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Volumn 8, Issue 8, 2008, Pages 1645-1660

Application of 16O/18O reverse proteolytic labeling to determine the effect of biofilm culture on the cell envelope proteome of Porphyromonas gingivalis W50

Author keywords

18O; Biofilm; Comparative proteomics; Planktonic; Porphyromonas gingivalis

Indexed keywords

BACTERIAL PROTEIN; FRDAB ENZYME; OXYGEN; OXYGEN 18; PROTEIN CPG70; PROTEIN HAGA; PROTEIN HMUY; PROTEIN IHTB; PROTEIN PG99; PROTEIN RGPA; PROTEIN W50; PROTEOME; TRYPSIN; UNCLASSIFIED DRUG;

EID: 42549084285     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700557     Document Type: Article
Times cited : (47)

References (67)
  • 2
    • 0033583045 scopus 로고    scopus 로고
    • Forging a link between biofilms and disease
    • Potera, C., Forging a link between biofilms and disease. Science 1999, 283, 1837-1839.
    • (1999) Science , vol.283 , pp. 1837-1839
    • Potera, C.1
  • 3
    • 0024232979 scopus 로고
    • Antibody response to Pseudomonas aeruginosa surface protein antigens in a rat model of chronic lung infection
    • Cochrane, D. M., Brown, M. R., Anwar, H., Weller, P. H. et al., Antibody response to Pseudomonas aeruginosa surface protein antigens in a rat model of chronic lung infection. J. Med. Microbiol. 1988, 27, 255-261.
    • (1988) J. Med. Microbiol , vol.27 , pp. 255-261
    • Cochrane, D.M.1    Brown, M.R.2    Anwar, H.3    Weller, P.H.4
  • 4
    • 0020085314 scopus 로고
    • Virulence of black-pigmented Bacteroides strains from periodontal pockets and other sites in experimentally induced skin lesions in mice
    • van Steenbergen, T. J., Kastelein, P., Touw, J. J., de Graaff, J., Virulence of black-pigmented Bacteroides strains from periodontal pockets and other sites in experimentally induced skin lesions in mice. J. Periodontal Res. 1982, 17, 41-49.
    • (1982) J. Periodontal Res , vol.17 , pp. 41-49
    • van Steenbergen, T.J.1    Kastelein, P.2    Touw, J.J.3    de Graaff, J.4
  • 5
    • 0024353087 scopus 로고
    • Heterogeneity of virulence among strains of Bacteroides gingivalis
    • Neiders, M. E., Chen, P. B., Suido, H., Reynolds, H. S. et al., Heterogeneity of virulence among strains of Bacteroides gingivalis. J. Periodontal Res. 1989, 24, 192-198.
    • (1989) J. Periodontal Res , vol.24 , pp. 192-198
    • Neiders, M.E.1    Chen, P.B.2    Suido, H.3    Reynolds, H.S.4
  • 7
    • 33747861527 scopus 로고    scopus 로고
    • Techniques for the growth of Porphyromonas gingivalis biofilms
    • Davey, M. E., Techniques for the growth of Porphyromonas gingivalis biofilms. Periodontol. 2000 2006, 42, 27-35.
    • (2006) Periodontol. 2000 , vol.42 , pp. 27-35
    • Davey, M.E.1
  • 8
    • 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., 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.2    Rimmer, S.3    Webb, M.4
  • 9
    • 0036157549 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm
    • Sauer, K., Camper, A. K., Ehrlich, G. D., Costerton, J. W., Davies, D. G., Pseudomonas aeruginosa displays multiple phenotypes during development as a biofilm. J. Bacteriol. 2002, 184, 1140-1154.
    • (2002) J. Bacteriol , vol.184 , pp. 1140-1154
    • Sauer, K.1    Camper, A.K.2    Ehrlich, G.D.3    Costerton, J.W.4    Davies, D.G.5
  • 10
    • 13244252298 scopus 로고    scopus 로고
    • Differential protein expression by Porphyromonas gingivalis in response to secreted epithelial cell components
    • Zhang, Y., Wang, T., Chen, W., Yilmaz, O. et al., Differential protein expression by Porphyromonas gingivalis in response to secreted epithelial cell components. Proteomics 2005, 5, 198-211.
