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Volumn 16, Issue 1, 2016, Pages

Novel cationic peptide TP359 down-regulates the expression of outer membrane biogenesis genes in Pseudomonas aeruginosa: A potential TP359 anti-microbial mechanism

Author keywords

Antimicrobial effect; Antimicrobial peptides; Pseudomonas aeruginosa

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; MEMBRANE PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; PORIN; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; OPRF PROTEIN, PSEUDOMONAS AERUGINOSA; OUTER MEMBRANE PROTEIN;

EID: 84983283339     PISSN: None     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/s12866-016-0808-2     Document Type: Article
Times cited : (9)

References (57)
  • 1
    • 39449115488 scopus 로고    scopus 로고
    • Mechanism and inhibition of LpxC: An essential zinc-dependent deacetylase of bacterial lipid A synthesis
    • 1:CAS:528:DC%2BD1cXitVGjt70%3D 18289052 3022321
    • Barb AW, Zhou P. Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis. Curr Pharm Biotechnol. 2008;9:9-15.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 9-15
    • Barb, A.W.1    Zhou, P.2
  • 2
    • 84947036953 scopus 로고    scopus 로고
    • Antimicrobial peptides: Possible anti-infective agents
    • Narayana JL, Chen JY. Antimicrobial peptides: Possible anti-infective agents. Peptides. 2015;72:88-94.
    • (2015) Peptides , vol.72 , pp. 88-94
    • Narayana, J.L.1    Chen, J.Y.2
  • 3
    • 0242353107 scopus 로고    scopus 로고
    • Antimicrobial peptides in animals and their role in host defences
    • 1:CAS:528:DC%2BD3sXos1Khtrg%3D 14602364
    • Brogden KA, Ackermann M, McCray Jr PB, Tack BF. Antimicrobial peptides in animals and their role in host defences. Int J Antimicrob Agents. 2003;22:465-78.
    • (2003) Int J Antimicrob Agents , vol.22 , pp. 465-478
    • Brogden, K.A.1    Ackermann, M.2    McCray, P.B.3    Tack, B.F.4
  • 5
    • 84943816958 scopus 로고    scopus 로고
    • Defensive remodeling: How bacterial surface properties and biofilm formation promote resistance to antimicrobial peptides
    • Nuri R, Shprung T, Shai Y. Defensive remodeling: How bacterial surface properties and biofilm formation promote resistance to antimicrobial peptides. Biochim Biophys Acta. 2015;11:3089-100.
    • (2015) Biochim Biophys Acta , vol.11 , pp. 3089-3100
    • Nuri, R.1    Shprung, T.2    Shai, Y.3
  • 6
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • 1:CAS:528:DC%2BD3sXisVKgsLg%3D 12615953
    • Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev. 2003;55:27-55.
    • (2003) Pharmacol Rev , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 7
    • 50249103779 scopus 로고    scopus 로고
    • Antimicrobial peptides: Natural templates for synthetic membrane-active compounds
    • 1:CAS:528:DC%2BD1cXhtVansr3E 18661101
    • Giuliani A, Pirri G, Bozzi A, Di Giulio A, Aschi M, Rinaldi AC. Antimicrobial peptides: natural templates for synthetic membrane-active compounds. Cell Mol Life Sci. 2008;65:2450-60.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2450-2460
    • Giuliani, A.1    Pirri, G.2    Bozzi, A.3    Di Giulio, A.4    Aschi, M.5    Rinaldi, A.C.6
  • 8
    • 0034424412 scopus 로고    scopus 로고
    • Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa
    • 1:CAS:528:DC%2BD3MXhs1Kit74%3D 11083634 90199
    • Zhang L, Dhillon P, Yan H, Farmer S, Hancock REW. Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa. Antimicrob Agents Chemother. 2000;44:3317-21.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 3317-3321
    • Zhang, L.1    Dhillon, P.2    Yan, H.3    Farmer, S.4    Hancock, R.E.W.5
  • 9
    • 3242795872 scopus 로고    scopus 로고
    • Risk factors for multidrug-resistant Pseudomonas aeruginosa nosocomial infection
    • 1:STN:280:DC%2BD2czjsVyktQ%3D%3D 15236849
    • Defez C, Fabbro-Peray P, Bouziges N, Gouby A, Mahamat A, Daurès JP, et al. Risk factors for multidrug-resistant Pseudomonas aeruginosa nosocomial infection. J Hosp Infect. 2004;57:209-16.
