메뉴 건너뛰기




Volumn 72, Issue 6, 2004, Pages 3138-3146

Borrelia burgdorferi binds to, invades, and colonizes native type I collagen lattices

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ALBUMIN; COLLAGEN; COLLAGEN TYPE 1; DECORIN; GELATIN; GLYCOSAMINOGLYCAN; PROTEINASE K;

EID: 2542590242     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.72.6.3138-3146.2004     Document Type: Article
Times cited : (54)

References (58)
  • 1
    • 0020598076 scopus 로고
    • Lyme disease spirochetes and ixodid tick spirochetes share a common surface antigenic determinant defined by a monoclonal antibody
    • Barbour, A. G., S. L. Tessier, and W. J. Todd. 1983. Lyme disease spirochetes and ixodid tick spirochetes share a common surface antigenic determinant defined by a monoclonal antibody. Infect. Immun. 41:795-804.
    • (1983) Infect. Immun. , vol.41 , pp. 795-804
    • Barbour, A.G.1    Tessier, S.L.2    Todd, W.J.3
  • 2
    • 0003054974 scopus 로고
    • Collagen fibril assembly, deposition and organization into tissue-specific matrices
    • P. D. Yurchenco, D. E. Birk, and R. P. Mechan (ed.). Academic Press, New York, N.Y.
    • Birk, D. E., and T. F. Linsenmayer. 1994. Collagen fibril assembly, deposition and organization into tissue-specific matrices, p. 91-128. In P. D. Yurchenco, D. E. Birk, and R. P. Mechan (ed.), Extracellular matrix assembly and structure. Academic Press, New York, N.Y.
    • (1994) Extracellular Matrix Assembly and Structure , pp. 91-128
    • Birk, D.E.1    Linsenmayer, T.F.2
  • 3
    • 0034285218 scopus 로고    scopus 로고
    • Time-lapse confocal reflection microscopy of collagen fibrillogenesis and extracellular matrix assembly in vitro
    • Brightman, A. O., B. P. Rajwa, J. E. Sturgis, M. E. McCallister, J. P. Robinson, and S. L. Voytik-Harbin. 2000. Time-lapse confocal reflection microscopy of collagen fibrillogenesis and extracellular matrix assembly in vitro. Biopolymers 54:222-234.
    • (2000) Biopolymers , vol.54 , pp. 222-234
    • Brightman, A.O.1    Rajwa, B.P.2    Sturgis, J.E.3    McCallister, M.E.4    Robinson, J.P.5    Voytik-Harbin, S.L.6
  • 4
    • 0033543568 scopus 로고    scopus 로고
    • Adherence of Borrelia burgdorferi. Identification of critical lysine residues in DbpA required for decorin binding
    • Brown, E. L., P. B. Guo, P. O'Neal, and M. Hook. 1999. Adherence of Borrelia burgdorferi. Identification of critical lysine residues in DbpA required for decorin binding. J. Biol. Chem. 274:26272-26278.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26272-26278
    • Brown, E.L.1    Guo, P.B.2    O'Neal, P.3    Hook, M.4
  • 6
    • 0033016382 scopus 로고    scopus 로고
    • Access of antibody or trypsin to an integral outer membrane protein (P66) of Borrelia burgdorferi is hindered by Osp lipoproteins
    • Bunikis, J., and A. G. Barbour. 1999. Access of antibody or trypsin to an integral outer membrane protein (P66) of Borrelia burgdorferi is hindered by Osp lipoproteins. Infect. Immun. 67:2874-2883.
    • (1999) Infect. Immun. , vol.67 , pp. 2874-2883
    • Bunikis, J.1    Barbour, A.G.2
  • 7
    • 0036948288 scopus 로고    scopus 로고
    • Genetics of motility and chemotaxis of a fascinating group of bacteria: The spirochetes
    • Charon, N. W., and S. F. Goldstein. 2002. Genetics of motility and chemotaxis of a fascinating group of bacteria: the spirochetes. Annu. Rev. Genet. 36:47-73.
