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Volumn 193, Issue 2, 2011, Pages 411-420

Membrane topology and DNA-binding ability of the streptococcal cpsa protein

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BETA GALACTOSIDASE; MEMBRANE PROTEIN; MEMBRANE PROTEIN CPSA; UNCLASSIFIED DRUG;

EID: 78650897914     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01098-10     Document Type: Article
Times cited : (30)

References (52)
  • 1
    • 0031906872 scopus 로고    scopus 로고
    • Adherence of Streptococcus pneumoniae to human bronchial epithelial cells (BEAS-2B)
    • Adamou, J. E., T. M. Wizemann, P. Barren, and S. Langermann. 1998. Adherence of Streptococcus pneumoniae to human bronchial epithelial cells (BEAS-2B). Infect. Immun. 66:820-822.
    • (1998) Infect. Immun. , vol.66 , pp. 820-822
    • Adamou, J.E.1    Wizemann, T.M.2    Barren, P.3    Langermann, S.4
  • 2
    • 0141891397 scopus 로고    scopus 로고
    • Positive correlation between tyrosine phosphorylation of CpsD and capsular polysaccharide production in Streptococcus pneumoniae
    • Bender, M. H., R. T. Cartee, and J. Yother. 2003. Positive correlation between tyrosine phosphorylation of CpsD and capsular polysaccharide production in Streptococcus pneumoniae. J. Bacteriol. 185:6057-6066.
    • (2003) J. Bacteriol. , vol.185 , pp. 6057-6066
    • Bender, M.H.1    Cartee, R.T.2    Yother, J.3
  • 3
    • 14044266307 scopus 로고    scopus 로고
    • The putative autolysin regulator LytR in Streptococcus mutans plays a role in cell division and is growth-phase regulated
    • Chatfield, C. H., H. Koo, and R. G. Quivey, Jr. 2005. The putative autolysin regulator LytR in Streptococcus mutans plays a role in cell division and is growth-phase regulated. Microbiology 151:625-631.
    • (2005) Microbiology , vol.151 , pp. 625-631
    • Chatfield, C.H.1    Koo, H.2    Quivey Jr., R.G.3
  • 4
    • 0035808397 scopus 로고    scopus 로고
    • Functional analysis in type Ia group B Streptococcus of a cluster of genes involved in extracellular polysaccharide production by diverse species of streptococci
    • Cieslewicz, M. J., D. L. Kasper, Y. Wang, and M. R. Wessels. 2001. Functional analysis in type Ia group B Streptococcus of a cluster of genes involved in extracellular polysaccharide production by diverse species of streptococci. J. Biol. Chem. 276:139-146.
    • (2001) J. Biol. Chem. , vol.276 , pp. 139-146
    • Cieslewicz, M.J.1    Kasper, D.L.2    Wang, Y.3    Wessels, M.R.4
  • 5
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G., and G. von Heijne. 1994. TopPred II: An improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10:685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 6
    • 0026098804 scopus 로고
    • Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation
    • DiRita, V. J., and J. J. Mekalanos. 1991. Periplasmic interaction between two membrane regulatory proteins, ToxR and ToxS, results in signal transduction and transcriptional activation. Cell 64:29-37.
    • (1991) Cell , vol.64 , pp. 29-37
    • DiRita, V.J.1    Mekalanos, J.J.2
  • 7
    • 0030883192 scopus 로고    scopus 로고
    • Constitutive expression of fibronectin binding in Streptococcus pyogenes as a result of anaerobic activation of rofA
    • Fogg, G. C., and M. G. Caparon. 1997. Constitutive expression of fibronectin binding in Streptococcus pyogenes as a result of anaerobic activation of rofA. J. Bacteriol. 179:6172-6180.
    • (1997) J. Bacteriol. , vol.179 , pp. 6172-6180
    • Fogg, G.C.1    Caparon, M.G.2
  • 8
    • 0035086370 scopus 로고    scopus 로고
    • Streptococcus iniae virulence is associated with a distinct genetic profile
    • Fuller, J. D., D. J. Bast, V. Nizet, D. E. Low, and J. C. de Azavedo. 2001. Streptococcus iniae virulence is associated with a distinct genetic profile. Infect. Immun. 69:1994-2000.