    • (2005) Proteomics , vol.5 , pp. 198-211
    • Zhang, Y.1    Wang, T.2    Chen, W.3    Yilmaz, O.4
  • 11
    • 31344481247 scopus 로고    scopus 로고
    • Proteomics-based analysis of a counter-oxidative stress system in Porphyromonas gingivalis
    • Okano, S., Shibata, Y., Shiroza, T., Abiko, Y., Proteomics-based analysis of a counter-oxidative stress system in Porphyromonas gingivalis. Proteomics 2006, 6, 251-258.
    • (2006) Proteomics , vol.6 , pp. 251-258
    • Okano, S.1    Shibata, Y.2    Shiroza, T.3    Abiko, Y.4
  • 12
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., Mann, M., Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 2005, 1, 252-262.
    • (2005) Nat. Chem. Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 13
    • 0007533116 scopus 로고
    • The kinetics of the chymo-trypsin-catalyzed oxygen exchange of carboxylic acids
    • Bender, M. L., Kemp, K. C., The kinetics of the chymo-trypsin-catalyzed oxygen exchange of carboxylic acids. J. Am. Chem. Soc. 1957, 79, 116.
    • (1957) J. Am. Chem. Soc , vol.79 , pp. 116
    • Bender, M.L.1    Kemp, K.C.2
  • 14
    • 0030068923 scopus 로고    scopus 로고
    • 18O into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry
    • 18O into peptide fragments and its application for protein sequencing by electrospray and matrix-assisted laser desorption/ionization mass spectrometry. Electrophoresis 1996, 17, 945-953.
    • (1996) Electrophoresis , vol.17 , pp. 945-953
    • Schnolzer, M.1    Jedrzejewski, P.2    Lehmann, W.D.3
  • 15
    • 0035384687 scopus 로고    scopus 로고
    • 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • 18O labeling for comparative proteomics: model studies with two serotypes of adenovirus. Anal. Chem. 2001, 73, 2836-2842.
    • (2001) Anal. Chem , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 16
    • 20244374564 scopus 로고    scopus 로고
    • Quantitative profiling of the detergent-resistant membrane proteome of iota-b toxin induced vero cells
    • Blonder, J., Hale, M. L., Chan, K. C., Yu, L. R. et al., Quantitative profiling of the detergent-resistant membrane proteome of iota-b toxin induced vero cells. J. Proteome Res 2005, 4, 523-531.
    • (2005) J. Proteome Res , vol.4 , pp. 523-531
    • Blonder, J.1    Hale, M.L.2    Chan, K.C.3    Yu, L.R.4
  • 18
    • 0033106490 scopus 로고    scopus 로고
    • 18O-labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching
    • 18O-labeling of N-glycosylation sites to improve the identification of gel-separated glycoproteins using peptide mass mapping and database searching. Anal. Chem. 1999, 71, 1431-1440.
    • (1999) Anal. Chem , vol.71 , pp. 1431-1440
    • Kuster, B.1    Mann, M.2
  • 20
    • 0030960366 scopus 로고    scopus 로고
    • Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko, A., Chernushevich, I., Ens, W., Standing, K. G. et al., Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom. 1997, 11, 1015-1024.
    • (1997) Rapid Commun. Mass Spectrom , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Ens, W.3    Standing, K.G.4
  • 21
    • 25844524834 scopus 로고    scopus 로고
    • Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC
    • Gevaert, K., Staes, A., Van Damme, J., De Groot, S. et al., Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics 2005, 5, 3589-3599.
    • (2005) Proteomics , vol.5 , pp. 3589-3599
    • Gevaert, K.1    Staes, A.2    Van Damme, J.3    De Groot, S.4
  • 22
    • 0022493331 scopus 로고
    • Biofilm thickness measurements by light microscopy
    • Bakke, R., Olsson, P. Q., Biofilm thickness measurements by light microscopy. J. Microbiol. Methods 1986, 5, 93-98.
    • (1986) J. Microbiol. Methods , vol.5 , pp. 93-98
    • Bakke, R.1    Olsson, P.Q.2
  • 23
    • 0033764531 scopus 로고    scopus 로고
    • Quantification of biofilm structures by the novel computer program COMSTAT
    • Heydorn, A., Nielsen, A. T., Hentzer, M., Sternberg, C. et al., Quantification of biofilm structures by the novel computer program COMSTAT. Microbiology 2000, 146, 2395-2407.
