메뉴 건너뛰기




Volumn 73, Issue 11, 2005, Pages 7485-7494

Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; AMINO ACID; GLYCOPROTEIN; LAMININ; LAMININ 1; LAMININ 10; LAMININ 4; LAMININ 8; MEROSIN; PROTEIN TP0751; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 27744587898     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.11.7485-7494.2005     Document Type: Article
Times cited : (55)

References (81)
  • 1
    • 27744573923 scopus 로고    scopus 로고
    • Institute of Medical Statistics CR. Institute of Medical Statistics, Prague, Czech Republic
    • Anonymous 2001. Venereal disease 2000. Institute of Medical Statistics CR. Institute of Medical Statistics, Prague, Czech Republic.
    • (2001) Venereal Disease 2000
  • 2
    • 2342585502 scopus 로고    scopus 로고
    • Vancouver facing syphilis outbreak
    • Anonymous. 2004. Vancouver facing syphilis outbreak. AIDS Patient Care STDS 18:186.
    • (2004) AIDS Patient Care STDS , vol.18 , pp. 186
  • 3
    • 0031661502 scopus 로고    scopus 로고
    • The role of laminins in basement membrane function
    • Aumailley, M., and N. Smyth. 1998. The role of laminins in basement membrane function. J. Anat. 193:1-21.
    • (1998) J. Anat. , vol.193 , pp. 1-21
    • Aumailley, M.1    Smyth, N.2
  • 4
    • 0036316243 scopus 로고    scopus 로고
    • Regulation of microvascular permeability by vascular endothelial growth factors
    • Bates, D. O., N. J. Hillman, B. Williams, C. R. Neal, and T. M. Pocock. 2002. Regulation of microvascular permeability by vascular endothelial growth factors. J. Anat. 200:581-597.
    • (2002) J. Anat. , vol.200 , pp. 581-597
    • Bates, D.O.1    Hillman, N.J.2    Williams, B.3    Neal, C.R.4    Pocock, T.M.5
  • 5
    • 0032930002 scopus 로고    scopus 로고
    • Biology and pathology of the skin basement membrane zone
    • Bruckner-Tuderman, L. 1999. Biology and pathology of the skin basement membrane zone. Matrix Biol. 18:3-4.
    • (1999) Matrix Biol. , vol.18 , pp. 3-4
    • Bruckner-Tuderman, L.1
  • 6
    • 0037781976 scopus 로고    scopus 로고
    • Synthetic peptide vaccine and antibody therapeutic development: Prevention and treatment of Pseudomonas aeruginosa
    • Cachia, P. J., and R. S. Hodges. 2003. Synthetic peptide vaccine and antibody therapeutic development: prevention and treatment of Pseudomonas aeruginosa. Biopolymers 71:141-168.
    • (2003) Biopolymers , vol.71 , pp. 141-168
    • Cachia, P.J.1    Hodges, R.S.2
  • 7
    • 0037408253 scopus 로고    scopus 로고
    • Identification of a Treponema pallidum laminin-binding protein
    • Cameron, C. E. 2003. Identification of a Treponema pallidum laminin-binding protein. Infect. Immun. 71:2525-2533.
    • (2003) Infect. Immun. , vol.71 , pp. 2525-2533
    • Cameron, C.E.1
  • 8
    • 0034122411 scopus 로고    scopus 로고
    • Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92
    • Cameron, C. E., S. A. Lukehart, C. Castro, B. Molini, C. Godornes, and W. C. Van Voorhis. 2000. Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92. J. Infect. Dis. 181:1401-1413.
    • (2000) J. Infect. Dis. , vol.181 , pp. 1401-1413
    • Cameron, C.E.1    Lukehart, S.A.2    Castro, C.3    Molini, B.4    Godornes, C.5    Van Voorhis, W.C.6
  • 9
    • 0347962100 scopus 로고    scopus 로고
    • Primary and secondary syphilis-United States, 2002
    • Centers for Disease Control and Prevention. 2003. Primary and secondary syphilis-United States, 2002. Morb. Mortal. Wkly. Rep. 52:1117-1120.
