메뉴 건너뛰기




Volumn 63, Issue 12, 2011, Pages 988-999

Surface plasmon resonance in monitoring of complement activation on biomaterials

Author keywords

Complement activation; Nonspecific protein adsorption; Polymer coating; Self assembled monolayer; Surface plasmon resonance; The alternative pathway; The classical pathway

Indexed keywords

CLASSICAL PATHWAY; COMPLEMENT ACTIVATION; NON-SPECIFIC PROTEIN ADSORPTION; POLYMER COATING; SURFACE PLASMONS; THE ALTERNATIVE PATHWAY;

EID: 80052150500     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2011.06.018     Document Type: Review
Times cited : (31)

References (108)
  • 2
    • 77955883153 scopus 로고    scopus 로고
    • Complement: a key system for immune surveillance and homeostasis
    • Ricklin D., Hajishengallis G., Yang K., Lambris J.D. Complement: a key system for immune surveillance and homeostasis. Nat. Immunol. 2010, 11:785-797.
    • (2010) Nat. Immunol. , vol.11 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 3
    • 0021618203 scopus 로고
    • Complement activation during hemodialysis: clinical observations, proposed mechanisms, and theoretical implications
    • Chenoweth D.E. Complement activation during hemodialysis: clinical observations, proposed mechanisms, and theoretical implications. Artif. Organs 1984, 8:281-290.
    • (1984) Artif. Organs , vol.8 , pp. 281-290
    • Chenoweth, D.E.1
  • 4
    • 0022572342 scopus 로고
    • Biocompatibility of different hemodialysis membranes: activation of complement and leukopenia
    • Wegmuller E., Montandon A., Nydegger U., Descoeudres C. Biocompatibility of different hemodialysis membranes: activation of complement and leukopenia. Int. J. Artif. Organs 1986, 9:85-92.
    • (1986) Int. J. Artif. Organs , vol.9 , pp. 85-92
    • Wegmuller, E.1    Montandon, A.2    Nydegger, U.3    Descoeudres, C.4
  • 5
    • 39549123065 scopus 로고    scopus 로고
    • Complement activation during cardiopulmonary bypass: Evidence for generation of C3a and C5a anaphylatoxins
    • Chenoweth D.E., Cooper S.W., Hugli T.E., Stewart R.W., Blackstone E.H., Kinklin J.W. Complement activation during cardiopulmonary bypass: Evidence for generation of C3a and C5a anaphylatoxins. N. Engl. J. Med. 2001, 344:1058-1066.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1058-1066
    • Chenoweth, D.E.1    Cooper, S.W.2    Hugli, T.E.3    Stewart, R.W.4    Blackstone, E.H.5    Kinklin, J.W.6
  • 6
    • 0028465473 scopus 로고
    • Activation of plasma components by leukocyte removal filters
    • Gu Y.J., van Oeveren W. Activation of plasma components by leukocyte removal filters. ASAIO J. 1994, 40:598-601.
    • (1994) ASAIO J. , vol.40 , pp. 598-601
    • Gu, Y.J.1    van Oeveren, W.2
  • 7
    • 0023790056 scopus 로고
    • Structure-function relationship in the inhibitory effect of heparin on complement activation: Independency of the anti-coagulant and anti-complementary sites on the heparin molecule
    • Maillet F., Petitou M., Choay J., Kazatchkine D. Structure-function relationship in the inhibitory effect of heparin on complement activation: Independency of the anti-coagulant and anti-complementary sites on the heparin molecule. Mol. Immunol. 1988, 25:917-923.
    • (1988) Mol. Immunol. , vol.25 , pp. 917-923
    • Maillet, F.1    Petitou, M.2    Choay, J.3    Kazatchkine, D.4
  • 9
    • 0028501340 scopus 로고
    • Using Elisa to evaluate complement activation by reference biomaterials
    • Berger M., Broxup B., Sefton M.V. Using Elisa to evaluate complement activation by reference biomaterials. J. Mater. Sci. Mater. Med. 1994, 5:622-627.
    • (1994) J. Mater. Sci. Mater. Med. , vol.5 , pp. 622-627
    • Berger, M.1    Broxup, B.2    Sefton, M.V.3
  • 10
    • 0032855378 scopus 로고    scopus 로고
    • Complement activation by PEO-grafted glass surfaces
    • Kidane A., Park K. Complement activation by PEO-grafted glass surfaces. J. Biomed. Mater. Res. 1999, 48:640-647.
    • (1999) J. Biomed. Mater. Res. , vol.48 , pp. 640-647
    • Kidane, A.1    Park, K.2
  • 11
    • 24044534447 scopus 로고    scopus 로고
    • Complement inhibition reduces material-induced leukocyte activation with PEG modified polystyrene beads (TentagelTM) but not polystyrene beads
    • Gorbet M.B., Sefton M.V. Complement inhibition reduces material-induced leukocyte activation with PEG modified polystyrene beads (TentagelTM) but not polystyrene beads. J. Biomed. Mater. Res. 2005, 74A:511-522.
    • (2005) J. Biomed. Mater. Res. , vol.74 A , pp. 511-522
    • Gorbet, M.B.1    Sefton, M.V.2
  • 12
    • 33745335810 scopus 로고    scopus 로고
    • Complement activation by sulfonated poly(ethylene glycol)-acrylate copolymers through alternative pathway
    • Jang H.S., Ryu K.E., Ahn W.S., Chun H.J., Park H.D., Kim Y.H. Complement activation by sulfonated poly(ethylene glycol)-acrylate copolymers through alternative pathway. Colloids Surf. B 2006, 50:141-146.
    • (2006) Colloids Surf. B , vol.50 , pp. 141-146
    • Jang, H.S.1    Ryu, K.E.2    Ahn, W.S.3    Chun, H.J.4    Park, H.D.5    Kim, Y.H.6
  • 15
    • 0028584384 scopus 로고
    • Real-time biospecific interaction analysis
    • Lundström I. Real-time biospecific interaction analysis. Biosens. Bioelectron. 1994, 9:725-736.
    • (1994) Biosens. Bioelectron. , vol.9 , pp. 725-736
    • Lundström, I.1
  • 18
    • 0344177897 scopus 로고    scopus 로고
    • