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Volumn 8, Issue 6, 2012, Pages

The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYCLIC GMP; GUANYLATE CYCLASE; MEMBRANE ENZYME; PROTEIN YFIBNR; UNCLASSIFIED DRUG; MEMBRANE PROTEIN;

EID: 84864052471     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002760     Document Type: Article
Times cited : (97)

References (99)
  • 1
    • 34247210823 scopus 로고    scopus 로고
    • Microbial ecology of the cystic fibrosis lung
    • Harrison F, (2007) Microbial ecology of the cystic fibrosis lung. Microbiology 153: 917-923.
    • (2007) Microbiology , vol.153 , pp. 917-923
    • Harrison, F.1
  • 2
  • 3
    • 78751522378 scopus 로고    scopus 로고
    • Parallel Evolution in Pseudomonas aeruginosa over 39,000 Generations In Vivo
    • Huse HK, Kwon T, Zlosnik JE, Speert DP, Marcotte EM, et al. (2010) Parallel Evolution in Pseudomonas aeruginosa over 39,000 Generations In Vivo. MBio 1: e00199-10.
    • (2010) MBio , vol.1
    • Huse, H.K.1    Kwon, T.2    Zlosnik, J.E.3    Speert, D.P.4    Marcotte, E.M.5
  • 4
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan JRDV, (1996) Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiol Rev 60: 539-574.
    • (1996) Microbiol Rev , vol.60 , pp. 539-574
    • Govan, J.R.D.V.1
  • 5
    • 23744479941 scopus 로고    scopus 로고
    • Characterization of colony morphology variants isolated from Pseudomonas aeruginosa biofilms
    • Kirisits MJ, Prost L, Starkey M, Parsek MR, (2005) Characterization of colony morphology variants isolated from Pseudomonas aeruginosa biofilms. Appl Environ Microbiol 71: 4809-4821.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4809-4821
    • Kirisits, M.J.1    Prost, L.2    Starkey, M.3    Parsek, M.R.4
  • 6
    • 0242417146 scopus 로고    scopus 로고
    • Highly adherent small-colony variants of Pseudomonas aeruginosa in cystic fibrosis lung infection
    • Haussler S, Ziegler I, Lottel A, von Gotz F, Rohde M, et al. (2003) Highly adherent small-colony variants of Pseudomonas aeruginosa in cystic fibrosis lung infection. J Med Microbiol 52: 295-301.
    • (2003) J Med Microbiol , vol.52 , pp. 295-301
    • Haussler, S.1    Ziegler, I.2    Lottel, A.3    von Gotz, F.4    Rohde, M.5
  • 8
    • 34247092332 scopus 로고    scopus 로고
    • Development and persistence of antimicrobial resistance in Pseudomonas aeruginosa: a longitudinal observation in mechanically ventilated patients
    • Reinhardt A, Kohler T, Wood P, Rohner P, Dumas JL, et al. (2007) Development and persistence of antimicrobial resistance in Pseudomonas aeruginosa: a longitudinal observation in mechanically ventilated patients. Antimicrob Agents Chemother 51: 1341-1350.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 1341-1350
    • Reinhardt, A.1    Kohler, T.2    Wood, P.3    Rohner, P.4    Dumas, J.L.5
  • 9
    • 18844476270 scopus 로고    scopus 로고
    • Fatal outcome of lung transplantation in cystic fibrosis patients due to small-colony variants of the Burkholderia cepacia complex
    • Haussler S, Lehmann C, Breselge C, Rohde M, Classen M, et al. (2003) Fatal outcome of lung transplantation in cystic fibrosis patients due to small-colony variants of the Burkholderia cepacia complex. Eur J Clin Microbiol Infect Dis 22: 249-253.
    • (2003) Eur J Clin Microbiol Infect Dis , vol.22 , pp. 249-253
    • Haussler, S.1    Lehmann, C.2    Breselge, C.3    Rohde, M.4    Classen, M.5
  • 10
    • 33845629463 scopus 로고    scopus 로고
    • Haemophilus haemolyticus: a human respiratory tract commensal to be distinguished from Haemophilus influenzae
    • Murphy TF, Brauer AL, Sethi S, Kilian M, Cai X, et al. (2007) Haemophilus haemolyticus: a human respiratory tract commensal to be distinguished from Haemophilus influenzae. J Infect Dis 195: 81-89.
    • (2007) J Infect Dis , vol.195 , pp. 81-89
    • Murphy, T.F.1    Brauer, A.L.2    Sethi, S.3    Kilian, M.4    Cai, X.5
  • 11
    • 77950405367 scopus 로고    scopus 로고
    • YfiBNR mediates cyclic di-GMP dependent small colony variant formation and persistence in Pseudomonas aeruginosa
    • Malone JG, Jaeger T, Spangler C, Ritz D, Spang A, et al. (2010) YfiBNR mediates cyclic di-GMP dependent small colony variant formation and persistence in Pseudomonas aeruginosa. PLoS Pathog 6: e1000804.
    • (2010) PLoS Pathog , vol.6
    • Malone, J.G.1    Jaeger, T.2    Spangler, C.3    Ritz, D.4    Spang, A.5
  • 12
    • 0035173818 scopus 로고    scopus 로고
    • Biofilms and planktonic cells of Pseudomonas aeruginosa have similar resistance to killing by antimicrobials
    • Spoering AL, Lewis K, (2001) Biofilms and planktonic cells of Pseudomonas aeruginosa have similar resistance to killing by antimicrobials. J Bacteriol 183: 6746-6751.