    • (2003) Morb. Mortal. Wkly. Rep. , vol.52 , pp. 1117-1120
  • 10
    • 0034075654 scopus 로고    scopus 로고
    • Form and function: The laminin family of heterotrimers
    • Colognato, H., and P. D. Yurchenco. 2000. Form and function: the laminin family of heterotrimers. Dev. Dyn. 218:213-234.
    • (2000) Dev. Dyn. , vol.218 , pp. 213-234
    • Colognato, H.1    Yurchenco, P.D.2
  • 11
    • 0001405964 scopus 로고
    • Rate of multiplication of Treponema pallidum in normal and immune rabbits
    • Cumberland, M. C., and T. B. Turner. 1949. Rate of multiplication of Treponema pallidum in normal and immune rabbits. Am. J. Syph. 33: 201-212.
    • (1949) Am. J. Syph. , vol.33 , pp. 201-212
    • Cumberland, M.C.1    Turner, T.B.2
  • 13
    • 0345381943 scopus 로고    scopus 로고
    • Expression and biological role of laminin-1
    • Ekblom, P., P. Lonai, and J. F. Talts. 2003. Expression and biological role of laminin-1. Matrix Biol. 22:35-47.
    • (2003) Matrix Biol. , vol.22 , pp. 35-47
    • Ekblom, P.1    Lonai, P.2    Talts, J.F.3
  • 14
    • 0033764688 scopus 로고    scopus 로고
    • Insertional inactivation of the prtP gene of Treponema denticola confirms dentilisin's disruption of epithelial junctions
    • Ellen, R. P., K. S. Ko, C. M. Lo, D. A. Grove, and K. Ishihara. 2000. Insertional inactivation of the prtP gene of Treponema denticola confirms dentilisin's disruption of epithelial junctions. J. Mol. Microbiol. Biotechnol. 2:581-586.
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 581-586
    • Ellen, R.P.1    Ko, K.S.2    Lo, C.M.3    Grove, D.A.4    Ishihara, K.5
  • 17
    • 0031900968 scopus 로고    scopus 로고
    • Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola
    • Fenno, J. C., P. M. Hannam, W. K. Leung, M. Tamura, V. J. Uitto, and B. C. McBride. 1998. Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola. Infect. Immun. 66: 1869-1877.
    • (1998) Infect. Immun. , vol.66 , pp. 1869-1877
    • Fenno, J.C.1    Hannam, P.M.2    Leung, W.K.3    Tamura, M.4    Uitto, V.J.5    McBride, B.C.6
  • 18
    • 0029863955 scopus 로고    scopus 로고
    • Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola
    • Fenno, J. C., K. H. Muller, and B. C. McBride. 1996. Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola. J. Bacteriol. 178:2489-2497.
    • (1996) J. Bacteriol. , vol.178 , pp. 2489-2497
    • Fenno, J.C.1    Muller, K.H.2    McBride, B.C.3
  • 19
    • 0034064780 scopus 로고    scopus 로고
    • Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment
    • Fenno, J. C., M. Tamura, P. M. Hannam, G. W. Wong, R. A. Chan, and B. C. McBride. 2000. Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment. Infect. Immun. 68:1884-1892.
    • (2000) Infect. Immun. , vol.68 , pp. 1884-1892
    • Fenno, J.C.1    Tamura, M.2    Hannam, P.M.3    Wong, G.W.4    Chan, R.A.5    McBride, B.C.6
  • 20
    • 4244150709 scopus 로고
    • Attachment of treponemes to cell surfaces
    • R. F. Schell and D. M. Musher (ed.). Marcel Dekker, New York, N.Y.
    • Fitzgerald, T. J. 1983. Attachment of treponemes to cell surfaces, p. 195-228. In R. F. Schell and D. M. Musher (ed.), Pathogenesis and immunology of treponemal infections. Marcel Dekker, New York, N.Y.
