메뉴 건너뛰기




Volumn 31, Issue 4, 1999, Pages 1051-1064

Characterization of nra, a global negative regulator gene in group A streptococci

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; COLLAGEN; FIBRONECTIN;

EID: 0033039873     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01241.x     Document Type: Article
Times cited : (162)

References (53)
  • 2
    • 0025690140 scopus 로고
    • Structure and nucleotide sequence of the Bacillus subtilis phenylalanyl-tRNA synthetase genes
    • Brakhage, A.A., Wozny, M., and Putzer, H. (1990) Structure and nucleotide sequence of the Bacillus subtilis phenylalanyl-tRNA synthetase genes. Biochimie 72: 725-734.
    • (1990) Biochimie , vol.72 , pp. 725-734
    • Brakhage, A.A.1    Wozny, M.2    Putzer, H.3
  • 3
    • 0025751633 scopus 로고
    • Genetic manipulation of pathogenic streptococci
    • Caparon, M.G., and Scott, J.R. (1991) Genetic manipulation of pathogenic streptococci. Methods Enzymol 204: 556-586.
    • (1991) Methods Enzymol , vol.204 , pp. 556-586
    • Caparon, M.G.1    Scott, J.R.2
  • 4
    • 0026808610 scopus 로고
    • Environmental regulation of virulence in group A streptococci: Transcription of the gene encoding M protein is stimulated by carbon dioxide
    • Caparon, M.G., Geist, R.T., Perez-Casal, J., and Scott, J.R. (1992) Environmental regulation of virulence in group A streptococci: transcription of the gene encoding M protein is stimulated by carbon dioxide. J Bacteriol 174: 5693-5701.
    • (1992) J Bacteriol , vol.174 , pp. 5693-5701
    • Caparon, M.G.1    Geist, R.T.2    Perez-Casal, J.3    Scott, J.R.4
  • 5
    • 0028586830 scopus 로고
    • Cloning, sequence analysis, and expression of the genes encoding the two sub-units of the methylotrophic bacterium W3A1 electron transfer flavoprotein
    • Chen, D., and Swenson, R.P. (1994) Cloning, sequence analysis, and expression of the genes encoding the two sub-units of the methylotrophic bacterium W3A1 electron transfer flavoprotein. J Biol Chem 269: 32120-32130.
    • (1994) J Biol Chem , vol.269 , pp. 32120-32130
    • Chen, D.1    Swenson, R.P.2
  • 6
    • 0027131437 scopus 로고
    • VirR and Mry are homologous trans-acting regulators of M protein and C5a peptidase expression in group A streptococci
    • Chen, C., Bormann, N., and Cleary, P.P. (1993) VirR and Mry are homologous trans-acting regulators of M protein and C5a peptidase expression in group A streptococci. Mol Gen Genet 241: 685-693.
    • (1993) Mol Gen Genet , vol.241 , pp. 685-693
    • Chen, C.1    Bormann, N.2    Cleary, P.P.3
  • 7
    • 0029099312 scopus 로고
    • Hyaluronic acid synthesis operon (has) expression in group A streptococci
    • Crater, D.L., and van de Rijn, I. (1995) Hyaluronic acid synthesis operon (has) expression in group A streptococci. J Biol Chem 270: 18452-18458.
    • (1995) J Biol Chem , vol.270 , pp. 18452-18458
    • Crater, D.L.1    Van de Rijn, I.2
  • 8
    • 0029796449 scopus 로고    scopus 로고
    • Molecular cloning and expression of the spsB gene encoding an essential type I signal peptidase from Staphylococcus aureus
    • Cregg, K.M., Wilding, E.I., and Black, M.T. (1996) Molecular cloning and expression of the spsB gene encoding an essential type I signal peptidase from Staphylococcus aureus. J Bacteriol 178: 5712-5718.
    • (1996) J Bacteriol , vol.178 , pp. 5712-5718
    • Cregg, K.M.1    Wilding, E.I.2    Black, M.T.3
  • 9
    • 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 Caparon, M.G. (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
  • 10
    • 0028237244 scopus 로고
    • The identification of rofA, a positive-acting regulatory component of prtF expression: Use of an mgd-based shuttle mutagenesis strategy in Streptococcus pyogenes
    • Fogg, G.C., Gibson, C.M., and Caparon, M.G. (1994) The identification of rofA, a positive-acting regulatory component of prtF expression: use of an mgd-based shuttle mutagenesis strategy in Streptococcus pyogenes. Mol Microbiol 11: 671-684.
