메뉴 건너뛰기




Volumn 41, Issue 1, 1998, Pages 120-130

Surface analysis of human plasma fibronectin adsorbed to commercially pure titanium materials

Author keywords

Atomic force microscopy; Contact angle; Fibronectin; Implant surface; Titanium

Indexed keywords

ADSORPTION; ATOMIC FORCE MICROSCOPY; BLOOD; CONTACT ANGLE; PROTEINS; TITANIUM;

EID: 0032126449     PISSN: 00219304     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4636(199807)41:1<120::AID-JBM15>3.0.CO;2-R     Document Type: Article
Times cited : (126)

References (62)
  • 2
    • 0001269332 scopus 로고
    • Interactions of epithelial cells with foreign surfaces
    • D. M. Brunette, "Interactions of epithelial cells with foreign surfaces," CRC Crit. Rev. Biocompat., 1, 323-370 (1986).
    • (1986) CRC Crit. Rev. Biocompat. , vol.1 , pp. 323-370
    • Brunette, D.M.1
  • 3
    • 0023026232 scopus 로고
    • Surface science aspects on inorganic biomaterials
    • B. Kasemo and J. Lausmaa, "Surface science aspects on inorganic biomaterials," CRC Crit. Rev. Biocompat., 2, 335-380 (1986).
    • (1986) CRC Crit. Rev. Biocompat. , vol.2 , pp. 335-380
    • Kasemo, B.1    Lausmaa, J.2
  • 4
    • 0019866783 scopus 로고
    • Possible function of mesenchyme cell-derived fibronectin during formation of basal lamina
    • A. G. Brownell, C. C. Bessern, and H. C. Slavkin, "Possible function of mesenchyme cell-derived fibronectin during formation of basal lamina," Proc. Natl Acad. Sci. USA, 78, 3711-3715 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 3711-3715
    • Brownell, A.G.1    Bessern, C.C.2    Slavkin, H.C.3
  • 5
    • 0018139596 scopus 로고
    • Inhibition of limb chondrogenesis in vitro by vitamin A: Alteration in cell surface characteristics
    • C.A. Lewis, R. M. Pratt, J. P. Pennypacker, and J. R. Hassell, "Inhibition of limb chondrogenesis in vitro by vitamin A: Alteration in cell surface characteristics," Dev. Biol., 64, 31-47 (1978).
    • (1978) Dev. Biol. , vol.64 , pp. 31-47
    • Lewis, C.A.1    Pratt, R.M.2    Pennypacker, J.P.3    Hassell, J.R.4
  • 6
    • 0018178127 scopus 로고
    • Synthesis and extracellular deposition of fibronectin in chondrocyte cultures
    • W. Dessau, J. Sasse, R. Timpl, F. Jilek, and K. von der Mark, "Synthesis and extracellular deposition of fibronectin in chondrocyte cultures," J. Cell Biol., 79, 342-355 (1978).
    • (1978) J. Cell Biol. , vol.79 , pp. 342-355
    • Dessau, W.1    Sasse, J.2    Timpl, R.3    Jilek, F.4    Von Der Mark, K.5
  • 7
    • 0018286392 scopus 로고
    • Enhanced cellular fibronectin accumulation in chondrocytes treated with vitamin A
    • R. M. Pratt and K. M. Yamada, "Enhanced cellular fibronectin accumulation in chondrocytes treated with vitamin A," Cell, 17, 821-826 (1979).
    • (1979) Cell , vol.17 , pp. 821-826
    • Pratt, R.M.1    Yamada, K.M.2
  • 8
    • 0023367927 scopus 로고
    • Fibronectin: A brief overview of its structure, function, and physiology
    • R. A. Proctor, "Fibronectin: A brief overview of its structure, function, and physiology," Rev. Infect. Dis., 9, S317-S321 (1987).
