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Volumn 78, Issue , 2013, Pages 197-210

Quantitative proteomic analysis of the exoelectrogenic bacterium Arcobacter butzleri ED-1 reveals increased abundance of a flagellin protein under anaerobic growth on an insoluble electrode

Author keywords

Arcobacter butzleri ED 1; Biofilm; Exoelectrogenesis; ITRAQ; Microbial fuel cell; Proteome

Indexed keywords

ADHESIN; CITRAMALIC ACID; CITRIC ACID; CYTOCHROME; FLAGELLIN; METHYLCITRIC ACID; PROTEIN TONB; PROTEOME; SODIUM CHLORIDE COTRANSPORTER; UNCLASSIFIED DRUG;

EID: 84871731339     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.09.039     Document Type: Article
Times cited : (23)

References (57)
  • 1
    • 64749084426 scopus 로고    scopus 로고
    • Exoelectrogenic bacteria that power microbial fuel cells
    • Logan B.E. Exoelectrogenic bacteria that power microbial fuel cells. Nat Rev Microbiol 2009, 7:375-381.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 375-381
    • Logan, B.E.1
  • 2
    • 57049119571 scopus 로고    scopus 로고
    • The microbe electric: conversion of organic matter to electricity
    • Lovley D. The microbe electric: conversion of organic matter to electricity. Curr Opin Biotechnol 2008, 19:564-571.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 564-571
    • Lovley, D.1
  • 3
    • 22344440310 scopus 로고    scopus 로고
    • Power generation in fed-batch microbial fuel cells as a function of ionic strength, temperature, and reactor configuration
    • Liu H., Cheng S.A., Logan B.E. Power generation in fed-batch microbial fuel cells as a function of ionic strength, temperature, and reactor configuration. Environ Sci Technol 2005, 39:5488-5493.
    • (2005) Environ Sci Technol , vol.39 , pp. 5488-5493
    • Liu, H.1    Cheng, S.A.2    Logan, B.E.3
  • 4
    • 47049103719 scopus 로고    scopus 로고
    • Towards practical implementation of bioelectrochemical wastewater treatment
    • Rozendal R.A., Hamelers H.V., Rabaey K., Keller J., et al. Towards practical implementation of bioelectrochemical wastewater treatment. Trends Biotechnol 2008, 26:450-459.
    • (2008) Trends Biotechnol , vol.26 , pp. 450-459
    • Rozendal, R.A.1    Hamelers, H.V.2    Rabaey, K.3    Keller, J.4
  • 5
    • 80053630813 scopus 로고    scopus 로고
    • Hydrogen production from inexhaustible supplies of fresh and salt water using microbial reverse-electrodialysis electrolysis cells
    • Kim Y., Logan B.E. Hydrogen production from inexhaustible supplies of fresh and salt water using microbial reverse-electrodialysis electrolysis cells. Proc Natl Acad Sci U S A 2011, 108:16176-16181.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 16176-16181
    • Kim, Y.1    Logan, B.E.2
  • 6
    • 0037337606 scopus 로고    scopus 로고
    • Electricity production by Geobacter sulfurreducens attached to electrodes
    • Bond D.R., Lovley D.R. Electricity production by Geobacter sulfurreducens attached to electrodes. Appl Environ Microbiol 2003, 69:1548-1555.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 1548-1555
    • Bond, D.R.1    Lovley, D.R.2
  • 7
    • 35949000517 scopus 로고    scopus 로고
    • Current production and metal oxide reduction by Shewanella oneidensis MR-1 wild type and mutants
    • Bretschger O., Obraztsova A., Sturm C., Chang I., et al. Current production and metal oxide reduction by Shewanella oneidensis MR-1 wild type and mutants. Appl Environ Microbiol 2007, 73:7003-7012.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7003-7012
    • Bretschger, O.1    Obraztsova, A.2    Sturm, C.3    Chang, I.4
  • 8
    • 71549170875 scopus 로고    scopus 로고
    • A kinetic perspective on extracellular electron transfer by anode-respiring bacteria
    • Torres C.I., Marcus A.K., Lee H.S., Parameswaran P., et al. A kinetic perspective on extracellular electron transfer by anode-respiring bacteria. FEMS Microbiol Rev 2009, 34:3-17.