    • (1994) Mol Microbiol , vol.11 , pp. 671-684
    • Fogg, G.C.1    Gibson, C.M.2    Caparon, M.G.3
  • 11
    • 0027401714 scopus 로고
    • Pneumococcal cell wall mediates pneumococcal attachment and cytopathology to human endothelial cells
    • Geelen, S., Bhattacharyya, C., and Tuomanen, E. (1993) Pneumococcal cell wall mediates pneumococcal attachment and cytopathology to human endothelial cells. Infect Immun 61: 1538-1543.
    • (1993) Infect Immun , vol.61 , pp. 1538-1543
    • Geelen, S.1    Bhattacharyya, C.2    Tuomanen, E.3
  • 12
    • 0029785171 scopus 로고    scopus 로고
    • Insertional inactivation of Streptococcus pyogenes sod suggests that prtF is regulated in response to a superoxide signal
    • Gibson, C.M., and Caparon, M.G. (1996) Insertional inactivation of Streptococcus pyogenes sod suggests that prtF is regulated in response to a superoxide signal. J Bacteriol 178: 4688-4695.
    • (1996) J Bacteriol , vol.178 , pp. 4688-4695
    • Gibson, C.M.1    Caparon, M.G.2
  • 13
    • 0029888893 scopus 로고    scopus 로고
    • Structural dissection and functional analysis of the complex promoter of the streptokinase gene from Streptococus equisimilis H46A
    • Gräfe, S., Ellinger, T., and Malke, H. (1996) Structural dissection and functional analysis of the complex promoter of the streptokinase gene from Streptococus equisimilis H46A. Med Microbiol Immunol 185: 11-17.
    • (1996) Med Microbiol Immunol , vol.185 , pp. 11-17
    • Gräfe, S.1    Ellinger, T.2    Malke, H.3
  • 15
    • 0026661424 scopus 로고
    • Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus (Streptococcus pyogenes)
    • Hanski, E., and Caparon, M. (1992) Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus (Streptococcus pyogenes). Proc Natl Acad Sci USA 89: 6172-6176.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6172-6176
    • Hanski, E.1    Caparon, M.2
  • 16
    • 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., Horwitz, P.A., and Caparon, M.G. (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    Horwitz, P.A.2    Caparon, M.G.3
  • 17
    • 0029744998 scopus 로고    scopus 로고
    • Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains
    • Jaffe, J., Natanson-Yaron, S., Caparon, M.G., and Hanski, E. (1996) Protein F2, a novel fibronectin-binding protein from Streptococcus pyogenes, possesses two binding domains. Mol Microbiol 21: 373-384.
    • (1996) Mol Microbiol , vol.21 , pp. 373-384
    • Jaffe, J.1    Natanson-Yaron, S.2    Caparon, M.G.3    Hanski, E.4
  • 18
    • 0031015056 scopus 로고    scopus 로고
    • Structure, function and immunogenicity of streptococcal antigen I/II polypeptides
    • Jenkinson, H.F., and Demuth, D.R. (1997) Structure, function and immunogenicity of streptococcal antigen I/II polypeptides. Mol Microbiol 23: 183-190.
    • (1997) Mol Microbiol , vol.23 , pp. 183-190
    • Jenkinson, H.F.1    Demuth, D.R.2
  • 19
    • 0026673031 scopus 로고
    • M protein gene typing of Streptococcus pyogenes by nonradioactively labeled oligonucleotide probes
    • Kaufhold, A., Podbielski, A., Johnson, D.R., Kaplan, E.L., and Lütticken, R. (1992) M protein gene typing of Streptococcus pyogenes by nonradioactively labeled oligonucleotide probes. J Clin Microbiol 30: 2391-2397.
    • (1992) J Clin Microbiol , vol.30 , pp. 2391-2397
    • Kaufhold, A.1    Podbielski, A.2    Johnson, D.R.3    Kaplan, E.L.4    Lütticken, R.5
  • 20
    • 0030814729 scopus 로고    scopus 로고
    • Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria
    • Kleerebezem, M., Quadri, L.E.N., Kuipers, O.P., and de Vos, W.M. (1997) Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Mol Microbiol 24: 895-904.
    • (1997) Mol Microbiol , vol.24 , pp. 895-904
    • Kleerebezem, M.1    Quadri, L.E.N.2    Kuipers, O.P.3    De Vos, W.M.4
  • 21
    • 0028341747 scopus 로고
    • Streptococcus pyogenes type IIa IgG Fc receptor expression is co-ordinately regulated with M protein and streptococcal C5a peptidase
    • La Penta, D., Zhang, X.P., and Cleary, P.P. (1994) Streptococcus pyogenes type IIa IgG Fc receptor expression is co-ordinately regulated with M protein and streptococcal C5a peptidase. Mol Microbiol 12: 873-879.
    • (1994) Mol Microbiol , vol.12 , pp. 873-879
    • La Penta, D.1    Zhang, X.P.2    Cleary, P.P.3
  • 22
    • 0030753825 scopus 로고    scopus 로고
    • Role of mga in growth phase regulation of virulence genes of the group A streptococcus
    • McIver, K., and Scott, J.R. (1997) Role of mga in growth phase regulation of virulence genes of the group A streptococcus. J Bacteriol 179: 5178-5187.
    • (1997) J Bacteriol , vol.179 , pp. 5178-5187
    • McIver, K.1    Scott, J.R.2
  • 23
    • 0028867355 scopus 로고
    • Regulation of virulence by environmental signals in group A streptococci: Influence of osmolarity, temperature, gas exchange, and iron limitation in emm transcription
    • McIver, K.S., Heath, A.S., and Scott, J.R. (1995) Regulation of virulence by environmental signals in group A streptococci: influence of osmolarity, temperature, gas exchange, and iron limitation in emm transcription. Infect Immun 63: 4540-4542.
    • (1995) Infect Immun , vol.63 , pp. 4540-4542
    • McIver, K.S.1    Heath, A.S.2    Scott, J.R.3
  • 24
    • 0028918857 scopus 로고
    • Cloning and expression of the heterodimeric deoxyguanosine kinase/deoxyadenosine kinase of Lactobacillus acidophilus R-26
    • Ma, G.T., Hong, Y.S., and Ives, D.H. (1995) Cloning and expression of the heterodimeric deoxyguanosine kinase/deoxyadenosine kinase of Lactobacillus acidophilus R-26. J Biol Chem 270: 6595-6601.
    • (1995) J Biol Chem , vol.270 , pp. 6595-6601
    • Ma, G.T.1    Hong, Y.S.2    Ives, D.H.3
  • 25
    • 0028981682 scopus 로고
    • The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-ntrB-ntrC operon and are negatively regulated
    • Machado, H.B., Yates, M.G., Funayama, S., Rigo, L.U., Steffens, M.B.R., Souza, E.M., et al. (1995) The ntrBC genes of Azospirillum brasilense are part of a nifR3-like-ntrB-ntrC operon and are negatively regulated. Can J Microbiol 41: 674-684.
    • (1995) Can J Microbiol , vol.41 , pp. 674-684
    • Machado, H.B.1    Yates, M.G.2    Funayama, S.3    Rigo, L.U.4    Steffens, M.B.R.5    Souza, E.M.6
  • 26
    • 0025005040 scopus 로고
    • Comparison of epidemic and endemic group G streptococci by restriction enzyme analysis
    • Martin, N.J., Kaplan, E.L., Gerber, M.A., Menegus, M.A., Randolph, M., Bell, K., et al. (1990) Comparison of epidemic and endemic group G streptococci by restriction enzyme analysis. J Clin Microbiol 28: 1881-1886.
    • (1990) J Clin Microbiol , vol.28 , pp. 1881-1886
    • Martin, N.J.1    Kaplan, E.L.2    Gerber, M.A.3    Menegus, M.A.4    Randolph, M.5    Bell, K.6
  • 27
    • 0028955430 scopus 로고
    • Distribution of fibronectin-binding proteins among group A streptococci of different M types
    • Natanson, S., Sela, S., Moses, A.E., Musser, J.M., Caparon, M.G., and Hanski, E. (1995) Distribution of fibronectin-binding proteins among group A streptococci of different M types. J Infect Dis 171: 871-878.
    • (1995) J Infect Dis , vol.171 , pp. 871-878
    • Natanson, S.1    Sela, S.2    Moses, A.E.3    Musser, J.M.4    Caparon, M.G.5    Hanski, E.6
  • 28
    • 0028700721 scopus 로고
    • Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin
    • Ogasawara, N., Nakai, S., and Yoshikawa, H. (1994) Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin. DNA Res 1: 1-14.
