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Volumn , Issue , 2011, Pages 637-651

The effect of bacterial toxins on platelet function

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EID: 79958072759     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-90-481-9295-3_36     Document Type: Chapter
Times cited : (2)

References (121)
  • 1
    • 35448968988 scopus 로고    scopus 로고
    • Comparison of the effects of macrolides, amoxicillin, ceftriaxone, doxycycline, tobramycin and fluoroquinolones, on the production of pneumolysin by Streptococcus pneumoniae in vitro
    • Anderson, R., Steel, H.C., Cockeran, R., von Gottberg, A., de Gouveia, L., Klugman, K.P., Mitchell, T.J., Feldman, C., 2007. Comparison of the effects of macrolides, amoxicillin, ceftriaxone, doxycycline, tobramycin and fluoroquinolones, on the production of pneumolysin by Streptococcus pneumoniae in vitro. J. Antimicrob. Chemother. 60, 1155-1158.
    • (2007) J. Antimicrob. Chemother , vol.60 , pp. 1155-1158
    • Anderson, R.1    Steel, H.C.2    Cockeran, R.3    Von Gottberg, A.4    De Gouveia, L.5    Klugman, K.P.6    Mitchell, T.J.7    Feldman, C.8
  • 3
    • 0025006396 scopus 로고
    • Staphylococcus aureus alpha-toxin attack on human platelets promotes assembly of the prothrombinase complex
    • Arvand, M., Bhakdi, S., Dahlback, B., Preissner, K.T., 1990. Staphylococcus aureus alpha-toxin attack on human platelets promotes assembly of the prothrombinase complex. J. Biol. Chem. 265, 14377-14381.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14377-14381
    • Arvand, M.1    Bhakdi, S.2    Dahlback, B.3    Preissner, K.T.4
  • 4
    • 0031656714 scopus 로고    scopus 로고
    • Molecular analysis of the capsule gene region of group A Streptococcus: The has AB genes are sufficient for capsule expression
    • Ashbaugh, C.D., Alberti, S., Wessels, M.R., 1998. Molecular analysis of the capsule gene region of group A Streptococcus: The has AB genes are sufficient for capsule expression. J. Bacteriol. 180, 4955-4959.
    • (1998) J. Bacteriol , vol.180 , pp. 4955-4959
    • Ashbaugh, C.D.1    Alberti, S.2    Wessels, M.R.3
  • 5
    • 30444436765 scopus 로고    scopus 로고
    • Platelet Toll-like receptor expression modulates lipopolysaccharide-induced thrombocytopenia and tumor necrosis factor-α production in vivo
    • Aslam, R., Speck, E.R., Kim, M., Crow, A.R., Bang, K.W.A., Nestel, F.P., Ni, H., Lazarus, A.H., Freedman, J., Semple, J.W., 2006. Platelet Toll-like receptor expression modulates lipopolysaccharide-induced thrombocytopenia and tumor necrosis factor-α production in vivo. Blood 107, 637-641.
    • (2006) Blood , vol.107 , pp. 637-641
    • Aslam, R.1    Speck, E.R.2    Kim, M.3    Crow, A.R.4    Bang, K.W.A.5    Nestel, F.P.6    Ni, H.7    Lazarus, A.H.8    Freedman, J.9    Semple, J.W.10
  • 6
    • 0033256554 scopus 로고    scopus 로고
    • Role of Staphylococcus aureus hemolytic toxin-alpha in pathogenesis of infectious endocarditis: Studies in vitro
    • Baliakina, E.V., Gerasimovskaia, E.V., Romanov, Iu.A., Atakhanov, Sh.E., 1999. Role of Staphylococcus aureus hemolytic toxin-alpha in pathogenesis of infectious endocarditis: studies in vitro. Ter. Arkh. 71, 28-31.
    • (1999) Ter. Arkh. , vol.71 , pp. 28-31
    • Baliakina, E.V.1    Gerasimovskaia, E.V.2    Romanov, I.A.3    Atakhanov, S.E.4
  • 7
    • 0030862228 scopus 로고    scopus 로고
    • Hyperproduction of alpha-toxin by Staphylococcus aureus results in paradoxically reduced virulence in experimental endocarditis: A host defense role for platelet microbicidal proteins
    • Bayer, A.S., Ramos, M.D., Menzies, B.E., Yeaman, M.R., Shen, A.J., Cheung, A.L., 1997. Hyperproduction of alpha-toxin by Staphylococcus aureus results in paradoxically reduced virulence in experimental endocarditis: A host defense role for platelet microbicidal proteins. Infect. Immun. 65, 4652-4660.
    • (1997) Infect. Immun. , vol.65 , pp. 4652-4660
    • Bayer, A.S.1    Ramos, M.D.2    Menzies, B.E.3    Yeaman, M.R.4    Shen, A.J.5    Cheung, A.L.6
  • 8
    • 0030911920 scopus 로고    scopus 로고
    • Differences in virulence for mice among Streptococcus pneumoniae strains of capsular types 2, 3, 4, 5, and 6 are not attributable to differences in pneumolysin production
    • Benton, K.A., Paton, J.C., Briles, D.E., 1997. Differences in virulence for mice among Streptococcus pneumoniae strains of capsular types 2, 3, 4, 5, and 6 are not attributable to differences in pneumolysin production. Infect. Immun. 65, 1237-1244.
    • (1997) Infect. Immun. , vol.65 , pp. 1237-1244
    • Benton, K.A.1    Paton, J.C.2    Briles, D.E.3
  • 9
    • 0028285166 scopus 로고
    • Synthetic lipopeptide Pam3CysSer(Lys)4 is an effective activator of human platelets
    • Berg, M., Offermanns, S., Seifert, R., Schultz, G., 1994. Synthetic lipopeptide Pam3CysSer(Lys)4 is an effective activator of human platelets. Am. J. Physiol. Cell Physiol. 266, C1684-C1691.
    • (1994) Am. J. Physiol. Cell Physiol , vol.266 , pp. C1684-C1691
    • Berg, M.1    Offermanns, S.2    Seifert, R.3    Schultz, G.4
  • 10
    • 0013852911 scopus 로고
    • Staphylococcal alpha toxin
    • Bernheimer, A.W., 1965. Staphylococcal alpha toxin. Ann. N.Y. Acad. Sci. 128, 112-123.
    • (1965) Ann. N.Y. Acad. Sci , vol.128 , pp. 112-123
    • Bernheimer, A.W.1
  • 11
    • 78651179134 scopus 로고
    • Effect of staphylococcal and other bacterial toxins on platelets in vitro
    • Bernheimer, A.W., Schwartz, L.L., 1965. Effect of staphylococcal and other bacterial toxins on platelets in vitro. J. Pathol. Bacteriol. 89, 209-223.
    • (1965) J. Pathol. Bacteriol , vol.89 , pp. 209-223
    • Bernheimer, A.W.1    Schwartz, L.L.2
  • 12
    • 0026811238 scopus 로고
    • Effect of insertional inactivation of the genes encoding pneumolysin and autolysin on the virulence of Streptococcus pneumoniae type 3
    • Berry, A.M., Paton, J.C., Hansman, D., 1992. Effect of insertional inactivation of the genes encoding pneumolysin and autolysin on the virulence of Streptococcus pneumoniae type 3. Microb. Pathog. 12, 87-93.
    • (1992) Microb. Pathog , vol.12 , pp. 87-93
    • Berry, A.M.1    Paton, J.C.2    Hansman, D.3
  • 13
    • 0024355265 scopus 로고
    • Reduced virulence of a defined pneumolysin-negative mutant of Streptococcus pneumoniae
    • Berry, A.M., Yother, J., Briles, D.E., Hansman, D., Paton, J.C., 1989. Reduced virulence of a defined pneumolysin-negative mutant of Streptococcus pneumoniae. Infect. Immun. 57, 2037-2042.
    • (1989) Infect. Immun. , vol.57 , pp. 2037-2042
    • Berry, A.M.1    Yother, J.2    Briles, D.E.3    Hansman, D.4    Paton, J.C.5
  • 14
    • 0346731246 scopus 로고    scopus 로고
    • How we detect microbes and respond to them: The Toll-like receptors and their transducers
    • Beutler, B., Hoebe, K., Du, X., Ulevitch, R.J., 2003. How we detect microbes and respond to them: The Toll-like receptors and their transducers. J. Leukoc. Biol. 74, 479-485.
    • (2003) J. Leukoc. Biol. , vol.74 , pp. 479-485
    • Beutler, B.1    Hoebe, K.2    Du, X.3    Ulevitch, R.J.4
  • 15
    • 0029916264 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: Prototypes of pore-forming bacterial cytolysins
    • Bhakdi, S., Bayley, H., Valeva, A., Walev, I., Walker, B., Kehoe, M., Palmer, M., 1996. Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch. Microbiol. 165, 73-79.
    • (1996) Arch. Microbiol , vol.165 , pp. 73-79
    • Bhakdi, S.1    Bayley, H.2    Valeva, A.3    Walev, I.4    Walker, B.5    Kehoe, M.6    Palmer, M.7
  • 17
    • 0030034479 scopus 로고    scopus 로고
    • Streptococcal infections of skin and soft tissues
    • Bisno, A.L., Stevens, D.L., 1996. Streptococcal infections of skin and soft tissues. N. Engl. J.Med. 334, 240-245.
    • (1996) N. Engl. J.Med , vol.334 , pp. 240-245
    • Bisno, A.L.1    Stevens, D.L.2
  • 18
    • 24644475670 scopus 로고    scopus 로고
    • Vascular dysfunction and ischemic destruction of tissue in Streptococcus pyogenes infection: The role of streptolysin O-induced platelet/neutrophil complexes
    • Bryant, A.E., Bayer, C.R., Chen, R.Y., Guth, P.H., Wallace, R.J., Stevens, D.L., 2005. Vascular dysfunction and ischemic destruction of tissue in Streptococcus pyogenes infection: The role of streptolysin O-induced platelet/neutrophil complexes. J. Infect. Dis. 192, 1014-1022.
    • (2005) J. Infect. Dis , vol.192 , pp. 1014-1022
    • Bryant, A.E.1    Bayer, C.R.2    Chen, R.Y.3    Guth, P.H.4    Wallace, R.J.5    Stevens, D.L.6
  • 20
    • 0034500018 scopus 로고    scopus 로고
    • Mechanisms of antibiotic resistance and tolerance in Streptococcus pneumoniae
    • Charpentier, E., Tuomanen, E., 2000. Mechanisms of antibiotic resistance and tolerance in Streptococcus pneumoniae. Microbes Infect. 2, 1855-1864.
    • (2000) Microbes Infect , vol.2 , pp. 1855-1864
    • Charpentier, E.1    Tuomanen, E.2
  • 22
    • 0037103529 scopus 로고    scopus 로고
    • Pneumolysin activates the synthesis and release of interleukin-8 by human neutrophils in vitro
    • Cockeran, R., Durandt, C., Feldman, C., Mitchell, T.J., Anderson, R., 2002. Pneumolysin activates the synthesis and release of interleukin-8 by human neutrophils in vitro. J. Infect. Dis. 186, 562-565.
    • (2002) J. Infect. Dis. , vol.186 , pp. 562-565
    • Cockeran, R.1    Durandt, C.2    Feldman, C.3    Mitchell, T.J.4    Anderson, R.5
  • 23
    • 0031025792 scopus 로고    scopus 로고
    • Analysis of 281, 797 consecutive blood cultures performed over an eight-year period: Trends in microorganisms isolated and the value of anaerobic culture of blood
    • Cockerill, F.R., Hughes, J.G., Vetter, E.A., Mueller, R.A., Weaver, A.L., Ilstrup, D.M., Rosenblatt, J.E., Wilson, W.R., 1997. Analysis of 281, 797 consecutive blood cultures performed over an eight-year period: Trends in microorganisms isolated and the value of anaerobic culture of blood. Clin. Infect. Dis. 24, 403-418.
    • (1997) Clin. Infect. Dis. , vol.24 , pp. 403-418
    • Cockerill, F.R.1    Hughes, J.G.2    Vetter, E.A.3    Mueller, R.A.4    Weaver, A.L.5    Ilstrup, D.M.6    Rosenblatt, J.E.7    Wilson, W.R.8
  • 25
    • 0031695246 scopus 로고    scopus 로고
    • Shiga toxin binds human platelets via globotriaosylceramide (Pk Antigen) and a novel platelet glycosphingolipid
    • Cooling, L.L.W., Walker, K.E., Gille, T., Koerner, T.A.W., 1998. Shiga toxin binds human platelets via globotriaosylceramide (Pk Antigen) and a novel platelet glycosphingolipid. Infect. Immun. 66, 4355-4366.
    • (1998) Infect. Immun , vol.66 , pp. 4355-4366
    • Cooling, L.L.W.1    Walker, K.E.2    Gille, T.3    Koerner, T.A.W.4
  • 26
    • 65649102674 scopus 로고    scopus 로고
    • Staphylococcus aureus bloodstream infections: Definitions and treatment
    • Corey, G.R., 2009. Staphylococcus aureus bloodstream infections: definitions and treatment. Clin. Infect. Dis. 48(Suppl 4), S254-S259.
    • (2009) Clin. Infect. Dis. , vol.48 , pp. S254-S259
    • Corey, G.R.1
  • 27
    • 0023881352 scopus 로고
    • Endotoxin-induced platelet activation in human whole blood in vitro
    • Csako, G., Suba, E., Elin, R., 1988. Endotoxin-induced platelet activation in human whole blood in vitro. Thromb. Haemost. 59, 378-382.
    • (1988) Thromb. Haemost , vol.59 , pp. 378-382
    • Csako, G.1    Suba, E.2    Elin, R.3
  • 29
    • 0031784033 scopus 로고    scopus 로고
    • Molecular basis for structural diversity in the core regions of the lipopolysaccharides of Escherichia coli and Salmonella enterica
    • David, E.H., Jeremy, A.Y., Chris, W., 1998. Molecular basis for structural diversity in the core regions of the lipopolysaccharides of Escherichia coli and Salmonella enterica. Mol. Micro. 30, 221-232.
    • (1998) Mol. Micro , vol.30 , pp. 221-232
    • David, E.H.1    Jeremy, A.Y.2    Chris, W.3
  • 30
    • 0019328405 scopus 로고
    • Toxic-shock syndrome: Epidemiologic features, recurrence, risk factors, and prevention
    • Davis, J.P., Chesney, P.J., Wand, P.J., LaVenture, M., 1980. Toxic-shock syndrome: epidemiologic features, recurrence, risk factors, and prevention. N. Engl. J. Med. 303, 1429-1435.
    • (1980) N. Engl. J. Med , vol.303 , pp. 1429-1435
    • Davis, J.P.1    Chesney, P.J.2    Wand, P.J.3    LaVenture, M.4
  • 31
    • 70449421592 scopus 로고    scopus 로고
    • Staphylococcal superantigen-like 5 activates platelets and supports platelet adhesion under flow conditions, which involves glycoprotein Ibα and αIIbβ3
    • de Haas, C., Weeterings, C., Vughs, M., de Groot, P.G., van Strijp, J., Lisman, T., 2009. Staphylococcal superantigen-like 5 activates platelets and supports platelet adhesion under flow conditions, which involves glycoprotein Ibα and αIIbβ3. J. Thromb. Haemostas. 7, 1867-1874.
    • (2009) J. Thromb. Haemostas , vol.7 , pp. 1867-1874
    • De Haas, C.1    Weeterings, C.2    Vughs, M.3    De Groot, P.G.4    Van Strijp, J.5    Lisman, T.6
  • 32
    • 71049125775 scopus 로고    scopus 로고
    • Role of Toll-like receptors 2 and 4 in pulmonary inflammation and injury induced by pneumolysin in mice
    • Dessing, M.C., Hirst, R.A., de Vos, A.F., van der Poll, T., 2009. Role of Toll-like receptors 2 and 4 in pulmonary inflammation and injury induced by pneumolysin in mice. PLoS One 4, e7993.
    • (2009) PLoS One , vol.4 , pp. e7993
    • Dessing, M.C.1    Hirst, R.A.2    De Vos, A.F.3    Van Der Poll, T.4
  • 33
    • 40449109127 scopus 로고    scopus 로고
    • Tolllike receptor 4 ligand can differentially modulate the release of cytokines by human platelets
    • Fabrice, C., Hind, H.-C., Sandrine, L., Olivier, D., Bruno, P., Archie, M., Olivier, G., 2008. Tolllike receptor 4 ligand can differentially modulate the release of cytokines by human platelets. Br. J. Haematol. 141, 84-91.
    • (2008) Br. J. Haematol , vol.141 , pp. 84-91
    • Fabrice, C.1    Hind, H.-C.2    Sandrine, L.3    Olivier, D.4    Bruno, P.5    Archie, M.6    Olivier, G.7
  • 34
    • 33646854563 scopus 로고    scopus 로고
    • The interaction of bacterial pathogens with platelets
    • Fitzgerald, J.R., Foster, T.J., Cox, D., 2006. The interaction of bacterial pathogens with platelets. Nat. Rev. Microbiol. 4, 445-457.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 445-457
    • Fitzgerald, J.R.1    Foster, T.J.2    Cox, D.3
  • 35
    • 66949139751 scopus 로고    scopus 로고
    • The gingipains: Scissors and glue of the periodontal pathogen, Porphyromonas gingivalis
    • Fitzpatrick, R.E., Wijeyewickrema, L.C., Pike, R.N., 2009. The gingipains: scissors and glue of the periodontal pathogen, Porphyromonas gingivalis. Future Microbiol. 4, 471-487.
    • (2009) Future Microbiol , vol.4 , pp. 471-487
    • Fitzpatrick, R.E.1    Wijeyewickrema, L.C.2    Pike, R.N.3
  • 36
    • 52049123299 scopus 로고    scopus 로고
    • The bacterial superantigen and superantigen-like proteins
    • Fraser, J., Proft, T., 2008. The bacterial superantigen and superantigen-like proteins. Immunol. Rev. 225, 226-243.
    • (2008) Immunol. Rev. , vol.225 , pp. 226-243
    • Fraser, J.1    Proft, T.2
  • 37
    • 44449120695 scopus 로고    scopus 로고
    • Intravenous Shiga toxin 2 promotes enteritis and renal injury characterized by polymorphonuclear leukocyte infiltration and thrombosis in Dutch Belted rabbits
    • García, A., Marini, R.P., Catalfamo, J.L., Knox, K.A., Schauer, D.B., Rogers, A.B., Fox, J.G., 2008. Intravenous Shiga toxin 2 promotes enteritis and renal injury characterized by polymorphonuclear leukocyte infiltration and thrombosis in Dutch Belted rabbits. Microbes Infect. 10, 650-656.
    • (2008) Microbes Infect. , vol.10 , pp. 650-656
    • García, A.1    Marini, R.P.2    Catalfamo, J.L.3    Knox, K.A.4    Schauer, D.B.5    Rogers, A.B.6    Fox, J.G.7
  • 38
    • 0024405234 scopus 로고
    • Effect of toxic shock syndrome toxin-1 on human hemostatic parameters
    • Gareau, R., Gruda, J., Micusan, V., 1989. Effect of toxic shock syndrome toxin-1 on human hemostatic parameters. Thromb. Res. 54, 349-356.
    • (1989) Thromb. Res. , vol.54 , pp. 349-356
    • Gareau, R.1    Gruda, J.2    Micusan, V.3
  • 41
    • 27844538829 scopus 로고    scopus 로고
    • Shiga toxin 2 and lipopolysaccharide cause monocytic THP-1 cells to release factors which activate platelet function
    • Guessous, F., Marcinkiewicz, M., Polanowska-Grabowska, R., Keepers, T., Obrig, T., Gear, A., 2005a. Shiga toxin 2 and lipopolysaccharide cause monocytic THP-1 cells to release factors which activate platelet function. Thromb. Haemost. 94, 1019-1027.
    • (2005) Thromb. Haemost. , vol.94 , pp. 1019-1027
    • Guessous, F.1    Marcinkiewicz, M.2    Polanowska-Grabowska, R.3    Keepers, T.4    Obrig, T.5    Gear, A.6
  • 42
    • 28444432684 scopus 로고    scopus 로고
    • Shiga Toxin 2 and lipopolysaccharide induce human microvascular endothelial cells to release chemokines and factors that stimulate platelet function
    • Guessous, F., Marcinkiewicz, M., Polanowska-Grabowska, R., Kongkhum, S., Heatherly, D., Obrig, T., Gear, A.R.L., 2005b. Shiga Toxin 2 and lipopolysaccharide induce human microvascular endothelial cells to release chemokines and factors that stimulate platelet function. Infect. Immun. 73, 8306-8316.
    • (2005) Infect. Immun. , vol.73 , pp. 8306-8316
    • Guessous, F.1    Marcinkiewicz, M.2    Polanowska-Grabowska, R.3    Kongkhum, S.4    Heatherly, D.5    Obrig, T.6    Gear, A.R.L.7
  • 43
    • 70349621788 scopus 로고    scopus 로고
    • Down-Regulation of platelet surface CD47 expression in Escherichia coli O157:H7 infection-induced thrombocytopenia
    • Guo, Y.-L., Liu, D.-Q., Bian, Z., Zhang, C.-Y., Zen, K., 2009. Down-Regulation of platelet surface CD47 expression in Escherichia coli O157:H7 infection-induced thrombocytopenia. PLoS ONE 4, e7131.
    • (2009) PLoS ONE , vol.4 , pp. e7131
    • Guo, Y.-L.1    Liu, D.-Q.2    Bian, Z.3    Zhang, C.-Y.4    Zen, K.5
  • 44
    • 68249146095 scopus 로고    scopus 로고
    • Aggregation and microparticle production through Toll-like receptor 4 activation in platelets from recently menopausal women
    • Hashimoto, K., Jayachandran, M., Owen, W., Miller, V., 2009. Aggregation and microparticle production through Toll-like receptor 4 activation in platelets from recently menopausal women. J. Cardiovasc. Pharmacol. 54, 57-62.
    • (2009) J. Cardiovasc. Pharmacol. , vol.54 , pp. 57-62
    • Hashimoto, K.1    Jayachandran, M.2    Owen, W.3    Miller, V.4
  • 45
    • 0025947639 scopus 로고
    • Staphylococcus aureus alpha-toxin dual mechanism of binding to target cells
    • Hildebrand, A., Pohl, M., Bhakdi, S., 1991. Staphylococcus aureus alpha-toxin. Dual mechanism of binding to target cells. J. Biol. Chem. 266, 17195-17200.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17195-17200
    • Hildebrand, A.1    Pohl, M.2    Bhakdi, S.3
  • 46
    • 0028176663 scopus 로고
    • Pneumolysin stimulates production of tumor necrosis factor alpha and interleukin-1 beta by human mononuclear phagocytes
    • Houldsworth, S., Andrew, P.W., Mitchell, T.J., 1994. Pneumolysin stimulates production of tumor necrosis factor alpha and interleukin-1 beta by human mononuclear phagocytes. Infect. Immun. 62, 1501-1503.
