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Volumn 201, Issue , 2015, Pages 2-14

Quorum quenching enzymes

Author keywords

Acylases; Lactonases; Oxidoreductases; Quorum quenching; Quorum sensing

Indexed keywords

AMINO ACIDS; BACTERIA; BIOCONTROL; BIODEGRADATION; BIOFILMS; BIOFOULING; BIOREACTORS; CROPS; DISEASE CONTROL; MOLECULES; QUENCHING;

EID: 84938611404     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.09.001     Document Type: Article
Times cited : (264)

References (134)
  • 1
    • 33751221972 scopus 로고    scopus 로고
    • The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase
    • Afriat L., Roodveldt C., Manco G., Tawfik D.S. The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase. Biochemistry 2006, 45:13677-13686.
    • (2006) Biochemistry , vol.45 , pp. 13677-13686
    • Afriat, L.1    Roodveldt, C.2    Manco, G.3    Tawfik, D.S.4
  • 2
    • 71049149587 scopus 로고    scopus 로고
    • Transgenic Amorphophallus konjac expressing synthesized acyl-homoserine lactonase (aiiA) gene exhibit enhanced resistance to soft rot disease
    • Ban H., Chai X., Lin Y., Zhou Y., Peng D., Zhou Y., Zou Y., Yu Z., Sun M. Transgenic Amorphophallus konjac expressing synthesized acyl-homoserine lactonase (aiiA) gene exhibit enhanced resistance to soft rot disease. Plant Cell Rep. 2009, 28:1847-1855.
    • (2009) Plant Cell Rep. , vol.28 , pp. 1847-1855
    • Ban, H.1    Chai, X.2    Lin, Y.3    Zhou, Y.4    Peng, D.5    Zhou, Y.6    Zou, Y.7    Yu, Z.8    Sun, M.9
  • 3
    • 84879271805 scopus 로고    scopus 로고
    • In planta biocontrol of Pectobacterium atrosepticum by Rhodococcus erythropolis involves silencing of pathogen communication by the rhodococcal gamma-lactone catabolic pathway
    • Barbey C., Crépin A., Bergeau D., Ouchiha A., Mijouin L., Taupin L., Orange N., Feuilloley M., Dufour A., Burini J.-F., Latour X. In planta biocontrol of Pectobacterium atrosepticum by Rhodococcus erythropolis involves silencing of pathogen communication by the rhodococcal gamma-lactone catabolic pathway. PLOS ONE 2013, 8(6):e66642.
    • (2013) PLOS ONE , vol.8 , Issue.6 , pp. e66642
    • Barbey, C.1    Crépin, A.2    Bergeau, D.3    Ouchiha, A.4    Mijouin, L.5    Taupin, L.6    Orange, N.7    Feuilloley, M.8    Dufour, A.9    Burini, J.-F.10    Latour, X.11
  • 5
    • 84882392687 scopus 로고    scopus 로고
    • The evolutionary origins of detoxifying enzymes: the mammalian serum paraoxonases (PONs) relate to bacterial homoserine lactonases
    • Bar-Rogovsky H., Hugenmatter A., Tawfik D.S. The evolutionary origins of detoxifying enzymes: the mammalian serum paraoxonases (PONs) relate to bacterial homoserine lactonases. J. Biol. Chem. 2013, 288:23914-23927.
    • (2013) J. Biol. Chem. , vol.288 , pp. 23914-23927
    • Bar-Rogovsky, H.1    Hugenmatter, A.2    Tawfik, D.S.3
  • 8
    • 76249128454 scopus 로고    scopus 로고
    • The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket
    • Bokhove M., Nadal Jimenez P., Quax W.J., Dijkstra B.W. The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:686-691.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 686-691
    • Bokhove, M.1    Nadal Jimenez, P.2    Quax, W.J.3    Dijkstra, B.W.4
  • 10
    • 84897939370 scopus 로고    scopus 로고
    • Effect of dietary N-acyl homoserine lactonase on the immune response and the gut microbiota of zebrafish, Danio rerio, infected with Aeromonas hydrophila
    • Cao Y., Liu Y., Mao W., Chen R., He S., Gao X., Zjou Z., Yao B. Effect of dietary N-acyl homoserine lactonase on the immune response and the gut microbiota of zebrafish, Danio rerio, infected with Aeromonas hydrophila. J. World Aquac. Soc. 2014, 45:149-162.
    • (2014) J. World Aquac. Soc. , vol.45 , pp. 149-162
    • Cao, Y.1    Liu, Y.2    Mao, W.3    Chen, R.4    He, S.5    Gao, X.6    Zjou, Z.7    Yao, B.8
  • 11
    • 0043030084 scopus 로고    scopus 로고
    • The Ti plasmid of Agrobacterium tumefaciens harbors an attM-paralogous gene, aiiB, also encoding N-acyl homoserine lactonase activity
    • Carlier A., Uroz S., Smadja B., Fray R., Latour X., Dessaux Y., Faure D. The Ti plasmid of Agrobacterium tumefaciens harbors an attM-paralogous gene, aiiB, also encoding N-acyl homoserine lactonase activity. Appl. Environ. Microbiol. 2003, 69:4989-4993.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4989-4993
    • Carlier, A.1    Uroz, S.2    Smadja, B.3    Fray, R.4    Latour, X.5    Dessaux, Y.6    Faure, D.7
  • 12
    • 79952353193 scopus 로고    scopus 로고
    • Characterization of N-acylhomoserine lactone-degrading bacteria associated with the Zingiber officinale (ginger) rhizosphere: co-existence of quorum quenching and quorum sensing in Acinetobacter and Burkholderia
    • Chan K.-G., Atkinson S., Mathee K., Sam C.-K., Chhabra S.R., Cámara M., Koh C.-L., Williams P. Characterization of N-acylhomoserine lactone-degrading bacteria associated with the Zingiber officinale (ginger) rhizosphere: co-existence of quorum quenching and quorum sensing in Acinetobacter and Burkholderia. BMC Microbiol. 2011, 11:51.
    • (2011) BMC Microbiol. , vol.11 , pp. 51
    • Chan, K.-G.1    Atkinson, S.2    Mathee, K.3    Sam, C.-K.4    Chhabra, S.R.5    Cámara, M.6    Koh, C.-L.7    Williams, P.8
  • 13
    • 66649089733 scopus 로고    scopus 로고
    • A probable aculeacin A acylase from the Ralstonia solanacearum GMI1000 is N-acyl-homoserine lactone acylase with quorum-quenching activity
    • Chen C.-N., Chen C.-J., Liao C.-T., Lee C.-Y. A probable aculeacin A acylase from the Ralstonia solanacearum GMI1000 is N-acyl-homoserine lactone acylase with quorum-quenching activity. BMC Microbiol. 2009, 9:89.
    • (2009) BMC Microbiol. , vol.9 , pp. 89
    • Chen, C.-N.1    Chen, C.-J.2    Liao, C.-T.3    Lee, C.-Y.4
  • 14
    • 77952447435 scopus 로고    scopus 로고
    • High yield expression of an AHL-lactonase from Bacillus sp. B546 in Pichia pastoris and its application to reduce Aeromonas hydrophila mortality in aquaculture
    • Chen R., Zhou Z., Cao Y., Bai Y., Yao B. High yield expression of an AHL-lactonase from Bacillus sp. B546 in Pichia pastoris and its application to reduce Aeromonas hydrophila mortality in aquaculture. Microb. Cell Fact. 2010, 9:39.
