메뉴 건너뛰기




Volumn 174, Issue 10, 2005, Pages 6299-6307

Binding of the complement inhibitor C4bp to serogroup B Neisseria meningitidis

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT; COMPLEMENT C4B INHIBITOR; COMPLEMENT INHIBITOR; POLYSIALIC ACID; PORIN A; PORIN B3; PROPERDIN; UNCLASSIFIED DRUG;

EID: 18644372663     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.174.10.6299     Document Type: Article
Times cited : (92)

References (51)
  • 1
    • 0033957876 scopus 로고    scopus 로고
    • Update on meningococcal disease with emphasis on pathogenesis and clinical management
    • van Deuren, M., P. Brandtzaeg, and J. W. van der Meer. 2000, Update on meningococcal disease with emphasis on pathogenesis and clinical management. Clin. Microbiol. Rev. 13: 144-166.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 144-166
    • Van Deuren, M.1    Brandtzaeg, P.2    Van Der Meer, J.W.3
  • 2
    • 0023272273 scopus 로고
    • An IgG monoclonal antibody to group B meningococci cross-reacts with developmemally regulated polysialic acid units of glycoproteins in neural and extraneural tissues
    • Finne, J., D. Bitter-Suermann, C. Goridis, and U. Finne. 1987. An IgG monoclonal antibody to group B meningococci cross-reacts with developmemally regulated polysialic acid units of glycoproteins in neural and extraneural tissues. J. Immunol. 138: 4402-4407.
    • (1987) J. Immunol. , vol.138 , pp. 4402-4407
    • Finne, J.1    Bitter-Suermann, D.2    Goridis, C.3    Finne, U.4
  • 5
    • 0030888166 scopus 로고    scopus 로고
    • Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis: Conformational stability and porin activity
    • Minetti, C. A. S. A., J. Y. Tai, M. S. Blake, J. K. Pullen, S. M. Liang, and D. P. Remeta. 1997. Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis: conformational stability and porin activity. J. Biol. Chem. 272: 10710-10720.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10710-10720
    • Minetti, C.A.S.A.1    Tai, J.Y.2    Blake, M.S.3    Pullen, J.K.4    Liang, S.M.5    Remeta, D.P.6
  • 6
    • 0032566609 scopus 로고    scopus 로고
    • Characterization of the structure, function, and conformational stability of PorB class 3 protein from Neisseria meningitidis: A porin with unusual physicochemical properties
    • Minetti, C. A. S. A., M. S. Blake, and D. P. Remeta. 1998. Characterization of the structure, function, and conformational stability of PorB class 3 protein from Neisseria meningitidis: a porin with unusual physicochemical properties. J. Biol. Chem. 273: 25329-25338.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25329-25338
    • Minetti, C.A.S.A.1    Blake, M.S.2    Remeta, D.P.3
  • 7
    • 0032954440 scopus 로고    scopus 로고
    • Structural and evolutionary inference from molecular variation in Neisseria porins
    • Derrick, J. P., R. Urwin, J. Suker, I. M. Feavers, and M. C. J. Maiden. 1999. Structural and evolutionary inference from molecular variation in Neisseria porins. Infect. Immun. 67: 2406-2413.
    • (1999) Infect. Immun. , vol.67 , pp. 2406-2413
    • Derrick, J.P.1    Urwin, R.2    Suker, J.3    Feavers, I.M.4    Maiden, M.C.J.5
  • 8
    • 0031767021 scopus 로고    scopus 로고
    • A gonococcal porA pseudogene: Implications for understanding the evolution and pathogenicity of Neisseria gonorrhoeae
    • Feavers, I. M., and M. C. J. Maiden. 1998. A gonococcal porA pseudogene: implications for understanding the evolution and pathogenicity of Neisseria gonorrhoeae. Mol. Microbiol. 30: 647-656.
    • (1998) Mol. Microbiol. , vol.30 , pp. 647-656
    • Feavers, I.M.1    Maiden, M.C.J.2
  • 9
    • 0023085007 scopus 로고
    • Sialic acid of group B Neisseria meningitidis regulates alternative complement pathway activation
    • Jarvis, G. A., and N. A. Vedros. 1987. Sialic acid of group B Neisseria meningitidis regulates alternative complement pathway activation. Infect. Immun. 55: 174-180.
