메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages 973-980

Vitronectin in host pathogen interactions and antimicrobial therapeutic applications

Author keywords

Bacteria; Complement system; Extracellular matrix; Innate immunity; Integrins; Vitronectin

Indexed keywords

BACTERIA (MICROORGANISMS); EUKARYOTA;

EID: 81755161453     PISSN: 1895104X     EISSN: 16443632     Source Type: Journal    
DOI: 10.2478/s11535-011-0077-x     Document Type: Review
Times cited : (6)

References (68)
  • 1
    • 0031746579 scopus 로고    scopus 로고
    • Role of vitronectin and its receptors in haemostasis and vascular remodeling
    • Preissner K. T., Seiffert D., Role of vitronectin and its receptors in haemostasis and vascular remodeling, Thromb. Res., 1998, 89, 1-21.
    • (1998) Thromb. Res. , vol.89 , pp. 1-21
    • Preissner, K.T.1    Seiffert, D.2
  • 2
    • 82155181745 scopus 로고    scopus 로고
    • A forward loop between glioma and microglia: Glioma-derived extracellular matrix-activated microglia secrete IL-18 to enhance the migration of glioma cells, J
    • DOI: 10. 1002/jcp. 22746
    • Yeh W. L., Lu D. Y., Liou H. C., Fu W. M., A forward loop between glioma and microglia: Glioma-derived extracellular matrix-activated microglia secrete IL-18 to enhance the migration of glioma cells, J. Cell Physiol., 2011, DOI: 10. 1002/jcp. 22746.
    • (2011) Cell Physiol
    • Yeh, W.L.1    Lu, D.Y.2    Liou, H.C.3    Fu, W.M.4
  • 3
    • 33646845673 scopus 로고    scopus 로고
    • Vitronectin in atherosclerotic disease
    • Ekmekci O. B., Ekmekci H., Vitronectin in atherosclerotic disease, Clin. Chim. Acta., 2006, 368, 77-83.
    • (2006) Clin. Chim. Acta. , vol.368 , pp. 77-83
    • Ekmekci, O.B.1    Ekmekci, H.2
  • 4
    • 24044505137 scopus 로고    scopus 로고
    • Vitronectin: a possible determinant of adenovirus type 19 tropism for human corneal epithelium
    • Xiao J., Natarajan K., Rajala M. S., Astley R. A., Ramadan R. T., Chodosh J., Vitronectin: a possible determinant of adenovirus type 19 tropism for human corneal epithelium, Am. J. Ophthalmol., 2005, 140, 363-369.
    • (2005) Am. J. Ophthalmol. , vol.140 , pp. 363-369
    • Xiao, J.1    Natarajan, K.2    Rajala, M.S.3    Astley, R.A.4    Ramadan, R.T.5    Chodosh, J.6
  • 5
    • 70349437186 scopus 로고    scopus 로고
    • Complement regulators and inhibitory proteins
    • Zipfel P. F., Skerka C., Complement regulators and inhibitory proteins, Nat. Rev. Immunol., 2009, 9, 729-740.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 729-740
    • Zipfel, P.F.1    Skerka, C.2
  • 6
    • 0023389423 scopus 로고
    • Specific binding of the human S protein (vitronectin) to streptococci, Staphylococcus aureus, and Escherichia coli
    • Chhatwal G. S., Preissner K. T., Muller-Berghaus G., Blobel H., Specific binding of the human S protein (vitronectin) to streptococci, Staphylococcus aureus, and Escherichia coli, Infect. Immun., 1987, 55, 1878-1883.
    • (1987) Infect. Immun. , vol.55 , pp. 1878-1883
    • Chhatwal, G.S.1    Preissner, K.T.2    Muller-Berghaus, G.3    Blobel, H.4
  • 7
    • 77958565410 scopus 로고    scopus 로고
    • Vitronectin in bacterial pathogenesis: a host protein used in complement escape and cellular invasion
    • Singh B., Su Y. C., Riesbeck K., Vitronectin in bacterial pathogenesis: a host protein used in complement escape and cellular invasion, Mol. Microbiol., 2010, 78, 545-560.
