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Volumn 74, Issue 10, 2006, Pages 5625-5635

The transcriptional regulator RovS controls the attachment of Streptococcus agalactiae to human epithelial cells and the expression of virulence genes

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FIBRINOGEN RECEPTOR; PROTEIN CYL; PROTEIN FBSA; PROTEIN GBS0230; PROTEIN ROGB; PROTEIN SODA; UNCLASSIFIED DRUG;

EID: 33749237158     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.00667-06     Document Type: Article
Times cited : (39)

References (52)
  • 1
    • 0003086414 scopus 로고
    • Group B streptococcal infections
    • J. S. Remington and J. O. Klein (ed.). The W. B. Saunders Co., Philadelphia, Pa.
    • Baker, C. J., and M. S. Edwards. 1995. Group B streptococcal infections, p. 980-1054. In J. S. Remington and J. O. Klein (ed.), Infectious disease of the fetus and newborn infant. The W. B. Saunders Co., Philadelphia, Pa.
    • (1995) Infectious Disease of the Fetus and Newborn Infant , pp. 980-1054
    • Baker, C.J.1    Edwards, M.S.2
  • 2
    • 0036266052 scopus 로고    scopus 로고
    • Identification of novel adhesins from group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding
    • Beckmann, C., J. D. Waggoner, T. O. Harris, G. S. Tamura, and C. E. Rubens. 2002. Identification of novel adhesins from group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding. Infect. Immun. 70:2869-2876.
    • (2002) Infect. Immun. , vol.70 , pp. 2869-2876
    • Beckmann, C.1    Waggoner, J.D.2    Harris, T.O.3    Tamura, G.S.4    Rubens, C.E.5
  • 3
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge, A., and L. Björck. 1995. Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J. Biol. Chem. 270:9862-9867.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9862-9867
    • Berge, A.1    Björck, L.2
  • 4
    • 0028061282 scopus 로고
    • Promoter structure, promoter recognition, and transcription activation in prokaryotes
    • Busby, S. A., and R. H. Ebright. 1994. Promoter structure, promoter recognition, and transcription activation in prokaryotes. Cell 79:743-746.
    • (1994) Cell , vol.79 , pp. 743-746
    • Busby, S.A.1    Ebright, R.H.2
  • 5
    • 6044244836 scopus 로고    scopus 로고
    • Rgg regulates growth phase-dependent expression of proteins associated with secondary metabolism and stress in Streptococcus pyogenes
    • Chaussee, M. A., E. A. Callegari, and M. S. Chaussee. 2004. Rgg regulates growth phase-dependent expression of proteins associated with secondary metabolism and stress in Streptococcus pyogenes. J. Bacteriol. 186:7091-7099.
    • (2004) J. Bacteriol. , vol.186 , pp. 7091-7099
    • Chaussee, M.A.1    Callegari, E.A.2    Chaussee, M.S.3
  • 6
    • 0033041979 scopus 로고    scopus 로고
    • The rgg gene of Streptococcus pyogenes NZ131 positively influences extracellular SPE B production
    • Chaussee, M. S., D. Ajdic, and J. J. Ferretti. 1999. The rgg gene of Streptococcus pyogenes NZ131 positively influences extracellular SPE B production. Infect. Immun. 67:1715-1722.
    • (1999) Infect. Immun. , vol.67 , pp. 1715-1722
    • Chaussee, M.S.1    Ajdic, D.2    Ferretti, J.J.3
  • 7
    • 0036153610 scopus 로고    scopus 로고
    • Rgg influences the expression of multiple regulatory loci to coregulate virulence factor expression in Streptococcus pyogenes
    • Chaussee, M. S., G. L. Sylva, D. E. Sturdevant, L. M. Smoot, M. R. Graham, R. O. Watson, and J. M. Musser. 2002. Rgg influences the expression of multiple regulatory loci to coregulate virulence factor expression in Streptococcus pyogenes. Infect. Immun. 70:762-770.
    • (2002) Infect. Immun. , vol.70 , pp. 762-770
    • Chaussee, M.S.1    Sylva, G.L.2    Sturdevant, D.E.3    Smoot, L.M.4    Graham, M.R.5    Watson, R.O.6    Musser, J.M.7
  • 8
    • 0035139884 scopus 로고    scopus 로고
    • Identification of Rgg-regulated exoproteins of Streptococcus pyogenes
    • Chaussee, M. S., R. O. Watson, J. C. Smoot, and J. M. Musser. 2001. Identification of Rgg-regulated exoproteins of Streptococcus pyogenes. Infect. Immun. 69:822-831.
