메뉴 건너뛰기
Journal of Bacteriology
Volumn 197, Issue 3, 2015, Pages 529-541
Ubiquitin activates patatin-like phospholipases from multiple bacterial species
Author keywords

[No Author keywords available]
Indexed keywords

ASPARTIC ACID; PATATIN LIKE PHOSPHOLIPASE; PHOSPHATE; PHOSPHATIDYL 4,5 BISPHOSPHATE; PHOSPHOLIPASE; SERINE; UBIQUITIN; UNCLASSIFIED DRUG; ENZYME ACTIVATOR;
EID: 84920836378     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02402-14     Document Type: Article
Times cited : (36)
References (64)
  • 1
    • 0024234475 scopus 로고
    • Properties and purification of an arachidonoyl-hydrolyzing phospholipase A2 from a macrophage cell line, RAW 2647
    • Leslie CC, Voelker DR, Channon JY, Wall MM, Zelarney PT. 1988. Properties and purification of an arachidonoyl-hydrolyzing phospholipase A2 from a macrophage cell line, RAW 2647. Biochim Biophys Acta 963:476-492.
    • (1988) Biochim Biophys Acta , vol.963 , pp. 476-492
    • Leslie, C.C.1    Voelker, D.R.2    Channon, J.Y.3    Wall, M.M.4    Zelarney, P.T.5
  • 2
    • 66349090778 scopus 로고    scopus 로고
    • Phospholipase A2 structure/function, mechanism, and signaling
    • Burke JE, Dennis EA. 2009. Phospholipase A2 structure/function, mechanism, and signaling. J Lipid Res 50(Suppl):S237-S242. http://dx.doi.org/10.1194/jlr.R800033-JLR200.
    • (2009) J Lipid Res , vol.50 , pp. S237-S242
    • Burke, J.E.1    Dennis, E.A.2
  • 4
    • 0037207142 scopus 로고    scopus 로고
    • The crystal structure of the H48Q active site mutant of human group IIA secreted phospholipase A2 at 1.5 A resolution provides an insight into the catalytic mechanism
    • Edwards SH, Thompson D, Baker SF, Wood SP, Wilton DC. 2002. The crystal structure of the H48Q active site mutant of human group IIA secreted phospholipase A2 at 1.5 A resolution provides an insight into the catalytic mechanism. Biochemistry 41:15468-15476. http://dx.doi.org/10.1021/bi020485z.
    • (2002) Biochemistry , vol.41 , pp. 15468-15476
    • Edwards, S.H.1    Thompson, D.2    Baker, S.F.3    Wood, S.P.4    Wilton, D.C.5
  • 5
    • 0035141328 scopus 로고    scopus 로고
    • Toward understanding interfacial activation of secretory phospholipase A2 (PLA2): membrane surface properties and membrane-induced structural changes in the enzyme contribute synergistically to PLA2 activation
    • Tatulian SA. 2001. Toward understanding interfacial activation of secretory phospholipase A2 (PLA2): membrane surface properties and membrane-induced structural changes in the enzyme contribute synergistically to PLA2 activation. Biophys J 80:789-800. http://dx.doi.org/10.1016/S0006-3495(01)76058-4.
    • (2001) Biophys J , vol.80 , pp. 789-800
    • Tatulian, S.A.1
  • 6
    • 0032510696 scopus 로고    scopus 로고
    • Interfacial recognition by bee venom phospholipase A2: insights into nonelectrostatic molecular determinants by charge reversal mutagenesis
    • Ghomashchi F, Lin Y, Hixon MS, Yu BZ, Annand R, Jain MK, Gelb MH. 1998. Interfacial recognition by bee venom phospholipase A2: insights into nonelectrostatic molecular determinants by charge reversal mutagenesis. Biochemistry 37:6697-6710. http://dx.doi.org/10.1021/bi972525i.
    • (1998) Biochemistry , vol.37 , pp. 6697-6710
    • Ghomashchi, F.1    Lin, Y.2    Hixon, M.S.3    Yu, B.Z.4    Annand, R.5    Jain, M.K.6    Gelb, M.H.7
  • 7
    • 0037155144 scopus 로고    scopus 로고
    • Bactericidal properties of human and murine groups I, II, V, X, and XII secreted phospholipases A(2)
    • Koduri RS, Gronroos JO, Laine VJ, Le Calvez C, Lambeau G, Nevalainen TJ, Gelb MH. 2002. Bactericidal properties of human and murine groups I, II, V, X, and XII secreted phospholipases A(2). J Biol Chem 277:5849-5857. http://dx.doi.org/10.1074/jbc.M109699200.