    • (1987) Infect. Immun. , vol.55 , pp. 174-180
    • Jarvis, G.A.1    Vedros, N.A.2
  • 10
    • 0028364942 scopus 로고
    • Contribution of genes from the capsule gene complex (cps) to lipooligosaccharide biosynthesis and serum resistance in Neisseria meningitidis
    • Hammerschmidt, S., C. Birkholz, U. Zähringer, B. D. Robertson, J. van Putten, O. Ebeling, and M. Frosch. 1994. Contribution of genes from the capsule gene complex (cps) to lipooligosaccharide biosynthesis and serum resistance in Neisseria meningitidis. Mol. Microbiol. 11: 885-896.
    • (1994) Mol. Microbiol. , vol.11 , pp. 885-896
    • Hammerschmidt, S.1    Birkholz, C.2    Zähringer, U.3    Robertson, B.D.4    Van Putten, J.5    Ebeling, O.6    Frosch, M.7
  • 11
    • 0028260801 scopus 로고
    • Regulation of alternative pathway complement activation by glycosaminoglycans: Specificity of the polyanion binding site on factor H
    • Meri, S., and M. K. Pangburn. 1994. Regulation of alternative pathway complement activation by glycosaminoglycans: specificity of the polyanion binding site on factor H. Biochem. Biophys. Res. Commun. 198: 52-59.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 52-59
    • Meri, S.1    Pangburn, M.K.2
  • 12
    • 0035825093 scopus 로고    scopus 로고
    • Development of natural immunity to Neisseria meningitidis
    • Pollard, A. J., and C. Frasch. 2001. Development of natural immunity to Neisseria meningitidis. Vaccine 19: 1327-1346.
    • (2001) Vaccine , vol.19 , pp. 1327-1346
    • Pollard, A.J.1    Frasch, C.2
  • 13
    • 0036865204 scopus 로고    scopus 로고
    • Structural and functional studies of complement inhibitor C4b-binding protein
    • Blom, A. M. 2002. Structural and functional studies of complement inhibitor C4b-binding protein. Biochem. Soc. Transact. 30(Pt. 6): 978-982.
    • (2002) Biochem. Soc. Transact. , vol.30 , Issue.PART 6 , pp. 978-982
    • Blom, A.M.1
  • 14
    • 0035920160 scopus 로고    scopus 로고
    • Structural requirements for the complement regulatory activities of C4BP
    • Blom, A. M., L. Kask, and B. Dahlback. 2001. Structural requirements for the complement regulatory activities of C4BP. J. Biol. Chem. 276: 27136-27144.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27136-27144
    • Blom, A.M.1    Kask, L.2    Dahlback, B.3
  • 15
    • 0242646437 scopus 로고    scopus 로고
    • Bordetella pertussis binds the human complement regulator C4BP: Role of filamentous hemagglutinin
    • Berggård, K., E. Johnsson, F. R. Mooi, and G. Lindahl. 1997. Bordetella pertussis binds the human complement regulator C4BP: role of filamentous hemagglutinin. Infect. Immun. 65: 3638-3643.
    • (1997) Infect. Immun. , vol.65 , pp. 3638-3643
    • Berggård, K.1    Johnsson, E.2    Mooi, F.R.3    Lindahl, G.4
  • 16
    • 0030866740 scopus 로고    scopus 로고
    • Human C4BP binds to the hypervariable N-terminal region of many members in the streptococcal M protein family
    • Johnsson, E., A. Thern, B. Dahlback, L. O. Heden, M. Wikstrom, and G. Lindahl. 1997. Human C4BP binds to the hypervariable N-terminal region of many members in the streptococcal M protein family. Adv. Exp. Med. Biol. 418: 505-510.
    • (1997) Adv. Exp. Med. Biol. , vol.418 , pp. 505-510
    • Johnsson, E.1    Thern, A.2    Dahlback, B.3    Heden, L.O.4    Wikstrom, M.5    Lindahl, G.6
  • 17
    • 0036885109 scopus 로고    scopus 로고
    • A novel interaction of outer membrane protein A with C4b binding protein mediates serum resistance of Escherichia coli K1
    • Prasadarao, N. V., A. M. Blom. B. O. Villoutreix, and L. C. Linsangan. 2002. A novel interaction of outer membrane protein A with C4b binding protein mediates serum resistance of Escherichia coli K1. J. Immunol. 169: 6352-6360.