    • (2001) Infect. Immun. , vol.69 , pp. 822-831
    • Chaussee, M.S.1    Watson, R.O.2    Smoot, J.C.3    Musser, J.M.4
  • 9
    • 0141960369 scopus 로고    scopus 로고
    • Rgg coordinates virulence factor synthesis and metabolism in Streptococcus pyogenes
    • Chaussee, M. S., G. A. Somerville, L. Reitzer, and J. M. Musser. 2003. Rgg coordinates virulence factor synthesis and metabolism in Streptococcus pyogenes. J. Bacteriol. 185:6016-6024.
    • (2003) J. Bacteriol. , vol.185 , pp. 6016-6024
    • Chaussee, M.S.1    Somerville, G.A.2    Reitzer, L.3    Musser, J.M.4
  • 10
    • 0027220749 scopus 로고
    • Inactivation of the streptococcal erythrogenic toxin B gene (speB) in Streptococcus pyogenes
    • Chaussee, M. S., D. Gerlach, C.-E. Yu, and J. J. Ferretti. 1993. Inactivation of the streptococcal erythrogenic toxin B gene (speB) in Streptococcus pyogenes. Infect. Immun. 61:3719-3723.
    • (1993) Infect. Immun. , vol.61 , pp. 3719-3723
    • Chaussee, M.S.1    Gerlach, D.2    Yu, C.-E.3    Ferretti, J.J.4
  • 11
    • 0036117970 scopus 로고    scopus 로고
    • The group B streptococcal C5a peptidase is both a specific protease and an invasin
    • Cheng, Q., D. Stafslien, S. S. Purushothaman, and P. Cleary. 2002. The group B streptococcal C5a peptidase is both a specific protease and an invasin. Infect. Immun. 70:2408-2413.
    • (2002) Infect. Immun. , vol.70 , pp. 2408-2413
    • Cheng, Q.1    Stafslien, D.2    Purushothaman, S.S.3    Cleary, P.4
  • 12
    • 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
  • 13
    • 0037080038 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin/cytolysin promotes invasion of human lung epithelial cells and the release of interleukin-8
    • Doran, K. S., J. C. Chang, V. M. Benoit, I. Eckmann, and V. Nizet. 2002. Group B streptococcal beta-hemolysin/cytolysin promotes invasion of human lung epithelial cells and the release of interleukin-8. J. Infect. Dis. 185:196-203.
    • (2002) J. Infect. Dis. , vol.185 , pp. 196-203
    • Doran, K.S.1    Chang, J.C.2    Benoit, V.M.3    Eckmann, I.4    Nizet, V.5
  • 14
    • 0026305697 scopus 로고
    • Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor
    • Dubendorff, J. W., and F. W. Studier. 1991. Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor. J. Mol. Biol. 219:45-59.
    • (1991) J. Mol. Biol. , vol.219 , pp. 45-59
    • Dubendorff, J.W.1    Studier, F.W.2
  • 15
    • 0001656006 scopus 로고
    • Neonatal sepsis and other infections due to group B beta-hemolytic streptococci
    • Eickhoff, T. C., J. O. Klein, K. L. Daly, D. I. Ingall, and M. Finland. 1964. Neonatal sepsis and other infections due to group B beta-hemolytic streptococci. N. Engl. J. Med. 271:1221-1228.
    • (1964) N. Engl. J. Med. , vol.271 , pp. 1221-1228
    • Eickhoff, T.C.1    Klein, J.O.2    Daly, K.L.3    Ingall, D.I.4    Finland, M.5
  • 17
    • 0042324298 scopus 로고    scopus 로고
    • Analysis of RogB-controlled virulence mechanisms and gene repression in Streptococcus agalactiae
    • Gutekunst, H., B. J. Eikmanns, and D. J. Reinscheid. 2003. Analysis of RogB-controlled virulence mechanisms and gene repression in Streptococcus agalactiae. Infect. Immun. 71:5056-5064.
    • (2003) Infect. Immun. , vol.71 , pp. 5056-5064
    • Gutekunst, H.1    Eikmanns, B.J.2    Reinscheid, D.J.3
  • 18
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1985. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1985) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 20
    • 17044377416 scopus 로고    scopus 로고
    • Virulence role of group B Streptococcus beta-hemolysin/cytolysin in a neonatal rabbit model of early-onset pulmonary infection
    • Hensler, M. E., G. Y. Liu, S. Sobczak, K. Benirschke, V. Nizet, and G. P. Heldt. 2005. Virulence role of group B Streptococcus beta-hemolysin/cytolysin in a neonatal rabbit model of early-onset pulmonary infection. J. Infect. Dis. 191:1287-1291.
