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Volumn 11, Issue 3, 2011, Pages 339-351

Quantitative protein expression and cell surface characteristics of Escherichia coli MG1655 biofilms

Author keywords

Biofilm; Electrophoretic mobility; Global proteomics; Infra red spectroscopy; ITRAQ ; Microbiology

Indexed keywords

ABC TRANSPORTER; BACTERIAL DNA; BACTERIOFERRITIN; CYTOCHROME B; ESCHERICHIA COLI PROTEIN; GLUTAMATE DECARBOXYLASE; HEAT SHOCK PROTEIN 70; PENTOSE PHOSPHATE; PEROXIREDOXIN; THIOREDOXIN PEROXIDASE; TRICARBOXYLIC ACID;

EID: 79251474723     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000386     Document Type: Article
Times cited : (21)

References (56)
  • 2
    • 67349266189 scopus 로고    scopus 로고
    • Cross-talk mechanisms in biofilm formation and responses to environmental and physiological stress in Escherichia coli
    • Landini, P., Cross-talk mechanisms in biofilm formation and responses to environmental and physiological stress in Escherichia coli. Res. Microbiol. 2009, 160, 259-266.
    • (2009) Res. Microbiol. , vol.160 , pp. 259-266
    • Landini, P.1
  • 3
    • 0037384574 scopus 로고    scopus 로고
    • Global gene expression in Escherichia coli biofilms
    • Schembri, M. A., Kjærgaard, K., Klemm, P., Global gene expression in Escherichia coli biofilms. Mol. Microbiol. 2003, 48, 253-267.
    • (2003) Mol. Microbiol. , vol.48 , pp. 253-267
    • Schembri, M.A.1    Kjærgaard, K.2    Klemm, P.3
  • 4
    • 58149250473 scopus 로고    scopus 로고
    • Insights on Escherichia coli biofilm formation and inhibition from whole-transcriptome profiling
    • Wood, T. K., Insights on Escherichia coli biofilm formation and inhibition from whole-transcriptome profiling. Environ. Microbiol. 2009, 11, 1-15.
    • (2009) Environ. Microbiol. , vol.11 , pp. 1-15
    • Wood, T.K.1
  • 5
    • 10744232444 scopus 로고    scopus 로고
    • Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression
    • Beloin, C., Valle, J., Latour-Lambert, P., Faure, P. et al., Global impact of mature biofilm lifestyle on Escherichia coli K-12 gene expression. Mol. Microbiol. 2004, 51, 659-674.
    • (2004) Mol. Microbiol. , vol.51 , pp. 659-674
    • Beloin, C.1    Valle, J.2    Latour-Lambert, P.3    Faure, P.4
  • 6
    • 33846104333 scopus 로고    scopus 로고
    • Temporal gene-expression in Escherichia coli K-12 biofilms
    • Domka, J., Lee, J., Bansal, T., Wood, T. K., Temporal gene-expression in Escherichia coli K-12 biofilms. Environ. Microbiol. 2007, 9, 332-346.
    • (2007) Environ. Microbiol. , vol.9 , pp. 332-346
    • Domka, J.1    Lee, J.2    Bansal, T.3    Wood, T.K.4
  • 7
    • 33747099865 scopus 로고    scopus 로고
    • Global analysis of candidate genes important for fitness in a competitive biofilm using DNA-array-based transposon mapping
    • Junker, L. M., Peters, J. E., Hay, A. G., Global analysis of candidate genes important for fitness in a competitive biofilm using DNA-array-based transposon mapping. Microbiology 2006, 152, 2233-2245.
    • (2006) Microbiology , vol.152 , pp. 2233-2245
    • Junker, L.M.1    Peters, J.E.2    Hay, A.G.3
  • 9
    • 0032870733 scopus 로고    scopus 로고
    • Abiotic surface sensing and biofilm-dependent regulation of gene expression in Escherichia coli
    • Prigent-Combaret, C., Vidal, O., Dorel, C., Lejeune, P., Abiotic surface sensing and biofilm-dependent regulation of gene expression in Escherichia coli. J. Bacteriol. 1999, 181, 5993-6002.