    • (2001) Infect. Immun. , vol.69 , pp. 1994-2000
    • Fuller, J.D.1    Bast, D.J.2    Nizet, V.3    Low, D.E.4    De Azavedo, J.C.5
  • 9
    • 0034090275 scopus 로고    scopus 로고
    • The RofA binding site of Streptococcus pyogenes is utilized in multiple transcriptional pathways
    • Granok, A. B., A. Claiborne, R. P. Ross, and M. G. Caparon. 2000. The RofA binding site of Streptococcus pyogenes is utilized in multiple transcriptional pathways. J. Bacteriol. 182:1529-1540.
    • (2000) J. Bacteriol. , vol.182 , pp. 1529-1540
    • Granok, A.B.1    Claiborne, A.2    Ross, R.P.3    Caparon, M.G.4
  • 10
    • 23344444876 scopus 로고    scopus 로고
    • Illustration of pneumococcal polysaccharide capsule during adherence and invasion of epithelial cells
    • Hammerschmidt, S., et al. 2005. Illustration of pneumococcal polysaccharide capsule during adherence and invasion of epithelial cells. Infect. Immun. 73:4653-4667.
    • (2005) Infect. Immun. , vol.73 , pp. 4653-4667
    • Hammerschmidt, S.1
  • 11
    • 0038782198 scopus 로고    scopus 로고
    • Molecular analysis of the Enterococcus faecalis serotype 2 polysaccharide determinant
    • Hancock, L. E., B. D. Shepard, and M. S. Gilmore. 2003. Molecular analysis of the Enterococcus faecalis serotype 2 polysaccharide determinant. J. Bacteriol. 185:4393-4401.
    • (2003) J. Bacteriol. , vol.185 , pp. 4393-4401
    • Hancock, L.E.1    Shepard, B.D.2    Gilmore, M.S.3
  • 12
    • 0026469139 scopus 로고
    • Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells
    • Hanski, E., P. A. Horowitz, and M. G. Caparon. 1992. Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect. Immun. 60:5119-5125.
    • (1992) Infect. Immun. , vol.60 , pp. 5119-5125
    • Hanski, E.1    Horowitz, P.A.2    Caparon, M.G.3
  • 13
    • 0030029878 scopus 로고    scopus 로고
    • Genetic analysis of the interaction between Vibrio cholerae transcription activator ToxR and toxT promoter DNA
    • Higgins, D. E., and V. J. DiRita. 1996. Genetic analysis of the interaction between Vibrio cholerae transcription activator ToxR and toxT promoter DNA. J. Bacteriol. 178:1080-1087.
    • (1996) J. Bacteriol. , vol.178 , pp. 1080-1087
    • Higgins, D.E.1    DiRita, V.J.2
  • 14
    • 60849100217 scopus 로고    scopus 로고
    • Phylogenetic distribution and membrane topology of the LytR-CpsA-Psr protein family
    • Hubscher, J., L. Luthy, B. Berger-Bachi, and P. Stutzmann Meier. 2008. Phylogenetic distribution and membrane topology of the LytR-CpsA-Psr protein family. BMC Genomics 9:617.
    • (2008) BMC Genomics , vol.9 , pp. 617
    • Hubscher, J.1    Luthy, L.2    Berger-Bachi, B.3    Stutzmann Meier, P.4
  • 15
    • 65649084860 scopus 로고    scopus 로고
    • MsrR contributes to cell surface characteristics and virulence in Staphylococcus aureus
    • Hubscher, J., et al. 2009. MsrR contributes to cell surface characteristics and virulence in Staphylococcus aureus. FEMS Microbiol. Lett. 295:251-260.
    • (2009) FEMS Microbiol. Lett. , vol.295 , pp. 251-260
    • Hubscher, J.1
  • 16
    • 0027772958 scopus 로고
    • Sliding clamps of DNA polymerases
    • Kuriyan, J., and M. O'Donnell. 1993. Sliding clamps of DNA polymerases. J. Mol. Biol. 234:915-925.
