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Volumn 7, Issue 12, 2012, Pages

Non-Traditional Antibacterial Screening Approaches for the Identification of Novel Inhibitors of the Glyoxylate Shunt in Gram-Negative Pathogens

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; GLYOXYLIC ACID;

EID: 84871156127     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0051732     Document Type: Article
Times cited : (43)

References (39)
  • 1
    • 0030624532 scopus 로고    scopus 로고
    • Antibiotic resistance: an ecological imbalance
    • discussion 9-14
    • Levy SB (1997) Antibiotic resistance: an ecological imbalance. Ciba Found Symp 207: 1-9; discussion 9-14.
    • (1997) Ciba Found Symp , vol.207 , pp. 1-9
    • Levy, S.B.1
  • 2
    • 0033653688 scopus 로고    scopus 로고
    • The impact of antibiotic use on resistance development and persistence
    • Barbosa TM, Levy SB, (2000) The impact of antibiotic use on resistance development and persistence. Drug Resist Updat 3: 303-311.
    • (2000) Drug Resist Updat , vol.3 , pp. 303-311
    • Barbosa, T.M.1    Levy, S.B.2
  • 3
    • 57749107808 scopus 로고    scopus 로고
    • Bad bugs, no drugs: no ESKAPE! An update from the Infectious Diseases Society of America
    • Boucher HW, Talbot GH, Bradley JS, Edwards JE, Gilbert D, et al. (2009) Bad bugs, no drugs: no ESKAPE! An update from the Infectious Diseases Society of America. Clin Infect Dis 48: 1-12.
    • (2009) Clin Infect Dis , vol.48 , pp. 1-12
    • Boucher, H.W.1    Talbot, G.H.2    Bradley, J.S.3    Edwards, J.E.4    Gilbert, D.5
  • 4
    • 78751477224 scopus 로고    scopus 로고
    • Challenges of antibacterial discovery
    • Silver LL, (2011) Challenges of antibacterial discovery. Clin Microbiol Rev 24: 71-109.
    • (2011) Clin Microbiol Rev , vol.24 , pp. 71-109
    • Silver, L.L.1
  • 5
  • 6
    • 0035804157 scopus 로고    scopus 로고
    • Design and evaluation of pilicides: potential novel antibacterial agents directed against uropathogenic Escherichia coli
    • Svensson A, Larsson A, Emtenas H, Hedenstrom M, Fex T, et al. (2001) Design and evaluation of pilicides: potential novel antibacterial agents directed against uropathogenic Escherichia coli. Chembiochem 2: 915-918.
    • (2001) Chembiochem , vol.2 , pp. 915-918
    • Svensson, A.1    Larsson, A.2    Emtenas, H.3    Hedenstrom, M.4    Fex, T.5
  • 7
    • 0028947038 scopus 로고
    • A phase I study of chemically synthesized verotoxin (Shiga-like toxin) Pk-trisaccharide receptors attached to chromosorb for preventing hemolytic-uremic syndrome
    • Armstrong GD, Rowe PC, Goodyer P, Orrbine E, Klassen TP, et al. (1995) A phase I study of chemically synthesized verotoxin (Shiga-like toxin) Pk-trisaccharide receptors attached to chromosorb for preventing hemolytic-uremic syndrome. J Infect Dis 171: 1042-1045.
    • (1995) J Infect Dis , vol.171 , pp. 1042-1045
    • Armstrong, G.D.1    Rowe, P.C.2    Goodyer, P.3    Orrbine, E.4    Klassen, T.P.5
  • 9
    • 77955474327 scopus 로고    scopus 로고
    • Synthesis and bacterial biofilm inhibition studies of ethyl N-(2-phenethyl) carbamate derivatives
    • Rogers SA, Whitehead DC, Mullikin T, Melander C, (2010) Synthesis and bacterial biofilm inhibition studies of ethyl N-(2-phenethyl) carbamate derivatives. Org Biomol Chem 8: 3857-3859.
