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Volumn 86, Issue 3, 2012, Pages 580-593

Iron and pH-responsive FtrABCD ferrous iron utilization system of Bordetella species

Author keywords

[No Author keywords available]

Indexed keywords

ALCALIGIN; BACTERIAL PROTEIN; FERROUS ION; HEME; PROTEIN TONB; SIDEROPHORE;

EID: 84868112030     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12003     Document Type: Article
Times cited : (30)

References (76)
  • 1
    • 0028962035 scopus 로고
    • Ectopic expression of the flagellar regulon alters development of the Bordetella-host interaction
    • Akerley, B.J., Cotter, P.A., and Miller, J.F. (1995) Ectopic expression of the flagellar regulon alters development of the Bordetella-host interaction. Cell 80: 611-620.
    • (1995) Cell , vol.80 , pp. 611-620
    • Akerley, B.J.1    Cotter, P.A.2    Miller, J.F.3
  • 2
    • 33748675699 scopus 로고    scopus 로고
    • The Bordetella bfe system: growth and transcriptional response to siderophores, catechols, and neuroendocrine catecholamines
    • Anderson, M.T., and Armstrong, S.K. (2006) The Bordetella bfe system: growth and transcriptional response to siderophores, catechols, and neuroendocrine catecholamines. J Bacteriol 188: 5731-5740.
    • (2006) J Bacteriol , vol.188 , pp. 5731-5740
    • Anderson, M.T.1    Armstrong, S.K.2
  • 4
    • 0033818865 scopus 로고    scopus 로고
    • New virulence-activated and virulence-repressed genes identified by systematic gene inactivation and generation of transcriptional fusions in Bordetella pertussis
    • Antoine, R., Alonso, S., Raze, D., Coutte, L., Lesjean, S., Willery, E., etal. (2000) New virulence-activated and virulence-repressed genes identified by systematic gene inactivation and generation of transcriptional fusions in Bordetella pertussis. J Bacteriol 182: 5902-5905.
    • (2000) J Bacteriol , vol.182 , pp. 5902-5905
    • Antoine, R.1    Alonso, S.2    Raze, D.3    Coutte, L.4    Lesjean, S.5    Willery, E.6
  • 5
    • 0027511916 scopus 로고
    • Isolation and characterization of Bordetella bronchiseptica mutants deficient in siderophore activity
    • Armstrong, S.K., and Clements, M.O. (1993) Isolation and characterization of Bordetella bronchiseptica mutants deficient in siderophore activity. J Bacteriol 175: 1144-1152.
    • (1993) J Bacteriol , vol.175 , pp. 1144-1152
    • Armstrong, S.K.1    Clements, M.O.2
  • 6
    • 84860007213 scopus 로고    scopus 로고
    • Involvement of multiple distinct Bordetella receptor proteins in the utilization of iron liberated from transferrin by host catecholamine stress hormones
    • Armstrong, S.K., Brickman, T.J., and Suhadolc, R.J. (2012) Involvement of multiple distinct Bordetella receptor proteins in the utilization of iron liberated from transferrin by host catecholamine stress hormones. Mol Microbiol 84: 446-462.
    • (2012) Mol Microbiol , vol.84 , pp. 446-462
    • Armstrong, S.K.1    Brickman, T.J.2    Suhadolc, R.J.3
  • 7
    • 0031018138 scopus 로고    scopus 로고
    • An iron-regulated outer-membrane protein specific to Bordetella bronchiseptica and homologous to ferric siderophore receptors
    • Beall, B., and Hoenes, T. (1997) An iron-regulated outer-membrane protein specific to Bordetella bronchiseptica and homologous to ferric siderophore receptors. Microbiology 143: 135-145.
    • (1997) Microbiology , vol.143 , pp. 135-145
    • Beall, B.1    Hoenes, T.2
  • 8
    • 0029622422 scopus 로고
    • A Bordetella pertussis fepA homologue required for utilization of exogenous ferric enterobactin
    • Beall, B., and Sanden, G.N. (1995) A Bordetella pertussis fepA homologue required for utilization of exogenous ferric enterobactin. Microbiology 141: 3193-3205.