    • (2010) Mol. Microbiol. , vol.78 , pp. 545-560
    • Singh, B.1    Su, Y.C.2    Riesbeck, K.3
  • 8
    • 61949389320 scopus 로고    scopus 로고
    • Integrinlinked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells
    • Bergmann S., Lang A., Rohde M., Agarwal V., Rennemeier C., Grashoff C., et al., Integrinlinked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells, J. Cell Sci., 2009, 122, 256-267.
    • (2009) J.Cell Sci. , vol.122 , pp. 256-267
    • Bergmann, S.1    Lang, A.2    Rohde, M.3    Agarwal, V.4    Rennemeier, C.5    Grashoff, C.6
  • 9
    • 77954067912 scopus 로고    scopus 로고
    • Neisseria meningitidis Opc invasin binds to the sulphated tyrosines of activated vitronectin to attach to and invade human brain endothelial cells
    • Sa E. C. C., Griffiths N. J., Virji M., Neisseria meningitidis Opc invasin binds to the sulphated tyrosines of activated vitronectin to attach to and invade human brain endothelial cells, PLoS Pathog., 2010, 6, e1000911.
    • (2010) PLoS Pathog. , vol.6
    • Sa, E.C.C.1    Griffiths, N.J.2    Virji, M.3
  • 10
    • 0025831155 scopus 로고
    • Structure and biological role of vitronectin
    • Preissner K. T., Structure and biological role of vitronectin, Annu. Rev. Cell. Biol., 1991, 7, 275-310.
    • (1991) Annu. Rev. Cell. Biol. , vol.7 , pp. 275-310
    • Preissner, K.T.1
  • 11
    • 0031954123 scopus 로고    scopus 로고
    • Binding sites on native and multimeric vitronectin exhibit similar affinity for heparin the influence of self-association and multivalence on ligand binding
    • Peterson C. B., Binding sites on native and multimeric vitronectin exhibit similar affinity for heparin the influence of self-association and multivalence on ligand binding, Trends Cardiovasc. Med., 1998, 8, 124-131.
    • (1998) Trends Cardiovasc. Med. , vol.8 , pp. 124-131
    • Peterson, C.B.1
  • 12
    • 0030900930 scopus 로고    scopus 로고
    • Native and multimeric vitronectin exhibit similar affinity for heparin. Differences in heparin binding properties induced upon denaturation are due to self-association into a multivalent form
    • Zhuang P., Chen A. I., Peterson C. B., Native and multimeric vitronectin exhibit similar affinity for heparin. Differences in heparin binding properties induced upon denaturation are due to self-association into a multivalent form, J. Biol. Chem., 1997, 272, 6858-6867.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6858-6867
    • Zhuang, P.1    Chen, A.I.2    Peterson, C.B.3
  • 13
    • 0027422577 scopus 로고
    • Binding and processing of multimeric vitronectin by vascular endothelial cells
    • Volker W., Hess S., Vischer P., Preissner K. T., Binding and processing of multimeric vitronectin by vascular endothelial cells, J. Histochem. Cytochem., 1993, 41, 1823-1832.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1823-1832
    • Volker, W.1    Hess, S.2    Vischer, P.3    Preissner, K.T.4
  • 14
    • 64349111953 scopus 로고    scopus 로고
    • Interactions of plasminogen activator inhibitor-1 with vitronectin involve an extensive binding surface and induce mutual conformational rearrangements
    • Blouse G. E., Dupont D. M., Schar C. R., Jensen J. K., Minor K. H., Anagli J. Y., et al., Interactions of plasminogen activator inhibitor-1 with vitronectin involve an extensive binding surface and induce mutual conformational rearrangements, Biochemistry, 2009, 48, 1723-1735.
