메뉴 건너뛰기




Volumn 1, Issue , 2007, Pages 107-130

Biocompatibility of Microsystems

Author keywords

Biocompatibility; Cell adhesion; Chemisorption; Foreign body reactions; Host response; Hydrogelc; Peptide amphiphiles; Polymer brush; Protein adsorption; RGD; Self assembled monolayers (SAM); Self assembly; Surface modification; Surfaces

Indexed keywords


EID: 84865763739     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-044452190-3.00001-X     Document Type: Chapter
Times cited : (5)

References (124)
  • 2
    • 0025205276 scopus 로고
    • Integrins and other cell-adhesion molecules
    • Albelda S.M., Buck C.A. Integrins and other cell-adhesion molecules. FASEB J. 1990, 4:2868.
    • (1990) FASEB J. , vol.4 , pp. 2868
    • Albelda, S.M.1    Buck, C.A.2
  • 4
    • 0027350745 scopus 로고
    • Surface modification of polymeric biomaterials with poly(ethylene oxide), albumin, and heparin for reduced thrombogenicity
    • Amiji M., Park K. Surface modification of polymeric biomaterials with poly(ethylene oxide), albumin, and heparin for reduced thrombogenicity. J. Biomater. Sci. Polym. Ed. 1993, 4:217.
    • (1993) J. Biomater. Sci. Polym. Ed. , vol.4 , pp. 217
    • Amiji, M.1    Park, K.2
  • 5
    • 43949164802 scopus 로고
    • Cardiovascular device retrieval and evaluation
    • Anderson J.M. Cardiovascular device retrieval and evaluation. Cardiovasc. Pathol. 1993, 2:33-41.
    • (1993) Cardiovasc. Pathol. , vol.2 , pp. 33-41
    • Anderson, J.M.1
  • 6
    • 0028213869 scopus 로고
    • In-vivo biocompatibility of implantable delivery systems and biomaterials
    • Anderson J.M. In-vivo biocompatibility of implantable delivery systems and biomaterials. Eur. J. Pharm. Biopharm. 1994, 40:1.
    • (1994) Eur. J. Pharm. Biopharm. , vol.40 , pp. 1
    • Anderson, J.M.1
  • 7
    • 0035168305 scopus 로고    scopus 로고
    • Biological responses to materials
    • Anderson J.M. Biological responses to materials. Annu. Rev. Mater. Res. 2001, 31:81-110.
    • (2001) Annu. Rev. Mater. Res. , vol.31 , pp. 81-110
    • Anderson, J.M.1
  • 8
    • 0000228929 scopus 로고    scopus 로고
    • Inflammation, wound healing and the foreign-body response
    • Academic Press, San Diego, CA, B.D. Ratner (Ed.)
    • Anderson J.M., et al. Inflammation, wound healing and the foreign-body response. Biomaterials - An Introduction to Materials in Medicine 1996, 296. Academic Press, San Diego, CA. 2nd edn. B.D. Ratner (Ed.).
    • (1996) Biomaterials - An Introduction to Materials in Medicine , pp. 296
    • Anderson, J.M.1
  • 9
    • 0023468837 scopus 로고
    • Protein adsorption and materials biocompatibility - A tutorial review and suggested hypotheses
    • Andrade J.D., Hlady V. Protein adsorption and materials biocompatibility - A tutorial review and suggested hypotheses. Adv. Polym. Sci. 1986, 79:1.
    • (1986) Adv. Polym. Sci. , vol.79 , pp. 1
    • Andrade, J.D.1    Hlady, V.2
  • 11
    • 33845228791 scopus 로고    scopus 로고
    • Poly(ethylene oxide) and protein resistance - Principles, problems, and possibilities
    • Andrade J.D., Hlady V., Jeon S.I. Poly(ethylene oxide) and protein resistance - Principles, problems, and possibilities. Adv. Chem. Ser. 1996, 248:51.
    • (1996) Adv. Chem. Ser. , vol.248 , pp. 51
    • Andrade, J.D.1    Hlady, V.2    Jeon, S.I.3
  • 13
    • 6344262257 scopus 로고    scopus 로고
    • Differential modulation of human melanoma cell metalloproteinase expression by alpha(2)beta(1) integrin and CD44 triple-helical ligands derived from type IV collagen
    • Baronas-Lowell D., Lauer-Fields J.L., Borgia J.A., Sferrazza G.F., Al-Ghoul M., Minond D., Fields G.B. Differential modulation of human melanoma cell metalloproteinase expression by alpha(2)beta(1) integrin and CD44 triple-helical ligands derived from type IV collagen. J. Biol. Chem. 2004, 279:43503.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43503
    • Baronas-Lowell, D.1    Lauer-Fields, J.L.2    Borgia, J.A.3    Sferrazza, G.F.4    Al-Ghoul, M.5    Minond, D.6    Fields, G.B.7
  • 14
    • 0346463073 scopus 로고    scopus 로고
    • Induction of endothelial cell activation by a triple helical alpha(2)beta(1) integrin ligand, derived from type I collagen alpha 1(I)496-507
    • Baronas-Lowell D., Lauer-Fields J.L., Fields G.B. Induction of endothelial cell activation by a triple helical alpha(2)beta(1) integrin ligand, derived from type I collagen alpha 1(I)496-507. J. Biol. Chem. 2004, 279:952.