    • (1995) Microbiology , vol.141 , pp. 3193-3205
    • Beall, B.1    Sanden, G.N.2
  • 9
    • 2642697838 scopus 로고    scopus 로고
    • Identification and characterization of alcR, a gene encoding an AraC-like regulator of alcaligin siderophore biosynthesis and transport genes in Bordetella pertussis and Bordetella bronchiseptica
    • Beaumont, F.C., Kang, H.Y., Brickman, T.J., and Armstrong, S.K. (1998) Identification and characterization of alcR, a gene encoding an AraC-like regulator of alcaligin siderophore biosynthesis and transport genes in Bordetella pertussis and Bordetella bronchiseptica. J Bacteriol 180: 862-870.
    • (1998) J Bacteriol , vol.180 , pp. 862-870
    • Beaumont, F.C.1    Kang, H.Y.2    Brickman, T.J.3    Armstrong, S.K.4
  • 10
    • 0030608380 scopus 로고    scopus 로고
    • Colicins B and Ia as novel counterselective agents in interspecies conjugal DNA transfers from colicin-sensitive Escherichia coli donors to other gram-negative recipient species
    • Brickman, T.J., and Armstrong, S.K. (1996a) Colicins B and Ia as novel counterselective agents in interspecies conjugal DNA transfers from colicin-sensitive Escherichia coli donors to other gram-negative recipient species. Gene 178: 39-42.
    • (1996) Gene , vol.178 , pp. 39-42
    • Brickman, T.J.1    Armstrong, S.K.2
  • 11
    • 0030027612 scopus 로고    scopus 로고
    • The ornithine decarboxylase gene odc is required for alcaligin siderophore biosynthesis in Bordetella spp: putrescine is a precursor of alcaligin
    • Brickman, T.J., and Armstrong, S.K. (1996b) The ornithine decarboxylase gene odc is required for alcaligin siderophore biosynthesis in Bordetella spp: putrescine is a precursor of alcaligin. J Bacteriol 178: 54-60.
    • (1996) J Bacteriol , vol.178 , pp. 54-60
    • Brickman, T.J.1    Armstrong, S.K.2
  • 12
    • 0032871252 scopus 로고    scopus 로고
    • Essential role of the iron-regulated outer membrane receptor FauA in alcaligin siderophore-mediated iron uptake in Bordetella species
    • Brickman, T.J., and Armstrong, S.K. (1999) Essential role of the iron-regulated outer membrane receptor FauA in alcaligin siderophore-mediated iron uptake in Bordetella species. J Bacteriol 181: 5958-5966.
    • (1999) J Bacteriol , vol.181 , pp. 5958-5966
    • Brickman, T.J.1    Armstrong, S.K.2
  • 13
    • 18944400737 scopus 로고    scopus 로고
    • Bordetella AlcS transporter functions in alcaligin siderophore export and is central to inducer sensing in positive regulation of alcaligin system gene expression
    • Brickman, T.J., and Armstrong, S.K. (2005) Bordetella AlcS transporter functions in alcaligin siderophore export and is central to inducer sensing in positive regulation of alcaligin system gene expression. J Bacteriol 187: 3650-3661.
    • (2005) J Bacteriol , vol.187 , pp. 3650-3661
    • Brickman, T.J.1    Armstrong, S.K.2
  • 14
    • 35649003856 scopus 로고    scopus 로고
    • Impact of alcaligin siderophore utilization on in vivo growth of Bordetella pertussis
    • Brickman, T.J., and Armstrong, S.K. (2007) Impact of alcaligin siderophore utilization on in vivo growth of Bordetella pertussis. Infect Immun 75: 5305-5312.
    • (2007) Infect Immun , vol.75 , pp. 5305-5312
    • Brickman, T.J.1    Armstrong, S.K.2
  • 15
    • 0029978133 scopus 로고    scopus 로고
    • Purification, spectroscopic analysis and biological activity of the macrocyclic dihydroxamate siderophore alcaligin produced by Bordetella pertussis and Bordetella bronchiseptica
    • Brickman, T.J., Hansel, J.G., Miller, M.J., and Armstrong, S.K. (1996) Purification, spectroscopic analysis and biological activity of the macrocyclic dihydroxamate siderophore alcaligin produced by Bordetella pertussis and Bordetella bronchiseptica. Biometals 9: 191-203.