    • (1994) DNA Res , vol.1 , pp. 1-14
    • Ogasawara, N.1    Nakai, S.2    Yoshikawa, H.3
  • 29
    • 0027413670 scopus 로고
    • Positive transcriptional control of mry regulates virulence in the group A streptococcus
    • Okada, N., Geist, R.T., and Caparon, M.G. (1993) Positive transcriptional control of mry regulates virulence in the group A streptococcus. Mol Microbiol 7: 893-903.
    • (1993) Mol Microbiol , vol.7 , pp. 893-903
    • Okada, N.1    Geist, R.T.2    Caparon, M.G.3
  • 30
    • 0028023460 scopus 로고
    • M protein and protein F act as important determinants of cell-specific tropism of streptococcus pyogenes in skin tissue
    • Okada, N., Pentland, A.P., Falk, P., and Caparon, M.G. (1994) M protein and protein F act as important determinants of cell-specific tropism of streptococcus pyogenes in skin tissue. J Clin Invest 94: 965-977.
    • (1994) J Clin Invest , vol.94 , pp. 965-977
    • Okada, N.1    Pentland, A.P.2    Falk, P.3    Caparon, M.G.4
  • 31
    • 0028935315 scopus 로고
    • Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus
    • Okada, N., Liszewski, M.K., Atkinson, J.P., and Caparon, M. (1995) Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus. Proc Natl Acad Sci USA 92: 2489-2493.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2489-2493
    • Okada, N.1    Liszewski, M.K.2    Atkinson, J.P.3    Caparon, M.4
  • 32
    • 0029986634 scopus 로고    scopus 로고
    • A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix
    • Ozeri, V., Tovi, A., Burstein, I., Natanson-Yaron, S., Caparon, M.G., Yamada, K.M., et al. (1996) A two-domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix. EMBO J 15: 989-998.
    • (1996) EMBO J , vol.15 , pp. 989-998
    • Ozeri, V.1    Tovi, A.2    Burstein, I.3    Natanson-Yaron, S.4    Caparon, M.G.5    Yamada, K.M.6
  • 33
    • 0025865798 scopus 로고
    • Mry, a trans-acting positive regulator of the M protein gene of Streptococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems
    • Perez-Casal, J., Caparon, M.G., and Scott, J.R. (1991) Mry, a trans-acting positive regulator of the M protein gene of Streptococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems. J Bacteriol 173: 2617-2624.
    • (1991) J Bacteriol , vol.173 , pp. 2617-2624
    • Perez-Casal, J.1    Caparon, M.G.2    Scott, J.R.3
  • 34
    • 0031776883 scopus 로고    scopus 로고
    • The group A streptococcal dipeptide permease (Dpp) is involved in the uptake of essential amino acids and affects the expression of cysteine protease
    • Podbielski, A., and Leonard, B.A.B. (1998) The group A streptococcal dipeptide permease (Dpp) is involved in the uptake of essential amino acids and affects the expression of cysteine protease. Mol Microbiol 28: 1323-1334.
    • (1998) Mol Microbiol , vol.28 , pp. 1323-1334
    • Podbielski, A.1    Leonard, B.A.B.2
  • 35
    • 0026702422 scopus 로고
    • Surface protein-CAT reporter fusions demonstrate differential gene expression in the vir regulon of Streptococcus pyogenes
    • Podbielski, A., Peterson, J.A., and Cleary, P. (1992) Surface protein-CAT reporter fusions demonstrate differential gene expression in the vir regulon of Streptococcus pyogenes. Mol Microbiol 6: 2253-2265.
    • (1992) Mol Microbiol , vol.6 , pp. 2253-2265
    • Podbielski, A.1    Peterson, J.A.2    Cleary, P.3
  • 36
    • 0028861517 scopus 로고
    • The group A streptococcal virR49 gene controls expression of four structural vir regulon genes
    • Podbielski, A., Flosdorff, A., and Weber-Heynemann, J. (1995) The group A streptococcal virR49 gene controls expression of four structural vir regulon genes. Infect Immun 63: 9-20.
    • (1995) Infect Immun , vol.63 , pp. 9-20
    • Podbielski, A.1    Flosdorff, A.2    Weber-Heynemann, J.3
  • 37
    • 0030476579 scopus 로고    scopus 로고
    • What is the size of the group A streptococcal vir regulon? The Mga regulator affects expression of secreted and surface virulence factors
    • Podbielski, A., Woischnik, M., Pohl, B., and Schmidt, K.H. (1996a) What is the size of the group A streptococcal vir regulon? The Mga regulator affects expression of secreted and surface virulence factors. Med Microbiol Immunol 185: 171-181.