    • (2002) Annu. Rev. Genet. , vol.36 , pp. 47-73
    • Charon, N.W.1    Goldstein, S.F.2
  • 8
    • 0035428016 scopus 로고    scopus 로고
    • Adhesion mechanisms of the Lyme disease spirochete, Borrelia burgdorferi
    • Coburn, J. 2001. Adhesion mechanisms of the Lyme disease spirochete, Borrelia burgdorferi. Curr. Drug Targets Infect. Disord. 1:171-179.
    • (2001) Curr. Drug Targets Infect. Disord. , vol.1 , pp. 171-179
    • Coburn, J.1
  • 9
    • 0033233457 scopus 로고    scopus 로고
    • Characterization of a candidate Borrelia burgdorferi beta3-chain integrin ligand identified using a phage display library
    • Coburn, J., W. Chege, L. Magoun, S. C. Bodary, and J. M. Leong. 1999. Characterization of a candidate Borrelia burgdorferi beta3-chain integrin ligand identified using a phage display library. Mol. Microbiol. 34:926-940.
    • (1999) Mol. Microbiol. , vol.34 , pp. 926-940
    • Coburn, J.1    Chege, W.2    Magoun, L.3    Bodary, S.C.4    Leong, J.M.5
  • 10
    • 0031924314 scopus 로고    scopus 로고
    • Integrins α(v)β3 and α5β1 mediate attachment of Lyme disease spirochetes to human cells
    • Coburn, J., L. Magoun, S. C. Bodary, and J. M. Leong. 1998. Integrins α(v)β3 and α5β1 mediate attachment of Lyme disease spirochetes to human cells. Infect. Immun. 66:1946-1952.
    • (1998) Infect. Immun. , vol.66 , pp. 1946-1952
    • Coburn, J.1    Magoun, L.2    Bodary, S.C.3    Leong, J.M.4
  • 11
    • 0037306601 scopus 로고    scopus 로고
    • Regulation of expression of the Borrelia burgdorferi β(3)-chain integrin ligand, P66, in ticks and in culture
    • Cugini, C., M. Medrano, T. G. Schwan, and J. Coburn. 2003. Regulation of expression of the Borrelia burgdorferi β(3)-chain integrin ligand, P66, in ticks and in culture. Infect. Immun. 71:1001-1007.
    • (2003) Infect. Immun. , vol.71 , pp. 1001-1007
    • Cugini, C.1    Medrano, M.2    Schwan, T.G.3    Coburn, J.4
  • 12
    • 0035055365 scopus 로고    scopus 로고
    • Delineation of Borrelia burgdorferi p66 sequences required for integrin α(IIb)β(3) recognition
    • Defoe, G., and J. Coburn. 2001. Delineation of Borrelia burgdorferi p66 sequences required for integrin α(IIb)β(3) recognition. Infect. Immun. 69:3455-3459.
    • (2001) Infect. Immun. , vol.69 , pp. 3455-3459
    • Defoe, G.1    Coburn, J.2
  • 14
    • 0036166738 scopus 로고    scopus 로고
    • Identification of loci critical for replication and compatibility of a Borrelia burgdorferi cp32 plasmid and use of a cp32-based shuttle vector for the expression of fluorescent reporters in the Lyme disease spirochaete
    • Eggers, C. H., M. J. Caimano, M. L. Clawson, W. G. Miller, D. S. Samuels, and J. D. Radolf. 2002. Identification of loci critical for replication and compatibility of a Borrelia burgdorferi cp32 plasmid and use of a cp32-based shuttle vector for the expression of fluorescent reporters in the Lyme disease spirochaete. Mol. Microbiol. 43:281-295.
    • (2002) Mol. Microbiol. , vol.43 , pp. 281-295
    • Eggers, C.H.1    Caimano, M.J.2    Clawson, M.L.3    Miller, W.G.4    Samuels, D.S.5    Radolf, J.D.6
  • 15
    • 0015402532 scopus 로고
    • Collagen substrata for studies on cell behavior
    • Elsdale, T., and J. Bard. 1972. Collagen substrata for studies on cell behavior. J. Cell Biol. 54:626-637.