    • (2009) Biochemistry , vol.48 , pp. 1723-1735
    • Blouse, G.E.1    Dupont, D.M.2    Schar, C.R.3    Jensen, J.K.4    Minor, K.H.5    Anagli, J.Y.6
  • 15
    • 0037155822 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor type 1 promotes the self-association of vitronectin into complexes exhibiting altered incorporation into the extracellular matrix
    • Minor K. H., Peterson C. B., Plasminogen activator inhibitor type 1 promotes the self-association of vitronectin into complexes exhibiting altered incorporation into the extracellular matrix, J. Biol. Chem., 2002, 277, 10337-10345.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10337-10345
    • Minor, K.H.1    Peterson, C.B.2
  • 16
    • 0036646067 scopus 로고    scopus 로고
    • New insights into heparin binding to vitronectin: studies with monoclonal antibodies
    • Underwood P. A., Kirkpatrick A., Mitchell S. M., New insights into heparin binding to vitronectin: studies with monoclonal antibodies, Biochem. J., 2002, 365, 57-67.
    • (2002) Biochem. J. , vol.365 , pp. 57-67
    • Underwood, P.A.1    Kirkpatrick, A.2    Mitchell, S.M.3
  • 17
    • 0029847859 scopus 로고    scopus 로고
    • The behaviour of human vitronectin in vivo: effects of complement activation, conformation and phosphorylation
    • Peake P. W., Greenstein J. D., Pussell B. A., Charlesworth J. A., The behaviour of human vitronectin in vivo: effects of complement activation, conformation and phosphorylation, Clin. Exp. Immunol., 1996, 106, 416-422.
    • (1996) Clin. Exp. Immunol. , vol.106 , pp. 416-422
    • Peake, P.W.1    Greenstein, J.D.2    Pussell, B.A.3    Charlesworth, J.A.4
  • 18
    • 3242699717 scopus 로고    scopus 로고
    • uPA and uPAR in fibrinolysis, immunity and pathology
    • Mondino A., Blasi F., uPA and uPAR in fibrinolysis, immunity and pathology, Trends Immunol., 2004, 25, 450-455.
    • (2004) Trends Immunol. , vol.25 , pp. 450-455
    • Mondino, A.1    Blasi, F.2
  • 19
    • 77956520647 scopus 로고    scopus 로고
    • The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1
    • Haiko J., Laakkonen L., Juuti K., Kalkkinen N., Korhonen T. K., The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1, J. Bacteriol., 2010, 192, 4553-4561.
    • (2010) J. Bacteriol. , vol.192 , pp. 4553-4561
    • Haiko, J.1    Laakkonen, L.2    Juuti, K.3    Kalkkinen, N.4    Korhonen, T.K.5
  • 20
    • 33846922738 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor type 1 is protective during severe Gram-negative pneumonia
    • Renckens R., Roelofs J. J., Bonta P. I., Florquin S., de Vries C. J., Levi M., et al., Plasminogen activator inhibitor type 1 is protective during severe Gram-negative pneumonia, Blood, 2007, 109, 1593-1601.
    • (2007) Blood , vol.109 , pp. 1593-1601
    • Renckens, R.1    Roelofs, J.J.2    Bonta, P.I.3    Florquin, S.4    de Vries, C.J.5    Levi, M.6
  • 21
    • 18844375381 scopus 로고    scopus 로고
    • Pleiotropic functions of plasminogen activator inhibitor-1
    • Lijnen H. R., Pleiotropic functions of plasminogen activator inhibitor-1, J. Thromb. Haemost., 2005, 3, 35-45.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 35-45
    • Lijnen, H.R.1
  • 22
    • 51949083035 scopus 로고    scopus 로고
    • Helicobacter pylori infection stimulates plasminogen activator inhibitor 1 production by gastric epithelial cells
    • Keates A. C., Tummala S., Peek R. M., Jr., Csizmadia E., Kunzli B., Becker K., et al., Helicobacter pylori infection stimulates plasminogen activator inhibitor 1 production by gastric epithelial cells, Infect. Immun., 2008, 76, 3992-3999.
