메뉴 건너뛰기




Volumn 18, Issue 1, 2008, Pages 15-24

Biomimetic polymers to control cell adhesion

Author keywords

Biomimetic polymers; Cell adhesion; Integrins; Nanoparticles; RGD sequence; Surface modification

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; INTEGRIN; MACROGOL; NANOPARTICLE; POLYMER; POLYSACCHARIDE; PROTEOGLYCAN;

EID: 39449105631     PISSN: 17732247     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1773-2247(08)50002-5     Document Type: Review
Times cited : (9)

References (110)
  • 1
    • 0042562089 scopus 로고    scopus 로고
    • Biomimetic materials for tissue engineering
    • Shin H., Jo S., Mikos A.G. - Biomimetic materials for tissue engineering. - Biomaterials, 24, 4353-4364, 2003.
    • (2003) Biomaterials , vol.24 , pp. 4353-4364
    • Shin, H.1    Jo, S.2    Mikos, A.G.3
  • 2
    • 4444292034 scopus 로고    scopus 로고
    • Bottom-up design of biomimetic assemblies
    • Tu R.S., Tirrell M. - Bottom-up design of biomimetic assemblies. - Adv.Drug Delivery Rev., 56, 1537-1563, 2004.
    • (2004) Adv.Drug Delivery Rev , vol.56 , pp. 1537-1563
    • Tu, R.S.1    Tirrell, M.2
  • 4
    • 34247846240 scopus 로고    scopus 로고
    • Biocompatibility and osteogenesis of biomimetic nano-hydroxyapatite/polyamide composite scaffolds for bone tissue engineering
    • Wang H., Li Y., Zuo Y., Li J., Ma S., Cheng L. - Biocompatibility and osteogenesis of biomimetic nano-hydroxyapatite/polyamide composite scaffolds for bone tissue engineering. - Biomaterials, 28, 3338-3348, 2007.
    • (2007) Biomaterials , vol.28 , pp. 3338-3348
    • Wang, H.1    Li, Y.2    Zuo, Y.3    Li, J.4    Ma, S.5    Cheng, L.6
  • 7
    • 15244343346 scopus 로고    scopus 로고
    • In vitro study on bone formation and surface topography from the standpoint of biomechanics
    • Kawahara H., Soeda Y., Niwa K., Takahashi M., Kawahara D., Araki N. - In vitro study on bone formation and surface topography from the standpoint of biomechanics. - J.Mater.Sci. - Mater.Med., 15, 1297-1307, 2004.
    • (2004) J.Mater.Sci. - Mater.Med , vol.15 , pp. 1297-1307
    • Kawahara, H.1    Soeda, Y.2    Niwa, K.3    Takahashi, M.4    Kawahara, D.5    Araki, N.6
  • 8
    • 0037342910 scopus 로고    scopus 로고
    • Chemically patterned, metal oxide based surfaces produced by photolithographic techniques for studying protein- and cell-surface interactions I: Microfabrication and surface characterization
    • Winkelmann M., Gold J., Hauert R., Kasemo B., Spencer N.D., Brunette D.M., Textor M. - Chemically patterned, metal oxide based surfaces produced by photolithographic techniques for studying protein- and cell-surface interactions I: Microfabrication and surface characterization. - Biomaterials, 24, 1133-1145, 2003.
    • (2003) Biomaterials , vol.24 , pp. 1133-1145
    • Winkelmann, M.1    Gold, J.2    Hauert, R.3    Kasemo, B.4    Spencer, N.D.5    Brunette, D.M.6    Textor, M.7
  • 9
    • 0037404371 scopus 로고    scopus 로고
    • Engineering cell adhesive surfaces that direct integrin [alpha]5[beta]1 binding using a recombinant fragment of fibronectin
    • Cutler S.M., Garcia A.J. - Engineering cell adhesive surfaces that direct integrin [alpha]5[beta]1 binding using a recombinant fragment of fibronectin. - Biomaterials, 24, 1759-1770, 2003.
    • (2003) Biomaterials , vol.24 , pp. 1759-1770
    • Cutler, S.M.1    Garcia, A.J.2
  • 10
    • 34248216395 scopus 로고    scopus 로고
    • Controlling cell adhesion to surfaces via associating bioactive triblock proteins
    • Fischer S.E., Liu X., Mao H.Q., Harden J.L. - Controlling cell adhesion to surfaces via associating bioactive triblock proteins. - Biomaterials, 28, 3325-3337, 2007.
    • (2007) Biomaterials , vol.28 , pp. 3325-3337
    • Fischer, S.E.1    Liu, X.2    Mao, H.Q.3    Harden, J.L.4
  • 11
    • 33847607091 scopus 로고    scopus 로고
    • RGD-Functionalized polymer brushes as substrates for the integrin specific adhesion of human umbilical vein endothelial cells
    • Tugulu S., Silacci P., Stergiopulos N., Klok H.A. - RGD-Functionalized polymer brushes as substrates for the integrin specific adhesion of human umbilical vein endothelial cells. - Biomaterials, 28, 2536-2546, 2007.
    • (2007) Biomaterials , vol.28 , pp. 2536-2546
    • Tugulu, S.1    Silacci, P.2    Stergiopulos, N.3    Klok, H.A.4
  • 12
    • 0026737633 scopus 로고
    • Prevention of protein adsorption and platelet adhesion on surfaces by PEO/PPO/PEO triblock copolymers
    • Amiji M., Park K. - Prevention of protein adsorption and platelet adhesion on surfaces by PEO/PPO/PEO triblock copolymers. - Biomaterials, 13, 682-692, 1992.