    • (1983) Pathogenesis and Immunology of Treponemal Infections , pp. 195-228
    • Fitzgerald, T.J.1
  • 21
    • 0016773244 scopus 로고
    • Treponema pallidum (Nichols strain) in tissue cultures: Cellular attachment, entry, and survival
    • Fitzgerald, T. J., J. N. Miller, and J. A. Sykes. 1975. Treponema pallidum (Nichols strain) in tissue cultures: cellular attachment, entry, and survival. Infect. Immun. 11:1133-1140.
    • (1975) Infect. Immun. , vol.11 , pp. 1133-1140
    • Fitzgerald, T.J.1    Miller, J.N.2    Sykes, J.A.3
  • 22
    • 84906417349 scopus 로고
    • Attachment of Treponema pallidum to fibronectin, laminin, collagen IV, and collagen I, and blockage of attachment by immune rabbit IgG
    • Fitzgerald, T. J., L. A. Repesh, D. R. Blanco, and J. N. Miller. 1984. Attachment of Treponema pallidum to fibronectin, laminin, collagen IV, and collagen I, and blockage of attachment by immune rabbit IgG. Br. J. Vener. Dis. 60:357-363.
    • (1984) Br. J. Vener. Dis. , vol.60 , pp. 357-363
    • Fitzgerald, T.J.1    Repesh, L.A.2    Blanco, D.R.3    Miller, J.N.4
  • 23
    • 0026629423 scopus 로고
    • Laminin enhances binding of Toxoplasma gondii tachyzoites to J774 murine macrophage cells
    • Furtado, G. C., M. Slowik, H. K. Kleinman, and K. A. Joiner. 1992. Laminin enhances binding of Toxoplasma gondii tachyzoites to J774 murine macrophage cells. Infect. Immun. 60:2337-2342.
    • (1992) Infect. Immun. , vol.60 , pp. 2337-2342
    • Furtado, G.C.1    Slowik, M.2    Kleinman, H.K.3    Joiner, K.A.4
  • 25
    • 0033082746 scopus 로고    scopus 로고
    • Isolation of a laminin-binding protein from the protozoan parasite Leishmania donovani that may mediate cell adhesion
    • Ghosh, A., K. Bandyopadhyay, L. Kole, and P. K. Das. 1999. Isolation of a laminin-binding protein from the protozoan parasite Leishmania donovani that may mediate cell adhesion. Biochem. J. 337:551-558.
    • (1999) Biochem. J. , vol.337 , pp. 551-558
    • Ghosh, A.1    Bandyopadhyay, K.2    Kole, L.3    Das, P.K.4
  • 27
    • 0035063962 scopus 로고    scopus 로고
    • Inhibition of hydrophobic protein-mediated Candida albicans attachment to endothelial cells during physiologic shear flow
    • Glee, P. M., J. E. Cutler, E. E. Benson, R. F. Bargatze, and K. C. Hazen. 2001. Inhibition of hydrophobic protein-mediated Candida albicans attachment to endothelial cells during physiologic shear flow. Infect. Immun. 69:2815-2820.
    • (2001) Infect. Immun. , vol.69 , pp. 2815-2820
    • Glee, P.M.1    Cutler, J.E.2    Benson, E.E.3    Bargatze, R.F.4    Hazen, K.C.5
  • 28
    • 0037059038 scopus 로고    scopus 로고
    • Complex interactions between the laminin alpha 4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo
    • Gonzalez, A. M., M. Gonzales, G. S. Herron, U. Nagavarapu, S. B. Hopkinson, D. Tsuruta, and J. C. Jones. 2002. Complex interactions between the laminin alpha 4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo. Proc. Natl. Acad. Sci. USA. 99:16075-16080.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 16075-16080
    • Gonzalez, A.M.1    Gonzales, M.2    Herron, G.S.3    Nagavarapu, U.4    Hopkinson, S.B.5    Tsuruta, D.6    Jones, J.C.7
  • 29
    • 0034981867 scopus 로고    scopus 로고
    • Laminin-2/4 from human placenta is a better adhesion agent for primary keratinocytes than laminin-1 from EHS sarcoma
    • Gorelik, J. V., O. A. Cherepanova, I. V. Voronkina, I. A. Diakonen, M. I. Blinova, and G. P. Pinaev. 2001. Laminin-2/4 from human placenta is a better adhesion agent for primary keratinocytes than laminin-1 from EHS sarcoma. Cell. Biol. Int. 25:395-402.
