메뉴 건너뛰기




Volumn , Issue , 2007, Pages 297-308

Matrix effects

Author keywords

[No Author keywords available]

Indexed keywords


EID: 65349184882     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012370615-7/50025-1     Document Type: Chapter
Times cited : (3)

References (94)
  • 1
    • 0026737633 scopus 로고
    • Prevention of protein adsorption and platelet adhesion on surfaces by PEO PPO PEO triblock copolymers
    • M. Amiji and K. Park (1992) Prevention of protein adsorption and platelet adhesion on surfaces by PEO PPO PEO triblock copolymers. Biomaterials 13 682-692
    • (1992) Biomaterials , vol.13 , pp. 682-692
    • Amiji, M.1    Park, K.2
  • 2
    • 0023468837 scopus 로고
    • Protein adsorption and materials biocompatibility: a tutorial review and suggested hypotheses
    • J.D. Andrade and V. Hlady (1986) Protein adsorption and materials biocompatibility: a tutorial review and suggested hypotheses. Adv. Polym. Sci. 79 1-63
    • (1986) Adv. Polym. Sci , vol.79 , pp. 1-63
    • Andrade, J.D.1    Hlady, V.2
  • 3
  • 5
    • 0036745861 scopus 로고    scopus 로고
    • Integrins in development: moving on, responding to, and sticking to the extracellular matrix
    • C. Bokel and N.H. Brown (2002) Integrins in development: moving on, responding to, and sticking to the extracellular matrix. Dev. Cell 3 311-321
    • (2002) Dev. Cell , vol.3 , pp. 311-321
    • Bokel, C.1    Brown, N.H.2
  • 6
    • 29044447052 scopus 로고    scopus 로고
    • Mechanisms of focal adhesion kinase regulation
    • L.A. Cohen and J.L. Guan (2005) Mechanisms of focal adhesion kinase regulation. Curr. Cancer Drug Targets 5 629-643
    • (2005) Curr. Cancer Drug Targets , vol.5 , pp. 629-643
    • Cohen, L.A.1    Guan, J.L.2
  • 7
    • 0031796751 scopus 로고    scopus 로고
    • Integrin signaling: cytoskeletal complexes, map kinase activation, and regulation of gene expression
    • E.H.J. Danen, R.M. Lafrenie, S. Miyamoto and K.M. Yamada (1998) Integrin signaling: cytoskeletal complexes, map kinase activation, and regulation of gene expression. Cell Adh. Commun. 6 217-224
    • (1998) Cell Adh. Commun , vol.6 , pp. 217-224
    • Danen, E.H.J.1    Lafrenie, R.M.2    Miyamoto, S.3    Yamada, K.M.4
  • 8
    • 0024477452 scopus 로고
    • (ARG-GLY-ASP)N-albumin conjugates as a model substratum for integrin-mediated cell adhesion
    • Y.N. Danilov and R.L. Juliano (1989) (ARG-GLY-ASP)N-albumin conjugates as a model substratum for integrin-mediated cell adhesion. Exp. Cell Res. 182 186-196
    • (1989) Exp. Cell Res , vol.182 , pp. 186-196
    • Danilov, Y.N.1    Juliano, R.L.2
  • 9
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • D.E. Discher, P. Janmey and Y.-L. Wang (2005) Tissue cells feel and respond to the stiffness of their substrate. Science 310 1139-1143
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.-L.3
  • 10
    • 0028116664 scopus 로고
    • Polymer networks with grafted cell-adhesion peptides for highly biospecific cell adhesive substrates
    • P.D. Drumheller and J.A. Hubbell (1994) Polymer networks with grafted cell-adhesion peptides for highly biospecific cell adhesive substrates. Anal. Biochem. 222 380-388
    • (1994) Anal. Biochem , vol.222 , pp. 380-388
    • Drumheller, P.D.1    Hubbell, J.A.2
  • 11
    • 0028765062 scopus 로고
    • Multifunctional poly(ethylene glycol) semiinterpenetrating polymer networks as highly selective adhesive substrates for bioadhesive peptide grafting
    • P.D. Drumheller, D.L. Elbert and J.A. Hubbell (1994) Multifunctional poly(ethylene glycol) semiinterpenetrating polymer networks as highly selective adhesive substrates for bioadhesive peptide grafting. Biotechnol. Bioeng. 43 772-780