    • (2005) J. Infect. Dis. , vol.191 , pp. 1287-1291
    • Hensler, M.E.1    Liu, G.Y.2    Sobczak, S.3    Benirschke, K.4    Nizet, V.5    Heldt, G.P.6
  • 22
    • 0027262508 scopus 로고
    • Protein-protein communication within the transcription apparatus
    • Ishihama, A. 1993. Protein-protein communication within the transcription apparatus. J. Bacteriol. 175:2483-2489.
    • (1993) J. Bacteriol. , vol.175 , pp. 2483-2489
    • Ishihama, A.1
  • 23
    • 0033815580 scopus 로고    scopus 로고
    • 2+) permease in Streptococcus gordonii is regulated by a diphtheria toxin metallorepressor-like protein ScaR
    • 2+) permease in Streptococcus gordonii is regulated by a diphtheria toxin metallorepressor-like protein ScaR. Mol. Microbiol. 38:140-153.
    • (2000) Mol. Microbiol. , vol.38 , pp. 140-153
    • Jakubovics, N.S.1    Smith, A.W.2    Jenkinson, H.F.3
  • 24
    • 0027893017 scopus 로고
    • A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
    • Kapur, V., S. Topouzis, M. W. Jajesky, L.-L. Li, M. R. Hamrick, R. J. Patti, and J. M. Musser. 1993. A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin. Microb. Pathog. 15:327-346.
    • (1993) Microb. Pathog. , vol.15 , pp. 327-346
    • Kapur, V.1    Topouzis, S.2    Jajesky, M.W.3    Li, L.-L.4    Hamrick, M.R.5    Patti, R.J.6    Musser, J.M.7
  • 25
    • 0027931766 scopus 로고
    • Vaccination with streptococcal extracellular cysteine protease (interleukin-1 beta convertase) protects mice against challenge with heterologous group a streptococci
    • Kapur, V., J. T. Maffei, R. S. Greer, L.-L. Li, G. J. Adams, and J. M. Musser. 1994. Vaccination with streptococcal extracellular cysteine protease (interleukin-1 beta convertase) protects mice against challenge with heterologous group A streptococci. Microb. Pathog. 16:443-450.
    • (1994) Microb. Pathog. , vol.16 , pp. 443-450
    • Kapur, V.1    Maffei, J.T.2    Greer, R.S.3    Li, L.-L.4    Adams, G.J.5    Musser, J.M.6
  • 26
    • 0025457662 scopus 로고
    • Analysis of the diurnal expression patterns of the tomato chlorophyll a/b binding protein genes. Influence of light and characterization of the gene family
    • Kellmann, J.-W., E. Piechersky, and B. Piechulla. 1990. Analysis of the diurnal expression patterns of the tomato chlorophyll a/b binding protein genes. Influence of light and characterization of the gene family. Phytochem. Phytobiol. 52:35-41.
    • (1990) Phytochem. Phytobiol. , vol.52 , pp. 35-41
    • Kellmann, J.-W.1    Piechersky, E.2    Piechulla, B.3
  • 27
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon, W. R., C. M. Gibson, and M. G. Caparon. 1998. A role for trigger factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J. 17:6263-6275.
    • (1998) EMBO J. , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 28
    • 0041387460 scopus 로고    scopus 로고
    • Role of RopB in growth phase expression of the SpeB cysteine protease of Streptococcus pyogenes
    • Neely, M. N., W. R. Lyon, D. L. Runft, and M. Caparon. 2003. Role of RopB in growth phase expression of the SpeB cysteine protease of Streptococcus pyogenes. J. Bacteriol. 185:5166-5174.
    • (2003) J. Bacteriol. , vol.185 , pp. 5166-5174
    • Neely, M.N.1    Lyon, W.R.2    Runft, D.L.3    Caparon, M.4
  • 29
    • 0030870211 scopus 로고    scopus 로고
    • A matrix form of fibronectin mediates enhanced binding of Streptococcus pyogenes to host tissue
    • Okada, N., M. Watarai, V. Ozeri, E. Hanski, M. Caparon, and C. Sasakawa. 1997. A matrix form of fibronectin mediates enhanced binding of Streptococcus pyogenes to host tissue. J. Biol. Chem. 272:26978-26984.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26978-26984
    • Okada, N.1    Watarai, M.2    Ozeri, V.3    Hanski, E.4    Caparon, M.5    Sasakawa, C.6
  • 30
    • 0029320145 scopus 로고
    • A versatile quick-prep of genomic DNA from gram-positive bacteria
    • Pospiech, A., and B. Neumann. 1995. A versatile quick-prep of genomic DNA from gram-positive bacteria. Trends Genet. 11:217-218.