    • (1996) Med Microbiol Immunol , vol.185 , pp. 171-181
    • Podbielski, A.1    Woischnik, M.2    Pohl, B.3    Schmidt, K.H.4
  • 38
    • 0029798285 scopus 로고    scopus 로고
    • Molecular characterization of group A streptococcal (GAS) oligopeptide permease (Opp) and its effect on cysteine protease production
    • Podbielski, A., Pohl, B., Woischnik, M., Körner, C., Schmidt, K.H., Rozdzinski, E., et al. (1996b) Molecular characterization of group A streptococcal (GAS) oligopeptide permease (Opp) and its effect on cysteine protease production. Mol Microbiol 21: 1087-1099.
    • (1996) Mol Microbiol , vol.21 , pp. 1087-1099
    • Podbielski, A.1    Pohl, B.2    Woischnik, M.3    Körner, C.4    Schmidt, K.H.5    Rozdzinski, E.6
  • 39
    • 0030600488 scopus 로고    scopus 로고
    • Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS)
    • Podbielski, A., Spellerberg, B., Woischnik, M., Pohl, B., and Lütticken, R. (1996c) Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS). Gene 177: 137-147.
    • (1996) Gene , vol.177 , pp. 137-147
    • Podbielski, A.1    Spellerberg, B.2    Woischnik, M.3    Pohl, B.4    Lütticken, R.5
  • 40
    • 0030696221 scopus 로고    scopus 로고
    • Structural principles of prokaryotic gene regulatory proteins and the evolution of repressors and gene activators
    • Prag, G., Greenberg, S., and Oppenheim, A.B. (1997) Structural principles of prokaryotic gene regulatory proteins and the evolution of repressors and gene activators. Mol Microbiol 26: 619-620.
    • (1997) Mol Microbiol , vol.26 , pp. 619-620
    • Prag, G.1    Greenberg, S.2    Oppenheim, A.B.3
  • 41
    • 0018901441 scopus 로고
    • Growth characteristics of group A streptococci in a new chemically defined medium
    • Van de Rijn, I., and Kessler, R.E. (1980) Growth characteristics of group A streptococci in a new chemically defined medium. Infect Immun 27: 444-448.
    • (1980) Infect Immun , vol.27 , pp. 444-448
    • Van de Rijn, I.1    Kessler, R.E.2
  • 42
    • 0028942685 scopus 로고
    • Cloning and sequence analysis of a novel member of the single-stranded DNA binding protein family
    • Rikke, B.A., Vellanoweth, R.L., Her, S., Chatterjee, B., and Roy, A.K. (1995) Cloning and sequence analysis of a novel member of the single-stranded DNA binding protein family. Biochim Biophys Acta 1261: 143-146.
    • (1995) Biochim Biophys Acta , vol.1261 , pp. 143-146
    • Rikke, B.A.1    Vellanoweth, R.L.2    Her, S.3    Chatterjee, B.4    Roy, A.K.5
  • 44
    • 0026687972 scopus 로고
    • A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism
    • Russell, R.R.B., Aduse-Opoku, J., Sutcliffe, I.C., Tao, L., and Ferretti, J.J. (1992) A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolism. J Biol Chem 267: 4631-4637.
    • (1992) J Biol Chem , vol.267 , pp. 4631-4637
    • Russell, R.R.B.1    Aduse-Opoku, J.2    Sutcliffe, I.C.3    Tao, L.4    Ferretti, J.J.5
  • 45
    • 0027321128 scopus 로고
    • Multiple binding of type 3 streptococcal M protein to human fibrinogen, albumin and fibronectin
    • Schmidt, K.H., Mann, K.H., Cooney, J., and Köhler, W. (1993) Multiple binding of type 3 streptococcal M protein to human fibrinogen, albumin and fibronectin. FEMS Immunol Med Microbiol 7: 135-144.
    • (1993) FEMS Immunol Med Microbiol , vol.7 , pp. 135-144
    • Schmidt, K.H.1    Mann, K.H.2    Cooney, J.3    Köhler, W.4
  • 46
    • 0027763194 scopus 로고
    • Protein F: An adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains
    • Sela, S., Aviv, A., Tovi, A., Burstein, I., Caparon, M.G., and Hanski, E. (1993) Protein F: an adhesin of Streptococcus pyogenes binds fibronectin via two distinct domains. Mol Microbiol 10: 1049-1055.