    • (1999) J. Bacteriol. , vol.181 , pp. 5993-6002
    • Prigent-Combaret, C.1    Vidal, O.2    Dorel, C.3    Lejeune, P.4
  • 10
    • 33645222919 scopus 로고    scopus 로고
    • Differentiation of outer membrane proteins from Salmonella enterica serotypes using Fourier transform infrared spectroscopy and chemometrics
    • Kim, S., Kim, H., Reuhs, B. L., Mauer, L. J., Differentiation of outer membrane proteins from Salmonella enterica serotypes using Fourier transform infrared spectroscopy and chemometrics. Lett. Appl. Microbiol. 2006, 42, 229-234.
    • (2006) Lett. Appl. Microbiol. , vol.42 , pp. 229-234
    • Kim, S.1    Kim, H.2    Reuhs, B.L.3    Mauer, L.J.4
  • 11
    • 33748109925 scopus 로고    scopus 로고
    • Proteomic analysis of Escherichia coli biofilms reveals the overexpression of the outer membrane protein OmpA
    • Orme, R., Douglas, C. W. I., Rimmer, S., Webb, M., Proteomic analysis of Escherichia coli biofilms reveals the overexpression of the outer membrane protein OmpA. Proteomics 2006, 6, 4269-4277.
    • (2006) Proteomics , vol.6 , pp. 4269-4277
    • Orme, R.1    Douglas, C.W.I.2    Rimmer, S.3    Webb, M.4
  • 12
    • 0037167481 scopus 로고    scopus 로고
    • A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode
    • Trémoulet, F., Duché, O., Namane, A., Martinie, B., Labadie, J.-C., A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode. FEMS Microbiol. Lett. 2002, 215, 7-14.
    • (2002) FEMS Microbiol. Lett. , vol.215 , pp. 7-14
    • Trémoulet, F.1    Duché, O.2    Namane, A.3    Martinie, B.4    Labadie, J.-C.5
  • 13
    • 58149383896 scopus 로고    scopus 로고
    • Impact of rpoS deletion on the proteome of Escherichia coli grown planktonically and as biofilm
    • Collet, A., Cosette, P., Beloin, C., Ghigo, J.-M. et al., Impact of rpoS deletion on the proteome of Escherichia coli grown planktonically and as biofilm. J. Proteome Res. 2008, 7, 4659-4669.
    • (2008) J. Proteome Res. , vol.7 , pp. 4659-4669
    • Collet, A.1    Cosette, P.2    Beloin, C.3    Ghigo, J.-M.4
  • 14
    • 0033534555 scopus 로고    scopus 로고
    • Surface characterization and on-line activity measurements of microorganisms by capillary zone electrophoresis
    • Torimura, M., Ito, S., Kano, K., Ikeda, T. et al., Surface characterization and on-line activity measurements of microorganisms by capillary zone electrophoresis. J. Chromatogr. B: Biomed. Sci. Appl. 1999, 721, 31-37.
    • (1999) J. Chromatogr. B: Biomed. Sci. Appl. , vol.721 , pp. 31-37
    • Torimura, M.1    Ito, S.2    Kano, K.3    Ikeda, T.4
  • 15
    • 29844436813 scopus 로고    scopus 로고
    • Role of nonadsorbing polymers in bacterial aggregation
    • Eboigbodin, K. E., Newton, J. R. A., Routh, A. F., Biggs, C. A., Role of nonadsorbing polymers in bacterial aggregation. Langmuir 2005, 21, 12315-12319.
    • (2005) Langmuir , vol.21 , pp. 12315-12319
    • Eboigbodin, K.E.1    Newton, J.R.A.2    Routh, A.F.3    Biggs, C.A.4
  • 16
    • 0042563255 scopus 로고    scopus 로고
    • Influence of growth phase on bacterial cell electrokinetic characteristics examined by soft particle electrophoresis theory
    • Hayashi, H., Seiki, H., Tsuneda, S., Hirata, A., Sasaki, H., Influence of growth phase on bacterial cell electrokinetic characteristics examined by soft particle electrophoresis theory. J. Colloid Interface Sci. 2003, 264, 565-568.
    • (2003) J. Colloid Interface Sci. , vol.264 , pp. 565-568
    • Hayashi, H.1    Seiki, H.2    Tsuneda, S.3    Hirata, A.4    Sasaki, H.5
  • 18
    • 44249128693 scopus 로고    scopus 로고
    • Electrostatic behavior of the charge-regulated bacterial cell surface
    • Hong, Y., Brown, D. G., Electrostatic behavior of the charge-regulated bacterial cell surface. Langmuir 2008, 24, 5003-5009.