    • (2010) Org Biomol Chem , vol.8 , pp. 3857-3859
    • Rogers, S.A.1    Whitehead, D.C.2    Mullikin, T.3    Melander, C.4
  • 10
    • 0037256665 scopus 로고    scopus 로고
    • Induction and inhibition of Pseudomonas aeruginosa quorum sensing by synthetic autoinducer analogs
    • Smith KM, Bu Y, Suga H, (2003) Induction and inhibition of Pseudomonas aeruginosa quorum sensing by synthetic autoinducer analogs. Chem Biol 10: 81-89.
    • (2003) Chem Biol , vol.10 , pp. 81-89
    • Smith, K.M.1    Bu, Y.2    Suga, H.3
  • 11
    • 0041989633 scopus 로고    scopus 로고
    • Attenuation of Pseudomonas aeruginosa virulence by quorum sensing inhibitors
    • Hentzer M, Wu H, Andersen JB, Riedel K, Rasmussen TB, et al. (2003) Attenuation of Pseudomonas aeruginosa virulence by quorum sensing inhibitors. EMBO J 22: 3803-3815.
    • (2003) EMBO J , vol.22 , pp. 3803-3815
    • Hentzer, M.1    Wu, H.2    Andersen, J.B.3    Riedel, K.4    Rasmussen, T.B.5
  • 12
    • 84865768680 scopus 로고    scopus 로고
    • In vivo-validated essential genes identified in Acinetobacter baumannii by using human ascites overlap poorly with essential genes detected on laboratory media
    • Umland TC, Schultz LW, MacDonald U, Beanan JM, Olson R, et al. (2012) In vivo-validated essential genes identified in Acinetobacter baumannii by using human ascites overlap poorly with essential genes detected on laboratory media. MBio 3.
    • (2012) MBio , vol.3
    • Umland, T.C.1    Schultz, L.W.2    MacDonald, U.3    Beanan, J.M.4    Olson, R.5
  • 13
    • 44349103106 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa twitching motility-mediated chemotaxis towards phospholipids and fatty acids: specificity and metabolic requirements
    • Miller RM, Tomaras AP, Barker AP, Voelker DR, Chan ED, et al. (2008) Pseudomonas aeruginosa twitching motility-mediated chemotaxis towards phospholipids and fatty acids: specificity and metabolic requirements. J Bacteriol 190: 4038-4049.
    • (2008) J Bacteriol , vol.190 , pp. 4038-4049
    • Miller, R.M.1    Tomaras, A.P.2    Barker, A.P.3    Voelker, D.R.4    Chan, E.D.5
  • 14
    • 62649094413 scopus 로고    scopus 로고
    • Transmembrane passage of hydrophobic compounds through a protein channel wall
    • Hearn EM, Patel DR, Lepore BW, Indic M, van den Berg B, (2009) Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 458: 367-370.
    • (2009) Nature , vol.458 , pp. 367-370
    • Hearn, E.M.1    Patel, D.R.2    Lepore, B.W.3    Indic, M.4    van den Berg, B.5
  • 15
    • 0028058149 scopus 로고
    • Molecular and biochemical analyses of fatty acid transport, metabolism, and gene regulation in Escherichia coli
    • Black PN, DiRusso CC, (1994) Molecular and biochemical analyses of fatty acid transport, metabolism, and gene regulation in Escherichia coli. Biochim Biophys Acta 1210: 123-145.
    • (1994) Biochim Biophys Acta , vol.1210 , pp. 123-145
    • Black, P.N.1    DiRusso, C.C.2
  • 16
    • 25644448726 scopus 로고    scopus 로고
    • Multidrug resistance in Klebsiella pneumoniae MGH78578 and cloning of genes responsible for the resistance
    • Ogawa W, Li DW, Yu P, Begum A, Mizushima T, et al. (2005) Multidrug resistance in Klebsiella pneumoniae MGH78578 and cloning of genes responsible for the resistance. Biol Pharm Bull 28: 1505-1508.
    • (2005) Biol Pharm Bull , vol.28 , pp. 1505-1508
    • Ogawa, W.1    Li, D.W.2    Yu, P.3    Begum, A.4    Mizushima, T.5
  • 18
    • 0029061955 scopus 로고
    • An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosa
    • Schweizer HP, Hoang TT, (1995) An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosa. Gene 158: 15-22.