    • (1993) J. Mol. Biol. , vol.234 , pp. 915-925
    • Kuriyan, J.1    O'Donnell, M.2
  • 17
    • 0026673165 scopus 로고
    • Sequencing and analysis of the Bacillus subtilis lytRABC divergon: A regulatory unit encom- passing the structural genes of the N-acetylmuramoyl-L- alanine amidase and its modifier
    • Lazarevic, V., P. Margot, B. Soldo, and D. Karamata. 1992. Sequencing and analysis of the Bacillus subtilis lytRABC divergon: A regulatory unit encom- passing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier. J. Gen. Microbiol. 138:1949-1961.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1949-1961
    • Lazarevic, V.1    Margot, P.2    Soldo, B.3    Karamata, D.4
  • 18
    • 0027537345 scopus 로고
    • Identification of a genetic element (psr) which negatively controls expression of Enterococcus hirae penicillin-binding protein 5
    • Ligozzi, M., F. Pittaluga, and R. Fontana. 1993. Identification of a genetic element (psr) which negatively controls expression of Enterococcus hirae penicillin-binding protein 5. J. Bacteriol. 175:2046-2051.
    • (1993) J. Bacteriol. , vol.175 , pp. 2046-2051
    • Ligozzi, M.1    Pittaluga, F.2    Fontana, R.3
  • 19
    • 0025037615 scopus 로고
    • Improved vector system for constructing transcriptional fusions that ensures independent translation of lacZ
    • Linn, T., and R. St. Pierre. 1990. Improved vector system for constructing transcriptional fusions that ensures independent translation of lacZ. J. Bacteriol. 172:1077-1084.
    • (1990) J. Bacteriol. , vol.172 , pp. 1077-1084
    • Linn, T.1    Pierre, R.S.2
  • 20
    • 33846939959 scopus 로고    scopus 로고
    • Streptococcus iniae capsule impairs phagocytic clearance and contributes to virulence in fish
    • Locke, J. B., et al. 2007. Streptococcus iniae capsule impairs phagocytic clearance and contributes to virulence in fish. J. Bacteriol. 189:1279-1287.
    • (2007) J. Bacteriol. , vol.189 , pp. 1279-1287
    • Locke, J.B.1
  • 21
    • 33847741407 scopus 로고    scopus 로고
    • Analysis of the polysaccharide capsule of the systemic pathogen Streptococcus iniae and its implications in virulence
    • Lowe, B. A., J. D. Miller, and M. N. Neely. 2007. Analysis of the polysaccharide capsule of the systemic pathogen Streptococcus iniae and its implications in virulence. Infect. Immun. 75:1255-1264.
    • (2007) Infect. Immun. , vol.75 , pp. 1255-1264
    • Lowe, B.A.1    Miller, J.D.2    Neely, M.N.3
  • 22
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • Maddocks, S. E., and P. C. Oyston. 2008. Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154:3609-3623.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 23
    • 0035016182 scopus 로고    scopus 로고
    • Requirement for capsule in colonization by Streptococcus pneumoniae
    • Magee, A. D., and J. Yother. 2001. Requirement for capsule in colonization by Streptococcus pneumoniae. Infect. Immun. 69:3755-3761.
    • (2001) Infect. Immun. , vol.69 , pp. 3755-3761
    • Magee, A.D.1    Yother, J.2
  • 24
    • 0026047004 scopus 로고
    • Analysis of membrane protein topology using alkaline phosphatase and beta-galactosidase gene fusions
    • Manoil, C. 1991. Analysis of membrane protein topology using alkaline phosphatase and beta-galactosidase gene fusions. Methods Cell Biol. 34:61-75.
    • (1991) Methods Cell Biol. , vol.34 , pp. 61-75
    • Manoil, C.1
  • 25
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C., and J. Beckwith. 1986. A genetic approach to analyzing membrane protein topology. Science 233:1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 26
    • 0025095225 scopus 로고
    • Alkaline phosphatase fusions: Sensors of subcellular location
    • Manoil, C., J. J. Mekalanos, and J. Beckwith. 1990. Alkaline phosphatase fusions: sensors of subcellular location. J. Bacteriol. 172:515-518.