    • (2004) J. Biol. Chem. , vol.279 , pp. 952
    • Baronas-Lowell, D.1    Lauer-Fields, J.L.2    Fields, G.B.3
  • 16
    • 0017074308 scopus 로고
    • Asbestos-related diseases of lung and other organs - their epidemiology and implications for clinical practice
    • Becklake M.R. Asbestos-related diseases of lung and other organs - their epidemiology and implications for clinical practice. Am. Rev. Resp. Disease 1976, 114(1):187.
    • (1976) Am. Rev. Resp. Disease , vol.114 , Issue.1 , pp. 187
    • Becklake, M.R.1
  • 17
    • 0033134642 scopus 로고    scopus 로고
    • Versatile derivatisation of solid support media for covalent bonding on DNA-microchips
    • Beier M., Hoheisel J.D. Versatile derivatisation of solid support media for covalent bonding on DNA-microchips. Nucleic Acid Res. 1999, 27:1970.
    • (1999) Nucleic Acid Res. , vol.27 , pp. 1970
    • Beier, M.1    Hoheisel, J.D.2
  • 18
  • 19
    • 0029113344 scopus 로고
    • Synthetic lipidation of peptides and aminoacids - monolayer structure and properties
    • Berndt P., Fields G.B., Tirrell M. Synthetic lipidation of peptides and aminoacids - monolayer structure and properties. J. Am. Chem. Soc. 1995, 117:9515.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9515
    • Berndt, P.1    Fields, G.B.2    Tirrell, M.3
  • 20
    • 21644448118 scopus 로고    scopus 로고
    • Polymerized vesicles carrying molecular recognition sites
    • Biesalski M., Tu R., Tirrell M. Polymerized vesicles carrying molecular recognition sites. Langmuir 2005, 21:5663.
    • (2005) Langmuir , vol.21 , pp. 5663
    • Biesalski, M.1    Tu, R.2    Tirrell, M.3
  • 21
    • 28444443687 scopus 로고    scopus 로고
    • Cell adhesion on a polymerized peptide-amphiphile monolayer
    • Biesalski M., Knaebel A., Tu R., Tirrell M. Cell adhesion on a polymerized peptide-amphiphile monolayer. Biomaterials 2006, 27:1259.
    • (2006) Biomaterials , vol.27 , pp. 1259
    • Biesalski, M.1    Knaebel, A.2    Tu, R.3    Tirrell, M.4
  • 23
    • 0001670092 scopus 로고
    • The terminal grafting of poly(ethylene oxide) chains to silica surfaces
    • Bridger K., Vincent B. The terminal grafting of poly(ethylene oxide) chains to silica surfaces. Eur. Polym. J. 1980, 16:1017.
    • (1980) Eur. Polym. J. , vol.16 , pp. 1017
    • Bridger, K.1    Vincent, B.2
  • 24
    • 33845265640 scopus 로고    scopus 로고
    • The multiple-channel cochlear implant: The interface between sound and the central nervous system for hearing, speech, and language in deaf people - A personal perspective
    • [Review]
    • Clark G.M. The multiple-channel cochlear implant: The interface between sound and the central nervous system for hearing, speech, and language in deaf people - A personal perspective. Philos. Trans. R. Soc. Lond. B Biol. Sci. 2006, 361:791. [Review].
    • (2006) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.361 , pp. 791
    • Clark, G.M.1
  • 26
    • 21444433775 scopus 로고    scopus 로고
    • Ultrathin polymer monolayers for promotion of cell growth on bioprosthetic materials - Evolution of a new concept to improve long term performance of biologic heart valves
    • Dahm M., Ruhe J., Berchthold B., Prufer D., Prucker O., Chang B.J., Wallrath A., Oelert H. Ultrathin polymer monolayers for promotion of cell growth on bioprosthetic materials - Evolution of a new concept to improve long term performance of biologic heart valves. Biomed. Mater. Eng. 2004, 14:419.
    • (2004) Biomed. Mater. Eng. , vol.14 , pp. 419
    • Dahm, M.1    Ruhe, J.2    Berchthold, B.3    Prufer, D.4    Prucker, O.5    Chang, B.J.6    Wallrath, A.7    Oelert, H.8
  • 27
    • 0029048823 scopus 로고
    • Role of the heparin-binding domain of fibronectin in attachment and spreading of human bone-derived cells
    • Dalton B.A., McFarland C.D., Underwood P.A., Steele J.G. Role of the heparin-binding domain of fibronectin in attachment and spreading of human bone-derived cells. J. Cell Sci. 1995, 108:2083.