    • (2009) FEMS Microbiol Rev , vol.34 , pp. 3-17
    • Torres, C.I.1    Marcus, A.K.2    Lee, H.S.3    Parameswaran, P.4
  • 9
    • 73349134931 scopus 로고    scopus 로고
    • Characterization of an electron conduit between bacteria and the extracellular environment
    • Hartshorne R.S., Reardon C.L., Ross D., Nuester J., et al. Characterization of an electron conduit between bacteria and the extracellular environment. Proc Natl Acad Sci U S A 2009, 106:22169-22174.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 22169-22174
    • Hartshorne, R.S.1    Reardon, C.L.2    Ross, D.3    Nuester, J.4
  • 10
    • 33746624663 scopus 로고    scopus 로고
    • Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms
    • Gorby Y.A., Yanina S., McLean J.S., Rosso K., et al. Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms. Proc Natl Acad Sci U S A 2006, 103:11358-11363.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11358-11363
    • Gorby, Y.A.1    Yanina, S.2    McLean, J.S.3    Rosso, K.4
  • 11
    • 66249098568 scopus 로고    scopus 로고
    • Anode biofilm transcriptomics reveals outer surface components essential for high density current production in Geobacter sulfurreducens fuel cells
    • Nevin K.P., Kim B.C., Glaven R.H., Johnson J.P., et al. Anode biofilm transcriptomics reveals outer surface components essential for high density current production in Geobacter sulfurreducens fuel cells. PLoS One 2009, 10.1371/journal.pone.0005628.
    • (2009) PLoS One
    • Nevin, K.P.1    Kim, B.C.2    Glaven, R.H.3    Johnson, J.P.4
  • 12
    • 80052557316 scopus 로고    scopus 로고
    • Tunable metallic-like conductivity in microbial nanowire networks
    • Malvankar N.S., Vargas M., Nevin K.P., Franks A.E., et al. Tunable metallic-like conductivity in microbial nanowire networks. Nat Nano 2011, 2011(6):573-579.
    • (2011) Nat Nano , vol.2011 , Issue.6 , pp. 573-579
    • Malvankar, N.S.1    Vargas, M.2    Nevin, K.P.3    Franks, A.E.4
  • 13
    • 18344391948 scopus 로고    scopus 로고
    • Microbial phenazine production enhances electron transfer in biofuel cells
    • Rabaey K., Boon N., Hofte M., Verstraete W. Microbial phenazine production enhances electron transfer in biofuel cells. Environ Sci Technol 2005, 39:3401-3408.
    • (2005) Environ Sci Technol , vol.39 , pp. 3401-3408
    • Rabaey, K.1    Boon, N.2    Hofte, M.3    Verstraete, W.4
  • 14
    • 41649085415 scopus 로고    scopus 로고
    • Shewanella secretes flavins that mediate extracellular electron transfer
    • Marsili E., Baron D.B., Shikhare I.D., Coursolle D., et al. Shewanella secretes flavins that mediate extracellular electron transfer. Proc Natl Acad Sci U S A 2008, 105:3968-3973.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3968-3973
    • Marsili, E.1    Baron, D.B.2    Shikhare, I.D.3    Coursolle, D.4
  • 15
    • 0039808935 scopus 로고
    • Bioelectrochemical energy conversion
    • Berk R.S., Canfield J.H. Bioelectrochemical energy conversion. Appl Microbiol 1964, 12:10-12.
    • (1964) Appl Microbiol , vol.12 , pp. 10-12
    • Berk, R.S.1    Canfield, J.H.2
  • 16
    • 0034660186 scopus 로고    scopus 로고
    • Potential for nonenzymatic reduction of Fe (III) via electron shuttling in subsurface sediments
    • Nevin K.P., Lovley D.R. Potential for nonenzymatic reduction of Fe (III) via electron shuttling in subsurface sediments. Environ Sci Technol 2000, 34:2472-2478.
    • (2000) Environ Sci Technol , vol.34 , pp. 2472-2478
    • Nevin, K.P.1    Lovley, D.R.2
  • 17
    • 72949099697 scopus 로고    scopus 로고
    • Novel electrochemically active bacterium phylogenetically related to Arcobacter butzleri, isolated from a microbial fuel cell
    • Fedorovich V., Knighton M.C., Pagaling E., Ward F.B., et al. Novel electrochemically active bacterium phylogenetically related to Arcobacter butzleri, isolated from a microbial fuel cell. Appl Environ Microbiol 2009, 75:7326-7334.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 7326-7334
    • Fedorovich, V.1    Knighton, M.C.2    Pagaling, E.3    Ward, F.B.4
  • 18
    • 80655128410 scopus 로고    scopus 로고
    • Complete genome sequences of Arcobacter butzleri ED-1 and Arcobacter sp. strain l, both isolated from a microbial fuel cell
    • Toh H., Sharma V.K., Oshima K., Kondo S., et al. Complete genome sequences of Arcobacter butzleri ED-1 and Arcobacter sp. strain l, both isolated from a microbial fuel cell. J Bacteriol 2011, 10.1128/JB.06084-11.
    • (2011) J Bacteriol
    • Toh, H.1    Sharma, V.K.2    Oshima, K.3    Kondo, S.4
  • 19
    • 43349108455 scopus 로고    scopus 로고
    • The complete genome sequence and analysis of the epsilonproteobacterium Arcobacter butzleri
    • Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., et al. The complete genome sequence and analysis of the epsilonproteobacterium Arcobacter butzleri. PLoS One 2007, 2:e1358.
    • (2007) PLoS One , vol.2
    • Miller, W.G.1    Parker, C.T.2    Rubenfield, M.3    Mendz, G.L.4
  • 20
    • 44249125986 scopus 로고    scopus 로고
    • Isolation of the exoelectrogenic bacterium Ochrobactrum anthropi YZ-1 by using a U-tube microbial fuel cell
    • Zuo Y., Xing D.F., Regan J.M., Logan B.E. Isolation of the exoelectrogenic bacterium Ochrobactrum anthropi YZ-1 by using a U-tube microbial fuel cell. Appl Environ Microbiol 2008, 74:3130-3137.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 3130-3137
    • Zuo, Y.1    Xing, D.F.2    Regan, J.M.3    Logan, B.E.4
  • 21
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly"
    • Ow S.Y., Salim M., Noirel J., Evans C., et al. iTRAQ underestimation in simple and complex mixtures: "the good, the bad and the ugly". J Proteome Res 2009, 8:5347-5355.
    • (2009) J Proteome Res , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4
  • 22
    • 0026637182 scopus 로고
    • Polyphasic taxonomic study of the emended genus Arcobacter with Arcobacter butzleri comb. nov. and Arcobacter skirrowii sp. nov., an aerotolerant bacterium isolated from veterinary specimens
    • Vandamme P., Vancanneyt M., Pot B., Mels L., et al. Polyphasic taxonomic study of the emended genus Arcobacter with Arcobacter butzleri comb. nov. and Arcobacter skirrowii sp. nov., an aerotolerant bacterium isolated from veterinary specimens. Int J Syst Bacteriol 1992, 42:344-356.