    • (2004) J Hosp Infect , vol.57 , pp. 209-216
    • Defez, C.1    Fabbro-Peray, P.2    Bouziges, N.3    Gouby, A.4    Mahamat, A.5    Daurès, J.P.6
  • 10
    • 0020731751 scopus 로고
    • Infections caused by Pseudomonas aeruginosa
    • 1:STN:280:DyaL3s7ps1Ojtg%3D%3D 6405475
    • Bodey GP, Bolivar R, Fainstein V, Jadeja L. Infections caused by Pseudomonas aeruginosa. Rev Infect Dis. 1983;5:279-313.
    • (1983) Rev Infect Dis , vol.5 , pp. 279-313
    • Bodey, G.P.1    Bolivar, R.2    Fainstein, V.3    Jadeja, L.4
  • 12
    • 84918778416 scopus 로고    scopus 로고
    • Effects of azithromycin on Pseudomonas aeruginosa isolates from catheter-associated urinary tract infection
    • 1:CAS:528:DC%2BC2cXjtFWrtLs%3D 25574236 4280936
    • Xu Z, Gao Y, He J, Xu W, Jiang M, Jin H. Effects of azithromycin on Pseudomonas aeruginosa isolates from catheter-associated urinary tract infection. Exp Ther Med. 2014;9:569-72.
    • (2014) Exp Ther Med , vol.9 , pp. 569-572
    • Xu, Z.1    Gao, Y.2    He, J.3    Xu, W.4    Jiang, M.5    Jin, H.6
  • 13
    • 33750577582 scopus 로고    scopus 로고
    • Enhancement of antimicrobial activity against Pseudomonas aeruginosa by coadministration of G10KHc and tobramycin
    • 1:CAS:528:DC%2BD28XhtFOkt7bO 16940063 1635211
    • Eckert R, Keith MB, Greenberg EP, Qi F, Yarbrough DK, He J, et al. Enhancement of antimicrobial activity against Pseudomonas aeruginosa by coadministration of G10KHc and tobramycin. Antimicrob Agents Chemother. 2006;50:3833-8.
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 3833-3838
    • Eckert, R.1    Keith, M.B.2    Greenberg, E.P.3    Qi, F.4    Yarbrough, D.K.5    He, J.6
  • 14
    • 77149173463 scopus 로고    scopus 로고
    • Protection against Pseudomonas aeruginosa lung infection in mice by recombinant OprF-pulsed dendritic cell immunization
    • 20070893 2820439
    • Peluso L, de Luca C, Bozza S, Leonardi A, Giovannini G, Lavorgna A, et al. Protection against Pseudomonas aeruginosa lung infection in mice by recombinant OprF-pulsed dendritic cell immunization. BMC Microbiol. 2010;10:9.
    • (2010) BMC Microbiol , vol.10 , pp. 9
    • Peluso, L.1    De Luca, C.2    Bozza, S.3    Leonardi, A.4    Giovannini, G.5    Lavorgna, A.6
  • 15
    • 33846284918 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa chronic colonization in cystic fibrosis patients
    • 17224667
    • Murray TS, Egan M, Kazmierczak BI. Pseudomonas aeruginosa chronic colonization in cystic fibrosis patients. Curr Opin Pediatr. 2007;19:83-8.
    • (2007) Curr Opin Pediatr , vol.19 , pp. 83-88
    • Murray, T.S.1    Egan, M.2    Kazmierczak, B.I.3
  • 16
    • 84878113691 scopus 로고    scopus 로고
    • Respiratory bacterial infections in cystic fibrosis
    • 23449384
    • Ciofu O, Hansen CR, Hoiby N. Respiratory bacterial infections in cystic fibrosis. Curr Opin Pulm Med. 2013;19:251-8.