    • (1990) J. Bacteriol. , vol.172 , pp. 515-518
    • Manoil, C.1    Mekalanos, J.J.2    Beckwith, J.3
  • 27
    • 0026688561 scopus 로고
    • Prevention of C3 deposition by capsular polysaccharide is a virulence mechanism of type III group B streptococci
    • Marques, M. B., D. L. Kasper, M. K. Pangburn, and M. R. Wessels. 1992. Prevention of C3 deposition by capsular polysaccharide is a virulence mechanism of type III group B streptococci. Infect. Immun. 60:3986-3993.
    • (1992) Infect. Immun. , vol.60 , pp. 3986-3993
    • Marques, M.B.1    Kasper, D.L.2    Pangburn, M.K.3    Wessels, M.R.4
  • 28
    • 0029829905 scopus 로고    scopus 로고
    • Evidence that the PBP 5 synthesis repressor (psr) of Enterococcus hirae is also involved in the regulation of cell wall composition and other cell wallrelated properties
    • Massidda, O., R. Kariyama, L. Daneo-Moore, and G. D. Shockman. 1996. Evidence that the PBP 5 synthesis repressor (psr) of Enterococcus hirae is also involved in the regulation of cell wall composition and other cell wallrelated properties. J. Bacteriol. 178:5272-5278.
    • (1996) J. Bacteriol. , vol.178 , pp. 5272-5278
    • Massidda, O.1    Kariyama, R.2    Daneo-Moore, L.3    Shockman, G.D.4
  • 29
    • 12844276013 scopus 로고    scopus 로고
    • Large-scale screen highlights the importance of capsule for virulence in the zoonotic pathogen Streptococcus iniae
    • Miller, J. D., and M. N. Neely. 2005. Large-scale screen highlights the importance of capsule for virulence in the zoonotic pathogen Streptococcus iniae. Infect. Immun. 73:921-934.
    • (2005) Infect. Immun. , vol.73 , pp. 921-934
    • Miller, J.D.1    Neely, M.N.2
  • 30
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Miller, J. H. 1972. Experiments in molecular genetics, p. 352-358. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics , pp. 352-358
    • Miller, J.H.1
  • 31
    • 0023667819 scopus 로고
    • Cholera toxin transcriptional activator toxR is a transmembrane DNA binding protein
    • Miller, V. L., R. K. Taylor, and J. J. Mekalanos. 1987. Cholera toxin transcriptional activator toxR is a transmembrane DNA binding protein. Cell 48:271-279.
    • (1987) Cell , vol.48 , pp. 271-279
    • Miller, V.L.1    Taylor, R.K.2    Mekalanos, J.J.3
  • 32
    • 0036134946 scopus 로고    scopus 로고
    • Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase
    • Morona, J. K., R. Morona, D. C. Miller, and J. C. Paton. 2002. Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase. J. Bacteriol. 184:577-583.
    • (2002) J. Bacteriol. , vol.184 , pp. 577-583
    • Morona, J.K.1    Morona, R.2    Miller, D.C.3    Paton, J.C.4
  • 33
    • 26944487606 scopus 로고    scopus 로고
    • Contribution of biofilm regulatory protein A of Streptococcus mutans, to systemic virulence
    • Nakano, K., K. Fujita, K. Nishimura, R. Nomura, and T. Ooshima. 2005. Contribution of biofilm regulatory protein A of Streptococcus mutans, to systemic virulence. Microbes Infect. 7:1246-1255.
    • (2005) Microbes Infect. , vol.7 , pp. 1246-1255
    • Nakano, K.1    Fujita, K.2    Nishimura, K.3    Nomura, R.4    Ooshima, T.5
  • 34
    • 34848846150 scopus 로고    scopus 로고
    • The epidemiology of invasive group A streptococcal infection and potential vaccine implications: United States, 2000-2004
    • O'Loughlin, R. E., et al. 2007. The epidemiology of invasive group A streptococcal infection and potential vaccine implications: United States, 2000- 2004. Clin. Infect. Dis. 45:853-862.