    • (2001) Cell. Biol. Int. , vol.25 , pp. 395-402
    • Gorelik, J.V.1    Cherepanova, O.A.2    Voronkina, I.V.3    Diakonen, I.A.4    Blinova, M.I.5    Pinaev, G.P.6
  • 30
    • 0025117758 scopus 로고
    • Cellular location of a Treponema denticola chymotrypsinlike protease and importance of the protease in migration through the basement membrane
    • Grenier, D., V. J. Uitto, and B. C. McBride. 1990. Cellular location of a Treponema denticola chymotrypsinlike protease and importance of the protease in migration through the basement membrane. Infect. Immun. 58: 347-351.
    • (1990) Infect. Immun. , vol.58 , pp. 347-351
    • Grenier, D.1    Uitto, V.J.2    McBride, B.C.3
  • 31
    • 0027934798 scopus 로고
    • Interactional invasion of endothelial cell monolayers
    • Haake, D. A., and M. A. Lovett. 1994. Interactional invasion of endothelial cell monolayers. Methods Enzymol. 236:447-463.
    • (1994) Methods Enzymol. , vol.236 , pp. 447-463
    • Haake, D.A.1    Lovett, M.A.2
  • 32
    • 0037145037 scopus 로고    scopus 로고
    • Integrins. Bidirectional, allosteric signaling machines
    • Hynes, R. 2002. Integrins. Bidirectional, allosteric signaling machines. Cell 110:673.
    • (2002) Cell , vol.110 , pp. 673
    • Hynes, R.1
  • 36
    • 0034429849 scopus 로고    scopus 로고
    • Plasminogen activation in degradation and penetration of extracellular matrices and basement membranes by invasive bacteria
    • Lahteenmaki, K., P. Kuusela, and T. K. Korhonen. 2000. Plasminogen activation in degradation and penetration of extracellular matrices and basement membranes by invasive bacteria. Methods 21:125-132.
    • (2000) Methods , vol.21 , pp. 125-132
    • Lahteenmaki, K.1    Kuusela, P.2    Korhonen, T.K.3
  • 37
    • 0037561088 scopus 로고    scopus 로고
    • Receptors for Treponema pallidum attachment to the surface and matrix proteins of cultured human dermal microvascular endothelial cells
    • Lee, J. H., H. J. Choi, J. Jung, M. G. Lee, J. B. Lee, and K. H. Lee. 2003. Receptors for Treponema pallidum attachment to the surface and matrix proteins of cultured human dermal microvascular endothelial cells. Yonsei Med. J. 44:371-378.
    • (2003) Yonsei Med. J. , vol.44 , pp. 371-378
    • Lee, J.H.1    Choi, H.J.2    Jung, J.3    Lee, M.G.4    Lee, J.B.5    Lee, K.H.6
  • 39
    • 0023970247 scopus 로고
    • Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development
    • Leivo, I., and E. Engvall. 1988. Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development. Proc. Natl. Acad. Sci. USA 85:1544-1548.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1544-1548
    • Leivo, I.1    Engvall, E.2
  • 41
    • 0022555838 scopus 로고
    • Biochemical interactions of tumor cells with the basement membrane
    • Liotta, L. A., C. N. Rao, and U. M. Wewer. 1986. Biochemical interactions of tumor cells with the basement membrane. Annu. Rev. Biochem. 55: 1037-1057.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1037-1057
    • Liotta, L.A.1    Rao, C.N.2    Wewer, U.M.3
  • 42
    • 9244255314 scopus 로고    scopus 로고
    • The C-terminal fragment of the internal 110-kilodalton passenger domain of the Hap protein of nontypeable Haemophilus influenzas is a potential vaccine candidate
    • Liu, D. F., K. W. Mason, M. Mastri, M. Pazirandeh, D. Cutter, D. L. Fink, J. W. St. Gerne III, D. Zhu, and B. A. Green. 2004. The C-terminal fragment of the internal 110-kilodalton passenger domain of the Hap protein of nontypeable Haemophilus influenzas is a potential vaccine candidate. Infect. Immun. 72:6961-6968.