    • (2013) Curr Opin Pulm Med , vol.19 , pp. 251-258
    • Ciofu, O.1    Hansen, C.R.2    Hoiby, N.3
  • 17
    • 0036431716 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa in cystic fibrosis: Pathogenesis and persistence
    • 12297059
    • Davies JC. Pseudomonas aeruginosa in cystic fibrosis: pathogenesis and persistence. Paediatr Respir Rev. 2002;3:128-34.
    • (2002) Paediatr Respir Rev , vol.3 , pp. 128-134
    • Davies, J.C.1
  • 19
    • 79955763337 scopus 로고    scopus 로고
    • Pneumonia due to Pseudomonas aeruginosa: Part II: Antimicrobial resistance, pharmacodynamic concepts, and antibiotic therapy convert from a non-mucoid to a mucoid state
    • 21540216
    • Sun H, Fujitani S, Quintiliani R, Yu VL. Pneumonia due to Pseudomonas aeruginosa: part II: antimicrobial resistance, pharmacodynamic concepts, and antibiotic therapy convert from a non-mucoid to a mucoid state. Chest. 2011;139:1172-85.
    • (2011) Chest , vol.139 , pp. 1172-1185
    • Sun, H.1    Fujitani, S.2    Quintiliani, R.3    Yu, V.L.4
  • 20
    • 34547109626 scopus 로고    scopus 로고
    • Mucoid Pseudomonas in cystic fibrosis
    • 17580270
    • Pritt B, O'Brien L, Winn W. Mucoid Pseudomonas in cystic fibrosis. Am J Clin Pathol. 2007;128(1):32-4.
    • (2007) Am J Clin Pathol , vol.128 , Issue.1 , pp. 32-34
    • Pritt, B.1    O'Brien, L.2    Winn, W.3
  • 21
    • 0034878704 scopus 로고    scopus 로고
    • Alginate overproduction affects Pseudomonas aeruginosa biofilm structure and function
    • 1:CAS:528:DC%2BD3MXmsFyqtLc%3D 11514525 95424
    • Hentzer M, Teitzel GM, Balzer GJ, Heydorn A, Molin S, Givskov M, et al. Alginate overproduction affects Pseudomonas aeruginosa biofilm structure and function. J Bacteriol. 2001;183:5395-401.
    • (2001) J Bacteriol , vol.183 , pp. 5395-5401
    • Hentzer, M.1    Teitzel, G.M.2    Balzer, G.J.3    Heydorn, A.4    Molin, S.5    Givskov, M.6
  • 22
    • 12844270608 scopus 로고    scopus 로고
    • Longitudinal development of mucoid Pseudomonas aeruginosa infection and lung disease progression in children with cystic fibrosis
    • 1:CAS:528:DC%2BD2MXhtVWqsLc%3D 15687313
    • Li Z, Kosorok MR, Farrell PM, Laxova A, West SE, Green CG, et al. Longitudinal development of mucoid Pseudomonas aeruginosa infection and lung disease progression in children with cystic fibrosis. JAMA. 2005;293:581-8.
    • (2005) JAMA , vol.293 , pp. 581-588
    • Li, Z.1    Kosorok, M.R.2    Farrell, P.M.3    Laxova, A.4    West, S.E.5    Green, C.G.6
  • 23
    • 0025366711 scopus 로고
    • Phenotypic conversion of Pseudomonas aeruginosa in cystic fibrosis
    • 1:STN:280:DyaK3czjvVentQ%3D%3D 2116444 267893
    • Fegan M, Francis P, Hayward AC, Davis GH, Fuerst JA. Phenotypic conversion of Pseudomonas aeruginosa in cystic fibrosis. J Clin Microbiol. 1990;28:1143-6.
    • (1990) J Clin Microbiol , vol.28 , pp. 1143-1146
    • Fegan, M.1    Francis, P.2    Hayward, A.C.3    Davis, G.H.4    Fuerst, J.A.5
  • 25
    • 77955413607 scopus 로고    scopus 로고
    • Early eradication of Pseudomonas aeruginosa in patients with cystic fibrosis
    • 20692633 4001925
    • Stuart B, Lin JH, Mogayzel Jr PJ. Early eradication of Pseudomonas aeruginosa in patients with cystic fibrosis. Paediatr Respir Rev. 2010;11:177-84.