    • (2002) J Biol Chem , vol.277 , pp. 5849-5857
    • Koduri, R.S.1    Gronroos, J.O.2    Laine, V.J.3    Le Calvez, C.4    Lambeau, G.5    Nevalainen, T.J.6    Gelb, M.H.7
  • 8
    • 23444442916 scopus 로고    scopus 로고
    • Secretory phospholipase A2 enzymes in atherogenesis
    • Webb NR. 2005. Secretory phospholipase A2 enzymes in atherogenesis. Curr Opin Lipidol 16:341-344. http://dx.doi.org/10.1097/01.mol.0000169355.20395.55.
    • (2005) Curr Opin Lipidol , vol.16 , pp. 341-344
    • Webb, N.R.1
  • 9
    • 0027378499 scopus 로고
    • Mammalian nonpancreatic phospholipases A2
    • Kudo I, Murakami M, Hara S, Inoue K. 1993. Mammalian nonpancreatic phospholipases A2. Biochim Biophys Acta 1170:217-231. http://dx.doi.org/10.1016/0005-2760(93)90003-R.
    • (1993) Biochim Biophys Acta , vol.1170 , pp. 217-231
    • Kudo, I.1    Murakami, M.2    Hara, S.3    Inoue, K.4
  • 10
    • 0031560233 scopus 로고    scopus 로고
    • The perturbed membrane of cells undergoing apoptosis is susceptible to type II secretory phospholipase A2 to liberate arachidonic acid
    • Atsumi G, Murakami M, Tajima M, Shimbara S, Hara N, Kudo I. 1997. The perturbed membrane of cells undergoing apoptosis is susceptible to type II secretory phospholipase A2 to liberate arachidonic acid. Biochim Biophys Acta 1349:43-54. http://dx.doi.org/10.1016/S0005-2760(97)00082-9.
    • (1997) Biochim Biophys Acta , vol.1349 , pp. 43-54
    • Atsumi, G.1    Murakami, M.2    Tajima, M.3    Shimbara, S.4    Hara, N.5    Kudo, I.6
  • 11
    • 84872502406 scopus 로고    scopus 로고
    • Phospholipases A2: unveiling the secrets of a functionally versatile group of snake venom toxins
    • Gutiérrez JM, Lomonte B. 2013. Phospholipases A2: unveiling the secrets of a functionally versatile group of snake venom toxins. Toxicon 62:27-39. http://dx.doi.org/10.1016/j.toxicon.2012.09.006.
    • (2013) Toxicon , vol.62 , pp. 27-39
    • Gutiérrez, J.M.1    Lomonte, B.2
  • 12
    • 84870518212 scopus 로고    scopus 로고
    • Emerging roles of secreted phospholipase A(2) enzymes: an update
    • Murakami M, Lambeau G. 2013. Emerging roles of secreted phospholipase A(2) enzymes: an update. Biochimie 95:43-50. http://dx.doi.org/10.1016/j.biochi.2012.09.007.
    • (2013) Biochimie , vol.95 , pp. 43-50
    • Murakami, M.1    Lambeau, G.2
  • 15
    • 0030836586 scopus 로고    scopus 로고
    • Properties and regulation of cytosolic phospholipase A2
    • Leslie CC. 1997. Properties and regulation of cytosolic phospholipase A2. J Biol Chem 272:16709-16712. http://dx.doi.org/10.1074/jbc.272.27.16709.
    • (1997) J Biol Chem , vol.272 , pp. 16709-16712
    • Leslie, C.C.1
  • 16
    • 0033617291 scopus 로고    scopus 로고
    • Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism
    • Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS. 1999. Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Cell 97:349-360.