    • (1972) J. Cell Biol. , vol.54 , pp. 626-637
    • Elsdale, T.1    Bard, J.2
  • 16
    • 0038132181 scopus 로고    scopus 로고
    • Decorin-binding proteins A and B confer distinct mammalian cell type-specific attachment by Borrelia burgdorferi, the Lyme disease spirochete
    • Fischer, J. R., N. Parveen, L. Magoun, and J. M. Leong. 2003. Decorin-binding proteins A and B confer distinct mammalian cell type-specific attachment by Borrelia burgdorferi, the Lyme disease spirochete. Proc. Natl. Acad. Sci. USA 100:7307-7312.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7307-7312
    • Fischer, J.R.1    Parveen, N.2    Magoun, L.3    Leong, J.M.4
  • 17
    • 0037306373 scopus 로고    scopus 로고
    • Assembly of collagen matrices as a phase transition revealed by structural and rheologic studies
    • Forgacs, G., S. A. Newman, B. Hinner, C. W. Maier, and E. Sackmann. 2003. Assembly of collagen matrices as a phase transition revealed by structural and rheologic studies. Biophys. J. 84:1272-1280.
    • (2003) Biophys. J. , vol.84 , pp. 1272-1280
    • Forgacs, G.1    Newman, S.A.2    Hinner, B.3    Maier, C.W.4    Sackmann, E.5
  • 18
    • 0018569335 scopus 로고
    • Collagen fibril formation in vitro. The role of the nonhelical terminal regions
    • Gelman, R. A., D. C. Poppke, and K. A. Piez. 1979. Collagen fibril formation in vitro. The role of the nonhelical terminal regions. J. Biol. Chem. 254:11741-11745.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11741-11745
    • Gelman, R.A.1    Poppke, D.C.2    Piez, K.A.3
  • 19
    • 0030588118 scopus 로고    scopus 로고
    • Borrelia burgdorferi possesses a collagenolytic activity
    • Grab, D. J., R. Kennedy, and M. T. Philipp. 1996. Borrelia burgdorferi possesses a collagenolytic activity. FEMS Microbiol. Lett. 144:39-45.
    • (1996) FEMS Microbiol. Lett. , vol.144 , pp. 39-45
    • Grab, D.J.1    Kennedy, R.2    Philipp, M.T.3
  • 21
    • 0029117215 scopus 로고
    • Adherence of Borrelia burgdorferi to the proteoglycan decorin
    • Guo, P. B., S. J. Norris, L. C. Rosenberg, and M. Hook. 1995. Adherence of Borrelia burgdorferi to the proteoglycan decorin. Infect. Immun. 69:3467-3472.
    • (1995) Infect. Immun. , vol.69 , pp. 3467-3472
    • Guo, P.B.1    Norris, S.J.2    Rosenberg, L.C.3    Hook, M.4
  • 22
    • 0031925530 scopus 로고    scopus 로고
    • Active and passive immunity against Borrelia burgdorferi decorin binding protein A (DbpA) protects against infection
    • Hanson, M. S., D. R. Cassatt, P. B. Guo, N. K. Patel, M. P. McCarthy, D. W. Dorward, and M. Hook. 1998. Active and passive immunity against Borrelia burgdorferi decorin binding protein A (DbpA) protects against infection. Infect. Immun. 66:2143-2153.
    • (1998) Infect. Immun. , vol.66 , pp. 2143-2153
    • Hanson, M.S.1    Cassatt, D.R.2    Guo, P.B.3    Patel, N.K.4    McCarthy, M.P.5    Dorward, D.W.6    Hook, M.7
  • 23
    • 0032767986 scopus 로고    scopus 로고
    • Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells
    • Joh, D., E. R. Wann, B. Kreikemeyer, P. Speziale, and M. Hook. 1999. Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells. Matrix Biol. 18:211-223.
    • (1999) Matrix Biol. , vol.18 , pp. 211-223
    • Joh, D.1    Wann, E.R.2    Kreikemeyer, B.3    Speziale, P.4    Hook, M.5
  • 24
    • 0025087320 scopus 로고
    • Motility of Lyme disease spirochetes in fluids as viscous as the extracellular matrix
    • Kimsey, R. B., and A. Spielman. 1990. Motility of Lyme disease spirochetes in fluids as viscous as the extracellular matrix. J. Infect. Dis. 162:1205-1208.
    • (1990) J. Infect. Dis. , vol.162 , pp. 1205-1208
    • Kimsey, R.B.1    Spielman, A.2
  • 25
    • 0023084416 scopus 로고
    • An improved colloidal silver staining method of protein blots on nitrocellulose membranes
    • Kovarik, A., K. Hlubinova, A. Vrbenska, and J. Prachar. 1987. An improved colloidal silver staining method of protein blots on nitrocellulose membranes. Folia Biol. (Prague) 33:253-257.
    • (1987) Folia Biol. (Prague) , vol.33 , pp. 253-257
    • Kovarik, A.1    Hlubinova, K.2    Vrbenska, A.3    Prachar, J.4
  • 26
    • 0035168796 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular matrix and growth control
    • Kresse, H., and E. Schonherr. 2001. Proteoglycans of the extracellular matrix and growth control. J. Cell. Physiol. 189:266-274.
    • (2001) J. Cell. Physiol. , vol.189 , pp. 266-274
    • Kresse, H.1    Schonherr, E.2
  • 27
    • 0036758402 scopus 로고    scopus 로고
    • Size control of decorin dermatan sulfate during remodeling of collagen fibrils in healing skin
    • Kuwaba, K., M. Kobayashi, Y. Nomura, S. Irie, and Y. Koyama. 2001. Size control of decorin dermatan sulfate during remodeling of collagen fibrils in healing skin. J. Dermatol. Sci. 29:185-194.
    • (2001) J. Dermatol. Sci. , vol.29 , pp. 185-194
    • Kuwaba, K.1    Kobayashi, M.2    Nomura, Y.3    Irie, S.4    Koyama, Y.5
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0038325663 scopus 로고    scopus 로고
    • CNE, a collagen-binding protein of Streptococcus equi
    • Lannergard, J., L. Frykberg, and B. Guss. 2003. CNE, a collagen-binding protein of Streptococcus equi. FEMS Microbiol. Lett. 222:69-74.
    • (2003) FEMS Microbiol. Lett. , vol.222 , pp. 69-74
    • Lannergard, J.1    Frykberg, L.2    Guss, B.3
  • 30
    • 0031888094 scopus 로고    scopus 로고
    • Different classes of proteoglycans contribute to the attachment of Borrelia burgdorferi to cultured endothelial and brain cells
    • Leong, J. M., H. Wang, L. Magoun, J. A. Field, P. E. Morrissey, D. Robbins, J. B. Tatro, J. Corburn, and N. Parveen. 1998. Different classes of proteoglycans contribute to the attachment of Borrelia burgdorferi to cultured endothelial and brain cells. Infect. Immun. 66:994-999.
    • (1998) Infect. Immun. , vol.66 , pp. 994-999
    • Leong, J.M.1    Wang, H.2    Magoun, L.3    Field, J.A.4    Morrissey, P.E.5    Robbins, D.6    Tatro, J.B.7    Corburn, J.8    Parveen, N.9
  • 31
    • 0034112496 scopus 로고    scopus 로고
    • Variable small protein (Vsp)-dependent and Vsp-independent pathways for glycosaminoglycan recognition by relapsing fever spirochaetes
    • Magoun, L., W. R. Zuckert, D. Robbins, N. Parveen, K. R. Alugupalli, T. G. Schwan, A. G. Barbour, and J. M. Leong. 2000. Variable small protein (Vsp)-dependent and Vsp-independent pathways for glycosaminoglycan recognition by relapsing fever spirochaetes. Mol. Microbiol. 36:886-897.
    • (2000) Mol. Microbiol. , vol.36 , pp. 886-897
    • Magoun, L.1    Zuckert, W.R.2    Robbins, D.3    Parveen, N.4    Alugupalli, K.R.5    Schwan, T.G.6    Barbour, A.G.7    Leong, J.M.8
  • 33
    • 0032822616 scopus 로고    scopus 로고
    • The effect of motility and cell-surface polymers on bacterial attachment
    • Morisaki, H., S. Nagai, H. Ohshima, E. Ikemoto, and K. Kogure. 1999. The effect of motility and cell-surface polymers on bacterial attachment. Microbiology 145:2797-2802.