    • (1995) Trends Genet. , vol.11 , pp. 217-218
    • Pospiech, A.1    Neumann, B.2
  • 31
    • 0035685114 scopus 로고    scopus 로고
    • Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus agalactiae involves a novel two-component regulatory system
    • Poyart, C., M. C. Lamy, C. Boumaila, F. Fiedler, and P. Trieu-Cuot. 2001. Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus agalactiae involves a novel two-component regulatory system. J. Bacteriol. 183:6324-6334.
    • (2001) J. Bacteriol. , vol.183 , pp. 6324-6334
    • Poyart, C.1    Lamy, M.C.2    Boumaila, C.3    Fiedler, F.4    Trieu-Cuot, P.5
  • 32
    • 0034924910 scopus 로고    scopus 로고
    • Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae
    • Poyart, C., E. Pellegrini, O. Gaillot, C. Boumaila, M. Baptista, and P. Trieu-Cuot. 2001. Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae. Infect. Immun. 69:5098-5106.
    • (2001) Infect. Immun. , vol.69 , pp. 5098-5106
    • Poyart, C.1    Pellegrini, E.2    Gaillot, O.3    Boumaila, C.4    Baptista, M.5    Trieu-Cuot, P.6
  • 33
    • 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
  • 34
    • 0033051428 scopus 로고    scopus 로고
    • Functional analyses of the promoters in the lantibiotic mutacin II biosynthetic locus in Streptococcus mutans
    • Qi, F., P. Chen, and P. W. Caufield. 1999. Functional analyses of the promoters in the lantibiotic mutacin II biosynthetic locus in Streptococcus mutans. Appl. Environ. Microbiol. 65:652-658.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 652-658
    • Qi, F.1    Chen, P.2    Caufield, P.W.3
  • 36
    • 1342325449 scopus 로고    scopus 로고
    • Relevance of peptide uptake systems to the physiology and virulence of Streptococcus agalactiae
    • Samen, U., B. Gottschalk, B. J. Eikmanns, and D. J. Reinscheid. 2004. Relevance of peptide uptake systems to the physiology and virulence of Streptococcus agalactiae. J. Bacteriol. 186:1398-1408.
    • (2004) J. Bacteriol. , vol.186 , pp. 1398-1408
    • Samen, U.1    Gottschalk, B.2    Eikmanns, B.J.3    Reinscheid, D.J.4
  • 37
    • 0031984335 scopus 로고    scopus 로고
    • A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation
    • Sanders, J. W., K. Leenhouts, J. Burghoorn, J. R. Brands, G. Venema, and J. Kok. 1998. A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation. Mol. Microbiol. 27:299-310.
    • (1998) Mol. Microbiol. , vol.27 , pp. 299-310
    • Sanders, J.W.1    Leenhouts, K.2    Burghoorn, J.3    Brands, J.R.4    Venema, G.5    Kok, J.6
  • 38
    • 0036428743 scopus 로고    scopus 로고
    • A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites
    • Schubert, A., K. Zakikhany, M. Schreiner, R. Frank, B. Spellerberg, B. J. Eikmanns, and D. J. Reinscheid. 2002. A fibrinogen receptor from group B Streptococcus interacts with fibrinogen by repetitive units with novel ligand binding sites. Mol. Microbiol. 46:557-569.
    • (2002) Mol. Microbiol. , vol.46 , pp. 557-569
    • Schubert, A.1    Zakikhany, K.2    Schreiner, M.3    Frank, R.4    Spellerberg, B.5    Eikmanns, B.J.6    Reinscheid, D.J.7
  • 42
    • 0032935929 scopus 로고    scopus 로고
    • Identification of genetic determinants for the hemolytic activity of Streptococcus agalactiae by ISS1 transposition
    • Spellerberg, B., B. Pohl, G. Haase, S. Martin, J. Weber-Heynemann, and R. Lütticken. 1999. Identification of genetic determinants for the hemolytic activity of Streptococcus agalactiae by ISS1 transposition. J. Bacteriol. 181:3212-3219.
    • (1999) J. Bacteriol. , vol.181 , pp. 3212-3219
    • Spellerberg, B.1    Pohl, B.2    Haase, G.3    Martin, S.4    Weber-Heynemann, J.5    Lütticken, R.6
  • 43
    • 0029796450 scopus 로고    scopus 로고
    • Rgg is a positive transcriptional regulator of the Streptococcus gordonii gtfG gene
    • Sulavik, M. C., and D. B. Clewell. 1996. Rgg is a positive transcriptional regulator of the Streptococcus gordonii gtfG gene. J. Bacteriol. 178:5826-5830.