    • (2010) Paediatr Respir Rev , vol.11 , pp. 177-184
    • Stuart, B.1    Lin, J.H.2    Mogayzel, P.J.3
  • 26
    • 34548684339 scopus 로고    scopus 로고
    • PEPstr: A de novo method for tertiary structure prediction of small bioactive peptides
    • 1:CAS:528:DC%2BD2sXhtFansbrI 17897087
    • Kaur H, Garg A, Raghava GP. PEPstr: a de novo method for tertiary structure prediction of small bioactive peptides. Protein Pept Lett. 2007;14:626-31.
    • (2007) Protein Pept Lett , vol.14 , pp. 626-631
    • Kaur, H.1    Garg, A.2    Raghava, G.P.3
  • 27
    • 84983299889 scopus 로고    scopus 로고
    • Methods for Dilution Antimicrobial Susceptibility
    • ICLSI CLSI document M07-A9. Wayne: Clinical and Laboratory Standards Institute
    • ICLSI. Methods for Dilution Antimicrobial Susceptibility. Tests for Bacteria That Grow Aerobically; Approved Standard - Ninth Edition. CLSI document M07-A9. Wayne: Clinical and Laboratory Standards Institute; 2012.
    • (2012) Tests for Bacteria That Grow Aerobically; Approved Standard - Ninth Edition
  • 28
    • 84939618236 scopus 로고    scopus 로고
    • Silver-coated carbon nanotubes downregulate the expression of Pseudomonas aeruginosa virulence genes: A potential mechanism for their antimicrobial effect
    • 1:CAS:528:DC%2BC28XitFWiu74%3D 26346483 4531027
    • Dosunmu E, Chaudhari AA, Singh SR, Dennis VA, Pillai SR. Silver-coated carbon nanotubes downregulate the expression of Pseudomonas aeruginosa virulence genes: a potential mechanism for their antimicrobial effect. Int J Nanomedicine. 2015;10:5025-34.
    • (2015) Int J Nanomedicine , vol.10 , pp. 5025-5034
    • Dosunmu, E.1    Chaudhari, A.A.2    Singh, S.R.3    Dennis, V.A.4    Pillai, S.R.5
  • 29
    • 0026663130 scopus 로고
    • Tests for bactericidal effects of antimicrobial agents: Technical performance and clinical relevance
    • 1:CAS:528:DyaK3sXjsFersw%3D%3D 1423219 358258
    • Peterson LR, Shanholtzer CJ. Tests for bactericidal effects of antimicrobial agents: technical performance and clinical relevance. Clin Microbiol Rev. 1992;5:420-32.
    • (1992) Clin Microbiol Rev , vol.5 , pp. 420-432
    • Peterson, L.R.1    Shanholtzer, C.J.2
  • 31
    • 84880092437 scopus 로고    scopus 로고
    • Anti-inflammatory effects of silver-polyvinyl pyrrolidone (Ag-PVP) nanoparticles in mouse macrophages infected with live Chlamydia trachomatis
    • 23882139 3709643
    • Yilma AN, Singh SR, Dixit S, Dennis VA. Anti-inflammatory effects of silver-polyvinyl pyrrolidone (Ag-PVP) nanoparticles in mouse macrophages infected with live Chlamydia trachomatis. Int J Nanomedicine. 2013;8:2421-32.
