메뉴 건너뛰기




Volumn 25, Issue 4, 2016, Pages 787-803

One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams

Author keywords

multidrug resistant bacteria; penicillin binding protein; resistance; lactam; lactamase

Indexed keywords

3 [[2 (2 AMINO 4 THIAZOLYL) 2 [[(1,4 DIHYDRO 1,5 DIHYDROXY 4 OXO 2 PYRIDINYL)METHOXY]IMINO]ACETYL]AMINO] 4 METHYL 2 OXO 1 AZETIDINESULFONIC ACID; AMPICILLIN; ASPERGILLOMARASMINE A; AVIBACTAM PLUS CEFTAROLINE; BAL 29880; BAL 90072; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; CARBAPENEM DERIVATIVE; CARBENICILLIN; CEFOXITIN; CEFTAROLINE; CEFTOBIPROLE; CEFTOLOZANE PLUS TAZOBACTAM; CEPHALOSPORIN DERIVATIVE; CILASTATIN; CILASTATIN PLUS IMIPENEM PLUS RELEBACTAM; MERPENEM PLUS VABORBACTAM; ML 302F; NITROCEFIN; PENICILLIN BINDING PROTEIN; PENICILLIN DERIVATIVE; PHENYLARGININE BETA NAPHTHYLAMIDE; PORIN; SIDEROPHORE; UNCLASSIFIED DRUG; VABORBACTAM; ANTIINFECTIVE AGENT;

EID: 84960157138     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2889     Document Type: Review
Times cited : (78)

References (138)
  • 1
    • 84877279350 scopus 로고    scopus 로고
    • Platforms for antibiotic discovery
    • Lewis K, (2013) Platforms for antibiotic discovery. Nat Rev Drug Discov 12: 371-387.
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 371-387
    • Lewis, K.1
  • 3
    • 77957980707 scopus 로고    scopus 로고
    • Origins and evolution of antibiotic resistance
    • Davies J, Davies D, (2010) Origins and evolution of antibiotic resistance. Microbiol Mol Biol Rev 74: 417-433.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 417-433
    • Davies, J.1    Davies, D.2
  • 4
    • 0024039854 scopus 로고
    • An enzyme from bacteria able to destroy penicillin. 1940
    • Abraham EP, Chain E, (1988) An enzyme from bacteria able to destroy penicillin. 1940. Rev Infect Dis 10: 677-678.
    • (1988) Rev Infect Dis , vol.10 , pp. 677-678
    • Abraham, E.P.1    Chain, E.2
  • 5
    • 80053247739 scopus 로고    scopus 로고
    • Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from Gram-negative bacteria
    • Bush K, Fisher JF, (2011) Epidemiological expansion, structural studies, and clinical challenges of new β-lactamases from Gram-negative bacteria. Annu Rev Microbiol 65: 455-478.
    • (2011) Annu Rev Microbiol , vol.65 , pp. 455-478
    • Bush, K.1    Fisher, J.F.2
  • 6
    • 77957770819 scopus 로고    scopus 로고
    • Alarming β-lactamase-mediated resistance in multidrug-resistant Enterobacteriaceae
    • Bush K, (2010) Alarming β-lactamase-mediated resistance in multidrug-resistant Enterobacteriaceae. Curr Opin Microbiol 13: 558-564.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 558-564
    • Bush, K.1
  • 7
    • 84871652077 scopus 로고    scopus 로고
    • Underlying mechanisms of carbapenem resistance in extended-spectrum β-lactamase-producing Klebsiella pneumoniae and Escherichia coli isolates at a tertiary care centre in Lebanon: Role of OXA-48 and NDM-1 carbapenemases
    • Baroud M, Dandache I, Araj GF, Wakim R, Kanj S, Kanafani Z, Khairallah M, Sabra A, Shehab M, Dbaibo G, Matar GM, (2013) Underlying mechanisms of carbapenem resistance in extended-spectrum β-lactamase-producing Klebsiella pneumoniae and Escherichia coli isolates at a tertiary care centre in Lebanon: role of OXA-48 and NDM-1 carbapenemases. Int J Antimicrob Agents 41: 75-79.
    • (2013) Int J Antimicrob Agents , vol.41 , pp. 75-79
    • Baroud, M.1    Dandache, I.2    Araj, G.F.3    Wakim, R.4    Kanj, S.5    Kanafani, Z.6    Khairallah, M.7    Sabra, A.8    Shehab, M.9    Dbaibo, G.10    Matar, G.M.11
  • 8
    • 80053651253 scopus 로고    scopus 로고
    • Extended-spectrum β-lactamases in Gram negative bacteria
    • Rawat D, Nair D, (2010) Extended-spectrum β-lactamases in Gram negative bacteria. J Glob Infect Dis 2: 263-274.
    • (2010) J Glob Infect Dis , vol.2 , pp. 263-274
    • Rawat, D.1    Nair, D.2
  • 9
    • 84900306147 scopus 로고    scopus 로고
    • Who will develop new antibacterial agents?
    • Cole ST, (2014) Who will develop new antibacterial agents? Philos Trans R Soc London B Biol Sci 369: 20130430.
    • (2014) Philos Trans R Soc London B Biol Sci , vol.369 , pp. 20130430
    • Cole, S.T.1
  • 10
    • 84874077280 scopus 로고    scopus 로고
    • Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 β-lactamase for the acylation reaction
    • Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L, (2013) Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 β-lactamase for the acylation reaction. J Biol Chem 288: 4715-4722.
    • (2013) J Biol Chem , vol.288 , pp. 4715-4722
    • Tomanicek, S.J.1    Standaert, R.F.2    Weiss, K.L.3    Ostermann, A.4    Schrader, T.E.5    Ng, J.D.6    Coates, L.7
  • 11
    • 84893391938 scopus 로고    scopus 로고
    • Targeting metallo-β-lactamase enzymes in antibiotic resistance
    • King DT, Strynadka NC, (2013) Targeting metallo-β-lactamase enzymes in antibiotic resistance. Future Med Chem 5: 1243-1263.
    • (2013) Future Med Chem , vol.5 , pp. 1243-1263
    • King, D.T.1    Strynadka, N.C.2
  • 12
    • 84882239083 scopus 로고    scopus 로고
    • The ABCD's of β-lactamase nomenclature
    • Bush K, (2013) The ABCD's of β-lactamase nomenclature. J Infect Chemother 19: 549-559.