    • (1996) J. Bacteriol. , vol.178 , pp. 5826-5830
    • Sulavik, M.C.1    Clewell, D.B.2
  • 44
    • 0026708281 scopus 로고
    • Identification of a gene, rgg, which regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis
    • Sulavik, M. C., G. Tardif, and D. B. Clewell. 1992. Identification of a gene, rgg, which regulates expression of glucosyltransferase and influences the Spp phenotype of Streptococcus gordonii Challis. J. Bacteriol. 174:3577-3586.
    • (1992) J. Bacteriol. , vol.174 , pp. 3577-3586
    • Sulavik, M.C.1    Tardif, G.2    Clewell, D.B.3
  • 45
    • 0034524338 scopus 로고    scopus 로고
    • Co-operative binding of human fibronectin to Sfb1 protein triggers streptococcal invasion into respiratory epithelial cells
    • Talay, S. R., A. Zock, M. Rohde, G. Molinari, M. Oggioni, G. Pozzi, C. A. Guzman, and G. S. Chhatwal. 2000. Co-operative binding of human fibronectin to Sfb1 protein triggers streptococcal invasion into respiratory epithelial cells. Cell. Microbiol. 2:521-535.
    • (2000) Cell. Microbiol. , vol.2 , pp. 521-535
    • Talay, S.R.1    Zock, A.2    Rohde, M.3    Molinari, G.4    Oggioni, M.5    Pozzi, G.6    Guzman, C.A.7    Chhatwal, G.S.8
  • 47
    • 0025861975 scopus 로고
    • Shuttle vectors containing a multiple cloning site and a lacZ alpha gene for conjugal transfer of DNA from Escherichia coli to gram-positive bacteria
    • Trieu-Cuot, P., C. Carlier, C. Poyart-Salmeron, and P. Courvalin. 1991. Shuttle vectors containing a multiple cloning site and a lacZ alpha gene for conjugal transfer of DNA from Escherichia coli to gram-positive bacteria. Gene 102:99-104.
    • (1991) Gene , vol.102 , pp. 99-104
    • Trieu-Cuot, P.1    Carlier, C.2    Poyart-Salmeron, C.3    Courvalin, P.4
  • 48
    • 0029975360 scopus 로고    scopus 로고
    • Entry and intracellular survival of group B streptococci in J774 macrophages
    • Valentin-Weigand, P., P. Benkel, M. Rohde, and G. S. Chhatwal. 1996. Entry and intracellular survival of group B streptococci in J774 macrophages. Infect. Immun. 64:2467-2473.
    • (1996) Infect. Immun. , vol.64 , pp. 2467-2473
    • Valentin-Weigand, P.1    Benkel, P.2    Rohde, M.3    Chhatwal, G.S.4
  • 49
    • 0036128730 scopus 로고    scopus 로고
    • Genetic analysis of the rgg-gtfG junctional region and its role in Streptococcus gordonii glucosyltransferase activity
    • Vickerman, M. M., and P. E. Minick. 2002. Genetic analysis of the rgg-gtfG junctional region and its role in Streptococcus gordonii glucosyltransferase activity. Infect. Immun. 70:1703-1714.
    • (2002) Infect. Immun. , vol.70 , pp. 1703-1714
    • Vickerman, M.M.1    Minick, P.E.2
  • 50
  • 51
    • 3242879355 scopus 로고    scopus 로고
    • PredictRegulon: A web server for the prediction of the regulatory protein binding sites and operons in prokaryote genomes
    • Yellboina, S., J. Seshadri, M. S. Kumar, and A. Ranjan. 2004. PredictRegulon: a web server for the prediction of the regulatory protein binding sites and operons in prokaryote genomes. Nucleic Acids Res. 32:W318-W320.
    • (2004) Nucleic Acids Res. , vol.32
    • Yellboina, S.1    Seshadri, J.2    Kumar, M.S.3    Ranjan, A.4
  • 52
    • 0027124375 scopus 로고
    • Group B streptococcal disease in the United States, 1990: Report from a multistate active surveillance system
    • Zangwill, K. M., A. Schuchat, and J. D. Wenger. 1992. Group B streptococcal disease in the United States, 1990: report from a multistate active surveillance system. Morb. Mortal. Wkly. Rep. CDC Surveill. Summ. 41:25-32.
    • (1992) Morb. Mortal. Wkly. Rep. CDC Surveill. Summ. , vol.41 , pp. 25-32
    • Zangwill, K.M.1    Schuchat, A.2    Wenger, J.D.3


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