    • (2008) Infect. Immun. , vol.76 , pp. 3992-3999
    • Keates, A.C.1    Tummala, S.2    Peek Jr., R.M.3    Csizmadia, E.4    Kunzli, B.5    Becker, K.6
  • 23
    • 66449098781 scopus 로고    scopus 로고
    • Activation of plasminogen activator inhibitor implicates protease InhA in the acute-phase response to Bacillus anthracis infection
    • Chung M. C., Jorgensen S. C., Popova T. G., Tonry J. H., Bailey C. L., Popov S. G., Activation of plasminogen activator inhibitor implicates protease InhA in the acute-phase response to Bacillus anthracis infection, J. Med. Microbiol., 2009, 58, 737-744.
    • (2009) J. Med. Microbiol. , vol.58 , pp. 737-744
    • Chung, M.C.1    Jorgensen, S.C.2    Popova, T.G.3    Tonry, J.H.4    Bailey, C.L.5    Popov, S.G.6
  • 24
    • 0035816636 scopus 로고    scopus 로고
    • The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis Cleaves and inactivates plasminogen activator inhibitor type 1
    • Urano T., Ihara H., Umemura K., Suzuki Y., Oike M., Akita S., et al., The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis Cleaves and inactivates plasminogen activator inhibitor type 1, J. Biol. Chem., 2001, 276, 24690-24696.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24690-24696
    • Urano, T.1    Ihara, H.2    Umemura, K.3    Suzuki, Y.4    Oike, M.5    Akita, S.6
  • 26
    • 39749156319 scopus 로고    scopus 로고
    • The human fibrinolytic system is a target for the staphylococcal metalloprotease aureolysin
    • Beaufort N., Wojciechowski P., Sommerhoff C. P., Szmyd G., Dubin G., Eick S., et al., The human fibrinolytic system is a target for the staphylococcal metalloprotease aureolysin, Biochem. J., 2008, 410, 157-165.
    • (2008) Biochem. J. , vol.410 , pp. 157-165
    • Beaufort, N.1    Wojciechowski, P.2    Sommerhoff, C.P.3    Szmyd, G.4    Dubin, G.5    Eick, S.6
  • 27
    • 0027893017 scopus 로고
    • A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
    • Kapur V., Topouzis S., Majesky M. W., Li L. L., Hamrick M. R., Hamill R. J., et al., A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin, Microb. Pathog., 1993, 15, 327-346.
    • (1993) Microb. Pathog. , vol.15 , pp. 327-346
    • Kapur, V.1    Topouzis, S.2    Majesky, M.W.3    Li, L.L.4    Hamrick, M.R.5    Hamill, R.J.6
  • 28
    • 35048837277 scopus 로고    scopus 로고
    • Cwp84, a surface-associated protein of Clostridium difficile, is a cysteine protease with degrading activity on extracellular matrix proteins
    • Janoir C., Pechine S., Grosdidier C., Collignon A., Cwp84, a surface-associated protein of Clostridium difficile, is a cysteine protease with degrading activity on extracellular matrix proteins, J. Bacteriol., 2007, 189, 7174-7180.
    • (2007) J. Bacteriol. , vol.189 , pp. 7174-7180
    • Janoir, C.1    Pechine, S.2    Grosdidier, C.3    Collignon, A.4
  • 29
    • 68249086824 scopus 로고    scopus 로고
    • Complement evasion strategies of pathogens-acquisition of inhibitors and beyond
    • Blom A. M., Hallstrom T., Riesbeck K., Complement evasion strategies of pathogens-acquisition of inhibitors and beyond, Mol. Immunol., 2009, 46, 2808-2817.
    • (2009) Mol. Immunol. , vol.46 , pp. 2808-2817
    • Blom, A.M.1    Hallstrom, T.2    Riesbeck, K.3
  • 30
    • 70149120375 scopus 로고    scopus 로고
    • Nontypeable Haemophilus influenzae protein E binds vitronectin and is important for serum resistance
    • Hallstrom T., Blom A. M., Zipfel P. F., Riesbeck K., Nontypeable Haemophilus influenzae protein E binds vitronectin and is important for serum resistance, J. Immunol., 2009, 183, 2593-2601.