    • (1992) Biomaterials , vol.13 , pp. 682-692
    • Amiji, M.1    Park, K.2
  • 13
    • 0032560218 scopus 로고    scopus 로고
    • Biomimetic engineering of non-adhesive glycocalyx-like surfaces using oligosaccharide surfactant polymers
    • Holland N.B., Qiu Y., Ruegsegger M., Marchant R.E. - Biomimetic engineering of non-adhesive glycocalyx-like surfaces using oligosaccharide surfactant polymers. - Nature, 392, 799-801, 1998.
    • (1998) Nature , vol.392 , pp. 799-801
    • Holland, N.B.1    Qiu, Y.2    Ruegsegger, M.3    Marchant, R.E.4
  • 14
    • 0033971979 scopus 로고    scopus 로고
    • Mucin coating on polymeric material surfaces to suppress bacterial adhesion
    • Shi L., Ardehali R., Caldwell K.D., Valint P. - Mucin coating on polymeric material surfaces to suppress bacterial adhesion. - Colloids Surf.B: Biointerfaces, 17, 229-239, 2000.
    • (2000) Colloids Surf.B: Biointerfaces , vol.17 , pp. 229-239
    • Shi, L.1    Ardehali, R.2    Caldwell, K.D.3    Valint, P.4
  • 15
    • 0034996764 scopus 로고    scopus 로고
    • Long-circulating and target-specific nanoparticles: Theory to practice
    • Moghimi S.M., Hunter A.C., Murray J.C. - Long-circulating and target-specific nanoparticles: theory to practice. - Pharmacol. Rev., 53, 283-318, 2001.
    • (2001) Pharmacol. Rev , vol.53 , pp. 283-318
    • Moghimi, S.M.1    Hunter, A.C.2    Murray, J.C.3
  • 17
    • 27944466697 scopus 로고    scopus 로고
    • Exploring and engineering the cell surface interface
    • Stevens M.M., George J.H. - Exploring and engineering the cell surface interface. - Science, 310, 1135-1138, 2005.
    • (2005) Science , vol.310 , pp. 1135-1138
    • Stevens, M.M.1    George, J.H.2
  • 18
    • 0030271572 scopus 로고    scopus 로고
    • Macromolecular organization of basement membranes
    • Timpl R. - Macromolecular organization of basement membranes. - Curr.Opin.Cell Biol., 8, 618-624, 1996.
    • (1996) Curr.Opin.Cell Biol , vol.8 , pp. 618-624
    • Timpl, R.1
  • 19
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation in extracellular matrix proteins
    • Hohenester E., Engel J. - Domain structure and organisation in extracellular matrix proteins. - Matrix Biol., 21, 115-128, 2002.
    • (2002) Matrix Biol , vol.21 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 20
    • 0033995774 scopus 로고    scopus 로고
    • Extracellular matrix cell adhesion peptides: Functional applications in orthopedic materials
    • LeBaron R.G., Athanasiou K.A. - Extracellular matrix cell adhesion peptides: functional applications in orthopedic materials. - Tissue Eng., 6, 85-103, 2000.
    • (2000) Tissue Eng , vol.6 , pp. 85-103
    • LeBaron, R.G.1    Athanasiou, K.A.2
  • 22
    • 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, 24, 4385-4415, 2003.
    • (2003) Biomaterials , vol.24 , pp. 4385-4415
    • Hersel, U.1    Dahmen, C.2    Kessler, H.3
  • 23
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • van der Flier A., Sonnenberg A. - Function and interactions of integrins. - Cell Tissue Res., 305, 285-298, 2001.
    • (2001) Cell Tissue Res , vol.305 , pp. 285-298
    • van der Flier, A.1    Sonnenberg, A.2
  • 24
    • 0035895505 scopus 로고    scopus 로고
    • Venter J.C, Adams M.D, Myers E.W, Li P.W, Mural R.J, Sutton G.G, Smith H.O, Yandell M, Evans C.A, Holt R.A, Gocayne J.D, Amanatides P, Ballew R.M, Huson D.H, Wortman J.R, Zhang Q, Kodira C.D, Zheng X.H, Chen L, Skupski M, Subramanian G, Thomas P.D, Zhang J, Gabor Miklos G.L, Nelson C, Broder S, Clark A.G, Nadeau J, McKusick V.A, Zinder N, Levine A.J, Roberts R.J, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Francesco V.D, Dunn P, Eilbeck K, Evangelista C, Gabrielian A.E, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman T.J, Higgins M.E, Ji R.R, Ke Z, Ketchum K.A, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov G.V, Milshina N, Moore H.M, Naik A.K, N
    • Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Francesco V.D., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z.Y., Wang A., Wang X., Wang J., Wei M.H., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S.C., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfei B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A.D., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoras W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M. - The sequence of the human genome. - Science, 291, 1304-1351, 2001.
  • 26
    • 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, 309, 30-33, 1984.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 27
    • 0001810875 scopus 로고    scopus 로고
    • Recognition sites of RGD-dependent integrins
    • J.A.Eble Ed
    • Pfaff M. - Recognition sites of RGD-dependent integrins. - In: Integrin-Ligand Interaction, J.A.Eble Ed., 1997, pp. 101-121.
    • (1997) Integrin-Ligand Interaction , pp. 101-121
    • Pfaff, M.1
  • 28
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion
    • Pierschbacher M.D., Ruoslahti E. - Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. - J.Biol.Chem., 262, 17294-17298, 1987.
    • (1987) J.Biol.Chem , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 29
    • 0029298915 scopus 로고
    • Synthesis and use of a new bromoacetyl-derivatized heterotrifunctional amino acid for conjugation of cyclic rgd-containing peptides derived from human bone sialoprotein
    • Ivanov B., Grzesik W., Robey F.A. - Synthesis and use of a new bromoacetyl-derivatized heterotrifunctional amino acid for conjugation of cyclic rgd-containing peptides derived from human bone sialoprotein. - Bioconjugate Chem., 6, 269-277, 1995.