    • (1994) Infect. Immun. , vol.62 , pp. 1501-1503
    • Houldsworth, S.1    Andrew, P.W.2    Mitchell, T.J.3
  • 47
    • 79958077685 scopus 로고    scopus 로고
    • Staphylococcal superantigen-like 5 induces platelet activation and thrombosis via binding to GPIbα and GPVI
    • Hu, H., Peter, K., 2009. Staphylococcal superantigen-like 5 induces platelet activation and thrombosis via binding to GPIbα and GPVI. Circulation 120, S1080.
    • (2009) Circulation , vol.120 , pp. S1080
    • Hu, H.1    Peter, K.2
  • 48
    • 0022253233 scopus 로고
    • Conformational alteration in alpha-toxin from Staphylococcus aureus concomitant with the transformation of the water-soluble monomer to the membrane oligomer
    • Ikigai, H., Nakae, T., 1985. Conformational alteration in alpha-toxin from Staphylococcus aureus concomitant with the transformation of the water-soluble monomer to the membrane oligomer. Biochem. Biophys. Res. Commun. 130, 175-181.
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 175-181
    • Ikigai, H.1    Nakae, T.2
  • 49
    • 33845432462 scopus 로고    scopus 로고
    • Staphylococcal secretory inhibitor of platelet microbicidal protein is associated with prostatitis source
    • Ivanov, I.B., Gritsenko, V.A., Kuzmin, M.D., 2006. Staphylococcal secretory inhibitor of platelet microbicidal protein is associated with prostatitis source. J. Med. Microbiol. 55, 1645-1648.
    • (2006) J. Med. Microbiol. , vol.55 , pp. 1645-1648
    • Ivanov, I.B.1    Gritsenko, V.A.2    Kuzmin, M.D.3
  • 50
    • 33846160633 scopus 로고    scopus 로고
    • In vivo effects of lipopolysaccharide and TLR4 on platelet production and activity: Implications for thrombotic risk
    • Jayachandran, M., Brunn, G.J., Karnicki, K., Miller, R.S., Owen, W.G., Miller, V.M., 2007. In vivo effects of lipopolysaccharide and TLR4 on platelet production and activity: Implications for thrombotic risk. J. Appl. Physiol. 102, 429-433.
    • (2007) J. Appl. Physiol. , vol.102 , pp. 429-433
    • Jayachandran, M.1    Brunn, G.J.2    Karnicki, K.3    Miller, R.S.4    Owen, W.G.5    Miller, V.M.6
  • 51
    • 0019389568 scopus 로고
    • Effects of pneumolysin on human polymorphonuclear leukocytes and platelets
    • Johnson, M.K., Boese-Marrazzo, D., Pierce, W.A., 1981. Effects of pneumolysin on human polymorphonuclear leukocytes and platelets. Infect. Immun. 34, 171-176.
    • (1981) Infect. Immun. , vol.34 , pp. 171-176
    • Johnson, M.K.1    Boese-Marrazzo, D.2    Pierce, W.A.3
  • 52
    • 0018917907 scopus 로고
    • Binding of cholesterol by sulfhydryl-activated cytolysins
    • Johnson, M.K., Geoffroy, C., Alouf, J.E., 1980. Binding of cholesterol by sulfhydryl-activated cytolysins. Infect. Immun. 27, 97-101.
    • (1980) Infect. Immun. , vol.27 , pp. 97-101
    • Johnson, M.K.1    Geoffroy, C.2    Alouf, J.E.3
  • 53
    • 2142763016 scopus 로고    scopus 로고
    • CD4-T-lymphocyte interactions with pneumolysin and pneumococci suggest a crucial protective role in the host response to pneumococcal infection
    • Kadioglu, A., Coward, W., Colston, M.J., Hewitt, C.R., Andrew, P.W., 2004. CD4-T-lymphocyte interactions with pneumolysin and pneumococci suggest a crucial protective role in the host response to pneumococcal infection. Infect. Immun. 72, 2689-2697.
    • (2004) Infect. Immun , vol.72 , pp. 2689-2697
    • Kadioglu, A.1    Coward, W.2    Colston, M.J.3    Hewitt, C.R.4    Andrew, P.W.5
  • 54
    • 0023068574 scopus 로고
    • Production and purification of Streptococcus pneumoniae hemolysin (pneumolysin)
    • Kanclerski, K., Mollby, R., 1987. Production and purification of Streptococcus pneumoniae hemolysin (pneumolysin). J. Clin. Microbiol. 25, 222-225.
    • (1987) J. Clin. Microbiol , vol.25 , pp. 222-225
    • Kanclerski, K.1    Mollby, R.2
  • 55
    • 0035874529 scopus 로고    scopus 로고
    • Platelet activation by Shiga toxin and circulatory factors as a pathogenetic mechanism in the hemolytic uremic syndrome
    • Karpman, D., Papadopoulou, D., Nilsson, K., Sjogren, A.C., Mikaelsson, C., Lethagen, S., 2001. Platelet activation by Shiga toxin and circulatory factors as a pathogenetic mechanism in the hemolytic uremic syndrome. Blood 97, 3100-3108.
    • (2001) Blood , vol.97 , pp. 3100-3108
    • Karpman, D.1    Papadopoulou, D.2    Nilsson, K.3    Sjogren, A.C.4    Mikaelsson, C.5    Lethagen, S.6
  • 56
    • 0023491913 scopus 로고
    • Nucleotide sequence of the streptolysin O (SLO) gene: Structural homologies between SLO and other membrane-damaging, thiol-activated toxins
    • Kehoe, M.A., Miller, L., Walker, J.A., Boulnois, G.J., 1987. Nucleotide sequence of the streptolysin O (SLO) gene: structural homologies between SLO and other membrane-damaging, thiol-activated toxins. Infect. Immun. 55, 3228-3232.
    • (1987) Infect. Immun , vol.55 , pp. 3228-3232
    • Kehoe, M.A.1    Miller, L.2    Walker, J.A.3    Boulnois, G.J.4
  • 57
    • 38349100137 scopus 로고    scopus 로고
    • Platelet activation by Histophilus somni and its lipooligosaccharide induces endothelial cell proinflammatory responses and platelet internalization
    • Kuckleburg, C., McClenahan, D., Czuprynski, C., 2008a. Platelet activation by Histophilus somni and its lipooligosaccharide induces endothelial cell proinflammatory responses and platelet internalization. Shock 29, 189-196.
    • (2008) Shock , vol.29 , pp. 189-196
    • Kuckleburg, C.1    McClenahan, D.2    Czuprynski, C.3
  • 58
    • 38949147872 scopus 로고    scopus 로고
    • Endothelial cell apoptosis induced by bacteriaactivated platelets requires caspase-8 and -9 and generation of reactive oxygen species
    • Kuckleburg, C., Tiwari, R., Czuprynski, C., 2008b. Endothelial cell apoptosis induced by bacteriaactivated platelets requires caspase-8 and -9 and generation of reactive oxygen species. Thromb. Haemost. 99, 363-372.
    • (2008) Thromb. Haemost. , vol.99 , pp. 363-372
    • Kuckleburg, C.1    Tiwari, R.2    Czuprynski, C.3
  • 59
    • 11844256977 scopus 로고    scopus 로고
    • Bovine platelets activated by Haemophilus somnus and its LOS induce apoptosis in bovine endothelial cells
    • Kuckleburg, C.J., Sylte, M.J., Inzana, T.J., Corbeil, L.B., Darien, B.J., Czuprynski, C.J., 2005. Bovine platelets activated by Haemophilus somnus and its LOS induce apoptosis in bovine endothelial cells. Microb. Pathogen 38, 23-32.