    • (2013) J Infect Chemother , vol.19 , pp. 549-559
    • Bush, K.1
  • 13
    • 36348944684 scopus 로고    scopus 로고
    • Structure and dynamics of CTX-M enzymes reveal insights into substrate accommodation by extended-spectrum beta-lactamases
    • Delmas J, Chen Y, Prati F, Robin F, Shoichet BK, Bonnet R, (2008) Structure and dynamics of CTX-M enzymes reveal insights into substrate accommodation by extended-spectrum beta-lactamases. J Mol Biol 375: 192-201.
    • (2008) J Mol Biol , vol.375 , pp. 192-201
    • Delmas, J.1    Chen, Y.2    Prati, F.3    Robin, F.4    Shoichet, B.K.5    Bonnet, R.6
  • 15
    • 0035807996 scopus 로고    scopus 로고
    • Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases
    • Golemi D, Maveyraud L, Vakulenko S, Samama JP, Mobashery S, (2001) Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases. Proc Natl Acad Sci USA 98: 14280-14285.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14280-14285
    • Golemi, D.1    Maveyraud, L.2    Vakulenko, S.3    Samama, J.P.4    Mobashery, S.5
  • 16
    • 61449127371 scopus 로고    scopus 로고
    • Re-examining the role of Lys67 in class C beta-lactamase catalysis
    • Chen Y, McReynolds A, Shoichet BK, (2009) Re-examining the role of Lys67 in class C beta-lactamase catalysis. Protein Sci 18: 662-669.
    • (2009) Protein Sci , vol.18 , pp. 662-669
    • Chen, Y.1    McReynolds, A.2    Shoichet, B.K.3
  • 18
    • 84896968084 scopus 로고    scopus 로고
    • New β-lactamase inhibitors: A therapeutic renaissance in an MDR world
    • Drawz SM, Papp-Wallace KM, Bonomo RA, (2014) New β-lactamase inhibitors: a therapeutic renaissance in an MDR world. Antimicrob Agents Chemother 58: 1835-1846.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 1835-1846
    • Drawz, S.M.1    Papp-Wallace, K.M.2    Bonomo, R.A.3
  • 20
    • 84872844727 scopus 로고    scopus 로고
    • New β-lactam-β-lactamase inhibitor combinations in clinical development
    • Shlaes DM, (2013) New β-lactam-β-lactamase inhibitor combinations in clinical development. Ann N Y Acad Sci 1277: 105-114.
    • (2013) Ann N y Acad Sci , vol.1277 , pp. 105-114
    • Shlaes, D.M.1
  • 21
    • 84880714408 scopus 로고    scopus 로고
    • Activity of biapenem (RPX2003) combined with the boronate β-lactamase inhibitor RPX7009 against carbapenem-resistant Enterobacteriaceae
    • Livermore DM, Mushtaq S, (2013) Activity of biapenem (RPX2003) combined with the boronate β-lactamase inhibitor RPX7009 against carbapenem-resistant Enterobacteriaceae. J Antimicrob Chemother 68: 1825-1831.
    • (2013) J Antimicrob Chemother , vol.68 , pp. 1825-1831
    • Livermore, D.M.1    Mushtaq, S.2
  • 22
    • 81155162497 scopus 로고    scopus 로고
    • Diazabicyclooctanes (DBOs): A potent new class of non-β-lactam β-lactamase inhibitors
    • Coleman K, (2011) Diazabicyclooctanes (DBOs): a potent new class of non-β-lactam β-lactamase inhibitors. Curr Opin Microbiol 14: 550-555.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 550-555
    • Coleman, K.1
  • 24
    • 84894441748 scopus 로고    scopus 로고
    • Ceftazidime-avibactam: An evidence-based review of its pharmacology and potential use in the treatment of Gram-negative bacterial infections
    • Lagacé-Wiens P, Walkty A, Karlowsky JA, (2014) Ceftazidime-avibactam: an evidence-based review of its pharmacology and potential use in the treatment of Gram-negative bacterial infections. Core Evid 9: 13-25.
    • (2014) Core Evid , vol.9 , pp. 13-25
    • Lagacé-Wiens, P.1    Walkty, A.2    Karlowsky, J.A.3
  • 25
    • 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 β-lactamases
    • Lahiri SD, Mangani S, Durand-Reville T, Benvenuti M, De Luca F, Sanyal G, Docquier JD, (2013) Structural insight into potent broad-spectrum inhibition with reversible recyclization mechanism: avibactam in complex with CTX-M-15 and Pseudomonas aeruginosa AmpC β-lactamases. Antimicrob Agents Chemother 57: 2496-2505.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 2496-2505
    • Lahiri, S.D.1    Mangani, S.2    Durand-Reville, T.3    Benvenuti, M.4    De Luca, F.5    Sanyal, G.6    Docquier, J.D.7
  • 28
  • 29
    • 79958711382 scopus 로고    scopus 로고
    • Boron-containing inhibitors of synthetases
    • Baker SJ, Tomsho JW, Benkovic SJ, (2011) Boron-containing inhibitors of synthetases. Chem Soc Rev 40: 4279-4285.
    • (2011) Chem Soc Rev , vol.40 , pp. 4279-4285
    • Baker, S.J.1    Tomsho, J.W.2    Benkovic, S.J.3
  • 31
    • 0029760859 scopus 로고    scopus 로고
    • Structure-based design of a potent transition state analogue for TEM-1 beta-lactamase
    • Strynadka NC, Martin R, Jensen SE, Gold M, Jones JB, (1996) Structure-based design of a potent transition state analogue for TEM-1 beta-lactamase. Nat Struct Biol 3: 688-695.
    • (1996) Nat Struct Biol , vol.3 , pp. 688-695
    • Strynadka, N.C.1    Martin, R.2    Jensen, S.E.3    Gold, M.4    Jones, J.B.5
  • 32
    • 0037405256 scopus 로고    scopus 로고
    • Boronic acid compounds as potential pharmaceutical agents
    • Yang W, Gao X, Wang B, (2003) Boronic acid compounds as potential pharmaceutical agents. Med Res Rev 23: 346-368.