    • (2008) Langmuir , vol.24 , pp. 5003-5009
    • Hong, Y.1    Brown, D.G.2
  • 19
    • 20444390064 scopus 로고    scopus 로고
    • Influence of growth phase on adhesion kinetics of Escherichia coli D21g
    • Walker, S., Hill, J. E., Redman, J. A., Elimelech, M., Influence of growth phase on adhesion kinetics of Escherichia coli D21g. Appl. Environ. Microbiol. 2005, 71, 3093-3099.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 3093-3099
    • Walker, S.1    Hill, J.E.2    Redman, J.A.3    Elimelech, M.4
  • 20
    • 34548598563 scopus 로고    scopus 로고
    • Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance
    • Lee, J., Page, R., García-Contreras, R., Palermino, J.-M. et al., Structure and function of the Escherichia coli protein YmgB: a protein critical for biofilm formation and acid-resistance. J. Mol. Biol. 2007, 373, 11-26.
    • (2007) J. Mol. Biol. , vol.373 , pp. 11-26
    • Lee, J.1    Page, R.2    García-Contreras, R.3    Palermino, J.-M.4
  • 21
    • 22444443683 scopus 로고    scopus 로고
    • Relevance of electrokinetic theory for "soft" particles to bacterial cells: implications for bacterial adhesion
    • de Kerchove, A. J., Elimelech, M., Relevance of electrokinetic theory for "soft" particles to bacterial cells: implications for bacterial adhesion. Langmuir 2005, 21, 6462-6472.
    • (2005) Langmuir , vol.21 , pp. 6462-6472
    • de Kerchove, A.J.1    Elimelech, M.2
  • 22
    • 4344598752 scopus 로고    scopus 로고
    • Infrared Spectroscopy in Microbiology
    • Wiley, Chichester.
    • Naumann, D., Infrared Spectroscopy in Microbiology. Wiley, Chichester 2000.
    • (2000)
    • Naumann, D.1
  • 23
    • 39749105880 scopus 로고    scopus 로고
    • Characterization of the extracellular polymeric substances produced by Escherichia coli using infrared spectroscopic, proteomic, and aggregation studies
    • Eboigbodin, K. E., Biggs, C. A., Characterization of the extracellular polymeric substances produced by Escherichia coli using infrared spectroscopic, proteomic, and aggregation studies. Biomacromolecules 2008, 9, 686-695.
    • (2008) Biomacromolecules , vol.9 , pp. 686-695
    • Eboigbodin, K.E.1    Biggs, C.A.2
  • 24
    • 33646570847 scopus 로고    scopus 로고
    • Isobaric Tags for Relative and Absolute Quantitation (iTRAQ) reproducibility: implication of multiple injections
    • Chong, P. K., Gan, C. S., Pham, T. K., Wright, P. C., Isobaric Tags for Relative and Absolute Quantitation (iTRAQ) reproducibility: implication of multiple injections. J. Proteome Res. 2006, 5, 1232-1240.
    • (2006) J. Proteome Res. , vol.5 , pp. 1232-1240
    • Chong, P.K.1    Gan, C.S.2    Pham, T.K.3    Wright, P.C.4
  • 25
    • 60849087991 scopus 로고    scopus 로고
    • 2 fixation in Nostoc punctiforme ATCC 29133 through cellular enrichments and iTRAQ shotgun proteomics
    • 2 fixation in Nostoc punctiforme ATCC 29133 through cellular enrichments and iTRAQ shotgun proteomics. J. Proteome Res. 2009, 8, 187-198.
    • (2009) J. Proteome Res. , vol.8 , pp. 187-198
    • Ow, S.Y.1    Noirel, J.2    Cardona, T.3    Taton, A.4
  • 26
    • 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
  • 27
    • 33847340190 scopus 로고    scopus 로고
    • Technical, experimental, and biological variations in Isobaric Tags for Relative and Absolute Quantitation (iTRAQ)
    • Gan, C. S., Chong, P. K., Pham, T. K., Wright, P. C., Technical, experimental, and biological variations in Isobaric Tags for Relative and Absolute Quantitation (iTRAQ). J. Proteome Res. 2007, 6, 821-827.