    • (1995) Gene , vol.158 , pp. 15-22
    • Schweizer, H.P.1    Hoang, T.T.2
  • 19
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang TT, Karkhoff-Schweizer RR, Kutchma AJ, Schweizer HP, (1998) A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212: 77-86.
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 20
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski DH, Helinski DR, (1979) Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proceedings of the National Academy of Sciences 76: 1648-1652.
    • (1979) Proceedings of the National Academy of Sciences , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 21
    • 20144388608 scopus 로고    scopus 로고
    • Novel mouse model of chronic Pseudomonas aeruginosa lung infection mimicking cystic fibrosis
    • Hoffmann N, Rasmussen TB, Jensen PO, Stub C, Hentzer M, et al. (2005) Novel mouse model of chronic Pseudomonas aeruginosa lung infection mimicking cystic fibrosis. Infect Immun 73: 2504-2514.
    • (2005) Infect Immun , vol.73 , pp. 2504-2514
    • Hoffmann, N.1    Rasmussen, T.B.2    Jensen, P.O.3    Stub, C.4    Hentzer, M.5
  • 22
    • 0020494578 scopus 로고
    • Inhibition of isocitrate lyase by 3-nitropropionate, a reaction-intermediate analogue
    • Schloss JV, Cleland WW, (1982) Inhibition of isocitrate lyase by 3-nitropropionate, a reaction-intermediate analogue. Biochemistry 21: 4420-4427.
    • (1982) Biochemistry , vol.21 , pp. 4420-4427
    • Schloss, J.V.1    Cleland, W.W.2
  • 23
    • 0033003760 scopus 로고    scopus 로고
    • A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays
    • Zhang JH, Chung TD, Oldenburg KR, (1999) A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J Biomol Screen 4: 67-73.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 24
    • 0017851838 scopus 로고
    • Isolation and characterization of isocitrate lyase from a thermophilic Bacillus sp
    • Chell RM, Sundaram TK, Wilkinson AE, (1978) Isolation and characterization of isocitrate lyase from a thermophilic Bacillus sp. Biochem J 173: 165-177.
    • (1978) Biochem J , vol.173 , pp. 165-177
    • Chell, R.M.1    Sundaram, T.K.2    Wilkinson, A.E.3
  • 25
    • 0027752066 scopus 로고
    • Purification of the glyoxylate cycle enzyme malate synthase from maize (Zea mays L.) and characterization of a proteolytic fragment
    • Khan AS, Van Driessche E, Kanarek L, Beeckmans S, (1993) Purification of the glyoxylate cycle enzyme malate synthase from maize (Zea mays L.) and characterization of a proteolytic fragment. Protein Expr Purif 4: 519-528.
    • (1993) Protein Expr Purif , vol.4 , pp. 519-528
    • Khan, A.S.1    van Driessche, E.2    Kanarek, L.3    Beeckmans, S.4
  • 27
    • 0037449771 scopus 로고    scopus 로고
    • Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis
    • Smith CV, Huang CC, Miczak A, Russell DG, Sacchettini JC, et al. (2003) Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J Biol Chem 278: 1735-1743.
    • (2003) J Biol Chem , vol.278 , pp. 1735-1743
    • Smith, C.V.1    Huang, C.C.2    Miczak, A.3    Russell, D.G.4    Sacchettini, J.C.5
  • 29
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 30
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Luthy R, Eisenberg D, (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science 253: 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 31
    • 31544450787 scopus 로고    scopus 로고
    • Novel procedure for modeling ligand/receptor induced fit effects
    • Sherman W, Day T, Jacobson MP, Friesner RA, Farid R, (2006) Novel procedure for modeling ligand/receptor induced fit effects. J Med Chem 49: 534-553.