    • (1995) J. Cell Sci. , vol.108 , pp. 2083
    • Dalton, B.A.1    McFarland, C.D.2    Underwood, P.A.3    Steele, J.G.4
  • 28
    • 0000192090 scopus 로고
    • Thermal stability of self-assembled monolayers
    • Delamarche E., Michel B., Kang H. Thermal stability of self-assembled monolayers. Langmuir 1994, 10:4103.
    • (1994) Langmuir , vol.10 , pp. 4103
    • Delamarche, E.1    Michel, B.2    Kang, H.3
  • 29
  • 32
    • 0029724374 scopus 로고    scopus 로고
    • Surface treatments of polymers for biocompatibility
    • Elbert D.L., Hubbell J.A. Surface treatments of polymers for biocompatibility. Annu. Rev. Mater. Sci. 1996, 26:365.
    • (1996) Annu. Rev. Mater. Sci. , vol.26 , pp. 365
    • Elbert, D.L.1    Hubbell, J.A.2
  • 33
    • 32644467413 scopus 로고    scopus 로고
    • Surface engineering approaches to micropattern surfaces for cell-based assays
    • Falconet D., Csucs G., Grandin H.M., Textor M. Surface engineering approaches to micropattern surfaces for cell-based assays. Biomaterials 2006, 27:3044.
    • (2006) Biomaterials , vol.27 , pp. 3044
    • Falconet, D.1    Csucs, G.2    Grandin, H.M.3    Textor, M.4
  • 34
    • 0031603860 scopus 로고    scopus 로고
    • Proteinlike molecular architecture: Biomaterial applications for inducing cellular receptor binding and signal transduction
    • Fields G.B., Lauer J.L., Dori Y., Forns P., Yu Y.C., Tirrell M. Proteinlike molecular architecture: Biomaterial applications for inducing cellular receptor binding and signal transduction. Biopolymers 1998, 47:143.
    • (1998) Biopolymers , vol.47 , pp. 143
    • Fields, G.B.1    Lauer, J.L.2    Dori, Y.3    Forns, P.4    Yu, Y.C.5    Tirrell, M.6
  • 35
  • 37
    • 0026434555 scopus 로고
    • A neuron-silicon junction - a Retzius cell of the leech on an insulated-gate field-effect transistor
    • Fromherz P., Offenhäuser A., Vetter T., Weis J. A neuron-silicon junction - a Retzius cell of the leech on an insulated-gate field-effect transistor. Science 1991, 252(5010):1290.
    • (1991) Science , vol.252 , Issue.5010 , pp. 1290
    • Fromherz, P.1    Offenhäuser, A.2    Vetter, T.3    Weis, J.4
  • 38
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • Geiger B., Bershadsky A. Assembly and mechanosensory function of focal contacts. Curr. Opin. Cell Biol. 2001, 13:584.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 584
    • Geiger, B.1    Bershadsky, A.2
  • 39
    • 0033794569 scopus 로고    scopus 로고
    • Complexity and specificity of integrin signaling
    • Giancotti F.G. Complexity and specificity of integrin signaling. Nat. Cell Biol. 2000, 2:E13.
    • (2000) Nat. Cell Biol. , vol.2 , pp. E13
    • Giancotti, F.G.1
  • 40
    • 0033551899 scopus 로고    scopus 로고
    • Transduction - Integrin signaling
    • Giancotti F.G., Ruoslahti E. Transduction - Integrin signaling. Science 1999, 285:1028.
    • (1999) Science , vol.285 , pp. 1028
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 43
    • 0027263208 scopus 로고
    • Nickel sensitivity and the implantation of orthopedic prostheses
    • Gawkrodger D.J. Nickel sensitivity and the implantation of orthopedic prostheses. Contact Dermatitis 1993, 28:257.
    • (1993) Contact Dermatitis , vol.28 , pp. 257
    • Gawkrodger, D.J.1
  • 44
    • 0033881609 scopus 로고    scopus 로고
    • Polymeric biomaterials
    • Griffith L.G. Polymeric biomaterials. Acta Mater. 2000, 48:263.
    • (2000) Acta Mater. , vol.48 , pp. 263
    • Griffith, L.G.1
  • 45
    • 0003472957 scopus 로고
    • Plenum Press, New York, J.M. Harris (Ed.)
    • Poly(Ethylene Glycol) Chemistry 1992, Plenum Press, New York. J.M. Harris (Ed.).
    • (1992) Poly(Ethylene Glycol) Chemistry
  • 48
    • 0032773487 scopus 로고    scopus 로고
    • Designing biomaterials to direct biological responses
    • Healy K.E., Rezania A., Stile R.A. Designing biomaterials to direct biological responses. Ann. NY Acad. Sci. 1999, 875:24.