    • (1994) Biotechnol. Bioeng , vol.43 , pp. 772-780
    • Drumheller, P.D.1    Elbert, D.L.2    Hubbell, J.A.3
  • 13
    • 0032033222 scopus 로고    scopus 로고
    • Self-assembly and steric stabilization at heterogeneous, biological surfaces using adsorbing block copolymers
    • D.L. Elbert and J.A. Hubbell (1998) Self-assembly and steric stabilization at heterogeneous, biological surfaces using adsorbing block copolymers. Chem. Biol. 5 177-183
    • (1998) Chem. Biol , vol.5 , pp. 177-183
    • Elbert, D.L.1    Hubbell, J.A.2
  • 14
    • 0031733974 scopus 로고    scopus 로고
    • Diversity does make a difference: fibroblast growth factor-heparin interactions
    • S. Faham, R.J. Linhardt and D.C. Rees (1998) Diversity does make a difference: fibroblast growth factor-heparin interactions. Curr. Opin. Str. Biol. 8 578-586
    • (1998) Curr. Opin. Str. Biol , vol.8 , pp. 578-586
    • Faham, S.1    Linhardt, R.J.2    Rees, D.C.3
  • 15
  • 16
    • 33745762953 scopus 로고    scopus 로고
    • Autologous morphogen gradients by subtle interstitial flow and matrix interactions
    • M.E. Fleury, K.C. Boardman and M.A. Swartz (2006) Autologous morphogen gradients by subtle interstitial flow and matrix interactions. Biophys. J. 91 113-121
    • (2006) Biophys. J , vol.91 , pp. 113-121
    • Fleury, M.E.1    Boardman, K.C.2    Swartz, M.A.3
  • 18
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • S.M. Frisch, K. Vuori, E. Ruoslahti and P.Y. ChanHui (1996) Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol. 134 793-799
    • (1996) J. Cell Biol , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    ChanHui, P.Y.4
  • 20
    • 33644529130 scopus 로고    scopus 로고
    • Capturing complex 3D tissue physiology in vitro
    • L.G. Griffith and M.A. Swartz (2006) Capturing complex 3D tissue physiology in vitro. Nat. Rev. Mol. Cell Biol. 7 211-224
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 211-224
    • Griffith, L.G.1    Swartz, M.A.2
  • 21
    • 0038738331 scopus 로고    scopus 로고
    • Fibroblast biology in three-dimensional collagen matrices
    • F. Grinnell (2003) Fibroblast biology in three-dimensional collagen matrices. Trends Cell Biol. 13 264-269
    • (2003) Trends Cell Biol , vol.13 , pp. 264-269
    • Grinnell, F.1
  • 22
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • B.M. Gumbiner (2005) Regulation of cadherin-mediated adhesion in morphogenesis. Nat. Rev. Mol. Cell Biol. 6 622-634
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 23
    • 14244262503 scopus 로고    scopus 로고
    • Matnix-bound sixth Ig-like domain of cell adhesion molecule l1 acts as an angiogenic factor by ligating alpha-V-beta-3-integrin and activating vegf-r2
    • H. Hall and J.A. Hubbell (2004) Matnix-bound sixth Ig-like domain of cell adhesion molecule l1 acts as an angiogenic factor by ligating alpha-V-beta-3-integrin and activating vegf-r2. Microvasc. Res. 68 169-178
    • (2004) Microvasc. Res , vol.68 , pp. 169-178
    • Hall, H.1    Hubbell, J.A.2
  • 24
    • 0028765038 scopus 로고
    • Spatial distribution of mammalian cells dictated by material surface chemistry
    • K.E. Healy, B. Lom and P.E. Hockberger (1994) Spatial distribution of mammalian cells dictated by material surface chemistry. Biotechnol. Bioeng. 43 792-800
    • (1994) Biotechnol. Bioeng , vol.43 , pp. 792-800
    • Healy, K.E.1    Lom, B.2    Hockberger, P.E.3
  • 25
    • 27644453468 scopus 로고    scopus 로고
    • Synergy between interstitial flow and vegf directs capillary morphogenesis in vitro through a gradient amplification mechanism
    • C.L.E. Helm, M.E. Fleury, A.H. Zisch, F. Boschetti and M.A. Swartz (2005) Synergy between interstitial flow and vegf directs capillary morphogenesis in vitro through a gradient amplification mechanism. Proc. Nat. Acad. Sci. USA 102 15779-15784