    • (1987) Rev. Infect. Dis. , vol.9
    • Proctor, R.A.1
  • 9
    • 0020478961 scopus 로고
    • Fibronectin adsorption on hydrophilic and Hydrophobic surfaces detected by antibody binding and analyzed during cell adhesion in serum containing solution
    • F. Grinnell and M. K. Feld, "Fibronectin adsorption on hydrophilic and Hydrophobic surfaces detected by antibody binding and analyzed during cell adhesion in serum containing solution," J. Biol. Chem., 257, 4888-4893 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 4888-4893
    • Grinnell, F.1    Feld, M.K.2
  • 10
    • 0021054031 scopus 로고
    • Fibronectin mediated binding and phagocytosis of polystyrene latex beads by baby hamster kidney cells
    • D. D. McAbee and F. Grinnell, "Fibronectin mediated binding and phagocytosis of polystyrene latex beads by baby hamster kidney cells," J. Cell Biol., 97, 1515-1523 (1983).
    • (1983) J. Cell Biol. , vol.97 , pp. 1515-1523
    • McAbee, D.D.1    Grinnell, F.2
  • 11
    • 0024581438 scopus 로고
    • Fluorescence energy transfer detects changes in fibronectin structure upon surface binding
    • C. E. Wolff and C.-S. Lai, "Fluorescence energy transfer detects changes in fibronectin structure upon surface binding," Arch. Biochem. Biophys., 268, 536-545 (1989).
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 536-545
    • Wolff, C.E.1    Lai, C.-S.2
  • 12
    • 0025319175 scopus 로고
    • Inter-sulphydryl distances in plasma fibronectin determined by fluorescence energy transfer: Effect of environmental factors
    • C. E. Wolff and C.-S. Lai, "Inter-sulphydryl distances in plasma fibronectin determined by fluorescence energy transfer: Effect of environmental factors," Biochemistry, 29, 3354-3361 (1990).
    • (1990) Biochemistry , vol.29 , pp. 3354-3361
    • Wolff, C.E.1    Lai, C.-S.2
  • 13
    • 0027928433 scopus 로고
    • The conformation of fibronectin on self-assembled monolayers with different surface composition: An FTIR/ATR study
    • S.-S. Cheng, K. K. Chittur, C. N. Sukenik, L A. Culp, and K. Lewandowska, "The conformation of fibronectin on self-assembled monolayers with different surface composition: an FTIR/ATR study," J. Colloid Interface Sci., 162, 135-143 (1994).
    • (1994) J. Colloid Interface Sci. , vol.162 , pp. 135-143
    • Cheng, S.-S.1    Chittur, K.K.2    Sukenik, C.N.3    Culp, L.A.4    Lewandowska, K.5
  • 14
    • 0017557557 scopus 로고
    • A total internal-reflection technique for the examination of protein adsorption
    • R. W. Watkin and C. R. Robertson, "A total internal-reflection technique for the examination of protein adsorption," J. Biomed. Mater. Res., 11, 915-938 (1977).
    • (1977) J. Biomed. Mater. Res. , vol.11 , pp. 915-938
    • Watkin, R.W.1    Robertson, C.R.2
  • 15
    • 1242312866 scopus 로고
    • Scanning tunneling microscopy for studying the biomaterial-biological tissue interface
    • R. Emch, X. Clivaz, C. Taylor-Denes, P. Vaudaux, P. Descouts, "Scanning tunneling microscopy for studying the biomaterial-biological tissue interface," J. Vac. Sci. Technol., A8, 655-658 (1990).
    • (1990) J. Vac. Sci. Technol. , vol.A8 , pp. 655-658
    • Emch, R.1    Clivaz, X.2    Taylor-Denes, C.3    Vaudaux, P.4    Descouts, P.5
  • 16
    • 0026898352 scopus 로고
    • Morphological difference between fibronectin sprayed on mica and on PMMA
    • R. Emch, F. Zenhausern, M. Jobin, M. Taborelli, and P. Descouts, "Morphological difference between fibronectin sprayed on mica and on PMMA," Ultramicroscopy, 42-44, 1155-1160 (1992).