    • (1999) Microbiology , vol.145 , pp. 2797-2802
    • Morisaki, H.1    Nagai, S.2    Ohshima, H.3    Ikemoto, E.4    Kogure, K.5
  • 35
    • 0345268707 scopus 로고    scopus 로고
    • Clinical isolates of Enterococcus faecium exhibit strain-specific collagen binding mediated by Acm, a new member of the MSCRAMM family
    • Nallapareddy, S. R., G. M. Weinstock, and B. E. Murray. 2003. Clinical isolates of Enterococcus faecium exhibit strain-specific collagen binding mediated by Acm, a new member of the MSCRAMM family. Mol. Microbiol. 47:1733-1743.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1733-1743
    • Nallapareddy, S.R.1    Weinstock, G.M.2    Murray, B.E.3
  • 36
    • 0021845918 scopus 로고
    • Matrix-driven translocation of cells and nonliving particles
    • Newman, S. A., D. A. Frenz, J. J. Tomasek, and D. D. Rabuzzi. 1985. Matrix-driven translocation of cells and nonliving particles. Science 228:885-889.
    • (1985) Science , vol.228 , pp. 885-889
    • Newman, S.A.1    Frenz, D.A.2    Tomasek, J.J.3    Rabuzzi, D.D.4
  • 37
    • 0026488056 scopus 로고
    • Low-passage-associated proteins of Borrelia burgdorferi B31: Characterization and molecular cloning of OspD, a surface-exposed, plasmid-encoded lipoprotein
    • Norris, S. J., C. J. Carter, J. K. Howell, and A. G. Barbour. 1992. Low-passage-associated proteins of Borrelia burgdorferi B31: characterization and molecular cloning of OspD, a surface-exposed, plasmid-encoded lipoprotein. Infect. Immun. 60:4662-4672.
    • (1992) Infect. Immun. , vol.60 , pp. 4662-4672
    • Norris, S.J.1    Carter, C.J.2    Howell, J.K.3    Barbour, A.G.4
  • 38
    • 0029057891 scopus 로고
    • High- and low-infectivity phenotypes of clonal populations of in vitro-cultured Borrelia burgdorferi
    • Norris, S. J., J. K. Howell, S. A. Garza, M. S. Ferdows, and A. G. Barbour. 1995. High- and low-infectivity phenotypes of clonal populations of in vitro-cultured Borrelia burgdorferi. Infect. Immun. 63:2206-2212.
    • (1995) Infect. Immun. , vol.63 , pp. 2206-2212
    • Norris, S.J.1    Howell, J.K.2    Garza, S.A.3    Ferdows, M.S.4    Barbour, A.G.5
  • 39
    • 0346666691 scopus 로고    scopus 로고
    • Adaptation of the Lyme disease spirochete to the mammalian host environment results in enhanced glycosaminoglycan and host cell binding
    • Parveen, N., M. J. Caimano, J. D. Radolf, and J. M. Leong. 2003. Adaptation of the Lyme disease spirochete to the mammalian host environment results in enhanced glycosaminoglycan and host cell binding. Mol. Microbiol. 47:1433-1444.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1433-1444
    • Parveen, N.1    Caimano, M.J.2    Radolf, J.D.3    Leong, J.M.4
  • 40
    • 0034096379 scopus 로고    scopus 로고
    • Identification of a candidate glycosaminoglycan-binding adhesin of the Lyme disease spirochete Borrelia burgdorferi
    • Parveen, N., and J. M. Leong. 2000. Identification of a candidate glycosaminoglycan-binding adhesin of the Lyme disease spirochete Borrelia burgdorferi. Mol. Microbiol. 35:1220-1234.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1220-1234
    • Parveen, N.1    Leong, J.M.2
  • 41
    • 0033051017 scopus 로고    scopus 로고
    • Strain variation in glycosaminoglycan recognition influences cell-type-specific binding by Lyme disease spirochetes
    • Parveen, N., D. Robbins, and J. M. Leong. 1999. Strain variation in glycosaminoglycan recognition influences cell-type-specific binding by Lyme disease spirochetes. Infect. Immun. 67:1743-1749.
    • (1999) Infect. Immun. , vol.67 , pp. 1743-1749
    • Parveen, N.1    Robbins, D.2    Leong, J.M.3
  • 42
    • 0035007253 scopus 로고    scopus 로고
    • Mapping the ligand-binding region of Borrelia burgdorferi fibronectin-binding protein BBK32
    • Probert, W. S., J. H. Kim, M. Hook, and B. J. Johnson. 2001. Mapping the ligand-binding region of Borrelia burgdorferi fibronectin-binding protein BBK32. Infect. Immun. 69:4129-4133.