    • (1999) Ann. NY Acad. Sci. , vol.875 , pp. 24
    • Healy, K.E.1    Rezania, A.2    Stile, R.A.3
  • 49
    • 0031904307 scopus 로고    scopus 로고
    • Robotic three-dimensional positioning of a stimulation electrode in the brain
    • Hefti J.L., Epitaux M., Glauser D., Frankhauser H. Robotic three-dimensional positioning of a stimulation electrode in the brain. Comput. Aided Surg. 1998, 3:1.
    • (1998) Comput. Aided Surg. , vol.3 , pp. 1
    • Hefti, J.L.1    Epitaux, M.2    Glauser, D.3    Frankhauser, H.4
  • 50
    • 0032007690 scopus 로고    scopus 로고
    • Incorporation of adhesion peptides into nonadhesive hydrogels useful for tissue resurfacing
    • Hern D.L., Hubbell J.A. Incorporation of adhesion peptides into nonadhesive hydrogels useful for tissue resurfacing. J. Biomed. Mater. Res. 1998, 39:266.
    • (1998) J. Biomed. Mater. Res. , vol.39 , pp. 266
    • Hern, D.L.1    Hubbell, J.A.2
  • 51
    • 0041559949 scopus 로고    scopus 로고
    • RGD modified polymers: biomaterials for stimulated cell adhesion and beyond
    • Hersel U., Dahmen C., Kessler H. RGD modified polymers: biomaterials for stimulated cell adhesion and beyond. Biomaterials 2003, 24:4385.
    • (2003) Biomaterials , vol.24 , pp. 4385
    • Hersel, U.1    Dahmen, C.2    Kessler, H.3
  • 54
    • 0025602916 scopus 로고
    • The molecular basis and specificity of integrin ligand interactions
    • Humphries M.J. The molecular basis and specificity of integrin ligand interactions. J. Cell Sci. 1990, 97:585.
    • (1990) J. Cell Sci. , vol.97 , pp. 585
    • Humphries, M.J.1
  • 55
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: Bidirectional, allosteric signaling machines. Cell 2002, 110:673.
    • (2002) Cell , vol.110 , pp. 673
    • Hynes, R.O.1
  • 57
    • 0034899970 scopus 로고    scopus 로고
    • Nanoscale clustering of RGD peptides at surfaces using comb polymers. 2. Surface segregation of comb polymers in polylactide
    • Irvine D.J., Ruzette A.V.G., Mayes A.M., Griffith L.G. Nanoscale clustering of RGD peptides at surfaces using comb polymers. 2. Surface segregation of comb polymers in polylactide. Biomacromolecules 2001, 2:545.
    • (2001) Biomacromolecules , vol.2 , pp. 545
    • Irvine, D.J.1    Ruzette, A.V.G.2    Mayes, A.M.3    Griffith, L.G.4
  • 58
    • 0033080573 scopus 로고    scopus 로고
    • Effects of surface-coupled polyethylene oxide on human macrophage adhesion and foreign body giant cell formation in vitro
    • Jenney C.R., Anderson J.M. Effects of surface-coupled polyethylene oxide on human macrophage adhesion and foreign body giant cell formation in vitro. J. Biomed. Mater. Res. 1999, 44:206.
    • (1999) J. Biomed. Mater. Res. , vol.44 , pp. 206
    • Jenney, C.R.1    Anderson, J.M.2
  • 59
    • 0026122420 scopus 로고
    • Protein surface interactions in the presence of polyethylene oxide 1. Simplified theory
    • Jeon S.I., Lee J.H., Andrade J.D., De Gennes P.G. Protein surface interactions in the presence of polyethylene oxide 1. Simplified theory. J. Colloid Interface Sci. 1991, 142:149.
    • (1991) J. Colloid Interface Sci. , vol.142 , pp. 149
    • Jeon, S.I.1    Lee, J.H.2    Andrade, J.D.3    De Gennes, P.G.4
  • 61
    • 0000918399 scopus 로고    scopus 로고
    • On the adsorption process in polymer brushes: A Monte Carlo study
    • Kopf A., Baschnagel J., Wittmer J., Binder K. On the adsorption process in polymer brushes: A Monte Carlo study. Macromolecules 1996, 29:1433.
    • (1996) Macromolecules , vol.29 , pp. 1433
    • Kopf, A.1    Baschnagel, J.2    Wittmer, J.3    Binder, K.4
  • 62
    • 85070017580 scopus 로고
    • Polyreactions on pigment surfaces 7. Reactions of polymers with chlorosilane end groups on silicon dioxide surfaces
    • Krenkler K.P., Laible R., Hamann K. Polyreactions on pigment surfaces 7. Reactions of polymers with chlorosilane end groups on silicon dioxide surfaces. Angew. Makromol. Chem. 1953, 53:101.