    • (1992) Ultramicroscopy , vol.42-44 , pp. 1155-1160
    • Emch, R.1    Zenhausern, F.2    Jobin, M.3    Taborelli, M.4    Descouts, P.5
  • 18
    • 0028831314 scopus 로고
    • Determination of heatshock transcription factor 2 stoichiometry at looped DNA complexes using scanning force microscopy
    • C. Wyman, E. Grotkopp, C. Bustamante, H. C. M. Nelson, "Determination of heatshock transcription factor 2 stoichiometry at looped DNA complexes using scanning force microscopy," EMBO J., 14, 117-123 (1995).
    • (1995) EMBO J. , vol.14 , pp. 117-123
    • Wyman, C.1    Grotkopp, E.2    Bustamante, C.3    Nelson, H.C.M.4
  • 19
    • 0001876846 scopus 로고
    • Fibronectins
    • A. Rich (ed.), Springer-Verlag, New York
    • R. O. Hynes, Fibronectins, Springer Series in Molecular Biology, A. Rich (ed.), Springer-Verlag, New York, 1990, pp. 200-364.
    • (1990) Springer Series in Molecular Biology , pp. 200-364
    • Hynes, R.O.1
  • 20
    • 0001041888 scopus 로고
    • Auger and X-ray photoelectron spectroscopic and electrochemical characterization of titanium thin film electrodes
    • N. R. Armstrong and R. K. Quinn, "Auger and X-ray photoelectron spectroscopic and electrochemical characterization of titanium thin film electrodes," Surf. Sci., 67, 451-468 (1977).
    • (1977) Surf. Sci. , vol.67 , pp. 451-468
    • Armstrong, N.R.1    Quinn, R.K.2
  • 21
    • 0001439181 scopus 로고
    • Oxidation kinetics of titanium films in model physiologic environments
    • K. E. Healy and P. Ducheyne, "Oxidation kinetics of titanium films in model physiologic environments," J. Colloid Interface Sci., 150, 404-417 (1992).
    • (1992) J. Colloid Interface Sci. , vol.150 , pp. 404-417
    • Healy, K.E.1    Ducheyne, P.2
  • 22
    • 0026747757 scopus 로고
    • Hydration and preferential molecular adsorption on titanium in vitro
    • K. E. Healy and P. Ducheyne, "Hydration and preferential molecular adsorption on titanium in vitro," Biomaterials, 13, 553-561 (1992).
    • (1992) Biomaterials , vol.13 , pp. 553-561
    • Healy, K.E.1    Ducheyne, P.2
  • 23
    • 7144260252 scopus 로고
    • X-ray photoelectron spectroscopy of amino acids, polypeptides and simple carbohydrates
    • M. Z. Atassi and E. Appella (eds.), Plenum Press, New York
    • K. E. Dombrowski, S. E. Wright, J. C. Birkbeck, and W. E. Moddeman, "X-ray photoelectron spectroscopy of amino acids, polypeptides and simple carbohydrates," in Methods in Protein Surface Analysis, M. Z. Atassi and E. Appella (eds.), Plenum Press, New York, 1995, pp. 251-260.
    • (1995) Methods in Protein Surface Analysis , pp. 251-260
    • Dombrowski, K.E.1    Wright, S.E.2    Birkbeck, J.C.3    Moddeman, W.E.4
  • 24
    • 0001449206 scopus 로고
    • Performance of XPS analysis of model biochemical compounds
    • P. A. Gerin, P. B. Dengis, and P. G. Rouxhet, "Performance of XPS analysis of model biochemical compounds," J. Chim. Phys., 92, 1043-1065 (1995).
    • (1995) J. Chim. Phys. , vol.92 , pp. 1043-1065
    • Gerin, P.A.1    Dengis, P.B.2    Rouxhet, P.G.3
  • 26
    • 49149147744 scopus 로고
    • An experimental study of some effects of solid surface roughness on wetting
    • J. F. Oliver, C. Huh, and S. G. Mason, "An experimental study of some effects of solid surface roughness on wetting," Coll. Surfaces, 1, 79-104 (1980).