    • (2003) Med Res Rev , vol.23 , pp. 346-368
    • Yang, W.1    Gao, X.2    Wang, B.3
  • 33
    • 77957867755 scopus 로고    scopus 로고
    • Activity of BAL30376 (monobactam BAL19764+BAL29880+clavulanate) versus Gram-negative bacteria with characterized resistance mechanisms
    • Livermore DM, Mushtaq S, Warner M, (2010) Activity of BAL30376 (monobactam BAL19764+BAL29880+clavulanate) versus Gram-negative bacteria with characterized resistance mechanisms. J Antimicrob Chemother 65: 2382-2395.
    • (2010) J Antimicrob Chemother , vol.65 , pp. 2382-2395
    • Livermore, D.M.1    Mushtaq, S.2    Warner, M.3
  • 34
    • 77952614275 scopus 로고    scopus 로고
    • In vitro properties of BAL30072, a novel siderophore sulfactam with activity against multiresistant gram-negative bacilli
    • Page MG, Dantier C, Desarbre E, (2010) In vitro properties of BAL30072, a novel siderophore sulfactam with activity against multiresistant gram-negative bacilli. Antimicrob Agents Chemother 54: 2291-2302.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 2291-2302
    • Page, M.G.1    Dantier, C.2    Desarbre, E.3
  • 35
    • 84879022343 scopus 로고    scopus 로고
    • Human simulated studies of aztreonam and aztreonam-avibactam to evaluate activity against challenging Gram-negative organisms, including metallo-β-lactamase producers
    • Crandon JL, Nicolau DP, (2013) Human simulated studies of aztreonam and aztreonam-avibactam to evaluate activity against challenging Gram-negative organisms, including metallo-β-lactamase producers. Antimicrob Agents Chemother 57: 3299-3306.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 3299-3306
    • Crandon, J.L.1    Nicolau, D.P.2
  • 37
    • 79959870774 scopus 로고    scopus 로고
    • Thiophenyl oxime-derived phosphonates as nano-molar class C beta-lactamase inhibitors reducing MIC of imipenem against Pseudomonas aeruginosa and Acinetobacter baumannii
    • Tan Q, Ogawa AM, Raghoobar SL, Wisniewski D, Colwell L, Park YW, Young K, Hermes JD, Dininno FP, Hammond ML, (2011) Thiophenyl oxime-derived phosphonates as nano-molar class C beta-lactamase inhibitors reducing MIC of imipenem against Pseudomonas aeruginosa and Acinetobacter baumannii. Bioorg Med Chem Lett 21: 4363-4365.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 4363-4365
    • Tan, Q.1    Ogawa, A.M.2    Raghoobar, S.L.3    Wisniewski, D.4    Colwell, L.5    Park, Y.W.6    Young, K.7    Hermes, J.D.8    Dininno, F.P.9    Hammond, M.L.10
  • 40
    • 22144437663 scopus 로고    scopus 로고
    • Bacterial resistance to antibiotics: Modified target sites
    • Lambert PA, (2005) Bacterial resistance to antibiotics: modified target sites. Adv Drug Deliv Rev 57: 1471-1485.
    • (2005) Adv Drug Deliv Rev , vol.57 , pp. 1471-1485
    • Lambert, P.A.1
  • 41
    • 69249083586 scopus 로고    scopus 로고
    • Waves of resistance: Staphylococcus aureus in the antibiotic era
    • Chambers HF, Deleo FR, (2009) Waves of resistance: Staphylococcus aureus in the antibiotic era. Nat Rev Microbiol 7: 629-641.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 629-641
    • Chambers, H.F.1    Deleo, F.R.2
  • 42
    • 84858398621 scopus 로고    scopus 로고
    • The rise of the Enterococcus: Beyond vancomycin resistance
    • Arias CA, Murray BE, (2012) The rise of the Enterococcus: beyond vancomycin resistance. Nat Rev Microbiol 10: 266-278.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 266-278
    • Arias, C.A.1    Murray, B.E.2
  • 43
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis
    • Sauvage E, Kerff F, Terrak M, Ayala JA, Charlier P, (2008) The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32: 234-258.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 44
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas A, Banzhaf M, Gross CA, Vollmer W, (2012) From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol 10: 123-136.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 45
    • 39149104344 scopus 로고    scopus 로고
    • Penicillin-binding proteins and beta-lactam resistance
    • Zapun A, Contreras-Martel C, Vernet T, (2008) Penicillin-binding proteins and beta-lactam resistance. FEMS Microbiol Rev 32: 361-385.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 361-385
    • Zapun, A.1    Contreras-Martel, C.2    Vernet, T.3
  • 46
    • 37049001066 scopus 로고    scopus 로고
    • Hospitalizations and deaths caused by methicillin-resistant Staphylococcus aureus, United States, 1999-2005
    • Klein E, Smith DL, Laxminarayan R, (2007) Hospitalizations and deaths caused by methicillin-resistant Staphylococcus aureus, United States, 1999-2005. Emerg Infect Dis 13: 1840-1846.
    • (2007) Emerg Infect Dis , vol.13 , pp. 1840-1846
    • Klein, E.1    Smith, D.L.2    Laxminarayan, R.3
  • 47
    • 0036829003 scopus 로고    scopus 로고
    • Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus
    • Lim D, Strynadka NC, (2002) Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus. Nat Struct Biol 9: 870-876.
    • (2002) Nat Struct Biol , vol.9 , pp. 870-876
    • Lim, D.1    Strynadka, N.C.2
  • 48
    • 0035831262 scopus 로고    scopus 로고
    • A proteolytic transmembrane signaling pathway and resistance to beta-lactams in staphylococci
    • Zhang HZ, Hackbarth CJ, Chansky KM, Chambers HF, (2001) A proteolytic transmembrane signaling pathway and resistance to beta-lactams in staphylococci. Science 291: 1962-1965.
    • (2001) Science , vol.291 , pp. 1962-1965
    • Zhang, H.Z.1    Hackbarth, C.J.2    Chansky, K.M.3    Chambers, H.F.4
  • 49
    • 0028289341 scopus 로고
    • Dissemination among staphylococci of DNA sequences associated with methicillin resistance
    • Archer GL, Niemeyer DM, Thanassi JA, Pucci MJ, (1994) Dissemination among staphylococci of DNA sequences associated with methicillin resistance. Antimicrob Agents Chemother 38: 447-454.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 447-454
    • Archer, G.L.1    Niemeyer, D.M.2    Thanassi, J.A.3    Pucci, M.J.4
  • 50
    • 13944282888 scopus 로고    scopus 로고
    • Activation for catalysis of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus by bacterial cell wall
    • Fuda C, Hesek D, Lee M, Morio K, Nowak T, Mobashery S, (2005) Activation for catalysis of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus by bacterial cell wall. J Am Chem Soc 127: 2056-2057.