    • (2000) Microbiology , vol.146 , pp. 2395-2407
    • Heydorn, A.1    Nielsen, A.T.2    Hentzer, M.3    Sternberg, C.4
  • 24
    • 0034978867 scopus 로고    scopus 로고
    • Sodium ion-driven serine/threonine transport in Porphyromonas gingivalis
    • Dashper, S. G., Brownfield, L., Slakeski, N., Zilm, P. S. et al., Sodium ion-driven serine/threonine transport in Porphyromonas gingivalis. J. Bacteriol. 2001, 183, 4142-4148.
    • (2001) J. Bacteriol , vol.183 , pp. 4142-4148
    • Dashper, S.G.1    Brownfield, L.2    Slakeski, N.3    Zilm, P.S.4
  • 25
    • 0036533761 scopus 로고    scopus 로고
    • Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50
    • Veith, P. D., Talbo, G. H., Slakeski, N., Dashper, S. G. et al., Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50. Biochem. J. 2002, 363, 105-115.
    • (2002) Biochem. J , vol.363 , pp. 105-115
    • Veith, P.D.1    Talbo, G.H.2    Slakeski, N.3    Dashper, S.G.4
  • 26
    • 13244262721 scopus 로고    scopus 로고
    • 18O-labeling quantitative proteomics using an ion trap mass spectrometer
    • 18O-labeling quantitative proteomics using an ion trap mass spectrometer. Proteomics 2005, 5, 16-23.
    • (2005) Proteomics , vol.5 , pp. 16-23
    • Sakai, J.1    Kojima, S.2    Yanagi, K.3    Kanaoka, M.4
  • 28
    • 14844360847 scopus 로고    scopus 로고
    • The human proteome
    • Probability-based evaluation of peptide and protein identifications from tandem mass spectrometry and SEQUEST analysis
    • Qian, W. J., Liu, T., Monroe, M. E., Strittmatter, E. F. et al., Probability-based evaluation of peptide and protein identifications from tandem mass spectrometry and SEQUEST analysis:The human proteome. J. Proteome Res. 2005, 4, 53-62.
    • (2005) J. Proteome Res , vol.4 , pp. 53-62
    • Qian, W.J.1    Liu, T.2    Monroe, M.E.3    Strittmatter, E.F.4
  • 29
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., Cottrell, J. S., Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 31
    • 33646927488 scopus 로고    scopus 로고
    • Quantitative proteomics of the archaeon Methanococcus maripaludis validated by microarray analysis and real time PCR
    • Xia, Q., Hendrickson, E. L., Zhang, Y., Wang, T. et al., Quantitative proteomics of the archaeon Methanococcus maripaludis validated by microarray analysis and real time PCR. Mol. Cell. Proteomics2006, 5, 868-881.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 868-881
    • Xia, Q.1    Hendrickson, E.L.2    Zhang, Y.3    Wang, T.4
  • 32
    • 0035375137 scopus 로고    scopus 로고
    • Computational analysis of microarray data
    • Quackenbush, J., Computational analysis of microarray data. Nat. Rev. Genet. 2001, 2, 418-427.
    • (2001) Nat. Rev. Genet , vol.2 , pp. 418-427
    • Quackenbush, J.1
  • 33
    • 33746218840 scopus 로고    scopus 로고
    • Prediction of protein subcellular localization
    • Yu, C. S., Chen, Y. C., Lu, C. H., Hwang, J. K., Prediction of protein subcellular localization. Proteins 2006, 64, 643-651.
    • (2006) Proteins , vol.64 , pp. 643-651
    • Yu, C.S.1    Chen, Y.C.2    Lu, C.H.3    Hwang, J.K.4
  • 35
    • 4444271864 scopus 로고    scopus 로고
    • Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18
    • Staes, A., Demol, H., Van Damme, J., Martens, L. et al., Global differential non-gel proteomics by quantitative and stable labeling of tryptic peptides with oxygen-18. J. Proteome Res. 2004, 3, 786-791.