    • (1953) Angew. Makromol. Chem. , vol.53 , pp. 101
    • Krenkler, K.P.1    Laible, R.2    Hamann, K.3
  • 63
    • 0001036325 scopus 로고
    • Patterned self-assembled monolayers and mesoscale phenomena
    • Kumar A., Abbott N.L., Kim E. Patterned self-assembled monolayers and mesoscale phenomena. Acc. Chem. Res. 1995, 28:219.
    • (1995) Acc. Chem. Res. , vol.28 , pp. 219
    • Kumar, A.1    Abbott, N.L.2    Kim, E.3
  • 64
    • 0032744402 scopus 로고    scopus 로고
    • Investigation into the mechanism of bacterial adhesion to hydrogel-coated surfaces
    • Kunz R., Anders C., Heinrich L., Gersonde K. Investigation into the mechanism of bacterial adhesion to hydrogel-coated surfaces. J. Mater. Sci. Mater. Med. 1999, 10:649.
    • (1999) J. Mater. Sci. Mater. Med. , vol.10 , pp. 649
    • Kunz, R.1    Anders, C.2    Heinrich, L.3    Gersonde, K.4
  • 65
    • 0019009034 scopus 로고
    • Formation of chemically bound polymer layers on oxide surfaces and their role in colloidal stability
    • Laible R., Hamann K. Formation of chemically bound polymer layers on oxide surfaces and their role in colloidal stability. Adv. Colloid Interface Sci. 1980, 13:65.
    • (1980) Adv. Colloid Interface Sci. , vol.13 , pp. 65
    • Laible, R.1    Hamann, K.2
  • 66
    • 0028787292 scopus 로고
    • Physiological and toxicological changes in the skin resulting from the action and interaction of metal ions
    • Lansdown A.B.G. Physiological and toxicological changes in the skin resulting from the action and interaction of metal ions. Crit. Rev. Toxicol. 1995, 25:397.
    • (1995) Crit. Rev. Toxicol. , vol.25 , pp. 397
    • Lansdown, A.B.G.1
  • 67
    • 2442553856 scopus 로고    scopus 로고
    • Microarrays of peptides elevated on the protein layer for efficient protein kinase assay
    • Lee S.J., Lee S.Y. Microarrays of peptides elevated on the protein layer for efficient protein kinase assay. Appl. Microbiol. Biotechnol. 2004, 64:289.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 289
    • Lee, S.J.1    Lee, S.Y.2
  • 68
    • 0033450061 scopus 로고    scopus 로고
    • Polyethyloxazoline monolayers for polymer supported biomembrane models
    • Lehmann T., Ruehe J. Polyethyloxazoline monolayers for polymer supported biomembrane models. Macromol. Symp. 1999, 142:1.
    • (1999) Macromol. Symp. , vol.142 , pp. 1
    • Lehmann, T.1    Ruehe, J.2
  • 69
    • 0027357578 scopus 로고
    • Does polyethylene oxide possess a low thrombogenicity
    • Llanos G.R., Sefton M.V. Does polyethylene oxide possess a low thrombogenicity. J. Biomater. Sci. Polym. Ed. 1993, 4:381.
    • (1993) J. Biomater. Sci. Polym. Ed. , vol.4 , pp. 381
    • Llanos, G.R.1    Sefton, M.V.2
  • 72
    • 0037841389 scopus 로고    scopus 로고
    • Convenient synthesis of glycosylated hydroxylysine derivatives for use in solid-phase peptide synthesis
    • Malkar N.B., Lauer-Fields J.L., Juska D., Fields G.B. Convenient synthesis of glycosylated hydroxylysine derivatives for use in solid-phase peptide synthesis. Biomacromolecules 2003, 4:518.
    • (2003) Biomacromolecules , vol.4 , pp. 518
    • Malkar, N.B.1    Lauer-Fields, J.L.2    Juska, D.3    Fields, G.B.4
  • 73
    • 2542523027 scopus 로고    scopus 로고
    • Biomimetic peptide-amphiphiles for functional biomaterials: The role of GRGDSP and PHSRN
    • Mardillovitch A., Kokkoli E. Biomimetic peptide-amphiphiles for functional biomaterials: The role of GRGDSP and PHSRN. Biomacromolecules 2004, 5:950.
    • (2004) Biomacromolecules , vol.5 , pp. 950
    • Mardillovitch, A.1    Kokkoli, E.2
  • 74
    • 33645509724 scopus 로고    scopus 로고
    • Design of a novel fibronectin-mimetic peptide-amphiphile for functionalized biomaterials
    • Mardillovitch A., Craig J.A., McCammon M.Q., Garg A., Kokkoli E. Design of a novel fibronectin-mimetic peptide-amphiphile for functionalized biomaterials. Langmuir 2006, 22:3259.