    • (2001) J Bacteriol , vol.183 , pp. 6746-6751
    • Spoering, A.L.1    Lewis, K.2
  • 13
    • 0026135443 scopus 로고
    • Longitudinal studies of virulence factors of Pseudomonas aeruginosa in cystic fibrosis
    • Burke V, Robinson JO, Richardson CJ, Bundell CS, (1991) Longitudinal studies of virulence factors of Pseudomonas aeruginosa in cystic fibrosis. Pathology 23: 145-148.
    • (1991) Pathology , vol.23 , pp. 145-148
    • Burke, V.1    Robinson, J.O.2    Richardson, C.J.3    Bundell, C.S.4
  • 14
    • 34548428704 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa cupA-encoded fimbriae expression is regulated by a GGDEF and EAL domain-dependent modulation of the intracellular level of cyclic diguanylate
    • Meissner A, Wild V, Simm R, Rohde M, Erck C, et al. (2007) Pseudomonas aeruginosa cupA-encoded fimbriae expression is regulated by a GGDEF and EAL domain-dependent modulation of the intracellular level of cyclic diguanylate. Environ Microbiol 9: 2475-2485.
    • (2007) Environ Microbiol , vol.9 , pp. 2475-2485
    • Meissner, A.1    Wild, V.2    Simm, R.3    Rohde, M.4    Erck, C.5
  • 15
    • 26444582915 scopus 로고    scopus 로고
    • A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels
    • Hickman JW, Tifrea DF, Harwood CS, (2005) A chemosensory system that regulates biofilm formation through modulation of cyclic diguanylate levels. Proc Natl Acad Sci U S A 102: 14422-14427.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14422-14427
    • Hickman, J.W.1    Tifrea, D.F.2    Harwood, C.S.3
  • 16
    • 66149084428 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa rugose small-colony variants have adaptations that likely promote persistence in the cystic fibrosis lung
    • Starkey M, Hickman JH, Ma L, Zhang N, De Long S, et al. (2009) Pseudomonas aeruginosa rugose small-colony variants have adaptations that likely promote persistence in the cystic fibrosis lung. J Bacteriol 191: 3492-3503.
    • (2009) J Bacteriol , vol.191 , pp. 3492-3503
    • Starkey, M.1    Hickman, J.H.2    Ma, L.3    Zhang, N.4    de Long, S.5
  • 17
    • 2642572004 scopus 로고    scopus 로고
    • Biofilm formation by the small colony variant phenotype of Pseudomonas aeruginosa
    • Haussler S, (2004) Biofilm formation by the small colony variant phenotype of Pseudomonas aeruginosa. Environ Microbiol 6: 546-551.
    • (2004) Environ Microbiol , vol.6 , pp. 546-551
    • Haussler, S.1
  • 18
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • Hengge R, (2009) Principles of c-di-GMP signalling in bacteria. Nat Rev Microbiol 7: 263-273.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 263-273
    • Hengge, R.1
  • 19
    • 33845403359 scopus 로고    scopus 로고
    • Mechanisms of cyclic-di-GMP signaling in bacteria
    • Jenal U, Malone J, (2006) Mechanisms of cyclic-di-GMP signaling in bacteria. Annu Rev Genet 40: 385-407.
    • (2006) Annu Rev Genet , vol.40 , pp. 385-407
    • Jenal, U.1    Malone, J.2
  • 20
    • 34547682212 scopus 로고    scopus 로고
    • The second messenger bis-(3′-5′)-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa
    • Merighi M, Lee VT, Hyodo M, Hayakawa Y, Lory S, (2007) The second messenger bis-(3′-5′)-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa. Mol Microbiol 65: 876-895.
    • (2007) Mol Microbiol , vol.65 , pp. 876-895
    • Merighi, M.1    Lee, V.T.2    Hyodo, M.3    Hayakawa, Y.4    Lory, S.5
  • 21
    • 34548303826 scopus 로고    scopus 로고
    • A cyclic-di-GMP receptor required for bacterial exopolysaccharide production
    • Lee VT, Matewish JM, Kessler JL, Hyodo M, Kayakawa Y, et al. (2007) A cyclic-di-GMP receptor required for bacterial exopolysaccharide production. Mol Microbiol 65: 1474-1484.
    • (2007) Mol Microbiol , vol.65 , pp. 1474-1484
    • Lee, V.T.1    Matewish, J.M.2    Kessler, J.L.3    Hyodo, M.4    Kayakawa, Y.5
  • 22
    • 47249089614 scopus 로고    scopus 로고
    • Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
    • Hickman JW, Harwood CS, (2008) Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor. Mol Microbiol 69: 376-389.
    • (2008) Mol Microbiol , vol.69 , pp. 376-389
    • Hickman, J.W.1    Harwood, C.S.2
  • 23
    • 13144257722 scopus 로고    scopus 로고
    • A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes
    • Kulasekara HD, Ventre I, Kulasekara BR, Lazdunski A, Filloux A, et al. (2005) A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes. Mol Microbiol 55: 368-380.