    • (2004) J. Proteome Res , vol.3 , pp. 786-791
    • Staes, A.1    Demol, H.2    Van Damme, J.3    Martens, L.4
  • 37
    • 1042284932 scopus 로고    scopus 로고
    • Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: The yeast salinity stress response
    • Li, J., Steen, H., Gygi, S. P., Protein profiling with cleavable isotope-coded affinity tag (cICAT) reagents: the yeast salinity stress response. Mol. Cell. Proteomics 2003, 2, 1198-1204.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1198-1204
    • Li, J.1    Steen, H.2    Gygi, S.P.3
  • 38
    • 29144470147 scopus 로고    scopus 로고
    • Two-dimensional fluorescence difference gel electrophoretic analysis of Streptococcus mutans biofilms
    • Rathsam, C., Eaton, R. E., Simpson, C. L., Browne, G. V. et al., Two-dimensional fluorescence difference gel electrophoretic analysis of Streptococcus mutans biofilms. J. Proteome Res. 2005, 4, 2161-2173.
    • (2005) J. Proteome Res , vol.4 , pp. 2161-2173
    • Rathsam, C.1    Eaton, R.E.2    Simpson, C.L.3    Browne, G.V.4
  • 39
    • 0022635403 scopus 로고
    • Effect of hemin on the physiology and virulence of Bacteroides gingivalis W50
    • McKee, A. S., McDermid, A. S., Baskerville, A., Dowsett, A. B. et al., Effect of hemin on the physiology and virulence of Bacteroides gingivalis W50. Infect. Immun. 1986, 52, 349-355.
    • (1986) Infect. Immun , vol.52 , pp. 349-355
    • McKee, A.S.1    McDermid, A.S.2    Baskerville, A.3    Dowsett, A.B.4
  • 40
    • 23044493465 scopus 로고    scopus 로고
    • A novel Porphyromonas gingivalis FeoB plays a role in manganese accumulation
    • Dashper, S. G., Butler, C. A., Lissel, J. P., Paolini, R. A. et al., A novel Porphyromonas gingivalis FeoB plays a role in manganese accumulation. J. Biol. Chem. 2005, 280, 28095-28102.
    • (2005) J. Biol. Chem , vol.280 , pp. 28095-28102
    • Dashper, S.G.1    Butler, C.A.2    Lissel, J.P.3    Paolini, R.A.4
  • 41
    • 27144469038 scopus 로고    scopus 로고
    • Continuous culture-making a comeback?
    • Hoskisson, P. A., Hobbs, G., Continuous culture-making a comeback? Microbiology 2005, 151, 3153-3159.
    • (2005) Microbiology , vol.151 , pp. 3153-3159
    • Hoskisson, P.A.1    Hobbs, G.2
  • 42
    • 33845450679 scopus 로고    scopus 로고
    • Global comparison of the membrane subproteomes between a multidrug-resistant Acinetobacter baumannii strain and a reference strain
    • Siroy, A., Cosette, P., Seyer, D., Lemaitre-Guillier, C. et al., Global comparison of the membrane subproteomes between a multidrug-resistant Acinetobacter baumannii strain and a reference strain. J. Proteome Res.2006, 5, 3385-3398.
    • (2006) J. Proteome Res , vol.5 , pp. 3385-3398
    • Siroy, A.1    Cosette, P.2    Seyer, D.3    Lemaitre-Guillier, C.4
  • 45
    • 33751396690 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of detergent-resistant membranes from chemical synapses: Evidence for cholesterol as spatial organizer of synaptic vesicle cycling
    • Jia, J. Y., Lamer, S., Schumann, M., Schmidt, M. R. et al., Quantitative proteomics analysis of detergent-resistant membranes from chemical synapses: Evidence for cholesterol as spatial organizer of synaptic vesicle cycling. Mol. Cell. Proteomics 2006, 5, 2060-2071.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2060-2071
    • Jia, J.Y.1    Lamer, S.2    Schumann, M.3    Schmidt, M.R.4
  • 48
    • 11544375741 scopus 로고    scopus 로고
    • Ion formation in MALDI mass spectrometry
    • Zenobi, R., Knochenmuss, R., Ion formation in MALDI mass spectrometry. Mass Spectrom. Rev. 1998, 17, 337-366.
    • (1998) Mass Spectrom. Rev , vol.17 , pp. 337-366
    • Zenobi, R.1    Knochenmuss, R.2
  • 49
    • 33749023323 scopus 로고    scopus 로고
    • The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis
    • Seers, C. A., Slakeski, N., Veith, P. D., Nikolof, T. et al., The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis. J. Bacteriol. 2006, 188, 6376-6386.