    • (2005) J Am Chem Soc , vol.127 , pp. 2056-2057
    • Fuda, C.1    Hesek, D.2    Lee, M.3    Morio, K.4    Nowak, T.5    Mobashery, S.6
  • 51
    • 0032755508 scopus 로고    scopus 로고
    • Antibiotic resistance as a stress response: Complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin
    • De Lencastre H, Wu SW, Pinho MG, Ludovice AM, Filipe S, Gardete S, Sobral R, Gill S, Chung M, Tomasz A, (1999) Antibiotic resistance as a stress response: complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin. Microb Drug Resist 5: 163-175.
    • (1999) Microb Drug Resist , vol.5 , pp. 163-175
    • De Lencastre, H.1    Wu, S.W.2    Pinho, M.G.3    Ludovice, A.M.4    Filipe, S.5    Gardete, S.6    Sobral, R.7    Gill, S.8    Chung, M.9    Tomasz, A.10
  • 53
    • 0035943720 scopus 로고    scopus 로고
    • Kinetics of beta-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance
    • Lu WP, Kincaid E, Sun Y, Bauer MD, (2001) Kinetics of beta-lactam interactions with penicillin-susceptible and -resistant penicillin-binding protein 2x proteins from Streptococcus pneumoniae. Involvement of acylation and deacylation in beta-lactam resistance. J Biol Chem 276: 31494-31501.
    • (2001) J Biol Chem , vol.276 , pp. 31494-31501
    • Lu, W.P.1    Kincaid, E.2    Sun, Y.3    Bauer, M.D.4
  • 54
    • 0033580616 scopus 로고    scopus 로고
    • Penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus: Kinetic characterization of its interactions with beta-lactams using electrospray mass spectrometry
    • Lu WP, Sun Y, Bauer MD, Paule S, Koenigs PM, Kraft WG, (1999) Penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus: kinetic characterization of its interactions with beta-lactams using electrospray mass spectrometry. Biochemistry 38: 6537-6546.
    • (1999) Biochemistry , vol.38 , pp. 6537-6546
    • Lu, W.P.1    Sun, Y.2    Bauer, M.D.3    Paule, S.4    Koenigs, P.M.5    Kraft, W.G.6
  • 55
    • 34147160821 scopus 로고    scopus 로고
    • Anti-MRSA beta-lactams in development, with a focus on ceftobiprole: The first anti-MRSA beta-lactam to demonstrate clinical efficacy
    • Bush K, Heep M, Macielag MJ, Noel GJ, (2007) Anti-MRSA beta-lactams in development, with a focus on ceftobiprole: the first anti-MRSA beta-lactam to demonstrate clinical efficacy. Expert Opin Investig Drugs 16: 419-429.
    • (2007) Expert Opin Investig Drugs , vol.16 , pp. 419-429
    • Bush, K.1    Heep, M.2    Macielag, M.J.3    Noel, G.J.4
  • 56
    • 37149012591 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of ceftobiprole, an anti-MRSA cephalosporin with broad-spectrum activity
    • Murthy B, Schmitt-Hoffmann A, (2008) Pharmacokinetics and pharmacodynamics of ceftobiprole, an anti-MRSA cephalosporin with broad-spectrum activity. Clin Pharmacokinet 47: 21-33.
    • (2008) Clin Pharmacokinet , vol.47 , pp. 21-33
    • Murthy, B.1    Schmitt-Hoffmann, A.2
  • 57
    • 35948961490 scopus 로고    scopus 로고
    • Interactions of ceftobiprole with beta-lactamases from molecular classes A to D
    • Queenan AM, Shang W, Kania M, Page MG, Bush K, (2007) Interactions of ceftobiprole with beta-lactamases from molecular classes A to D. Antimicrob Agents Chemother 51: 3089-3095.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3089-3095
    • Queenan, A.M.1    Shang, W.2    Kania, M.3    Page, M.G.4    Bush, K.5
  • 58
    • 4344660156 scopus 로고    scopus 로고
    • Cephalosporins in clinical development
    • Page MG, (2004) Cephalosporins in clinical development. Expert Opin Investig Drugs 13: 973-985.
    • (2004) Expert Opin Investig Drugs , vol.13 , pp. 973-985
    • Page, M.G.1
  • 59
    • 84866344574 scopus 로고    scopus 로고
    • Structural insights into the anti-methicillin-resistant Staphylococcus aureus (MRSA) activity of ceftobiprole
    • Lovering AL, Gretes MC, Safadi SS, Danel F, de Castro L, Page MG, Strynadka NC, (2012) Structural insights into the anti-methicillin-resistant Staphylococcus aureus (MRSA) activity of ceftobiprole. J Biol Chem 287: 32096-32102.
    • (2012) J Biol Chem , vol.287 , pp. 32096-32102
    • Lovering, A.L.1    Gretes, M.C.2    Safadi, S.S.3    Danel, F.4    De Castro, L.5    Page, M.G.6    Strynadka, N.C.7
  • 60
    • 64049102289 scopus 로고    scopus 로고
    • Binding of small-molecule ligands to proteins: "what you see" is not always "what you get
    • Mobley DL, Dill KA, (2009) Binding of small-molecule ligands to proteins: "what you see" is not always "what you get ". Structure 17: 489-498.
    • (2009) Structure , vol.17 , pp. 489-498
    • Mobley, D.L.1    Dill, K.A.2
  • 61
    • 0032526053 scopus 로고    scopus 로고
    • Reaction of soluble penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus with beta-lactams and acyclic substrates: Kinetics in homogeneous solution
    • Graves-Woodward K, Pratt RF, (1998) Reaction of soluble penicillin-binding protein 2a of methicillin-resistant Staphylococcus aureus with beta-lactams and acyclic substrates: kinetics in homogeneous solution. Biochem J 332: 755-761.