    • (2005) Microb. Pathogen , vol.38 , pp. 23-32
    • Kuckleburg, C.J.1    Sylte, M.J.2    Inzana, T.J.3    Corbeil, L.B.4    Darien, B.J.5    Czuprynski, C.J.6
  • 60
    • 64849091225 scopus 로고    scopus 로고
    • Gram-positive toxic shock syndromes
    • Lappin, E., Ferguson, A.J., 2009. Gram-positive toxic shock syndromes. Lancet Infect. Dis. 9, 281-290.
    • (2009) Lancet Infect. Dis , vol.9 , pp. 281-290
    • Lappin, E.1    Ferguson, A.J.2
  • 61
    • 33749991856 scopus 로고    scopus 로고
    • Trends in detection of warfare agents: Detection methods for ricin, staphylococcal enterotoxin B and T-2 toxin
    • Ler, S.G., Lee, F.K., Gopalakrishnakone, P., 2006. Trends in detection of warfare agents: detection methods for ricin, staphylococcal enterotoxin B and T-2 toxin. J. Chromatog. A. 1133, 1-12.
    • (2006) J. Chromatog. A , vol.1133 , pp. 1-12
    • Ler, S.G.1    Lee, F.K.2    Gopalakrishnakone, P.3
  • 62
    • 3242781031 scopus 로고    scopus 로고
    • Osteomyelitis
    • Lew, D.P., Waldvogel, F.A., 2004. Osteomyelitis. Lancet 364, 369-379.
    • (2004) Lancet , vol.364 , pp. 369-379
    • Lew, D.P.1    Waldvogel, F.A.2
  • 63
  • 64
  • 65
    • 0030989690 scopus 로고    scopus 로고
    • The pneumococcal cell wall degrading enzymes: A modular design to create new lysins?
    • Lopez, R., Garcia, E., Garcia, P., Garcia, J.L., 1997. The pneumococcal cell wall degrading enzymes: A modular design to create new lysins? Microb. Drug Resist. 3, 199-211.
    • (1997) Microb. Drug Resist , vol.3 , pp. 199-211
    • Lopez, R.1    Garcia, E.2    Garcia, P.3    Garcia, J.L.4
  • 66
    • 0034923238 scopus 로고    scopus 로고
    • Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion
    • Lourbakos, A., Potempa, J., Travis, J., D'Andrea, M.R., Andrade-Gordon, P., Santulli, R., Mackie, E.J., Pike, R.N., 2001a. Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion. Infect. Immun. 69, 5121-5130.
    • (2001) Infect. Immun. , vol.69 , pp. 5121-5130
    • Lourbakos, A.1    Potempa, J.2    Travis, J.3    D'Andrea, M.R.4    Andrade-Gordon, P.5    Santulli, R.6    Mackie, E.J.7    Pike, R.N.8
  • 67
    • 0035877969 scopus 로고    scopus 로고
    • Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: A new trait in microbial pathogenicity
    • Lourbakos, A., Yuan, Y., Jenkins, A.L., Travis, J., Andrade-Gordon, P., Santulli, R., Potempa, J., Pike, R.N., 2001b. Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: A new trait in microbial pathogenicity. Blood 97, 3790-3797.
    • (2001) Blood , vol.97 , pp. 3790-3797
    • Lourbakos, A.1    Yuan, Y.2    Jenkins, A.L.3    Travis, J.4    Andrade-Gordon, P.5    Santulli, R.6    Potempa, J.7    Pike, R.N.8
  • 68
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy, F.D., 1998. Staphylococcus aureus infections. N. Engl. J. Med. 339, 520-532.
    • (1998) N. Engl. J. Med. , vol.339 , pp. 520-532
    • Lowy, F.D.1
  • 69
    • 63149104710 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Epidemiology, risk factors, and strategies for prevention
    • Lynch, J.P., Zhanel, G.G., 2009. Streptococcus pneumoniae: epidemiology, risk factors, and strategies for prevention. Semin. Respir. Crit. Care Med. 30, 189-209.
    • (2009) Semin. Respir. Crit. Care Med , vol.30 , pp. 189-209
    • Lynch, J.P.1    Zhanel, G.G.2
  • 71
    • 0014103859 scopus 로고
    • Platelet damaging factor, a fifth activity of staphylococcal alpha-toxin
    • Manohar, M., Maheswaran, S.K., Frommes, S.P., Lindorfer, R.K., 1967. Platelet damaging factor, a fifth activity of staphylococcal alpha-toxin. J. Bacteriol. 94, 224-231.
    • (1967) J. Bacteriol , vol.94 , pp. 224-231
    • Manohar, M.1    Maheswaran, S.K.2    Frommes, S.P.3    Lindorfer, R.K.4
  • 72
    • 0025879875 scopus 로고
    • Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute-phase protein
    • Mitchell, T.J., Andrew, P.W., Saunders, F.K., Smith, A.N., Boulnois, G.J., 1991. Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute-phase protein. Mol. Microbiol. 5, 1883-1888.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1883-1888
    • Mitchell, T.J.1    Andrew, P.W.2    Saunders, F.K.3    Smith, A.N.4    Boulnois, G.J.5
  • 74
    • 28444481356 scopus 로고    scopus 로고
    • Structure/function relationships of lipoteichoic acids
    • Morath, S., von Aulock, S., Hartung, T., 2005. Structure/function relationships of lipoteichoic acids. J. Endotoxin. Res. 11, 348-356.
    • (2005) J. Endotoxin. Res. , vol.11 , pp. 348-356
    • Morath, S.1    Von Aulock, S.2    Hartung, T.3
  • 75
    • 0347948546 scopus 로고    scopus 로고
    • Infective endocarditis
    • Moreillon, P., Que, Y.A., 2004. Infective endocarditis. Lancet 363, 139-149.
    • (2004) Lancet , vol.363 , pp. 139-149
    • Moreillon, P.1    Que, Y.A.2
  • 76
    • 0028062876 scopus 로고
    • Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form
    • Morgan, P.J., Hyman, S.C., Byron, O., Andrew, P.W., Mitchell, T.J., Rowe, A.J., 1994. Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. J. Biol. Chem. 269, 25315-25320.
    • (1994) J. Biol. Chem , vol.269 , pp. 25315-25320
    • Morgan, P.J.1    Hyman, S.C.2    Byron, O.3    Andrew, P.W.4    Mitchell, T.J.5    Rowe, A.J.6
  • 77
    • 54249109480 scopus 로고    scopus 로고
    • Inhibitory effects of staphylococcal enterotoxin type B on human platelet adhesion in vitro
    • Morganti, R., Marcondes, S., Baldasso, P., Marangoni, S., De Nucci, G., Antunes, E., 2008. Inhibitory effects of staphylococcal enterotoxin type B on human platelet adhesion in vitro. Platelets 19, 432-439.
    • (2008) Platelets , vol.19 , pp. 432-439
    • Morganti, R.1    Marcondes, S.2    Baldasso, P.3    Marangoni, S.4    De Nucci, G.5    Antunes, E.6
  • 78
    • 0035885951 scopus 로고    scopus 로고
    • Verotoxin-1-induced up-regulation of adhesive molecules renders microvascular endothelial cells thrombogenic at high shear stress
    • Morigi, M., Galbusera, M., Binda, E., Imberti, B., Gastoldi, S., Remuzzi, A., Zoja, C., Remuzzi, G., 2001. Verotoxin-1-induced up-regulation of adhesive molecules renders microvascular endothelial cells thrombogenic at high shear stress. Blood 98, 1828-1835.
    • (2001) Blood , vol.98 , pp. 1828-1835
    • Morigi, M.1    Galbusera, M.2    Binda, E.3    Imberti, B.4    Gastoldi, S.5    Remuzzi, A.6    Zoja, C.7    Remuzzi, G.8
  • 79
    • 0027506510 scopus 로고
    • Staphylococcus aureus bacteremia and endocarditis. New diagnostic and therapeutic concepts
    • Mortara, L.A., Bayer, A.S., 1993. Staphylococcus aureus bacteremia and endocarditis. New diagnostic and therapeutic concepts. Infect. Dis. Clin. North Am. 7, 53-68.