    • (2013) Int J Nanomedicine , vol.8 , pp. 2421-2432
    • Yilma, A.N.1    Singh, S.R.2    Dixit, S.3    Dennis, V.A.4
  • 32
    • 84908276445 scopus 로고    scopus 로고
    • Ramoplanin at bactericidal concentrations induces bacterial membrane depolarization in Staphylococcus aureus
    • 25182650 4249368
    • Cheng M, Huang JX, Ramu S, Butler MS, Cooper MA. Ramoplanin at bactericidal concentrations induces bacterial membrane depolarization in Staphylococcus aureus. Antimicrob Agents Chemother. 2014;58:6819-27.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 6819-6827
    • Cheng, M.1    Huang, J.X.2    Ramu, S.3    Butler, M.S.4    Cooper, M.A.5
  • 33
    • 84866362629 scopus 로고    scopus 로고
    • Different patterns of expression and of IL-10 modulation of inflammatory mediators from macrophages of Lyme disease-resistant and -susceptible mice
    • 1:CAS:528:DC%2BC38XhsVSjur7O 23024745 3443101
    • Gautam A, Dixit S, Embers M, Gautam R, Philipp MT, Singh SR, et al. Different patterns of expression and of IL-10 modulation of inflammatory mediators from macrophages of Lyme disease-resistant and -susceptible mice. PLoS One. 2012;7:e43860.
    • (2012) PLoS One , vol.7 , pp. e43860
    • Gautam, A.1    Dixit, S.2    Embers, M.3    Gautam, R.4    Philipp, M.T.5    Singh, S.R.6
  • 34
    • 84905409048 scopus 로고    scopus 로고
    • A proteomic approach to understand the role of the outer membrane porins in the organic solvent-tolerance of Pseudomonas aeruginosa PseA
    • 1:CAS:528:DC%2BC2cXhs1eqsrfM 25089526 4121210
    • Hemamalini R, Khare S. A proteomic approach to understand the role of the outer membrane porins in the organic solvent-tolerance of Pseudomonas aeruginosa PseA. PLoS One. 2014;9:e103788.
    • (2014) PLoS One , vol.9 , pp. e103788
    • Hemamalini, R.1    Khare, S.2
  • 35
    • 84873658266 scopus 로고    scopus 로고
    • A Peptide derived from phage Display Library Exhibits Antimicrobial Activity against E. Coli and Pseudomonas aeruginosa
    • 1:CAS:528:DC%2BC3sXjtFKgt70%3D
    • Rao SS, Ketha VKM, Atreya CD. A Peptide derived from phage Display Library Exhibits Antimicrobial Activity against E. coli and Pseudomonas aeruginosa. PLoS One. 2013;8:e56081.
    • (2013) PLoS One , vol.8 , pp. e56081
    • Rao, S.S.1    Ketha, V.K.M.2    Atreya, C.D.3
  • 36
    • 84866334456 scopus 로고    scopus 로고
    • Transcription of the oprF gene of Pseudomonas aeruginosa is dependent mainly on the SigX sigma factor and is sucrose induced
    • Emeline B, Gwendoline G, Alexis B, Manjeet B, Olivier M, Julien V, et al. Transcription of the oprF gene of Pseudomonas aeruginosa is dependent mainly on the SigX sigma factor and is sucrose induced. J Bacteriol. 2012;194:4301-11.
    • (2012) J Bacteriol , vol.194 , pp. 4301-4311
    • Emeline, B.1    Gwendoline, G.2    Alexis, B.3    Manjeet, B.4    Olivier, M.5    Julien, V.6
  • 37
    • 77955377305 scopus 로고    scopus 로고
    • Damage of the bacterial cell envelope by antimicrobial peptides gramicidin S and PGLa as revealed by transmission and scanning electron microscopy
    • 1:CAS:528:DC%2BC3cXhtVOms7nL 20530225 2916356
    • Hartmann M, Berditsch M, Hawecker J, Ardakani MF, Gerthsen D, Ulrich AS. Damage of the bacterial cell envelope by antimicrobial peptides gramicidin S and PGLa as revealed by transmission and scanning electron microscopy. Antimicrob Agents Chemother. 2010;54:3132-42.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 3132-3142
    • Hartmann, M.1    Berditsch, M.2    Hawecker, J.3    Ardakani, M.F.4    Gerthsen, D.5    Ulrich, A.S.6
  • 38
    • 77955658184 scopus 로고    scopus 로고
    • Selective toxicity of antimicrobial peptide S-thanatin on bacteria
    • 1:CAS:528:DC%2BC3cXhtVaqur3K 20600431
    • Wu G, Wu H, Fan X, Zhao R, Li X, Wang S, et al. Selective toxicity of antimicrobial peptide S-thanatin on bacteria. Peptides. 2010;31:1669-73.