    • (2005) Mol Microbiol , vol.55 , pp. 368-380
    • Kulasekara, H.D.1    Ventre, I.2    Kulasekara, B.R.3    Lazdunski, A.4    Filloux, A.5
  • 24
    • 76449122382 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa uses a cyclic-di-GMP-regulated adhesin to reinforce the biofilm extracellular matrix
    • Borlee BR, Goldman AD, Murakami K, Samudrala R, Wozniak DJ, et al. (2010) Pseudomonas aeruginosa uses a cyclic-di-GMP-regulated adhesin to reinforce the biofilm extracellular matrix. Mol Microbiol 75: 827-842.
    • (2010) Mol Microbiol , vol.75 , pp. 827-842
    • Borlee, B.R.1    Goldman, A.D.2    Murakami, K.3    Samudrala, R.4    Wozniak, D.J.5
  • 25
    • 78650396058 scopus 로고    scopus 로고
    • Modulation of Pseudomonas aeruginosa biofilm dispersal by a cyclic-Di-GMP phosphodiesterase with a putative hypoxia-sensing domain
    • An S, Wu J, Zhang LH, (2010) Modulation of Pseudomonas aeruginosa biofilm dispersal by a cyclic-Di-GMP phosphodiesterase with a putative hypoxia-sensing domain. Appl Environ Microbiol 76: 8160-8173.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 8160-8173
    • An, S.1    Wu, J.2    Zhang, L.H.3
  • 26
    • 33644516891 scopus 로고    scopus 로고
    • Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3′-5′)-cyclic-GMP in virulence
    • Kulasakara H, Lee V, Brencic A, Liberati N, Urbach J, et al. (2006) Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3′-5′)-cyclic-GMP in virulence. Proc Natl Acad Sci U S A 103: 2839-2844.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2839-2844
    • Kulasakara, H.1    Lee, V.2    Brencic, A.3    Liberati, N.4    Urbach, J.5
  • 27
    • 14544291492 scopus 로고    scopus 로고
    • A three-component regulatory system regulates biofilm maturation and type III secretion in Pseudomonas aeruginosa
    • Kuchma SL, Connolly JP, O'Toole GA, (2005) A three-component regulatory system regulates biofilm maturation and type III secretion in Pseudomonas aeruginosa. J Bacteriol 187: 1441-1454.
    • (2005) J Bacteriol , vol.187 , pp. 1441-1454
    • Kuchma, S.L.1    Connolly, J.P.2    O'Toole, G.A.3
  • 28
    • 82155202495 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa sensor RetS switches Type III and Type VI secretion via c-di-GMP signalling
    • Moscoso JA, Mikkelsen H, Heeb S, Williams P, Filloux A, (2011) The Pseudomonas aeruginosa sensor RetS switches Type III and Type VI secretion via c-di-GMP signalling. Environ Microbiol 13: 3128-38.
    • (2011) Environ Microbiol , vol.13 , pp. 3128-3138
    • Moscoso, J.A.1    Mikkelsen, H.2    Heeb, S.3    Williams, P.4    Filloux, A.5
  • 29
    • 0345097587 scopus 로고    scopus 로고
    • FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa
    • Huang B, Whitchurch CB, Mattick JS, (2003) FimX, a multidomain protein connecting environmental signals to twitching motility in Pseudomonas aeruginosa. J Bacteriol 185: 7068-7076.
    • (2003) J Bacteriol , vol.185 , pp. 7068-7076
    • Huang, B.1    Whitchurch, C.B.2    Mattick, J.S.3
  • 30
    • 33646397872 scopus 로고    scopus 로고
    • Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa
    • Kazmierczak BI, Lebron MB, Murray TS, (2006) Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa. Mol Microbiol 60: 1026-1043.
    • (2006) Mol Microbiol , vol.60 , pp. 1026-1043
    • Kazmierczak, B.I.1    Lebron, M.B.2    Murray, T.S.3
  • 31
    • 0030042096 scopus 로고    scopus 로고
    • Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa
    • Alm RA, Bodero AJ, Free PD, Mattick JS, (1996) Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa. J Bacteriol 178: 46-53.
    • (1996) J Bacteriol , vol.178 , pp. 46-53
    • Alm, R.A.1    Bodero, A.J.2    Free, P.D.3    Mattick, J.S.4
  • 32
    • 79952168685 scopus 로고    scopus 로고
    • Specific Control of Pseudomonas aeruginosa Surface-Associated Behaviors by Two c-di-GMP Diguanylate Cyclases
    • Merritt JH, Ha DG, Cowles KN, Lu W, Morales DK, et al. (2010) Specific Control of Pseudomonas aeruginosa Surface-Associated Behaviors by Two c-di-GMP Diguanylate Cyclases. MBio 1: e00183-10.
    • (2010) MBio , vol.1
    • Merritt, J.H.1    Ha, D.G.2    Cowles, K.N.3    Lu, W.4    Morales, D.K.5
  • 33
    • 34848889244 scopus 로고    scopus 로고
    • A comprehensive genetic characterization of bacterial motility
    • Girgis HS, Liu Y, Ryu WS, Tavazoie S, (2007) A comprehensive genetic characterization of bacterial motility. PLoS Genet 3: 1644-1660.
