antimicrobials in the era of multidrug resistance
    • Pogue JM, Marchaim D, Kaye D, Kaye KS. Revisiting "older" antimicrobials in the era of multidrug resistance. Pharmacotherapy 2011; 31: 912-21.
    • (2011) Pharmacotherapy , vol.31 , pp. 912-921
    • Pogue, J.M.1    Marchaim, D.2    Kaye, D.3    Kaye, K.S.4
  • 23
    • 84858278979 scopus 로고    scopus 로고
    • Fourteen years in resistance
    • Livermore DM. Fourteen years in resistance. Int J Antimicrob Agents 2012; 39: 283-94.
    • (2012) Int J Antimicrob Agents , vol.39 , pp. 283-294
    • Livermore, D.M.1
  • 24
    • 84878278251 scopus 로고    scopus 로고
    • For the Infectious Diseases Society of America 10 Ã- '20 Progress-development of new drugs active against gram-negative bacilli: An update from the infectious diseases society of america
    • Boucher HW, Talbot GH, Benjamin DK, et al. for the Infectious Diseases Society of America 10 Ã- '20 Progress-development of new drugs active against gram-negative bacilli: An update from the infectious diseases society of america. Clin Infect Dis 2013; 56: 1685-94.
    • (2013) Clin Infect Dis , vol.56 , pp. 1685-1694
    • Boucher, H.W.1    Talbot, G.H.2    Benjamin, D.K.3
  • 26
    • 0025870126 scopus 로고
    • A standard numbering scheme for the class A s-lactamases
    • Ambler RP, Coulson AF, Frere JM, et al. A standard numbering scheme for the class A s-lactamases. Biochem J 1991; 276 (Pt 1): 269-70.
    • (1991) Biochem J , vol.276 , pp. 269-270
    • Ambler, R.P.1    Coulson, A.F.2    Frere, J.M.3
  • 29
    • 78649697323 scopus 로고    scopus 로고
    • Emerging carbapenemases: A global perspective
    • Walsh TR. Emerging carbapenemases: a global perspective. Int J Antimicrob Agents 2010; 36 (Suppl 3): S8-14.
    • (2010) Int J Antimicrob Agents , vol.36 , pp. S8-S14
    • Walsh, T.R.1
  • 30
    • 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 2011; 9: 555-70.
    • (2011) Expert Rev Anti Infect Ther , vol.9 , pp. 555-570
    • Patel, G.1    Bonomo, R.A.2
  • 32
    • 84930486688 scopus 로고    scopus 로고
    • Global spread of Carbapenemaseproducing Enterobacteriaceae
    • Nordmann P, Naas T, Poirel L. Global spread of Carbapenemaseproducing Enterobacteriaceae. Emerg Infect Dis 2011; 17: 1791-8.
    • (2011) Emerg Infect Dis , vol.17 , pp. 1791-1798
    • Nordmann, P.1    Naas, T.2    Poirel, L.3
  • 33
    • 0018143694 scopus 로고
    • CP-45, 899, a 8-lactamase inhibitor that extends the antibacterial spectrum of o-lactams: Initial bacteriological characterization
    • English AR, Retsema JA, Girard AE, Lynch JE, Barth WE. CP-45, 899, a 8-lactamase inhibitor that extends the antibacterial spectrum of o-lactams: initial bacteriological characterization. Antimicrob Agents Chemother 1978; 14: 414-9.
    • (1978) Antimicrob Agents Chemother , vol.14 , pp. 414-419
    • English, A.R.1    Retsema, J.A.2    Girard, A.E.3    Lynch, J.E.4    Barth, W.E.5
  • 34
    • 79954599167 scopus 로고    scopus 로고
    • Identification of products of inhibition of GES-2 S- lactamase by tazobactam by x-ray crystallography and spectrometry
    • Frase H, Smith CA, Toth M, Champion MM, Mobashery S, Vakulenko SB. Identification of products of inhibition of GES-2 S- lactamase by tazobactam by x-ray crystallography and spectrometry. J Biol Chem 2011; 286: 14396-409.
    • (2011) J Biol Chem , vol.286 , pp. 14396-14409
    • Frase, H.1    Smith, C.A.2    Toth, M.3    Champion, M.M.4    Mobashery, S.5    Vakulenko, S.B.6
  • 36
    • 15444338960 scopus 로고    scopus 로고
    • X-ray analysis of the NMC-A N-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity
    • Swaren P, Maveyraud L, Raquet X, et al. X-ray analysis of the NMC-A N-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity. J Biol Chem 1998; 273: 26714-21.
    • (1998) J Biol Chem , vol.273 , pp. 26714-26721
    • Swaren, P.1    Maveyraud, L.2    Raquet, X.3
  • 37
    • 0028031303 scopus 로고
    • Analysis of a carbapenem-hydrolyzing class A A-lactamase from Enterobacter cloacae and of its LysR-type regulatory protein
    • Naas T, Nordmann P. Analysis of a carbapenem-hydrolyzing class A A-lactamase from Enterobacter cloacae and of its LysR-type regulatory protein. Proc Natl Acad Sci USA 1994; 91: 7693-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7693-7697
    • Naas, T.1    Nordmann, P.2
  • 39
    • 84872871981 scopus 로고    scopus 로고
    • Metallo-β-lactamase structure and function
    • Palzkill T. Metallo-β-lactamase structure and function. Ann NY Acad Sci 2013; 1277: 91-104.
    • (2013) Ann NY Acad Sci , vol.1277 , pp. 91-104
    • Palzkill, T.1
  • 40
    • 77957165689 scopus 로고    scopus 로고
    • Design, synthesis, and crystal structures of 6-alkylidene-2'-substituted penicillanic acid sulfones as potent inhibitors of Acinetobacter baumannii OXA-24 carbapenemase
    • Bou G, Santillana E, Sheri A, et al. Design, synthesis, and crystal structures of 6-alkylidene-2'-substituted penicillanic acid sulfones as potent inhibitors of Acinetobacter baumannii OXA-24 carbapenemase. J Am Chem Soc 2010; 132: 13320-31.