    • (1992) Int J Syst Bacteriol , vol.42 , pp. 344-356
    • Vandamme, P.1    Vancanneyt, M.2    Pot, B.3    Mels, L.4
  • 23
    • 0035977375 scopus 로고    scopus 로고
    • Development of a new protocol for the isolation and quantification of Arcobacter species from poultry products
    • Houf K., Devriese L.A., De Zutter L., Van Hoof J., et al. Development of a new protocol for the isolation and quantification of Arcobacter species from poultry products. Int J Food Microbiol 2001, 71:189-196.
    • (2001) Int J Food Microbiol , vol.71 , pp. 189-196
    • Houf, K.1    Devriese, L.A.2    De Zutter, L.3    Van Hoof, J.4
  • 24
    • 76149120848 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of Sulfolobus solfataricus membrane proteins
    • Pham T.K., Sierocinski P., van der Oost J., Wright P.C. Quantitative proteomic analysis of Sulfolobus solfataricus membrane proteins. J Proteome Res 2010, 9:1165-1172.
    • (2010) J Proteome Res , vol.9 , pp. 1165-1172
    • Pham, T.K.1    Sierocinski, P.2    van der Oost, J.3    Wright, P.C.4
  • 25
    • 77956130622 scopus 로고    scopus 로고
    • A quantitative proteomic analysis of biofilm adaptation by the periodontal pathogen Tannerella forsythia
    • Pham T.K., Roy S., Noirel J., Douglas I., et al. A quantitative proteomic analysis of biofilm adaptation by the periodontal pathogen Tannerella forsythia. Proteomics 2010, 10:3130-3141.
    • (2010) Proteomics , vol.10 , pp. 3130-3141
    • Pham, T.K.1    Roy, S.2    Noirel, J.3    Douglas, I.4
  • 26
    • 33645466243 scopus 로고    scopus 로고
    • Toward the complete membrane proteome: high coverage of integral membrane proteins through transmembrane peptide detection
    • Fischer F., Wolters D., Rogner M., Poetsch A. Toward the complete membrane proteome: high coverage of integral membrane proteins through transmembrane peptide detection. Mol Cell Proteomics 2006, 5:444-453.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 444-453
    • Fischer, F.1    Wolters, D.2    Rogner, M.3    Poetsch, A.4
  • 27
    • 79952774780 scopus 로고    scopus 로고
    • Methods in quantitative proteomics: setting iTRAQ on the right track
    • Noirel J., Evans C., Salim M., Mukherjee J., et al. Methods in quantitative proteomics: setting iTRAQ on the right track. Curr Proteomics 2010, 8:17-30.
    • (2010) Curr Proteomics , vol.8 , pp. 17-30
    • Noirel, J.1    Evans, C.2    Salim, M.3    Mukherjee, J.4
  • 28
    • 77952979841 scopus 로고    scopus 로고
    • Balancing robust quantification and identification for iTRAQ: application of UHR-ToF MS
    • Ow S.Y., Noirel J., Salim M., Evans C., et al. Balancing robust quantification and identification for iTRAQ: application of UHR-ToF MS. Proteomics 2010, 10:2205-2213.
    • (2010) Proteomics , vol.10 , pp. 2205-2213
    • Ow, S.Y.1    Noirel, J.2    Salim, M.3    Evans, C.4
  • 29
    • 0041358793 scopus 로고    scopus 로고
    • OLAV: towards high-throughput tandem mass spectrometry data identification
    • Colinge J., Masselot A., Giron M., Dessingy T., et al. OLAV: towards high-throughput tandem mass spectrometry data identification. Proteomics 2003, 3:1454-1463.
    • (2003) Proteomics , vol.3 , pp. 1454-1463
    • Colinge, J.1    Masselot, A.2    Giron, M.3    Dessingy, T.4
  • 30
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias J.E., Gygi S.P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 2007, 4:207-214.
    • (2007) Nat Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 31
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias J.E., Haas W., Faherty B.K., Gygi S.P. Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat Methods 2005, 2:667-675.