    • (2002) J. Immunol. , vol.169 , pp. 6352-6360
    • Prasadarao, N.V.1    Blom, A.M.2    Villoutreix, B.O.3    Linsangan, L.C.4
  • 18
    • 0141890189 scopus 로고    scopus 로고
    • Evasion of phagocytosis through cooperation between two ligand-binding regions in Streptococcus pyogenes M protein
    • Carlsson, F., K. Berggard, M. Stalhammar-Carlemalm, and G. Lindahl. 2003. Evasion of phagocytosis through cooperation between two ligand-binding regions in Streptococcus pyogenes M protein. J. Exp. Med. 198: 1057-1068.
    • (2003) J. Exp. Med. , vol.198 , pp. 1057-1068
    • Carlsson, F.1    Berggard, K.2    Stalhammar-Carlemalm, M.3    Lindahl, G.4
  • 20
    • 0020530378 scopus 로고
    • Purification of human C4b-binding protein and formation of its complex with vitamin K-dependent protein S
    • Dahlbäck, B. 1983. Purification of human C4b-binding protein and formation of its complex with vitamin K-dependent protein S. Biochem. J. 209: 847-856.
    • (1983) Biochem. J. , vol.209 , pp. 847-856
    • Dahlbäck, B.1
  • 21
    • 0035920160 scopus 로고    scopus 로고
    • Structural requirements for the complement regulatory activities of C4BP
    • Blom, A. M., L. Kask, and B. Dahlbäck. 2001. Structural requirements for the complement regulatory activities of C4BP. J. Biol. Chem. 276: 27136-27144.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27136-27144
    • Blom, A.M.1    Kask, L.2    Dahlbäck, B.3
  • 22
    • 0030890121 scopus 로고    scopus 로고
    • The amino-terminal module of the C4b-binding protein α-chain is crucial for C4b binding and factor I-cofactor function
    • Härdig, Y., A. Hillarp, and B. Dahlbäck. 1997. The amino-terminal module of the C4b-binding protein α-chain is crucial for C4b binding and factor I-cofactor function. Biochem. J. 323(Pt. 6): 469-475.
    • (1997) Biochem. J. , vol.323 , Issue.PART 6 , pp. 469-475
    • Härdig, Y.1    Hillarp, A.2    Dahlbäck, B.3
  • 24
    • 0018377442 scopus 로고
    • Serotypes of Neisseria meningitidis isolated from patients in Norway during the first six months of 1978
    • Holten, E. 1979. Serotypes of Neisseria meningitidis isolated from patients in Norway during the first six months of 1978. J. Clin. Microbiol. 9: 186-188.
    • (1979) J. Clin. Microbiol. , vol.9 , pp. 186-188
    • Holten, E.1
  • 25
    • 0025347045 scopus 로고
    • Isolation of Neisseria meningitidis mutants deficient in class 1 (PorA) and class 3 (PorB) outer membrane proteins
    • Tommassen, J., P. Vermeij, M. Struyve, R. Benz, and J. T. Poolman. 1990. Isolation of Neisseria meningitidis mutants deficient in class 1 (PorA) and class 3 (PorB) outer membrane proteins. Infect. Immun. 58: 1355-1359.
    • (1990) Infect. Immun. , vol.58 , pp. 1355-1359
    • Tommassen, J.1    Vermeij, P.2    Struyve, M.3    Benz, R.4    Poolman, J.T.5
  • 26
    • 9144232334 scopus 로고    scopus 로고
    • Neisserial lipooligosaccharide is a target for complement component C4b: Inner core phosphoethanolamine residues define C4b linkage specificity
    • Ram, S., A. D. Cox, J. C. Wright, U. Vogel, S. Getzlaff, R. Boden, J, Li, J. S. Plested, S. Meri, S. Gulati, et al. 2003. Neisserial lipooligosaccharide is a target for complement component C4b: inner core phosphoethanolamine residues define C4b linkage specificity. J. Biol. Chem. 278: 50853-50862.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50853-50862
    • Ram, S.1    Cox, A.D.2    Wright, J.C.3    Vogel, U.4    Getzlaff, S.5    Boden, R.6    Li, J.7    Plested, J.S.8    Meri, S.9    Gulati, S.10
  • 27
    • 0032957239 scopus 로고    scopus 로고
    • Role of lipopolysaccharide sialylation in serum resistance of serogroup B and C meningococcal disease isolates
    • Vogel, U., H. Claus, G. Heinze, and M. Frosch. 1999. Role of lipopolysaccharide sialylation in serum resistance of serogroup B and C meningococcal disease isolates. Infect. Immun. 67: 954-957.