    • (2006) Langmuir , vol.22 , pp. 3259
    • Mardillovitch, A.1    Craig, J.A.2    McCammon, M.Q.3    Garg, A.4    Kokkoli, E.5
  • 76
    • 0025881229 scopus 로고
    • An RGD spacing of 440nm is sufficient for integrin α, β-3-mediated fibroblast spreading and 140nm for focal contact and stress fiber formation
    • Massia S.P., Hubbell J.A. An RGD spacing of 440nm is sufficient for integrin α, β-3-mediated fibroblast spreading and 140nm for focal contact and stress fiber formation. J. Cell Biol. 1991, 114:1089.
    • (1991) J. Cell Biol. , vol.114 , pp. 1089
    • Massia, S.P.1    Hubbell, J.A.2
  • 77
  • 78
    • 0025907474 scopus 로고
    • The CS5 petide is a 2nd site in the IIICS region of fibronectin recognized by the integrin α-4-β-1-inhibition of α-4-β-1 function by RGD peptide homologs
    • Mould A.P., Komoriya A., Yamada K.M., Humphries M.J. The CS5 petide is a 2nd site in the IIICS region of fibronectin recognized by the integrin α-4-β-1-inhibition of α-4-β-1 function by RGD peptide homologs. J. Biol. Chem. 1991, 266:3579.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3579
    • Mould, A.P.1    Komoriya, A.2    Yamada, K.M.3    Humphries, M.J.4
  • 79
    • 0030000062 scopus 로고    scopus 로고
    • Using self-assembled monolayers to understand the interactions of man-made surfaces with proteins and cells
    • Mrksich M., Whitesides G.M. Using self-assembled monolayers to understand the interactions of man-made surfaces with proteins and cells. Annu. Rev. Biophys. Biomol. Struct. 1996, 25:55.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 55
    • Mrksich, M.1    Whitesides, G.M.2
  • 81
    • 0033818254 scopus 로고    scopus 로고
    • The role of membrane lipids in regulation of integrin functions
    • Pande G. The role of membrane lipids in regulation of integrin functions. Curr. Opin. Cell Biol. 2000, 12:569.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 569
    • Pande, G.1
  • 83
    • 0034494961 scopus 로고    scopus 로고
    • Focal adhesions: structure and dynamics
    • Petit V., Thiery J.P. Focal adhesions: structure and dynamics. Biology of the Cell 2000, 92:477.
    • (2000) Biology of the Cell , vol.92 , pp. 477
    • Petit, V.1    Thiery, J.P.2
  • 84
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984, 309:30.
    • (1984) Nature , vol.309 , pp. 30
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 85
    • 0001511468 scopus 로고
    • Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
    • Pierschbacher M.D., Ruoslahti E. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc. Natl. Acad. Sci. USA 1984, 81:5985.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5985
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 88
    • 0347356734 scopus 로고    scopus 로고
    • Synthesis of polymer brushes using atom transfer radical polymerization
    • Pyun J., Kowalewski T., Matyjaszewski K. Synthesis of polymer brushes using atom transfer radical polymerization. Macromol. Rapid Commun. 2003, 24:1043.
    • (2003) Macromol. Rapid Commun. , vol.24 , pp. 1043
    • Pyun, J.1    Kowalewski, T.2    Matyjaszewski, K.3
  • 89
    • 0031963203 scopus 로고    scopus 로고
    • DNA chips: State-of-the-art
    • Ramsay G. DNA chips: State-of-the-art. Nat. Biotechnol. 1998, 16:40.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 40
    • Ramsay, G.1
  • 90
    • 4444330267 scopus 로고    scopus 로고
    • Biomaterials: Where we have been and where we are going
    • Ratner B.D., Bryant S.J. Biomaterials: Where we have been and where we are going. Annu. Rev. Biomed. Eng. 2004, 6:41-75.
    • (2004) Annu. Rev. Biomed. Eng. , vol.6 , pp. 41-75
    • Ratner, B.D.1    Bryant, S.J.2
  • 91
    • 0033054299 scopus 로고    scopus 로고
    • Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of the matrix deposited by osteoblast-like cells
    • Rezania A., Healy K.E. Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of the matrix deposited by osteoblast-like cells. Biotechnol. Prog. 1999, 15:19.
    • (1999) Biotechnol. Prog. , vol.15 , pp. 19
    • Rezania, A.1    Healy, K.E.2
  • 94
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 1996, 12:697.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697
    • Ruoslahti, E.1
  • 95
    • 0023637601 scopus 로고
    • New perspectives in cell-adhesion - RGD and integrins
    • Ruoslahti E., Pierschbacher M.D. New perspectives in cell-adhesion - RGD and integrins. Science 1987, 238:491.
    • (1987) Science , vol.238 , pp. 491
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 96
    • 0033611506 scopus 로고    scopus 로고
    • A controlled-release microchip
    • Santini J.T., Cima M.J., Langer R. A controlled-release microchip. Nature 1999, 397:335.