    • (1996) Biometals , vol.9 , pp. 191-203
    • Brickman, T.J.1    Hansel, J.G.2    Miller, M.J.3    Armstrong, S.K.4
  • 16
    • 33644749142 scopus 로고    scopus 로고
    • Heme transport contributes to in vivo fitness of Bordetella pertussis during primary infection in mice
    • Brickman, T.J., Vanderpool, C.K., and Armstrong, S.K. (2006) Heme transport contributes to in vivo fitness of Bordetella pertussis during primary infection in mice. Infect Immun 74: 1741-1744.
    • (2006) Infect Immun , vol.74 , pp. 1741-1744
    • Brickman, T.J.1    Vanderpool, C.K.2    Armstrong, S.K.3
  • 17
    • 51649085624 scopus 로고    scopus 로고
    • Differential expression of Bordetella pertussis iron transport system genes during infection
    • Brickman, T.J., Hanawa, T., Anderson, M.T., Suhadolc, R.J., and Armstrong, S.K. (2008) Differential expression of Bordetella pertussis iron transport system genes during infection. Mol Microbiol 70: 3-14.
    • (2008) Mol Microbiol , vol.70 , pp. 3-14
    • Brickman, T.J.1    Hanawa, T.2    Anderson, M.T.3    Suhadolc, R.J.4    Armstrong, S.K.5
  • 18
    • 80052544163 scopus 로고    scopus 로고
    • Transcriptional profiling of the iron starvation response in Bordetella pertussis provides new insights into siderophore utilization and virulence gene expression
    • Brickman, T.J., Cummings, C.A., Liew, S.-Y., Relman, D.A., and Armstrong, S.K. (2011) Transcriptional profiling of the iron starvation response in Bordetella pertussis provides new insights into siderophore utilization and virulence gene expression. J Bacteriol 193: 4798-4812.
    • (2011) J Bacteriol , vol.193 , pp. 4798-4812
    • Brickman, T.J.1    Cummings, C.A.2    Liew, S.-Y.3    Relman, D.A.4    Armstrong, S.K.5
  • 21
    • 77955338180 scopus 로고    scopus 로고
    • Structure and function of P19, a high-affinity iron transporter of the human pathogen Campylobacter jejuni
    • Chan, A.C.K., Doukov, T.I., Scofield, M., Tom-Yew, S.A.L., Ramin, A.B., Mackichan, J.K., etal. (2010) Structure and function of P19, a high-affinity iron transporter of the human pathogen Campylobacter jejuni. J Mol Biol 401: 590-604.
    • (2010) J Mol Biol , vol.401 , pp. 590-604
    • Chan, A.C.K.1    Doukov, T.I.2    Scofield, M.3    Tom-Yew, S.A.L.4    Ramin, A.B.5    Mackichan, J.K.6
  • 22
    • 0028021507 scopus 로고
    • BvgAS-mediated signal transduction: analysis of phase-locked regulatory mutants of Bordetella bronchiseptica in a rabbit model
    • Cotter, P.A., and Miller, J.F. (1994) BvgAS-mediated signal transduction: analysis of phase-locked regulatory mutants of Bordetella bronchiseptica in a rabbit model. Infect Immun 62: 3381-3390.
    • (1994) Infect Immun , vol.62 , pp. 3381-3390
    • Cotter, P.A.1    Miller, J.F.2
  • 23
    • 0030993684 scopus 로고    scopus 로고
    • A mutation in the Bordetella bronchiseptica bvgS gene results in reduced virulence and increased resistance to starvation, and identifies a new class of Bvg-regulated antigens
    • Cotter, P.A., and Miller, J.F. (1997) A mutation in the Bordetella bronchiseptica bvgS gene results in reduced virulence and increased resistance to starvation, and identifies a new class of Bvg-regulated antigens. Mol Microbiol 24: 671-685.