    • (2007) PLoS Genet , vol.3 , pp. 1644-1660
    • Girgis, H.S.1    Liu, Y.2    Ryu, W.S.3    Tavazoie, S.4
  • 34
    • 36749091176 scopus 로고    scopus 로고
    • Mutational activation of niche-specific genes provides insight into regulatory networks and bacterial function in a complex environment
    • Giddens SR, Jackson RW, Moon CD, Jacobs MA, Zhang XX, et al. (2007) Mutational activation of niche-specific genes provides insight into regulatory networks and bacterial function in a complex environment. Proc Natl Acad Sci U S A 104: 18247-18252.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 18247-18252
    • Giddens, S.R.1    Jackson, R.W.2    Moon, C.D.3    Jacobs, M.A.4    Zhang, X.X.5
  • 35
    • 72449190549 scopus 로고    scopus 로고
    • Adaptive divergence in experimental populations of Pseudomonas fluorescens. IV. Genetic constraints guide evolutionary trajectories in a parallel adaptive radiation
    • McDonald MJ, Gehrig SM, Meintjes PL, Zhang XX, Rainey PB, (2009) Adaptive divergence in experimental populations of Pseudomonas fluorescens. IV. Genetic constraints guide evolutionary trajectories in a parallel adaptive radiation. Genetics 183: 1041-1053.
    • (2009) Genetics , vol.183 , pp. 1041-1053
    • McDonald, M.J.1    Gehrig, S.M.2    Meintjes, P.L.3    Zhang, X.X.4    Rainey, P.B.5
  • 37
    • 67650863623 scopus 로고    scopus 로고
    • Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885)
    • Ueda A, Wood TK, (2009) Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885). PLoS Pathog 5: e1000483.
    • (2009) PLoS Pathog , vol.5
    • Ueda, A.1    Wood, T.K.2
  • 38
    • 80052315142 scopus 로고    scopus 로고
    • MrkH, a novel c-di-GMP-dependent transcriptional activator, controls klebsiella pneumoniae biofilm formation by regulating type 3 fimbriae expression
    • Wilksch JJ, Yang J, Clements A, Gabbe JL, Short KR, et al. (2011) MrkH, a novel c-di-GMP-dependent transcriptional activator, controls klebsiella pneumoniae biofilm formation by regulating type 3 fimbriae expression. PLoS Pathog 7: e1002204.
    • (2011) PLoS Pathog , vol.7
    • Wilksch, J.J.1    Yang, J.2    Clements, A.3    Gabbe, J.L.4    Short, K.R.5
  • 39
    • 0141531993 scopus 로고    scopus 로고
    • The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli
    • Pappalardo L, Janausch IG, Vijayan V, Zientz E, Junker J, et al. (2003) The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli. J Biol Chem 278: 39185-39188.
    • (2003) J Biol Chem , vol.278 , pp. 39185-39188
    • Pappalardo, L.1    Janausch, I.G.2    Vijayan, V.3    Zientz, E.4    Junker, J.5
  • 40
    • 0141643091 scopus 로고    scopus 로고
    • The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain
    • Reinelt S, Hofmann E, Gerharz T, Bott M, Madden DR, (2003) The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain. J Biol Chem 278: 39189-39196.
    • (2003) J Biol Chem , vol.278 , pp. 39189-39196
    • Reinelt, S.1    Hofmann, E.2    Gerharz, T.3    Bott, M.4    Madden, D.R.5
  • 41
    • 40049093270 scopus 로고    scopus 로고
    • A ligand-induced switch in the periplasmic domain of sensor histidine kinase CitA
    • Sevvana M, Vijayan V, Zweckstetter M, Reinelt S, Madden DR, et al. (2008) A ligand-induced switch in the periplasmic domain of sensor histidine kinase CitA. J Mol Biol 377: 512-523.
    • (2008) J Mol Biol , vol.377 , pp. 512-523
    • Sevvana, M.1    Vijayan, V.2    Zweckstetter, M.3    Reinelt, S.4    Madden, D.R.5
  • 42
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • Moglich A, Ayers RA, Moffat K, (2009) Structure and signaling mechanism of Per-ARNT-Sim domains. Structure 17: 1282-1294.
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Moglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 43
    • 15444362702 scopus 로고    scopus 로고
    • Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling
    • Key J, Moffat K, (2005) Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling. Biochemistry 44: 4627-4635.
    • (2005) Biochemistry , vol.44 , pp. 4627-4635
    • Key, J.1    Moffat, K.2
  • 44
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: photoresponsive signaling modules coupled to diverse output domains
    • Crosson S, Rajagopal S, Moffat K, (2003) The LOV domain family: photoresponsive signaling modules coupled to diverse output domains. Biochemistry 42: 2-10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 45
    • 41449111029 scopus 로고    scopus 로고
    • Changes at the KinA PAS-A dimerization interface influence histidine kinase function
    • Lee J, Tomchick DR, Brautigam CA, Machius M, Kort R, et al. (2008) Changes at the KinA PAS-A dimerization interface influence histidine kinase function. Biochemistry 47: 4051-4064.
    • (2008) Biochemistry , vol.47 , pp. 4051-4064
    • Lee, J.1    Tomchick, D.R.2    Brautigam, C.A.3    Machius, M.4    Kort, R.5
  • 46
    • 9144260515 scopus 로고    scopus 로고
    • Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain
    • Razeto A, Ramakrishnan V, Litterst CM, Giller K, Griesinger C, et al. (2004) Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain. J Mol Biol 336: 319-329.
    • (2004) J Mol Biol , vol.336 , pp. 319-329
    • Razeto, A.1    Ramakrishnan, V.2    Litterst, C.M.3    Giller, K.4    Griesinger, C.5
  • 47
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB, (1999) PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol Mol Biol Rev 63: 479-506.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 48
    • 75749103345 scopus 로고    scopus 로고
    • Extracytoplasmic PAS-like domains are common in signal transduction proteins
    • Chang C, Tesar C, Gu M, Babnigg G, Joachimiak A, et al. (2009) Extracytoplasmic PAS-like domains are common in signal transduction proteins. J Bacteriol 192: 1156-1159.