    • (2005) Nat Methods , vol.2 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 32
    • 21644483165 scopus 로고    scopus 로고
    • A comparison of the consistency of proteome quantitation using two-dimensional electrophoresis and shotgun isobaric tagging in Escherichia coli cells
    • Choe L.H., Aggarwal K., Franck Z., Lee K.H. A comparison of the consistency of proteome quantitation using two-dimensional electrophoresis and shotgun isobaric tagging in Escherichia coli cells. Electrophoresis 2005, 26:2437-2449.
    • (2005) Electrophoresis , vol.26 , pp. 2437-2449
    • Choe, L.H.1    Aggarwal, K.2    Franck, Z.3    Lee, K.H.4
  • 33
    • 11144220879 scopus 로고    scopus 로고
    • In the Archaea Haloferax volcanii, membrane protein biogenesis and protein synthesis rates are affected by decreased ribosomal binding to the translocon
    • Ring G., Eichler J. In the Archaea Haloferax volcanii, membrane protein biogenesis and protein synthesis rates are affected by decreased ribosomal binding to the translocon. J Biol Chem 2004, 279:53160-53166.
    • (2004) J Biol Chem , vol.279 , pp. 53160-53166
    • Ring, G.1    Eichler, J.2
  • 35
    • 77952837901 scopus 로고    scopus 로고
    • Proteomic expression profiling of Haemophilus influenzae grown in pooled human sputum from adults with chronic obstructive pulmonary disease reveal antioxidant and stress responses
    • Qu J., Lesse A.J., Brauer A.L., Cao J., et al. Proteomic expression profiling of Haemophilus influenzae grown in pooled human sputum from adults with chronic obstructive pulmonary disease reveal antioxidant and stress responses. BMC Microbiol 2010, 10:162.
    • (2010) BMC Microbiol , vol.10 , pp. 162
    • Qu, J.1    Lesse, A.J.2    Brauer, A.L.3    Cao, J.4
  • 37
    • 33645467362 scopus 로고    scopus 로고
    • Comparative proteome analysis of Staphylococcus aureus biofilm and planktonic cells and correlation with transcriptome profiling
    • Resch A., Leicht S., Saric M., Pasztor L., et al. Comparative proteome analysis of Staphylococcus aureus biofilm and planktonic cells and correlation with transcriptome profiling. Proteomics 2006, 6:1867-1877.
    • (2006) Proteomics , vol.6 , pp. 1867-1877
    • Resch, A.1    Leicht, S.2    Saric, M.3    Pasztor, L.4
  • 38
    • 34250348370 scopus 로고    scopus 로고
    • Flagellar motility is critical for Listeria monocytogenes biofilm formation
    • Lemon K.P., Higgins D.E., Kolter R. Flagellar motility is critical for Listeria monocytogenes biofilm formation. J Bacteriol 2007, 189:4418-4424.
    • (2007) J Bacteriol , vol.189 , pp. 4418-4424
    • Lemon, K.P.1    Higgins, D.E.2    Kolter, R.3
  • 39
    • 0031724115 scopus 로고    scopus 로고
    • Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development
    • O'Toole G.A., Kolter R. Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development. Mol Microbiol 1998, 30:295-304.
    • (1998) Mol Microbiol , vol.30 , pp. 295-304
    • O'Toole, G.A.1    Kolter, R.2
  • 41
    • 33744967758 scopus 로고    scopus 로고
    • Proteomic analysis of Campylobacter jejuni 11168 biofilms reveals a role for the motility complex in biofilm formation
    • Kalmokoff M., Lanthier P., Tremblay T.L., Foss M., et al. Proteomic analysis of Campylobacter jejuni 11168 biofilms reveals a role for the motility complex in biofilm formation. J Bacteriol 2006, 188:4312-4320.