    • (2007) J. Proteome Res. , vol.6 , pp. 821-827
    • Gan, C.S.1    Chong, P.K.2    Pham, T.K.3    Wright, P.C.4
  • 28
    • 56649116091 scopus 로고    scopus 로고
    • Identifying differentially expressed subnetworks with MMG
    • Noirel, J., Sanguinetti, G., Wright, P. C., Identifying differentially expressed subnetworks with MMG. Bioinformatics 2008, 24, 2792-2793.
    • (2008) Bioinformatics , vol.24 , pp. 2792-2793
    • Noirel, J.1    Sanguinetti, G.2    Wright, P.C.3
  • 29
    • 41949107946 scopus 로고    scopus 로고
    • MMG: a probabilistic tool to identify submodules of metabolic pathways
    • Sanguinetti, G., Noirel, J., Wright, P. C., MMG: a probabilistic tool to identify submodules of metabolic pathways. Bioinformatics 2008, 24, 1078-1084.
    • (2008) Bioinformatics , vol.24 , pp. 1078-1084
    • Sanguinetti, G.1    Noirel, J.2    Wright, P.C.3
  • 30
    • 33845268007 scopus 로고    scopus 로고
    • Protein expression in Escherichia coli S17-1 biofilms: impact of indole
    • Collet, A., Vilain, S., Cosette, P., Junter, G. et al., Protein expression in Escherichia coli S17-1 biofilms: impact of indole. Antonie van Leeuwenhoek 2007, 91, 71-85.
    • (2007) Antonie van Leeuwenhoek , vol.91 , pp. 71-85
    • Collet, A.1    Vilain, S.2    Cosette, P.3    Junter, G.4
  • 31
    • 20444428661 scopus 로고    scopus 로고
    • Role of bacterial cell surface structures in Escherichia coli biofilm formation
    • Van Houdt, R., Michiels, C. W., Role of bacterial cell surface structures in Escherichia coli biofilm formation. Res. Microbiol. 2005, 156, 626-633.
    • (2005) Res. Microbiol. , vol.156 , pp. 626-633
    • Van Houdt, R.1    Michiels, C.W.2
  • 32
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T. et al., The complete genome sequence of Escherichia coli K-12. Science 1997, 277, 1453-1462.
    • (1997) Science , vol.277 , pp. 1453-1462
    • Blattner, F.R.1    Plunkett 3rd, G.2    Bloch, C.A.3    Perna, N.T.4
  • 33
    • 34250658490 scopus 로고    scopus 로고
    • Investigating the surface properties of Escherichia coli under glucose controlled conditions and its effect on aggregation
    • Eboigbodin, K. E., Ojeda, J. J., Biggs, C. A., Investigating the surface properties of Escherichia coli under glucose controlled conditions and its effect on aggregation. Langmuir 2007, 23, 6691-6697.
    • (2007) Langmuir , vol.23 , pp. 6691-6697
    • Eboigbodin, K.E.1    Ojeda, J.J.2    Biggs, C.A.3
  • 35
    • 0002105768 scopus 로고
    • Relative Importance of Surface Free Energy as a Measure of Hydrophobicity in Bacterial Adhesion to Solid Surfaces
    • American Society for Microbiology, Washington, DC.
    • Busscher, H., Sjollema, J., van der Mei, H., Relative Importance of Surface Free Energy as a Measure of Hydrophobicity in Bacterial Adhesion to Solid Surfaces, American Society for Microbiology, Washington, DC 1990.
    • (1990)
    • Busscher, H.1    Sjollema, J.2    van der Mei, H.3
  • 36
    • 33645221151 scopus 로고    scopus 로고
    • Influence of culture heterogeneity in cell surface charge on adhesion and biofilm formation by Enterococcus faecalis
    • van Merode, A. E. J., van der Mei, H. C., Busscher, H. J., Krom, B. P., Influence of culture heterogeneity in cell surface charge on adhesion and biofilm formation by Enterococcus faecalis. J. Bacteriol. 2006, 188, 2421-2426.
    • (2006) J. Bacteriol. , vol.188 , pp. 2421-2426
    • van Merode, A.E.J.1    van der Mei, H.C.2    Busscher, H.J.3    Krom, B.P.4
  • 37
    • 5344261722 scopus 로고    scopus 로고
    • Significance of cell electrokinetic properties determined by soft-particle analysis in bacterial adhesion onto a solid surface
    • Tsuneda, S., Aikawa, H., Hayashi, H., Hirata, A., Significance of cell electrokinetic properties determined by soft-particle analysis in bacterial adhesion onto a solid surface. J. Colloid Interface Sci. 2004, 279, 410-417.