    • (2010) Microb. Cell Fact. , vol.9 , pp. 39
    • Chen, R.1    Zhou, Z.2    Cao, Y.3    Bai, Y.4    Yao, B.5
  • 15
    • 84893122077 scopus 로고    scopus 로고
    • Design of quorum quenching microbial vessel to enhance cell viability for biofouling control in membrane bioreactor
    • Cheong W.-S., Kim S.-R., Oh H.-S., Lee S.H., Yeon K.-M., Lee C.-H., Lee J.-K. Design of quorum quenching microbial vessel to enhance cell viability for biofouling control in membrane bioreactor. J. Microbiol. Biotechnol. 2014, 24:97-105.
    • (2014) J. Microbiol. Biotechnol. , vol.24 , pp. 97-105
    • Cheong, W.-S.1    Kim, S.-R.2    Oh, H.-S.3    Lee, S.H.4    Yeon, K.-M.5    Lee, C.-H.6    Lee, J.-K.7
  • 16
    • 84881452540 scopus 로고    scopus 로고
    • Isolation and identification of indigenous quorum quenching bacteria, Pseudomonas sp. 1A1, for biofouling control in MBR
    • Cheong W.-S., Lee C.-H., Moon Y.-H., Oh H.-S., Kim S.-R., Lee S.H., Lee C.-H., Lee J.-K. Isolation and identification of indigenous quorum quenching bacteria, Pseudomonas sp. 1A1, for biofouling control in MBR. Ind. Eng. Chem. Res. 2013, 52:10554-10560.
    • (2013) Ind. Eng. Chem. Res. , vol.52 , pp. 10554-10560
    • Cheong, W.-S.1    Lee, C.-H.2    Moon, Y.-H.3    Oh, H.-S.4    Kim, S.-R.5    Lee, S.H.6    Lee, C.-H.7    Lee, J.-K.8
  • 17
    • 33947257935 scopus 로고    scopus 로고
    • Interference of quorum sensing and virulence of the rice pathogen Burkholderia glumae by an engineered endophytic bacterium
    • Cho H.-S., Park S.-Y., Ryu C.-M., Kim J.F., Kim J.-G., Park S.-H. Interference of quorum sensing and virulence of the rice pathogen Burkholderia glumae by an engineered endophytic bacterium. FEMS Microbiol. Ecol. 2007, 60:14-23.
    • (2007) FEMS Microbiol. Ecol. , vol.60 , pp. 14-23
    • Cho, H.-S.1    Park, S.-Y.2    Ryu, C.-M.3    Kim, J.F.4    Kim, J.-G.5    Park, S.-H.6
  • 18
    • 66149192520 scopus 로고    scopus 로고
    • Directed evolution of a quorum-quenching lactonase from Mycobacterium avium subsp. paratuberculosis K-10 in the amidohydrolase superfamily
    • Chow J.Y., Wu L., Yew W.S. Directed evolution of a quorum-quenching lactonase from Mycobacterium avium subsp. paratuberculosis K-10 in the amidohydrolase superfamily. Biochemistry 2009, 48:4344-4353.
    • (2009) Biochemistry , vol.48 , pp. 4344-4353
    • Chow, J.Y.1    Wu, L.2    Yew, W.S.3
  • 19
    • 78650352337 scopus 로고    scopus 로고
    • Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily
    • Chow J.Y., Xue B., Lee K.H., Tung A., Wu L., Robinson R.C., Yew W.S. Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily. J. Biol. Chem. 2010, 285:40911-40920.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40911-40920
    • Chow, J.Y.1    Xue, B.2    Lee, K.H.3    Tung, A.4    Wu, L.5    Robinson, R.C.6    Yew, W.S.7
  • 21
    • 47249093153 scopus 로고    scopus 로고
    • A single mutation in P450BM-3 enhances acyl homoserine lactone:acyl homoserine substrate binding selectivity nearly 250-fold
    • Chowdhary P.K., Stewart L., Lopez C., Haines D.C. A single mutation in P450BM-3 enhances acyl homoserine lactone:acyl homoserine substrate binding selectivity nearly 250-fold. J. Biotechnol. 2008, 135:374-376.
    • (2008) J. Biotechnol. , vol.135 , pp. 374-376
    • Chowdhary, P.K.1    Stewart, L.2    Lopez, C.3    Haines, D.C.4
  • 23
    • 34248580696 scopus 로고    scopus 로고
    • Growth promotion of quorum-quenching bacteria in the rhizosphere of Solanum tuberosum
    • Cirou A., Diallo S., Kurt C., Latour X., Faure D. Growth promotion of quorum-quenching bacteria in the rhizosphere of Solanum tuberosum. Environ. Microbiol. 2007, 9:1511-1522.
    • (2007) Environ. Microbiol. , vol.9 , pp. 1511-1522
    • Cirou, A.1    Diallo, S.2    Kurt, C.3    Latour, X.4    Faure, D.5
  • 24
    • 81355122651 scopus 로고    scopus 로고
    • Gamma-caprolactone stimulates growth of quorum-quenching Rhodococcus populations in a large-scale hydroponic system for culturing Solanum tuberosum
    • Cirou A., Raffoux A., Diallo S., Latour X., Dessaux Y., Faure D. Gamma-caprolactone stimulates growth of quorum-quenching Rhodococcus populations in a large-scale hydroponic system for culturing Solanum tuberosum. Res. Microbiol. 2011, 162:945-950.
    • (2011) Res. Microbiol. , vol.162 , pp. 945-950
    • Cirou, A.1    Raffoux, A.2    Diallo, S.3    Latour, X.4    Dessaux, Y.5    Faure, D.6
  • 25
    • 84899919093 scopus 로고    scopus 로고
    • Peptide pheromone signaling in Streptococcus and Enterococcus
    • Cook L.C., Federle M.J. Peptide pheromone signaling in Streptococcus and Enterococcus. FEMS Microbiol. Rev. 2014, 38:473-492.
    • (2014) FEMS Microbiol. Rev. , vol.38 , pp. 473-492
    • Cook, L.C.1    Federle, M.J.2
  • 26
    • 84858971457 scopus 로고    scopus 로고
    • N-Acyl homoserine lactones in diverse Pectobacterium and Dickeya plant pathogens: diversity, abundance, and involvement in virulence
    • Crépin A., Beury-Cirou A., Barbey C., Farmer C., Hélias V., Burini J.-F., Faure D., Latour X. N-Acyl homoserine lactones in diverse Pectobacterium and Dickeya plant pathogens: diversity, abundance, and involvement in virulence. Sensors 2012, 12:3484-3497.
    • (2012) Sensors , vol.12 , pp. 3484-3497
    • Crépin, A.1    Beury-Cirou, A.2    Barbey, C.3    Farmer, C.4    Hélias, V.5    Burini, J.-F.6    Faure, D.7    Latour, X.8
  • 28
    • 81355139004 scopus 로고    scopus 로고
    • Transgenic plants expressing the quorum quenching lactonase AttM do not significantly alter root-associated bacterial populations
    • D'Angelo-Picard C., Chapelle E., Ratet P., Faure D., Dessaux Y. Transgenic plants expressing the quorum quenching lactonase AttM do not significantly alter root-associated bacterial populations. Res. Microbiol. 2011, 162:951-958.
    • (2011) Res. Microbiol. , vol.162 , pp. 951-958
    • D'Angelo-Picard, C.1    Chapelle, E.2    Ratet, P.3    Faure, D.4    Dessaux, Y.5
  • 29
    • 77957656132 scopus 로고    scopus 로고
    • Can bacteria evolve resistance to quorum sensing disruption?
    • Defoirdt T., Boon N., Bossier P. Can bacteria evolve resistance to quorum sensing disruption?. PLoS Pathog. 2010, 6(7):e1000989.