    • (1980) Coll. Surfaces , vol.1 , pp. 79-104
    • Oliver, J.F.1    Huh, C.2    Mason, S.G.3
  • 27
    • 0016972923 scopus 로고
    • Mineralogical heterogeneity of ore particles and its effects on the interfacial characteristics
    • R. D. Kulkarni and P. Somasundaran, "Mineralogical heterogeneity of ore particles and its effects on the interfacial characteristics," Powder Tech., 14, 279-285 (1976).
    • (1976) Powder Tech. , vol.14 , pp. 279-285
    • Kulkarni, R.D.1    Somasundaran, P.2
  • 28
    • 0001190770 scopus 로고
    • Alterations in properties of samples during their preparation by grinding
    • I. J. Lin and P. Somasundaran, "Alterations in properties of samples during their preparation by grinding," Powder Tech., 6, 171-180 (1972).
    • (1972) Powder Tech. , vol.6 , pp. 171-180
    • Lin, I.J.1    Somasundaran, P.2
  • 29
    • 0028630401 scopus 로고
    • Surface energy characterization of unalloyed titanium implants
    • D. V. Kilpadi and J. E. Lemons, "Surface energy characterization of unalloyed titanium implants," J. Biomed. Mater. Res., 28, 1419-1425 (1994).
    • (1994) J. Biomed. Mater. Res. , vol.28 , pp. 1419-1425
    • Kilpadi, D.V.1    Lemons, J.E.2
  • 30
    • 0001439217 scopus 로고
    • Changes in contact angles as a function of time on some pre-oxidized biomaterials
    • Y. Oshida, R. Sachdeva, and S. Miyazaki, "Changes in contact angles as a function of time on some pre-oxidized biomaterials," J. Mater. Sci. Mater. Med., 3, 306-312 (1992).
    • (1992) J. Mater. Sci. Mater. Med. , vol.3 , pp. 306-312
    • Oshida, Y.1    Sachdeva, R.2    Miyazaki, S.3
  • 31
    • 0027670289 scopus 로고
    • Effects of shot-penning on surface contact angles of biomaterials
    • Y. Oshida, R. Sachdeva, S. Miyazaki, and J. Daly, "Effects of shot-penning on surface contact angles of biomaterials," J. Mater. Sci. Mater. Med., 4, 443-447 (1993).
    • (1993) J. Mater. Sci. Mater. Med. , vol.4 , pp. 443-447
    • Oshida, Y.1    Sachdeva, R.2    Miyazaki, S.3    Daly, J.4
  • 32
    • 0024145064 scopus 로고
    • Titanium and calcium phosphate ceramic dental implants, surface, coatings, and interfaces
    • P. Ducheyne, "Titanium and calcium phosphate ceramic dental implants, surface, coatings, and interfaces," Oral Implantol., 14, 325-340 (1988).
    • (1988) Oral Implantol. , vol.14 , pp. 325-340
    • Ducheyne, P.1
  • 33
    • 0025807957 scopus 로고
    • Effect of surface treatment on the dissolution of titanium-based implant materials
    • A. Wisbey, P. J. Gregson, L. M. Peter, and M. Tuke, "Effect of surface treatment on the dissolution of titanium-based implant materials," Biomaterials, 12, 470-473 (1991).
    • (1991) Biomaterials , vol.12 , pp. 470-473
    • Wisbey, A.1    Gregson, P.J.2    Peter, L.M.3    Tuke, M.4
  • 34
    • 0027432344 scopus 로고
    • Studies on the tissue adhesive capability to titanium by dynamic wettability test and cell attachment, in vitro
    • D. Kawahara, Y. Kimura, M. Nakamura, and H. Kawahara, "Studies on the tissue adhesive capability to titanium by dynamic wettability test and cell attachment, in vitro," Clin. Mater., 14, 229-233 (1993).