    • (2004) Infect. Immun. , vol.72 , pp. 6961-6968
    • Liu, D.F.1    Mason, K.W.2    Mastri, M.3    Pazirandeh, M.4    Cutter, D.5    Fink, D.L.6    St. Gerne III, J.W.7    Zhu, D.8    Green, B.A.9
  • 43
    • 0018884754 scopus 로고
    • Characterization of lymphocyte responsiveness in early experimental syphilis. II. Nature of cellular infiltration and Treponema pallidum distribution in testicular lesions
    • Lukehart, S. A., S. A. Baker-Zander, R. M. Lloyd, and S. Sell. 1980. Characterization of lymphocyte responsiveness in early experimental syphilis. II. Nature of cellular infiltration and Treponema pallidum distribution in testicular lesions. J. Immunol. 124:461-467.
    • (1980) J. Immunol. , vol.124 , pp. 461-467
    • Lukehart, S.A.1    Baker-Zander, S.A.2    Lloyd, R.M.3    Sell, S.4
  • 44
    • 0018861516 scopus 로고
    • Characterization of lymphocyte responsiveness in early experimental syphilis. I. In vitro response to mitogens and Treponema pallidum antigens
    • Lukehart, S. A., S. A. Baker-Zander, and S. Sell. 1980. Characterization of lymphocyte responsiveness in early experimental syphilis. I. In vitro response to mitogens and Treponema pallidum antigens. J. Immunol. 124:454-460.
    • (1980) J. Immunol. , vol.124 , pp. 454-460
    • Lukehart, S.A.1    Baker-Zander, S.A.2    Sell, S.3
  • 45
    • 0006147019 scopus 로고
    • Syphilis
    • E. Braunwald, K. L. Isselbacher, R. G. Petersdorf, J. D. Wilson, J. B. Martin, and A. S. Fauci (ed.). McGraw-Hill Book Company, New York, N.Y.
    • Lukehart, S. A., and K. K. Holmes. 1991. Syphilis, p. 651-661. In E. Braunwald, K. L. Isselbacher, R. G. Petersdorf, J. D. Wilson, J. B. Martin, and A. S. Fauci (ed.), Harrison's principles of internal medicine. McGraw-Hill Book Company, New York, N.Y.
    • (1991) Harrison's Principles of Internal Medicine , pp. 651-661
    • Lukehart, S.A.1    Holmes, K.K.2
  • 46
    • 0031783641 scopus 로고    scopus 로고
    • Expression of vascular endothelial growth factor in human oral squamous cell carcinoma: Its association with tumour progression and p53 gene status
    • Maeda, T., S. Matsumura, H. Hiranuma, A. Jikko, S. Furukawa, T. Ishida, and H. Fuchihata. 1998. Expression of vascular endothelial growth factor in human oral squamous cell carcinoma: its association with tumour progression and p53 gene status. J. Clin. Pathol. 51:771-775.
    • (1998) J. Clin. Pathol. , vol.51 , pp. 771-775
    • Maeda, T.1    Matsumura, S.2    Hiranuma, H.3    Jikko, A.4    Furukawa, S.5    Ishida, T.6    Fuchihata, H.7
  • 47
  • 49
    • 0036606894 scopus 로고    scopus 로고
    • Are trends in HIV, gonorrhoea, and syphilis worsening in western Europe?
    • Nicoll, A., and F. F. Hamers. 2002. Are trends in HIV, gonorrhoea, and syphilis worsening in western Europe? BMJ 324:1324-1327.
    • (2002) BMJ , vol.324 , pp. 1324-1327
    • Nicoll, A.1    Hamers, F.F.2
  • 50
    • 0032526037 scopus 로고    scopus 로고
    • Vaccination with a recombinant fragment of collagen adhesin provides protection against Staphylococcus aureus-mediated septic death
    • Nilsson, I. M., J. M. Patti, T. Bremell, M. Hook, and A. Tarkowski. 1998. Vaccination with a recombinant fragment of collagen adhesin provides protection against Staphylococcus aureus-mediated septic death. J. Clin. Investig. 101:2640-2649.