    • (2009) J. Immunol. , vol.183 , pp. 2593-2601
    • Hallstrom, T.1    Blom, A.M.2    Zipfel, P.F.3    Riesbeck, K.4
  • 31
    • 33745324685 scopus 로고    scopus 로고
    • Haemophilus influenzae surface fibrils contribute to serum resistance by interacting with vitronectin
    • Hallstrom T., Trajkovska E., Forsgren A., Riesbeck K., Haemophilus influenzae surface fibrils contribute to serum resistance by interacting with vitronectin, J. Immunol., 2006, 177, 430-436.
    • (2006) J. Immunol. , vol.177 , pp. 430-436
    • Hallstrom, T.1    Trajkovska, E.2    Forsgren, A.3    Riesbeck, K.4
  • 32
    • 79959572234 scopus 로고    scopus 로고
    • Haemophilus influenzae protein E recognizes the C-terminal domain of vitronectin and modulates the membrane attack complex
    • Singh B., Jalalvand F., Morgelin M., Zipfel P., Blom A. M., Riesbeck K., Haemophilus influenzae protein E recognizes the C-terminal domain of vitronectin and modulates the membrane attack complex, Mol. Microbiol., 2011, 81, 80-98.
    • (2011) Mol. Microbiol. , vol.81 , pp. 80-98
    • Singh, B.1    Jalalvand, F.2    Morgelin, M.3    Zipfel, P.4    Blom, A.M.5    Riesbeck, K.6
  • 33
    • 60549098245 scopus 로고    scopus 로고
    • Localization of the domains of the Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectin
    • Leduc I., Olsen B., Elkins, C., Localization of the domains of the Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectin, Infect. Immun., 2009, 77, 657-666.
    • (2009) Infect. Immun. , vol.77 , pp. 657-666
    • Leduc, I.1    Olsen, B.2    Elkins, C.3
  • 34
    • 33644775555 scopus 로고    scopus 로고
    • Binding of vitronectin by the Moraxella catarrhalis UspA2 protein interferes with late stages of the complement cascade
    • Attia A. S., Ram S., Rice P. A., Hansen E. J., Binding of vitronectin by the Moraxella catarrhalis UspA2 protein interferes with late stages of the complement cascade, Infect. Immun., 2006, 74, 1597-1611.
    • (2006) Infect. Immun. , vol.74 , pp. 1597-1611
    • Attia, A.S.1    Ram, S.2    Rice, P.A.3    Hansen, E.J.4
  • 35
    • 77949396489 scopus 로고    scopus 로고
    • Vitronectin binds to the head region of Moraxella catarrhalis ubiquitous surface protein A2 and confers complement-inhibitory activity
    • Singh B., Blom A. M., Unal C., Nilson B., Morgelin M., Riesbeck K., Vitronectin binds to the head region of Moraxella catarrhalis ubiquitous surface protein A2 and confers complement-inhibitory activity, Mol. Microbiol., 2010, 75, 1426-1444.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1426-1444
    • Singh, B.1    Blom, A.M.2    Unal, C.3    Nilson, B.4    Morgelin, M.5    Riesbeck, K.6
  • 36
    • 0032489349 scopus 로고    scopus 로고
    • Vitronectin-dependent invasion of epithelial cells by Neisseria gonorrhoeae involves alpha(v) integrin receptors
    • Dehio M., Gomez-Duarte O. G., Dehio C., Meyer T. F., Vitronectin-dependent invasion of epithelial cells by Neisseria gonorrhoeae involves alpha(v) integrin receptors, FEBS Lett., 1998, 424, 84-88.
    • (1998) FEBS Lett. , vol.424 , pp. 84-88
    • Dehio, M.1    Gomez-Duarte, O.G.2    Dehio, C.3    Meyer, T.F.4
  • 37
    • 23444447782 scopus 로고
    • Binding and internalization of microorganisms by integrin receptors
    • Isberg R. R., Tran van Nhieu G., Binding and internalization of microorganisms by integrin receptors, Trends Microbiol., 1994, 2, 10-14.