    • (2009) J Bacteriol , vol.192 , pp. 1156-1159
    • Chang, C.1    Tesar, C.2    Gu, M.3    Babnigg, G.4    Joachimiak, A.5
  • 49
    • 68249111866 scopus 로고    scopus 로고
    • Peptidoglycan-associated lipoprotein (Pal) of Gram-negative bacteria: function, structure, role in pathogenesis and potential application in immunoprophylaxis
    • Godlewska R, Wisniewska K, Pietras Z, Jagusztyn-Krynicka EK, (2009) Peptidoglycan-associated lipoprotein (Pal) of Gram-negative bacteria: function, structure, role in pathogenesis and potential application in immunoprophylaxis. FEMS Microbiol Lett 298: 1-11.
    • (2009) FEMS Microbiol Lett , vol.298 , pp. 1-11
    • Godlewska, R.1    Wisniewska, K.2    Pietras, Z.3    Jagusztyn-Krynicka, E.K.4
  • 50
    • 77956850709 scopus 로고    scopus 로고
    • The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor
    • Yeh YC, Comolli LR, Downing KH, Shapiro L, McAdams HH, (2010) The caulobacter Tol-Pal complex is essential for outer membrane integrity and the positioning of a polar localization factor. J Bacteriol 192: 4847-4858.
    • (2010) J Bacteriol , vol.192 , pp. 4847-4858
    • Yeh, Y.C.1    Comolli, L.R.2    Downing, K.H.3    Shapiro, L.4    McAdams, H.H.5
  • 51
    • 70349205369 scopus 로고    scopus 로고
    • Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins
    • Bonsor DA, Hecht O, Vankemmelbeke M, Sharma A, Krachler AM, et al. (2009) Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins. EMBO J 28: 2846-2857.
    • (2009) EMBO J , vol.28 , pp. 2846-2857
    • Bonsor, D.A.1    Hecht, O.2    Vankemmelbeke, M.3    Sharma, A.4    Krachler, A.M.5
  • 52
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • Gerding MA, Ogata Y, Pecora ND, Niki H, de Boer PA, (2007) The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol Microbiol 63: 1008-1025.
    • (2007) Mol Microbiol , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    de Boer, P.A.5
  • 53
    • 34547659282 scopus 로고    scopus 로고
    • Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
    • Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, et al. (2007) Structure of BeF3--modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 15: 915-927.
    • (2007) Structure , vol.15 , pp. 915-927
    • Wassmann, P.1    Chan, C.2    Paul, R.3    Beck, A.4    Heerklotz, H.5
  • 54
    • 34247202706 scopus 로고    scopus 로고
    • The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain
    • Malone JG, Williams R, Christen M, Jenal U, Spiers AJ, et al. (2007) The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain. Microbiology 153: 980-994.
    • (2007) Microbiology , vol.153 , pp. 980-994
    • Malone, J.G.1    Williams, R.2    Christen, M.3    Jenal, U.4    Spiers, A.J.5
  • 55
    • 33745402876 scopus 로고    scopus 로고
    • Adaptive divergence in experimental populations of Pseudomonas fluorescens. II. Role of the GGDEF regulator WspR in evolution and development of the wrinkly spreader phenotype
    • Goymer P, Kahn SG, Malone JG, Gehrig SM, Spiers AJ, et al. (2006) Adaptive divergence in experimental populations of Pseudomonas fluorescens. II. Role of the GGDEF regulator WspR in evolution and development of the wrinkly spreader phenotype. Genetics 173: 515-526.
    • (2006) Genetics , vol.173 , pp. 515-526
    • Goymer, P.1    Kahn, S.G.2    Malone, J.G.3    Gehrig, S.M.4    Spiers, A.J.5
  • 56
    • 77957949467 scopus 로고    scopus 로고
    • Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases
    • Parkinson JS, (2010) Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases. Annu Rev Microbiol 64: 101-122.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 101-122
    • Parkinson, J.S.1
  • 57
    • 70350163201 scopus 로고    scopus 로고
    • Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors
    • Zhou Q, Ames P, Parkinson JS, (2009) Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors. Mol Microbiol 73: 801-814.
    • (2009) Mol Microbiol , vol.73 , pp. 801-814
    • Zhou, Q.1    Ames, P.2    Parkinson, J.S.3
  • 58
    • 0026747875 scopus 로고
    • Mutational analysis reveals functional similarity between NARX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins
    • Collins LA, Egan SM, Stewart V, (1992) Mutational analysis reveals functional similarity between NARX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins. J Bacteriol 174: 3667-3675.
    • (1992) J Bacteriol , vol.174 , pp. 3667-3675
    • Collins, L.A.1    Egan, S.M.2    Stewart, V.3
  • 59
    • 53849112614 scopus 로고    scopus 로고
    • Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor
    • Ames P, Zhou Q, Parkinson JS, (2008) Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor. J Bacteriol 190: 6676-6685.