    • (2001) Infect. Immun. , vol.69 , pp. 4129-4133
    • Probert, W.S.1    Kim, J.H.2    Hook, M.3    Johnson, B.J.4
  • 43
    • 0002946694 scopus 로고    scopus 로고
    • Natural history of Lyme disease
    • D. W. Rahn and J. Evans (ed.). American College of Physicians, Philadelphia, Pa
    • Rahn, D. W. 1998. Natural history of Lyme disease, p. 35-48. In D. W. Rahn and J. Evans (ed.), Lyme disease. American College of Physicians, Philadelphia, Pa.
    • (1998) Lyme Disease , pp. 35-48
    • Rahn, D.W.1
  • 44
    • 0027158861 scopus 로고
    • The cryptic ospC gene of Borrelia burgdorferi B31 is located on a circular plasmid
    • Sadziene, A., B. Wilske, M. S. Ferdows, and A. G. Barbour. 1993. The cryptic ospC gene of Borrelia burgdorferi B31 is located on a circular plasmid. Infect. Immun. 61:2192-2195.
    • (1993) Infect. Immun. , vol.61 , pp. 2192-2195
    • Sadziene, A.1    Wilske, B.2    Ferdows, M.S.3    Barbour, A.G.4
  • 45
    • 0028915521 scopus 로고
    • Decorin-type I collagen interaction. Presence of separate core protein-binding domains
    • Schonherr, E., H. Hausser, L. Beavan, and H. Kresse. 1995. Decorin-type I collagen interaction. Presence of separate core protein-binding domains. J. Biol. Chem. 270:8877-8883.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8877-8883
    • Schonherr, E.1    Hausser, H.2    Beavan, L.3    Kresse, H.4
  • 46
    • 0037408416 scopus 로고    scopus 로고
    • Adhesive surface proteins of Erysipelothrix rhusiopathiae bind to polystyrene, fibronectin, and type I and IV collagens
    • Shimoji, Y., Y. Ogawa, M. Osaki, H. Kabeya, S. Maruyama, T. Mikami, and T. Sekizaki. 2003. Adhesive surface proteins of Erysipelothrix rhusiopathiae bind to polystyrene, fibronectin, and type I and IV collagens. J. Bacteriol. 185:2739-2748.
    • (2003) J. Bacteriol. , vol.185 , pp. 2739-2748
    • Shimoji, Y.1    Ogawa, Y.2    Osaki, M.3    Kabeya, H.4    Maruyama, S.5    Mikami, T.6    Sekizaki, T.7
  • 47
    • 0037387120 scopus 로고    scopus 로고
    • In vitro susceptibility testing of four antibiotics against Borrelia burgdorferi: A comparison of results for the three genospecies Borrelia afzelii, Borrelia garinii, and Borrelia burgdorferi sensu stricto
    • Sicklinger, M., R. Wienecke, and U. Neubert. 2003. In vitro susceptibility testing of four antibiotics against Borrelia burgdorferi: a comparison of results for the three genospecies Borrelia afzelii, Borrelia garinii, and Borrelia burgdorferi sensu stricto. J. Clin. Microbiol. 41:1791-1793.
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 1791-1793
    • Sicklinger, M.1    Wienecke, R.2    Neubert, U.3
  • 48
    • 0033753245 scopus 로고    scopus 로고
    • Downregulation of class II molecules on epidermal Langerhans cells in Lyme borreliosis
    • Silberer, M., F. Koszik, G. Stingl, and E. Aberer. 2000. Downregulation of class II molecules on epidermal Langerhans cells in Lyme borreliosis. Br. J. Dermatol. 143:786-794.
    • (2000) Br. J. Dermatol. , vol.143 , pp. 786-794
    • Silberer, M.1    Koszik, F.2    Stingl, G.3    Aberer, E.4
  • 50
    • 0031717878 scopus 로고    scopus 로고
    • Decorin gene transfer-mediated suppression of TGF-beta synthesis abrogates experimental malignant glioma growth in vivo
    • Stander, M., U. Naumann, L. Dumitrescu, M. Heneka, P. Loschmann, E. Gulbins, J. Dichgans, and M. Weller. 1998. Decorin gene transfer-mediated suppression of TGF-beta synthesis abrogates experimental malignant glioma growth in vivo. Gene Ther. 5:1187-1194.