    • (1999) Nature , vol.397 , pp. 335
    • Santini, J.T.1    Cima, M.J.2    Langer, R.3
  • 97
    • 0033572873 scopus 로고    scopus 로고
    • Tissue heart valves: Current challenges and future research perspectives
    • Schoen F.J., Levy R.J. Tissue heart valves: Current challenges and future research perspectives. Biomed. J. Mater. Res. 1999, 47:439.
    • (1999) Biomed. J. Mater. Res. , vol.47 , pp. 439
    • Schoen, F.J.1    Levy, R.J.2
  • 99
  • 100
    • 3042628701 scopus 로고    scopus 로고
    • Self-assembled monolayers of dendritic polyglycerol derivatives on gold that resist the adsorption of proteins
    • Siegers C., Biesalski M., Haag R. Self-assembled monolayers of dendritic polyglycerol derivatives on gold that resist the adsorption of proteins. Chem. Eur. J. 2004, 10:2831.
    • (2004) Chem. Eur. J. , vol.10 , pp. 2831
    • Siegers, C.1    Biesalski, M.2    Haag, R.3
  • 101
    • 0032522286 scopus 로고    scopus 로고
    • Effect of surface wettability on the adsorption of proteins and detergents
    • Sigal G.B., Mrksich M., Whitesides G.M. Effect of surface wettability on the adsorption of proteins and detergents. J. Am. Chem. Soc. 1998, 120:3464-3473.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3464-3473
    • Sigal, G.B.1    Mrksich, M.2    Whitesides, G.M.3
  • 103
    • 0029962816 scopus 로고    scopus 로고
    • DNA chips: Analyzing sequence by hybridization to oligonucleotides on a large scale
    • Southern E.M. DNA chips: Analyzing sequence by hybridization to oligonucleotides on a large scale. Trends Genet. 1996, 12:110.
    • (1996) Trends Genet. , vol.12 , pp. 110
    • Southern, E.M.1
  • 104
    • 33646862381 scopus 로고    scopus 로고
    • Application of micro- and nano-electromechanical devices to drug delivery
    • Staples M., Daniel K., Cima M.G., Langer R. Application of micro- and nano-electromechanical devices to drug delivery. Pharm. Res. 2006, 23:847.
    • (2006) Pharm. Res. , vol.23 , pp. 847
    • Staples, M.1    Daniel, K.2    Cima, M.G.3    Langer, R.4
  • 105
    • 23044519690 scopus 로고    scopus 로고
    • Tethered polymer layers: phase transitions and reduction of protein adsorption
    • Szleifer I., Carignano M.A. Tethered polymer layers: phase transitions and reduction of protein adsorption. Macromol. Rapid Commun. 2000, 21:423.
    • (2000) Macromol. Rapid Commun. , vol.21 , pp. 423
    • Szleifer, I.1    Carignano, M.A.2
  • 106
    • 0037051027 scopus 로고    scopus 로고
    • The role of surface science in bioengineered materials
    • Tirrell M., Kokkoli E., Biesalski M. The role of surface science in bioengineered materials. Surf. Sci. 2002, 500:61.
    • (2002) Surf. Sci. , vol.500 , pp. 61
    • Tirrell, M.1    Kokkoli, E.2    Biesalski, M.3
  • 107
    • 1342283649 scopus 로고    scopus 로고
    • Swelling behavior of thin, surface-attached polymer networks
    • Toomey R., Freidank D., Rühe J. Swelling behavior of thin, surface-attached polymer networks. Macromolecules 2004, 37:882.
    • (2004) Macromolecules , vol.37 , pp. 882
    • Toomey, R.1    Freidank, D.2    Rühe, J.3
  • 108
    • 0027268112 scopus 로고
    • Frontiers in biotechnology - biotech gets a grip on cell-adhesion
    • Travis J. Frontiers in biotechnology - biotech gets a grip on cell-adhesion. Science 1993, 260:906.
    • (1993) Science , vol.260 , pp. 906
    • Travis, J.1
  • 109
    • 0024640392 scopus 로고
    • Grafting onto carbon-black by the reaction of reactive carbon-black having epoxide groups with several polymers
    • Tsubokawa N., Kuroda A., Sone Y. Grafting onto carbon-black by the reaction of reactive carbon-black having epoxide groups with several polymers. J. Polym. Sci. 1989, A27:1701.
    • (1989) J. Polym. Sci. , vol.A27 , pp. 1701
    • Tsubokawa, N.1    Kuroda, A.2    Sone, Y.3
  • 110
    • 0025406097 scopus 로고
    • Grafting onto carbon-black - reaction of functional groups on carbon-black with acyl chloride-capped polymers
    • Tsubokawa N., Hosoya M., Yanadori K., Sone Y. Grafting onto carbon-black - reaction of functional groups on carbon-black with acyl chloride-capped polymers. J. Macromol. Sci. Chem. 1990, A27:445.
    • (1990) J. Macromol. Sci. Chem. , vol.A27 , pp. 445
    • Tsubokawa, N.1    Hosoya, M.2    Yanadori, K.3    Sone, Y.4
  • 112
    • 0025008334 scopus 로고
    • Differentiation of canacular cell processes in bone-cells by basement-membrane matrix components - regulation by discrete domains of laminin
    • Vukicevic S., Luyten F.P., Kleinman H.K., Reddi A.H. Differentiation of canacular cell processes in bone-cells by basement-membrane matrix components - regulation by discrete domains of laminin. Cell 1990, 63:437.
    • (1990) Cell , vol.63 , pp. 437
    • Vukicevic, S.1    Luyten, F.P.2    Kleinman, H.K.3    Reddi, A.H.4
  • 113
    • 0005729736 scopus 로고
    • The electrochemical desorption of N-alkanthiol monolayers from polycrystalline Au and Ag electrodes
    • Widrig C.A., Chung C., Porter M.D. The electrochemical desorption of N-alkanthiol monolayers from polycrystalline Au and Ag electrodes. J. Electroanal. Chem. 1991, 310:335.
    • (1991) J. Electroanal. Chem. , vol.310 , pp. 335
    • Widrig, C.A.1    Chung, C.2    Porter, M.D.3
  • 114
    • 2142648866 scopus 로고    scopus 로고
    • Year-end perspectives: New technologies
    • Williams D. Year-end perspectives: New technologies. Med. Device Technol. 2003, 14:10.
    • (2003) Med. Device Technol. , vol.14 , pp. 10
    • Williams, D.1
  • 116
    • 0035371722 scopus 로고    scopus 로고
    • Biomaterials integrated with electronic elements: en route to bioelectronics
    • Willner I., Willner B. Biomaterials integrated with electronic elements: en route to bioelectronics. Trends Biotechnol. 2001, 19:222.
    • (2001) Trends Biotechnol. , vol.19 , pp. 222
    • Willner, I.1    Willner, B.2
  • 117
    • 0034063226 scopus 로고    scopus 로고
    • Adsorption of plasma proteins on polyethylene oxide-modified lipid bilayers studied by total internal reflection fluorescence
    • Xu Z., Marchant R.E. Adsorption of plasma proteins on polyethylene oxide-modified lipid bilayers studied by total internal reflection fluorescence. Biomaterials 2000, 21:1075.
    • (2000) Biomaterials , vol.21 , pp. 1075
    • Xu, Z.1    Marchant, R.E.2
  • 118
    • 0000184438 scopus 로고    scopus 로고
    • Studies of the electrochemical removal and efficient re-formation of a monolayer of hexadecanethiol self-assembled at an Au(111) single crystal in aqueous solutions
    • Yang D.F., Wilde C.P., Morin M. Studies of the electrochemical removal and efficient re-formation of a monolayer of hexadecanethiol self-assembled at an Au(111) single crystal in aqueous solutions. Langmuir 1997, 13:243.
    • (1997) Langmuir , vol.13 , pp. 243
    • Yang, D.F.1    Wilde, C.P.2    Morin, M.3
  • 119
    • 0033320821 scopus 로고    scopus 로고
    • Protein interactions with poly(ethylene glycol) self-assembled monolayers on glass substrates: Diffusion and adsorption
    • Yang Z.H., Galloway J.A., Yu H.U. Protein interactions with poly(ethylene glycol) self-assembled monolayers on glass substrates: Diffusion and adsorption. Langmuir 1999, 15:8405.
    • (1999) Langmuir , vol.15 , pp. 8405
    • Yang, Z.H.1    Galloway, J.A.2    Yu, H.U.3
  • 121
    • 0001176483 scopus 로고
    • Irreversible polymer adsorption from semidilute and moderately dense solutions
    • Zajac R., Chakrabarti A. Irreversible polymer adsorption from semidilute and moderately dense solutions. Phys. Rev. E 1995, 52:6536.
    • (1995) Phys. Rev. E , vol.52 , pp. 6536
    • Zajac, R.1    Chakrabarti, A.2
  • 122
    • 0034755942 scopus 로고    scopus 로고
    • Components of cell-matrix adhesions
    • Zamir E., Geiger B. Components of cell-matrix adhesions. J. Cell Sci. 2001, 114:3583.
    • (2001) J. Cell Sci. , vol.114 , pp. 3583
    • Zamir, E.1    Geiger, B.2
  • 123
    • 0034206768 scopus 로고    scopus 로고
    • Polymer brushes: surface-immobilized macromolecules
    • Zhao B., Brittain W.J. Polymer brushes: surface-immobilized macromolecules. Prog. Polym. Sci. 2000, 25:677.
    • (2000) Prog. Polym. Sci. , vol.25 , pp. 677
    • Zhao, B.1    Brittain, W.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.