    • (2010) Peptides , vol.31 , pp. 1669-1673
    • Wu, G.1    Wu, H.2    Fan, X.3    Zhao, R.4    Li, X.5    Wang, S.6
  • 39
    • 33645119895 scopus 로고    scopus 로고
    • Investigation of the cytotoxicity of eukaryotic and prokaryotic antimicrobial peptides in intestinal epithelial cells invitro
    • Mahera S, McCleana S. Investigation of the cytotoxicity of eukaryotic and prokaryotic antimicrobial peptides in intestinal epithelial cells invitro. Biochem Pharmacol. 2006;71:1289-98.
    • (2006) Biochem Pharmacol , vol.71 , pp. 1289-1298
    • Mahera, S.1    McCleana, S.2
  • 40
    • 1442314720 scopus 로고    scopus 로고
    • Cell entry and antimicrobial properties of eukaryotic cell-penetrating peptides
    • 1:CAS:528:DC%2BD2cXht1GjtLs%3D 14656995
    • Nekhotiaeva N, Elmquist A, Rajarao GK, Hällbrink M, Langel U, Good L. Cell entry and antimicrobial properties of eukaryotic cell-penetrating peptides. FASEB J. 2004;18:394-6.
    • (2004) FASEB J , vol.18 , pp. 394-396
    • Nekhotiaeva, N.1    Elmquist, A.2    Rajarao, G.K.3    Hällbrink, M.4    Langel, U.5    Good, L.6
  • 41
    • 84892170602 scopus 로고    scopus 로고
    • Antibiotic development challenges: The various mechanisms of action of antimicrobial peptides and of bacterial resistance
    • 24367355 3856679
    • Guilhelmelli F, Vilela N, Albuquerque P, Derengowski Lda S, Silva-Pereira I, Kyaw CM. Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance. Front Microbiol. 2013;4:353.
    • (2013) Front Microbiol , vol.4 , pp. 353
    • Guilhelmelli, F.1    Vilela, N.2    Albuquerque, P.3    Derengowski Lda, S.4    Silva-Pereira, I.5    Kyaw, C.M.6
  • 42
    • 84872856945 scopus 로고    scopus 로고
    • Peptide antimicrobials: Cell wall as a bacterial target
    • 1:CAS:528:DC%2BC3sXjtVCgtbk%3D 23302022
    • Yount NY, Yeaman MR. Peptide antimicrobials: cell wall as a bacterial target. Ann N Y Acad Sci. 2013;1277:127-38.
    • (2013) Ann N y Acad Sci , vol.1277 , pp. 127-138
    • Yount, N.Y.1    Yeaman, M.R.2
  • 43
    • 0034921952 scopus 로고    scopus 로고
    • Diversity in antistaphylococcal mechanisms among membrane-targeting antimicrobial peptides
    • 1:CAS:528:DC%2BD3MXlsV2hsrs%3D 11447168 98582
    • Koo SP, Bayer AS, Yeaman MR. Diversity in antistaphylococcal mechanisms among membrane-targeting antimicrobial peptides. Infect Immun. 2001;69:4916-22.
    • (2001) Infect Immun , vol.69 , pp. 4916-4922
    • Koo, S.P.1    Bayer, A.S.2    Yeaman, M.R.3
  • 44
    • 84867320805 scopus 로고    scopus 로고
    • Specific association of lectin LecB with the surface of Pseudomonas aeruginosa: Role of outer membrane protein OprF
    • 1:CAS:528:DC%2BC38XhsFCitrjE 23056489 3466170
    • Funken H, Bartels KM, Wilhelm S, Brocker M, Bott M, Bains M, et al. Specific association of lectin LecB with the surface of Pseudomonas aeruginosa: role of outer membrane protein OprF. PLoS One. 2012;7:e46857.