    • (1997) Mol Microbiol , vol.24 , pp. 671-685
    • Cotter, P.A.1    Miller, J.F.2
  • 24
    • 0037092054 scopus 로고    scopus 로고
    • Reduction of iron by extracellular iron reductases: implications for microbial iron acquisition
    • Cowart, R.E. (2002) Reduction of iron by extracellular iron reductases: implications for microbial iron acquisition. Arch Biochem Biophys 400: 273-281.
    • (2002) Arch Biochem Biophys , vol.400 , pp. 273-281
    • Cowart, R.E.1
  • 25
    • 0022639413 scopus 로고
    • Role of pyocyanin in the acquisition of iron from transferrin
    • Cox, C.D. (1986) Role of pyocyanin in the acquisition of iron from transferrin. Infect Immun 52: 263-270.
    • (1986) Infect Immun , vol.52 , pp. 263-270
    • Cox, C.D.1
  • 27
    • 0000788083 scopus 로고
    • Determination of subnanomolar levels of iron(II) and total dissolved iron in seawater by flow-Injection analysis with chemiluminescence detection
    • Elrod, V.A., Johnson, K.S., and Coale, K.H. (1991) Determination of subnanomolar levels of iron(II) and total dissolved iron in seawater by flow-Injection analysis with chemiluminescence detection. Anal Chem 63: 893-898.
    • (1991) Anal Chem , vol.63 , pp. 893-898
    • Elrod, V.A.1    Johnson, K.S.2    Coale, K.H.3
  • 28
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D.H., and Helinski, D.R. (1979) Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc Natl Acad Sci USA 76: 1648-1652.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 29
    • 33751269096 scopus 로고    scopus 로고
    • Mechanisms of acid and base secretion by the airway epithelium
    • Fischer, H., and Widdicombe, J.H. (2006) Mechanisms of acid and base secretion by the airway epithelium. J Membr Biol 211: 139-150.
    • (2006) J Membr Biol , vol.211 , pp. 139-150
    • Fischer, H.1    Widdicombe, J.H.2
  • 30
    • 33748670718 scopus 로고    scopus 로고
    • A new ferrous iron-uptake transporter, EfeU (YcdN), from Escherichia coli
    • Große, C., Scherer, J., Koch, D., Otto, M., Taudte, N., and Grass, G. (2006) A new ferrous iron-uptake transporter, EfeU (YcdN), from Escherichia coli. Mol Microbiol 62: 120-131.
    • (2006) Mol Microbiol , vol.62 , pp. 120-131
    • Große, C.1    Scherer, J.2    Koch, D.3    Otto, M.4    Taudte, N.5    Grass, G.6
  • 31
    • 0002369613 scopus 로고
    • Ferrous iron transport mutants in Escherichia coli K12
    • Hantke, K. (1987) Ferrous iron transport mutants in Escherichia coli K12. FEMS Microbiol Lett 44: 53-57.
    • (1987) FEMS Microbiol Lett , vol.44 , pp. 53-57
    • Hantke, K.1
  • 32
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: molecular control of mammalian iron metabolism
    • Hentze, M.W., Muckenthaler, M.U., and Andrews, N.C. (2004) Balancing acts: molecular control of mammalian iron metabolism. Cell 117: 285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 34
    • 0027487221 scopus 로고
    • Characterization of the ferrous iron uptake system of Escherichia coli
    • Kammler, M., Schön, C., and Hantke, K. (1993) Characterization of the ferrous iron uptake system of Escherichia coli. J Bacteriol 175: 6212-6219.
    • (1993) J Bacteriol , vol.175 , pp. 6212-6219
    • Kammler, M.1    Schön, C.2    Hantke, K.3
  • 35
    • 0001876465 scopus 로고
    • Studies on Haemophilus pertussis. V. Relation between the phase of bacilli and the progress of the whooping-cough
    • Kasuga, T., Nakase, Y., Ukishima, K., and Takatsu, K. (1954) Studies on Haemophilus pertussis. V. Relation between the phase of bacilli and the progress of the whooping-cough. Kitasato Arch Exp Med 27: 57-62.