    • (2004) J. Colloid Interface Sci. , vol.279 , pp. 410-417
    • Tsuneda, S.1    Aikawa, H.2    Hayashi, H.3    Hirata, A.4
  • 38
    • 33746344334 scopus 로고    scopus 로고
    • Characterization of Bordetella pertussis growing as biofilm by chemical analysis and FT-IR spectroscopy
    • Bosch, A., Serra, D., Prieto, C., Schmitt, J. et al., Characterization of Bordetella pertussis growing as biofilm by chemical analysis and FT-IR spectroscopy. Appl. Microbiol. Biotechnol. 2006, 71, 736-747.
    • (2006) Appl. Microbiol. Biotechnol. , vol.71 , pp. 736-747
    • Bosch, A.1    Serra, D.2    Prieto, C.3    Schmitt, J.4
  • 39
    • 42449147502 scopus 로고    scopus 로고
    • Characterization of the cell surface and cell wall chemistry of drinking water bacteria by combining XPS, FTIR spectroscopy, modeling, and potentiometric titrations
    • Ojeda, J. J., Romero-Gonzalez, M. E., Bachmann, R. T., Edyvean, R. G., Banwart, S. A., Characterization of the cell surface and cell wall chemistry of drinking water bacteria by combining XPS, FTIR spectroscopy, modeling, and potentiometric titrations. Langmuir 2008, 24, 4032-4040.
    • (2008) Langmuir , vol.24 , pp. 4032-4040
    • Ojeda, J.J.1    Romero-Gonzalez, M.E.2    Bachmann, R.T.3    Edyvean, R.G.4    Banwart, S.A.5
  • 40
    • 73749085045 scopus 로고    scopus 로고
    • Analysis of changes in attenuated total reflection FTIR fingerprints of Pseudomonas fluorescens from planktonic state to nascent biofilm state
    • Quilès, F., Humbert, F., Delille, A., Analysis of changes in attenuated total reflection FTIR fingerprints of Pseudomonas fluorescens from planktonic state to nascent biofilm state. Spectrochim. Acta Part A: Mol. Biomol. Spectrosc. 2010, 75, 610-616.
    • (2010) Spectrochim. Acta Part A: Mol. Biomol. Spectrosc. , vol.75 , pp. 610-616
    • Quilès, F.1    Humbert, F.2    Delille, A.3
  • 41
    • 0000669882 scopus 로고    scopus 로고
    • FTIR spectroscopy applied to bacterial cells as a novel method for monitoring complex biotechnological processes
    • Schuster, K. C., Mertens, F., Gapes, J. R., FTIR spectroscopy applied to bacterial cells as a novel method for monitoring complex biotechnological processes. Vib. Spectrosc. 1999, 19, 467-477.
    • (1999) Vib. Spectrosc. , vol.19 , pp. 467-477
    • Schuster, K.C.1    Mertens, F.2    Gapes, J.R.3
  • 42
    • 57649170771 scopus 로고    scopus 로고
    • Proteome approaches combined with Fourier transform infrared spectroscopy revealed a distinctive biofilm physiology in Bordetella pertussis
    • Serra, D. O., Lücking, G., Weiland, F., Schulz, S. et al., Proteome approaches combined with Fourier transform infrared spectroscopy revealed a distinctive biofilm physiology in Bordetella pertussis. Proteomics 2008, 8, 4995-5010.
    • (2008) Proteomics , vol.8 , pp. 4995-5010
    • Serra, D.O.1    Lücking, G.2    Weiland, F.3    Schulz, S.4
  • 43
    • 68049089931 scopus 로고    scopus 로고
    • Analysis of bacteria on steel surfaces using reflectance micro-Fourier transform infrared spectroscopy
    • Ojeda, J. J., Romero-Gonzalez, M. E., Banwart, S. A., Analysis of bacteria on steel surfaces using reflectance micro-Fourier transform infrared spectroscopy. Anal. Chem. 2009, 81, 6467-6473.
    • (2009) Anal. Chem. , vol.81 , pp. 6467-6473
    • Ojeda, J.J.1    Romero-Gonzalez, M.E.2    Banwart, S.A.3
  • 44
    • 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, C. W. 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, C.W.I.4
  • 46
    • 39249084651 scopus 로고    scopus 로고
    • RpoS regulation of gene expression during exponential growth of Escherichia coli K12
    • Dong, T., Kirchhof, M., Schellhorn, H., RpoS regulation of gene expression during exponential growth of Escherichia coli K12. Mol. Genet. Genomics 2008, 279, 267-277.