    • (2005) Proc. Nat. Acad. Sci. USA , vol.102 , pp. 15779-15784
    • Helm, C.L.E.1    Fleury, M.E.2    Zisch, A.H.3    Boschetti, F.4    Swartz, M.A.5
  • 26
    • 12644260439 scopus 로고    scopus 로고
    • Micropatterning gradients and controlling surface densities of photoactivatable biomolecules on self-assembled monolayers of oligo(ethylene glycol) alkanethio
    • C.B. Herbert, T.L. McLernon, C.L. Hypolite, D.N. Adams, L. Pikus, C.C. Huang, G.B. Fields, P.C. Letourneau, M.D. Distefano and W.S. Hu (1997) Micropatterning gradients and controlling surface densities of photoactivatable biomolecules on self-assembled monolayers of oligo(ethylene glycol) alkanethio. Chem. Biol. 4 731-737
    • (1997) Chem. Biol , vol.4 , pp. 731-737
    • Herbert, C.B.1    McLernon, T.L.2    Hypolite, C.L.3    Adams, D.N.4    Pikus, L.5    Huang, C.C.6    Fields, G.B.7    Letourneau, P.C.8    Distefano, M.D.9    Hu, W.S.10
  • 27
    • 0035135778 scopus 로고    scopus 로고
    • Poly(l-lysine)-Gpoly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption
    • N.P. Huang, R. Michel, J. Voros, M. Textor, R. Hofer, A. Rossi, D.L. Elbert, J.A. Hubbell and N.D. Spencer (2001) Poly(l-lysine)-Gpoly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption. Langmuir 17 489-498
    • (2001) Langmuir , vol.17 , pp. 489-498
    • Huang, N.P.1    Michel, R.2    Voros, J.3    Textor, M.4    Hofer, R.5    Rossi, A.6    Elbert, D.L.7    Hubbell, J.A.8    Spencer, N.D.9
  • 28
    • 0029007273 scopus 로고
    • Biomaterials in tissue engineering
    • J.A. Hubbell (1995) Biomaterials in tissue engineering. Biotechnology 13 565-576
    • (1995) Biotechnology , vol.13 , pp. 565-576
    • Hubbell, J.A.1
  • 29
    • 0026448194 scopus 로고
    • The neural cell-adhesion molecule (nCAM) heparin-binding domain binds to cell-surface heparansulfate proteoglycans
    • S.G. Kallapur and R.A. Akeson (1992) The neural cell-adhesion molecule (nCAM) heparin-binding domain binds to cell-surface heparansulfate proteoglycans. J. Neurosci. Res. 33 538-548
    • (1992) J. Neurosci. Res , vol.33 , pp. 538-548
    • Kallapur, S.G.1    Akeson, R.A.2
  • 30
    • 0030699118 scopus 로고    scopus 로고
    • Integrins in morphogenesis and signaling
    • B.Z. Katz and K.M. Yamada (1997) Integrins in morphogenesis and signaling. Biochimie 79 467-476
    • (1997) Biochimie , vol.79 , pp. 467-476
    • Katz, B.Z.1    Yamada, K.M.2
  • 31
    • 18044399825 scopus 로고    scopus 로고
    • Poly(llysine)-G-poly(ethylene glycol) layers on metal oxide surfaces: attachmnet mechanism and effects of polymer architecture on resistance to protein adsorp
    • G.L. Kenausis, J. Voros, D.L. Elbert, N.P. Huang, R. Hofer, L. Ruiz-Taylor, M. Textor, J.A. Hubbell and N.D. Spencer (2000) Poly(llysine)-G-poly(ethylene glycol) layers on metal oxide surfaces: attachmnet mechanism and effects of polymer architecture on resistance to protein adsorp. J. Phys. Chem. B 104 3298-3309
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3298-3309
    • Kenausis, G.L.1    Voros, J.2    Elbert, D.L.3    Huang, N.P.4    Hofer, R.5    Ruiz-Taylor, L.6    Textor, M.7    Hubbell, J.A.8    Spencer, N.D.9
  • 32
    • 0024259975 scopus 로고
    • Controlled outgrowth of dissociated neurons on patterned substrates
    • D. Kleinfeld, K.H. Kahler and P.E. Hockberger (1988) Controlled outgrowth of dissociated neurons on patterned substrates. J. Neurosci. 8 4098-4120
    • (1988) J. Neurosci , vol.8 , pp. 4098-4120
    • Kleinfeld, D.1    Kahler, K.H.2    Hockberger, P.E.3
  • 34
    • 0023870741 scopus 로고