    • (1954) Kitasato Arch Exp Med , vol.27 , pp. 57-62
    • Kasuga, T.1    Nakase, Y.2    Ukishima, K.3    Takatsu, K.4
  • 36
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria
    • Keen, N.T., Tamaki, S., Kobayashi, D., and Trollinger, D. (1988) Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria. Gene 70: 191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 37
    • 0037893024 scopus 로고    scopus 로고
    • The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen
    • Kehres, D.G., Zaharik, M.L., Finlay, B.B., and Maguire, M.E. (2000) The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen. Mol Microbiol 36: 1085-1100.
    • (2000) Mol Microbiol , vol.36 , pp. 1085-1100
    • Kehres, D.G.1    Zaharik, M.L.2    Finlay, B.B.3    Maguire, M.E.4
  • 39
    • 0025877147 scopus 로고
    • Spectrophotometric determination of iron (II) in seawater at nanomolar concentrations
    • King, J.D., Lin, J., and Kester, D.R. (1991) Spectrophotometric determination of iron (II) in seawater at nanomolar concentrations. Anal Chim Acta 247: 125-132.
    • (1991) Anal Chim Acta , vol.247 , pp. 125-132
    • King, J.D.1    Lin, J.2    Kester, D.R.3
  • 40
    • 79960149723 scopus 로고    scopus 로고
    • Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11
    • Koch, D., Chan, A.C.K., Murphy, M.E.P., Lilie, H., Grass, G., and Nies, D.H. (2011) Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11. J Biol Chem 286: 25317-25330.
    • (2011) J Biol Chem , vol.286 , pp. 25317-25330
    • Koch, D.1    Chan, A.C.K.2    Murphy, M.E.P.3    Lilie, H.4    Grass, G.5    Nies, D.H.6
  • 41
    • 33646893459 scopus 로고    scopus 로고
    • Evidence for iron channeling in the Fet3p-Ftr1p high-affinity iron uptake complex in the yeast plasma membrane
    • Kwok, E.Y., Severance, S., and Kosman, D.J. (2006) Evidence for iron channeling in the Fet3p-Ftr1p high-affinity iron uptake complex in the yeast plasma membrane. Biochemistry 45: 6317-6327.
    • (2006) Biochemistry , vol.45 , pp. 6317-6327
    • Kwok, E.Y.1    Severance, S.2    Kosman, D.J.3
  • 42
    • 0033729426 scopus 로고    scopus 로고
    • Generation of deletion and point mutations with one primer in a single cloning step
    • Makarova, O., Kamberov, E., and Margolis, B. (2000) Generation of deletion and point mutations with one primer in a single cloning step. Biotechniques 29: 970-972.
    • (2000) Biotechniques , vol.29 , pp. 970-972
    • Makarova, O.1    Kamberov, E.2    Margolis, B.3
  • 43
    • 17444421538 scopus 로고    scopus 로고
    • Molecular pathogenesis, epidemiology, and clinical manifestations of respiratory infections due to Bordetella pertussis and other Bordetella subspecies
    • Mattoo, S., and Cherry, J.D. (2005) Molecular pathogenesis, epidemiology, and clinical manifestations of respiratory infections due to Bordetella pertussis and other Bordetella subspecies. Clin Microbiol Rev 18: 326-382.
    • (2005) Clin Microbiol Rev , vol.18 , pp. 326-382
    • Mattoo, S.1    Cherry, J.D.2
  • 44
  • 45
    • 0042866137 scopus 로고    scopus 로고
    • Physiology and molecular biology of dietary iron absorption
    • Miret, S., Simpson, R.J., and McKie, A.T. (2003) Physiology and molecular biology of dietary iron absorption. Annu Rev Nutr 23: 283-301.
    • (2003) Annu Rev Nutr , vol.23 , pp. 283-301
    • Miret, S.1    Simpson, R.J.2    McKie, A.T.3
  • 46
    • 34848869068 scopus 로고    scopus 로고
    • Passively released heme from hemoglobin and myoglobin is a potential source of nutrient iron for Bordetella bronchiseptica
    • Mocny, J.C., Olson, J.S., and Connell, T.D. (2007) Passively released heme from hemoglobin and myoglobin is a potential source of nutrient iron for Bordetella bronchiseptica. Infect Immun 75: 4857-4866.