    • (2010) J Am Chem Soc , vol.132 , pp. 13320-13331
    • Bou, G.1    Santillana, E.2    Sheri, A.3
  • 41
  • 42
    • 65749120570 scopus 로고    scopus 로고
    • Crystal structure of the OXA-48 t-lactamase reveals mechanistic diversity among class D carbapenemases
    • Docquier JD, Calderone V, De Luca F, et al. Crystal structure of the OXA-48 t-lactamase reveals mechanistic diversity among class D carbapenemases. Chem Biol 2009; 16: 540-7.
    • (2009) Chem Biol , vol.16 , pp. 540-547
    • Docquier, J.D.1    Calderone, V.2    De Luca, F.3
  • 43
    • 34248326126 scopus 로고    scopus 로고
    • Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis
    • Santillana E, Beceiro A, Bou G, Romero A. Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis. Proc Natl Acad Sci USA 2007; 104: 5354- 9.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5354-5359
    • Santillana, E.1    Beceiro, A.2    Bou, G.3    Romero, A.4
  • 45
    • 0032226545 scopus 로고    scopus 로고
    • How. -lactamases have driven pharmaceutical drug discovery. From mechanistic knowledge to clinical circumvention
    • Bush K, Mobashery S. How. -lactamases have driven pharmaceutical drug discovery. From mechanistic knowledge to clinical circumvention. Adv Exp Med Biol 1998; 456: 71-98.
    • (1998) Adv Exp Med Biol , vol.456 , pp. 71-98
    • Bush, K.1    Mobashery, S.2
  • 46
    • 0032032930 scopus 로고    scopus 로고
    • Catalytic properties of class A c-lactamases: Efficiency and diversity
    • Matagne A, Lamotte-Brasseur J, Frere JM. Catalytic properties of class A c-lactamases: efficiency and diversity. Biochem J 1998; 330 (Pt 2): 581-98.
    • (1998) Biochem J , vol.330 , pp. 581-598
    • Matagne, A.1    Lamotte-Brasseur, J.2    Frere, J.M.3
  • 47
    • 0024557806 scopus 로고
    • Isolation of a Staphylococcus aureus β-lactamase-dicloxacillin complex and kinetic studies on the reactivation of the enzyme
    • Hardy LW, Kirsch JF. Isolation of a Staphylococcus aureus β-lactamase-dicloxacillin complex and kinetic studies on the reactivation of the enzyme. Arch Biochem Biophys 1989; 268: 338-48.
    • (1989) Arch Biochem Biophys , vol.268 , pp. 338-348
    • Hardy, L.W.1    Kirsch, J.F.2
  • 48
    • 55849091037 scopus 로고    scopus 로고
    • Carbapenems and SHV-1 β-lactamase form different acyl-enzyme populations in crystals and solution
    • Kalp M, Carey PR. Carbapenems and SHV-1 β-lactamase form different acyl-enzyme populations in crystals and solution. Biochemistry 2008; 47: 11830-7.
    • (2008) Biochemistry , vol.47 , pp. 11830-11837
    • Kalp, M.1    Carey, P.R.2
  • 49
    • 0032562183 scopus 로고    scopus 로고
    • Crystal structure of an acylation transition-state analog of the TEM-1 a-lactamase. Mechanistic implications for class A i-lactamases
    • Maveyraud L, Pratt RF, Samama JP. Crystal structure of an acylation transition-state analog of the TEM-1 a-lactamase. Mechanistic implications for class A i-lactamases. Biochemistry 1998; 37: 2622-8.
    • (1998) Biochemistry , vol.37 , pp. 2622-2628
    • Maveyraud, L.1    Pratt, R.F.2    Samama, J.P.3
  • 50
    • 52449111304 scopus 로고    scopus 로고
    • Inhibition of class A I- lactamases by carbapenems: Crystallographic observation of two conformations of meropenem in SHV-1
    • Nukaga M, Bethel CR, Thomson JM, et al. Inhibition of class A I- lactamases by carbapenems: crystallographic observation of two conformations of meropenem in SHV-1. J Am Chem Soc 2008; 130: 12656-62.
    • (2008) J Am Chem Soc , vol.130 , pp. 12656-12662
    • Nukaga, M.1    Bethel, C.R.2    Thomson, J.M.3
  • 51
    • 0027193696 scopus 로고
    • Biochemical properties of a carbapenem-hydrolyzing p-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli
    • Nordmann P, Mariotte S, Naas T, Labia R, Nicolas MH. Biochemical properties of a carbapenem-hydrolyzing p-lactamase from Enterobacter cloacae and cloning of the gene into Escherichia coli. Antimicrob Agents Chemother 1993; 37: 939-46.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 939-946
    • Nordmann, P.1    Mariotte, S.2    Naas, T.3    Labia, R.4    Nicolas, M.H.5
  • 52
    • 0029069435 scopus 로고
    • Interactions of biapenem with active-site serine and metallo-a-lactamases
    • Felici A, Perilli M, Segatore B, et al. Interactions of biapenem with active-site serine and metallo-a-lactamases. Antimicrob Agents Chemother 1995; 39: 1300-5.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1300-1305
    • Felici, A.1    Perilli, M.2    Segatore, B.3
  • 53
    • 0032246850 scopus 로고    scopus 로고
    • Enzymatic resistance to imipenem in gramnegative bacilli: NMC-A, an original carbapenemase
    • Boyer-Mariotte S. Enzymatic resistance to imipenem in gramnegative bacilli: NMC-A, an original carbapenemase. Ann Pharm Fr 1998; 56: 244-9.
    • (1998) Ann Pharm Fr , vol.56 , pp. 244-249
    • Boyer-Mariotte, S.1
  • 54
    • 0031036293 scopus 로고    scopus 로고
    • A disulfide bridge near the active site of carbapenem-hydrolyzing class A b- lactamases might explain their unusual substrate profile
    • Raquet X, Lamotte-Brasseur J, Bouillenne F, Frere JM. A disulfide bridge near the active site of carbapenem-hydrolyzing class A b- lactamases might explain their unusual substrate profile. Proteins 1997; 27: 47-58.
    • (1997) Proteins , vol.27 , pp. 47-58
    • Raquet, X.1    Lamotte-Brasseur, J.2    Bouillenne, F.3    Frere, J.M.4
  • 55
    • 0032502332 scopus 로고    scopus 로고
    • Role of the omega-loop in the activity, substrate specificity, and structure of class A o-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 o-lactamase. Biochemistry 1998; 37: 3286-96.
    • (1998) Biochemistry , vol.37 , pp. 3286-3296
    • Banerjee, S.1    Pieper, U.2    Kapadia, G.3    Pannell, L.K.4    Herzberg, O.5
  • 56
    • 0027408874 scopus 로고
    • Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type i-lactamases probed by site-directed mutagenesis and threedimensional modeling
    • Huletsky A, Knox JR, Levesque RC. Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type i-lactamases probed by site-directed mutagenesis and threedimensional modeling. J Biol Chem 1993; 268: 3690-7.
    • (1993) J Biol Chem , vol.268 , pp. 3690-3697
    • Huletsky, A.1    Knox, J.R.2    Levesque, R.C.3
  • 57
    • 0028170640 scopus 로고
    • TEM F-lactamase mutants hydrolysing third-generation cephalosporins. A kinetic and molecular modelling analysis
    • Raquet X, Lamotte-Brasseur J, Fonze E, Goussard S, Courvalin P, Frere JM. TEM F-lactamase mutants hydrolysing third-generation cephalosporins. A kinetic and molecular modelling analysis. J Mol Biol 1994; 244: 625-39.
    • (1994) J Mol Biol , vol.244 , pp. 625-639
    • Raquet, X.1    Lamotte-Brasseur, J.2    Fonze, E.3    Goussard, S.4    Courvalin, P.5    Frere, J.M.6
  • 58
    • 0029738864 scopus 로고    scopus 로고
    • Crystal Structure of 6α-(Hydroxymethyl) penicillanate Complexed to the TEM-1 β-Lactamase from Escherichia coli: Evidence on the mechanism of action of a novel inhibitor designed by a computer-aided process
    • Maveyraud L, Massova I, Birck C, Miyashita K, Samama JP, Mobashery S. Crystal Structure of 6α-(Hydroxymethyl) penicillanate Complexed to the TEM-1 β-Lactamase from Escherichia coli: Evidence on the mechanism of action of a novel inhibitor designed by a computer-aided process. J Am Chem Soc 1996; 118: 7435-646.
    • (1996) J Am Chem Soc , vol.118 , pp. 7435-7646
    • Maveyraud, L.1    Massova, I.2    Birck, C.3    Miyashita, K.4    Samama, J.P.5    Mobashery, S.6
  • 59
    • 0030020367 scopus 로고    scopus 로고
    • Quantification of the extent of attenuation of the rate of turnover chemistry of the TEM-1 α- lactamase by the α-1R-hydroxyethyl group in substrates
    • Miyashita K, Massova I, Mobashery S. Quantification of the extent of attenuation of the rate of turnover chemistry of the TEM-1 α- lactamase by the α-1R-hydroxyethyl group in substrates. Bioorg Med Chem Lett 1996; 6: 319-322.
    • (1996) Bioorg Med Chem Lett , vol.6 , pp. 319-322
    • Miyashita, K.1    Massova, I.2    Mobashery, S.3
  • 60
    • 0030587499 scopus 로고    scopus 로고
    • A kinetic study of NMC-A o-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins
    • Mariotte-Boyer S, Nicolas-Chanoine MH, Labia R. A kinetic study of NMC-A o-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins. FEMS Microbiol Lett 1996; 143: 29-33.
    • (1996) FEMS Microbiol Lett , vol.143 , pp. 29-33
    • Mariotte-Boyer, S.1    Nicolas-Chanoine, M.H.2    Labia, R.3
  • 61
    • 0032538055 scopus 로고    scopus 로고
    • Inhibition of the NMC-A M-lactamase by a penicillanic acid derivative and the structural bases for the increase in substrate profile of this antibiotic resistance enzyme
    • Mourey L, Miyashita K, Swaren P, Bulychev A, Samama JP, Mobashery S. Inhibition of the NMC-A M-lactamase by a penicillanic acid derivative and the structural bases for the increase in substrate profile of this antibiotic resistance enzyme. J Am Chem Soc 1998; 120: 9382-3.
    • (1998) J Am Chem Soc , vol.120 , pp. 9382-9383
    • Mourey, L.1    Miyashita, K.2    Swaren, P.3    Bulychev, A.4    Samama, J.P.5    Mobashery, S.6
  • 63
    • 84896724608 scopus 로고    scopus 로고
    • Carbapenemase-producing Enterobacteriaceae: Overview of a major public health challenge
    • Nordmann P. Carbapenemase-producing Enterobacteriaceae: overview of a major public health challenge. Med Mal Infect 2014; 44: 51-6.
    • (2014) Med Mal Infect , vol.44 , pp. 51-56
    • Nordmann, P.1
  • 64
    • 0025366291 scopus 로고
    • Biochemical characterization of a a-lactamase that hydrolyzes penems and carbapenems from two Serratia marcescens isolates
    • Yang YJ, Wu PJ, Livermore DM. Biochemical characterization of a a-lactamase that hydrolyzes penems and carbapenems from two Serratia marcescens isolates. Antimicrob Agents Chemother 1990; 34: 755-8.
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 755-758
    • Yang, Y.J.1    Wu, P.J.2    Livermore, D.M.3
  • 65
    • 0033734984 scopus 로고    scopus 로고
    • SME-type carbapenem- hydrolyzing class A h-lactamases from geographically diverse Serratia marcescens strains
    • Queenan AM, Torres-Viera C, Gold HS, et al. SME-type carbapenem- hydrolyzing class A h-lactamases from geographically diverse Serratia marcescens strains. Antimicrob Agents Chemother 2000; 44: 3035-9.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 3035-3039
    • Queenan, A.M.1    Torres-Viera, C.2    Gold, H.S.3
  • 68
    • 33845223883 scopus 로고    scopus 로고
    • Emergence of serine carbapenemases (KPC and SME) among clinical strains of Enterobacteriaceae isolated in the United States Medical Centers: Report from the MYSTIC Program (1999-2005)
    • Deshpande LM, Rhomberg PR, Sader HS, Jones RN. Emergence of serine carbapenemases (KPC and SME) among clinical strains of Enterobacteriaceae isolated in the United States Medical Centers: report from the MYSTIC Program (1999-2005). Diagn Microbiol Infect Dis 2006; 56: 367-72.