    • (1998) Gene Ther. , vol.5 , pp. 1187-1194
    • Stander, M.1    Naumann, U.2    Dumitrescu, L.3    Heneka, M.4    Loschmann, P.5    Gulbins, E.6    Dichgans, J.7    Weller, M.8
  • 52
    • 0029098129 scopus 로고
    • Decorin-binding sites for collagen type I are mainly located in leucine-rich repeats 4-5
    • Svensson, L., D. Heinegard, and A. OIdberg. 1995. Decorin-binding sites for collagen type I are mainly located in leucine-rich repeats 4-5. J. Biol. Chem. 270:20712-20716.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20712-20716
    • Svensson, L.1    Heinegard, D.2    Oidberg, A.3
  • 53
    • 0033939582 scopus 로고    scopus 로고
    • Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG-S motifs in the amino-terminal half of the protein involved in collagen binding
    • Tahir, Y. E., P. Kuusela, and M. Skurnik. 2000. Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG-S motifs in the amino-terminal half of the protein involved in collagen binding. Mol. Microbiol. 37:192-206.
    • (2000) Mol. Microbiol. , vol.37 , pp. 192-206
    • Tahir, Y.E.1    Kuusela, P.2    Skurnik, M.3
  • 54
    • 0031444004 scopus 로고    scopus 로고
    • Adherence of human oral spirochetes by collagen-binding proteins
    • Umemoto, T., M. Li, and I. Namikawa. 1997. Adherence of human oral spirochetes by collagen-binding proteins. Microbiol. Immunol. 41:917-923.
    • (1997) Microbiol. Immunol. , vol.41 , pp. 917-923
    • Umemoto, T.1    Li, M.2    Namikawa, I.3
  • 55
    • 0028106461 scopus 로고
    • Binding of host-associated treponeme proteins to collagens and laminin: A possible mechanism of spirochetal adherence to host tissues
    • Umemoto, T., and I. Namikawa. 1994. Binding of host-associated treponeme proteins to collagens and laminin: a possible mechanism of spirochetal adherence to host tissues. Microbiol. Immunol. 38:655-663.
    • (1994) Microbiol. Immunol. , vol.38 , pp. 655-663
    • Umemoto, T.1    Namikawa, I.2
  • 56
    • 0002522145 scopus 로고
    • Glycosaminoglycans and proteoglycans
    • P. D. Yurchenco, D. E. Birk, and R. P. Mechan (ed.). Academic Press, New York, N.Y.
    • Vogel, K. G. 1994. Glycosaminoglycans and proteoglycans, p. 243-279. In P. D. Yurchenco, D. E. Birk, and R. P. Mechan (ed.), Extracellular matrix assembly and structure. Academic Press, New York, N.Y.
    • (1994) Extracellular Matrix Assembly and Structure , pp. 243-279
    • Vogel, K.G.1
  • 57
    • 0021715115 scopus 로고
    • Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon
    • Vogel, K. G., M. Paulsson, and D. Heinegard. 1984. Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem. J. 223:587-597.
    • (1984) Biochem. J. , vol.223 , pp. 587-597
    • Vogel, K.G.1    Paulsson, M.2    Heinegard, D.3
  • 58
    • 0242269883 scopus 로고    scopus 로고
    • Selective up-regulation of matrix metalloproteinase-9 expression in human erythema migrans skin lesions of acute Lyme disease
    • Zhao, Z., H. Chang, R. P. Trevino, K. Whren, J. Bhawan, and M. S. Klempner. 2003. Selective up-regulation of matrix metalloproteinase-9 expression in human erythema migrans skin lesions of acute Lyme disease. J. Infect. Dis. 188:1098-1104.
    • (2003) J. Infect. Dis. , vol.188 , pp. 1098-1104
    • Zhao, Z.1    Chang, H.2    Trevino, R.P.3    Whren, K.4    Bhawan, J.5    Klempner, M.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.