    • (2007) Infect Immun , vol.75 , pp. 4857-4866
    • Mocny, J.C.1    Olson, J.S.2    Connell, T.D.3
  • 47
    • 0028847512 scopus 로고
    • Identification of alcaligin as the siderophore produced by Bordetella pertussis and B. bronchiseptica
    • Moore, C.H., Foster, L.A., Gerbig, D.G., Dyer, D.W., and Gibson, B.W. (1995) Identification of alcaligin as the siderophore produced by Bordetella pertussis and B. bronchiseptica. J Bacteriol 177: 1116-1118.
    • (1995) J Bacteriol , vol.177 , pp. 1116-1118
    • Moore, C.H.1    Foster, L.A.2    Gerbig, D.G.3    Dyer, D.W.4    Gibson, B.W.5
  • 48
    • 14944341462 scopus 로고    scopus 로고
    • Innate host defense of the lung: effects of lung-lining fluid pH
    • Ng, A.W., Bidani, A., and Heming, T.A. (2004) Innate host defense of the lung: effects of lung-lining fluid pH. Lung 182: 297-317.
    • (2004) Lung , vol.182 , pp. 297-317
    • Ng, A.W.1    Bidani, A.2    Heming, T.A.3
  • 49
    • 0032832385 scopus 로고    scopus 로고
    • Disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, haemin and haemoglobin as iron sources
    • Nicholson, M.L., and Beall, B. (1999) Disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, haemin and haemoglobin as iron sources. Microbiology 145: 2453-2461.
    • (1999) Microbiology , vol.145 , pp. 2453-2461
    • Nicholson, M.L.1    Beall, B.2
  • 50
    • 3042855363 scopus 로고    scopus 로고
    • Iron acquisition and regulation in Campylobacter jejuni
    • Palyada, K., Threadgill, D., and Stintzi, A. (2004) Iron acquisition and regulation in Campylobacter jejuni. J Bacteriol 186: 4714-4729.
    • (2004) J Bacteriol , vol.186 , pp. 4714-4729
    • Palyada, K.1    Threadgill, D.2    Stintzi, A.3
  • 51
    • 0042355274 scopus 로고    scopus 로고
    • Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica
    • Parkhill, J., Sebaihia, M., Preston, A., Murphy, L., Thomson, N., Harris, D., etal. (2003) Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica. Nat Genet 35: 32-40.
    • (2003) Nat Genet , vol.35 , pp. 32-40
    • Parkhill, J.1    Sebaihia, M.2    Preston, A.3    Murphy, L.4    Thomson, N.5    Harris, D.6
  • 52
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen, T.N., Brunak, S., von Heijne, G., and Nielsen, H. (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 53
    • 33749241473 scopus 로고    scopus 로고
    • Redox speciation of iron in waters by resin-based column chromatography
    • Pohl, P., and Prusisz, B. (2006) Redox speciation of iron in waters by resin-based column chromatography. Trends Anal Chem 25: 909-916.
    • (2006) Trends Anal Chem , vol.25 , pp. 909-916
    • Pohl, P.1    Prusisz, B.2
  • 54
    • 34248647893 scopus 로고    scopus 로고
    • TonB-dependent energy transduction between outer and cytoplasmic membranes
    • Postle, K., and Larsen, R.A. (2007) TonB-dependent energy transduction between outer and cytoplasmic membranes. Biometals 20: 453-465.
    • (2007) Biometals , vol.20 , pp. 453-465
    • Postle, K.1    Larsen, R.A.2
  • 55
    • 0035045572 scopus 로고    scopus 로고
    • Expression of the putative siderophore receptor gene bfrZ is controlled by the extracytoplasmic-function sigma factor BupI in Bordetella bronchiseptica
    • Pradel, E., and Locht, C. (2001) Expression of the putative siderophore receptor gene bfrZ is controlled by the extracytoplasmic-function sigma factor BupI in Bordetella bronchiseptica. J Bacteriol 183: 2910-2917.