    • (2006) Diagn Microbiol Infect Dis , vol.56 , pp. 367-372
    • Deshpande, L.M.1    Rhomberg, P.R.2    Sader, H.S.3    Jones, R.N.4
  • 69
    • 0028897553 scopus 로고
    • Characterization of an LysR family protein, SmeR from Serratia marcescens S6, its effect on expression of the carbapenem-hydrolyzing e-lactamase Sme-1, and comparison of this regulator with other c-lactamase regulators
    • Naas T, Livermore DM, Nordmann P. Characterization of an LysR family protein, SmeR from Serratia marcescens S6, its effect on expression of the carbapenem-hydrolyzing e-lactamase Sme-1, and comparison of this regulator with other c-lactamase regulators. Antimicrob Agents Chemother 1995; 39: 629-37.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 629-637
    • Naas, T.1    Livermore, D.M.2    Nordmann, P.3
  • 70
    • 80053910606 scopus 로고    scopus 로고
    • Detection of 2 SME- 1 carbapenemase-producing Serratia marcescens in Detroit
    • Fairfax MR, Queenan AM, Lephart PR, et al. Detection of 2 SME- 1 carbapenemase-producing Serratia marcescens in Detroit. Diagn Microbiol Infect Dis 2011; 71: 325-6.
    • (2011) Diagn Microbiol Infect Dis , vol.71 , pp. 325-326
    • Fairfax, M.R.1    Queenan, A.M.2    Lephart, P.R.3
  • 71
    • 84861159406 scopus 로고    scopus 로고
    • Carbapenem-resistant Gram-negative bacilli in Canada 2009-10: Results from the Canadian Nosocomial Infection Surveillance Program (CNISP)
    • Mataseje LF, Bryce E, Roscoe D, et al. Carbapenem-resistant Gram-negative bacilli in Canada 2009-10: results from the Canadian Nosocomial Infection Surveillance Program (CNISP). J Antimicrob Chemother 2012; 67: 1359-67.
    • (2012) J Antimicrob Chemother , vol.67 , pp. 1359-1367
    • Mataseje, L.F.1    Bryce, E.2    Roscoe, D.3
  • 73
    • 0033998662 scopus 로고    scopus 로고
    • Biochemical sequence analyses of GES-1, a novel class A extendedspectrum s-lactamase, and the class 1 integron In52 from Klebsiella pneumoniae
    • Poirel L, Le Thomas I, Naas T, Karim A, Nordmann P. Biochemical sequence analyses of GES-1, a novel class A extendedspectrum s-lactamase, and the class 1 integron In52 from Klebsiella pneumoniae. Antimicrob Agents Chemother 2000; 44: 622- 32.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 622-632
    • Poirel, L.1    Le Thomas, I.2    Naas, T.3    Karim, A.4    Nordmann, P.5
  • 75
    • 0026801518 scopus 로고
    • Molecular structure of the acyl-enzyme intermediate in t-lactam hydrolysis at 1.7 A resolution
    • Strynadka NC, Adachi H, Jensen SE, et al. Molecular structure of the acyl-enzyme intermediate in t-lactam hydrolysis at 1.7 A resolution. Nature 1992; 359: 700-5.
    • (1992) Nature , vol.359 , pp. 700-705
    • Strynadka, N.C.1    Adachi, H.2    Jensen, S.E.3
  • 76
    • 0032794732 scopus 로고    scopus 로고
    • Role of ser-237 in the substrate specificity of the carbapenem-hydrolyzing class A c-lactamase Sme-1
    • Sougakoff W, Naas T, Nordmann P, Collatz E, Jarlier V. Role of ser-237 in the substrate specificity of the carbapenem-hydrolyzing class A c-lactamase Sme-1. Biochim Biophys Acta 1999; 1433: 153-8.
    • (1999) Biochim Biophys Acta , vol.1433 , pp. 153-158
    • Sougakoff, W.1    Naas, T.2    Nordmann, P.3    Collatz, E.4    Jarlier, V.5
  • 77
    • 84871658342 scopus 로고    scopus 로고
    • Detection systems for carbapenemase gene identification should include the SME serine carbapenemase
    • Bush K, Pannell M, Lock JL, et al. Detection systems for carbapenemase gene identification should include the SME serine carbapenemase. Int J Antimicrob Agents 2013; 41: 1-4.
    • (2013) Int J Antimicrob Agents , vol.41 , pp. 1-4
    • Bush, K.1    Pannell, M.2    Lock, J.L.3
  • 78
    • 0035084032 scopus 로고    scopus 로고
    • Novel carbapenemhydrolyzing N-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae
    • Yigit H, Queenan AM, Anderson GJ, et al. Novel carbapenemhydrolyzing N-lactamase, KPC-1, from a carbapenem-resistant strain of Klebsiella pneumoniae. Antimicrob Agents Chemother 2001; 45: 1151-61.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1151-1161
    • Yigit, H.1    Queenan, A.M.2    Anderson, G.J.3
  • 81
    • 33845210947 scopus 로고    scopus 로고
    • Occurrence and characterization of carbapenemase-producing Enterobacteriaceae: Report from the SENTRY Antimicrobial Surveillance Program (2000-2004)
    • Deshpande LM, Jones RN, Fritsche TR, Sader HS. Occurrence and characterization of carbapenemase-producing Enterobacteriaceae: report from the SENTRY Antimicrobial Surveillance Program (2000-2004). Microb Drug Resist 2006; 12: 223-30.
    • (2006) Microb Drug Resist , vol.12 , pp. 223-230
    • Deshpande, L.M.1    Jones, R.N.2    Fritsche, T.R.3    Sader, H.S.4
  • 82
    • 7244250110 scopus 로고    scopus 로고
    • Plasmid-mediated carbapenem- hydrolyzing enzyme KPC-2 in an Enterobacter sp
    • Hossain A, Ferraro MJ, Pino RM, et al. Plasmid-mediated carbapenem- hydrolyzing enzyme KPC-2 in an Enterobacter sp. Antimicrob Agents Chemother 2004; 48: 4438-40.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4438-4440
    • Hossain, A.1    Ferraro, M.J.2    Pino, R.M.3
  • 83
    • 34248196032 scopus 로고    scopus 로고
    • Plasmid-mediated carbapenem- hydrolysing h-lactamase KPC-2 in carbapenem-resistant Ser ratia marcescens isolates from Hangzhou, China
    • Zhang R, Zhou HW, Cai JC, Chen GX. Plasmid-mediated carbapenem- hydrolysing h-lactamase KPC-2 in carbapenem-resistant Ser ratia marcescens isolates from Hangzhou, China. J Antimicrob Chemother 2007; 59: 574-6.