    • (2012) PLoS One , vol.7 , pp. e46857
    • Funken, H.1    Bartels, K.M.2    Wilhelm, S.3    Brocker, M.4    Bott, M.5    Bains, M.6
  • 45
    • 0347777343 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa anaerobic respiration in biofilms: Relationships to cystic fibrosis pathogenesis
    • 1:CAS:528:DC%2BD38Xot12jurc%3D 12408810
    • Yoon SS, Hennigan RF, Hilliard GM, Ochsner UA, Parvatiyar K, Kamani MC, et al. Pseudomonas aeruginosa anaerobic respiration in biofilms: relationships to cystic fibrosis pathogenesis. Dev Cell. 2002;3:593-603.
    • (2002) Dev Cell , vol.3 , pp. 593-603
    • Yoon, S.S.1    Hennigan, R.F.2    Hilliard, G.M.3    Ochsner, U.A.4    Parvatiyar, K.5    Kamani, M.C.6
  • 46
    • 84872134823 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa peptidoglycan-associated outer membrane proteins in vesicle formation
    • 1:CAS:528:DC%2BC3sXltVOis7w%3D 23123904 3553829
    • Wessel AK, Liew J, Kwon T, Marcotte EM, Whiteley M. Role of Pseudomonas aeruginosa peptidoglycan-associated outer membrane proteins in vesicle formation. J Bacteriol. 2013;195:213-9.
    • (2013) J Bacteriol , vol.195 , pp. 213-219
    • Wessel, A.K.1    Liew, J.2    Kwon, T.3    Marcotte, E.M.4    Whiteley, M.5
  • 47
    • 84870373770 scopus 로고    scopus 로고
    • Manuka honey is bactericidal against Pseudomonas aeruginosa and results in differential expression of oprF and algD
    • 1:CAS:528:DC%2BC3sXhslGitrc%3D 23082035
    • Roberts AE, Maddocks SE, Cooper RA. Manuka honey is bactericidal against Pseudomonas aeruginosa and results in differential expression of oprF and algD. Microbiology. 2012;158:3005-13.
    • (2012) Microbiology , vol.158 , pp. 3005-3013
    • Roberts, A.E.1    Maddocks, S.E.2    Cooper, R.A.3
  • 48
    • 44349193490 scopus 로고    scopus 로고
    • Opr86 Is Essential for Viability and Is a Potential Candidate for a Protective Antigen against Biofilm Formation by Pseudomonas aeruginosa
    • 1:CAS:528:DC%2BD1cXmsVOmsLc%3D 18390657 2395022
    • Tashiro Y, Nomura N, Nakao R, Senpuku H, Kariyama R, Kumon H, et al. Opr86 Is Essential for Viability and Is a Potential Candidate for a Protective Antigen against Biofilm Formation by Pseudomonas aeruginosa. J Bacteriol. 2008;190:3969-78.
    • (2008) J Bacteriol , vol.190 , pp. 3969-3978
    • Tashiro, Y.1    Nomura, N.2    Nakao, R.3    Senpuku, H.4    Kariyama, R.5    Kumon, H.6
  • 49
    • 78651267246 scopus 로고    scopus 로고
    • Pseudomonas Genome Database: Improved comparative analysis and population genomics capability for Pseudomonas genomes
    • 1:CAS:528:DC%2BC3sXivF2msLs%3D 20929876
    • Winsor GL, Lam DK, Fleming L, Lo R, Whiteside MD, Yu NY, et al. Pseudomonas Genome Database: improved comparative analysis and population genomics capability for Pseudomonas genomes. Nucleic Acids Res. 2011;39:D596-600.
    • (2011) Nucleic Acids Res , vol.39 , pp. D596-600
    • Winsor, G.L.1    Lam, D.K.2    Fleming, L.3    Lo, R.4    Whiteside, M.D.5    Yu, N.Y.6
  • 50
    • 84870376877 scopus 로고    scopus 로고
    • Potent antibacterial antisense peptide-peptide nucleic acid conjugates against Pseudomonas aeruginosa
    • 1:CAS:528:DC%2BC38XhsVCjt73J 23030590 3464458
    • Ghosal A, Nielsen PE. Potent antibacterial antisense peptide-peptide nucleic acid conjugates against Pseudomonas aeruginosa. Nucleic Acid Ther. 2012;22:323-34.