    • (2010) PLoS Pathog. , vol.6 , Issue.7 , pp. e1000989
    • Defoirdt, T.1    Boon, N.2    Bossier, P.3
  • 30
    • 4744362419 scopus 로고    scopus 로고
    • Disruption of bacterial quorum sensing: an unexplored strategy to fight infections in aquaculture
    • Defoirdt T., Boon N., Bossier P., Verstraete W. Disruption of bacterial quorum sensing: an unexplored strategy to fight infections in aquaculture. Aquaculture 2004, 240:69-88.
    • (2004) Aquaculture , vol.240 , pp. 69-88
    • Defoirdt, T.1    Boon, N.2    Bossier, P.3    Verstraete, W.4
  • 31
    • 79959307336 scopus 로고    scopus 로고
    • Alternatives to antibiotics for the control of bacterial disease in aquaculture
    • Defoirdt T., Sorgeloos P., Bossier P. Alternatives to antibiotics for the control of bacterial disease in aquaculture. Curr. Opin. Microbiol. 2011, 14:251-258.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 251-258
    • Defoirdt, T.1    Sorgeloos, P.2    Bossier, P.3
  • 33
    • 14544284036 scopus 로고    scopus 로고
    • The contribution of MvfR to Pseudomonas aeruginosa pathogenesis and quorum sensing circuitry regulation: multiple quorum sensing-regulated genes are modulated without affecting lasRI, rhlRI or the production of N-acyl-l-homoserine lactones
    • Déziel E., Gopalan S., Tampakaki A.P., Lépine F., Padfield K.E., Saucier M., Xiao G., Rahme L.G. The contribution of MvfR to Pseudomonas aeruginosa pathogenesis and quorum sensing circuitry regulation: multiple quorum sensing-regulated genes are modulated without affecting lasRI, rhlRI or the production of N-acyl-l-homoserine lactones. Mol. Microbiol. 2005, 55:998-1014.
    • (2005) Mol. Microbiol. , vol.55 , pp. 998-1014
    • Déziel, E.1    Gopalan, S.2    Tampakaki, A.P.3    Lépine, F.4    Padfield, K.E.5    Saucier, M.6    Xiao, G.7    Rahme, L.G.8
  • 34
    • 0141595872 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa quinolone signal molecule overcomes the cell density-dependency of the quorum sensing hierarchy, regulates rhl-dependent genes at the onset of stationary phase and can be produced in the absence of LasR
    • Diggle S.P., Winzer K., Chhabra S.R., Worrall K.E., Cámara M., Williams P. The Pseudomonas aeruginosa quinolone signal molecule overcomes the cell density-dependency of the quorum sensing hierarchy, regulates rhl-dependent genes at the onset of stationary phase and can be produced in the absence of LasR. Mol. Microbiol. 2003, 50:29-43.
    • (2003) Mol. Microbiol. , vol.50 , pp. 29-43
    • Diggle, S.P.1    Winzer, K.2    Chhabra, S.R.3    Worrall, K.E.4    Cámara, M.5    Williams, P.6
  • 35
    • 0036205598 scopus 로고    scopus 로고
    • Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species
    • Dong Y.-H., Gusti A.R., Zhang Q., Xu J.-L., Zhang L.-H. Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species. Appl. Environ. Microbiol. 2002, 68:1754-1759.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1754-1759
    • Dong, Y.-H.1    Gusti, A.R.2    Zhang, Q.3    Xu, J.-L.4    Zhang, L.-H.5
  • 36
    • 0035859128 scopus 로고    scopus 로고
    • Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase
    • Dong Y.-H., Wang L.-H., Xu J.-L., Zhang H.-B., Zhang X.-F., Zhang L.-H. Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. Nature 2001, 411:813-817.
    • (2001) Nature , vol.411 , pp. 813-817
    • Dong, Y.-H.1    Wang, L.-H.2    Xu, J.-L.3    Zhang, H.-B.4    Zhang, X.-F.5    Zhang, L.-H.6
  • 37
    • 0034724191 scopus 로고    scopus 로고
    • AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora
    • Dong Y.-H., Xu J.-L., Li X.-Z., Zhang L.-H. AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:3526-3531.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3526-3531
    • Dong, Y.-H.1    Xu, J.-L.2    Li, X.-Z.3    Zhang, L.-H.4
  • 38
    • 21244491480 scopus 로고    scopus 로고
    • Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
    • Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., La Du B.N. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 2005, 46:1239-1247.
    • (2005) J. Lipid Res. , vol.46 , pp. 1239-1247
    • Draganov, D.I.1    Teiber, J.F.2    Speelman, A.3    Osawa, Y.4    Sunahara, R.5    La Du, B.N.6
  • 39
    • 77956338892 scopus 로고    scopus 로고
    • Membrane fouling in membrane bioreactors - characterisation, contradictions, cause and cures
    • Drews A. Membrane fouling in membrane bioreactors - characterisation, contradictions, cause and cures. J. Membr. Sci. 2010, 363:1-28.
    • (2010) J. Membr. Sci. , vol.363 , pp. 1-28
    • Drews, A.1
  • 40
    • 0030775686 scopus 로고    scopus 로고
    • Identification of 3-hydroxypalmitic acid methyl ester as a novel autoregulator controlling virulence in Ralstonia solanacearum
    • Flavier A.B., Clough S.J., Schell M.A., Denny T.P. Identification of 3-hydroxypalmitic acid methyl ester as a novel autoregulator controlling virulence in Ralstonia solanacearum. Mol. Microbiol. 1997, 26:251-259.
    • (1997) Mol. Microbiol. , vol.26 , pp. 251-259
    • Flavier, A.B.1    Clough, S.J.2    Schell, M.A.3    Denny, T.P.4
  • 41
    • 0036889038 scopus 로고    scopus 로고
    • Functions required for extracellular quinolone signaling by Pseudomonas aeruginosa
    • Gallagher L.A., McKnight S.L., Kuznetsova M.S., Pesci E.C., Manoil C. Functions required for extracellular quinolone signaling by Pseudomonas aeruginosa. J. Bacteriol. 2002, 184:6472-6480.
    • (2002) J. Bacteriol. , vol.184 , pp. 6472-6480
    • Gallagher, L.A.1    McKnight, S.L.2    Kuznetsova, M.S.3    Pesci, E.C.4    Manoil, C.5
  • 47
    • 68549122485 scopus 로고    scopus 로고
    • Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus
    • Hawwa R., Aikens J., Turner R.J., Santarsiero B.D., Mesecar A.D. Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus. Arch. Biochem. Biophys. 2009, 488:109-120.
    • (2009) Arch. Biochem. Biophys. , vol.488 , pp. 109-120
    • Hawwa, R.1    Aikens, J.2    Turner, R.J.3    Santarsiero, B.D.4    Mesecar, A.D.5
  • 49
    • 84867389293 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus
    • Hiblot J., Gotthard G., Chabriere E., Elias M. Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus. PLoS ONE 2012, 7(10):e47028.
    • (2012) PLoS ONE , vol.7 , Issue.10 , pp. e47028
    • Hiblot, J.1    Gotthard, G.2    Chabriere, E.3    Elias, M.4
  • 50
    • 84884515384 scopus 로고    scopus 로고
    • Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox
    • Hiblot J., Gotthard G., Elias M., Chabriere E. Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox. PLOS ONE 2013, 8(9):e75272.