    • (2006) J. Bacteriol , vol.188 , pp. 6376-6386
    • Seers, C.A.1    Slakeski, N.2    Veith, P.D.3    Nikolof, T.4
  • 50
    • 0035192014 scopus 로고    scopus 로고
    • Role of RgpA, RgpB, and Kgp proteinases in virulence of Porphyromonas gingivalis W50 in a murine lesion model
    • O'Brien-Simpson, N. M., Paolini, R. A., Hoffmann, B., Slakeski, N. et al., Role of RgpA, RgpB, and Kgp proteinases in virulence of Porphyromonas gingivalis W50 in a murine lesion model. Infect. Immun. 2001, 69, 7527-7534.
    • (2001) Infect. Immun , vol.69 , pp. 7527-7534
    • O'Brien-Simpson, N.M.1    Paolini, R.A.2    Hoffmann, B.3    Slakeski, N.4
  • 52
    • 0028942506 scopus 로고
    • The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain
    • Potempa, J., Pike, R., Travis, J., The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain. Infect. Immun. 1995, 63, 1176-1182.
    • (1995) Infect. Immun , vol.63 , pp. 1176-1182
    • Potempa, J.1    Pike, R.2    Travis, J.3
  • 53
    • 33847747459 scopus 로고    scopus 로고
    • but Not RgpA, are important for Porphyromonas gingivalis virulence in the murine periodontitis model
    • Pathirana, R. D., O'Brien-Simpson, N. M., Brammar, G. C., Slakeski, N., Reynolds, E. C., Kgp and RgpB, but Not RgpA, are important for Porphyromonas gingivalis virulence in the murine periodontitis model. Infect. Immun. 2007, 75, 1436-1442.
    • (2007) Infect. Immun , vol.75 , pp. 1436-1442
    • Pathirana, R.D.1    Simpson, O.2    Brammar, N.M.3    Slakeski, G.C.4    Reynolds, N.5    Kgp, E.C.6    RgpB7
  • 54
    • 0037189490 scopus 로고    scopus 로고
    • CPG70 is a novel basic metallocarboxypeptidase with C-terminal polycystic kidney disease domains from Porphyromonas gingivalis
    • Chen, Y. Y., Cross, K. J., Paolini, R. A., Fielding, J. E. et al., CPG70 is a novel basic metallocarboxypeptidase with C-terminal polycystic kidney disease domains from Porphyromonas gingivalis. J. Biol. Chem. 2002, 277, 23433-23440.
    • (2002) J. Biol. Chem , vol.277 , pp. 23433-23440
    • Chen, Y.Y.1    Cross, K.J.2    Paolini, R.A.3    Fielding, J.E.4
  • 55
    • 20144366153 scopus 로고    scopus 로고
    • Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis
    • Sato, K., Sakai, E., Veith, P. D., Shoji, M. et al., Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis. J. Biol. Chem. 2005, 280, 8668-8677.
    • (2005) J. Biol. Chem , vol.280 , pp. 8668-8677
    • Sato, K.1    Sakai, E.2    Veith, P.D.3    Shoji, M.4
  • 56
    • 33846604620 scopus 로고    scopus 로고
    • Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-Negative bacteria?
    • Nguyen, K. A., Travis, J., Potempa, J., Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-Negative bacteria? J. Bacteriol. 2007, 189, 833-843.
    • (2007) J. Bacteriol , vol.189 , pp. 833-843
    • Nguyen, K.A.1    Travis, J.2    Potempa, J.3
  • 58
    • 33750933470 scopus 로고    scopus 로고
    • Transcriptional organization, regulation and role of the Porphyr omonas gingivalis W83 hmu haemin-uptake locus
    • Lewis, J. P., Plata, K., Yu, F., Rosato, A., Anaya, C., Transcriptional organization, regulation and role of the Porphyr omonas gingivalis W83 hmu haemin-uptake locus. Microbiology 2006, 152, 3367-3382.
    • (2006) Microbiology , vol.152 , pp. 3367-3382
    • Lewis, J.P.1    Plata, K.2    Yu, F.3    Rosato, A.4    Anaya, C.5
  • 59
    • 33748787409 scopus 로고    scopus 로고
    • Purification and initial characterization of a novel Porphyromonas gingivalis HmuY protein expressed in Escherichia coli and insect cells
    • Olczak, T., Siudeja, K., Olczak, M., Purification and initial characterization of a novel Porphyromonas gingivalis HmuY protein expressed in Escherichia coli and insect cells. Protein Expr. Purif. 2006, 49, 299-306.