    • (1995) Bioconjugate Chem , vol.6 , pp. 269-277
    • Ivanov, B.1    Grzesik, W.2    Robey, F.A.3
  • 30
    • 0029778085 scopus 로고    scopus 로고
    • Structural and functional aspects of rgd-containing cyclic pentapeptides as highly potent and selective integrin anb3 antagonists
    • Haubner R., Gratias R., Diefenbach B., Goodman S.L., Jonczyk A., Kessler H. - Structural and functional aspects of rgd-containing cyclic pentapeptides as highly potent and selective integrin anb3 antagonists. - J.Am.Chem.Soc., 118, 7461-7472, 1996.
    • (1996) J.Am.Chem.Soc , vol.118 , pp. 7461-7472
    • Haubner, R.1    Gratias, R.2    Diefenbach, B.3    Goodman, S.L.4    Jonczyk, A.5    Kessler, H.6
  • 31
    • 0030589095 scopus 로고    scopus 로고
    • Automated solid-phase synthesis of cyclic peptides bearing a side-chain tail designed for subsequent chemical grafting
    • Delforge D., Art M., Gillon B., Dieu M., Delaive E., Raes M., Remade J. - Automated solid-phase synthesis of cyclic peptides bearing a side-chain tail designed for subsequent chemical grafting. - Anal. Biochem., 242, 180-186, 1996.
    • (1996) Anal. Biochem , vol.242 , pp. 180-186
    • Delforge, D.1    Art, M.2    Gillon, B.3    Dieu, M.4    Delaive, E.5    Raes, M.6    Remade, J.7
  • 32
    • 0032493643 scopus 로고    scopus 로고
    • Isolation, cloning, and sequence analysis of the integrin subunit alpha 10, a beta 1-associated collagen binding integrin expressed on chondrocytes
    • Camper L., Hellman U., Lundgren-Akerlund E. - Isolation, cloning, and sequence analysis of the integrin subunit alpha 10, a beta 1-associated collagen binding integrin expressed on chondrocytes. - J.Biol.Chem., 273, 20383-20389, 1998.
    • (1998) J.Biol.Chem , vol.273 , pp. 20383-20389
    • Camper, L.1    Hellman, U.2    Lundgren-Akerlund, E.3
  • 33
    • 0033520330 scopus 로고    scopus 로고
    • cDNA cloning and chromosomal localization of human alpha 11 integrin.A collagen-binding, I domain-containing, beta 1-associated integrin alpha -chain present in muscle tissues
    • Velling T., Kusche-Gullberg M., Sejersen T., Gullberg D. - cDNA cloning and chromosomal localization of human alpha 11 integrin.A collagen-binding, I domain-containing, beta 1-associated integrin alpha -chain present in muscle tissues. - J.Biol.Chem., 274, 25735-25742, 1999.
    • (1999) J.Biol.Chem , vol.274 , pp. 25735-25742
    • Velling, T.1    Kusche-Gullberg, M.2    Sejersen, T.3    Gullberg, D.4
  • 34
    • 0034614620 scopus 로고    scopus 로고
    • The collagen-binding A-domains of integrins alpha 1 beta 1 and alpha 2beta 1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens
    • Knight C.G., Morton L.F., Peachey A.R., Tuckwell D.S., Farndale R.W., Barnes M.J. - The collagen-binding A-domains of integrins alpha 1 beta 1 and alpha 2beta 1 recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. - J.Biol.Chem., 275, 35-40, 2000.
    • (2000) J.Biol.Chem , vol.275 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 40
    • 0031023713 scopus 로고    scopus 로고
    • Microbial adherence to and invasion through proteoglycans
    • Rostand K.S., Esko J.D. - Microbial adherence to and invasion through proteoglycans. - Infect.Immun., 65, 1-8, 1997.
    • (1997) Infect.Immun , vol.65 , pp. 1-8
    • Rostand, K.S.1    Esko, J.D.2
  • 41
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Ruoslahti E., Yamaguchi Y. - Proteoglycans as modulators of growth factor activities. - Cell, 64, 867-869, 1991.
    • (1991) Cell , vol.64 , pp. 867-869
    • Ruoslahti, E.1    Yamaguchi, Y.2
  • 42
    • 0030660196 scopus 로고    scopus 로고
    • Syndecans: Multifunctional cell-surface co-receptors
    • Carey D.J. - Syndecans: multifunctional cell-surface co-receptors. - Biochem.J., 327, 1-16, 1997.
    • (1997) Biochem.J , vol.327 , pp. 1-16
    • Carey, D.J.1
  • 43
    • 0028213641 scopus 로고
    • Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component
    • Woods A., Couchman J.R. - Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component. - Mol.Biol.Cell, 5, 183-192, 1994.
    • (1994) Mol.Biol.Cell , vol.5 , pp. 183-192
    • Woods, A.1    Couchman, J.R.2
  • 44
    • 0032925217 scopus 로고    scopus 로고
    • Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13
    • Bloom L., Ingham K.C., Hynes R.O. - Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13. - Mol.Biol.Cell, 10, 1521-1536, 1999.
    • (1999) Mol.Biol.Cell , vol.10 , pp. 1521-1536
    • Bloom, L.1    Ingham, K.C.2    Hynes, R.O.3
  • 45
    • 0022707292 scopus 로고
    • Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments
    • Woods A., Couchman J.R., Johansson S., Hook M. - Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments. - EMBO J., 5, 665-670, 1986.
    • (1986) EMBO J , vol.5 , pp. 665-670
    • Woods, A.1    Couchman, J.R.2    Johansson, S.3    Hook, M.4
  • 46
    • 0031884247 scopus 로고    scopus 로고
    • Neisseria meningitidis producing the Opc adhesin binds epithelial cell proteoglycan receptors
    • de Vries F.P., Cole R., Dankert J., Frosch M., van Putten J.P.M. - Neisseria meningitidis producing the Opc adhesin binds epithelial cell proteoglycan receptors. - Mol.Microbiol., 27, 1203-1212, 1998.