    • (1999) Cell , vol.97 , pp. 349-360
    • Dessen, A.1    Tang, J.2    Schmidt, H.3    Stahl, M.4    Clark, J.D.5    Seehra, J.6    Somers, W.S.7
  • 17
    • 33748316787 scopus 로고    scopus 로고
    • Properties of the group IV phospholipase A2 family
    • Ghosh M, Tucker DE, Burchett SA, Leslie CC. 2006. Properties of the group IV phospholipase A2 family. Prog Lipid Res 45:487-510. http://dx.doi.org/10.1016/j.plipres.2006.05.003.
    • (2006) Prog Lipid Res , vol.45 , pp. 487-510
    • Ghosh, M.1    Tucker, D.E.2    Burchett, S.A.3    Leslie, C.C.4
  • 19
  • 20
    • 33748745960 scopus 로고    scopus 로고
    • Characterization of the human patatin-like phospholipase family
    • Wilson PA, Gardner SD, Lambie NM, Commans SA, Crowther DJ. 2006. Characterization of the human patatin-like phospholipase family. J Lipid Res 47:1940-1949. http://dx.doi.org/10.1194/jlr.M600185-JLR200.
    • (2006) J Lipid Res , vol.47 , pp. 1940-1949
    • Wilson, P.A.1    Gardner, S.D.2    Lambie, N.M.3    Commans, S.A.4    Crowther, D.J.5
  • 21
    • 0034787011 scopus 로고    scopus 로고
    • Cloning, expression, purification and characterization of patatin, a novel phospholipase A
    • Hirschberg HJ, Simons JW, Dekker N, Egmond MR. 2001. Cloning, expression, purification and characterization of patatin, a novel phospholipase A. Eur J Biochem 268:5037-5044. http://dx.doi.org/10.1046/j.0014-2956.2001.02411.x.
    • (2001) Eur J Biochem , vol.268 , pp. 5037-5044
    • Hirschberg, H.J.1    Simons, J.W.2    Dekker, N.3    Egmond, M.R.4
  • 22
    • 0028853169 scopus 로고
    • Inhibition of Diabrotica larval growth by patatin, the lipid acyl hydrolase from potato tubers
    • Strickland JA, Orr GL, Walsh TA. 1995. Inhibition of Diabrotica larval growth by patatin, the lipid acyl hydrolase from potato tubers. Plant Physiol 109:667-674.
    • (1995) Plant Physiol , vol.109 , pp. 667-674
    • Strickland, J.A.1    Orr, G.L.2    Walsh, T.A.3
  • 23
    • 33646949950 scopus 로고    scopus 로고
    • Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells
    • VanRheenen SM, Luo ZQ, O'Connor T, Isberg RR. 2006. Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells. Infect Immun 74:3597-3606. http://dx.doi.org/10.1128/IAI.02060-05.
    • (2006) Infect Immun , vol.74 , pp. 3597-3606
    • VanRheenen, S.M.1    Luo, Z.Q.2    O'Connor, T.3    Isberg, R.R.4
  • 24
    • 3042608358 scopus 로고    scopus 로고
    • Variation in the effectors of the type III secretion system among Photorhabdus species as revealed by genomic analysis
    • Brugirard-Ricaud K, Givaudan A, Parkhill J, Boemare N, Kunst F, Zumbihl R, Duchaud E. 2004. Variation in the effectors of the type III secretion system among Photorhabdus species as revealed by genomic analysis. J Bacteriol 186:4376-4381. http://dx.doi.org/10.1128/JB.186.13.4376-4381.2004.
    • (2004) J Bacteriol , vol.186 , pp. 4376-4381
    • Brugirard-Ricaud, K.1    Givaudan, A.2    Parkhill, J.3    Boemare, N.4    Kunst, F.5    Zumbihl, R.6    Duchaud, E.7
  • 25
    • 80052551902 scopus 로고    scopus 로고
    • The Rickettsia prowazekii ExoU homologue possesses phospholipase A1 (PLA1), PLA2, and lyso-PLA2 activities and can function in the absence of any eukaryotic cofactors in vitro
    • Housley NA, Winkler HH, Audia JP. 2011. The Rickettsia prowazekii ExoU homologue possesses phospholipase A1 (PLA1), PLA2, and lyso-PLA2 activities and can function in the absence of any eukaryotic cofactors in vitro. J Bacteriol 193:4634-4642. http://dx.doi.org/10.1128/JB.00141-11.