    • (2008) J Bacteriol , vol.190 , pp. 6676-6685
    • Ames, P.1    Zhou, Q.2    Parkinson, J.S.3
  • 60
    • 53849132692 scopus 로고    scopus 로고
    • The tie that binds the dynamic duo: the connector between AS1 and AS2 in the HAMP domain of the Escherichia coli Tsr chemoreceptor
    • Manson MD, (2008) The tie that binds the dynamic duo: the connector between AS1 and AS2 in the HAMP domain of the Escherichia coli Tsr chemoreceptor. J Bacteriol 190: 6544-6547.
    • (2008) J Bacteriol , vol.190 , pp. 6544-6547
    • Manson, M.D.1
  • 61
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen
    • Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, et al. (2000) Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406: 959-964.
    • (2000) Nature , vol.406 , pp. 959-964
    • Stover, C.K.1    Pham, X.Q.2    Erwin, A.L.3    Mizoguchi, S.D.4    Warrener, P.5
  • 62
    • 1842335745 scopus 로고    scopus 로고
    • Molecular and immunological characterization of OprL, the 18 kDa outer-membrane peptidoglycan-associated lipoprotein (PAL) of Pseudomonas aeruginosa
    • Lim A Jr, De Vos D, Brauns M, Mossialos D, Gaballa A, et al. (1997) Molecular and immunological characterization of OprL, the 18 kDa outer-membrane peptidoglycan-associated lipoprotein (PAL) of Pseudomonas aeruginosa. Microbiology 143 (Pt 5): 1709-1716.
    • (1997) Microbiology , vol.143 , Issue.Pt 5 , pp. 1709-1716
    • Lim Jr., A.1    de Vos, D.2    Brauns, M.3    Mossialos, D.4    Gaballa, A.5
  • 63
    • 33144490288 scopus 로고    scopus 로고
    • Peptidoglycan recognition by Pal, an outer membrane lipoprotein
    • Parsons LM, Lin F, Orban J, (2006) Peptidoglycan recognition by Pal, an outer membrane lipoprotein. Biochemistry 45: 2122-2128.
    • (2006) Biochemistry , vol.45 , pp. 2122-2128
    • Parsons, L.M.1    Lin, F.2    Orban, J.3
  • 64
    • 68249111866 scopus 로고    scopus 로고
    • Peptidoglycan-associated lipoprotein (Pal) of Gram-negative bacteria: function, structure, role in pathogenesis and potential application in immunoprophylaxis
    • Godlewska R, Wisniewska K, Pietras Z, Jagusztyn-Krynicka EK, (2009) Peptidoglycan-associated lipoprotein (Pal) of Gram-negative bacteria: function, structure, role in pathogenesis and potential application in immunoprophylaxis. FEMS Microbiol Lett 298: 1-11.
    • (2009) FEMS Microbiol Lett , vol.298 , pp. 1-11
    • Godlewska, R.1    Wisniewska, K.2    Pietras, Z.3    Jagusztyn-Krynicka, E.K.4
  • 65
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell JC, McGovern K, Beckwith J, (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67: 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 66
    • 10344238965 scopus 로고    scopus 로고
    • Structural basis of activity and allosteric control of diguanylate cyclase
    • Chan C, Paul R, Samoray D, Amiot NC, Giese B, et al. (2004) Structural basis of activity and allosteric control of diguanylate cyclase. Proc Natl Acad Sci U S A 101: 17084-17089.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17084-17089
    • Chan, C.1    Paul, R.2    Samoray, D.3    Amiot, N.C.4    Giese, B.5
  • 67
  • 68
    • 62549150834 scopus 로고    scopus 로고
    • LapD is a bis-(3′,5′)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1
    • Newell PD, Monds RD, O'Toole GA, (2009) LapD is a bis-(3′,5′)-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1. Proc Natl Acad Sci U S A 106: 3461-3466.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3461-3466
    • Newell, P.D.1    Monds, R.D.2    O'Toole, G.A.3
  • 69
    • 79952266181 scopus 로고    scopus 로고
    • A c-di-GMP effector system controls cell adhesion by inside-out signaling and surface protein cleavage
    • Newell PD, Boyd CD, Sondermann H, O'Toole GA, (2011) A c-di-GMP effector system controls cell adhesion by inside-out signaling and surface protein cleavage. PLoS Biol 9: e1000587.
    • (2011) PLoS Biol , vol.9
    • Newell, P.D.1    Boyd, C.D.2    Sondermann, H.3    O'Toole, G.A.4
  • 70
    • 79952260048 scopus 로고    scopus 로고
    • Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis
    • Navarro MV, Newell PD, Krasteva PV, Chatterjee D, Madden DR, et al. (2011) Structural basis for c-di-GMP-mediated inside-out signaling controlling periplasmic proteolysis. PLoS Biol 9: e1000588.
    • (2011) PLoS Biol , vol.9
    • Navarro, M.V.1    Newell, P.D.2    Krasteva, P.V.3    Chatterjee, D.4    Madden, D.R.5
  • 71
    • 76449086560 scopus 로고    scopus 로고
    • Characterization of starvation-induced dispersion in Pseudomonas putida biofilms: genetic elements and molecular mechanisms
    • Gjermansen M, Nilsson M, Yang L, Tolker-Nielsen T, (2010) Characterization of starvation-induced dispersion in Pseudomonas putida biofilms: genetic elements and molecular mechanisms. Mol Microbiol 75: 815-826.