    • Adhesion of glycosaminoglycan-deficient Chinese hamster ovary cell mutants to fibronectin substrata
    • R.G. Lebaron, J.D. Esko, A. Woods, S. Johansson and M. Hook (1988) Adhesion of glycosaminoglycan-deficient Chinese hamster ovary cell mutants to fibronectin substrata. J. Cell Biol. 106 945-952
    • (1988) J. Cell Biol , vol.106 , pp. 945-952
    • Lebaron, R.G.1    Esko, J.D.2    Woods, A.3    Johansson, S.4    Hook, M.5
  • 35
    • 33748195976 scopus 로고    scopus 로고
    • Mechanism and dynamics of cadherin adhesion
    • Epub ahead of print
    • D. Leckband and A. Prakasam (2006) Mechanism and dynamics of cadherin adhesion. Annu. Rev. Biomed. Eng. Epub ahead of print
    • (2006) Annu. Rev. Biomed. Eng
    • Leckband, D.1    Prakasam, A.2
  • 36
    • 18044398972 scopus 로고    scopus 로고
    • Self-assembled monolayers of thiolates on metals as a form of nanotechnology
    • J.C. Love, L.A. Estroff, J.K. Kriebel, R.G. Nuzzo and G.M. Whitesides (2005) Self-assembled monolayers of thiolates on metals as a form of nanotechnology. Chem. Rev. 105 1103-1169
    • (2005) Chem. Rev , vol.105 , pp. 1103-1169
    • Love, J.C.1    Estroff, L.A.2    Kriebel, J.K.3    Nuzzo, R.G.4    Whitesides, G.M.5
  • 37
    • 19644367664 scopus 로고    scopus 로고
    • Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering
    • M.P. Lutolf and J.A. Hubbell (2005) Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering. Nature Biotechnol. 23 47-55
    • (2005) Nature Biotechnol , vol.23 , pp. 47-55
    • Lutolf, M.P.1    Hubbell, J.A.2
  • 39
    • 0031650702 scopus 로고    scopus 로고
    • Bio-specific sequences and domains in heparan sulphate and the regulation of cell growth and adhesion
    • M. Lyon and J.T. Gallagher (1998) Bio-specific sequences and domains in heparan sulphate and the regulation of cell growth and adhesion. Matrix Biol. 17 485-493
    • (1998) Matrix Biol , vol.17 , pp. 485-493
    • Lyon, M.1    Gallagher, J.T.2
  • 40
    • 0031713365 scopus 로고    scopus 로고
    • Fibronectin — structure, assembly, and cardiovascular implications
    • M.K. Magnusson and D.F. Mosher (1998) Fibronectin — structure, assembly, and cardiovascular implications. Arterioscl. Thromb. Vasc. Biol. 18 1363-1370
    • (1998) Arterioscl. Thromb. Vasc. Biol , vol.18 , pp. 1363-1370
    • Magnusson, M.K.1    Mosher, D.F.2
  • 41
    • 0033064811 scopus 로고    scopus 로고
    • Biophysical integration of effects of epidermal growth factor and fibronectin on fibroblast migration
    • G. Maheshwari, A. Wells, L.G. Griffith and D.A. Lauffenburger (1999) Biophysical integration of effects of epidermal growth factor and fibronectin on fibroblast migration. Biophys. J. 76 2814-2823
    • (1999) Biophys. J , vol.76 , pp. 2814-2823
    • Maheshwari, G.1    Wells, A.2    Griffith, L.G.3    Lauffenburger, D.A.4
  • 42
    • 27644473227 scopus 로고    scopus 로고
    • Stimulatory effects of a threedimensional microenvironment on cell-mediated fibronectin fibrillogenesis
    • Y. Mao and J.E. Schwarzbauer (2005) Stimulatory effects of a threedimensional microenvironment on cell-mediated fibronectin fibrillogenesis. J. Cell Sci. 118 4427-4436
    • (2005) J. Cell Sci , vol.118 , pp. 4427-4436
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 43
    • 0025300277 scopus 로고
    • Covalent surface immobilization of ARG-GLY-ASP-containing and TYR-ILE-GLY-SER-ARG-containing peptides to obtain well-defined cell-adhesive substrates
    • S.P. Massia and J.A. Hubbell (1990) Covalent surface immobilization of ARG-GLY-ASP-containing and TYR-ILE-GLY-SER-ARG-containing peptides to obtain well-defined cell-adhesive substrates. Anal. Biochem. 187 292-301
    • (1990) Anal. Biochem , vol.187 , pp. 292-301
    • Massia, S.P.1    Hubbell, J.A.2