    • (2008) Mol. Genet. Genomics , vol.279 , pp. 267-277
    • Dong, T.1    Kirchhof, M.2    Schellhorn, H.3
  • 47
    • 27144443126 scopus 로고    scopus 로고
    • Regulation of type 1 fimbriae synthesis and biofilm formation by the transcriptional regulator LrhA of Escherichia coli
    • Blumer, C., Kleefeld, A., Lehnen, D., Heintz, M. et al., Regulation of type 1 fimbriae synthesis and biofilm formation by the transcriptional regulator LrhA of Escherichia coli. Microbiology 2005, 151, 3287-3298.
    • (2005) Microbiology , vol.151 , pp. 3287-3298
    • Blumer, C.1    Kleefeld, A.2    Lehnen, D.3    Heintz, M.4
  • 48
    • 17044362306 scopus 로고    scopus 로고
    • Proteomics of Shewanella oneidensis MR-1 biofilm reveals differentially expressed proteins, including AggA and RibB
    • Vriendt, K. D., Theunissen, S., Carpentier, W., Smet, L. D. et al., Proteomics of Shewanella oneidensis MR-1 biofilm reveals differentially expressed proteins, including AggA and RibB. Proteomics 2005, 5, 1308-1316.
    • (2005) Proteomics , vol.5 , pp. 1308-1316
    • Vriendt, K.D.1    Theunissen, S.2    Carpentier, W.3    Smet, L.D.4
  • 49
    • 46649106145 scopus 로고    scopus 로고
    • Solubilization of Protein aggregates by the acid stress chaperones HdeA and HdeB
    • Malki, A., Le, H.-T., Milles, S., Kern, R. et al., Solubilization of Protein aggregates by the acid stress chaperones HdeA and HdeB. J. Biol. Chem. 2008, 283, 13679-13687.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13679-13687
    • Malki, A.1    Le, H.-T.2    Milles, S.3    Kern, R.4
  • 50
    • 33744456996 scopus 로고    scopus 로고
    • Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31
    • Mujacic, M., Baneyx, F., Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31. Mol. Microbiol. 2006, 60, 1576-1589.
    • (2006) Mol. Microbiol. , vol.60 , pp. 1576-1589
    • Mujacic, M.1    Baneyx, F.2
  • 51
    • 0026443939 scopus 로고
    • Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12
    • Hopkin, K. A., Papazian, M. A., Steinman, H. M., Functional differences between manganese and iron superoxide dismutases in Escherichia coli K-12. J. Biol. Chem. 1992, 267, 24253-24258.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24253-24258
    • Hopkin, K.A.1    Papazian, M.A.2    Steinman, H.M.3
  • 53
    • 33846805492 scopus 로고    scopus 로고
    • Global gene expression profiling of asymptomatic Bacteriuria Escherichia coli during biofilm growth in human urine
    • Hancock, V., Klemm, P., Global gene expression profiling of asymptomatic Bacteriuria Escherichia coli during biofilm growth in human urine. Infect. Immun. 2007, 75, 966-976.
    • (2007) Infect. Immun. , vol.75 , pp. 966-976
    • Hancock, V.1    Klemm, P.2
  • 54
    • 0033823598 scopus 로고    scopus 로고
    • Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157:H7
    • Choi, S. H., Baumler, D. J., Kaspar, C. W., Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157:H7. Appl. Environ. Microbiol. 2000, 66, 3911-3916.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3911-3916
    • Choi, S.H.1    Baumler, D.J.2    Kaspar, C.W.3
  • 55
    • 77954359815 scopus 로고    scopus 로고
    • Nuclear proteome dynamics in differentiating embryonic carcinoma (NTERA-2) cells
    • Pewsey, E., Bruce, C., Tonge, P., Evans, C. et al., Nuclear proteome dynamics in differentiating embryonic carcinoma (NTERA-2) cells. J. Proteome Res. 2010, 9, 3412-3426.
    • (2010) J. Proteome Res. , vol.9 , pp. 3412-3426
    • Pewsey, E.1    Bruce, C.2    Tonge, P.3    Evans, C.4


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