    • (2010) Mol Microbiol , vol.75 , pp. 815-826
    • Gjermansen, M.1    Nilsson, M.2    Yang, L.3    Tolker-Nielsen, T.4
  • 72
    • 0036889484 scopus 로고    scopus 로고
    • Autolysis and autoaggregation in Pseudomonas aeruginosa colony morphology mutants
    • D'Argenio DA, Calfee MW, Rainey PB, Pesci EC, (2002) Autolysis and autoaggregation in Pseudomonas aeruginosa colony morphology mutants. J Bacteriol 184: 6481-6489.
    • (2002) J Bacteriol , vol.184 , pp. 6481-6489
    • D'Argenio, D.A.1    Calfee, M.W.2    Rainey, P.B.3    Pesci, E.C.4
  • 73
    • 77954645140 scopus 로고    scopus 로고
    • Early adaptive developments of Pseudomonas aeruginosa after the transition from life in the environment to persistent colonization in the airways of human cystic fibrosis hosts
    • Rau MH, Hansen SK, Johansen HK, Thomsen LE, Workman CT, et al. (2010) Early adaptive developments of Pseudomonas aeruginosa after the transition from life in the environment to persistent colonization in the airways of human cystic fibrosis hosts. Environ Microbiol 12: 1643-1658.
    • (2010) Environ Microbiol , vol.12 , pp. 1643-1658
    • Rau, M.H.1    Hansen, S.K.2    Johansen, H.K.3    Thomsen, L.E.4    Workman, C.T.5
  • 75
    • 0034685940 scopus 로고    scopus 로고
    • High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection
    • Oliver A, Canton R, Campo P, Baquero F, Blazquez J, (2000) High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection. Science 288: 1251-1254.
    • (2000) Science , vol.288 , pp. 1251-1254
    • Oliver, A.1    Canton, R.2    Campo, P.3    Baquero, F.4    Blazquez, J.5
  • 76
    • 0037219570 scopus 로고    scopus 로고
    • Impact of large chromosomal inversions on the adaptation and evolution of Pseudomonas aeruginosa chronically colonizing cystic fibrosis lungs
    • Kresse AU, Dinesh SD, Larbig K, Romling U, (2003) Impact of large chromosomal inversions on the adaptation and evolution of Pseudomonas aeruginosa chronically colonizing cystic fibrosis lungs. Mol Microbiol 47: 145-158.
    • (2003) Mol Microbiol , vol.47 , pp. 145-158
    • Kresse, A.U.1    Dinesh, S.D.2    Larbig, K.3    Romling, U.4
  • 77
    • 79952222757 scopus 로고    scopus 로고
    • Positive signature-tagged mutagenesis in Pseudomonas aeruginosa: tracking patho-adaptive mutations promoting airways chronic infection
    • Bianconi I, Milani A, Cigana C, Paroni M, Levesque RC, et al. (2011) Positive signature-tagged mutagenesis in Pseudomonas aeruginosa: tracking patho-adaptive mutations promoting airways chronic infection. PLoS Pathog 7: e1001270.
    • (2011) PLoS Pathog , vol.7
    • Bianconi, I.1    Milani, A.2    Cigana, C.3    Paroni, M.4    Levesque, R.C.5
  • 78
    • 0003785155 scopus 로고
    • Cold Spring Harbor, New York, Cold Spring Harbor Laboratory Press
    • Miller JH, (1972) Experiments in molecular genetics Cold Spring Harbor, New York Cold Spring Harbor Laboratory Press pp. 352-355.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 79
    • 0034705144 scopus 로고    scopus 로고
    • An efficient recombination system for chromosome engineering in Escherichia coli
    • Yu D, Ellis HM, Lee EC, Jenkins NA, Copeland NG, et al. (2000) An efficient recombination system for chromosome engineering in Escherichia coli. Proc Natl Acad Sci U S A 97: 5978-5983.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5978-5983
    • Yu, D.1    Ellis, H.M.2    Lee, E.C.3    Jenkins, N.A.4    Copeland, N.G.5
  • 81
    • 21444457864 scopus 로고    scopus 로고
    • A Tn7-based broad-range bacterial cloning and expression system
    • Choi KH, Gaynor JB, White KG, Lopez C, Bosio CM, et al. (2005) A Tn7-based broad-range bacterial cloning and expression system. Nat Methods 2: 443-448.
    • (2005) Nat Methods , vol.2 , pp. 443-448
    • Choi, K.H.1    Gaynor, J.B.2    White, K.G.3    Lopez, C.4    Bosio, C.M.5
  • 82
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang TT, Karkhoff-Schweizer RR, Kutchma AJ, Schweizer HP, (1998) A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212: 77-86.
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 83
    • 0033621572 scopus 로고    scopus 로고
    • Small, stable shuttle vectors based on the minimal pVS1 replicon for use in gram-negative, plant-associated bacteria
    • Heeb S, Itoh Y, Nishijyo T, Schnider U, Keel C, et al. (2000) Small, stable shuttle vectors based on the minimal pVS1 replicon for use in gram-negative, plant-associated bacteria. Mol Plant Microbe Interact 13: 232-237.