    • (1998) J. Clin. Investig. , vol.101 , pp. 2640-2649
    • Nilsson, I.M.1    Patti, J.M.2    Bremell, T.3    Hook, M.4    Tarkowski, A.5
  • 52
    • 0032963472 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF)-mediated angiogenesis is associated with enhanced endothelial cell survival and induction of Bcl-2 expression
    • Nor, J. E., J. Christensen, D. J. Mooney, and P. J. Polverini. 1999. Vascular endothelial growth factor (VEGF)-mediated angiogenesis is associated with enhanced endothelial cell survival and induction of Bcl-2 expression. Am. J. Pathol. 154:375-384.
    • (1999) Am. J. Pathol. , vol.154 , pp. 375-384
    • Nor, J.E.1    Christensen, J.2    Mooney, D.J.3    Polverini, P.J.4
  • 53
    • 14844287044 scopus 로고    scopus 로고
    • Sexually transmitted infections and increased risk of co-infection with human immunodeficiency virus
    • Nusbaum, M. R., R. R. Wallace, L. M. Slatt, and E. C. Kondrad. 2004. Sexually transmitted infections and increased risk of co-infection with human immunodeficiency virus. J. Am. Osteopath. Assoc. 104:527-535.
    • (2004) J. Am. Osteopath. Assoc. , vol.104 , pp. 527-535
    • Nusbaum, M.R.1    Wallace, R.R.2    Slatt, L.M.3    Kondrad, E.C.4
  • 54
    • 0028074251 scopus 로고
    • Microbial adhesins recognizing extracellular matrix macromolecules
    • Patti, J. M., and M. Hook. 1994. Microbial adhesins recognizing extracellular matrix macromolecules. Curr. Opin. Cell Biol. 6:752-758.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 752-758
    • Patti, J.M.1    Hook, M.2
  • 56
    • 0035181363 scopus 로고    scopus 로고
    • Mycobacterium smegmatis laminin-binding glycoprotein shares epitopes with Mycobacterium tuberculosis heparin-binding haemagglutinin
    • Pethe, K., V. Puech, M. Daffe, C. Josenhans, H. Drobecq, C. Locht, and F. D. Menozzi. 2001. Mycobacterium smegmatis laminin-binding glycoprotein shares epitopes with Mycobacterium tuberculosis heparin-binding haemagglutinin. Mol. Microbiol. 39:89-99.
    • (2001) Mol. Microbiol. , vol.39 , pp. 89-99
    • Pethe, K.1    Puech, V.2    Daffe, M.3    Josenhans, C.4    Drobecq, H.5    Locht, C.6    Menozzi, F.D.7
  • 57
    • 0017123321 scopus 로고
    • Laboratory-associated infections: Summary and analysis of 3921 cases
    • Pike, R. M. 1976. Laboratory-associated infections: summary and analysis of 3921 cases. Health Lab. Sci. 13:105-114.
    • (1976) Health Lab. Sci. , vol.13 , pp. 105-114
    • Pike, R.M.1
  • 58
    • 0020698368 scopus 로고
    • Interaction of Treponema pallidum with isolated rabbit capillary tissues
    • Quist, E. E., L. A. Repesh, R. Zeleznikar, and T. J. Fitzgerald. 1983. Interaction of Treponema pallidum with isolated rabbit capillary tissues. Br. J. Vener. Dis. 59:11-20.
    • (1983) Br. J. Vener. Dis. , vol.59 , pp. 11-20
    • Quist, E.E.1    Repesh, L.A.2    Zeleznikar, R.3    Fitzgerald, T.J.4
  • 59
    • 0242489054 scopus 로고
    • Rapidity with which Spirochaeta pallida invades the bloodstream
    • Raiziss, G. W., and M. Severac. 1937. Rapidity with which Spirochaeta pallida invades the bloodstream. Arch. Dermatol. Syphilol. 35:1101-1109.