    • (1998) Biochem J , vol.332 , pp. 755-761
    • Graves-Woodward, K.1    Pratt, R.F.2
  • 62
    • 47749154496 scopus 로고    scopus 로고
    • Co-opting the cell wall in fighting methicillin-resistant Staphylococcus aureus: Potent inhibition of PBP 2a by two anti-MRSA beta-lactam antibiotics
    • Villegas-Estrada A, Lee M, Hesek D, Vakulenko SB, Mobashery S, (2008) Co-opting the cell wall in fighting methicillin-resistant Staphylococcus aureus: potent inhibition of PBP 2a by two anti-MRSA beta-lactam antibiotics. J Am Chem Soc 130: 9212-9213.
    • (2008) J Am Chem Soc , vol.130 , pp. 9212-9213
    • Villegas-Estrada, A.1    Lee, M.2    Hesek, D.3    Vakulenko, S.B.4    Mobashery, S.5
  • 64
    • 79953848771 scopus 로고    scopus 로고
    • Ceftaroline: A novel cephalosporin with activity against methicillin-resistant Staphylococcus aureus
    • Saravolatz LD, Stein GE, Johnson LB, (2011) Ceftaroline: a novel cephalosporin with activity against methicillin-resistant Staphylococcus aureus. Clin Infect Dis 52: 1156-1163.
    • (2011) Clin Infect Dis , vol.52 , pp. 1156-1163
    • Saravolatz, L.D.1    Stein, G.E.2    Johnson, L.B.3
  • 65
    • 77952578858 scopus 로고    scopus 로고
    • Binding of ceftaroline to penicillin-binding proteins of Staphylococcus aureus and Streptococcus pneumoniae
    • Moisan H, Pruneau M, Malouin F, (2010) Binding of ceftaroline to penicillin-binding proteins of Staphylococcus aureus and Streptococcus pneumoniae. J Antimicrob Chemother 65: 713-716.
    • (2010) J Antimicrob Chemother , vol.65 , pp. 713-716
    • Moisan, H.1    Pruneau, M.2    Malouin, F.3
  • 66
    • 25844432417 scopus 로고    scopus 로고
    • In vitro and in vivo antibacterial activities of SM-216601, a new broad-spectrum parenteral carbapenem
    • Ueda Y, Kanazawa K, Eguchi K, Takemoto K, Eriguchi Y, Sunagawa M, (2005) In vitro and in vivo antibacterial activities of SM-216601, a new broad-spectrum parenteral carbapenem. Antimicrob Agents Chemother 49: 4185-4196.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4185-4196
    • Ueda, Y.1    Kanazawa, K.2    Eguchi, K.3    Takemoto, K.4    Eriguchi, Y.5    Sunagawa, M.6
  • 68
    • 33748685267 scopus 로고    scopus 로고
    • Successful therapy of experimental endocarditis caused by vancomycin-resistant Staphylococcus aureus with a combination of vancomycin and beta-lactam antibiotics
    • Fox PM, Lampen RJ, Stumpf KS, Archer GL, Climo MW, (2006) Successful therapy of experimental endocarditis caused by vancomycin-resistant Staphylococcus aureus with a combination of vancomycin and beta-lactam antibiotics. Antimicrob Agents Chemother 50: 2951-2956.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 2951-2956
    • Fox, P.M.1    Lampen, R.J.2    Stumpf, K.S.3    Archer, G.L.4    Climo, M.W.5
  • 69
    • 84891510686 scopus 로고    scopus 로고
    • Beta-Lactams enhance vancomycin activity against methicillin-resistant Staphylococcus aureus bacteremia compared to vancomycin alone
    • Dilworth TJ, Ibrahim O, Hall P, Sliwinski J, Walraven C, Mercier RC, (2013) beta-Lactams enhance vancomycin activity against methicillin-resistant Staphylococcus aureus bacteremia compared to vancomycin alone. Antimicrob Agents Chemother 58: 102-109.
    • (2013) Antimicrob Agents Chemother , vol.58 , pp. 102-109
    • Dilworth, T.J.1    Ibrahim, O.2    Hall, P.3    Sliwinski, J.4    Walraven, C.5    Mercier, R.C.6
  • 71
    • 84857175339 scopus 로고    scopus 로고
    • Antistaphylococcal activity of TD-1792, a multivalent glycopeptide-cephalosporin antibiotic
    • Blais J, Lewis SR, Krause KM, Benton BM, (2011) Antistaphylococcal activity of TD-1792, a multivalent glycopeptide-cephalosporin antibiotic. Antimicrob Agents Chemother 56: 1584-1587.
    • (2011) Antimicrob Agents Chemother , vol.56 , pp. 1584-1587
    • Blais, J.1    Lewis, S.R.2    Krause, K.M.3    Benton, B.M.4
  • 74
    • 75749150190 scopus 로고    scopus 로고
    • Interaction of ceftobiprole with the low-affinity PBP 5 of Enterococcus faecium
    • Henry X, Amoroso A, Coyette J, Joris B, (2010) Interaction of ceftobiprole with the low-affinity PBP 5 of Enterococcus faecium. Antimicrob Agents Chemother 54: 953-955.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 953-955
    • Henry, X.1    Amoroso, A.2    Coyette, J.3    Joris, B.4
  • 75
    • 84862244127 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: The evolution of antimicrobial resistance to beta-lactams, fluoroquinolones and macrolides
    • Cornick JE, Bentley SD, (2012) Streptococcus pneumoniae: the evolution of antimicrobial resistance to beta-lactams, fluoroquinolones and macrolides. Microbes Infect 14: 573-583.
    • (2012) Microbes Infect , vol.14 , pp. 573-583
    • Cornick, J.E.1    Bentley, S.D.2
  • 76
    • 0031940944 scopus 로고    scopus 로고
    • Mosaic genes and their role in penicillin-resistant Streptococcus pneumoniae
    • Hakenbeck R, (1998) Mosaic genes and their role in penicillin-resistant Streptococcus pneumoniae. Electrophoresis 19: 597-601.
    • (1998) Electrophoresis , vol.19 , pp. 597-601
    • Hakenbeck, R.1
  • 77
    • 0242666312 scopus 로고    scopus 로고
    • The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains
    • Chesnel L, Pernot L, Lemaire D, Champelovier D, Croizé J, Dideberg O, Vernet T, Zapun A, (2003) The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains. J Biol Chem 278: 44448-44456.