    • (1993) Mol Microbiol , vol.10 , pp. 1049-1055
    • Sela, S.1    Aviv, A.2    Tovi, A.3    Burstein, I.4    Caparon, M.G.5    Hanski, E.6
  • 47
    • 0022407696 scopus 로고
    • Complete nucleotide sequence of macrolide-lincosamide-streptogramin B-resistance transposon Tn917 in Streptococcus faecalis
    • Shaw, J.H., and Clewell, D.B. (1985) Complete nucleotide sequence of macrolide-lincosamide-streptogramin B-resistance transposon Tn917 in Streptococcus faecalis. J Bacteriol 164: 782-796.
    • (1985) J Bacteriol , vol.164 , pp. 782-796
    • Shaw, J.H.1    Clewell, D.B.2
  • 48
    • 0027179317 scopus 로고
    • Molecular characterization of a negative regulator of Streptococcus sobrinus surface protein antigen gene
    • Takahashi, I., Okahashi, N., and Hamada, S. (1993) Molecular characterization of a negative regulator of Streptococcus sobrinus surface protein antigen gene. J Bacteriol 175: 4345-4353.
    • (1993) J Bacteriol , vol.175 , pp. 4345-4353
    • Takahashi, I.1    Okahashi, N.2    Hamada, S.3
  • 49
    • 0026706763 scopus 로고
    • Fibronectin-binding protein of Streptococcus pyogenes: Sequence of the binding domain involved in adherence of streptococci to epithelial cells
    • Talay, S.R., Valentin-Weigand, P., Jerlström, P.G., Timmis, K.N., and Chhatwal, G.S. (1992) Fibronectin-binding protein of Streptococcus pyogenes: sequence of the binding domain involved in adherence of streptococci to epithelial cells. Infect Immun 60: 3837-3844.
    • (1992) Infect Immun , vol.60 , pp. 3837-3844
    • Talay, S.R.1    Valentin-Weigand, P.2    Jerlström, P.G.3    Timmis, K.N.4    Chhatwal, G.S.5
  • 50
    • 0028018488 scopus 로고
    • Domain structure and conserved epitopes of Sfb protein, the fibronectin-binding adhesin of Streptococcus pyogenes
    • Talay, S.R., Valentin-Weigand, P., Timmis, K.N., and Chhatwal, G.S. (1994) Domain structure and conserved epitopes of Sfb protein, the fibronectin-binding adhesin of streptococcus pyogenes. Mol Microbiol 13:531-539.
    • (1994) Mol Microbiol , vol.13 , pp. 531-539
    • Talay, S.R.1    Valentin-Weigand, P.2    Timmis, K.N.3    Chhatwal, G.S.4
  • 51
    • 0001401601 scopus 로고
    • Practice and theory of enzyme immuno-assays
    • Burdon, R.H., and Van Knippenberg, R.H. (eds). Amsterdam: Elsevier
    • Tijssen, P. (1985) Practice and theory of enzyme immuno-assays. In Laboratory Techniques in Biochemistry and Molecular Biology. Burdon, R.H., and Van Knippenberg, R.H. (eds). Amsterdam: Elsevier.
    • (1985) Laboratory Techniques in Biochemistry and Molecular Biology
    • Tijssen, P.1
  • 52
    • 0027423484 scopus 로고
    • Adherence and fibronectin binding are environmentally regulated in the group A streptococci
    • Van Heyningen, T., Fogg, G., Yates, D., Hanski, E., and Caparon, M. (1993) Adherence and fibronectin binding are environmentally regulated in the group A streptococci. Mol Microbiol 9: 1213-1222.
    • (1993) Mol Microbiol , vol.9 , pp. 1213-1222
    • Van Heyningen, T.1    Fogg, G.2    Yates, D.3    Hanski, E.4    Caparon, M.5
  • 53
    • 0029827151 scopus 로고    scopus 로고
    • Temperature regulation of the streptococcal pyrogenic exotoxin A-encoding gene (speA)
    • Xu, S., and Collins, C.M. (1996) Temperature regulation of the streptococcal pyrogenic exotoxin A-encoding gene (speA). Infect Immun 64: 5399-5402.
    • (1996) Infect Immun , vol.64 , pp. 5399-5402
    • Xu, S.1    Collins, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.