  • 44
    • 0025881229 scopus 로고
    • An RGD spacing of 440 nm is sufficient for integrin alpha-V-beta-3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation
    • S.P. Massia and J.A. Hubbell (1991) An RGD spacing of 440 nm is sufficient for integrin alpha-V-beta-3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation. J. Cell Biol. 114 1089-1100
    • (1991) J. Cell Biol , vol.114 , pp. 1089-1100
    • Massia, S.P.1    Hubbell, J.A.2
  • 45
    • 0026774645 scopus 로고
    • Immobilized amines and basic amino acids as mimetic heparin-binding domains for cell-surface proteoglycanmediated adhesion
    • S.P. Massia and J.A. Hubbell (1992) Immobilized amines and basic amino acids as mimetic heparin-binding domains for cell-surface proteoglycanmediated adhesion. J. Biol. Chem. 267 10133-10141
    • (1992) J. Biol. Chem , vol.267 , pp. 10133-10141
    • Massia, S.P.1    Hubbell, J.A.2
  • 46
    • 0030271217 scopus 로고    scopus 로고
    • Control of cell adhesion, migration, and orientation on photochemically microprocessed surfaces
    • T. Matsuda and T. Sugawara (1996) Control of cell adhesion, migration, and orientation on photochemically microprocessed surfaces. J. Biomed. Mater. Res. 32 165-173
    • (1996) J. Biomed. Mater. Res , vol.32 , pp. 165-173
    • Matsuda, T.1    Sugawara, T.2
  • 48
    • 4644271368 scopus 로고    scopus 로고
    • Peptide arrays: towards routine implementation
    • D.H. Min and M. Mrksich (2004) Peptide arrays: towards routine implementation. Curr. Opin. Chem. Biol. 8 554-558
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 554-558
    • Min, D.H.1    Mrksich, M.2
  • 50
    • 0027593935 scopus 로고
    • Molecular design of 3-dimensional artificial extracellular matrix —photosensitive polymers containing cell adhesive peptide
    • M.J. Moghaddam and T. Matsuda (1993) Molecular design of 3-dimensional artificial extracellular matrix —photosensitive polymers containing cell adhesive peptide. J. Polym. Sci. A Polym. Chem. 31 1589-1597
    • (1993) J. Polym. Sci. A Polym. Chem , vol.31 , pp. 1589-1597
    • Moghaddam, M.J.1    Matsuda, T.2
  • 51
    • 0036898944 scopus 로고    scopus 로고
    • What can surface chemistry do for cell biology?
    • M. Mrksich (2002) What can surface chemistry do for cell biology? Curr. Opin. Chem. Biol. 6 794-797
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 794-797
    • Mrksich, M.1
  • 52
    • 0032527082 scopus 로고    scopus 로고
    • A novel method for surface modification to promote cell attachment to hydrophobic substrates
    • J.A. Neff, K.D. Caldwell and P.A. Tresco (1998) A novel method for surface modification to promote cell attachment to hydrophobic substrates. J. Biomed. Mater. Res. 40 511-519
    • (1998) J. Biomed. Mater. Res , vol.40 , pp. 511-519
    • Neff, J.A.1    Caldwell, K.D.2    Tresco, P.A.3
  • 53
    • 0032721971 scopus 로고    scopus 로고
    • Surface modification for controlled studies of cell-ligand interactions
    • J.A. Neff, P.A. Tresco and K.D. Caldwell (1999) Surface modification for controlled studies of cell-ligand interactions. Biomaterials 20 2377-2393
    • (1999) Biomaterials , vol.20 , pp. 2377-2393
    • Neff, J.A.1    Tresco, P.A.2    Caldwell, K.D.3
  • 54
    • 33646412022 scopus 로고    scopus 로고
    • Mechanisms of interstitial flowinduced remodeling of fibroblast-collagen cultures
    • C.P. Ng and M.A. Swartz (2006) Mechanisms of interstitial flowinduced remodeling of fibroblast-collagen cultures. Ann. Biomed. Eng. 34 446-454
    • (2006) Ann. Biomed. Eng , vol.34 , pp. 446-454
    • Ng, C.P.1    Swartz, M.A.2
  • 55
    • 0031257740 scopus 로고    scopus 로고
    • Integrin signaling: building connections beyond the focal contact?
    • T.E. Otoole (1997) Integrin signaling: building connections beyond the focal contact? Matrix Biol. 16 165-171
    • (1997) Matrix Biol , vol.16 , pp. 165-171
    • Otoole, T.E.1
  • 56
    • 0037462992 scopus 로고    scopus 로고
    • Pegylated nanoparticles for biological and pharmaceutical applications
    • H. Otsuka, Y. Nagasaki and K. Kataoka (2003) Pegylated nanoparticles for biological and pharmaceutical applications. Adv. Drug Deliv. Rev. 55 403-419
    • (2003) Adv. Drug Deliv. Rev , vol.55 , pp. 403-419
    • Otsuka, H.1    Nagasaki, Y.2    Kataoka, K.3
  • 57
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand-binding properties govern cell migration speed through cell-substratum adhesiveness
    • S.P. Palecek, J.C. Loftus, M.H. Ginsberg, D.A. Lauffenburger and A.F. Horwitz (1997) Integrin-ligand-binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385 537-540
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 59
    • 29144531874 scopus 로고    scopus 로고
    • Mechanobiology in the third dimension
    • J.A. Pedersen and M.A. Swartz (2005) Mechanobiology in the third dimension. Ann. Biomed. Eng. 33 1469-1490
    • (2005) Ann. Biomed. Eng , vol.33 , pp. 1469-1490
    • Pedersen, J.A.1    Swartz, M.A.2
  • 61
    • 0031746579 scopus 로고    scopus 로고
    • Role of vitronectin and its receptors in haemostasis and vascular remodeling
    • K.T. Preissner and D. Seiffert (1998) Role of vitronectin and its receptors in haemostasis and vascular remodeling. Thromb. Res. 89 1-21
    • (1998) Thromb. Res , vol.89 , pp. 1-21
    • Preissner, K.T.1    Seiffert, D.2
  • 62
    • 12044254336 scopus 로고
    • Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide) —a model system using self-assembled monolayers
    • K.L. Prime and G.M. Whitesides (1993) Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide) —a model system using self-assembled monolayers. J. Am. Chem. Soc. 115 10714-10721
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 10714-10721
    • Prime, K.L.1    Whitesides, G.M.2
  • 63
    • 23244447869 scopus 로고    scopus 로고
    • Molecularly engineered PEG hydrogels: a novel model system for proteolytically mediated cell migration
    • G.P. Raeber, M.P. Lutolf and J.A. Hubbell (2005) Molecularly engineered PEG hydrogels: a novel model system for proteolytically mediated cell migration. Biophys. J. 89 1374-1388
    • (2005) Biophys. J , vol.89 , pp. 1374-1388
    • Raeber, G.P.1    Lutolf, M.P.2    Hubbell, J.A.3
  • 64
    • 0027625983 scopus 로고
    • Selective neuronal cell attachment to a covalently patterned monoamine on fluorinated ethylene-propylene films
    • J.P. Ranieri, R. Bellamkonda, J. Jacob, T.G. Vargo, J.A. Gardella and P. Aebischer (1993) Selective neuronal cell attachment to a covalently patterned monoamine on fluorinated ethylene-propylene films. J. Biomed. Mater. Res. 27 917-925
    • (1993) J. Biomed. Mater. Res , vol.27 , pp. 917-925
    • Ranieri, J.P.1    Bellamkonda, R.2    Jacob, J.3    Vargo, T.G.4    Gardella, J.A.5    Aebischer, P.6
  • 66
    • 0033054299 scopus 로고    scopus 로고
    • Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of the matrix deposited by osteoblast-like cells
    • A. Rezania and K.E. Healy (1999) Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of the matrix deposited by osteoblast-like cells. Biotechnol. Prog. 15 19-32
    • (1999) Biotechnol. Prog , vol.15 , pp. 19-32
    • Rezania, A.1    Healy, K.E.2
  • 67
    • 0029119564 scopus 로고
    • A hierarchy of ECM-mediated signaling regulates tissue-specific gene expression
    • C.D. Roskelley, A. Srebrow and M.J. Bissell (1995) A hierarchy of ECM-mediated signaling regulates tissue-specific gene expression. Curr. Opin. Cell Biol. 7 736-747
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 736-747
    • Roskelley, C.D.1    Srebrow, A.2    Bissell, M.J.3
  • 70
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • E. Ruoslahti and M. Pierschbacher (1987) New perspectives in cell adhesion: RGD and integrins. Science 238 491-497
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.2
  • 71
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von willebrand factor
    • J.E. Sadler (1998) Biochemistry and genetics of von willebrand factor. Annu. Rev. Biochem. 67 395-424
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 72
    • 0033997601 scopus 로고    scopus 로고
    • Development of fibrin derivatives for controlled release of heparin-binding growth factors
    • S.E. Sakiyama-Elbert and J.A. Hubbell (2000) Development of fibrin derivatives for controlled release of heparin-binding growth factors. J. Control. Rel. 65 389-402
    • (2000) J. Control. Rel , vol.65 , pp. 389-402
    • Sakiyama-Elbert, S.E.1    Hubbell, J.A.2
  • 73
    • 1842509188 scopus 로고    scopus 로고
    • Laminin: the crux of basement membrane assembly
    • T. Sasaki, R. Fassler and E. Hohenester (2004) Laminin: the crux of basement membrane assembly. J. Cell Biol. 164 959-963
    • (2004) J. Cell Biol , vol.164 , pp. 959-963
    • Sasaki, T.1    Fassler, R.2    Hohenester, E.3
  • 74
    • 0032940534 scopus 로고    scopus 로고
    • Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa
    • J.C. Schense and J.A. Hubbell (1999) Cross-linking exogenous bifunctional peptides into fibrin gels with factor XIIIa. Bioconj. Chem. 10 75-81
    • (1999) Bioconj. Chem , vol.10 , pp. 75-81
    • Schense, J.C.1    Hubbell, J.A.2
  • 75
    • 0034049521 scopus 로고    scopus 로고
    • Enzymatic incorporation of bioactive peptides into fibrin matrices enhances neurite extension
    • J.C. Schense, J. Bloch, P. Aebischer and J.A. Hubbell (2000) Enzymatic incorporation of bioactive peptides into fibrin matrices enhances neurite extension. Nature Biotechnol. 18 415-419
    • (2000) Nature Biotechnol , vol.18 , pp. 415-419
    • Schense, J.C.1    Bloch, J.2    Aebischer, P.3    Hubbell, J.A.4
  • 76
    • 0033535485 scopus 로고    scopus 로고
    • Basement membranes: putting up the barriers
    • J.L. Schwarzbauer (1999) Basement membranes: putting up the barriers. Curr. Biol. 9 R242-R244
    • (1999) Curr. Biol , vol.9 , pp. R242-R244
    • Schwarzbauer, J.L.1
  • 77
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: biological consequences
    • S.D. Shapiro (1998) Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr. Opin. Cell Biol. 10 602-608
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 81
    • 0026493748 scopus 로고
    • Coplanar molecular assemblies of aminoalkylsilane and perfluorinated alkylsilane —characterization and geometric definition of mammalian-cell adhesion and
    • D.A. Stenger, J.H. Georger, C.S. Dulcey, J.J. Hickman, A.S. Rudolph, T.B. Nielsen, S.M. McCort and J.M. Calvert (1992) Coplanar molecular assemblies of aminoalkylsilane and perfluorinated alkylsilane —characterization and geometric definition of mammalian-cell adhesion and. J. Am. Chem. Soc. 114 8435-8442
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 8435-8442
    • Stenger, D.A.1    Georger, J.H.2    Dulcey, C.S.3    Hickman, J.J.4    Rudolph, A.S.5    Nielsen, T.B.6    McCort, S.M.7    Calvert, J.M.8
  • 82
    • 0030270607 scopus 로고    scopus 로고
    • Synthesis of phenylazidoderivatized substances and photochemical surface modification to immobilize functional groups
    • T. Sugawara and T. Matsuda (1996) Synthesis of phenylazidoderivatized substances and photochemical surface modification to immobilize functional groups. J. Biomed. Mater. Res. 32 157-164
    • (1996) J. Biomed. Mater. Res , vol.32 , pp. 157-164
    • Sugawara, T.1    Matsuda, T.2
  • 83
    • 0024443667 scopus 로고