    • (2001) J Bacteriol , vol.183 , pp. 2910-2917
    • Pradel, E.1    Locht, C.2
  • 56
    • 0034100621 scopus 로고    scopus 로고
    • Bordetella pertussis TonB, a Bvg-independent virulence determinant
    • Pradel, E., Guiso, N., Menozzi, F.D., and Locht, C. (2000) Bordetella pertussis TonB, a Bvg-independent virulence determinant. Infect Immun 68: 1919-1927.
    • (2000) Infect Immun , vol.68 , pp. 1919-1927
    • Pradel, E.1    Guiso, N.2    Menozzi, F.D.3    Locht, C.4
  • 57
    • 13944268797 scopus 로고    scopus 로고
    • A novel method for accurate operon predictions in all sequenced prokaryotes
    • Price, M., Huang, K., Alm, E., and Arkin, A. (2005) A novel method for accurate operon predictions in all sequenced prokaryotes. Nucleic Acids Res 33: 880-892.
    • (2005) Nucleic Acids Res , vol.33 , pp. 880-892
    • Price, M.1    Huang, K.2    Alm, E.3    Arkin, A.4
  • 58
    • 77949424566 scopus 로고    scopus 로고
    • EfeO-cupredoxins: major new members of the cupredoxin superfamily with roles in bacterial iron transport
    • Rajasekaran, M.B., Nilapwar, S., Andrews, S.C., and Watson, K.A. (2010) EfeO-cupredoxins: major new members of the cupredoxin superfamily with roles in bacterial iron transport. Biometals 23: 1-17.
    • (2010) Biometals , vol.23 , pp. 1-17
    • Rajasekaran, M.B.1    Nilapwar, S.2    Andrews, S.C.3    Watson, K.A.4
  • 61
    • 0034443266 scopus 로고    scopus 로고
    • Phagosome acidification has opposite effects on intracellular survival of Bordetella pertussis and B. bronchiseptica
    • Schneider, B., Gross, R., and Haas, A. (2000) Phagosome acidification has opposite effects on intracellular survival of Bordetella pertussis and B. bronchiseptica. Infect Immun 68: 7039-7048.
    • (2000) Infect Immun , vol.68 , pp. 7039-7048
    • Schneider, B.1    Gross, R.2    Haas, A.3
  • 63
    • 2942716756 scopus 로고    scopus 로고
    • The Ftr1p iron permease in the yeast plasma membrane: orientation, topology and structure-function relationships
    • Severance, S., Chakraborty, S., and Kosman, D.J. (2004) The Ftr1p iron permease in the yeast plasma membrane: orientation, topology and structure-function relationships. Biochem J 380: 487-496.
    • (2004) Biochem J , vol.380 , pp. 487-496
    • Severance, S.1    Chakraborty, S.2    Kosman, D.J.3
  • 64
    • 33744959238 scopus 로고    scopus 로고
    • Assembly, activation, and trafficking of the Fet3p·Ftr1p high affinity iron permease complex in Saccharomyces cerevisiae
    • Singh, A., Severance, S., Kaur, N., Wiltsie, W., and Kosman, D.J. (2006) Assembly, activation, and trafficking of the Fet3p·Ftr1p high affinity iron permease complex in Saccharomyces cerevisiae. J Biol Chem 281: 13355-13364.
    • (2006) J Biol Chem , vol.281 , pp. 13355-13364
    • Singh, A.1    Severance, S.2    Kaur, N.3    Wiltsie, W.4    Kosman, D.J.5
  • 65
    • 34250107503 scopus 로고
    • Promoters in the nodulation region of the Rhizobium leguminosarum Sym plasmid pRL1J1
    • Spaink, H.P., Okker, R.J.H., Wijffelman, C.A., Pees, E., and Lugtenberg, B.J.J. (1987) Promoters in the nodulation region of the Rhizobium leguminosarum Sym plasmid pRL1J1. Plant Mol Biol 9: 27-39.
    • (1987) Plant Mol Biol , vol.9 , pp. 27-39
    • Spaink, H.P.1    Okker, R.J.H.2    Wijffelman, C.A.3    Pees, E.4    Lugtenberg, B.J.J.5
  • 66
    • 0014862345 scopus 로고
    • A simple chemically defined medium for the production of phase I Bordetella pertussis
    • Stainer, D., and Scholte, M. (1970) A simple chemically defined medium for the production of phase I Bordetella pertussis. J Gen Microbiol 63: 211.