    • (2011) J Bacteriol , vol.193 , pp. 4634-4642
    • Housley, N.A.1    Winkler, H.H.2    Audia, J.P.3
  • 26
  • 29
    • 0142135037 scopus 로고    scopus 로고
    • In vivo phospholipase activity of the Pseudomonas aeruginosa cytotoxin ExoU and protection of mammalian cells with phospholipase A2 inhibitors
    • Phillips RM, Six DA, Dennis EA, Ghosh P. 2003. In vivo phospholipase activity of the Pseudomonas aeruginosa cytotoxin ExoU and protection of mammalian cells with phospholipase A2 inhibitors. J Biol Chem 278: 41326-41332. http://dx.doi.org/10.1074/jbc.M302472200.
    • (2003) J Biol Chem , vol.278 , pp. 41326-41332
    • Phillips, R.M.1    Six, D.A.2    Dennis, E.A.3    Ghosh, P.4
  • 30
    • 83355166268 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU
    • Anderson DM, Schmalzer KM, Sato H, Casey M, Terhune SS, Haas AL, Feix JB, Frank DW. 2011. Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU. Mol Microbiol 82:1454-1467. http://dx.doi.org/10.1111/j.1365-2958.2011.07904.x.
    • (2011) Mol Microbiol , vol.82 , pp. 1454-1467
    • Anderson, D.M.1    Schmalzer, K.M.2    Sato, H.3    Casey, M.4    Terhune, S.S.5    Haas, A.L.6    Feix, J.B.7    Frank, D.W.8
  • 31
    • 55849151286 scopus 로고    scopus 로고
    • Burkholderia thailandensis as a model system for the study of the virulence-associated type III secretion system of Burkholderia pseudomallei
    • Haraga A, West TE, Brittnacher MJ, Skerrett SJ, Miller SI. 2008. Burkholderia thailandensis as a model system for the study of the virulence-associated type III secretion system of Burkholderia pseudomallei. Infect Immun 76:5402-5411. http://dx.doi.org/10.1128/IAI.00626-08.
    • (2008) Infect Immun , vol.76 , pp. 5402-5411
    • Haraga, A.1    West, T.E.2    Brittnacher, M.J.3    Skerrett, S.J.4    Miller, S.I.5
  • 33
    • 80052687938 scopus 로고    scopus 로고
    • Characterisation of Legionella pneumophila phospholipases and their impact on host cells
    • Lang C, Flieger A. 2011. Characterisation of Legionella pneumophila phospholipases and their impact on host cells. Eur J Cell Biol 90:903-912. http://dx.doi.org/10.1016/j.ejcb.2010.12.003.
    • (2011) Eur J Cell Biol , vol.90 , pp. 903-912
    • Lang, C.1    Flieger, A.2
  • 34
    • 77949694407 scopus 로고    scopus 로고
    • Activation of ExoU phospholipase activity requires specific C-terminal regions
    • Schmalzer KM, Benson MA, Frank DW. 2010. Activation of ExoU phospholipase activity requires specific C-terminal regions. J Bacteriol 192:1801-1812. http://dx.doi.org/10.1128/JB.00904-09.
    • (2010) J Bacteriol , vol.192 , pp. 1801-1812
    • Schmalzer, K.M.1    Benson, M.A.2    Frank, D.W.3
  • 35
    • 77955302592 scopus 로고    scopus 로고
    • Role of the membrane localization domain of the Pseudomonas aeruginosa effector protein ExoU in cytotoxicity
    • Veesenmeyer JL, Howell H, Halavaty AS, Ahrens S, Anderson WF, Hauser AR. 2010. Role of the membrane localization domain of the Pseudomonas aeruginosa effector protein ExoU in cytotoxicity. Infect Immun 78:3346-3357. http://dx.doi.org/10.1128/IAI.00223-10.
    • (2010) Infect Immun , vol.78 , pp. 3346-3357
    • Veesenmeyer, J.L.1    Howell, H.2    Halavaty, A.S.3    Ahrens, S.4    Anderson, W.F.5    Hauser, A.R.6
  • 36
    • 84884182244 scopus 로고    scopus 로고
    • Identification of the major ubiquitin-binding domain of the Pseudomonas aeruginosa ExoU A2 phospholipase
    • Anderson DM, Feix JB, Monroe AL, Peterson FC, Volkman BF, Haas AL, Frank DW. 2013. Identification of the major ubiquitin-binding domain of the Pseudomonas aeruginosa ExoU A2 phospholipase. J Biol Chem 288:26741-26752. http://dx.doi.org/10.1074/jbc.M113.478529.