    • (1937) Arch. Dermatol. Syphilol. , vol.35 , pp. 1101-1109
    • Raiziss, G.W.1    Severac, M.2
  • 61
    • 0027931123 scopus 로고
    • Virulent Treponema pallidum promotes adhesion of leukocytes to human vascular endothelial cells
    • Riley, B. S., N. Oppenheimer-Marks, J. D. Radolf, and M. V. Norgard. 1994. Virulent Treponema pallidum promotes adhesion of leukocytes to human vascular endothelial cells. Infect. Immun. 62:4622-41625.
    • (1994) Infect. Immun. , vol.62 , pp. 4622-41625
    • Riley, B.S.1    Oppenheimer-Marks, N.2    Radolf, J.D.3    Norgard, M.V.4
  • 62
    • 0024309864 scopus 로고
    • In vitro model of Treponema pallidum invasiveness
    • Riviere, G. R., D. D. Thomas, and C. M. Cobb. 1989. In vitro model of Treponema pallidum invasiveness. Infect. Immun. 57:2267-2271.
    • (1989) Infect. Immun. , vol.57 , pp. 2267-2271
    • Riviere, G.R.1    Thomas, D.D.2    Cobb, C.M.3
  • 63
    • 0028981367 scopus 로고
    • The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin
    • Schnapp, L. M., N. Hatch, D. M. Ramos, I. V. Klimanskaya, D. Sheppard, and R. Pytela. 1995. The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin. J. Biol. Chem. 270: 23196-23202.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23196-23202
    • Schnapp, L.M.1    Hatch, N.2    Ramos, D.M.3    Klimanskaya, I.V.4    Sheppard, D.5    Pytela, R.6
  • 64
    • 0020646416 scopus 로고
    • The biology, pathology, and immunology of syphilis
    • Sell, S., and S. J. Norris. 1983. The biology, pathology, and immunology of syphilis. Int. Rev. Exp. Pathol. 24:203-276.
    • (1983) Int. Rev. Exp. Pathol. , vol.24 , pp. 203-276
    • Sell, S.1    Norris, S.J.2
  • 65
    • 0026506913 scopus 로고
    • Demonstration of Treponema pallidum in axons of cutaneous nerves in experimental chancres of rabbits
    • Sell, S., and J. Salman. 1992. Demonstration of Treponema pallidum in axons of cutaneous nerves in experimental chancres of rabbits. Sex. Transm. Dis. 19:1-6.
    • (1992) Sex. Transm. Dis. , vol.19 , pp. 1-6
    • Sell, S.1    Salman, J.2
  • 66
    • 13044286029 scopus 로고    scopus 로고
    • A 21-kDa surface protein of Mycobacterium leprae binds peripheral nerve laminin-2 and mediates Schwann cell invasion
    • Shimoji, Y., V. Ng, K. Matsumura, V. A. Fischetti, and A. Rambukkana. 1999. A 21-kDa surface protein of Mycobacterium leprae binds peripheral nerve laminin-2 and mediates Schwann cell invasion. Proc. Natl. Acad. Sci. USA 96:9857-9862.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9857-9862
    • Shimoji, Y.1    Ng, V.2    Matsumura, K.3    Fischetti, V.A.4    Rambukkana, A.5
  • 67
    • 0242721044 scopus 로고    scopus 로고
    • Escherichia coli K1 invasion increases human brain microvascular endothelial cell monolayer permeability by disassembling vascular-endothelial cadherins at tight junctions
    • Sukumaran, S. K., and N. V. Prasadarao. 2003. Escherichia coli K1 invasion increases human brain microvascular endothelial cell monolayer permeability by disassembling vascular-endothelial cadherins at tight junctions. J. Infect. Dis. 188:1295-1309.
    • (2003) J. Infect. Dis. , vol.188 , pp. 1295-1309
    • Sukumaran, S.K.1    Prasadarao, N.V.2
  • 68
    • 0024583796 scopus 로고
    • Interactions of Treponema pallidum with endothelial cell monolayers
    • Thomas, D. D., A. M. Fogelman, J. N. Miller, and M. A. Lovett. 1989. Interactions of Treponema pallidum with endothelial cell monolayers. Eur. J. Epidemiol. 5:15-21.