    • (2006) J Bacteriol , vol.188 , pp. 4312-4320
    • Kalmokoff, M.1    Lanthier, P.2    Tremblay, T.L.3    Foss, M.4
  • 42
    • 43349106943 scopus 로고    scopus 로고
    • Arcobacter spp. possess two very short flagellins of which FlaA is essential for motility
    • Ho H.T., Lipman L.J., Wosten M.M., van Asten A.J., et al. Arcobacter spp. possess two very short flagellins of which FlaA is essential for motility. FEMS Immunol Med Microbiol 2008, 53:85-95.
    • (2008) FEMS Immunol Med Microbiol , vol.53 , pp. 85-95
    • Ho, H.T.1    Lipman, L.J.2    Wosten, M.M.3    van Asten, A.J.4
  • 43
    • 21344461500 scopus 로고    scopus 로고
    • Extracellular electron transfer via microbial nanowires
    • Reguera G., McCarthy K.D., Mehta T., Nicoll J.S., et al. Extracellular electron transfer via microbial nanowires. Nature 2005, 435:1098-1101.
    • (2005) Nature , vol.435 , pp. 1098-1101
    • Reguera, G.1    McCarthy, K.D.2    Mehta, T.3    Nicoll, J.S.4
  • 44
    • 67650085480 scopus 로고    scopus 로고
    • Selection of a variant of Geobacter sulfurreducens with enhanced capacity for current production in microbial fuel cells
    • Yi H., Nevin K.P., Kim B.C., Franks A.E., et al. Selection of a variant of Geobacter sulfurreducens with enhanced capacity for current production in microbial fuel cells. Biosens Bioelectron 2009, 24:3498-3503.
    • (2009) Biosens Bioelectron , vol.24 , pp. 3498-3503
    • Yi, H.1    Nevin, K.P.2    Kim, B.C.3    Franks, A.E.4
  • 45
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel M.E., Klena J.D., Rivera-Amill V., Monteville M.R., et al. Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus. J Bacteriol 2004, 186:3296-3303.
    • (2004) J Bacteriol , vol.186 , pp. 3296-3303
    • Konkel, M.E.1    Klena, J.D.2    Rivera-Amill, V.3    Monteville, M.R.4
  • 46
    • 34547602473 scopus 로고    scopus 로고
    • MyHits: improvements to an interactive resource for analyzing protein sequences
    • Pagni M., Ioannidis V., Cerutti L., Zahn-Zabal M., et al. MyHits: improvements to an interactive resource for analyzing protein sequences. Nucleic Acids Res 2007, 35:W433-W437.
    • (2007) Nucleic Acids Res , vol.35
    • Pagni, M.1    Ioannidis, V.2    Cerutti, L.3    Zahn-Zabal, M.4
  • 47
    • 0034306307 scopus 로고    scopus 로고
    • The REPRO server: finding protein internal sequence repeats through the Web
    • George R.A., Heringa J. The REPRO server: finding protein internal sequence repeats through the Web. Trends Biochem Sci 2000, 25:515-517.
    • (2000) Trends Biochem Sci , vol.25 , pp. 515-517
    • George, R.A.1    Heringa, J.2
  • 48
    • 33745225414 scopus 로고    scopus 로고
    • Bug juice: harvesting electricity with microorganisms
    • Lovley D. Bug juice: harvesting electricity with microorganisms. Nat Rev Microbiol 2006, 4:497-508.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 497-508
    • Lovley, D.1
  • 49
    • 79951664165 scopus 로고    scopus 로고
    • How the xap locus put electrical "Zap" in Geobacter sulfurreducens biofilms
    • Magnuson T.S. How the xap locus put electrical "Zap" in Geobacter sulfurreducens biofilms. J Bacteriol 2011, 193:1021-1022.
    • (2011) J Bacteriol , vol.193 , pp. 1021-1022
    • Magnuson, T.S.1
  • 50
    • 0036669911 scopus 로고    scopus 로고
    • Cytochrome cbb(3) oxidase and bacterial microaerobic metabolism
    • Pitcher R.S., Brittain T., Watmough N.J. Cytochrome cbb(3) oxidase and bacterial microaerobic metabolism. Biochem Soc Trans 2002, 30:653-658.