    • (1998) Mol.Microbiol , vol.27 , pp. 1203-1212
    • de Vries, F.P.1    Cole, R.2    Dankert, J.3    Frosch, M.4    van Putten, J.P.M.5
  • 47
    • 0028256449 scopus 로고
    • Borrelia burgdorferi bind to epithelial cell proteoglycans
    • Isaacs R.D. - Borrelia burgdorferi bind to epithelial cell proteoglycans. - J.Clin.Invest., 93, 809-819, 1994.
    • (1994) J.Clin.Invest , vol.93 , pp. 809-819
    • Isaacs, R.D.1
  • 48
    • 0026716363 scopus 로고
    • Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates
    • Pancake S.J., Holt G.D., Mellouk S., Hoffman S.L. - Malaria sporozoites and circumsporozoite proteins bind specifically to sulfated glycoconjugates. - J.Cell Biol., 117, 1351-1357, 1992.
    • (1992) J.Cell Biol , vol.117 , pp. 1351-1357
    • Pancake, S.J.1    Holt, G.D.2    Mellouk, S.3    Hoffman, S.L.4
  • 49
    • 0026551062 scopus 로고
    • Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans
    • Shieh M.T., WuDunn D., Montgomery R.I., Esko J.D., Spear P.G. - Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. - J.Cell Biol., 116, 1273-1281, 1992.
    • (1992) J.Cell Biol , vol.116 , pp. 1273-1281
    • Shieh, M.T.1    WuDunn, D.2    Montgomery, R.I.3    Esko, J.D.4    Spear, P.G.5
  • 50
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 Tat requires cell surface heparan sulfate proteoglycans
    • Tyagi M., Rusnati M., Presta M., Giacca M. - Internalization of HIV-1 Tat requires cell surface heparan sulfate proteoglycans. - J.Biol.Chem., 276, 3254-3261, 2001.
    • (2001) J.Biol.Chem , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 51
    • 0030825186 scopus 로고    scopus 로고
    • Structural requirement of heparan sulfate for interaction with herpes simplex virus type 1 virions and isolated glycoprotein C
    • Feyzi E., Trybala E., Bergstrom T., Lindahl U., Spillmann D. - Structural requirement of heparan sulfate for interaction with herpes simplex virus type 1 virions and isolated glycoprotein C. - J.Biol.Chem., 272, 24850-24857, 1997.
    • (1997) J.Biol.Chem , vol.272 , pp. 24850-24857
    • Feyzi, E.1    Trybala, E.2    Bergstrom, T.3    Lindahl, U.4    Spillmann, D.5
  • 52
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty R.J., Krummenacher C., Cohen G.H., Eisenberg R.J., Spear P.G. - Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. - Science, 280, 1618-1620, 1998.
    • (1998) Science , vol.280 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 53
    • 0024584913 scopus 로고
    • Molecular modeling of protein- glycosaminoglycan interactions
    • Cardin A.D., Weintraub H.J. - Molecular modeling of protein- glycosaminoglycan interactions. - Arterioscler.Thromb.Vasc.Biol., 9, 21-32, 1989.
    • (1989) Arterioscler.Thromb.Vasc.Biol , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.2
  • 54
    • 0032702839 scopus 로고    scopus 로고
    • Protein-mediated macrophage adhesion and activation on biomaterials: A model for modulating cell behavior
    • Kao W.J., Hubbell J.A., Anderson J.M. - Protein-mediated macrophage adhesion and activation on biomaterials: a model for modulating cell behavior. - J.Mater.Sci.:Mater.Med., 10, 601-605, 1999.
    • (1999) J.Mater.Sci.:Mater.Med , vol.10 , pp. 601-605
    • Kao, W.J.1    Hubbell, J.A.2    Anderson, J.M.3
  • 55
    • 0035135285 scopus 로고    scopus 로고
    • Fibronectin modulates macrophage adhesion and FBGC formation: The role of RGD, PHSRN, and PRRARV domains
    • Kao W.J., Lee D., Schense J.C., Hubbell J.A. - Fibronectin modulates macrophage adhesion and FBGC formation: the role of RGD, PHSRN, and PRRARV domains. - J.Biomed.Mater.Res., 55, 79-88, 2001.
    • (2001) J.Biomed.Mater.Res , vol.55 , pp. 79-88
    • Kao, W.J.1    Lee, D.2    Schense, J.C.3    Hubbell, J.A.4
  • 56
    • 0032486492 scopus 로고    scopus 로고
    • Design and function of novel osteoblast-adhesive peptides for chemical modification of biomaterials
    • Kay C.D. - Design and function of novel osteoblast-adhesive peptides for chemical modification of biomaterials. - J.Biomed.Mater.Res., 40, 371-377, 1998.
    • (1998) J.Biomed.Mater.Res , vol.40 , pp. 371-377
    • Kay, C.D.1
  • 57
    • 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., 875, 24-35, 1999.
    • (1999) Ann.NY Acad.Sci , vol.875 , pp. 24-35
    • Healy, K.E.1    Rezania, A.2    Stile, R.A.3
  • 58
    • 0343353897 scopus 로고    scopus 로고
    • Clinical biocompatibility of biodegradable orthopaedic implants for internal fixation: A review
    • Bostman O., Pihlajamaki H. - Clinical biocompatibility of biodegradable orthopaedic implants for internal fixation: a review. - Biomaterials, 21, 2615-2621, 2000.