    • (1999) Infect. Immun. , vol.67 , pp. 954-957
    • Vogel, U.1    Claus, H.2    Heinze, G.3    Frosch, M.4
  • 29
    • 0001706880 scopus 로고
    • The relation of the meningococcidal activity of the blood to resistance to virulent meningococci
    • Matsunami, T., and J. A. Kolmer. 1918. The relation of the meningococcidal activity of the blood to resistance to virulent meningococci. J. Immunol. 3: 201-212.
    • (1918) J. Immunol. , vol.3 , pp. 201-212
    • Matsunami, T.1    Kolmer, J.A.2
  • 30
    • 0023219190 scopus 로고
    • Killing of Neisseria meningitidis by human neutrophils: Implications for normal and complement-deficient individuals
    • Ross, S. C., P. J. Rosenthal, H. M. Berberich, and P. Densen. 1987. Killing of Neisseria meningitidis by human neutrophils: implications for normal and complement-deficient individuals. J. Infect. Dis. 155: 1266-1275.
    • (1987) J. Infect. Dis. , vol.155 , pp. 1266-1275
    • Ross, S.C.1    Rosenthal, P.J.2    Berberich, H.M.3    Densen, P.4
  • 31
    • 0024362527 scopus 로고
    • Complement activation and endotoxin levels in systemic meningococcal disease
    • Brandtzaeg, P., T. E. Mollnes, and P. Kierulf. 1989. Complement activation and endotoxin levels in systemic meningococcal disease. J. Infect. Dis. 160: 58-65.
    • (1989) J. Infect. Dis. , vol.160 , pp. 58-65
    • Brandtzaeg, P.1    Mollnes, T.E.2    Kierulf, P.3
  • 34
    • 0030041379 scopus 로고    scopus 로고
    • The excessive complement activation in fulminant meningococcal septicemia is predominantly caused by alternative pathway activation
    • Brandtzaeg, P., K. Høgåsen, P. Kierulf, and T. E. Mollnes. 1996. The excessive complement activation in fulminant meningococcal septicemia is predominantly caused by alternative pathway activation. J. Infect. Dis. 173: 647-655.
    • (1996) J. Infect. Dis. , vol.173 , pp. 647-655
    • Brandtzaeg, P.1    Høgåsen, K.2    Kierulf, P.3    Mollnes, T.E.4
  • 35
    • 0030668781 scopus 로고    scopus 로고
    • Functional characterization of an isogenic meningococcal α-2,3-sialyltransferase mutant: The role of lipooligosaccharide sialylation for serum resistance in serogroup B meningococci
    • Vogel, U., H. Claus, G. Heinze, and M. Frosch. 1997. Functional characterization of an isogenic meningococcal α-2,3-sialyltransferase mutant: the role of lipooligosaccharide sialylation for serum resistance in serogroup B meningococci, Med. Microbiol Immunol. 186: 159-166.
    • (1997) Med. Microbiol. Immunol. , vol.186 , pp. 159-166
    • Vogel, U.1    Claus, H.2    Heinze, G.3    Frosch, M.4
  • 36
    • 0030748949 scopus 로고    scopus 로고
    • Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis
    • Vogel, U., A. Weinberger, R. Frank, A. Muller, J. Kohl, J. P. Atkinson, and M. Frosch. 1997. Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis. Infect. Immun. 65: 4022-4029.
    • (1997) Infect. Immun. , vol.65 , pp. 4022-4029
    • Vogel, U.1    Weinberger, A.2    Frank, R.3    Muller, A.4    Kohl, J.5    Atkinson, J.P.6    Frosch, M.7
  • 37
    • 0027394624 scopus 로고
    • A low serum concentration of mannan-binding protein is not associated with serogroup B or C meningococcal disease
    • Garred, P., T. E. Michaelsen, G. Bjune, S. Thiel, and A. Svejgaard. 1993. A low serum concentration of mannan-binding protein is not associated with serogroup B or C meningococcal disease. Scand. J. Immunol. 37: 468-470.