    • (2003) J Biol Chem , vol.278 , pp. 44448-44456
    • Chesnel, L.1    Pernot, L.2    Lemaire, D.3    Champelovier, D.4    Croizé, J.5    Dideberg, O.6    Vernet, T.7    Zapun, A.8
  • 78
    • 79959189164 scopus 로고    scopus 로고
    • Is Neisseria gonorrhoeae initiating a future era of untreatable gonorrhea?: Detailed characterization of the first strain with high-level resistance to ceftriaxone
    • Ohnishi M, Golparian D, Shimuta K, Saika T, Hoshina S, Iwasaku K, Nakayama S, Kitawaki J, Unemo M, (2011) Is Neisseria gonorrhoeae initiating a future era of untreatable gonorrhea?: detailed characterization of the first strain with high-level resistance to ceftriaxone. Antimicrob Agents Chemother 55: 3538-3545.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 3538-3545
    • Ohnishi, M.1    Golparian, D.2    Shimuta, K.3    Saika, T.4    Hoshina, S.5    Iwasaku, K.6    Nakayama, S.7    Kitawaki, J.8    Unemo, M.9
  • 81
    • 84867184096 scopus 로고    scopus 로고
    • Adaptive and mutational resistance: Role of porins and efflux pumps in drug resistance
    • Fernandez L, Hancock RE, (2012) Adaptive and mutational resistance: role of porins and efflux pumps in drug resistance. Clin Microbiol Rev 25: 661-681.
    • (2012) Clin Microbiol Rev , vol.25 , pp. 661-681
    • Fernandez, L.1    Hancock, R.E.2
  • 82
    • 0019814049 scopus 로고
    • Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin
    • Harder KJ, Nikaido H, Matsuhashi M, (1981) Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin. Antimicrob Agents Chemother 20: 549-552.
    • (1981) Antimicrob Agents Chemother , vol.20 , pp. 549-552
    • Harder, K.J.1    Nikaido, H.2    Matsuhashi, M.3
  • 84
    • 2942722257 scopus 로고    scopus 로고
    • Insertional inactivation of oprD in clinical isolates of Pseudomonas aeruginosa leading to carbapenem resistance
    • Wolter DJ, Hanson ND, Lister PD, (2004) Insertional inactivation of oprD in clinical isolates of Pseudomonas aeruginosa leading to carbapenem resistance. FEMS Microbiol Lett 236: 137-143.
    • (2004) FEMS Microbiol Lett , vol.236 , pp. 137-143
    • Wolter, D.J.1    Hanson, N.D.2    Lister, P.D.3
  • 85
    • 0032959773 scopus 로고    scopus 로고
    • Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids
    • Ochs MM, McCusker MP, Bains M, Hancock RE, (1999) Negative regulation of the Pseudomonas aeruginosa outer membrane porin OprD selective for imipenem and basic amino acids. Antimicrob Agents Chemother 43: 1085-1090.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 1085-1090
    • Ochs, M.M.1    McCusker, M.P.2    Bains, M.3    Hancock, R.E.4
  • 86
    • 0029892737 scopus 로고    scopus 로고
    • The role of specific surface loop regions in determining the function of the imipenem-specific pore protein OprD of Pseudomonas aeruginosa
    • Huang H, Hancock RE, (1996) The role of specific surface loop regions in determining the function of the imipenem-specific pore protein OprD of Pseudomonas aeruginosa. J Bacteriol 178: 3085-3090.
    • (1996) J Bacteriol , vol.178 , pp. 3085-3090
    • Huang, H.1    Hancock, R.E.2
  • 88
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: An archetype for microbial iron transport
    • Raymond KN, Dertz EA, Kim SS, (2003) Enterobactin: an archetype for microbial iron transport. Proc Natl Acad Sci USA 100: 3584-3588.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 89
    • 67651247638 scopus 로고    scopus 로고
    • Siderophores as drug delivery agents: Application of the "trojan Horse" strategy
    • Mollmann U, Heinisch L, Bauernfeind A, Kohler T, Ankel-Fuchs D, (2009) Siderophores as drug delivery agents: application of the "Trojan Horse" strategy. Biometals 22: 615-624.
    • (2009) Biometals , vol.22 , pp. 615-624
    • Mollmann, U.1    Heinisch, L.2    Bauernfeind, A.3    Kohler, T.4    Ankel-Fuchs, D.5
  • 90
    • 84931074436 scopus 로고    scopus 로고
    • Diverging roles of bacterial siderophores during infection
    • Holden VI, Bachman MA, (2015) Diverging roles of bacterial siderophores during infection. Metallomics 7: 986-995.
    • (2015) Metallomics , vol.7 , pp. 986-995
    • Holden, V.I.1    Bachman, M.A.2
  • 91
    • 84867155796 scopus 로고    scopus 로고
    • Structure, function and binding selectivity and stereoselectivity of siderophore-iron outer membrane transporters
    • Schalk IJ, Mislin GL, Brillet K, (2012) Structure, function and binding selectivity and stereoselectivity of siderophore-iron outer membrane transporters. Curr Top Membr 69: 37-66.
    • (2012) Curr Top Membr , vol.69 , pp. 37-66
    • Schalk, I.J.1    Mislin, G.L.2    Brillet, K.3
  • 94
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: Implications for the transport cycle
    • Chimento DP, Kadner RJ, Wiener MC, (2005) Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins 59: 240-251.
    • (2005) Proteins , vol.59 , pp. 240-251
    • Chimento, D.P.1    Kadner, R.J.2    Wiener, M.C.3
  • 95
    • 33744725409 scopus 로고
    • Recent studies on albomycin, a new antibiotic
    • Gause GF, (1955) Recent studies on albomycin, a new antibiotic. Br Med J 2: 1177-1179.
    • (1955) Br Med J , vol.2 , pp. 1177-1179
    • Gause, G.F.1
  • 97
    • 0029094662 scopus 로고
    • Salmycin A-D, Antibiotika aus Streptomyces violaceus, DSM 8286, mit Siderophor-Aminoglycosid-Struktur
    • Vértesy L, Aretz W, Fehlhaber H-W, Kogler H, (1995) Salmycin A-D, Antibiotika aus Streptomyces violaceus, DSM 8286, mit Siderophor-Aminoglycosid-Struktur. Helvetica Chim Acta 78: 46-60.
    • (1995) Helvetica Chim Acta , vol.78 , pp. 46-60
    • Vértesy, L.1    Aretz, W.2    Fehlhaber, H.-W.3    Kogler, H.4
  • 98
    • 84872850695 scopus 로고    scopus 로고
    • Siderophore conjugates
    • Page MG, (2013) Siderophore conjugates. Ann N Y Acad Sci 1277: 115-126.