    • (1993) Clin. Mater. , vol.14 , pp. 229-233
    • Kawahara, D.1    Kimura, Y.2    Nakamura, M.3    Kawahara, H.4
  • 35
    • 0029244582 scopus 로고
    • Scanning force microscopy analysis of the surface of ion-irradiated diamond
    • C. M. Demanet, S. Shrivastava, and J. P. F. Sellschop, "Scanning force microscopy analysis of the surface of ion-irradiated diamond," Surf. Interface Anal., 23, 115-119 (1995).
    • (1995) Surf. Interface Anal. , vol.23 , pp. 115-119
    • Demanet, C.M.1    Shrivastava, S.2    Sellschop, J.P.F.3
  • 36
    • 0019128611 scopus 로고
    • Electron microscopy study of fibronectin structure
    • V. E. Koteliansky, M. V. Bejanian, and V. N. Smirnov, "Electron microscopy study of fibronectin structure," FEBS Lett., 120, 283-286 (1980).
    • (1980) FEBS Lett. , vol.120 , pp. 283-286
    • Koteliansky, V.E.1    Bejanian, M.V.2    Smirnov, V.N.3
  • 38
    • 0019888221 scopus 로고
    • Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix
    • J. Engle, E. Odermatt, A. Engel, J. A. Madri, H. Furthmayr, H. Rohde, and R. Timpl, "Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix," J. Mol. Biol., 150, 97-120 (1981).
    • (1981) J. Mol. Biol. , vol.150 , pp. 97-120
    • Engle, J.1    Odermatt, E.2    Engel, A.3    Madri, J.A.4    Furthmayr, H.5    Rohde, H.6    Timpl, R.7
  • 39
    • 0019846214 scopus 로고
    • Fibronectin molecule visualized in electron microscopy: A long, thin, flexible strand
    • H. P. Erickson, N. Carrell, and J. McDonagh, "Fibronectin molecule visualized in electron microscopy: A long, thin, flexible strand," J. Cell. Biol., 91, 673-678 (1981).
    • (1981) J. Cell. Biol. , vol.91 , pp. 673-678
    • Erickson, H.P.1    Carrell, N.2    McDonagh, J.3
  • 40
    • 0020426096 scopus 로고
    • Conformational states of fibronectin: Effects of pH, ionic strength, and collagen binding
    • E. G. Williams, P. A. Janmey, J. D. Ferry, and D. F. Mosher, "Conformational states of fibronectin: Effects of pH, ionic strength, and collagen binding," J. Biol. Chem., 257, 14973-14978 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 14973-14978
    • Williams, E.G.1    Janmey, P.A.2    Ferry, J.D.3    Mosher, D.F.4
  • 41
    • 0001793324 scopus 로고
    • Physical properties of fibronectin
    • D. F. Mosher (ed.), Academic Press, Inc., New York
    • E. Odematt and J. Engel, "Physical properties of fibronectin," in Fibronectin, Biology of Extracellular Matrix, D. F. Mosher (ed.), Academic Press, Inc., New York, 1989, pp. 25-45.
    • (1989) Fibronectin, Biology of Extracellular Matrix , pp. 25-45
    • Odematt, E.1    Engel, J.2
  • 42
    • 0024506517 scopus 로고
    • Solution structure of human plasma fibronectin as a function of NaCl concentration determined by small-angle neutron diffraction
    • B. Sjöberg, M. Eriksson, E. Österlund, S. Pap, and K. Österlund, "Solution structure of human plasma fibronectin as a function of NaCl concentration determined by small-angle neutron diffraction," Eur. J. Biophys., 17, 5-11 (1989).