    • (2002) Biochem Soc Trans , vol.30 , pp. 653-658
    • Pitcher, R.S.1    Brittain, T.2    Watmough, N.J.3
  • 51
    • 35748976227 scopus 로고    scopus 로고
    • The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins
    • Garcia-Herrero A., Peacock R.S., Howard S.P., Vogel H.J. The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins. Mol Microbiol 2007, 66:872-889.
    • (2007) Mol Microbiol , vol.66 , pp. 872-889
    • Garcia-Herrero, A.1    Peacock, R.S.2    Howard, S.P.3    Vogel, H.J.4
  • 52
    • 46149094595 scopus 로고    scopus 로고
    • New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'?
    • Schauer K., Rodionov D.A., de Reuse H. New substrates for TonB-dependent transport: do we only see the 'tip of the iceberg'?. Trends Biochem Sci 2008, 33:330-338.
    • (2008) Trends Biochem Sci , vol.33 , pp. 330-338
    • Schauer, K.1    Rodionov, D.A.2    de Reuse, H.3
  • 53
    • 10744225021 scopus 로고    scopus 로고
    • The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli
    • Gimenez R., Nunez M.F., Badia J., Aguilar J., et al. The gene yjcG, cotranscribed with the gene acs, encodes an acetate permease in Escherichia coli. J Bacteriol 2003, 185:6448-6455.
    • (2003) J Bacteriol , vol.185 , pp. 6448-6455
    • Gimenez, R.1    Nunez, M.F.2    Badia, J.3    Aguilar, J.4
  • 54
    • 0037066717 scopus 로고    scopus 로고
    • Global expression profiling of acetate-grown Escherichia coli
    • Oh M.K., Rohlin L., Kao K.C., Liao J.C. Global expression profiling of acetate-grown Escherichia coli. J Biol Chem 2002, 277:13175-13183.
    • (2002) J Biol Chem , vol.277 , pp. 13175-13183
    • Oh, M.K.1    Rohlin, L.2    Kao, K.C.3    Liao, J.C.4
  • 55
    • 53449083335 scopus 로고    scopus 로고
    • Highly conserved genes in Geobacter species with expression patterns indicative of acetate limitation
    • Risso C., Methe B.A., Elifantz H., Holmes D.E., et al. Highly conserved genes in Geobacter species with expression patterns indicative of acetate limitation. Microbiol-Sgm 2008, 154:2589-2599.
    • (2008) Microbiol-Sgm , vol.154 , pp. 2589-2599
    • Risso, C.1    Methe, B.A.2    Elifantz, H.3    Holmes, D.E.4
  • 56
    • 75749119332 scopus 로고    scopus 로고
    • Acetate permease (ActP) is responsible for tellurite (TeO32-) uptake and resistance in cells of the facultative phototroph Rhodobacter capsulatus
    • Borghese R., Zannoni D. Acetate permease (ActP) is responsible for tellurite (TeO32-) uptake and resistance in cells of the facultative phototroph Rhodobacter capsulatus. Appl Environ Microbiol 2010, 76:942-944.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 942-944
    • Borghese, R.1    Zannoni, D.2
  • 57
    • 62149113666 scopus 로고    scopus 로고
    • Reconfiguring the quorum-sensing regulator SdiA of Escherichia coli to control biofilm formation via indole and N-acylhomoserine lactones
    • Lee J.T., Maeda T., Hong S.H., Wood T.K. Reconfiguring the quorum-sensing regulator SdiA of Escherichia coli to control biofilm formation via indole and N-acylhomoserine lactones. Appl Environ Microbiol 2009, 75:1703-1716.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 1703-1716
    • Lee, J.T.1    Maeda, T.2    Hong, S.H.3    Wood, T.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.