    • (2006) Protein Expr. Purif , vol.49 , pp. 299-306
    • Olczak, T.1    Siudeja, K.2    Olczak, M.3
  • 60
    • 0034025391 scopus 로고    scopus 로고
    • Ferritin from the obligate anaerobe Porphyromonas gingivalis: Purification, gene cloning and mutant studies
    • Ratnayake, D. B., Wai, S. N., Shi, Y., Amako, K. et al., Ferritin from the obligate anaerobe Porphyromonas gingivalis: Purification, gene cloning and mutant studies. Microbiology 2000, 146, 1119-1127.
    • (2000) Microbiology , vol.146 , pp. 1119-1127
    • Ratnayake, D.B.1    Wai, S.N.2    Shi, Y.3    Amako, K.4
  • 61
    • 0033760278 scopus 로고    scopus 로고
    • Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis
    • Dashper, S. G., Hendtlass, A., Slakeski, N., Jackson, C. et al., Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis. J. Bacteriol. 2000, 182, 6456-6462.
    • (2000) J. Bacteriol , vol.182 , pp. 6456-6462
    • Dashper, S.G.1    Hendtlass, A.2    Slakeski, N.3    Jackson, C.4
  • 62
    • 0038480719 scopus 로고    scopus 로고
    • The essential role of fumarate reductase in haem-dependent growth stimulation of Bacteroides fragilis
    • Baughn, A. D., Malamy, M. H., The essential role of fumarate reductase in haem-dependent growth stimulation of Bacteroides fragilis. Microbiology 2003, 149, 1551-1558.
    • (2003) Microbiology , vol.149 , pp. 1551-1558
    • Baughn, A.D.1    Malamy, M.H.2
  • 63
    • 0033873462 scopus 로고    scopus 로고
    • Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis
    • Takahashi, N., Sato, T., Yamada, T., Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis. J. Bacteriol. 2000, 182, 4704-4710.
    • (2000) J. Bacteriol , vol.182 , pp. 4704-4710
    • Takahashi, N.1    Sato, T.2    Yamada, T.3
  • 64
    • 0036192462 scopus 로고    scopus 로고
    • The universal stress protein paralogues of Escherichia coli are co-ordinately regulated and co-operate in the defence against DNA damage
    • Gustavsson, N., Diez, A., Nystrom, T., The universal stress protein paralogues of Escherichia coli are co-ordinately regulated and co-operate in the defence against DNA damage. Mol. Microbiol. 2002, 43, 107-117.
    • (2002) Mol. Microbiol , vol.43 , pp. 107-117
    • Gustavsson, N.1    Diez, A.2    Nystrom, T.3
  • 65
    • 0038013951 scopus 로고    scopus 로고
    • The bacterial universal stress protein: Function and regulation
    • Kvint, K., Nachin, L., Diez, A., Nystrom, T., The bacterial universal stress protein: function and regulation. Curr. Opin. Microbiol. 2003, 6, 140-145.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 140-145
    • Kvint, K.1    Nachin, L.2    Diez, A.3    Nystrom, T.4
  • 66
    • 28644440172 scopus 로고    scopus 로고
    • Biofilm formation by the periodontopathic bacteria Treponema denticola and Porphyromonas gingivalis
    • Kuramitsu, H. K., Chen, W., Ikegami, A., Biofilm formation by the periodontopathic bacteria Treponema denticola and Porphyromonas gingivalis. J. Periodontol.2005, 76, 2047-2051.
    • (2005) J. Periodontol , vol.76 , pp. 2047-2051
    • Kuramitsu, H.K.1    Chen, W.2    Ikegami, A.3
  • 67
    • 33646361297 scopus 로고    scopus 로고
    • Role of the Porphyromonas gingivalis InIJ protein in homotypic and heterotypic biofilm development
    • Capestany, C. A., Kuboniwa, M., Jung, I. Y., Park, Y. et al., Role of the Porphyromonas gingivalis InIJ protein in homotypic and heterotypic biofilm development. Infect. Immun.2006, 74, 3002-3005.
    • (2006) Infect. Immun , vol.74 , pp. 3002-3005
    • Capestany, C.A.1    Kuboniwa, M.2    Jung, I.Y.3    Park, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.