    • (1993) Infect. Dis. Clin. North Am , vol.7 , pp. 53-68
    • Mortara, L.A.1    Bayer, A.S.2
  • 80
    • 33645069437 scopus 로고    scopus 로고
    • Porphyromonas gingivalis-induced platelet aggregation in plasma depends on Hgp44 adhesin but not Rgp proteinase
    • Naito, M., Sakai, E., Shi, Y., Ideguchi, H., Shoji, M., Ohara, N., Yamamoto, K., Nakayama, K., 2006. Porphyromonas gingivalis-induced platelet aggregation in plasma depends on Hgp44 adhesin but not Rgp proteinase. Mol. Micro. 59, 152-167.
    • (2006) Mol. Micro. , vol.59 , pp. 152-167
    • Naito, M.1    Sakai, E.2    Shi, Y.3    Ideguchi, H.4    Shoji, M.5    Ohara, N.6    Yamamoto, K.7    Nakayama, K.8
  • 81
    • 51849088127 scopus 로고    scopus 로고
    • The periodontal pathogen Porphyromonas gingivalis sensitises human blood platelets to epinephrine
    • Nylander, M., Lindahl, T.L., Bengtsson, T., Grenegard, M., 2008. The periodontal pathogen Porphyromonas gingivalis sensitises human blood platelets to epinephrine. Platelets 19, 352-358.
    • (2008) Platelets , vol.19 , pp. 352-358
    • Nylander, M.1    Lindahl, T.L.2    Bengtsson, T.3    Grenegard, M.4
  • 83
    • 0023268257 scopus 로고
    • The mode of action of Shiga toxin on peptide elongation of eukaryotic protein synthesis
    • Obrig, T., Moran, T., Brown, J., 1987. The mode of action of Shiga toxin on peptide elongation of eukaryotic protein synthesis. Biochem. J. 244, 287-294.
    • (1987) Biochem. J , vol.244 , pp. 287-294
    • Obrig, T.1    Moran, T.2    Brown, J.3
  • 85
    • 0022460388 scopus 로고
    • Cloning and expression in Escherichia coli of the Streptococcus pneumoniae gene encoding pneumolysin
    • Paton, J.C., Berry, A.M., Lock, R.A., Hansman, D., Manning, P.A., 1986. Cloning and expression in Escherichia coli of the Streptococcus pneumoniae gene encoding pneumolysin. Infect. Immun. 54, 50-55.
    • (1986) Infect. Immun , vol.54 , pp. 50-55
    • Paton, J.C.1    Berry, A.M.2    Lock, R.A.3    Hansman, D.4    Manning, P.A.5
  • 86
    • 0020558325 scopus 로고
    • Inhibition of human polymorphonuclear leukocyte respiratory burst, bactericidal activity, and migration by pneumolysin
    • Paton, J.C., Ferrante, A., 1983. Inhibition of human polymorphonuclear leukocyte respiratory burst, bactericidal activity, and migration by pneumolysin. Infect. Immun. 41, 1212-1216.
    • (1983) Infect. Immun , vol.41 , pp. 1212-1216
    • Paton, J.C.1    Ferrante, A.2
  • 87
    • 0021363204 scopus 로고
    • Activation of human complement by the pneumococcal toxin pneumolysin
    • Paton, J.C., Rowan-Kelly, B., Ferrante, A., 1984. Activation of human complement by the pneumococcal toxin pneumolysin. Infect. Immun. 43, 1085-1087.
    • (1984) Infect. Immun. , vol.43 , pp. 1085-1087
    • Paton, J.C.1    Rowan-Kelly, B.2    Ferrante, A.3
  • 88
    • 0036189845 scopus 로고    scopus 로고
    • Aggregation of human platelets by gingipain-R from Porphyromonas gingivalis cells and membrane vesicles
    • Pham, K., Feik, D., Hammond, B.F., Rams, T.E., Whitaker, E.J., 2002. Aggregation of human platelets by gingipain-R from Porphyromonas gingivalis cells and membrane vesicles. Platelets 13, 21-30.
    • (2002) Platelets , vol.13 , pp. 21-30
    • Pham, K.1    Feik, D.2    Hammond, B.F.3    Rams, T.E.4    Whitaker, E.J.5
  • 89
    • 67349249343 scopus 로고    scopus 로고
    • Global serotype distribution among Streptococcus pneumoniae isolates causing otitis media in children: Potential implications for pneumococcal conjugate vaccines
    • Rodgers, G.L., Arguedas, A., Cohen, R., Dagan, R., 2009. Global serotype distribution among Streptococcus pneumoniae isolates causing otitis media in children: potential implications for pneumococcal conjugate vaccines. Vaccine 27, 3802-3810.
    • (2009) Vaccine , vol.27 , pp. 3802-3810
    • Rodgers, G.L.1    Arguedas, A.2    Cohen, R.3    Dagan, R.4
  • 90
    • 0027490912 scopus 로고
    • Tetrafibricin: A nonpeptidic fibrinogen receptor inhibitor from Streptomyces neyagawaensis (I) its GPIIb/IIIa blockage on solid phase binding assay
    • Satoh, T., Yamashita, Y., Kamiyama, T., Watanabe, J., Steiner, B., Hadváry, P., Arisawa, M., 1993. Tetrafibricin: A nonpeptidic fibrinogen receptor inhibitor from Streptomyces neyagawaensis (I) its GPIIb/IIIa blockage on solid phase binding assay. Thromb. Res. 72, 389-400.
    • (1993) Thromb. Res. , vol.72 , pp. 389-400
    • Satoh, T.1    Yamashita, Y.2    Kamiyama, T.3    Watanabe, J.4    Steiner, B.5    Hadváry, P.6    Arisawa, M.7
  • 92
    • 58649088469 scopus 로고    scopus 로고
    • Protease-activated receptors in cardiovascular health and diseases
    • Shah, R., 2009. Protease-activated receptors in cardiovascular health and diseases. Am. Heart J. 157, 253-262.
    • (2009) Am. Heart J. , vol.157 , pp. 253-262
    • Shah, R.1
  • 93
    • 34547909609 scopus 로고    scopus 로고
    • Severe streptococcal infection is associated with M protein-induced platelet activation and thrombus formation
    • Shannon, O., Hertzen, E., Norrby-Teglund, A., Morgelin, M., Sjobring, U., Bjorck, L., 2007. Severe streptococcal infection is associated with M protein-induced platelet activation and thrombus formation. Mol. Microbiol. 65, 1147-1157.
    • (2007) Mol. Microbiol , vol.65 , pp. 1147-1157
    • Shannon, O.1    Hertzen, E.2    Norrby-Teglund, A.3    Morgelin, M.4    Sjobring, U.5    Bjorck, L.6
  • 94
    • 51549106751 scopus 로고    scopus 로고
    • Lipopolysaccharide is a direct agonist for platelet RNA splicing
    • Shashkin, P.N., Brown, G.T., Ghosh, A., Marathe, G.K., McIntyre, T.M., 2008. Lipopolysaccharide is a direct agonist for platelet RNA splicing. J Immunol 181, 3495-3502.
    • (2008) J Immunol , vol.181 , pp. 3495-3502
    • Shashkin, P.N.1    Brown, G.T.2    Ghosh, A.3    Marathe, G.K.4    McIntyre, T.M.5
  • 95
    • 0034209772 scopus 로고    scopus 로고
    • Antiplatelet activity of Staphylococcus aureus lipoteichoic acid is mediated through a cyclic AMP pathway
    • Sheu, J.R., Hsiao, G., Lee, C., Chang, W., Lee, L.W., Su, C.H., Lin, C.H., 2000a. Antiplatelet activity of Staphylococcus aureus lipoteichoic acid is mediated through a cyclic AMP pathway. Thromb. Res. 99, 249-258.