    • (2000) Biomaterials , vol.21 , pp. 2615-2621
    • Bostman, O.1    Pihlajamaki, H.2
  • 59
    • 0033998768 scopus 로고    scopus 로고
    • Two different types of nonthrombogenic surfaces: PEG suppresses platelet adhesion ATP-independently but HEMA-St block copolymer requires ATP consumption of platelets to prevent adhesion
    • Uchida K., Yamato M., Ito E., Kwon O.H., Kikuchi A., Sakai K., Okano T. - Two different types of nonthrombogenic surfaces: PEG suppresses platelet adhesion ATP-independently but HEMA-St block copolymer requires ATP consumption of platelets to prevent adhesion. - J.Biomed.Mater.Res., 50, 585-590, 2000.
    • (2000) J.Biomed.Mater.Res , vol.50 , pp. 585-590
    • Uchida, K.1    Yamato, M.2    Ito, E.3    Kwon, O.H.4    Kikuchi, A.5    Sakai, K.6    Okano, T.7
  • 60
    • 0026122420 scopus 로고
    • Protein-surface interactions in the presence of polyethylene oxide : I.Simplified theory
    • Jeon S.I., Lee J.H., Andrade J.D., De Gennes P.G. - Protein-surface interactions in the presence of polyethylene oxide : I.Simplified theory. - J.Colloid Interface Sci., 142, 149-158, 1991.
    • (1991) J.Colloid Interface Sci , vol.142 , pp. 149-158
    • Jeon, S.I.1    Lee, J.H.2    Andrade, J.D.3    De Gennes, P.G.4
  • 61
    • 0026118420 scopus 로고
    • Protein-surface interactions in the presence of polyethylene oxide : II.Effect of protein size
    • Jeon S. I., Andrade J.D. - Protein-surface interactions in the presence of polyethylene oxide : II.Effect of protein size. - J.Colloid Interface Sci., 142, 159-166, 1991.
    • (1991) J.Colloid Interface Sci , vol.142 , pp. 159-166
    • Jeon, S.I.1    Andrade, J.D.2
  • 62
    • 33746192298 scopus 로고    scopus 로고
    • Protein adsorption from flowing Solutions on pure and maleic acid copolymer modified glass particles
    • Klose T., Welzel P.B., Werner C. - Protein adsorption from flowing Solutions on pure and maleic acid copolymer modified glass particles. - Colloids Surf.B: Biointerfaces, 51, 1-9, 2006.
    • (2006) Colloids Surf.B: Biointerfaces , vol.51 , pp. 1-9
    • Klose, T.1    Welzel, P.B.2    Werner, C.3
  • 63
    • 4143126687 scopus 로고    scopus 로고
    • Competitive adsorption of model charged proteins: The effect of total charge and charge distribution
    • Gong P., Szleifer I. - Competitive adsorption of model charged proteins: the effect of total charge and charge distribution. - J.Colloid Interface Sci., 278, 81-90, 2004.
    • (2004) J.Colloid Interface Sci , vol.278 , pp. 81-90
    • Gong, P.1    Szleifer, I.2
  • 64
    • 0026719563 scopus 로고
    • Surface-immobilized polyethylene oxide for bacterial repellence
    • Desai N.P., Hossainy S.F.A., Hubbell J.A. - Surface-immobilized polyethylene oxide for bacterial repellence. - Biomaterials, 13, 417-420, 1992.
    • (1992) Biomaterials , vol.13 , pp. 417-420
    • Desai, N.P.1    Hossainy, S.F.A.2    Hubbell, J.A.3
  • 65
    • 0032314248 scopus 로고    scopus 로고
    • Novel biomedical polymers for regulating serious biological reactions
    • Ishihara K., Iwasaki Y., Nakabayashi N. - Novel biomedical polymers for regulating serious biological reactions. - Mater. Sci.Eng.,C, 6, 253-259, 1998.
    • (1998) Mater. Sci.Eng.,C , vol.6 , pp. 253-259
    • Ishihara, K.1    Iwasaki, Y.2    Nakabayashi, N.3
  • 67
    • 5144230250 scopus 로고    scopus 로고
    • Surface engineering strategies for control of protein and cell interactions
    • Nath N., Hyun J., Ma H., Chilkoti A. - Surface engineering strategies for control of protein and cell interactions.- Surf.Sci., 570, 98-110, 2004.
    • (2004) Surf.Sci , vol.570 , pp. 98-110
    • Nath, N.1    Hyun, J.2    Ma, H.3    Chilkoti, A.4
  • 68
    • 0024635932 scopus 로고
    • Protein-resistant surfaces prepared by PEO-containing block copolymer surfactants
    • Lee J.H., Kopecek J., Andrade J.D. - Protein-resistant surfaces prepared by PEO-containing block copolymer surfactants. - J.Biomed.Mater.Res., 23, 351-368, 1989.
    • (1989) J.Biomed.Mater.Res , vol.23 , pp. 351-368
    • Lee, J.H.1    Kopecek, J.2    Andrade, J.D.3
  • 69
    • 33846706548 scopus 로고    scopus 로고
    • Customized PEG-Derived Copolymers for Tissue-Engineering Applications
    • Tessmar J., Goepferich A. - Customized PEG-Derived Copolymers for Tissue-Engineering Applications. - Macromol.Biosci., 7, 23-39, 2007.
    • (2007) Macromol.Biosci , vol.7 , pp. 23-39
    • Tessmar, J.1    Goepferich, A.2
  • 70
    • 0019690627 scopus 로고
    • Quasielastic light scattering measurements of polystyrene latices and conformation of poly(oxyethylene) adsorbed on the latices
    • Kato T., Nakamura K., Kawaguchi M., Takahashi A. - Quasielastic light scattering measurements of polystyrene latices and conformation of poly(oxyethylene) adsorbed on the latices. - Polym.J., 13, 1037-1043, 1981.
    • (1981) Polym.J , vol.13 , pp. 1037-1043
    • Kato, T.1    Nakamura, K.2    Kawaguchi, M.3    Takahashi, A.4
  • 71
    • 0024993790 scopus 로고
    • Surface properties of copolymers of alkyl methacrylates with, methoxy (polyethylene oxide) methacrylates and their application as protein-resistant coatings
    • Lee J.H., Kopeckova P., Kopecek J., Andrade J.D. - Surface properties of copolymers of alkyl methacrylates with, methoxy (polyethylene oxide) methacrylates and their application as protein-resistant coatings. - Biomaterials, 11, 455-464, 1990.
    • (1990) Biomaterials , vol.11 , pp. 455-464
    • Lee, J.H.1    Kopeckova, P.2    Kopecek, J.3    Andrade, J.D.4
  • 72
    • 0037323584 scopus 로고    scopus 로고
    • Poly(D,L-lactic acid)-poly(ethylene glycol)-monomethyl ether diblock copolymers control adhesion and osteoblastic differentiation of marrow stromal cells
    • Lieb E., Tessmar J., Hacker M., Fischbach C., Rose D., Blunk T., Mikos A.G., Goepferich A., Schulz M.B. - Poly(D,L-lactic acid)-poly(ethylene glycol)-monomethyl ether diblock copolymers control adhesion and osteoblastic differentiation of marrow stromal cells. - Tissue Eng., 9, 71-84, 2003.
    • (2003) Tissue Eng , vol.9 , pp. 71-84
    • Lieb, E.1    Tessmar, J.2    Hacker, M.3    Fischbach, C.4    Rose, D.5    Blunk, T.6    Mikos, A.G.7    Goepferich, A.8    Schulz, M.B.9
  • 74
    • 0031066175 scopus 로고    scopus 로고
    • Mucins and inflammatory bowel disease
    • Rhodes J.M. - Mucins and inflammatory bowel disease. - QJM, 90, 79-82, 1997.
    • (1997) QJM , vol.90 , pp. 79-82
    • Rhodes, J.M.1
  • 76
    • 15944409232 scopus 로고    scopus 로고
    • Impedance and QCM analysis of the protein resistance of self-assembled PEGylated alkanethiol layers on gold
    • Menz B., Knerr R., Goepferich A., Steinern C. - Impedance and QCM analysis of the protein resistance of self-assembled PEGylated alkanethiol layers on gold. - Biomaterials, 26, 4237-4243, 2005.
    • (2005) Biomaterials , vol.26 , pp. 4237-4243
    • Menz, B.1    Knerr, R.2    Goepferich, A.3    Steinern, C.4
  • 77
    • 33751518996 scopus 로고    scopus 로고
    • Measuring cell adhesion on RGD-modified, self-assembled PEG monolayers using the quartz crystal microbalance technique
    • Knerr R., Weiser B., Drotleff S., Steinem C., Goepferich A. - Measuring cell adhesion on RGD-modified, self-assembled PEG monolayers using the quartz crystal microbalance technique. - Macromol.Biosci., 6, 827-838, 2006.
    • (2006) Macromol.Biosci , vol.6 , pp. 827-838
    • Knerr, R.1    Weiser, B.2    Drotleff, S.3    Steinem, C.4    Goepferich, A.5
  • 78
    • 0022343943 scopus 로고
    • Improved endothelial cell seeding with cultured cells and fibronectin-coated grafts
    • Seeger J.M., Klingman N. - Improved endothelial cell seeding with cultured cells and fibronectin-coated grafts. - J.Surg.Res., 38, 641-647, 1985.
    • (1985) J.Surg.Res , vol.38 , pp. 641-647
    • Seeger, J.M.1    Klingman, N.2
  • 79
    • 0026016494 scopus 로고
    • Adult human endothelial cell seeding using expanded polytetrafluoroethylene vascular grafts: A comparison of four substrates
    • Thomson G.J., Vohra R.K., Carr M.H., Walker M.G. - Adult human endothelial cell seeding using expanded polytetrafluoroethylene vascular grafts: a comparison of four substrates. - Surgery, 109, 20-27, 1991.
    • (1991) Surgery , vol.109 , pp. 20-27
    • Thomson, G.J.1    Vohra, R.K.2    Carr, M.H.3    Walker, M.G.4
  • 80
    • 0025774297 scopus 로고
    • Comparison of different vascular prostheses and matrices in relation to endothelial seeding
    • Vohra R., Thomson G.J., Carr H.M., Sharma H., Walker M.G. - Comparison of different vascular prostheses and matrices in relation to endothelial seeding. - Br.J.Surg., 78, 417-420, 1991.
    • (1991) Br.J.Surg , vol.78 , pp. 417-420
    • Vohra, R.1    Thomson, G.J.2    Carr, H.M.3    Sharma, H.4    Walker, M.G.5
  • 81
    • 0025787024 scopus 로고
    • The effect of varying fibronectin concentration on the attachment of endothelial cells to polytetrafluoroethylene vascular grafts
    • Walker M.G., Vohra R.K., Thomson G.J., Sharma H., Carr H.M. - The effect of varying fibronectin concentration on the attachment of endothelial cells to polytetrafluoroethylene vascular grafts. - J.Vasc.Surg., 14, 124, 1991.
    • (1991) J.Vasc.Surg , vol.14 , pp. 124
    • Walker, M.G.1    Vohra, R.K.2    Thomson, G.J.3    Sharma, H.4    Carr, H.M.5
  • 82
    • 0024402028 scopus 로고
    • Precoating substrate and surface configuration determine adherence and spreading of seeded endothelial cells on polytetrafluoroethylene grafts
    • Kaehler J., Zilla P., Fasol R., Deutsch M., Kadletz M. - Precoating substrate and surface configuration determine adherence and spreading of seeded endothelial cells on polytetrafluoroethylene grafts. - J.Vasc.Surg., 9, 535-541, 1989.
    • (1989) J.Vasc.Surg , vol.9 , pp. 535-541
    • Kaehler, J.1    Zilla, P.2    Fasol, R.3    Deutsch, M.4    Kadletz, M.5
  • 83
    • 0030111469 scopus 로고    scopus 로고
    • Studies on the biocompatibility of materials: Fibroblast reorganization of substratum-bound fibronectin on surfaces varying in wettability
    • Altankov G., Grinnell F., Groth T. - Studies on the biocompatibility of materials: fibroblast reorganization of substratum-bound fibronectin on surfaces varying in wettability. - J.Biomed.Mater. Res., 30, 385-391, 1996.
    • (1996) J.Biomed.Mater. Res , vol.30 , pp. 385-391
    • Altankov, G.1    Grinnell, F.2    Groth, T.3
  • 84
    • 0027641056 scopus 로고
    • Effect of the conformation and orientation of adsorbed fibronectin on endothelial cell spreading and the strength of adhesion
    • Iuliano D.J., Saavedra S.S., Truskey G.A. - Effect of the conformation and orientation of adsorbed fibronectin on endothelial cell spreading and the strength of adhesion. - J.Biomed.Mater. Res., 27, 1103-1113, 1993.
    • (1993) J.Biomed.Mater. Res , vol.27 , pp. 1103-1113
    • Iuliano, D.J.1    Saavedra, S.S.2    Truskey, G.A.3
  • 85
    • 0026940917 scopus 로고
    • Cell-type-specific adhesion mechanisms mediated by fibronectin adsorbed to chemically derivatized substrata
    • Lewandowska K., Pergament E., Sukenik C.N., Culp L.A. - Cell-type-specific adhesion mechanisms mediated by fibronectin adsorbed to chemically derivatized substrata. - J.Biomed.Mater. Res., 26, 1343-1363, 1992.
    • (1992) J.Biomed.Mater. Res , vol.26 , pp. 1343-1363
    • Lewandowska, K.1    Pergament, E.2    Sukenik, C.N.3    Culp, L.A.4
  • 86
    • 0026261770 scopus 로고
    • Materials for enhancing cell adhesion by immobilization of cell-adhesive peptide
    • Ito Y., Kajihara M., Imanishi Y. - Materials for enhancing cell adhesion by immobilization of cell-adhesive peptide. - J.Biomed. Mater.Res., 25, 1325-1337, 1991.
    • (1991) J.Biomed. Mater.Res , vol.25 , pp. 1325-1337
    • Ito, Y.1    Kajihara, M.2    Imanishi, Y.3
  • 89
    • 0342433776 scopus 로고    scopus 로고
    • Synthesis of polyethylene glycol)-tethered polypropylene fumarate) and its modification with GRGD peptide
    • Jo S., Engel P.S., Mikos A.G. - Synthesis of polyethylene glycol)-tethered polypropylene fumarate) and its modification with GRGD peptide. - Polymer, 41, 7595-7604, 2000.
    • (2000) Polymer , vol.41 , pp. 7595-7604
    • Jo, S.1    Engel, P.S.2    Mikos, A.G.3
  • 90
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Hartmuth C.K. - Click chemistry: diverse chemical function from a few good reactions. - Angew.Chem.Int.Ed., 40, 2004-2021, 2001.
    • (2001) Angew.Chem.Int.Ed , vol.40 , pp. 2004-2021
    • Hartmuth, C.K.1
  • 91
    • 0348109450 scopus 로고    scopus 로고
    • The growing impact of click chemistry on drug discovery
    • Kolb H.C., Sharpless K.B. - The growing impact of click chemistry on drug discovery. - Drug Discovery Today, 8, 1128-1137, 2003.
    • (2003) Drug Discovery Today , vol.8 , pp. 1128-1137
    • Kolb, H.C.1    Sharpless, K.B.2
  • 92
    • 0037454346 scopus 로고    scopus 로고
    • Wang Q., Chan T.R., Hilgraf R., Fokin V.V., Sharpless K.B., Finn M.G. - Bioconjugation by copper(I)-catalyzed azide-alkyne [3+2] cycloaddition. - J.Am.Chem.Soc., 125, 3192-3193, 2003.
    • Wang Q., Chan T.R., Hilgraf R., Fokin V.V., Sharpless K.B., Finn M.G. - Bioconjugation by copper(I)-catalyzed azide-alkyne [3+2] cycloaddition. - J.Am.Chem.Soc., 125, 3192-3193, 2003.
  • 93
    • 0041692305 scopus 로고    scopus 로고
    • Link A.J., Tirrell D.A. - Cell surface labeling of Escherichia coli via copper(I)-catalyzed [3+2] cycloaddition. - J.Am.Chem.Soc., 125, 11164-11165, 2003.
    • Link A.J., Tirrell D.A. - Cell surface labeling of Escherichia coli via copper(I)-catalyzed [3+2] cycloaddition. - J.Am.Chem.Soc., 125, 11164-11165, 2003.
  • 94
    • 0141732270 scopus 로고    scopus 로고
    • Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae
    • Deiters A., Cropp T.A., Mukherji M., Chin J.W., Anderson J.C., Schultz P.G. - Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae. - J.Am.Chem.Soc., 125, 11782-11783, 2003.
    • (2003) J.Am.Chem.Soc , vol.125 , pp. 11782-11783
    • Deiters, A.1    Cropp, T.A.2    Mukherji, M.3    Chin, J.W.4    Anderson, J.C.5    Schultz, P.G.6
  • 95
    • 0345869853 scopus 로고    scopus 로고
    • Surface tailoring of poly(-lactic acid) by ligand-tethered amphiphilic polymer for promoting chondrocyte attachment and growth
    • Ji J., Zhu H., Shen J. - Surface tailoring of poly(-lactic acid) by ligand-tethered amphiphilic polymer for promoting chondrocyte attachment and growth. - Biomaterials, 25, 1859-1867, 2004.