    • (1994) Trends Microbiol. , vol.2 , pp. 10-14
    • Isberg, R.R.1    Tran van nhieu, G.2
  • 38
    • 0031589174 scopus 로고    scopus 로고
    • Identification of novel heparin-binding domains of vitronectin
    • Liang O. D., Rosenblatt S., Chhatwal G. S., Preissner K. T., Identification of novel heparin-binding domains of vitronectin, FEBS Lett., 1997, 407, 169-172.
    • (1997) FEBS Lett. , vol.407 , pp. 169-172
    • Liang, O.D.1    Rosenblatt, S.2    Chhatwal, G.S.3    Preissner, K.T.4
  • 39
    • 0027394326 scopus 로고
    • Vitronectin-mediated inhibition of complement: evidence for different binding sites for C5b-7 and C9
    • Milis L., Morris C. A., Sheehan M. C., Charlesworth J. A., Pussell B. A., Vitronectin-mediated inhibition of complement: evidence for different binding sites for C5b-7 and C9, Clin. Exp. Immunol., 1993, 92, 114-119.
    • (1993) Clin. Exp. Immunol. , vol.92 , pp. 114-119
    • Milis, L.1    Morris, C.A.2    Sheehan, M.C.3    Charlesworth, J.A.4    Pussell, B.A.5
  • 40
    • 0029074354 scopus 로고
    • Complement inhibition by human vitronectin involves non-heparin binding domains
    • Sheehan M., Morris C. A., Pussell B. A., Charlesworth J. A., Complement inhibition by human vitronectin involves non-heparin binding domains, Clin. Exp. Immunol., 1995, 101, 136-141.
    • (1995) Clin. Exp. Immunol. , vol.101 , pp. 136-141
    • Sheehan, M.1    Morris, C.A.2    Pussell, B.A.3    Charlesworth, J.A.4
  • 41
    • 0023887037 scopus 로고
    • The heparin binding domain of S-protein/vitronectin binds to complement components C7, C8, and C9 and perforin from cytolytic T-cells and inhibits their lytic activities
    • Tschopp J., Masson, D., Schafer, S., Peitsch, M., Preissner K. T., The heparin binding domain of S-protein/vitronectin binds to complement components C7, C8, and C9 and perforin from cytolytic T-cells and inhibits their lytic activities, Biochemistry, 1988, 27, 4103-4109.
    • (1988) Biochemistry , vol.27 , pp. 4103-4109
    • Tschopp, J.1    Masson, D.2    Schafer, S.3    Peitsch, M.4    Preissner, K.T.5
  • 42
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • Schmidtchen A., Frick I. M., Andersson E., Tapper H., Bjorck L., Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37, Mol. Microbiol., 2002, 46, 157-168.
    • (2002) Mol. Microbiol. , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.M.2    Andersson, E.3    Tapper, H.4    Bjorck, L.5
  • 43
    • 0035131955 scopus 로고    scopus 로고
    • Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin
    • Schmidtchen A., Frick I. M., Bjorck L., Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin, Mol. Microbiol., 2001, 39, 708-713.
    • (2001) Mol. Microbiol. , vol.39 , pp. 708-713
    • Schmidtchen, A.1    Frick, I.M.2    Bjorck, L.3
  • 45
    • 33745475017 scopus 로고    scopus 로고
    • Bacterial killing by heparin-binding peptides from PRELP and thrombospondin
    • Malmsten M., Davoudi M., Schmidtchen A., Bacterial killing by heparin-binding peptides from PRELP and thrombospondin, Matrix Biol., 2006, 25, 294-300.