    • (2013) J Biol Chem , vol.288 , pp. 26741-26752
    • Anderson, D.M.1    Feix, J.B.2    Monroe, A.L.3    Peterson, F.C.4    Volkman, B.F.5    Haas, A.L.6    Frank, D.W.7
  • 37
    • 76549098480 scopus 로고    scopus 로고
    • Recent insight into the pathogenicity mechanisms of the emergent pathogen Photorhabdus asymbiotica
    • Costa SC, Chavez CV, Jubelin G, Givaudan A, Escoubas JM, Brehelin M, Zumbihl R. 2010. Recent insight into the pathogenicity mechanisms of the emergent pathogen Photorhabdus asymbiotica. Microbes Infect 12:182-189. http://dx.doi.org/10.1016/j.micinf.2009.12.003.
    • (2010) Microbes Infect , vol.12 , pp. 182-189
    • Costa, S.C.1    Chavez, C.V.2    Jubelin, G.3    Givaudan, A.4    Escoubas, J.M.5    Brehelin, M.6    Zumbihl, R.7
  • 39
    • 0021285424 scopus 로고
    • Extracellular phospholipase A2 and lysophospholipase produced by Vibrio vulnificus
    • Testa J, Daniel LW, Kreger AS. 1984. Extracellular phospholipase A2 and lysophospholipase produced by Vibrio vulnificus. Infect Immun 45:458-463.
    • (1984) Infect Immun , vol.45 , pp. 458-463
    • Testa, J.1    Daniel, L.W.2    Kreger, A.S.3
  • 40
    • 84880654391 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate is a novel coactivator of the Pseudomonas aeruginosa cytotoxin ExoU
    • Tyson GH, Hauser AR. 2013. Phosphatidylinositol 4,5-bisphosphate is a novel coactivator of the Pseudomonas aeruginosa cytotoxin ExoU. Infect Immun 81:2873-2881. http://dx.doi.org/10.1128/IAI.00414-13.
    • (2013) Infect Immun , vol.81 , pp. 2873-2881
    • Tyson, G.H.1    Hauser, A.R.2
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680. http://dx.doi.org/10.1093/nar/22.22.4673.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 33745621121 scopus 로고    scopus 로고
    • Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin
    • Stirling FR, Cuzick A, Kelly SM, Oxley D, Evans TJ. 2006. Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin. Cell Microbiol 8:1294-1309. http://dx.doi.org/10.1111/j.1462-5822.2006.00710.x.
    • (2006) Cell Microbiol , vol.8 , pp. 1294-1309
    • Stirling, F.R.1    Cuzick, A.2    Kelly, S.M.3    Oxley, D.4    Evans, T.J.5
  • 45
    • 72449131834 scopus 로고    scopus 로고
    • A sensitive fluorescencebased assay for the detection of ExoU-mediated PLA(2) activity
    • Benson MA, Schmalzer KM, Frank DW. 2010. A sensitive fluorescencebased assay for the detection of ExoU-mediated PLA(2) activity. Clin Chim Acta 411:190-197. http://dx.doi.org/10.1016/j.cca.2009.10.025.
    • (2010) Clin Chim Acta , vol.411 , pp. 190-197
    • Benson, M.A.1    Schmalzer, K.M.2    Frank, D.W.3
  • 46
    • 84862908377 scopus 로고    scopus 로고
    • Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes
    • Hjerpe R, Thomas Y, Chen J, Zemla A, Curran S, Shpiro N, Dick LR, Kurz T. 2012. Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes. Biochem J 441:927-936. http://dx.doi.org/10.1042/BJ20111671.
    • (2012) Biochem J , vol.441 , pp. 927-936
    • Hjerpe, R.1    Thomas, Y.2    Chen, J.3    Zemla, A.4    Curran, S.5    Shpiro, N.6    Dick, L.R.7    Kurz, T.8
  • 47
    • 0023102474 scopus 로고
    • Microinjection of ubiquitin: intracellular distribution and metabolism in HeLa cells maintained under normal physiological conditions
    • Carlson N, Rechsteiner M. 1987. Microinjection of ubiquitin: intracellular distribution and metabolism in HeLa cells maintained under normal physiological conditions. J Cell Biol 104:537-546. http://dx.doi.org/10.1083/jcb.104.3.537.
    • (1987) J Cell Biol , vol.104 , pp. 537-546
    • Carlson, N.1    Rechsteiner, M.2
  • 48
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates
    • Haas AL, Bright PM. 1985. The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates. J Biol Chem 260: 12464-12473.
    • (1985) J Biol Chem , vol.260 , pp. 12464-12473
    • Haas, A.L.1    Bright, P.M.2
  • 49
    • 79961000536 scopus 로고    scopus 로고
    • Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools
    • Kaiser SE, Riley BE, Shaler TA, Trevino RS, Becker CH, Schulman H, Kopito RR. 2011. Protein standard absolute quantification (PSAQ) method for the measurement of cellular ubiquitin pools. Nat Methods 8:691-696. http://dx.doi.org/10.1038/nmeth.1649.
    • (2011) Nat Methods , vol.8 , pp. 691-696
    • Kaiser, S.E.1    Riley, B.E.2    Shaler, T.A.3    Trevino, R.S.4    Becker, C.H.5    Schulman, H.6    Kopito, R.R.7
  • 50
    • 0033580277 scopus 로고    scopus 로고
    • Broad-host-range expression vectors that carry the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator
    • Newman JR, Fuqua C. 1999. Broad-host-range expression vectors that carry the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator. Gene 227:197-203.
    • (1999) Gene , vol.227 , pp. 197-203
    • Newman, J.R.1    Fuqua, C.2
  • 51
    • 0034977803 scopus 로고    scopus 로고
    • Multiple domains are required for the toxic activity of Pseudomonas aeruginosa ExoU
    • Finck-Barbançon V, Frank DW. 2001. Multiple domains are required for the toxic activity of Pseudomonas aeruginosa ExoU. J Bacteriol 183:4330-4344. http://dx.doi.org/10.1128/JB.183.14.4330-4344.2001.
    • (2001) J Bacteriol , vol.183 , pp. 4330-4344
    • Finck-Barbançon, V.1    Frank, D.W.2
  • 52
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman MR, Yount NY. 2003. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55:27-55. http://dx.doi.org/10.1124/pr.55.1.2.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 54
    • 84904896550 scopus 로고    scopus 로고
    • Intoxication of host cells by the T3SS phospholipase ExoU: PI(4,5)P2-associated, cytoskeletal collapse and late phase membrane blebbing
    • Sato H, Frank DW. 2014. Intoxication of host cells by the T3SS phospholipase ExoU: PI(4,5)P2-associated, cytoskeletal collapse and late phase membrane blebbing. PLoS One 9:e103127. http://dx.doi.org/10.1371/journal.pone.0103127.
    • (2014) PLoS One , vol.9
    • Sato, H.1    Frank, D.W.2
  • 55
    • 78650140661 scopus 로고    scopus 로고
    • Culturability and survival of marine, freshwater and clinical Pseudomonas aeruginosa
    • Khan NH, Ahsan M, Taylor WD, Kogure K. 2010. Culturability and survival of marine, freshwater and clinical Pseudomonas aeruginosa. Microbes Environ 25:266-274. http://dx.doi.org/10.1264/jsme2.ME09178.
    • (2010) Microbes Environ , vol.25 , pp. 266-274
    • Khan, N.H.1    Ahsan, M.2    Taylor, W.D.3    Kogure, K.4
  • 56
    • 0035788450 scopus 로고    scopus 로고
    • Type III secretion in plant growth-promoting Pseudomonas fluorescens SBW25
    • Preston GM, Bertrand N, Rainey PB. 2001. Type III secretion in plant growth-promoting Pseudomonas fluorescens SBW25. Mol Microbiol 41: 999-1014. http://dx.doi.org/10.1046/j.1365-2958.2001.02560.x.
