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MeSH Review

Streptococcus bovis

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Disease relevance of Streptococcus bovis


High impact information on Streptococcus bovis


Chemical compound and disease context of Streptococcus bovis


Biological context of Streptococcus bovis


Anatomical context of Streptococcus bovis


Gene context of Streptococcus bovis


Analytical, diagnostic and therapeutic context of Streptococcus bovis


  1. Infective endocarditis caused by Streptococcus bovis resistant to the lethal effect of penicillin G. Savitch, C.B., Barry, A.L., Hoeprich, P.D. Arch. Intern. Med. (1978) [Pubmed]
  2. In vitro activity and beta-lactamase stability of FK-037, a parenteral cephalosporin. Neu, H.C., Chin, N.X., Huang, H.B. Antimicrob. Agents Chemother. (1993) [Pubmed]
  3. In-vitro activity of WIN 57273 compared to the activity of other fluoroquinolones and two beta-lactam antibiotics. Chin, N.X., Neu, H.C. J. Antimicrob. Chemother. (1991) [Pubmed]
  4. Formation of a clear zone on tannin-treated brain heart infusion agar by a Streptococcus sp. isolated from feces of koalas. Osawa, R. Appl. Environ. Microbiol. (1990) [Pubmed]
  5. Identification and characterization of the proBA operon of Streptococcus bovis. Campanile, C., Forlani, G., Basso, A.L., Marasco, R., Ricca, E., Sacco, M., Ferrara, L., De Felice, M. Appl. Environ. Microbiol. (1993) [Pubmed]
  6. In vitro activity of telithromycin against viridans group streptococci and Streptococcus bovis isolated from blood: antimicrobial susceptibility patterns in different groups of species. Rodríguez-Avial, I., Rodríguez-Avial, C., Culebras, E., Picazo, J.J. Antimicrob. Agents Chemother. (2005) [Pubmed]
  7. High prevalence of inducible erythromycin resistance among Streptococcus bovis isolates in Taiwan. Teng, L.J., Hsueh, P.R., Ho, S.W., Luh, K.T. Antimicrob. Agents Chemother. (2001) [Pubmed]
  8. Meningitis caused by Streptococcus in adults. Lerner, P.I. J. Infect. Dis. (1975) [Pubmed]
  9. Molecular characterization of CcpA and involvement of this protein in transcriptional regulation of lactate dehydrogenase and pyruvate formate-lyase in the ruminal bacterium Streptococcus bovis. Asanuma, N., Yoshii, T., Hino, T. Appl. Environ. Microbiol. (2004) [Pubmed]
  10. Ability of lysozyme and 2-deoxyglucose to differentiate human and bovine Streptococcus bovis strains. Kurtovic, A., Jarvis, G.N., Mantovani, H.C., Russell, J.B. J. Clin. Microbiol. (2003) [Pubmed]
  11. Low-affinity, high-capacity system of glucose transport in the ruminal bacterium Streptococcus bovis: evidence for a mechanism of facilitated diffusion. Russell, J.B. Appl. Environ. Microbiol. (1990) [Pubmed]
  12. Presumptive speciation of Streptococcus bovis and other group D streptococci from human sources by using arginine and pyruvate tests. Gross, K.C., Houghton, M.P., Senterfit, L.B. J. Clin. Microbiol. (1975) [Pubmed]
  13. Characterization of the L-malate permease gene (maeP) of Streptococcus bovis ATCC 15352. Kawai, S., Suzuki, H., Yamamoto, K., Kumagai, H. J. Bacteriol. (1997) [Pubmed]
  14. Relationship between intracellular phosphate, proton motive force, and rate of nongrowth energy dissipation (energy spilling) in Streptococcus bovis JB1. Bond, D.R., Russell, J.B. Appl. Environ. Microbiol. (1998) [Pubmed]
  15. Purification and characterization of a malic enzyme from the ruminal bacterium Streptococcus bovis ATCC 15352 and cloning and sequencing of its gene. Kawai, S., Suzuki, H., Yamamoto, K., Inui, M., Yukawa, H., Kumagai, H. Appl. Environ. Microbiol. (1996) [Pubmed]
  16. Protonmotive force regulates the membrane conductance of Streptococcus bovis in a non-ohmic fashion. Bond, D.R., Russell, J.B. Microbiology (Reading, Engl.) (2000) [Pubmed]
  17. The glutamine cyclotransferase reaction of Streptococcus bovis: a novel mechanism of deriving energy from non-oxidative and non-reductive deamination. Cook, G.M., Russell, J.B. FEMS Microbiol. Lett. (1993) [Pubmed]
  18. Effect of growth conditions on the Streptococcus bovis phosphoenolpyruvate glucose phosphotransferase system. Moore, G.A., Martin, S.A. J. Anim. Sci. (1991) [Pubmed]
  19. Phenotypic characterization of CO2-requiring strains of Streptococcus bovis from koalas. Osawa, R., Sly, L.I. Appl. Environ. Microbiol. (1991) [Pubmed]
  20. Adherence of glucan-positive and glucan-negative strains of Streptococcus bovis to human epithelial cells. Von Hunolstein, C., Ricci, M.L., Orefici, G. J. Med. Microbiol. (1993) [Pubmed]
  21. Determination of the sugar sequences and the glycosidic-bond arrangements of immunogenic heteroglycans. Pazur, J.H., Forsberg, L.S. Carbohydr. Res. (1978) [Pubmed]
  22. Purification and characterization of the extracellular alpha-amylase from Streptococcus bovis JB1. Freer, S.N. Appl. Environ. Microbiol. (1993) [Pubmed]
  23. Application of the extracellular alpha-amylase gene from Streptococcus bovis 148 to construction of a secretion vector for yogurt starter strains. Satoh, E., Ito, Y., Sasaki, Y., Sasaki, T. Appl. Environ. Microbiol. (1997) [Pubmed]
  24. Molecular characterization and expression of pyruvate formate-lyase-activating enzyme in a ruminal bacterium, Streptococcus bovis. Asanuma, N., Hino, T. Appl. Environ. Microbiol. (2002) [Pubmed]
  25. Structure and transcriptional regulation of the gene encoding pyruvate formate-lyase of a ruminal bacterium, Streptococcus bovis. Asanuma, N., Iwamoto, M., Hino, T. Microbiology (Reading, Engl.) (1999) [Pubmed]
  26. Bovicin HC5, a bacteriocin from Streptococcus bovis HC5. Mantovani, H.C., Hu, H., Worobo, R.W., Russell, J.B. Microbiology (Reading, Engl.) (2002) [Pubmed]
  27. Taxonomic dissection of the Streptococcus bovis group by analysis of manganese-dependent superoxide dismutase gene (sodA) sequences: reclassification of 'Streptococcus infantarius subsp. coli' as Streptococcus lutetiensis sp. nov. and of Streptococcus bovis biotype 11.2 as Streptococcus pasteurianus sp. nov. Poyart, C., Quesne, G., Trieu-Cuot, P. Int. J. Syst. Evol. Microbiol. (2002) [Pubmed]
  28. Effects of a strain of Saccharomyces cerevisiae (Levucell SC1), a microbial additive for ruminants, on lactate metabolism in vitro. Chaucheyras, F., Fonty, G., Bertin, G., Salmon, J.M., Gouet, P. Can. J. Microbiol. (1996) [Pubmed]
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