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MeSH Review

Pasteurella

 
 
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Disease relevance of Pasteurella

 

High impact information on Pasteurella

  • Pasteurella canis was the most common isolate of dog bites, and Past. multocida subspecies multocida and septica were the most common isolates of cat bites [6].
  • More from the pesky Pasteurella [7].
  • The N-terminal half of CNF2 showed striking homology (27% identity and 80% conserved residues) to the N-terminal portion of Pasteurella multocida toxin [8].
  • We show that the C-terminal 70 amino acids of leukotoxin from Pasteurella hemolytica can substitute functionally for the HlyA signal sequence [9].
  • Treatment of the cells with O-sialoglycoprotease from Pasteurella haemolytica, an enzyme that selectively cleaves mucin-type O-linked glycoproteins, reduced binding to purified P- and L-selectin in all cases [10].
 

Chemical compound and disease context of Pasteurella

  • Molecular directionality of polysaccharide polymerization by the Pasteurella multocida hyaluronan synthase [11].
  • The sequence of the pmHS enzyme is not very similar to the vertebrate heparin/heparan sulfate glycosyltransferases, EXT1 and 2, or to other Pasteurella glycosaminoglycan synthases that produce hyaluronan or chondroitin [12].
  • Treatment of Swiss 3T3 cells with a subsaturating concentration of recombinant Pasteurella multocida toxin (rPMT) markedly potentiated the production of inositol phosphates induced by bombesin, vasopressin, and endothelin but not by platelet-derived growth factor (PDGF) (AA and BB homodimers) [13].
  • Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins [14].
  • The intracellularly acting Pasteurella multocida toxin (PMT) is a potent mitogen that stimulates Gq-dependent formation of inositol trisphosphate [15].
 

Biological context of Pasteurella

 

Anatomical context of Pasteurella

 

Gene context of Pasteurella

 

Analytical, diagnostic and therapeutic context of Pasteurella

References

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  8. Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers. Oswald, E., Sugai, M., Labigne, A., Wu, H.C., Fiorentini, C., Boquet, P., O'Brien, A.D. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
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  10. Differential colon cancer cell adhesion to E-, P-, and L-selectin: role of mucin-type glycoproteins. Mannori, G., Crottet, P., Cecconi, O., Hanasaki, K., Aruffo, A., Nelson, R.M., Varki, A., Bevilacqua, M.P. Cancer Res. (1995) [Pubmed]
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  12. Identification and molecular cloning of a heparosan synthase from Pasteurella multocida type D. DeAngelis, P.L., White, C.L. J. Biol. Chem. (2002) [Pubmed]
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  15. Pasteurella multocida toxin facilitates inositol phosphate formation by bombesin through tyrosine phosphorylation of G alpha q. Baldwin, M.R., Pullinger, G.D., Lax, A.J. J. Biol. Chem. (2003) [Pubmed]
  16. Rapid chemoenzymatic synthesis of monodisperse hyaluronan oligosaccharides with immobilized enzyme reactors. DeAngelis, P.L., Oatman, L.C., Gay, D.F. J. Biol. Chem. (2003) [Pubmed]
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  19. A new tetracycline resistance determinant, Tet H, from Pasteurella multocida specifying active efflux of tetracycline. Hansen, L.M., McMurry, L.M., Levy, S.B., Hirsh, D.C. Antimicrob. Agents Chemother. (1993) [Pubmed]
  20. A heptosyltransferase mutant of Pasteurella multocida produces a truncated lipopolysaccharide structure and is attenuated in virulence. Harper, M., Cox, A.D., St Michael, F., Wilkie, I.W., Boyce, J.D., Adler, B. Infect. Immun. (2004) [Pubmed]
  21. Pasteurella haemolytica leukotoxin-induced increase in phospholipase A2 activity in bovine neutrophils. Wang, Z., Clarke, C., Clinkenbeard, K. Infect. Immun. (1998) [Pubmed]
  22. Induction of inflammatory cytokines in bovine alveolar macrophages following stimulation with Pasteurella haemolytica lipopolysaccharide. Yoo, H.S., Maheswaran, S.K., Lin, G., Townsend, E.L., Ames, T.R. Infect. Immun. (1995) [Pubmed]
  23. Enhanced adhesion of Pasteurella multocida to cultured turkey peripheral blood monocytes. Pruimboom, I.M., Rimler, R.B., Ackermann, M.R. Infect. Immun. (1999) [Pubmed]
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