    • (2013) PLOS ONE , vol.8 , Issue.9 , pp. e75272
    • Hiblot, J.1    Gotthard, G.2    Elias, M.3    Chabriere, E.4
  • 51
    • 0142040878 scopus 로고    scopus 로고
    • Utilization of acyl-homoserine lactone quorum signals for growth by a soil pseudomonad and Pseudomonas aeruginosa PAO1
    • Huang J.J., Han J.-I., Zhang L.-H., Leadbetter J.R. Utilization of acyl-homoserine lactone quorum signals for growth by a soil pseudomonad and Pseudomonas aeruginosa PAO1. Appl. Environ. Microbiol. 2003, 69:5941-5949.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5941-5949
    • Huang, J.J.1    Han, J.-I.2    Zhang, L.-H.3    Leadbetter, J.R.4
  • 52
    • 33144486525 scopus 로고    scopus 로고
    • Identification of QuiP, the product of gene PA1032, as the second acyl-homoserine lactone acylase of Pseudomonas aeruginosa PAO1
    • Huang J.J., Petersen A., Whiteley M., Leadbetter J.R. Identification of QuiP, the product of gene PA1032, as the second acyl-homoserine lactone acylase of Pseudomonas aeruginosa PAO1. Appl. Environ. Microbiol. 2006, 72:1190-1197.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1190-1197
    • Huang, J.J.1    Petersen, A.2    Whiteley, M.3    Leadbetter, J.R.4
  • 53
    • 84867304492 scopus 로고    scopus 로고
    • QsdH, a novel AHL lactonase in the RND-type inner membrane of marine Pseudoalteromonas byunsanensis strain 1A01261
    • Huang W., Lin Y., Yi S., Liu P., Shen J., Shao Z., Liu Z. QsdH, a novel AHL lactonase in the RND-type inner membrane of marine Pseudoalteromonas byunsanensis strain 1A01261. PLoS ONE 2012, 7(10):e46587.
    • (2012) PLoS ONE , vol.7 , Issue.10 , pp. e46587
    • Huang, W.1    Lin, Y.2    Yi, S.3    Liu, P.4    Shen, J.5    Shao, Z.6    Liu, Z.7
  • 54
    • 33846448470 scopus 로고    scopus 로고
    • Detection and characterization of bacteria from the potato rhizosphere degrading N-acyl-homoserine lactone
    • Jafra S., Przysowa J., Czajkowski R., Michta A., Garbeva P., Van der Wolf J.M. Detection and characterization of bacteria from the potato rhizosphere degrading N-acyl-homoserine lactone. Can. J. Microbiol. 2006, 52:1006-1015.
    • (2006) Can. J. Microbiol. , vol.52 , pp. 1006-1015
    • Jafra, S.1    Przysowa, J.2    Czajkowski, R.3    Michta, A.4    Garbeva, P.5    Van der Wolf, J.M.6
  • 55
    • 84870060086 scopus 로고    scopus 로고
    • Effect of quorum quenching on the reactor performance, biofouling and biomass characteristics in membrane bioreactors
    • Jiang W., Xia S., Liang J., Zhang Z., Hermanowicz S.W. Effect of quorum quenching on the reactor performance, biofouling and biomass characteristics in membrane bioreactors. Water Res. 2013, 47:187-196.
    • (2013) Water Res. , vol.47 , pp. 187-196
    • Jiang, W.1    Xia, S.2    Liang, J.3    Zhang, Z.4    Hermanowicz, S.W.5
  • 56
    • 79951639658 scopus 로고    scopus 로고
    • Enzyme-immobilized nanofiltration membrane to mitigate biofouling based on quorum quenching
    • Kim J.-H., Choi D.-C., Yeon K.-M., Kim S.-R., Lee C.-H. Enzyme-immobilized nanofiltration membrane to mitigate biofouling based on quorum quenching. Environ. Sci. Technol. 2011, 45:1601-1607.
    • (2011) Environ. Sci. Technol. , vol.45 , pp. 1601-1607
    • Kim, J.-H.1    Choi, D.-C.2    Yeon, K.-M.3    Kim, S.-R.4    Lee, C.-H.5
  • 57
    • 84872563885 scopus 로고    scopus 로고
    • Biofouling control with bead-entrapped quorum quenching bacteria in membrane bioreactors: physical and biological effects
    • Kim S.-R., Oh H.-S., Jo S.-J., Yeon K.-M., Lee C.-H., Lim D.-J., Lee C.-H., Lee J.-K. Biofouling control with bead-entrapped quorum quenching bacteria in membrane bioreactors: physical and biological effects. Environ. Sci. Technol. 2013, 47:836-842.
    • (2013) Environ. Sci. Technol. , vol.47 , pp. 836-842
    • Kim, S.-R.1    Oh, H.-S.2    Jo, S.-J.3    Yeon, K.-M.4    Lee, C.-H.5    Lim, D.-J.6    Lee, C.-H.7    Lee, J.-K.8
  • 60
    • 79961078497 scopus 로고    scopus 로고
    • Involvement of multiple loci in quorum quenching of autoinducer I molecules in the nitrogen-fixing symbiont Rhizobium (Sinorhizobium) sp. strain NGR234
    • Krysciak D., Schmeisser C., Preuß S., Riethausen J., Quitschau M., Grond S., Streit W.R. Involvement of multiple loci in quorum quenching of autoinducer I molecules in the nitrogen-fixing symbiont Rhizobium (Sinorhizobium) sp. strain NGR234. Appl. Environ. Microbiol. 2011, 77:5089-5099.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 5089-5099
    • Krysciak, D.1    Schmeisser, C.2    Preuß, S.3    Riethausen, J.4    Quitschau, M.5    Grond, S.6    Streit, W.R.7
  • 61
    • 84973246558 scopus 로고    scopus 로고
    • Rhodococcus erythropolis and its γ-lactone catabolic pathway: an unusual biocontrol system that disrupts pathogen quorum sensing communication
    • Latour X., Barbey C., Chane A., Groboillot A., Burini J.-F. Rhodococcus erythropolis and its γ-lactone catabolic pathway: an unusual biocontrol system that disrupts pathogen quorum sensing communication. Agronomy 2013, 3:816-838.
    • (2013) Agronomy , vol.3 , pp. 816-838
    • Latour, X.1    Barbey, C.2    Chane, A.3    Groboillot, A.4    Burini, J.-F.5
  • 62
    • 84874904560 scopus 로고    scopus 로고
    • Exploiting quorum sensing to confuse bacterial pathogens
    • LaSarre B., Federle M.J. Exploiting quorum sensing to confuse bacterial pathogens. Microbiol. Mol. Biol. Rev. 2013, 77:73-111.
    • (2013) Microbiol. Mol. Biol. Rev. , vol.77 , pp. 73-111
    • LaSarre, B.1    Federle, M.J.2
  • 63
    • 0034460299 scopus 로고    scopus 로고
    • Metabolism of acyl-homoserine lactone quorum-sensing signals by Variovorax paradoxus
    • Leadbetter J.R., Greenberg E.P. Metabolism of acyl-homoserine lactone quorum-sensing signals by Variovorax paradoxus. J. Bacteriol. 2000, 182:6921-6926.
    • (2000) J. Bacteriol. , vol.182 , pp. 6921-6926
    • Leadbetter, J.R.1    Greenberg, E.P.2
  • 64
    • 0036328528 scopus 로고    scopus 로고
    • Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis
    • Lee S.J., Park S.-Y., Lee J.-J., Yum D.-Y., Koo B.-T., Lee J.-K. Genes encoding the N-acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis. Appl. Environ. Microbiol. 2002, 68:3919-3924.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3919-3924
    • Lee, S.J.1    Park, S.-Y.2    Lee, J.-J.3    Yum, D.-Y.4    Koo, B.-T.5    Lee, J.-K.6
  • 66
    • 84898636775 scopus 로고    scopus 로고
    • Effective antifouling using quorum-quenching acylase stabilized in magnetically-separable mesoporous silica
    • Lee B., Yeon K.-M., Shim J., Kim S.-R., Lee C.-H., Lee J., Kim J. Effective antifouling using quorum-quenching acylase stabilized in magnetically-separable mesoporous silica. Biomacromolecules 2014, 15:1153-1159.