    • (1989) Eur. J. Biophys. , vol.17 , pp. 5-11
    • Sjöberg, B.1    Eriksson, M.2    Österlund, E.3    Pap, S.4    Österlund, K.5
  • 43
    • 0025361554 scopus 로고
    • Human plasma fibronectin structure probed by steady-state fluorescence polarization: Evidence for a rigid oblate structure
    • M. J. Benecky, C. G. Kolvenbach, R. W. Wine, J. P. DiOrio, and M. W. Mosesson, "Human plasma fibronectin structure probed by steady-state fluorescence polarization: Evidence for a rigid oblate structure," Biochemistry, 29, 3082-3091 (1990).
    • (1990) Biochemistry , vol.29 , pp. 3082-3091
    • Benecky, M.J.1    Kolvenbach, C.G.2    Wine, R.W.3    DiOrio, J.P.4    Mosesson, M.W.5
  • 44
    • 0025125007 scopus 로고
    • Unfolding transitions of fibronectin and its domains, stabilization and structural alternation of the N-terminal domain by heparin
    • M. Y. Khan, M. S. Medow, and S. A. Newman, "Unfolding transitions of fibronectin and its domains, stabilization and structural alternation of the N-terminal domain by heparin," Biochem. J., 270, 33-38 (1990).
    • (1990) Biochem. J. , vol.270 , pp. 33-38
    • Khan, M.Y.1    Medow, M.S.2    Newman, S.A.3
  • 45
    • 0025851977 scopus 로고
    • Ionic-strength- and pH-dependent conformational states of human plasma fibronectin
    • M. J. Benecky, R. W. Wine, C. G. Kolvenbach, and M. W. Mosesson, "Ionic-strength- and pH-dependent conformational states of human plasma fibronectin," Biochemistry, 30, 4298-4306 (1991).
    • (1991) Biochemistry , vol.30 , pp. 4298-4306
    • Benecky, M.J.1    Wine, R.W.2    Kolvenbach, C.G.3    Mosesson, M.W.4
  • 46
    • 0023686910 scopus 로고
    • The secondary structure of human plasma fibronectin: Conformational changes induced by acidic pH and elevated temperatures; a circular dichroic study
    • E. Österlund, "The secondary structure of human plasma fibronectin: Conformational changes induced by acidic pH and elevated temperatures; a circular dichroic study," Biochim. Biophys. Acta, 955, 330-336 (1988).
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 330-336
    • Österlund, E.1
  • 48
    • 0021288562 scopus 로고
    • Electron spin resonance spin label studies of plasma fibronectin: Effect of temperature
    • C.-S. Lai and N. M. Tooney, "Electron spin resonance spin label studies of plasma fibronectin: Effect of temperature," Arch. Biochem. Biophys., 228, 465-473 (1984).
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 465-473
    • Lai, C.-S.1    Tooney, N.M.2
  • 49
    • 0018373799 scopus 로고
    • The structure and stability of human plasma cold-insoluble globulin
    • S. S. Alexander, Jr., G. Colonna, and H. Edelhoch, "The structure and stability of human plasma cold-insoluble globulin," J. Biol. Chem., 254, 1501-1505 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 1501-1505
    • Alexander Jr., S.S.1    Colonna, G.2    Edelhoch, H.3
  • 50
    • 0024581438 scopus 로고
    • Fluorescence energy transfer detects changes in fibronectin structure upon surface binding
    • C. Wolff and C.-S. Lai, "Fluorescence energy transfer detects changes in fibronectin structure upon surface binding," Arch. Biochem. Biophys., 268, 536-545 (1989).
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 536-545
    • Wolff, C.1    Lai, C.-S.2
  • 51
    • 0021058825 scopus 로고
    • Fibronectin in extended and compact conformations
    • H. P. Erickson and N. A. Carrell, "Fibronectin in extended and compact conformations," J. Biol. Chem., 258, 14539-14544 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 14539-14544
    • Erickson, H.P.1    Carrell, N.A.2
  • 53
    • 0023785818 scopus 로고
    • One free sulfhydryl group of plasma fibronectin becomes titratable upon binding of the protein to solid substrates
    • C. Narasimhan, C.-S. Lai, A. Haas, and J. McCarthy, "One free sulfhydryl group of plasma fibronectin becomes titratable upon binding of the protein to solid substrates," Biochemistry, 27, 4970-4973 (1988).