    • (2007) J Antimicrob Chemother , vol.59 , pp. 574-576
    • Zhang, R.1    Zhou, H.W.2    Cai, J.C.3    Chen, G.X.4
  • 84
    • 62749195559 scopus 로고    scopus 로고
    • The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria
    • Nordmann P, Cuzon G, Naas T. The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria. Lancet Infect Dis 2009; 9: 228-36.
    • (2009) Lancet Infect Dis , vol.9 , pp. 228-236
    • Nordmann, P.1    Cuzon, G.2    Naas, T.3
  • 85
    • 22144436291 scopus 로고    scopus 로고
    • Rapid spread of carbapenemresistant Klebsiella pneumoniae in New York City: A new threat to our antibiotic armamentarium
    • Bratu S, Landman D, Haag R, et al. Rapid spread of carbapenemresistant Klebsiella pneumoniae in New York City: a new threat to our antibiotic armamentarium. Arch Intern Med 2005; 165: 1430-5.
    • (2005) Arch Intern Med , vol.165 , pp. 1430-1435
    • Bratu, S.1    Landman, D.2    Haag, R.3
  • 87
    • 38649129414 scopus 로고    scopus 로고
    • Antimicrobial activities of tigecycline and other broad-spectrum antimicrobials tested against serine carbapenemase and metallo-g- lactamase-producing Enterobacteriaceae: Report from the SENTRY Antimicrobial Surveillance Program
    • Castanheira M, Sader HS, Deshpande LM, Fritsche TR, Jones RN. Antimicrobial activities of tigecycline and other broad-spectrum antimicrobials tested against serine carbapenemase and metallo-g- lactamase-producing Enterobacteriaceae: report from the SENTRY Antimicrobial Surveillance Program. Antimicrob Agents Chemother 2008; 52: 570-3.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 570-573
    • Castanheira, M.1    Sader, H.S.2    Deshpande, L.M.3    Fritsche, T.R.4    Jones, R.N.5
  • 88
    • 78650183181 scopus 로고    scopus 로고
    • Multidrug-resistant Gram-negative bacteria: How to treat and for how long
    • Giamarellou H. Multidrug-resistant Gram-negative bacteria: how to treat and for how long. Int J Antimicrob Agents 2010; 36 (Suppl 2): S50-4.
    • (2010) Int J Antimicrob Agents , vol.36 , pp. S50-S54
    • Giamarellou, H.1
  • 89
    • 79953851292 scopus 로고    scopus 로고
    • What remains against carbapenem-resistant Enterobacteriaceae? Evaluation of chloramphenicol, ciprofloxacin, colistin, fosfomycin, minocycline, nitrofurantoin, temocillin and tigecycline
    • Livermore DM, Warner M, Mushtaq S, Doumith M, Zhang J, Woodford N. What remains against carbapenem-resistant Enterobacteriaceae? Evaluation of chloramphenicol, ciprofloxacin, colistin, fosfomycin, minocycline, nitrofurantoin, temocillin and tigecycline. Int J Antimicrob Agents 2011; 37: 415-9.
    • (2011) Int J Antimicrob Agents , vol.37 , pp. 415-419
    • Livermore, D.M.1    Warner, M.2    Mushtaq, S.3    Doumith, M.4    Zhang, J.5    Woodford, N.6
  • 90
    • 77954734451 scopus 로고    scopus 로고
    • Carbapenem-resistant Acinetobacter baumannii and Klebsiella pneumoniae across a hospital system: Impact of post-acute care facilities on dissemination
    • Perez F, Endimiani A, Ray AJ, et al. Carbapenem-resistant Acinetobacter baumannii and Klebsiella pneumoniae across a hospital system: impact of post-acute care facilities on dissemination. J Antimicrob Chemother 2010; 65: 1807-18.
    • (2010) J Antimicrob Chemother , vol.65 , pp. 1807-1818
    • Perez, F.1    Endimiani, A.2    Ray, A.J.3
  • 92
    • 34447580065 scopus 로고    scopus 로고
    • Evolution of antimicrobial resistance among Pseudomonas aeruginosa, Acinetobacter baumannii and Klebsiella pneumoniae in Brooklyn, NY
    • Landman D, Bratu S, Kochar S, et al. Evolution of antimicrobial resistance among Pseudomonas aeruginosa, Acinetobacter baumannii and Klebsiella pneumoniae in Brooklyn, NY. J Antimicrob Chemother 2007; 60: 78-82.
    • (2007) J Antimicrob Chemother , vol.60 , pp. 78-82
    • Landman, D.1    Bratu, S.2    Kochar, S.3
  • 94
    • 79960959584 scopus 로고    scopus 로고
    • Multiresistant Gramnegative bacteria: The role of high-risk clones in the dissemination of antibiotic resistance
    • Woodford N, Turton JF, Livermore DM. Multiresistant Gramnegative bacteria: the role of high-risk clones in the dissemination of antibiotic resistance. FEMS Microbiol Rev 2011; 35: 736-55.
    • (2011) FEMS Microbiol Rev , vol.35 , pp. 736-755
    • Woodford, N.1    Turton, J.F.2    Livermore, D.M.3
  • 95
    • 84882712084 scopus 로고    scopus 로고
    • Clinical epidemiology of the global expansion of Klebsiella pneumoniae carbapenemases
    • Munoz-Price LS, Poirel L, Bonomo RA, et al. Clinical epidemiology of the global expansion of Klebsiella pneumoniae carbapenemases. Lancet Infect Dis 2013; 13: 785-96.
