메뉴 건너뛰기




Volumn 4, Issue 3, 1998, Pages 298-302

Activation of the contact-phase system on bacterial surfaces - A clue to serious comlications in infections deseases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BLOOD CLOTTING FACTOR; BRADYKININ; CELL MEMBRANE PROTEIN;

EID: 2642635843     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0398-298     Document Type: Article
Times cited : (180)

References (27)
  • 2
    • 0024514997 scopus 로고
    • Kininogens, kinins and kinships
    • Müller-Esterl, W. Kininogens, kinins and kinships. Thromb. Haemost. 61, 2-6 (1989).
    • (1989) Thromb. Haemost. , vol.61 , pp. 2-6
    • Müller-Esterl, W.1
  • 3
    • 0022593032 scopus 로고
    • The contact activation system: Biochemistry and interactions of these surface-mediated defence reactions
    • Colman, R.W. & Schmaier, A.M. The contact activation system: Biochemistry and interactions of these surface-mediated defence reactions. Crit. Rev. Oncol. Hematol. 5, 57-85 (1986).
    • (1986) Crit. Rev. Oncol. Hematol. , vol.5 , pp. 57-85
    • Colman, R.W.1    Schmaier, A.M.2
  • 4
    • 0023201944 scopus 로고
    • The coagulation-kinin pathway of human plasma
    • Kaplan, A.P. & Silverberg, M. The coagulation-kinin pathway of human plasma, Blood 70, 1-15 (1987).
    • (1987) Blood , vol.70 , pp. 1-15
    • Kaplan, A.P.1    Silverberg, M.2
  • 5
    • 0027067804 scopus 로고
    • Bradykinin receptors: Pharmacological properties and biological roles
    • Hall, J.M. Bradykinin receptors: Pharmacological properties and biological roles. Pharmacol. Ther. 56, 131-190 (1992).
    • (1992) Pharmacol. Ther. , vol.56 , pp. 131-190
    • Hall, J.M.1
  • 6
    • 0024498519 scopus 로고
    • Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli
    • Olsén, A., Jonsson, A. & Normark, S. Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli. Naturells, 652-655 (1989).
    • (1989) Naturells , pp. 652-655
    • Olsén, A.1    Jonsson, A.2    Normark, S.3
  • 7
    • 0025833413 scopus 로고
    • Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis
    • Collinson, S.K., Emody, L., Müller, K.H., Trust, T.J. & Kay, W.W. Purification and characterization of thin, aggregative fimbriae from Salmonella enteritidis. J. Bacterial. 173, 4773-4781 (1991).
    • (1991) J. Bacterial. , vol.173 , pp. 4773-4781
    • Collinson, S.K.1    Emody, L.2    Müller, K.H.3    Trust, T.J.4    Kay, W.W.5
  • 8
    • 0027475041 scopus 로고
    • The RpoS sigma factor relieves H-NS-mediated transcriptional repression of csgA, the subunit gene of fibronectin-binding curli in Escherichia coli
    • Olsén, A., Arnqvist, A., Hammar, M., Sukupolvi, S. & Normark, S. The RpoS sigma factor relieves H-NS-mediated transcriptional repression of csgA, the subunit gene of fibronectin-binding curli in Escherichia coli. Mol. Microbiol. 7, 523-536 (1993).
    • (1993) Mol. Microbiol. , vol.7 , pp. 523-536
    • Olsén, A.1    Arnqvist, A.2    Hammar, M.3    Sukupolvi, S.4    Normark, S.5
  • 9
    • 0027434601 scopus 로고
    • Thin, aggregative fimbriae mediate binding of Salmonella enteritidis to fibronectin
    • Collinson, S.K., et al. Thin, aggregative fimbriae mediate binding of Salmonella enteritidis to fibronectin. J. Bacteriol. 175, 12-18 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 12-18
    • Collinson, S.K.1
  • 10
    • 0027942891 scopus 로고
    • Plasminogen, absorbed by Escherichia coli expressing curli or by Salmonella enteritidis expressing thin aggregative fimbriae, can be activated by simultaneously captured tissue-type plasminogen activator (t-PA)
    • Sjobring, U., Pohl, C. & Olsén, A. Plasminogen, absorbed by Escherichia coli expressing curli or by Salmonella enteritidis expressing thin aggregative fimbriae, can be activated by simultaneously captured tissue-type plasminogen activator (t-PA). Mol. Microbiol. 14, 443-452 (1994).
    • (1994) Mol. Microbiol. , vol.14 , pp. 443-452
    • Sjobring, U.1    Pohl, C.2    Olsén, A.3
  • 11
    • 0029889055 scopus 로고    scopus 로고
    • Assembly of human contact phase factors and release of bradykinin at the surface of curli-expressing Escherichia coli
    • Ben Nasr, A.B., Olsén, A., Sjobring, U., Müller-Esterl, W. & Björck, L. Assembly of human contact phase factors and release of bradykinin at the surface of curli-expressing Escherichia coli. Mol. Microbiol. 20, 927-935 (1996).
    • (1996) Mol. Microbiol , vol.20 , pp. 927-935
    • Ben Nasr, A.B.1    Olsén, A.2    Sjobring, U.3    Müller-Esterl, W.4    Björck, L.5
  • 13