    • (1989) Eur. J. Epidemiol. , vol.5 , pp. 15-21
    • Thomas, D.D.1    Fogelman, A.M.2    Miller, J.N.3    Lovett, M.A.4
  • 70
    • 0030271572 scopus 로고    scopus 로고
    • Macromolecular organization of basement membranes
    • Timpl, R. 1996. Macromolecular organization of basement membranes. Curr. Opin. Cell Biol. 8:618-624.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 618-624
    • Timpl, R.1
  • 71
    • 0023015217 scopus 로고
    • Structure, development, and molecular pathology of basement membranes
    • Timpl, R., and M. Dziadek. 1986. Structure, development, and molecular pathology of basement membranes. Int. Rev. Exp. Pathol. 29:1-112.
    • (1986) Int. Rev. Exp. Pathol. , vol.29 , pp. 1-112
    • Timpl, R.1    Dziadek, M.2
  • 76
    • 0028203398 scopus 로고
    • Binding of Paracoccidioides brasiliensis to laminin through surface glycoprotein gp43 leads to enhancement of fungal pathogenesis
    • Vicentini, A. P., J. L. Gesztesi, M. F. Franco, W. de Souza, J. Z. de Moraes, L. R. Travassos, and J. D. Lopes. 1994. Binding of Paracoccidioides brasiliensis to laminin through surface glycoprotein gp43 leads to enhancement of fungal pathogenesis. Infect. Immun. 62:1465-1469.
    • (1994) Infect. Immun. , vol.62 , pp. 1465-1469
    • Vicentini, A.P.1    Gesztesi, J.L.2    Franco, M.F.3    De Souza, W.4    De Moraes, J.Z.5    Travassos, L.R.6    Lopes, J.D.7
  • 78
    • 3042627486 scopus 로고    scopus 로고
    • Prevention of congenital syphilis-time for action
    • Walker, D. G., and G. J. Walker. 2004. Prevention of congenital syphilis-time for action. Bull. W. H. O. 82:401.
    • (2004) Bull. W. H. O. , vol.82 , pp. 401
    • Walker, D.G.1    Walker, G.J.2
  • 79
    • 8644246082 scopus 로고    scopus 로고
    • Cytokines, nitric oxide, and cGMP modulate the permeability of an in vitro model of the human blood-brain barrier
    • Wong, D., K. Dorovini-Zis, and S. R. Vincent. 2004. Cytokines, nitric oxide, and cGMP modulate the permeability of an in vitro model of the human blood-brain barrier. Exp. Neurol. 190:446-455.
    • (2004) Exp. Neurol. , vol.190 , pp. 446-455
    • Wong, D.1    Dorovini-Zis, K.2    Vincent, S.R.3
  • 80
    • 0031969264 scopus 로고    scopus 로고
    • Angiogenesis and tumor metastasis
    • Zetter, B. R. 1998. Angiogenesis and tumor metastasis. Annu. Rev. Med. 49:407-424.
    • (1998) Annu. Rev. Med. , vol.49 , pp. 407-424
    • Zetter, B.R.1
  • 81
    • 0032726068 scopus 로고    scopus 로고
    • Renaturation of recombinant Treponema pallidum rare outer membrane protein 1 into a trimeric, hydrophobic, and porin-active conformation
    • Zhang, H. H., D. R. Blanco, M. M. Exner, E. S. Shang, C. I. Champion, M. L. Phillips, J. N. Miller, and M. A. Lovett. 1999. Renaturation of recombinant Treponema pallidum rare outer membrane protein 1 into a trimeric, hydrophobic, and porin-active conformation. J. Bacteriol. 181:7168-7175.
    • (1999) J. Bacteriol. , vol.181 , pp. 7168-7175
    • Zhang, H.H.1    Blanco, D.R.2    Exner, M.M.3    Shang, E.S.4    Champion, C.I.5    Phillips, M.L.6    Miller, J.N.7    Lovett, M.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.