    • (2006) J Med Chem , vol.49 , pp. 534-553
    • Sherman, W.1    Day, T.2    Jacobson, M.P.3    Friesner, R.A.4    Farid, R.5
  • 32
    • 71049115075 scopus 로고    scopus 로고
    • Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis
    • Dunn MF, Ramirez-Trujillo JA, Hernandez-Lucas I, (2009) Major roles of isocitrate lyase and malate synthase in bacterial and fungal pathogenesis. Microbiology 155: 3166-3175.
    • (2009) Microbiology , vol.155 , pp. 3166-3175
    • Dunn, M.F.1    Ramirez-Trujillo, J.A.2    Hernandez-Lucas, I.3
  • 33
    • 33746481387 scopus 로고    scopus 로고
    • The product complex of M. tuberculosis malate synthase revisited
    • Anstrom DM, Remington SJ, (2006) The product complex of M. tuberculosis malate synthase revisited. Protein Sci 15: 2002-2007.
    • (2006) Protein Sci , vol.15 , pp. 2002-2007
    • Anstrom, D.M.1    Remington, S.J.2
  • 34
    • 0342794213 scopus 로고    scopus 로고
    • Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase
    • McKinney JD, Honer zu Bentrup K, Munoz-Elias EJ, Miczak A, Chen B, et al. (2000) Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 406: 735-738.
    • (2000) Nature , vol.406 , pp. 735-738
    • McKinney, J.D.1    Honer zu Bentrup, K.2    Munoz-Elias, E.J.3    Miczak, A.4    Chen, B.5
  • 35
    • 84859855723 scopus 로고    scopus 로고
    • Synthesis and characterization of pyruvate-isoniazid analogs and their copper complexes as potential ICL inhibitors
    • Shingnapurkar D, Dandawate P, Anson CE, Powell AK, Afrasiabi Z, et al. (2012) Synthesis and characterization of pyruvate-isoniazid analogs and their copper complexes as potential ICL inhibitors. Bioorg Med Chem Lett 22: 3172-3176.
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 3172-3176
    • Shingnapurkar, D.1    Dandawate, P.2    Anson, C.E.3    Powell, A.K.4    Afrasiabi, Z.5
  • 36
    • 48449102828 scopus 로고    scopus 로고
    • Virulence determinants from a cystic fibrosis isolate of Pseudomonas aeruginosa include isocitrate lyase
    • Lindsey TL, Hagins JM, Sokol PA, Silo-Suh LA, (2008) Virulence determinants from a cystic fibrosis isolate of Pseudomonas aeruginosa include isocitrate lyase. Microbiology 154: 1616-1627.
    • (2008) Microbiology , vol.154 , pp. 1616-1627
    • Lindsey, T.L.1    Hagins, J.M.2    Sokol, P.A.3    Silo-Suh, L.A.4
  • 37
    • 67650685860 scopus 로고    scopus 로고
    • Dynamics of adaptive microevolution of hypermutable Pseudomonas aeruginosa during chronic pulmonary infection in patients with cystic fibrosis
    • Hoboth C, Hoffmann R, Eichner A, Henke C, Schmoldt S, et al. (2009) Dynamics of adaptive microevolution of hypermutable Pseudomonas aeruginosa during chronic pulmonary infection in patients with cystic fibrosis. J Infect Dis 200: 118-130.
    • (2009) J Infect Dis , vol.200 , pp. 118-130
    • Hoboth, C.1    Hoffmann, R.2    Eichner, A.3    Henke, C.4    Schmoldt, S.5
  • 38
    • 79952228717 scopus 로고    scopus 로고
    • Malate synthase expression is deregulated in the Pseudomonas aeruginosa cystic fibrosis isolate FRD1
    • Hagins JM, Scoffield J, Suh SJ, Silo-Suh L, (2011) Malate synthase expression is deregulated in the Pseudomonas aeruginosa cystic fibrosis isolate FRD1. Can J Microbiol 57: 186-195.
    • (2011) Can J Microbiol , vol.57 , pp. 186-195
    • Hagins, J.M.1    Scoffield, J.2    Suh, S.J.3    Silo-Suh, L.4
  • 39
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski CA, Lombardo F, Dominy BW, Feeney PJ, (2001) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev 46: 3-26.
    • (2001) Adv Drug Deliv Rev , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4


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