    • (1993) Scand. J. Immunol. , vol.37 , pp. 468-470
    • Garred, P.1    Michaelsen, T.E.2    Bjune, G.3    Thiel, S.4    Svejgaard, A.5
  • 38
    • 0033608862 scopus 로고    scopus 로고
    • Association of variants of the gene fro mannose-binding lectin with susceptibility to meningococcal disease
    • Hibberd, M. L., M. Sumiya, J. A. Summerfield, R. Booy, M. Levin, and the Meningococcal Research Group. 1999. Association of variants of the gene fro mannose-binding lectin with susceptibility to meningococcal disease. Lancet 353: 1049-1053.
    • (1999) Lancet , vol.353 , pp. 1049-1053
    • Hibberd, M.L.1    Sumiya, M.2    Summerfield, J.A.3    Booy, R.4    Levin, M.5
  • 39
    • 0031914961 scopus 로고    scopus 로고
    • Activation of complement by mannose-binding lectin on isogenic mutants of Neisseria meningitidis serogroup B
    • Jack, D. L., A. W. Dodds, N. Anwar, C. A. Ison, A. Law, M. Frosch, M. W. Turner, and N. J. Klein. 1998. Activation of complement by mannose-binding lectin on isogenic mutants of Neisseria meningitidis serogroup B. J. Immunol. 160: 1346-1353.
    • (1998) J. Immunol. , vol.160 , pp. 1346-1353
    • Jack, D.L.1    Dodds, A.W.2    Anwar, N.3    Ison, C.A.4    Law, A.5    Frosch, M.6    Turner, M.W.7    Klein, N.J.8
  • 40
    • 0035479073 scopus 로고    scopus 로고
    • Mannose-binding lectin accelerates complement activation and increases serum killing of Neisseria meningitidis serogroup C
    • Jack, D. L., G. A. Jarvis, C. L. Booth, M. W. Turner, and N. J. Klein. 2001. Mannose-binding lectin accelerates complement activation and increases serum killing of Neisseria meningitidis serogroup C. J. Infect. Dis, 184: 836-845.
    • (2001) J. Infect. Dis. , vol.184 , pp. 836-845
    • Jack, D.L.1    Jarvis, G.A.2    Booth, C.L.3    Turner, M.W.4    Klein, N.J.5
  • 41
    • 1542724425 scopus 로고    scopus 로고
    • Mannose-binding lectin binds to two major outer membrane proteins, opacity protein and porin, of Neisseria meningitidis
    • Estabrook, M. M., D. L. Jack, N. J. Klein, and G. A. Jarvis, 2004. Mannose-binding lectin binds to two major outer membrane proteins, opacity protein and porin, of Neisseria meningitidis. J. Immunol. 172: 3784-3792.
    • (2004) J. Immunol. , vol.172 , pp. 3784-3792
    • Estabrook, M.M.1    Jack, D.L.2    Klein, N.J.3    Jarvis, G.A.4
  • 42
    • 0015853721 scopus 로고
    • Release of endotoxin in the form of cell wall blebs during in vitro growth of Neisseria meningitidis
    • Devoe, I. W., and J. E. Gilchrist. 1973. Release of endotoxin in the form of cell wall blebs during in vitro growth of Neisseria meningitidis. J. Exp. Med. 138: 1156-1167.
    • (1973) J. Exp. Med. , vol.138 , pp. 1156-1167
    • Devoe, I.W.1    Gilchrist, J.E.2
  • 43
    • 0037080373 scopus 로고    scopus 로고
    • Complement activation induced by purified Neisseria meningitidis lipopolysaccharide (LPS), outer membrane vesicles, whole bacteria, and an LPS-free mutant
    • Bjerre, A., B. Brusletto, T. E. Mollnes, E. Fritzsønn, E. Rosenqvist, E. Wedege. E. Namork, P. Kierulf, and P. Brandtzaeg. 2002. Complement activation induced by purified Neisseria meningitidis lipopolysaccharide (LPS), outer membrane vesicles, whole bacteria, and an LPS-free mutant. J. Infect. Dis. 185: 220-228.