    • (2014) Biomacromolecules , vol.15 , pp. 1153-1159
    • Lee, B.1    Yeon, K.-M.2    Shim, J.3    Kim, S.-R.4    Lee, C.-H.5    Lee, J.6    Kim, J.7
  • 67
    • 0037238544 scopus 로고    scopus 로고
    • Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes
    • Lin Y.-H., Xu J.-L., Hu J., Wang L.-H., Ong S.L., Leadbetter J.R., Zhang L.-H. Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Mol. Microbiol. 2003, 47:849-860.
    • (2003) Mol. Microbiol. , vol.47 , pp. 849-860
    • Lin, Y.-H.1    Xu, J.-L.2    Hu, J.3    Wang, L.-H.4    Ong, S.L.5    Leadbetter, J.R.6    Zhang, L.-H.7
  • 68
    • 23844552796 scopus 로고    scopus 로고
    • Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis
    • Liu D., Lepore B.W., Petsko G.A., Thomas P.W., Stone E.M., Fast W., Ringe D. Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:11882-11887.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 11882-11887
    • Liu, D.1    Lepore, B.W.2    Petsko, G.A.3    Thomas, P.W.4    Stone, E.M.5    Fast, W.6    Ringe, D.7
  • 69
    • 35448969842 scopus 로고    scopus 로고
    • Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens
    • Liu D., Thomas P.W., Momb J., Hoang Q.Q., Petsko G.A., Ringe D., Fast W. Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens. Biochemistry 2007, 46:11789-11799.
    • (2007) Biochemistry , vol.46 , pp. 11789-11799
    • Liu, D.1    Thomas, P.W.2    Momb, J.3    Hoang, Q.Q.4    Petsko, G.A.5    Ringe, D.6    Fast, W.7
  • 71
    • 77955589874 scopus 로고    scopus 로고
    • AidH, an alpha/beta hydrolase fold family member from an Ochrobactrum sp. strain, is a novel N-acylhomoserine lactonase
    • Mei G.-Y., Yan X.-X., Turak A., Luo Z.-Q., Zhang L.-Q. AidH, an alpha/beta hydrolase fold family member from an Ochrobactrum sp. strain, is a novel N-acylhomoserine lactonase. Appl. Environ. Microbiol. 2010, 76:4933-4942.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4933-4942
    • Mei, G.-Y.1    Yan, X.-X.2    Turak, A.3    Luo, Z.-Q.4    Zhang, L.-Q.5
  • 72
    • 33846923413 scopus 로고    scopus 로고
    • Quinoline, quinazoline and acridone alkaloids
    • Michael J.P. Quinoline, quinazoline and acridone alkaloids. Nat. Prod. Rep. 2007, 24:223-246.
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 223-246
    • Michael, J.P.1
  • 73
    • 38849111840 scopus 로고    scopus 로고
    • Quinoline, quinazoline and acridone alkaloids
    • Michael J.P. Quinoline, quinazoline and acridone alkaloids. Nat. Prod. Rep. 2008, 25:166-187.
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 166-187
    • Michael, J.P.1
  • 74
    • 0037528693 scopus 로고    scopus 로고
    • Degradation of pathogen quorum-sensing molecules by soil bacteria: a preventive and curative biological control mechanism
    • Molina L., Constantinescu F., Michel L., Reimmann C., Duffy B., Défago G. Degradation of pathogen quorum-sensing molecules by soil bacteria: a preventive and curative biological control mechanism. FEMS Microbiol. Ecol. 2003, 45:71-81.
    • (2003) FEMS Microbiol. Ecol. , vol.45 , pp. 71-81
    • Molina, L.1    Constantinescu, F.2    Michel, L.3    Reimmann, C.4    Duffy, B.5    Défago, G.6
  • 75
    • 47949117950 scopus 로고    scopus 로고
    • Identification and characterization of N-acylhomoserine lacone-acylase from the fish intestinal Shewanella sp. strain MIB015
    • Morohoshi T., Nakazawa S., Ebata A., Kato N., Ikeda T. Identification and characterization of N-acylhomoserine lacone-acylase from the fish intestinal Shewanella sp. strain MIB015. Biosci. Biotechnol. Biochem. 2008, 72:1887-1893.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1887-1893
    • Morohoshi, T.1    Nakazawa, S.2    Ebata, A.3    Kato, N.4    Ikeda, T.5
  • 76
    • 84855351474 scopus 로고    scopus 로고
    • Complete genome sequence and characterization of the N-acylhomoserine lactone-degrading gene of the potato leaf-associated Solibacillus silvestris
    • Morohoshi T., Tominaga Y., Someya N., Ikeda T. Complete genome sequence and characterization of the N-acylhomoserine lactone-degrading gene of the potato leaf-associated Solibacillus silvestris. J. Biosci. Bioeng. 2012, 113:20-25.
    • (2012) J. Biosci. Bioeng. , vol.113 , pp. 20-25
    • Morohoshi, T.1    Tominaga, Y.2    Someya, N.3    Ikeda, T.4
  • 77
    • 84893173700 scopus 로고    scopus 로고
    • A new role for penicillin acylases: degradation of acyl homoserine lactone quorum sensing signals by Kluyvera citrophila penicillin G acylase
    • Mukherji R., Varshney N.K., Panigrahi P., Suresh C.G., Prabhune A. A new role for penicillin acylases: degradation of acyl homoserine lactone quorum sensing signals by Kluyvera citrophila penicillin G acylase. Enzyme Microb. Technol. 2014, 56:1-7.
    • (2014) Enzyme Microb. Technol. , vol.56 , pp. 1-7
    • Mukherji, R.1    Varshney, N.K.2    Panigrahi, P.3    Suresh, C.G.4    Prabhune, A.5
  • 79
    • 40849093159 scopus 로고    scopus 로고
    • Virulence of plant pathogenic bacteria attenuated by degradation of fatty acid cell-to-cell signaling factors
    • Newman K.L., Chatterjee S., Ho K.A., Lindow S.E. Virulence of plant pathogenic bacteria attenuated by degradation of fatty acid cell-to-cell signaling factors. Mol. Plant-Microbe Interact. 2008, 21:326-334.
    • (2008) Mol. Plant-Microbe Interact. , vol.21 , pp. 326-334
    • Newman, K.L.1    Chatterjee, S.2    Ho, K.A.3    Lindow, S.E.4
  • 80
    • 73349114916 scopus 로고    scopus 로고
    • Bacterial quorum-sensing network architectures
    • Ng W.-L., Bassler B.L. Bacterial quorum-sensing network architectures. Annu. Rev. Genet. 2009, 43:197-222.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 197-222
    • Ng, W.-L.1    Bassler, B.L.2
  • 81
    • 79953192545 scopus 로고    scopus 로고
    • Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for disruption of quorum sensing
    • Ng F.S.W., Wright D.M., Seah S.Y.K. Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for disruption of quorum sensing. Appl. Environ. Microbiol. 2011, 77:1181-1186.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1181-1186
    • Ng, F.S.W.1    Wright, D.M.2    Seah, S.Y.K.3
  • 82
    • 77955778916 scopus 로고    scopus 로고
    • Quorum quenching bacteria protect Macrobrachium rosenbergii larvae from Vibrio harveyi infection
    • Nhan D.T., Cam D.T.V., Wille M., Defoirdt T., Bossier P., Sorgeloos P. Quorum quenching bacteria protect Macrobrachium rosenbergii larvae from Vibrio harveyi infection. J. Appl. Microbiol. 2010, 109:1007-1016.