    • (2006) Matrix Biol. , vol.25 , pp. 294-300
    • Malmsten, M.1    Davoudi, M.2    Schmidtchen, A.3
  • 46
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin A. D., Weintraub H. J., Molecular modeling of protein-glycosaminoglycan interactions, Arteriosclerosis, 1989, 9, 21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 48
    • 38549153167 scopus 로고    scopus 로고
    • Molecular basis of microbial adherence to prosthetic materials. Role of biofilms in prosthesis-associated infection
    • Vila J., Soriano A., Mensa J., [Molecular basis of microbial adherence to prosthetic materials. Role of biofilms in prosthesis-associated infection], Enferm. Infecc. Microbiol. Clin., 2008, 26, 48-54; quiz 55 (in Spanish).
    • (2008) Enferm. Infecc. Microbiol. Clin. , vol.26 , pp. 48-54
    • Vila, J.1    Soriano, A.2    Mensa, J.3
  • 49
    • 1842483412 scopus 로고    scopus 로고
    • Treatment of infections associated with surgical implants
    • Darouiche R. O., Treatment of infections associated with surgical implants, N. Engl. J. Med., 2004, 350, 1422-1429.
    • (2004) N. Engl. J. Med. , vol.350 , pp. 1422-1429
    • Darouiche, R.O.1
  • 50
    • 0024413691 scopus 로고
    • Conformational changes of plasma fibronectin detected upon adsorption to solid substrates: a spin-label study
    • Narasimhan C., Lai C. S., Conformational changes of plasma fibronectin detected upon adsorption to solid substrates: a spin-label study, Biochemistry, 1989, 28, 5041-5046.
    • (1989) Biochemistry , vol.28 , pp. 5041-5046
    • Narasimhan, C.1    Lai, C.S.2
  • 51
    • 0024581438 scopus 로고
    • Fluorescence energy transfer detects changes in fibronectin structure upon surface binding
    • Wolff C., Lai C. S., Fluorescence energy transfer detects changes in fibronectin structure upon surface binding, Arch. Biochem. Biophys., 1989, 268, 536-545.
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 536-545
    • Wolff, C.1    Lai, C.S.2
  • 52
    • 0030968382 scopus 로고    scopus 로고
    • Vitronectin may mediate staphylococcal adhesion to polymer surfaces in perfusing human cerebrospinal fluid
    • Lundberg F., Schliamser S., Ljungh A., Vitronectin may mediate staphylococcal adhesion to polymer surfaces in perfusing human cerebrospinal fluid, J. Med. Microbiol., 1997, 46, 285-296.
    • (1997) J. Med. Microbiol. , vol.46 , pp. 285-296
    • Lundberg, F.1    Schliamser, S.2    Ljungh, A.3
  • 53
    • 2942733320 scopus 로고    scopus 로고
    • Effect of hydrophilic coating on microorganism colonization in silicone tubing
    • Cagavi F., Akalan N., Celik H., Gur D., Guciz B., Effect of hydrophilic coating on microorganism colonization in silicone tubing, Acta Neurochir. (Wien), 2004, 146, 603-610.
    • (2004) Acta Neurochir. (Wien) , vol.146 , pp. 603-610
    • Cagavi, F.1    Akalan, N.2    Celik, H.3    Gur, D.4    Guciz, B.5
  • 54
    • 61849142128 scopus 로고    scopus 로고
    • Antibacterial and antifouling polymer brushes incorporating antimicrobial peptide
    • Glinel K., Jonas A. M., Jouenne T., Leprince J., Galas L., Huck W. T., Antibacterial and antifouling polymer brushes incorporating antimicrobial peptide, Bioconjug. Chem., 2009, 20, 71-77.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 71-77
    • Glinel, K.1    Jonas, A.M.2    Jouenne, T.3    Leprince, J.4    Galas, L.5    Huck, W.T.6
  • 55
    • 41949087871 scopus 로고    scopus 로고
    • Biofilms: recent developments on an old battle
    • de Carvalho C. C., Biofilms: recent developments on an old battle, Recent Pat. Biotechnol., 2007, 1, 49-57.