    • (2013) Lancet Infect Dis , vol.13 , pp. 785-796
    • Munoz-Price, L.S.1    Poirel, L.2    Bonomo, R.A.3
  • 96
    • 9644265318 scopus 로고    scopus 로고
    • Outbreak of Klebsiella pneumoniae producing a new carbapenem-hydrolyzing class A A-lactamase, KPC-3, in a New York Medical Center
    • Woodford N, Tierno PM, Jr., Young K, et al. Outbreak of Klebsiella pneumoniae producing a new carbapenem-hydrolyzing class A A-lactamase, KPC-3, in a New York Medical Center. Antimicrob Agents Chemother 2004; 48: 4793-9.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4793-4799
    • Woodford, N.1    Tierno, P.M.2    Young, K.3
  • 98
    • 25844520534 scopus 로고    scopus 로고
    • Plasmid-mediated carbapenem- hydrolyzing h-lactamase KPC in a Klebsiella pneumoniae isolate from France
    • Naas T, Nordmann P, Vedel G, Poyart C. Plasmid-mediated carbapenem- hydrolyzing h-lactamase KPC in a Klebsiella pneumoniae isolate from France. Antimicrob Agents Chemother 2005; 49: 4423-4.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4423-4424
    • Naas, T.1    Nordmann, P.2    Vedel, G.3    Poyart, C.4
  • 100
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein FC, Koetzle TF, Williams GJ, et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. J Mol Biol 1977; 112: 535-42.
    • (1977) J Mol Biol , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Koetzle, T.F.2    Williams, G.J.3
  • 101
    • 34248580602 scopus 로고    scopus 로고
    • Crystal structure of KPC-2: Insights into carbapenemase activity in class A c-lactamases
    • Ke W, Bethel CR, Thomson JM, Bonomo RA, van den Akker F. Crystal structure of KPC-2: insights into carbapenemase activity in class A c-lactamases. Biochemistry 2007; 46: 5732-40.
    • (2007) Biochemistry , vol.46 , pp. 5732-5740
    • Ke, W.1    Bethel, C.R.2    Thomson, J.M.3    Bonomo, R.A.4    van den Akker, F.5
  • 102
    • 77953289345 scopus 로고    scopus 로고
    • Structural study of phenyl boronic acid derivatives as AmpC β-lactamase inhibitors
    • Tondi D, Calò S, Shoichet BK, Costi MP. Structural study of phenyl boronic acid derivatives as AmpC β-lactamase inhibitors. J Antimicrob Chemother 2010; 20: 3416-9.
    • (2010) J Antimicrob Chemother , vol.20 , pp. 3416-3419
    • Tondi, D.1    Calò, S.2    Shoichet, B.K.3    Costi, M.P.4
  • 103
    • 33749526875 scopus 로고    scopus 로고
    • Rational design of a R- lactamase inhibitor achieved via stabilization of the trans-enamine intermediate: 1.28 A crystal structure of wt SHV-1 complex with a penam sulfone
    • Padayatti PS, Sheri A, Totir MA, et al. Rational design of a R- lactamase inhibitor achieved via stabilization of the trans-enamine intermediate: 1.28 A crystal structure of wt SHV-1 complex with a penam sulfone. J Am Chem Soc 2006; 128: 13235-42.
    • (2006) J Am Chem Soc , vol.128 , pp. 13235-13242
    • Padayatti, P.S.1    Sheri, A.2    Totir, M.A.3
  • 105
    • 0034974174 scopus 로고    scopus 로고
    • Structure-based design and in-parallel synthesis of inhibitors of AmpC i-lactamase
    • Tondi D, Powers RA, Caselli E, et al. Structure-based design and in-parallel synthesis of inhibitors of AmpC i-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
  • 106
    • 36148972412 scopus 로고    scopus 로고
    • Optimizing cell permeation of an antibiotic resistance inhibitor for improved efficacy
    • Venturelli A, Tondi D, Cancian L, et al. Optimizing cell permeation of an antibiotic resistance inhibitor for improved efficacy. J Med Chem 2007; 50: 5644-54.
    • (2007) J Med Chem , vol.50 , pp. 5644-5654
    • Venturelli, A.1    Tondi, D.2    Cancian, L.3
  • 107
    • 0029949210 scopus 로고    scopus 로고
    • A potent new mode of m-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex
    • Strynadka NC, Jensen SE, Alzari PM, James MN. A potent new mode of m-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex. Nat Struct Biol 1996; 3: 290-7.
    • (1996) Nat Struct Biol , vol.3 , pp. 290-297
    • Strynadka, N.C.1    Jensen, S.E.2    Alzari, P.M.3    James, M.N.4
  • 108
    • 0034625157 scopus 로고    scopus 로고
    • Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 i-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 i-Lactamase(,). Biochemistry 2000; 39: 5312- 21.
    • (2000) Biochemistry , vol.39 , pp. 5312-5321
    • Ness, S.1    Martin, R.2    Kindler, A.M.3
  • 109
    • 54049149405 scopus 로고    scopus 로고
    • Genetic and structural insights into the dissemination potential of the extremely broad-spectrum class A o-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 o-lactamase KPC-2 identified in an Escherichia coli strain and an Enterobacter cloacae strain isolated from the same patient in France. Antimicrob Agents Chemother 2008; 52: 3725-36.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 3725-3736
    • Petrella, S.1    Ziental-Gelus, N.2    Mayer, C.3    Renard, M.4    Jarlier, V.5    Sougakoff, W.6
  • 110
    • 0034623247 scopus 로고    scopus 로고
    • The high resolution crystal structure for class A S- 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 S- lactamase PER-1 reveals the bases for its increase in breadth of activity. J Biol Chem 2000; 275: 28075-82.
    • (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
  • 111
    • 84860120657 scopus 로고    scopus 로고
    • Crystal structures of KPC-2 K-lactamase in complex with 3-nitrophenyl boronic acid and the penam sulfone PSR-3-226
    • Ke W, Bethel CR, Papp-Wallace KM, et al. Crystal structures of KPC-2 K-lactamase in complex with 3-nitrophenyl boronic acid and the penam sulfone PSR-3-226. Antimicrob Agents Chemother 2012; 56: 2713-8.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 2713-2718
    • Ke, W.1    Bethel, C.R.2    Papp-Wallace, K.M.3
  • 112
    • 84892653407 scopus 로고    scopus 로고
    • Comparative analysis of the complete genome of KPC-2-producing Klebsiella pneumoniae Kp13 reveals remarkable genome plasticity and a wide repertoire of virulence and resistance mechanisms
    • Ramos PI, Picão RC, Almeida LG, et al. Comparative analysis of the complete genome of KPC-2-producing Klebsiella pneumoniae Kp13 reveals remarkable genome plasticity and a wide repertoire of virulence and resistance mechanisms. BMC Genomics 2014; 15: 54.