    • (2012) Nucleic Acid Ther , vol.22 , pp. 323-334
    • Ghosal, A.1    Nielsen, P.E.2
  • 51
    • 84883487894 scopus 로고    scopus 로고
    • (1) H, (1)(3) C and (1)(5) N assignments of the holo-acyl carrier protein of Pseudomonas aeruginosa
    • 1:CAS:528:DC%2BC3sXhtlOrsbrO 22843382
    • Duggan BM, Roca A, Zhang YM. (1) H, (1)(3) C and (1)(5) N assignments of the holo-acyl carrier protein of Pseudomonas aeruginosa. Biomol NMR Assign. 2013;7:225-8.
    • (2013) Biomol NMR Assign , vol.7 , pp. 225-228
    • Duggan, B.M.1    Roca, A.2    Zhang, Y.M.3
  • 52
    • 79251553514 scopus 로고    scopus 로고
    • Contribution of cell elongation to the biofilm formation of Pseudomonas aeruginosa during anaerobic respiration
    • 1:CAS:528:DC%2BC3MXht1Oiur8%3D 21267455 3022656
    • Yoon MY, Lee K, Park Y, Yoon SS. Contribution of cell elongation to the biofilm formation of Pseudomonas aeruginosa during anaerobic respiration. PLoS One. 2011;6:e16105.
    • (2011) PLoS One , vol.6 , pp. e16105
    • Yoon, M.Y.1    Lee, K.2    Park, Y.3    Yoon, S.S.4
  • 53
    • 17644401295 scopus 로고    scopus 로고
    • Peptide inhibitors of the essential cell division protein FtsA
    • 1:CAS:528:DC%2BD2MXjtlentLo%3D 15790573
    • Paradis-Bleau C, Sanschagrin F, Levesque RC. Peptide inhibitors of the essential cell division protein FtsA. Protein Eng Des Sel. 2005;18:85-91.
    • (2005) Protein Eng des Sel , vol.18 , pp. 85-91
    • Paradis-Bleau, C.1    Sanschagrin, F.2    Levesque, R.C.3
  • 54
    • 84887413806 scopus 로고    scopus 로고
    • Identification of novel genes responsible for overexpression of ampC in Pseudomonas aeruginosa PAO1
    • 24041903 3837884
    • Tsutsumi Y, Tomita H, Tanimoto K. Identification of novel genes responsible for overexpression of ampC in Pseudomonas aeruginosa PAO1. Antimicrob Agents Chemother. 2013;57:5987-93.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 5987-5993
    • Tsutsumi, Y.1    Tomita, H.2    Tanimoto, K.3
  • 55
    • 84859032202 scopus 로고    scopus 로고
    • The regulatory repertoire of Pseudomonas aeruginosa AmpC ss-lactamase regulator AmpR includes virulence genes
    • 1:CAS:528:DC%2BC38XlsFamsbc%3D 22479525 3315558
    • Balasubramanian D, Schneper L, Merighi M, Smith R, Narasimhan G, Lory S, et al. The regulatory repertoire of Pseudomonas aeruginosa AmpC ss-lactamase regulator AmpR includes virulence genes. PLoS One. 2012;7:e34067.
    • (2012) PLoS One , vol.7 , pp. e34067
    • Balasubramanian, D.1    Schneper, L.2    Merighi, M.3    Smith, R.4    Narasimhan, G.5    Lory, S.6
  • 56
    • 84884507153 scopus 로고    scopus 로고
    • Transcriptome profiling reveals links between ParS/ParR, MexEF-OprN, and quorum sensing in the regulation of adaptation and virulence in Pseudomonas aeruginosa
    • 1:CAS:528:DC%2BC3sXhvVKnurfK 24034668 3848899
    • Wang D, Seeve C, Pierson LS, Pierson EA. Transcriptome profiling reveals links between ParS/ParR, MexEF-OprN, and quorum sensing in the regulation of adaptation and virulence in Pseudomonas aeruginosa. BMC Genomics. 2013;14:618.
    • (2013) BMC Genomics , vol.14 , pp. 618
    • Wang, D.1    Seeve, C.2    Pierson, L.S.3    Pierson, E.A.4


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