    • (1988) Biochemistry , vol.27 , pp. 4970-4973
    • Narasimhan, C.1    Lai, C.-S.2    Haas, A.3    McCarthy, J.4
  • 54
    • 0024413691 scopus 로고
    • Conformational changes of plasma fibronectin detected upon adsorption to solid substrates: A spin-labeled study
    • C. Narasimhan and C.-S. Lai, "Conformational changes of plasma fibronectin detected upon adsorption to solid substrates: A spin-labeled study," Biochemistry, 28, 5041-5046 (1989).
    • (1989) Biochemistry , vol.28 , pp. 5041-5046
    • Narasimhan, C.1    Lai, C.-S.2
  • 55
    • 0021293224 scopus 로고
    • Physiology of fibronectin
    • D. F. Mosher, "Physiology of fibronectin," Ann. Rev. Med., 35, 561-575 (1984).
    • (1984) Ann. Rev. Med. , vol.35 , pp. 561-575
    • Mosher, D.F.1
  • 56
    • 0006169843 scopus 로고
    • Fibronectin in surface-adsorbed state
    • T. A. Herbett and J. L. Brash (eds.), American Chemical Society, Washington DC
    • V. Vogel, "Fibronectin in surface-adsorbed state," in Proteins at Interfaces. II. Fundamentals and Applications, T. A. Herbett and J. L. Brash (eds.), American Chemical Society, Washington DC, 1995, pp. 505-518.
    • (1995) Proteins at Interfaces. II. Fundamentals and Applications , pp. 505-518
    • Vogel, V.1
  • 57
    • 0023178166 scopus 로고
    • Fibronectin cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast
    • J. A. McDonald, B. J. Quade, T. J. Broekelmann, R. LaChance, K. Foreman, E. Hasegawa, and S. Akiyama, "Fibronectin cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast," J. Biol. Chem., 262, 2957-2967 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3    LaChance, R.4    Foreman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 58
    • 0025772946 scopus 로고
    • Five type I modules of fibronectin form a functional unit that binds to fibroblasts and Staphylococcus aureus
    • J. Sottile, J. Schwarzbauer, J. Selegue, and D. F. Mosher, "Five type I modules of fibronectin form a functional unit that binds to fibroblasts and Staphylococcus aureus," J. Biol. Chem., 266, 12840-12843 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 12840-12843
    • Sottile, J.1    Schwarzbauer, J.2    Selegue, J.3    Mosher, D.F.4
  • 59
    • 0025896188 scopus 로고
    • Identification of fibronectin sequences required for assembly of a fibrillar matrix
    • J. E. Schwarzbauer, "Identification of fibronectin sequences required for assembly of a fibrillar matrix," J. Cell. Biol., 113, 1463-1473 (1991).
    • (1991) J. Cell. Biol. , vol.113 , pp. 1463-1473
    • Schwarzbauer, J.E.1
  • 60
    • 0026652898 scopus 로고
    • A fibronectin self-assembly site involved in fibronectin matrix assembly: Reconstruction in a synthetic peptide
    • A. Morla and E. Ruoslahti, "A fibronectin self-assembly site involved in fibronectin matrix assembly: Reconstruction in a synthetic peptide," J. Cell Biol., 118, 421-429 (1992).
    • (1992) J. Cell Biol. , vol.118 , pp. 421-429
    • Morla, A.1    Ruoslahti, E.2
  • 61
    • 0021111985 scopus 로고
    • In vitro formation of disulfide-bonded fibronectin multimers
    • D. F. Mosher and R. B. Johnson, "In vitro formation of disulfide-bonded fibronectin multimers," J. Biol. Chem., 258, 6595-6601 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 6595-6601
    • Mosher, D.F.1    Johnson, R.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.