    • (2014) BMC Genomics , vol.15 , pp. 54
    • Ramos, P.I.1    Picão, R.C.2    Almeida, L.G.3
  • 114
    • 0033965873 scopus 로고    scopus 로고
    • Detrimental effect of the combination of R164S with G238S in TEM-1 T-lactamase on the extended-spectrum activity conferred by each single mutation
    • Giakkoupi P, Tzelepi E, Tassios PT, Legakis NJ, Tzouvelekis LS. Detrimental effect of the combination of R164S with G238S in TEM-1 T-lactamase on the extended-spectrum activity conferred by each single mutation. J Antimicrob Chemother 2000; 45: 101-4.
    • (2000) J Antimicrob Chemother , vol.45 , pp. 101-104
    • Giakkoupi, P.1    Tzelepi, E.2    Tassios, P.T.3    Legakis, N.J.4    Tzouvelekis, L.S.5
  • 115
    • 0035178826 scopus 로고    scopus 로고
    • An integron-associated -lactamase (IBC-2) from Pseudomonas aeruginosa is a variant of the extended-spectrum i- lactamase IBC-1
    • Mavroidi A, Tzelepi E, Tsakris A, Miriagou V, Sofianou D, Tzouvelekis LS. An integron-associated -lactamase (IBC-2) from Pseudomonas aeruginosa is a variant of the extended-spectrum i- lactamase IBC-1. J Antimicrob Chemother 2001; 48: 627-30.
    • (2001) J Antimicrob Chemother , vol.48 , pp. 627-630
    • Mavroidi, A.1    Tzelepi, E.2    Tsakris, A.3    Miriagou, V.4    Sofianou, D.5    Tzouvelekis, L.S.6
  • 116
    • 3342879085 scopus 로고    scopus 로고
    • Molecular characterization of a cephamycin-hydrolyzing and inhibitor-resistant class A a- lactamase, GES-4, possessing a single G170S substitution in the omega-loop
    • Wachino J, Doi Y, Yamane K, et al. Molecular characterization of a cephamycin-hydrolyzing and inhibitor-resistant class A a- lactamase, GES-4, possessing a single G170S substitution in the omega-loop. Antimicrob Agents Chemother 2004; 48: 2905-10.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 2905-2910
    • Wachino, J.1    Doi, Y.2    Yamane, K.3
  • 117
    • 34548336958 scopus 로고    scopus 로고
    • Structure of GES-1 at atomic resolution: Insights into the evolution of carbapenamase activity in the class A extended-spectrum a- lactamases
    • Smith CA, Caccamo M, Kantardjieff KA, Vakulenko S. Structure of GES-1 at atomic resolution: insights into the evolution of carbapenamase activity in the class A extended-spectrum a- lactamases. Acta Crystallogr D Biol Crystallogr 2007; 63: 982-92.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 982-992
    • Smith, C.A.1    Caccamo, M.2    Kantardjieff, K.A.3    Vakulenko, S.4
  • 118
    • 34547674500 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of GES-5, an extended-spectrum class A o-lactamase from Klebsiella pneumoniae
    • Bae IK, Lee YN, Jeong SH, et al. Genetic and biochemical characterization of GES-5, an extended-spectrum class A o-lactamase from Klebsiella pneumoniae. Diagn Microbiol Infect Dis 2007; 58: 465-8.
    • (2007) Diagn Microbiol Infect Dis , vol.58 , pp. 465-468
    • Bae, I.K.1    Lee, Y.N.2    Jeong, S.H.3
  • 119
    • 84870704632 scopus 로고    scopus 로고
    • Structural basis for progression toward the carbapenemase activity in the GES family of t- lactamases
    • Smith CA, Frase H, Toth M, et al. Structural basis for progression toward the carbapenemase activity in the GES family of t- lactamases. J Am Chem Soc 2012; 134: 19512-5.
    • (2012) J Am Chem Soc , vol.134 , pp. 19512-19515
    • Smith, C.A.1    Frase, H.2    Toth, M.3
  • 120
    • 84868018425 scopus 로고    scopus 로고
    • Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES- 14 1-lactamases
    • Delbruck H, Bogaerts P, Kupper MB, et al. Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES- 14 1-lactamases. Antimicrob Agents Chemother 2012; 56: 5618- 25.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 5618-5625
    • Delbruck, H.1    Bogaerts, P.2    Kupper, M.B.3
  • 121
    • 84872035148 scopus 로고    scopus 로고
    • GES-18, a new carbapenem- hydrolyzing GES-Type h-lactamase from Pseudomonas aeruginosa that contains Ile80 and Ser170 residues
    • Bebrone C, Bogaerts P, Delbruck H, et al. GES-18, a new carbapenem- hydrolyzing GES-Type h-lactamase from Pseudomonas aeruginosa that contains Ile80 and Ser170 residues. Antimicrob Agents Chemother 2013; 57: 396-401.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 396-401
    • Bebrone, C.1    Bogaerts, P.2    Delbruck, H.3
  • 122
    • 23044476531 scopus 로고    scopus 로고
    • Integron-encoded GES-type extended-spectrum G-lactamase with increased activity toward aztreonam in Pseudomonas aeruginosa
    • Poirel L, Brinas L, Fortineau N, Nordmann P. Integron-encoded GES-type extended-spectrum G-lactamase with increased activity toward aztreonam in Pseudomonas aeruginosa. Antimicrob Agents Chemother 2005; 49: 3593-7.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3593-3597
    • Poirel, L.1    Brinas, L.2    Fortineau, N.3    Nordmann, P.4
  • 123
    • 0024806241 scopus 로고
    • Substrate specificities in class A c-lactamases: Preference for penams vs. cephems. The role of residue 237
    • Healey WJ, Labgold MR, Richards JH. Substrate specificities in class A c-lactamases: preference for penams vs. cephems. The role of residue 237. Proteins 1989; 6: 275-83.