    • (2007) Clin. Infect. Dis. , vol.45 , pp. 853-862
    • O'Loughlin, R.E.1
  • 35
    • 0030007418 scopus 로고    scopus 로고
    • Cell growth rate regulates expression of group B Streptococcus type III capsular polysaccharide
    • Paoletti, L. C., R. A. Ross, and K. D. Johnson. 1996. Cell growth rate regulates expression of group B Streptococcus type III capsular polysaccharide. Infect. Immun. 64:1220-1226.
    • (1996) Infect. Immun. , vol.64 , pp. 1220-1226
    • Paoletti, L.C.1    Ross, R.A.2    Johnson, K.D.3
  • 36
    • 0031753364 scopus 로고    scopus 로고
    • Mutations in toxR and toxS that separate transcriptional activation from DNA binding at the cholera toxin gene promoter
    • Pfau, J. D., and R. K. Taylor. 1998. Mutations in toxR and toxS that separate transcriptional activation from DNA binding at the cholera toxin gene promoter. J. Bacteriol. 180:4724-4733.
    • (1998) J. Bacteriol. , vol.180 , pp. 4724-4733
    • Pfau, J.D.1    Taylor, R.K.2
  • 37
    • 43049170245 scopus 로고    scopus 로고
    • Epidemiology of invasive group B streptococcal disease in the United States, 1999-2005
    • Phares, C. R., et al. 2008. Epidemiology of invasive group B streptococcal disease in the United States, 1999-2005. JAMA 299:2056-2065.
    • (2008) JAMA , vol.299 , pp. 2056-2065
    • Phares, C.R.1
  • 38
    • 0028232931 scopus 로고
    • Growth of group B streptococci in human serum leads to increased cell surface sialic acid and decreased activation of the alternative complement pathway
    • Platt, M. W., N. Correa, Jr., and C. Mold. 1994. Growth of group B streptococci in human serum leads to increased cell surface sialic acid and decreased activation of the alternative complement pathway. Can. J. Microbiol. 40:99-105.
    • (1994) Can. J. Microbiol. , vol.40 , pp. 99-105
    • Platt, M.W.1    Correa Jr., N.2    Mold, C.3
  • 39
    • 0031573015 scopus 로고    scopus 로고
    • A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galactosidase in gram-positive bacteria
    • Poyart, C., and P. Trieu-Cuot. 1997. A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to beta-galactosidase in gram-positive bacteria. FEMS Microbiol. Lett. 156:193-198.
    • (1997) FEMS Microbiol. Lett. , vol.156 , pp. 193-198
    • Poyart, C.1    Trieu-Cuot, P.2
  • 40
    • 0035028433 scopus 로고    scopus 로고
    • Penicillin-binding protein 5 and expression of ampicillin resistance in Enterococcus faecium
    • Rice, L. B., et al. 2001. Penicillin-binding protein 5 and expression of ampicillin resistance in Enterococcus faecium. Antimicrob. Agents Chemother. 45:1480-1486.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1480-1486
    • Rice, L.B.1
  • 41
    • 0041767511 scopus 로고    scopus 로고
    • MsrR, a putative cell envelope-associated element involved in Staphylococcus aureus sarA attenuation
    • Rossi, J., M. Bischoff, A. Wada, and B. Berger-Bachi. 2003. MsrR, a putative cell envelope-associated element involved in Staphylococcus aureus sarA attenuation. Antimicrob. Agents Chemother. 47:2558-2564.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2558-2564
    • Rossi, J.1    Bischoff, M.2    Wada, A.3    Berger-Bachi, B.4
  • 42
    • 0029125560 scopus 로고
    • Phase-shift of polysaccharide capsule expression in group B streptococci, type III
    • Sellin, M., S. Hakansson, and M. Norgren. 1995. Phase-shift of polysaccharide capsule expression in group B streptococci, type III. Microb. Pathog. 18:401-415.