    • (2013) Ann N y Acad Sci , vol.1277 , pp. 115-126
    • Page, M.G.1
  • 99
    • 84896879592 scopus 로고    scopus 로고
    • Siderophore-dependent iron uptake systems as gates for antibiotic Trojan horse strategies against Pseudomonas aeruginosa
    • Mislin GL, Schalk IJ, (2014) Siderophore-dependent iron uptake systems as gates for antibiotic Trojan horse strategies against Pseudomonas aeruginosa. Metallomics 6: 408-420.
    • (2014) Metallomics , vol.6 , pp. 408-420
    • Mislin, G.L.1    Schalk, I.J.2
  • 100
    • 84886803095 scopus 로고    scopus 로고
    • Antibiotics in the clinical pipeline in 2013
    • Butler MS, Blaskovich MA, Cooper MA, (2013) Antibiotics in the clinical pipeline in 2013. J Antibiot 66: 571-591.
    • (2013) J Antibiot , vol.66 , pp. 571-591
    • Butler, M.S.1    Blaskovich, M.A.2    Cooper, M.A.3
  • 101
    • 84877127230 scopus 로고    scopus 로고
    • Combined effects of the siderophore monosulfactam BAL30072 and carbapenems on multidrug-resistant Gram-negative bacilli
    • Hofer B, Dantier C, Gebhardt K, Desarbre E, Schmitt-Hoffmann A, Page MG, (2013) Combined effects of the siderophore monosulfactam BAL30072 and carbapenems on multidrug-resistant Gram-negative bacilli. J Antimicrob Chemother 68: 1120-1129.
    • (2013) J Antimicrob Chemother , vol.68 , pp. 1120-1129
    • Hofer, B.1    Dantier, C.2    Gebhardt, K.3    Desarbre, E.4    Schmitt-Hoffmann, A.5    Page, M.G.6
  • 102
    • 84859602519 scopus 로고    scopus 로고
    • In vitro activity of the siderophore monosulfactam BAL30072 against meropenem-non-susceptible Acinetobacter baumannii
    • Higgins PG, Stefanik D, Page MG, Hackel M, Seifert H, (2012) In vitro activity of the siderophore monosulfactam BAL30072 against meropenem-non-susceptible Acinetobacter baumannii. J Antimicrob Chemother 67: 1167-1169.
    • (2012) J Antimicrob Chemother , vol.67 , pp. 1167-1169
    • Higgins, P.G.1    Stefanik, D.2    Page, M.G.3    Hackel, M.4    Seifert, H.5
  • 103
    • 77950215859 scopus 로고    scopus 로고
    • Activity of the siderophore monobactam BAL30072 against multiresistant non-fermenters
    • Mushtaq S, Warner M, Livermore D, (2010) Activity of the siderophore monobactam BAL30072 against multiresistant non-fermenters. J Antimicrob Chemother 65: 266-270.
    • (2010) J Antimicrob Chemother , vol.65 , pp. 266-270
    • Mushtaq, S.1    Warner, M.2    Livermore, D.3
  • 105
    • 84856729230 scopus 로고    scopus 로고
    • Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria
    • Nikaido H, Pages JM, (2012) Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria. FEMS Microbiol Rev 36: 340-363.
    • (2012) FEMS Microbiol Rev , vol.36 , pp. 340-363
    • Nikaido, H.1    Pages, J.M.2
  • 106
    • 84962044479 scopus 로고    scopus 로고
    • Sequential responses of bacteria to noxious agents (antibiotics) leading to accumulation of mutations and permanent resistance
    • Martins A, Spengler G, Molnar J, Amaral L, (2012) Sequential responses of bacteria to noxious agents (antibiotics) leading to accumulation of mutations and permanent resistance. Biochem Pharmacol 1: 104.
    • (2012) Biochem Pharmacol , vol.1 , pp. 104
    • Martins, A.1    Spengler, G.2    Molnar, J.3    Amaral, L.4
  • 107
    • 64649096369 scopus 로고    scopus 로고
    • Mechanisms of RND multidrug efflux pumps
    • Nikaido H, Takatsuka Y, (2009) Mechanisms of RND multidrug efflux pumps. Biochim Biophys Acta 1794: 769-781.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 769-781
    • Nikaido, H.1    Takatsuka, Y.2
  • 108
    • 0028067837 scopus 로고
    • Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: Resistance to tetracycline, chloramphenicol, and norfloxacin
    • Li XZ, Livermore DM, Nikaido H, (1994) Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: resistance to tetracycline, chloramphenicol, and norfloxacin. Antimicrob Agents Chemother 38: 1732-1741.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 1732-1741
    • Li, X.Z.1    Livermore, D.M.2    Nikaido, H.3
  • 113
    • 84937637657 scopus 로고    scopus 로고
    • Assembly and operation of bacterial tripartite multidrug efflux pumps
    • Du D, van Veen HW, Luisi BF, (2015) Assembly and operation of bacterial tripartite multidrug efflux pumps. Trends Microbiol 23: 311-319.
    • (2015) Trends Microbiol , vol.23 , pp. 311-319
    • Du, D.1    Van Veen, H.W.2    Luisi, B.F.3
  • 114
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S, Nakashima R, Yamashita E, Yamaguchi A, (2002) Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419: 587-593.
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 115
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A, (2006) Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443: 173-179.
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 116
    • 64649100965 scopus 로고    scopus 로고
    • Drug transport mechanism of the AcrB efflux pump
    • Pos KM, (2009) Drug transport mechanism of the AcrB efflux pump. Biochim Biophys Acta 1794: 782-793.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 782-793
    • Pos, K.M.1
  • 117
  • 119
    • 33644833626 scopus 로고    scopus 로고
    • Conformational flexibility in the multidrug efflux system protein AcrA
    • Mikolosko J, Bobyk K, Zgurskaya HI, Ghosh P, (2006) Conformational flexibility in the multidrug efflux system protein AcrA. Structure 14: 577-587.
    • (2006) Structure , vol.14 , pp. 577-587
    • Mikolosko, J.1    Bobyk, K.2    Zgurskaya, H.I.3    Ghosh, P.4
  • 122
    • 0028314541 scopus 로고
    • Multidrug resistance pumps in bacteria: Variations on a theme
    • Lewis K, (1994) Multidrug resistance pumps in bacteria: variations on a theme. Trends Biochem Sci 19: 119-123.