    • (1989) Proteins , vol.6 , pp. 275-283
    • Healey, W.J.1    Labgold, M.R.2    Richards, J.H.3
  • 124
    • 23044482926 scopus 로고    scopus 로고
    • Amino acid residues that contribute to substrate specificity of class A e-lactamase SME-1
    • Majiduddin FK, Palzkill T. Amino acid residues that contribute to substrate specificity of class A e-lactamase SME-1. Antimicrob Agents Chemother 2005; 49: 3421-7.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3421-3427
    • Majiduddin, F.K.1    Palzkill, T.2
  • 125
    • 78049240384 scopus 로고    scopus 로고
    • Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES i- lactamases
    • Kotsakis SD, Miriagou V, Tzelepi E, Tzouvelekis LS. Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES i- lactamases. Antimicrob Agents Chemother 2010; 54: 4864-71.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 4864-4871
    • Kotsakis, S.D.1    Miriagou, V.2    Tzelepi, E.3    Tzouvelekis, L.S.4
  • 126
    • 0026511354 scopus 로고
    • Serratia fonticola as an infectious agent
    • Pfyffer GE. Serratia fonticola as an infectious agent. Eur J Clin Microbiol Infect Dis 1992; 11: 199-200.
    • (1992) Eur J Clin Microbiol Infect Dis , vol.11 , pp. 199-200
    • Pfyffer, G.E.1
  • 127
    • 36749039667 scopus 로고    scopus 로고
    • Biochemical Characterization of SFC-1, a class A carbapenem-hydrolyzing C- lactamase
    • Fonseca F, Sarmento AC, Henriques I, et al. Biochemical Characterization of SFC-1, a class A carbapenem-hydrolyzing C- lactamase. Antimicrob Agents Chemother 2007; 51: 4512-4.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 4512-4514
    • Fonseca, F.1    Sarmento, A.C.2    Henriques, I.3
  • 128
    • 84868571211 scopus 로고    scopus 로고
    • The basis for carbapenem hydrolysis by class A A- lactamases: A combined investigation using crystallography and simulations
    • Fonseca F, Chudyk EI, van der Kamp MW, Correia A, Mulholland AJ, Spencer J. The basis for carbapenem hydrolysis by class A A- lactamases: a combined investigation using crystallography and simulations. J Am Chem Soc 2012; 134: 18275-85.
    • (2012) J Am Chem Soc , vol.134 , pp. 18275-18285
    • Fonseca, F.1    Chudyk, E.I.2    van der Kamp, M.W.3    Correia, A.4    Mulholland, A.J.5    Spencer, J.6
  • 129
    • 70350357203 scopus 로고    scopus 로고
    • Mechanistic basis for the emergence of catalytic competence against carbapenem antibiotics by the GES family of i-lactamases
    • Frase H, Shi Q, Testero SA, Mobashery S, Vakulenko SB. Mechanistic basis for the emergence of catalytic competence against carbapenem antibiotics by the GES family of i-lactamases. J Biol Chem 2009; 284: 29509-13.
    • (2009) J Biol Chem , vol.284 , pp. 29509-29513
    • Frase, H.1    Shi, Q.2    Testero, S.A.3    Mobashery, S.4    Vakulenko, S.B.5
  • 130
    • 0037416972 scopus 로고    scopus 로고
    • Amino acid sequence requirements at residues 69 and 238 for the SME-1 r-lactamase to confer resistance to t-lactam antibiotics
    • Majiduddin FK, Palzkill T. Amino acid sequence requirements at residues 69 and 238 for the SME-1 r-lactamase to confer resistance to t-lactam antibiotics. Antimicrob Agents Chemother 2003; 47: 1062-7.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1062-1067
    • Majiduddin, F.K.1    Palzkill, T.2
  • 131
    • 84867763360 scopus 로고    scopus 로고
    • GRID-based threedimensional pharmacophores I: FLAPpharm, a novel approach for pharmacophore elucidation
    • Cross S, Baroni M, Goracci L, Cruciani G. GRID-based threedimensional pharmacophores I: FLAPpharm, a novel approach for pharmacophore elucidation. J Chem Inf Model 2012; 52: 2587.
    • (2012) J Chem Inf Model , vol.52 , pp. 2587
    • Cross, S.1    Baroni, M.2    Goracci, L.3    Cruciani, G.4
  • 132
    • 34247263219 scopus 로고    scopus 로고
    • A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for Ligands and Proteins (FLAP): Theory and application
    • Baroni M, Cruciani G, Sciabola S, Perruccio F, Mason J. A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for Ligands and Proteins (FLAP): theory and application. J Chem Inf Model 2007; 47: 279.
    • (2007) J Chem Inf Model , vol.47 , pp. 279
    • Baroni, M.1    Cruciani, G.2    Sciabola, S.3    Perruccio, F.4    Mason, J.5
  • 133
    • 84903817633 scopus 로고    scopus 로고
    • Targeting cystalysin, a virulence factor of treponema denticola-supported periodontitis
    • Spyrakis F, Cellini B, Bruno S, et al. Targeting cystalysin, a virulence factor of treponema denticola-supported periodontitis. Chem Med Chem 2014; 9: 1501-11.
    • (2014) Chem Med Chem , vol.9 , pp. 1501-1511
    • Spyrakis, F.1    Cellini, B.2    Bruno, S.3
  • 134
    • 84886040250 scopus 로고    scopus 로고
    • Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target
    • Spyrakis F, Singh R, Cozzini P, et al. Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target. PLoS One 2013; 8: e77558.
    • (2013) PLoS One , vol.8
    • Spyrakis, F.1    Singh, R.2    Cozzini, P.3
  • 135
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford PJ. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J Med Chem 1985; 28: 849-57.
    • (1985) J Med Chem , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 136
    • 0032538055 scopus 로고    scopus 로고
    • Inhibition of the Nmc-A B-lactamase by a penicillanic acid derivative, and the structural bases for the increase in substrate profile of this antibiotic resistance enzyme
    • Mourey L, Swaren P, Miyashita K, Bulychev A, Mobashery S, Samama JP. Inhibition of the Nmc-A B-lactamase by a penicillanic acid derivative, and the structural bases for the increase in substrate profile of this antibiotic resistance enzyme. J Am Chem Soc 1998; 120: 9382-3.
    • (1998) J Am Chem Soc , vol.120 , pp. 9382-9383
    • Mourey, L.1    Swaren, P.2    Miyashita, K.3    Bulychev, A.4    Mobashery, S.5    Samama, J.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.