    • (2000) Thromb. Res , vol.99 , pp. 249-258
    • Sheu, J.R.1    Hsiao, G.2    Lee, C.3    Chang, W.4    Lee, L.W.5    Su, C.H.6    Lin, C.H.7
  • 96
    • 0034018372 scopus 로고    scopus 로고
    • Mechanisms involved in the antiplatelet activity of Staphylococcus aureus lipoteichoic acid in human platelets
    • Sheu, J.R., Lee, C.R., Lin, C.H., Hsiao, G., Ko, W.C., Chen, Y.C., Yen, M.H., 2000b. Mechanisms involved in the antiplatelet activity of Staphylococcus aureus lipoteichoic acid in human platelets. Thromb. Haemost. 83, 777-784.
    • (2000) Thromb. Haemost , vol.83 , pp. 777-784
    • Sheu, J.R.1    Lee, C.R.2    Lin, C.H.3    Hsiao, G.4    Ko, W.C.5    Chen, Y.C.6    Yen, M.H.7
  • 97
    • 0032833607 scopus 로고    scopus 로고
    • Complementdependent accumulation and degradation of platelets in the lung and liver induced by injection of lipopolysaccharides
    • Shibazaki, M., Kawabata, Y., Yokochi, T., Nishida, A., Takada, H., Endo, Y., 1999. Complementdependent accumulation and degradation of platelets in the lung and liver induced by injection of lipopolysaccharides. Infect. Immun. 67, 5186-5191.
    • (1999) Infect. Immun , vol.67 , pp. 5186-5191
    • Shibazaki, M.1    Kawabata, Y.2    Yokochi, T.3    Nishida, A.4    Takada, H.5    Endo, Y.6
  • 99
    • 42149118561 scopus 로고    scopus 로고
    • Critical involvement of pneumolysin in production of interleukin-1α and caspase-1- dependent cytokines in infection with Streptococcus pneumoniae in vitro: A novel function of pneumolysin in caspase-1 activation
    • Shoma, S., Tsuchiya, K., Kawamura, I., Nomura, T., Hara, H., Uchiyama, R., Daim, S., Mitsuyama, M., 2008. Critical involvement of pneumolysin in production of interleukin-1α and caspase-1- dependent cytokines in infection with Streptococcus pneumoniae in vitro: A novel function of pneumolysin in caspase-1 activation. Infect. Immun. 76, 1547-1557.
    • (2008) Infect. Immun. , vol.76 , pp. 1547-1557
    • Shoma, S.1    Tsuchiya, K.2    Kawamura, I.3    Nomura, T.4    Hara, H.5    Uchiyama, R.6    Daim, S.7    Mitsuyama, M.8
  • 100
    • 76549158997 scopus 로고
    • Action of staphylococcal toxin on human platelets
    • Siegel, I., Cohen, S., 1964. Action of staphylococcal toxin on human platelets. J. Infect. Dis. 114, 488-502.
    • (1964) J. Infect. Dis. , vol.114 , pp. 488-502
    • Siegel, I.1    Cohen, S.2
  • 101
    • 0041767440 scopus 로고    scopus 로고
    • Reduced release of pneumolysin by Streptococcus pneumoniae in vitro and in vivo after treatment with nonbacteriolytic antibiotics in comparison to ceftriaxone
    • Spreer, A., Kerstan, H., Bottcher, T., Gerber, J., Siemer, A., Zysk, G., Mitchell, T.J., Eiffert, H., Nau, R., 2003. Reduced release of pneumolysin by Streptococcus pneumoniae in vitro and in vivo after treatment with nonbacteriolytic antibiotics in comparison to ceftriaxone. Antimicrob. Agents Chemother. 47, 2649-2654.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 2649-2654
    • Spreer, A.1    Kerstan, H.2    Bottcher, T.3    Gerber, J.4    Siemer, A.5    Zysk, G.6    Mitchell, T.J.7    Eiffert, H.8    Nau, R.9
  • 102
    • 70349180857 scopus 로고    scopus 로고
    • Shiga toxin and lipopolysaccharide induce platelet-leukocyte aggregates and tissue factor release, a thrombotic mechanism in hemolytic uremic syndrome
    • Stahl, A., Sartz, L., Nelsson, A., Bekassy, Z., Karpman, D., 2009. Shiga toxin and lipopolysaccharide induce platelet-leukocyte aggregates and tissue factor release, a thrombotic mechanism in hemolytic uremic syndrome. PLoS One 4, e6990.
    • (2009) PLoS One , vol.4 , pp. e6990
    • Stahl, A.1    Sartz, L.2    Nelsson, A.3    Bekassy, Z.4    Karpman, D.5
  • 103
    • 33645579382 scopus 로고    scopus 로고
    • Lipopolysaccharide from enterohemorrhagic Escherichia coli binds to platelets through TLR4 and CD62 and is detected on circulating platelets in patients with hemolytic uremic syndrome
    • Stahl, A.-l., Svensson, M., Morgelin, M., Svanborg, C., Tarr, P.I., Mooney, J.C., Watkins, S.L., Johnson, R., Karpman, D., 2006. Lipopolysaccharide from enterohemorrhagic Escherichia coli binds to platelets through TLR4 and CD62 and is detected on circulating platelets in patients with hemolytic uremic syndrome. Blood 108, 167-176.
    • (2006) Blood , vol.108 , pp. 167-176
    • Stahl, A.-L.1    Svensson, M.2    Morgelin, M.3    Svanborg, C.4    Tarr, P.I.5    Mooney, J.C.6    Watkins, S.L.7    Johnson, R.8    Karpman, D.9
  • 104
    • 0024340460 scopus 로고
    • Severe group A streptococcal infections associated with a toxic shock-like syndrome and scarlet fever toxin A
    • Stevens, D.L., Tanner, M.H., Winship, J., Swarts, R., Ries, K.M., Schlievert, P.M., Kaplan, E., 1989. Severe group A streptococcal infections associated with a toxic shock-like syndrome and scarlet fever toxin A. N. Engl. J. Med. 321, 1-7.
    • (1989) N. Engl. J. Med , vol.321 , pp. 1-7
    • Stevens, D.L.1    Tanner, M.H.2    Winship, J.3    Swarts, R.4    Ries, K.M.5    Schlievert, P.M.6    Kaplan, E.7
  • 105
    • 0033524449 scopus 로고    scopus 로고
    • A natural variant of the cysteine protease virulence factor of group A Streptococcus with an arginine-glycine-aspartic acid (RGD) motif preferentially binds human integrins αVβ3 and αIIbβ3
    • Stockbauer, K.E., Magoun, L., Liu, M., Burns, E.H., Gubba, S., Renish, S., Pan, X., Bodary, S.C., Baker, E., Coburn, J., Leong, J.M., Musser, J.M., 1999. A natural variant of the cysteine protease virulence factor of group A Streptococcus with an arginine-glycine-aspartic acid (RGD) motif preferentially binds human integrins αVβ3 and αIIbβ3. Proc. Natl. Acad. Sci. U.S.A. 96, 242-247.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 242-247
    • Stockbauer, K.E.1    Magoun, L.2    Liu, M.3    Burns, E.H.4    Gubba, S.5    Renish, S.6    Pan, X.7    Bodary, S.C.8    Baker, E.9    Coburn, J.10    Leong, J.M.11    Musser, J.M.12
  • 106
    • 0032795615 scopus 로고    scopus 로고
    • Staging of the baboon response to group A streptococci administered intramuscularly: A descriptive study of the clinical symptoms and clinical chemical response patterns
    • Taylor, F.B. Jr., Bryant, A.E., Blick, K.E., Hack, E., Jansen, P.M., Kosanke, S.D., Stevens, D.L., 1999. Staging of the baboon response to group A streptococci administered intramuscularly: A descriptive study of the clinical symptoms and clinical chemical response patterns. Clin. Infect. Dis. 29, 167-177.