    • (1994) Trends Biochem Sci , vol.19 , pp. 119-123
    • Lewis, K.1
  • 124
    • 0028050605 scopus 로고
    • Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: Active efflux as a contributing factor to beta-lactam resistance
    • Li XZ, Ma D, Livermore DM, Nikaido H, (1994) Role of efflux pump(s) in intrinsic resistance of Pseudomonas aeruginosa: active efflux as a contributing factor to beta-lactam resistance. Antimicrob Agents Chemother 38: 1742-1752.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 1742-1752
    • Li, X.Z.1    Ma, D.2    Livermore, D.M.3    Nikaido, H.4
  • 125
    • 23044458428 scopus 로고    scopus 로고
    • Contribution of acquired carbapenem-hydrolyzing oxacillinases to carbapenem resistance in Acinetobacter baumannii
    • Heritier C, Poirel L, Lambert T, Nordmann P, (2005) Contribution of acquired carbapenem-hydrolyzing oxacillinases to carbapenem resistance in Acinetobacter baumannii. Antimicrob Agents Chemother 49: 3198-3202.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 3198-3202
    • Heritier, C.1    Poirel, L.2    Lambert, T.3    Nordmann, P.4
  • 126
    • 2142827105 scopus 로고    scopus 로고
    • Genetic and molecular characterization of beta-lactamase-negative ampicillin-resistant Haemophilus influenzae with unusually high resistance to ampicillin
    • Kaczmarek FS, Gootz TD, Dib-Hajj F, Shang W, Hallowell S, Cronan M, (2004) Genetic and molecular characterization of beta-lactamase-negative ampicillin-resistant Haemophilus influenzae with unusually high resistance to ampicillin. Antimicrob Agents Chemother 48: 1630-1639.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 1630-1639
    • Kaczmarek, F.S.1    Gootz, T.D.2    Dib-Hajj, F.3    Shang, W.4    Hallowell, S.5    Cronan, M.6
  • 128
    • 84908457716 scopus 로고    scopus 로고
    • Bacterial multidrug efflux pumps: Mechanisms, physiology and pharmacological exploitations
    • Sun J, Deng Z, Yan A, (2014) Bacterial multidrug efflux pumps: mechanisms, physiology and pharmacological exploitations. Biochem Biophys Res Commun 453: 254-267.
    • (2014) Biochem Biophys Res Commun , vol.453 , pp. 254-267
    • Sun, J.1    Deng, Z.2    Yan, A.3
  • 129
    • 84930947877 scopus 로고    scopus 로고
    • RND-type drug efflux pumps from Gram-negative bacteria: Molecular mechanism and inhibition
    • Venter H, Mowla R, Ohene-Agyei T, Ma S, (2015) RND-type drug efflux pumps from Gram-negative bacteria: molecular mechanism and inhibition. Front Microbiol 6: 377.
    • (2015) Front Microbiol , vol.6 , pp. 377
    • Venter, H.1    Mowla, R.2    Ohene-Agyei, T.3    Ma, S.4
  • 131
    • 2942615162 scopus 로고    scopus 로고
    • Detection and prevalence of active drug efflux mechanism in various multidrug-resistant Klebsiella pneumoniae strains from Turkey
    • Hasdemir UO, Chevalier J, Nordmann P, Pages JM, (2004) Detection and prevalence of active drug efflux mechanism in various multidrug-resistant Klebsiella pneumoniae strains from Turkey. J Clin Microbiol 42: 2701-2706.
    • (2004) J Clin Microbiol , vol.42 , pp. 2701-2706
    • Hasdemir, U.O.1    Chevalier, J.2    Nordmann, P.3    Pages, J.M.4
  • 132
    • 0034425544 scopus 로고    scopus 로고
    • High-level fluoroquinolone-resistant clinical isolates of Escherichia coli overproduce multidrug efflux protein AcrA
    • Mazzariol A, Tokue Y, Kanegawa TM, Cornaglia G, Nikaido H, (2000) High-level fluoroquinolone-resistant clinical isolates of Escherichia coli overproduce multidrug efflux protein AcrA. Antimicrob Agents Chemother 44: 3441-3443.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 3441-3443
    • Mazzariol, A.1    Tokue, Y.2    Kanegawa, T.M.3    Cornaglia, G.4    Nikaido, H.5
  • 134
    • 79151471178 scopus 로고    scopus 로고
    • Effect of 1-(1-Naphtylmethyl)-piperazine, an efflux pump inhibitor, on antimicrobial drug susceptibilities of clinical Acinetobacter baumannii isolates
    • Coban AY, Guney AK, Tanriverdi Cayci Y, Durupinar B, (2011) Effect of 1-(1-Naphtylmethyl)-piperazine, an efflux pump inhibitor, on antimicrobial drug susceptibilities of clinical Acinetobacter baumannii isolates. Curr Microbiol 62: 508-511.
    • (2011) Curr Microbiol , vol.62 , pp. 508-511
    • Coban, A.Y.1    Guney, A.K.2    Tanriverdi Cayci, Y.3    Durupinar, B.4
  • 135
    • 12944316448 scopus 로고    scopus 로고
    • Selected arylpiperazines are capable of reversing multidrug resistance in Escherichia coli overexpressing RND efflux pumps
    • Bohnert JA, Kern WV, (2005) Selected arylpiperazines are capable of reversing multidrug resistance in Escherichia coli overexpressing RND efflux pumps. Antimicrob Agents Chemother 49: 849-852.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 849-852
    • Bohnert, J.A.1    Kern, W.V.2
  • 136
    • 31544464121 scopus 로고    scopus 로고
    • Effect of 1-(1-naphthylmethyl)-piperazine, a novel putative efflux pump inhibitor, on antimicrobial drug susceptibility in clinical isolates of Enterobacteriaceae other than Escherichia coli
    • Schumacher A, Steinke P, Bohnert JA, Akova M, Jonas D, Kern WV, (2006) Effect of 1-(1-naphthylmethyl)-piperazine, a novel putative efflux pump inhibitor, on antimicrobial drug susceptibility in clinical isolates of Enterobacteriaceae other than Escherichia coli. J Antimicrob Chemother 57: 344-348.
    • (2006) J Antimicrob Chemother , vol.57 , pp. 344-348
    • Schumacher, A.1    Steinke, P.2    Bohnert, J.A.3    Akova, M.4    Jonas, D.5    Kern, W.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.