    • (2010) J. Appl. Microbiol. , vol.109 , pp. 1007-1016
    • Nhan, D.T.1    Cam, D.T.V.2    Wille, M.3    Defoirdt, T.4    Bossier, P.5    Sorgeloos, P.6
  • 83
  • 84
    • 84860434794 scopus 로고    scopus 로고
    • Control of membrane biofouling in MBR for wastewater treatment by quorum quenching bacteria encapsulated in microporous membrane
    • Oh H.-S., Yeon K.-M., Yang C.-S., Kim S.-R., Lee C.-H., Park S.Y., Han J.Y., Lee J.-K. Control of membrane biofouling in MBR for wastewater treatment by quorum quenching bacteria encapsulated in microporous membrane. Environ. Sci. Technol. 2012, 46:4877-4884.
    • (2012) Environ. Sci. Technol. , vol.46 , pp. 4877-4884
    • Oh, H.-S.1    Yeon, K.-M.2    Yang, C.-S.3    Kim, S.-R.4    Lee, C.-H.5    Park, S.Y.6    Han, J.Y.7    Lee, J.-K.8
  • 87
    • 33745684173 scopus 로고    scopus 로고
    • N-acylhomoserine lactonase-producing Rhodococcus spp. with different AHL-degrading activities
    • Park S.-Y., Hwang B.-J., Shin M.-H., Kim J.-A., Kim H.-K., Lee J.-K. N-acylhomoserine lactonase-producing Rhodococcus spp. with different AHL-degrading activities. FEMS Microbiol. Lett. 2006, 261:102-108.
    • (2006) FEMS Microbiol. Lett. , vol.261 , pp. 102-108
    • Park, S.-Y.1    Hwang, B.-J.2    Shin, M.-H.3    Kim, J.-A.4    Kim, H.-K.5    Lee, J.-K.6
  • 88
    • 18444375881 scopus 로고    scopus 로고
    • Identification of extracellular N-acylhomoserine lactone acylase from a Streptomyces sp. and its application to quorum quenching
    • Park S.-Y., Kang H.-O., Jang H.-S., Lee J.-K., Koo B.-T., Yum D.-Y. Identification of extracellular N-acylhomoserine lactone acylase from a Streptomyces sp. and its application to quorum quenching. Appl. Environ. Microbiol. 2005, 71:2632-2641.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2632-2641
    • Park, S.-Y.1    Kang, H.-O.2    Jang, H.-S.3    Lee, J.-K.4    Koo, B.-T.5    Yum, D.-Y.6
  • 89
    • 0038818560 scopus 로고    scopus 로고
    • AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria
    • Park S.-Y., Lee S.J., Oh T.-K., Oh J.-W., Koo B.-T., Yum D.-Y., Lee J.-K. AhlD, an N-acylhomoserine lactonase in Arthrobacter sp., and predicted homologues in other bacteria. Microbiology 2003, 149:1541-1550.
    • (2003) Microbiology , vol.149 , pp. 1541-1550
    • Park, S.-Y.1    Lee, S.J.2    Oh, T.-K.3    Oh, J.-W.4    Koo, B.-T.5    Yum, D.-Y.6    Lee, J.-K.7
  • 90
    • 68149164282 scopus 로고    scopus 로고
    • Application of quorum quenching to inhibit biofilm formation
    • Paul D., Kim Y.S., Ponnusamy K., Kweon J.H. Application of quorum quenching to inhibit biofilm formation. Environ. Eng. Sci. 2009, 26:1319-1324.
    • (2009) Environ. Eng. Sci. , vol.26 , pp. 1319-1324
    • Paul, D.1    Kim, Y.S.2    Ponnusamy, K.3    Kweon, J.H.4
  • 94
    • 38549147402 scopus 로고    scopus 로고
    • A metagenomic analysis of soil bacteria extends the diversity of quorum-quenching lactonases
    • Riaz K., Elmerich C., Moreira D., Raffoux A., Dessaux Y., Faure D. A metagenomic analysis of soil bacteria extends the diversity of quorum-quenching lactonases. Environ. Microbiol. 2008, 10:560-570.
    • (2008) Environ. Microbiol. , vol.10 , pp. 560-570
    • Riaz, K.1    Elmerich, C.2    Moreira, D.3    Raffoux, A.4    Dessaux, Y.5    Faure, D.6
  • 95
    • 77149149046 scopus 로고    scopus 로고
    • Acylhomoserine lactone production and degradation by the fish pathogen Tenacibaculum maritimum, a member of the Cytophaga-Flavobacterium-Bacteroides (CFB) group
    • Romero M., Avendano-Herrera R., Magarinos B., Cámara M., Otero A. Acylhomoserine lactone production and degradation by the fish pathogen Tenacibaculum maritimum, a member of the Cytophaga-Flavobacterium-Bacteroides (CFB) group. FEMS Microbiol. Lett. 2010, 304:131-139.
    • (2010) FEMS Microbiol. Lett. , vol.304 , pp. 131-139
    • Romero, M.1    Avendano-Herrera, R.2    Magarinos, B.3    Cámara, M.4    Otero, A.5
  • 96
    • 38849144610 scopus 로고    scopus 로고
    • Quorum quenching activity in Anabaena sp. PCC7120: identification of AiiC, a novel AHL-acylase
    • Romero M., Diggle S.P., Heeb S., Cámara M., Otero A. Quorum quenching activity in Anabaena sp. PCC7120: identification of AiiC, a novel AHL-acylase. FEMS Microbiol. Lett. 2008, 280:73-80.
    • (2008) FEMS Microbiol. Lett. , vol.280 , pp. 73-80
    • Romero, M.1    Diggle, S.P.2    Heeb, S.3    Cámara, M.4    Otero, A.5
  • 98
    • 77449107859 scopus 로고    scopus 로고
    • Cross species quorum quenching using a native AI-2 processing enzyme
    • Roy V., Fernandes R., Tsao C.-Y., Bentley W.E. Cross species quorum quenching using a native AI-2 processing enzyme. ACS Chem. Biol. 2010, 5:223-232.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 223-232
    • Roy, V.1    Fernandes, R.2    Tsao, C.-Y.3    Bentley, W.E.4
  • 99
    • 58149335526 scopus 로고    scopus 로고
    • Metagenome-derived clones encoding two novel lactonase family proteins involved in biofilm inhibition in Pseudomonas aeruginosa
    • Schipper C., Hornung C., Bijtenhoorn P., Quitschau M., Grond S., Streit W.R. Metagenome-derived clones encoding two novel lactonase family proteins involved in biofilm inhibition in Pseudomonas aeruginosa. Appl. Environ. Microbiol. 2009, 75:224-233.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 224-233
    • Schipper, C.1    Hornung, C.2    Bijtenhoorn, P.3    Quitschau, M.4    Grond, S.5    Streit, W.R.6
  • 101
    • 58149352996 scopus 로고    scopus 로고
    • Two dissimilar N-acyl-homoserine lactone acylases of Pseudomonas syringae influence colony and biofilm morphology
    • Shepherd R.W., Lindow S.E. Two dissimilar N-acyl-homoserine lactone acylases of Pseudomonas syringae influence colony and biofilm morphology. Appl. Environ. Microbiol. 2009, 75:45-53.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 45-53
    • Shepherd, R.W.1    Lindow, S.E.2
  • 102
    • 34250884486 scopus 로고    scopus 로고
    • Purification and characterization of a novel esterase (β-hydroxypalmitate methyl ester hydrolase) and prevention of the expression of virulence by Ralstonia solanacearum
    • Shinohara M., Nakajima N., Uehara Y. Purification and characterization of a novel esterase (β-hydroxypalmitate methyl ester hydrolase) and prevention of the expression of virulence by Ralstonia solanacearum. J. Appl. Microbiol. 2007, 103:152-162.