    • (1970) J Gen Microbiol , vol.63 , pp. 211
    • Stainer, D.1    Scholte, M.2
  • 67
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • Stearman, R., Yuan, D.S., Yamaguchi-Iwai, Y., Klausner, R.D., and Dancis, A. (1996) A permease-oxidase complex involved in high-affinity iron uptake in yeast. Science 271: 1552-1557.
    • (1996) Science , vol.271 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.S.2    Yamaguchi-Iwai, Y.3    Klausner, R.D.4    Dancis, A.5
  • 68
    • 33847670407 scopus 로고
    • Ferrozine-a new spectrophotometric reagent for iron
    • Stookey, L.L. (1970) Ferrozine-a new spectrophotometric reagent for iron. Anal Chem 42: 779-781.
    • (1970) Anal Chem , vol.42 , pp. 779-781
    • Stookey, L.L.1
  • 69
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: application to topology prediction
    • Tusnády, G.E., and Simon, I. (1998) Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J Mol Biol 283: 489-506.
    • (1998) J Mol Biol , vol.283 , pp. 489-506
    • Tusnády, G.E.1    Simon, I.2
  • 71
    • 0034967288 scopus 로고    scopus 로고
    • The Bordetella bhu locus is required for heme iron utilization
    • Vanderpool, C.K., and Armstrong, S.K. (2001) The Bordetella bhu locus is required for heme iron utilization. J Bacteriol 183: 4278-4287.
    • (2001) J Bacteriol , vol.183 , pp. 4278-4287
    • Vanderpool, C.K.1    Armstrong, S.K.2
  • 72
    • 0033117894 scopus 로고    scopus 로고
    • Extracellular iron reductases: identification of a new class of enzymes by siderophore-producing microorganisms
    • Vartivarian, S.E., and Cowart, R.E. (1999) Extracellular iron reductases: identification of a new class of enzymes by siderophore-producing microorganisms. Arch Biochem Biophys 364: 75-82.
    • (1999) Arch Biochem Biophys , vol.364 , pp. 75-82
    • Vartivarian, S.E.1    Cowart, R.E.2
  • 73
    • 0031690670 scopus 로고    scopus 로고
    • Iron-responsive gene regulation in a Campylobacter jejuni fur mutant
    • van Vliet, A.H., Wooldridge, K.G., and Ketley, J.M. (1998) Iron-responsive gene regulation in a Campylobacter jejuni fur mutant. J Bacteriol 180: 5291-5298.
    • (1998) J Bacteriol , vol.180 , pp. 5291-5298
    • van Vliet, A.H.1    Wooldridge, K.G.2    Ketley, J.M.3
  • 74
    • 41649111954 scopus 로고    scopus 로고
    • Redox reactions of phenazine antibiotics with ferric (hydr)oxides and molecular oxygen
    • Wang, Y., and Newman, D.K. (2008) Redox reactions of phenazine antibiotics with ferric (hydr)oxides and molecular oxygen. Environ Sci Technol 42: 2380.
    • (2008) Environ Sci Technol , vol.42 , pp. 2380
    • Wang, Y.1    Newman, D.K.2
  • 75
    • 33748766356 scopus 로고    scopus 로고
    • Characterization of ferric and ferrous iron transport systems in Vibrio cholerae
    • Wyckoff, E.E., Mey, A.R., Leimbach, A., Fisher, C.F., and Payne, S.M. (2006) Characterization of ferric and ferrous iron transport systems in Vibrio cholerae. J Bacteriol 188: 6515-6523.
    • (2006) J Bacteriol , vol.188 , pp. 6515-6523
    • Wyckoff, E.E.1    Mey, A.R.2    Leimbach, A.3    Fisher, C.F.4    Payne, S.M.5
  • 76
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu, N.Y., Wagner, J.R., Laird, M.R., Melli, G., Rey, S., Lo, R., etal. (2010) PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26: 1608-1615.
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6


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