    • (1995) Microb. Pathog. , vol.18 , pp. 401-415
    • Sellin, M.1    Hakansson, S.2    Norgren, M.3
  • 43
    • 0030885341 scopus 로고    scopus 로고
    • Control of the ToxR virulence regulon in Vibrio cholerae by environmental stimuli
    • Skorupski, K., and R. K. Taylor. 1997. Control of the ToxR virulence regulon in Vibrio cholerae by environmental stimuli. Mol. Microbiol. 25: 1003-1009.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1003-1009
    • Skorupski, K.1    Taylor, R.K.2
  • 44
    • 0035987266 scopus 로고    scopus 로고
    • Organization and characterization of the capsule biosynthesis locus of Streptococcus pneumoniae serotype 9V
    • van Selm, S., et al. 2002. Organization and characterization of the capsule biosynthesis locus of Streptococcus pneumoniae serotype 9V. Microbiology 148:1747-1755.
    • (2002) Microbiology , vol.148 , pp. 1747-1755
    • Van Selm, S.1
  • 45
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. 1992. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 46
    • 0030804035 scopus 로고    scopus 로고
    • Invasive infections due to a fish pathogen, Streptococcus iniae
    • Weinstein, M. R., et al. 1997. Invasive infections due to a fish pathogen, Streptococcus iniae. N. Engl. J. Med. 337:589-594.
    • (1997) N. Engl. J. Med. , vol.337 , pp. 589-594
    • Weinstein, M.R.1
  • 47
    • 0030210386 scopus 로고    scopus 로고
    • Invasive infection due to Streptococcus iniae: A new or previously unrecognized disease-Ontario, 1995-1996
    • Weinstein, M. R., D. E. Low, A. McGeer, et al. 1996. Invasive infection due to Streptococcus iniae: A new or previously unrecognized disease-Ontario, 1995-1996. Can. Commun. Dis. Rep. 22:129-132.
    • (1996) Can. Commun. Dis. Rep. , vol.22 , pp. 129-132
    • Weinstein, M.R.1    Low, D.E.2    McGeer, A.3
  • 48
    • 0034874741 scopus 로고    scopus 로고
    • Changes in availability of oxygen accentuate differences in capsular polysaccharide expression by phenotypic variants and clinical isolates of Streptococcus pneumoniae
    • Weiser, J. N., et al. 2001. Changes in availability of oxygen accentuate differences in capsular polysaccharide expression by phenotypic variants and clinical isolates of Streptococcus pneumoniae. Infect. Immun. 69:5430-5439.
    • (2001) Infect. Immun. , vol.69 , pp. 5430-5439
    • Weiser, J.N.1
  • 49
    • 33646003236 scopus 로고    scopus 로고
    • Influence of BrpA on critical virulence attributes of Streptococcus mutans
    • Wen, Z. T., H. V. Baker, and R. A. Burne. 2006. Influence of BrpA on critical virulence attributes of Streptococcus mutans. J. Bacteriol. 188:2983-2992.
    • (2006) J. Bacteriol. , vol.188 , pp. 2983-2992
    • Wen, Z.T.1    Baker, H.V.2    Burne, R.A.3
  • 50
    • 0036199307 scopus 로고    scopus 로고
    • Functional genomics approach to identifying genes required for biofilm development by Streptococcus mutans
    • Wen, Z. T., and R. A. Burne. 2002. Functional genomics approach to identifying genes required for biofilm development by Streptococcus mutans. Appl. Environ. Microbiol. 68:1196-1203.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1196-1203
    • Wen, Z.T.1    Burne, R.A.2
  • 51
    • 0032881671 scopus 로고    scopus 로고
    • Molecular characterization of type-specific capsular polysaccharide biosynthesis genes of Streptococcus agalactiae type Ia
    • Yamamoto, S., et al. 1999. Molecular characterization of type-specific capsular polysaccharide biosynthesis genes of Streptococcus agalactiae type Ia. J. Bacteriol. 181:5176-5184.
    • (1999) J. Bacteriol. , vol.181 , pp. 5176-5184
    • Yamamoto, S.1
  • 52
    • 0036955805 scopus 로고    scopus 로고
    • Multiple Streptococcus mutans genes are involved in biofilm formation
    • Yoshida, A., and H. K. Kuramitsu. 2002. Multiple Streptococcus mutans genes are involved in biofilm formation. Appl. Environ. Microbiol. 68:6283-6291.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 6283-6291
    • Yoshida, A.1    Kuramitsu, H.K.2


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