    • (2007) Recent Pat. Biotechnol. , vol.1 , pp. 49-57
    • de Carvalho, C.C.1
  • 56
    • 25144493664 scopus 로고    scopus 로고
    • Vancomycin covalently bonded to titanium beads kills Staphylococcus aureus
    • Jose B., Antoci V., Jr., Zeiger A. R., Wickstrom E., Hickok N. J., Vancomycin covalently bonded to titanium beads kills Staphylococcus aureus, Chem. Biol., 2005, 12, 1041-1048.
    • (2005) Chem. Biol. , vol.12 , pp. 1041-1048
    • Jose, B.1    Antoci Jr., V.2    Zeiger, A.R.3    Wickstrom, E.4    Hickok, N.J.5
  • 60
    • 79952187401 scopus 로고    scopus 로고
    • Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces
    • Costa, F., Carvalho, I. F., Montelaro, R. C., Gomes, P. and Martins, M. C., Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces, Acta Biomater., 2011, 7, 1431-1440.
    • (2011) Acta Biomater. , vol.7 , pp. 1431-1440
    • Costa, F.1    Carvalho, I.F.2    Montelaro, R.C.3    Gomes, P.4    Martins, M.C.5
  • 63
    • 0035082302 scopus 로고    scopus 로고
    • Characterization of vitronectin-binding proteins of Staphylococcus epidermidis
    • Li D. Q., Lundberg F., Ljungh A., Characterization of vitronectin-binding proteins of Staphylococcus epidermidis, Curr. Microbiol., 2001, 42, 361-367.
    • (2001) Curr. Microbiol. , vol.42 , pp. 361-367
    • Li, D.Q.1    Lundberg, F.2    Ljungh, A.3
  • 65
    • 0023848491 scopus 로고
    • Deposition of terminal C5b-9 complement complexes on erythrocytes and leukocytes during cardiopulmonary bypass
    • Salama A., Hugo F., Heinrich D., Hoge R., Muller R., Kiefel V., et al., Deposition of terminal C5b-9 complement complexes on erythrocytes and leukocytes during cardiopulmonary bypass, N. Engl. J. Med., 1988, 318, 408-414.
    • (1988) N. Engl. J. Med. , vol.318 , pp. 408-414
    • Salama, A.1    Hugo, F.2    Heinrich, D.3    Hoge, R.4    Muller, R.5    Kiefel, V.6
  • 66
    • 0031038359 scopus 로고    scopus 로고
    • Vitronectin-binding staphylococci enhance surface-associated complement activation
    • Lundberg F., Lea T., Ljungh A., Vitronectin-binding staphylococci enhance surface-associated complement activation, Infect. Immun., 1997, 65, 897-902.
    • (1997) Infect. Immun. , vol.65 , pp. 897-902
    • Lundberg, F.1    Lea, T.2    Ljungh, A.3
  • 67
    • 0032948821 scopus 로고    scopus 로고
    • Presence of vitronectin and activated complement factor C9 on ventriculoperitoneal shunts and temporary ventricular drainage catheters
    • Lundberg F., Li D. Q., Falkenback D., Lea T., Siesjo P., Soderstrom S., et al., Presence of vitronectin and activated complement factor C9 on ventriculoperitoneal shunts and temporary ventricular drainage catheters, J. Neurosurg., 1999, 90, 101-108.
    • (1999) J. Neurosurg. , vol.90 , pp. 101-108
    • Lundberg, F.1    Li, D.Q.2    Falkenback, D.3    Lea, T.4    Siesjo, P.5    Soderstrom, S.6
  • 68
    • 0031578234 scopus 로고    scopus 로고
    • The hemopexin-type repeats of human vitronectin are recognized by Streptococcus pyogenes
    • Liang O. D., Preissner K. T., Chhatwal G. S., The hemopexin-type repeats of human vitronectin are recognized by Streptococcus pyogenes, Biochem. Biophys. Res. Commun., 1997, 234, 445-449.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 445-449
    • Liang, O.D.1    Preissner, K.T.2    Chhatwal, G.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.