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 232-237
    • Heeb, S.1    Itoh, Y.2    Nishijyo, T.3    Schnider, U.4    Keel, C.5
  • 84
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach ME, Elzer PH, Hill DS, Robertson GT, Farris MA, et al. (1995) Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166: 175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5
  • 85
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution
    • Chung CT, Niemela SL, Miller RH, (1989) One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci U S A 86: 2172-2175.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 86
    • 63149152073 scopus 로고    scopus 로고
    • Critical evaluation of random mutagenesis by error-prone polymerase chain reaction protocols, Escherichia coli mutator strain, and hydroxylamine treatment
    • Rasila TS, Pajunen MI, Savilahti H, (2009) Critical evaluation of random mutagenesis by error-prone polymerase chain reaction protocols, Escherichia coli mutator strain, and hydroxylamine treatment. Anal Biochem 388: 71-80.
    • (2009) Anal Biochem , vol.388 , pp. 71-80
    • Rasila, T.S.1    Pajunen, M.I.2    Savilahti, H.3
  • 87
    • 0018421922 scopus 로고
    • Transduction of Pseudomonas aeruginosa with a mutant of bacteriophage E79
    • Morgan AF, (1979) Transduction of Pseudomonas aeruginosa with a mutant of bacteriophage E79. J Bacteriol 139: 137-140.
    • (1979) J Bacteriol , vol.139 , pp. 137-140
    • Morgan, A.F.1
  • 88
    • 84950280872 scopus 로고
    • Biocontrol of root diseases by Pseudomonas fluorescens CHA0: current concepts and experimental approaches
    • In: O'Gara F, Dowling DN, Boesten B, editors, Weinheim, Germany, Wiley-VCH
    • Voisard C, Bull CT, Keel C, Laville J, Maurhofer M, et al. (1994) Biocontrol of root diseases by Pseudomonas fluorescens CHA0: current concepts and experimental approaches. In: O'Gara F, Dowling DN, Boesten B, editors. Molecular Ecology of Rhizosphere Microorganisms Weinheim, Germany Wiley-VCH pp. 67-89.
    • (1994) Molecular Ecology of Rhizosphere Microorganisms , pp. 67-89
    • Voisard, C.1    Bull, C.T.2    Keel, C.3    Laville, J.4    Maurhofer, M.5
  • 90
    • 33746038139 scopus 로고    scopus 로고
    • Cell aggregation of Pseudomonas aeruginosa strain PAO1 as an energy-dependent stress response during growth with sodium dodecyl sulfate
    • Klebensberger J, Rui O, Fritz E, Schink B, Philipp B, (2006) Cell aggregation of Pseudomonas aeruginosa strain PAO1 as an energy-dependent stress response during growth with sodium dodecyl sulfate. Arch Microbiol 185: 417-427.
    • (2006) Arch Microbiol , vol.185 , pp. 417-427
    • Klebensberger, J.1    Rui, O.2    Fritz, E.3    Schink, B.4    Philipp, B.5
  • 91
    • 33646767117 scopus 로고    scopus 로고
    • Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities
    • Diab F, Bernard T, Bazire A, Haras D, Blanco C, et al. (2006) Succinate-mediated catabolite repression control on the production of glycine betaine catabolic enzymes in Pseudomonas aeruginosa PAO1 under low and elevated salinities. Microbiology 152: 1395-1406.
    • (2006) Microbiology , vol.152 , pp. 1395-1406
    • Diab, F.1    Bernard, T.2    Bazire, A.3    Haras, D.4    Blanco, C.5
  • 92
    • 0018074492 scopus 로고
    • Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier
    • Hancock RE, Nikaido H, (1978) Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and definition of the permeability barrier. J Bacteriol 136: 381-390.
    • (1978) J Bacteriol , vol.136 , pp. 381-390
    • Hancock, R.E.1    Nikaido, H.2
  • 93
    • 77952580705 scopus 로고    scopus 로고
    • A liquid chromatography-coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate
    • Spangler C, Bohm A, Jenal U, Seifert R, Kaever V, (2010) A liquid chromatography-coupled tandem mass spectrometry method for quantitation of cyclic di-guanosine monophosphate. J Microbiol Methods 81: 226-231.
    • (2010) J Microbiol Methods , vol.81 , pp. 226-231
    • Spangler, C.1    Bohm, A.2    Jenal, U.3    Seifert, R.4    Kaever, V.5
  • 94
    • 31644444476 scopus 로고    scopus 로고
    • MaGe: a microbial genome annotation system supported by synteny results
    • Vallenet D, Labarre L, Rouy Z, Barbe V, Bocs S, et al. (2006) MaGe: a microbial genome annotation system supported by synteny results. Nucleic Acids Res 34: 53-65.
    • (2006) Nucleic Acids Res , vol.34 , pp. 53-65
    • Vallenet, D.1    Labarre, L.2    Rouy, Z.3    Barbe, V.4    Bocs, S.5
  • 95
    • 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.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 96
    • 58149200948 scopus 로고    scopus 로고
    • The Ribosomal Database Project: improved alignments and new tools for rRNA analysis
    • Cole JR, Wang Q, Cardenas E, Fish J, Chai B, et al. (2009) The Ribosomal Database Project: improved alignments and new tools for rRNA analysis. Nucleic Acids Res 37: D141-145.
    • (2009) Nucleic Acids Res , vol.37
    • Cole, J.R.1    Wang, Q.2    Cardenas, E.3    Fish, J.4    Chai, B.5
  • 97
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S, (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 24: 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 98
    • 36949076934 scopus 로고
    • Numerical taxonomy
    • Sneath PH, Sokal RR, (1962) Numerical taxonomy. Nature 193: 855-860.
    • (1962) Nature , vol.193 , pp. 855-860
    • Sneath, P.H.1    Sokal, R.R.2


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