    • (2007) J. Appl. Microbiol. , vol.103 , pp. 152-162
    • Shinohara, M.1    Nakajima, N.2    Uehara, Y.3
  • 103
    • 84865312176 scopus 로고    scopus 로고
    • Paraoxonase 2 acts as a quorum sensing-quenching factor in human keratinocytes
    • Simanski M., Babucke S., Eberl L., Harder J. Paraoxonase 2 acts as a quorum sensing-quenching factor in human keratinocytes. J. Invest. Dermatol. 2012, 132:2296-2299.
    • (2012) J. Invest. Dermatol. , vol.132 , pp. 2296-2299
    • Simanski, M.1    Babucke, S.2    Eberl, L.3    Harder, J.4
  • 107
    • 33744552662 scopus 로고    scopus 로고
    • γ-Butyrolactones: Streptomyces signalling molecules regulating antibiotic production and differentiation
    • Takano E. γ-Butyrolactones: Streptomyces signalling molecules regulating antibiotic production and differentiation. Curr. Opin. Microbiol. 2006, 9:287-294.
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 287-294
    • Takano, E.1
  • 108
    • 84878758612 scopus 로고    scopus 로고
    • A metagenomic study highlights phylogenetic proximity of quorum-quenching and xenobiotic-degrading amidases of the AS-family
    • Tannières M., Beury-Cirou A., Vigouroux A., Mondy S., Pellissier F., Dessaux Y., Faure D. A metagenomic study highlights phylogenetic proximity of quorum-quenching and xenobiotic-degrading amidases of the AS-family. PLOS ONE 2013, 8(6):e65473.
    • (2013) PLOS ONE , vol.8 , Issue.6 , pp. e65473
    • Tannières, M.1    Beury-Cirou, A.2    Vigouroux, A.3    Mondy, S.4    Pellissier, F.5    Dessaux, Y.6    Faure, D.7
  • 109
    • 77149163329 scopus 로고    scopus 로고
    • Bicyclic compounds repress membrane vesicle production and Pseudomonas quinolone signal synthesis in Pseudomonas aeruginosa
    • Tashiro Y., Toyofuku M., Nakajima-Kambe T., Uchiyama H., Nomura N. Bicyclic compounds repress membrane vesicle production and Pseudomonas quinolone signal synthesis in Pseudomonas aeruginosa. FEMS Microbiol. Lett. 2010, 304:123-130.
    • (2010) FEMS Microbiol. Lett. , vol.304 , pp. 123-130
    • Tashiro, Y.1    Toyofuku, M.2    Nakajima-Kambe, T.3    Uchiyama, H.4    Nomura, N.5
  • 110
    • 46249112510 scopus 로고    scopus 로고
    • Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxodecanoyl)-l-homoserine lactone
    • Teiber J.F., Horke S., Haines D.C., Chowdhary P.K., Xiao J., Kramer G.L., Haley R.W., Draganov D.I. Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxodecanoyl)-l-homoserine lactone. Infect. Immun. 2008, 76:2512-2519.
    • (2008) Infect. Immun. , vol.76 , pp. 2512-2519
    • Teiber, J.F.1    Horke, S.2    Haines, D.C.3    Chowdhary, P.K.4    Xiao, J.5    Kramer, G.L.6    Haley, R.W.7    Draganov, D.I.8
  • 111
    • 84892420992 scopus 로고    scopus 로고
    • Quorum sensing and self-quorum quenching in the intracellular pathogen Brucella melitensis
    • Terwagne M., Mirabella A., Lemaire J., Deschamps C., De Bolle X., Letesson J.-J. Quorum sensing and self-quorum quenching in the intracellular pathogen Brucella melitensis. PLOS ONE 2013, 8(12):e82514.
    • (2013) PLOS ONE , vol.8 , Issue.12 , pp. e82514
    • Terwagne, M.1    Mirabella, A.2    Lemaire, J.3    Deschamps, C.4    De Bolle, X.5    Letesson, J.-J.6
  • 113
    • 77952303129 scopus 로고    scopus 로고
    • Biosynthesis of peptide signals in Gram-positive bacteria
    • Thoendel M., Horswill A.R. Biosynthesis of peptide signals in Gram-positive bacteria. Adv. Appl. Microbiol. 2010, 71:91-112.
    • (2010) Adv. Appl. Microbiol. , vol.71 , pp. 91-112
    • Thoendel, M.1    Horswill, A.R.2
  • 114
    • 56149124484 scopus 로고    scopus 로고
    • An acyl homoserine lactone-degrading microbial community improves the survival of first-feeding turbot larvae (Scophthalmus maximus L.)
    • Tinh N.T.N., Yen V.H.N., Dierckens K., Sorgeloos P., Bossier P. An acyl homoserine lactone-degrading microbial community improves the survival of first-feeding turbot larvae (Scophthalmus maximus L.). Aquaculture 2008, 285:56-62.
    • (2008) Aquaculture , vol.285 , pp. 56-62
    • Tinh, N.T.N.1    Yen, V.H.N.2    Dierckens, K.3    Sorgeloos, P.4    Bossier, P.5
  • 115
    • 8144220509 scopus 로고    scopus 로고
    • Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis
    • Ulrich R.L. Quorum quenching: enzymatic disruption of N-acylhomoserine lactone-mediated bacterial communication in Burkholderia thailandensis. Appl. Environ. Microbiol. 2004, 70:6173-6180.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6173-6180
    • Ulrich, R.L.1
  • 116
    • 27144516831 scopus 로고    scopus 로고
    • N-Acylhomoserine lactone quorum-sensing molecules are modified and degraded by Rhodococcus erythropolis W2 by both amidolytic and novel oxidoreductase activities
    • Uroz S., Chhabra S.R., Cámara M., Williams P., Oger P., Dessaux Y. N-Acylhomoserine lactone quorum-sensing molecules are modified and degraded by Rhodococcus erythropolis W2 by both amidolytic and novel oxidoreductase activities. Microbiology 2005, 151:3313-3322.
    • (2005) Microbiology , vol.151 , pp. 3313-3322
    • Uroz, S.1    Chhabra, S.R.2    Cámara, M.3    Williams, P.4    Oger, P.5    Dessaux, Y.6
  • 117
    • 0041923998 scopus 로고    scopus 로고
    • Novel bacteria degrading N-acylhomoserine lactones and their use as quenchers of quorum-sensing-regulated functions of plant-pathogenic bacteria
    • Uroz S., D'Angelo-Picard C., Carlier A., Elasri M., Sicot C., Petit A., Oger P., Faure S., Dessaux Y. Novel bacteria degrading N-acylhomoserine lactones and their use as quenchers of quorum-sensing-regulated functions of plant-pathogenic bacteria. Microbiology 2003, 149:1981-1989.
    • (2003) Microbiology , vol.149 , pp. 1981-1989
    • Uroz, S.1    D'Angelo-Picard, C.2    Carlier, A.3    Elasri, M.4    Sicot, C.5    Petit, A.6    Oger, P.7    Faure, S.8    Dessaux, Y.9
  • 118
    • 47249143336 scopus 로고    scopus 로고
    • Degradation of N-acyl homoserine lactone quorum-sensing signal molecules by forest root-associated fungi
    • Uroz S., Heinonsalo J. Degradation of N-acyl homoserine lactone quorum-sensing signal molecules by forest root-associated fungi. FEMS Microbiol. Ecol. 2008, 65:271-278.
    • (2008) FEMS Microbiol. Ecol. , vol.65 , pp. 271-278
    • Uroz, S.1    Heinonsalo, J.2
  • 119
    • 40549109554 scopus 로고    scopus 로고
    • A Rhodococcus qsdA-encoded enzyme defines a novel class of large-spectrum quorum-quenching lactonases
    • Uroz S., Oger P.M., Chapelle E., Adeline M.-T., Faure D., Dessaux Y. A Rhodococcus qsdA-encoded enzyme defines a novel class of large-spectrum quorum-quenching lactonases. Appl. Environ. Microbiol. 2008, 74:1357-1366.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1357-1366
    • Uroz, S.1    Oger, P.M.2    Chapelle, E.3    Adeline, M.-T.4    Faure, D.5    Dessaux, Y.6
  • 120
    • 33847167419 scopus 로고    scopus 로고
    • N-Acyl homoserine lactones are degraded via an amidolytic activity in Comamonas sp. strain D1
    • Uroz S., Oger P., Chhabra S.R., Cámara M., Williams P., Dessaux Y. N-Acyl homoserine lactones are degraded via an amidolytic activity in Comamonas sp. strain D1. Arch. Microbiol. 2007, 187:249-256.
    • (2007) Arch. Microbiol. , vol.187 , pp. 249-256
    • Uroz, S.1    Oger, P.2    Chhabra, S.R.3    Cámara, M.4    Williams, P.5    Dessaux, Y.6
  • 121
    • 70350743377 scopus 로고    scopus 로고
    • Enhancement of tolerance to soft rot disease in the transgenic Chinese cabbage (Brassica rapa L. ssp. pekinensis) inbred line, Kenshin
    • Vanjildorj E., Song S.Y., Yang Z.H., Choi J.E., Noh Y.S., Park S., Lim W.J., Cho K.M., Yun H.D., Lim Y.P. Enhancement of tolerance to soft rot disease in the transgenic Chinese cabbage (Brassica rapa L. ssp. pekinensis) inbred line, Kenshin. Plant Cell Rep. 2009, 28:1581-1591.
    • (2009) Plant Cell Rep. , vol.28 , pp. 1581-1591
    • Vanjildorj, E.1    Song, S.Y.2    Yang, Z.H.3    Choi, J.E.4    Noh, Y.S.5    Park, S.6    Lim, W.J.7    Cho, K.M.8    Yun, H.D.9    Lim, Y.P.10
  • 124
    • 77950576599 scopus 로고    scopus 로고
    • AiiM, a novel class of N-acylhomoserine lactonase from the leaf-associated bacterium Microbacterium testaceum
    • Wang W.-Z., Morohoshi T., Ikenoya M., Someya N., Ikeda T. AiiM, a novel class of N-acylhomoserine lactonase from the leaf-associated bacterium Microbacterium testaceum. Appl. Environ. Microbiol. 2010, 76:2524-2530.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2524-2530
    • Wang, W.-Z.1    Morohoshi, T.2    Ikenoya, M.3    Someya, N.4    Ikeda, T.5
  • 125
    • 84868620922 scopus 로고    scopus 로고
    • AidC, a novel N-acylhomoserine lactonase from the potato root-associated Cytophaga-Flavobacteria-Bacteroides (CFB) group bacterium Chryseobacterium sp. strain StRB126
    • Wang W.-Z., Morohoshi T., Someya N., Ikeda T. AidC, a novel N-acylhomoserine lactonase from the potato root-associated Cytophaga-Flavobacteria-Bacteroides (CFB) group bacterium Chryseobacterium sp. strain StRB126. Appl. Environ. Microbiol. 2012, 78:7985-7992.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 7985-7992
    • Wang, W.-Z.1    Morohoshi, T.2    Someya, N.3    Ikeda, T.4
  • 126
    • 1842791546 scopus 로고    scopus 로고
    • Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase)
    • Wang L.-H., Weng L.-X., Dong Y.-H., Zhang L.-H. Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase). J. Biol. Chem. 2004, 279:13645-13651.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13645-13651
    • Wang, L.-H.1    Weng, L.-X.2    Dong, Y.-H.3    Zhang, L.-H.4
  • 127
    • 37449026650 scopus 로고    scopus 로고
    • Quorum sensing, communication and cross-kingdom signalling in the bacterial world
    • Williams P. Quorum sensing, communication and cross-kingdom signalling in the bacterial world. Microbiology 2007, 153:3923-3938.
    • (2007) Microbiology , vol.153 , pp. 3923-3938
    • Williams, P.1
  • 128
    • 0037676088 scopus 로고    scopus 로고
    • LuxS quorum sensing: more than just a numbers game
    • Xavier K.B., Bassler B.L. LuxS quorum sensing: more than just a numbers game. Curr. Opin. Microbiol. 2003, 6:191-197.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 191-197
    • Xavier, K.B.1    Bassler, B.L.2
  • 129
    • 64349121094 scopus 로고    scopus 로고
    • Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily
    • Xiang D.F., Kolb P., Fedorov A.A., Meier M.M., Fedorov L.V., Nguyen T.T., Sterner R., Almo S.C., Shoichet B.K., Raushel F.M. Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily. Biochemistry 2009, 48:2237-2247.
    • (2009) Biochemistry , vol.48 , pp. 2237-2247
    • Xiang, D.F.1    Kolb, P.2    Fedorov, A.A.3    Meier, M.M.4    Fedorov, L.V.5    Nguyen, T.T.6    Sterner, R.7    Almo, S.C.8    Shoichet, B.K.9    Raushel, F.M.10
  • 130
    • 21244473275 scopus 로고    scopus 로고
    • Quorum quenching enzyme activity is widely conserved in the sera of mammalian species
    • Yang F., Wang L.-H., Wang J., Dong Y.-H., Hu J.Y., Zhang L.-H. Quorum quenching enzyme activity is widely conserved in the sera of mammalian species. FEBS Lett. 2005, 579:3713-3717.
    • (2005) FEBS Lett. , vol.579 , pp. 3713-3717
    • Yang, F.1    Wang, L.-H.2    Wang, J.3    Dong, Y.-H.4    Hu, J.Y.5    Zhang, L.-H.6
  • 132
    • 70349614420 scopus 로고    scopus 로고
    • Magnetic enzyme carrier for effective biofouling control in the membrane bioreactor based on enzymatic quorum quenching
    • Yeon K.-M., Lee C.-H., Kim J. Magnetic enzyme carrier for effective biofouling control in the membrane bioreactor based on enzymatic quorum quenching. Environ. Sci. Technol. 2009, 43:7403-7409.
    • (2009) Environ. Sci. Technol. , vol.43 , pp. 7403-7409
    • Yeon, K.-M.1    Lee, C.-H.2    Kim, J.3
  • 133
    • 33847123511 scopus 로고    scopus 로고
    • Fusion of the genes for AHL-lactonase and S-layer protein in Bacillus thuringiensis increases its ability to inhibit soft rot caused by Erwinia carotovora
    • Zhang L., Ruan L., Hu C., Wu H., Chen S., Yu Z., Sun M. Fusion of the genes for AHL-lactonase and S-layer protein in Bacillus thuringiensis increases its ability to inhibit soft rot caused by Erwinia carotovora. Appl. Microbiol. Biotechnol. 2007, 74:667-675.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 667-675
    • Zhang, L.1    Ruan, L.2    Hu, C.3    Wu, H.4    Chen, S.5    Yu, Z.6    Sun, M.7
  • 134
    • 0037007116 scopus 로고    scopus 로고
    • Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens
    • Zhang H.-B., Wang L.-H., Zhang L.-H. Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:4638-4643.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4638-4643
    • Zhang, H.-B.1    Wang, L.-H.2    Zhang, L.-H.3


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