    • (1999) Clin. Infect. Dis. , vol.29 , pp. 167-177
    • Taylor, F.B.1    Bryant, A.E.2    Blick, K.E.3    Hack, E.4    Jansen, P.M.5    Kosanke, S.D.6    Stevens, D.L.7
  • 108
    • 0032820504 scopus 로고    scopus 로고
    • Shiga toxins do not directly stimulate alpha-granule secretion or enhance aggregation of human platelets
    • Thorpe, C.M., Flaumenhaft, R., Hurley, B., Jacewicz, M., Acheson, D.W.K., Keusch, G.T., 1999. Shiga toxins do not directly stimulate alpha-granule secretion or enhance aggregation of human platelets. Acta Haematologica 102, 51-55.
    • (1999) Acta Haematologica , vol.102 , pp. 51-55
    • Thorpe, C.M.1    Flaumenhaft, R.2    Hurley, B.3    Jacewicz, M.4    Acheson, D.W.K.5    Keusch, G.T.6
  • 109
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • Tilley, S.J., Orlova, E.V., Gilbert, R.J., Andrew, P.W., Saibil, H.R., 2005. Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121, 247-256.
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.J.3    Andrew, P.W.4    Saibil, H.R.5
  • 110
    • 33646842255 scopus 로고    scopus 로고
    • Staphylococcal enterotoxin B initiates protein kinase C translocation and eicosanoid metabolism while inhibiting thrombininduced aggregation in human platelets
    • Tran, U., Boyle, T., Shupp, J., Hammamieh, R., Jett, M., 2006. Staphylococcal enterotoxin B initiates protein kinase C translocation and eicosanoid metabolism while inhibiting thrombininduced aggregation in human platelets. Mol. Cell. Biochem. 288, 171-178.
    • (2006) Mol. Cell. Biochem. , vol.288 , pp. 171-178
    • Tran, U.1    Boyle, T.2    Shupp, J.3    Hammamieh, R.4    Jett, M.5
  • 111
    • 0029924449 scopus 로고    scopus 로고
    • Molecular architecture of a toxin pore: A 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin
    • Valeva, A., Weisser, A., Walker, B., Kehoe, M., Bayley, H., Bhakdi, S., Palmer, M., 1996. Molecular architecture of a toxin pore: A 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin. EMBO J. 15, 1857-1864.
    • (1996) EMBO J , vol.15 , pp. 1857-1864
    • Valeva, A.1    Weisser, A.2    Walker, B.3    Kehoe, M.4    Bayley, H.5    Bhakdi, S.6    Palmer, M.7
  • 112
    • 70350498834 scopus 로고    scopus 로고
    • Pathogenesis, treatment, and prevention of pneumococcal pneumonia
    • van der Poll, T., Opal, S.M., 2009. Pathogenesis, treatment, and prevention of pneumococcal pneumonia. Lancet 374, 1543-1556.
    • (2009) Lancet , vol.374 , pp. 1543-1556
    • Van Der Poll, T.1    Opal, S.M.2
  • 113
    • 0023251174 scopus 로고
    • Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae
    • Walker, J.A., Allen, R.L., Falmagne, P., Johnson, M.K., Boulnois, G.J., 1987. Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae. Infect. Immun. 55, 1184-1189.
    • (1987) Infect. Immun , vol.55 , pp. 1184-1189
    • Walker, J.A.1    Allen, R.L.2    Falmagne, P.3    Johnson, M.K.4    Boulnois, G.J.5
  • 114
    • 27144467146 scopus 로고    scopus 로고
    • Agonists of toll-like receptor (TLR)2 and TLR4 are unable to modulate platelet activation by adenosine diphosphate and platelet activating factor
    • Ward, J.R., Bingle, L., Judge, H.M., Brown, S.B., Storey, R.F., Whyte, M.K., Dower, S.K., Buttle, D.J., Sabroe, I., 2005. Agonists of toll-like receptor (TLR)2 and TLR4 are unable to modulate platelet activation by adenosine diphosphate and platelet activating factor. Thromb. Haemost. 94, 831-838.
    • (2005) Thromb. Haemost , vol.94 , pp. 831-838
    • Ward, J.R.1    Bingle, L.2    Judge, H.M.3    Brown, S.B.4    Storey, R.F.5    Whyte, M.K.6    Dower, S.K.7    Buttle, D.J.8    Sabroe, I.9
  • 115
    • 0016121927 scopus 로고
    • Effects of the ionophore A23187 on blood platelets I. Influence on aggregation and secretion
    • White, J., Rao, G., Gerrard, J., 1974. Effects of the ionophore A23187 on blood platelets I. Influence on aggregation and secretion. Am. J. Pathol. 77, 135-149.
    • (1974) Am. J. Pathol. , vol.77 , pp. 135-149
    • White, J.1    Rao, G.2    Gerrard, J.3
  • 116
    • 0024465561 scopus 로고
    • An investigation into the effects of bacterial lipopolysaccharide on human platelets
    • Whitworth, N., Barradas, M., Mikhailidis, D., Dandona, P., 1989. An investigation into the effects of bacterial lipopolysaccharide on human platelets. Eur. J. Haematol. 43, 112-119.
    • (1989) Eur. J. Haematol. , vol.43 , pp. 112-119
    • Whitworth, N.1    Barradas, M.2    Mikhailidis, D.3    Dandona, P.4
  • 117
    • 0034965669 scopus 로고    scopus 로고
    • Effects in humans of intravenously administered endotoxin on soluble cell-adhesion molecule and inflammatory markers: A model of human diseases
    • Wilson, M., Blum, R., Dandona, P., Mousa, S., 2001. Effects in humans of intravenously administered endotoxin on soluble cell-adhesion molecule and inflammatory markers: A model of human diseases. Clin. Exper. Pharmacol. Physiol. 28, 376-380.
    • (2001) Clin. Exper. Pharmacol. Physiol , vol.28 , pp. 376-380
    • Wilson, M.1    Blum, R.2    Dandona, P.3    Mousa, S.4
  • 119
    • 33748098214 scopus 로고    scopus 로고
    • Antimicrobial peptides versus invasive infections
    • Yeaman, M., Bayer, A., 2006. Antimicrobial peptides versus invasive infections. Curr. Top. Microbiol. Immunol. 306, 111-152.
    • (2006) Curr. Top. Microbiol. Immunol , vol.306 , pp. 111-152
    • Yeaman, M.1    Bayer, A.2
  • 120
    • 0031984629 scopus 로고    scopus 로고
    • Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action
    • Yeaman, M.R., Bayer, A.S., Koo, S.P., Foss, W., Sullam, P.M., 1998. Platelet microbicidal proteins and neutrophil defensin disrupt the Staphylococcus aureus cytoplasmic membrane by distinct mechanisms of action. J. Clin. Invest. 101, 178-187.
    • (1998) J. Clin. Invest. , vol.101 , pp. 178-187
    • Yeaman, M.R.1    Bayer, A.S.2    Koo, S.P.3    Foss, W.4    Sullam, P.M.5
  • 121
    • 41649115159 scopus 로고    scopus 로고
    • TLR2 - promiscuous or specific? A critical re-evaluation of a receptor expressing apparent broad specificity
    • Zähringer, U., Lindner, B., Inamura, S., Heine, H., Alexander, C., 2008. TLR2 - promiscuous or specific? A critical re-evaluation of a receptor expressing apparent broad specificity. Immunobiology 213, 205-224.
    • (2008) Immunobiology , vol.213 , pp. 205-224
    • Zähringer, U.1    Lindner, B.2    Inamura, S.3    Heine, H.4    Alexander, C.5


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