    • (2002) J. Infect. Dis. , vol.185 , pp. 220-228
    • Bjerre, A.1    Brusletto, B.2    Mollnes, T.E.3    Fritzsønn, E.4    Rosenqvist, E.5    Wedege, E.6    Namork, E.7    Kierulf, P.8    Brandtzaeg, P.9
  • 44
    • 0036081311 scopus 로고    scopus 로고
    • Complement activation and formation of the membrane attack complex on serogroup B Neisseria meningitidis in the presence or absence of serum bactericidal activity
    • Drogari-Apiranthitou, M., E. J. Kuijper, N. Dekker, and J. Dankert. 2002. Complement activation and formation of the membrane attack complex on serogroup B Neisseria meningitidis in the presence or absence of serum bactericidal activity. Infect. Immun. 70: 3752-3758.
    • (2002) Infect. Immun. , vol.70 , pp. 3752-3758
    • Drogari-Apiranthitou, M.1    Kuijper, E.J.2    Dekker, N.3    Dankert, J.4
  • 46
    • 0029742453 scopus 로고    scopus 로고
    • Sialic acids of both the capsule and the sialylated lipooligosaccharide of Neisseria meningitis serogroup B are prerequisites for virulence of meningococci in the infant rat
    • Vogel, U., S. Hammerschmidt, and M. Frosch. 1996. Sialic acids of both the capsule and the sialylated lipooligosaccharide of Neisseria meningitis serogroup B are prerequisites for virulence of meningococci in the infant rat. Med. Microbiol Immunol 185: 81-87.
    • (1996) Med. Microbiol. Immunol. , vol.185 , pp. 81-87
    • Vogel, U.1    Hammerschmidt, S.2    Frosch, M.3
  • 47
    • 8944247272 scopus 로고    scopus 로고
    • Capsule phase variation in Neisseria meningitidis serogroup B by slipped-strand mispairing in the polysialyllransferase gene (siaD): Correlation with bacterial invasion and the outbreak of meningococcal disease
    • Hammerschmidt, S., A. Muller, H. Sillmann, M. Muhlenhoff, R. Borrow, A. Fox, J. van Putten, W. D. Zollinger, R. Gerardy-Schahn, and M. Frosch. 1996. Capsule phase variation in Neisseria meningitidis serogroup B by slipped-strand mispairing in the polysialyllransferase gene (siaD): correlation with bacterial invasion and the outbreak of meningococcal disease. Mol. Microbiol 20: 1211-1220.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1211-1220
    • Hammerschmidt, S.1    Muller, A.2    Sillmann, H.3    Muhlenhoff, M.4    Borrow, R.5    Fox, A.6    Van Putten, J.7    Zollinger, W.D.8    Gerardy-Schahn, R.9    Frosch, M.10
  • 48
    • 0030017276 scopus 로고    scopus 로고
    • Invasion of primary nasopharyngeal epithelial cells by Neisseria meningitidis is controlled by phase variation of multiple surface antigens
    • de Vries, F. P., A. van Der Ende, J. P. van Putten, and J. Dankert. 1996. Invasion of primary nasopharyngeal epithelial cells by Neisseria meningitidis is controlled by phase variation of multiple surface antigens. Infect. Immun. 64: 2998-3006.
    • (1996) Infect. Immun. , vol.64 , pp. 2998-3006
    • De Vries, F.P.1    Van Der Ende, A.2    Van Putten, J.P.3    Dankert, J.4
  • 49
    • 0040426308 scopus 로고
    • High molecular weight complex in human plasma between vitamin K-dependent protein S and complement component C4b-binding protein
    • Dahlbäck, B., and J. Stenflo. 1981. High molecular weight complex in human plasma between vitamin K-dependent protein S and complement component C4b-binding protein. Proc. Natl. Acad. Sci. USA 78: 2512-2516.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2512-2516
    • Dahlbäck, B.1    Stenflo, J.2
  • 50
    • 0022929854 scopus 로고
    • Inhibition of protein Ca cofactor function of human and bovine protein S by C4b-binding protein
    • Dahlbäck, B. 1986. Inhibition of protein Ca cofactor function of human and bovine protein S by C4b-binding protein, J. Biol. Chem. 261: 12022-12027.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12022-12027
    • Dahlbäck, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.