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie, B. & Furie, B.C. The molecular basis of blood coagulation. Cell 53, 505-518 (1988).
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 15
    • 0026055774 scopus 로고
    • One-step chromogenk equivalent of activated partial thromboplastin time evaluated for clinical application
    • Ponjee, G.A., Vader, H.L., de Wild, P.J., Janssen, C.W. & van der Graaf, F. One-step chromogenk equivalent of activated partial thromboplastin time evaluated for clinical application. Clin. Chem. 37, 1235-1244 (1991).
    • (1991) Clin. Chem. , vol.37 , pp. 1235-1244
    • Ponjee, G.A.1    Vader, H.L.2    De Wild, P.J.3    Janssen, C.W.4    Van Der Graaf, F.5
  • 16
    • 0027413558 scopus 로고
    • Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen
    • Scott, C.F., Whitaker, E.J., Hammond, B.F. & Colman, R.W. Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen. J. Biol. Chem. 268, 7935-7942 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 7935-7942
    • Scott, C.F.1    Whitaker, E.J.2    Hammond, B.F.3    Colman, R.W.4
  • 17
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A novel virulence mechanism
    • Herwald, H., Collin, M., Müller-Esterl, W. & Björck, L. Streptococcal cysteine proteinase releases kinins: A novel virulence mechanism. J. Exp. Med. 184, 665-673 (1996).
    • (1996) J. Exp. Med. , vol.184 , pp. 665-673
    • Herwald, H.1    Collin, M.2    Müller-Esterl, W.3    Björck, L.4
  • 18
    • 0022453669 scopus 로고
    • Tn1721 derivatives for transposon mutagenesis, restriction mapping and nucleotide sequence analysis
    • Ubben, D. & Schmitt, R. Tn1721 derivatives for transposon mutagenesis, restriction mapping and nucleotide sequence analysis. Gene 41, 145-152 (1986).
    • (1986) Gene , vol.41 , pp. 145-152
    • Ubben, D.1    Schmitt, R.2
  • 19
    • 0017659539 scopus 로고
    • Hemagglutination of human group A erythrocytes by enterotoxigenic Escherichia coli isolated from adults with diarrhea: Correlation with colonization factor
    • Evans, D.G., Evans, D.J.J. & Tjoa, W. Hemagglutination of human group A erythrocytes by enterotoxigenic Escherichia coli isolated from adults with diarrhea: Correlation with colonization factor. Infect. Immun. 18, 330-337 (1977).
    • (1977) Infect. Immun. , vol.18 , pp. 330-337
    • Evans, D.G.1    Evans, D.J.J.2    Tjoa, W.3
  • 20
    • 0028034957 scopus 로고
    • The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain
    • Hasan, A.A., Cines, D.B., Zhang, J. & Schmaier, A.M. The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain, J. Biol. Chem. 269, 31822-31830 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 31822-31830
    • Hasan, A.A.1    Cines, D.B.2    Zhang, J.3    Schmaier, A.M.4
  • 21
    • 0025368839 scopus 로고
    • High molecular weight kininogenbinding site of prekallikrein probed by monoclonal antibodies
    • Hock, J., Vogel, R., Linke, R.P. & Müller-Esterl, W. High molecular weight kininogenbinding site of prekallikrein probed by monoclonal antibodies. J. Biol. Chem. 265, 12005-12011 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 12005-12011
    • Hock, J.1    Vogel, R.2    Linke, R.P.3    Müller-Esterl, W.4
  • 22
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril
    • Fraker, P.J. & Speck, S.C.J. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril. Biochem. Biophys. Res. Commun. 80, 849-857 (1978).
    • (1978) Biochem. Biophys. Res. Commun. , vol.80 , pp. 849-857
    • Fraker, P.J.1    Speck, S.C.J.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0020049505 scopus 로고
    • Simplified performance of amidolytic factor X assay
    • Egberg, N. & Heedman, P.A. Simplified performance of amidolytic factor X assay. Thromb. Res, 25, 437-440 (1982).
    • (1982) Thromb. Res , vol.25 , pp. 437-440
    • Egberg, N.1    Heedman, P.A.2
  • 25
    • 0021233424 scopus 로고
    • A functional photometric assay for plasma fibrinogen
    • Becker, U., Bartl, K. & Wahlefeld, A.W. A functional photometric assay for plasma fibrinogen. Thromb. Res. 35, 475-484 (1984).
    • (1984) Thromb. Res. , vol.35 , pp. 475-484
    • Becker, U.1    Bartl, K.2    Wahlefeld, A.W.3
  • 26
    • 0016796678 scopus 로고
    • Heparin cofactor activity measured with an amidolytic method
    • Odegard, O.R., Lie, M. & Abildgaard, U. Heparin cofactor activity measured with an amidolytic method. Thromb. Res. 6, 287-294 (1975).
    • (1975) Thromb. Res. , vol.6 , pp. 287-294
    • Odegard, O.R.1    Lie, M.2    Abildgaard, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.