    • (2004) Biomaterials , vol.25 , pp. 1859-1867
    • Ji, J.1    Zhu, H.2    Shen, J.3
  • 97
    • 0035889827 scopus 로고    scopus 로고
    • Smooth muscle cell growth in photopolymerized hydrogels with cell adhesive and proteolytically degradable domains: Synthetic ECM analogs for tissue engineering
    • Mann B.K., Gobin A.S., Tsai A.T., Schmedlen R.H., West J.L. - Smooth muscle cell growth in photopolymerized hydrogels with cell adhesive and proteolytically degradable domains: synthetic ECM analogs for tissue engineering. - Biomaterials, 22, 3045-3051, 2001.
    • (2001) Biomaterials , vol.22 , pp. 3045-3051
    • Mann, B.K.1    Gobin, A.S.2    Tsai, A.T.3    Schmedlen, R.H.4    West, J.L.5
  • 98
    • 0034308316 scopus 로고    scopus 로고
    • Smooth muscle cell adhesion to tissue engineering scaffolds
    • Nikolovski J., Mooney D.J. - Smooth muscle cell adhesion to tissue engineering scaffolds. - Biomaterials, 21, 2025-2032, 2000.
    • (2000) Biomaterials , vol.21 , pp. 2025-2032
    • Nikolovski, J.1    Mooney, D.J.2
  • 99
    • 0037572325 scopus 로고    scopus 로고
    • RGD-grafted poly-I-lysine-graft-(polyethylene glycol) copolymers block non-specific protein adsorption while promoting cell adhesion
    • VandeVondele S., Vörös J., Hubbell J.A. - RGD-grafted poly-I-lysine-graft-(polyethylene glycol) copolymers block non-specific protein adsorption while promoting cell adhesion. - Biotechnol. Bioeng., 82, 784-790, 2003.
    • (2003) Biotechnol. Bioeng , vol.82 , pp. 784-790
    • VandeVondele, S.1    Vörös, J.2    Hubbell, J.A.3
  • 101
    • 33646384586 scopus 로고    scopus 로고
    • Parameters influencing the stealthiness of colloidal drug delivery systems
    • Vonarbourg A., Passirani C., Saulnier P., Benoit J.P. - Parameters influencing the stealthiness of colloidal drug delivery systems. - Biomaterials, 27, 4356-4373, 2006.
    • (2006) Biomaterials , vol.27 , pp. 4356-4373
    • Vonarbourg, A.1    Passirani, C.2    Saulnier, P.3    Benoit, J.P.4
  • 102
    • 0029360711 scopus 로고
    • Long circulating microparticulate drug carriers
    • Stolnik S., Ilium L., Davis S.S. - Long circulating microparticulate drug carriers. - Adv.Drug Delivery Rev., 16, 195-214, 1995.
    • (1995) Adv.Drug Delivery Rev , vol.16 , pp. 195-214
    • Stolnik, S.1    Ilium, L.2    Davis, S.S.3
  • 105
    • 4444350887 scopus 로고    scopus 로고
    • Surface-engineered nanoparticles as drug carriers
    • M.I.Baraton Ed, American Scientific Publishers
    • Gref, R. - Surface-engineered nanoparticles as drug carriers. - In: Synthesis, functionalization and surface treatment of nanoparticles, M.I.Baraton Ed., American Scientific Publishers, 2002, pp. 233-256.
    • (2002) Synthesis, functionalization and surface treatment of nanoparticles , pp. 233-256
    • Gref, R.1
  • 106
    • 0037275061 scopus 로고    scopus 로고
    • Colloidal drug carriers: Achievements and perspectives
    • Barratt G. - Colloidal drug carriers: achievements and perspectives. - Cell.Mol.Life Sci., 60, 21-37, 2003.
    • (2003) Cell.Mol.Life Sci , vol.60 , pp. 21-37
    • Barratt, G.1
  • 107
    • 0034107649 scopus 로고    scopus 로고
    • Cell adhesion inhibition by glycoliposomes: Effects of vesicle diameter and ligand density
    • Stahn R., Zeisig R. - Cell adhesion inhibition by glycoliposomes: effects of vesicle diameter and ligand density. - Tumor Biol., 21, 176-186, 2000.
    • (2000) Tumor Biol , vol.21 , pp. 176-186
    • Stahn, R.1    Zeisig, R.2
  • 109
    • 85031451980 scopus 로고    scopus 로고
    • Barbet, J. - Immunoliposomes. - In: Liposomes: New Systems and New Trends in Their Applications, Puisieux F., Couvreur, P., Delattre, J., Devissaguet, J.-P.Eds., Editions de Santé, Paris, 1995, pp. 159-191.
    • Barbet, J. - Immunoliposomes. - In: Liposomes: New Systems and New Trends in Their Applications, Puisieux F., Couvreur, P., Delattre, J., Devissaguet, J.-P.Eds., Editions de Santé, Paris, 1995, pp. 159-191.
  • 110
    • 85031436827 scopus 로고    scopus 로고
    • Zalipsky, S., Gittelman, J., Mullah, N.and Qazen, M.M. - Biologically active ligand-bearing polymer-grafted liposomes. - In: Targeting of Drugs 6: Strategies for Stealth Therapeutic Systems, G.Gregoriadis, McCormack, B.Eds., Plenum, New York, 1998, pp. 131-138.
    • Zalipsky, S., Gittelman, J., Mullah, N.and Qazen, M.M. - Biologically active ligand-bearing polymer-grafted liposomes. - In: Targeting of Drugs 6: Strategies for Stealth Therapeutic Systems, G.Gregoriadis, McCormack, B.Eds., Plenum, New York, 1998, pp. 131-138.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.