    • A synthetic peptide containing the ikvav sequence from the A-chain of laminin mediates cell attachment, migration, and neurite outgrowth
    • K. Tashiro, G.C. Sephel, B. Weeks, M. Sasaki, G.R. Martin, H.K. Kleinman and Y. Yamada (1989) A synthetic peptide containing the ikvav sequence from the A-chain of laminin mediates cell attachment, migration, and neurite outgrowth. J. Biol. Chem. 264 16174-16182
    • (1989) J. Biol. Chem , vol.264 , pp. 16174-16182
    • Tashiro, K.1    Sephel, G.C.2    Weeks, B.3    Sasaki, M.4    Martin, G.R.5    Kleinman, H.K.6    Yamada, Y.7
  • 85
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • A. van der Flier and A. Sonnenberg (2001) Function and interactions of integrins. Cell Tissue Res. 305 285-298
    • (2001) Cell Tissue Res , vol.305 , pp. 285-298
    • van der Flier, A.1    Sonnenberg, A.2
  • 86
    • 0037572325 scopus 로고    scopus 로고
    • RGD-grafted poly-l-lysine-graft-(polyethylene glycol) copolymers block nonspecific protein adsorption while promoting cell adhesion
    • S. VandeVondele, J. Voros and J.A. Hubbell (2003) RGD-grafted poly-l-lysine-graft-(polyethylene glycol) copolymers block nonspecific protein adsorption while promoting cell adhesion. Biotechnol. Bioeng. 82 784-790
    • (2003) Biotechnol. Bioeng , vol.82 , pp. 784-790
    • VandeVondele, S.1    Voros, J.2    Hubbell, J.A.3
  • 87
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their lignads
    • D. Vestweber and J.E. Blanks (1999) Mechanisms that regulate the function of the selectins and their lignads. Physiol. Rev. 79 181-213
    • (1999) Physiol. Rev , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.E.2
  • 88
    • 0031439129 scopus 로고    scopus 로고
    • Neural cell adhesion molecules of the immunoglobulin superfamily: role in axon growth and guidance
    • F.S. Walsh and P. Doherty (1997) Neural cell adhesion molecules of the immunoglobulin superfamily: role in axon growth and guidance. Annu. Rev. Cell Dev. Biol. 13 1997
    • (1997) Annu. Rev. Cell Dev. Biol , vol.13 , pp. 1997
    • Walsh, F.S.1    Doherty, P.2
  • 89
    • 0027195840 scopus 로고
    • A theoretical analysis for the effect of focal contact formation on cell-substrate attachment strength
    • M.D. Ward and D.A. Hammer (1993) A theoretical analysis for the effect of focal contact formation on cell-substrate attachment strength. Biophys. J. 64 936-959
    • (1993) Biophys. J , vol.64 , pp. 936-959
    • Ward, M.D.1    Hammer, D.A.2
  • 90
    • 0033084115 scopus 로고    scopus 로고
    • Microcontact printing for precise control of nerve cell growth in culture
    • B.C. Wheeler, J.M. Corey, G.J. Brewer and D.W. Branch (1999) Microcontact printing for precise control of nerve cell growth in culture. J. Biomech. Eng. 121 73-78
    • (1999) J. Biomech. Eng , vol.121 , pp. 73-78
    • Wheeler, B.C.1    Corey, J.M.2    Brewer, G.J.3    Branch, D.W.4
  • 91
    • 33644684958 scopus 로고    scopus 로고
    • Molecular engineering of surfaces using self-assembled monolayers
    • G.M. Whitesides, J.K. Kriebel and J.C. Love (2005) Molecular engineering of surfaces using self-assembled monolayers. Sci. Prog. 88 17-48
    • (2005) Sci. Prog , vol.88 , pp. 17-48
    • Whitesides, G.M.1    Kriebel, J.K.2    Love, J.C.3
  • 93
    • 0031258760 scopus 로고    scopus 로고
    • Integrin signaling
    • K.M. Yamada (1997) Integrin signaling. Matrix Biol. 16 137-141
    • (1997) Matrix Biol , vol.16 , pp. 137-141
    • Yamada, K.M.1
  • 94
    • 0026468460 scopus 로고
    • Functional domains of cell adhesion molecules
    • Y. Yamada and H.K. Kleinman (1992) Functional domains of cell adhesion molecules. Curr. Opin. Cell Biol. 4 819-823
    • (1992) Curr. Opin. Cell Biol , vol.4 , pp. 819-823
    • Yamada, Y.1    Kleinman, H.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.