    • (2001) Mol Microbiol , vol.41 , pp. 999-1014
    • Preston, G.M.1    Bertrand, N.2    Rainey, P.B.3
  • 57
    • 62449271421 scopus 로고    scopus 로고
    • The emerging human pathogen Photorhabdus asymbiotica is a facultative intracellular bacterium and induces apoptosis of macrophage-like cells
    • Costa SC, Girard PA, Brehelin M, Zumbihl R. 2009. The emerging human pathogen Photorhabdus asymbiotica is a facultative intracellular bacterium and induces apoptosis of macrophage-like cells. Infect Immun 77:1022-1030. http://dx.doi.org/10.1128/IAI.01064-08.
    • (2009) Infect Immun , vol.77 , pp. 1022-1030
    • Costa, S.C.1    Girard, P.A.2    Brehelin, M.3    Zumbihl, R.4
  • 58
    • 84863264532 scopus 로고    scopus 로고
    • Genome sequence of the highly efficient arsenite-oxidizing bacterium Achromobacter arsenitoxydans SY8
    • Li X, Hu Y, Gong J, Lin Y, Johnstone L, Rensing C, Wang G. 2012. Genome sequence of the highly efficient arsenite-oxidizing bacterium Achromobacter arsenitoxydans SY8. J Bacteriol 194:1243-1244. http://dx.doi.org/10.1128/JB.06667-11.
    • (2012) J Bacteriol , vol.194 , pp. 1243-1244
    • Li, X.1    Hu, Y.2    Gong, J.3    Lin, Y.4    Johnstone, L.5    Rensing, C.6    Wang, G.7
  • 61
    • 84861215846 scopus 로고    scopus 로고
    • Genome sequence of the polyhydroxybutyrate producer Pseudomonas extremaustralis, a highly stressresistant Antarctic bacterium
    • Tribelli PM, Raiger Iustman LJ, Catone MV, Di Martino C, Revale S, Mendez BS, Lopez NI. 2012. Genome sequence of the polyhydroxybutyrate producer Pseudomonas extremaustralis, a highly stressresistant Antarctic bacterium. J Bacteriol 194:2381-2382. http://dx.doi.org/10.1128/JB.00172-12.
    • (2012) J Bacteriol , vol.194 , pp. 2381-2382
    • Tribelli, P.M.1    Raiger Iustman, L.J.2    Catone, M.V.3    Di Martino, C.4    Revale, S.5    Mendez, B.S.6    Lopez, N.I.7
  • 62
    • 84997839837 scopus 로고    scopus 로고
    • Draft genome sequence of Pseudomonas plecoglossicida strain NB2011, the causative agent of white nodules in large yellow croaker (Larimichthys crocea)
    • e00586-13
    • Mao Z, Li M, Chen J. 2013. Draft genome sequence of Pseudomonas plecoglossicida strain NB2011, the causative agent of white nodules in large yellow croaker (Larimichthys crocea). Genome Announc 1(4): e00586-13. http://dx.doi.org/10.1128/genomeA.00586-13.
    • (2013) Genome Announc , vol.1 , Issue.4
    • Mao, Z.1    Li, M.2    Chen, J.3
  • 63
    • 75749111012 scopus 로고    scopus 로고
    • Pseudomonas syringae strains naturally lacking the classical P. syringae hrp/hrc locus are common leaf colonizers equipped with an atypical type III secretion system
    • Clarke CR, Cai R, Studholme DJ, Guttman DS, Vinatzer BA. 2010. Pseudomonas syringae strains naturally lacking the classical P. syringae hrp/hrc locus are common leaf colonizers equipped with an atypical type III secretion system. Mol Plant Microbe Interact 23:198-210. http://dx.doi.org/10.1094/MPMI-23-2-0198.
    • (2010) Mol Plant Microbe Interact , vol.23 , pp. 198-210
    • Clarke, C.R.1    Cai, R.2    Studholme, D.J.3    Guttman, D.S.4    Vinatzer, B.A.5
  • 64
    • 33646910500 scopus 로고    scopus 로고
    • Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens
    • Ogata H, La Scola B, Audic S, Renesto P, Blanc G, Robert C, Fournier PE, Claverie JM, Raoult D. 2006. Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens. PLoS Genet 2:e76. http://dx.doi.org/10.1371/journal.pgen.0020076.
    • (2006) PLoS Genet , vol.2
    • Ogata, H.1    La Scola, B.2    Audic, S.3    Renesto, P.4    Blanc, G.5    Robert, C.6    Fournier, P.E.7    Claverie, J.M.8    Raoult, D.9

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.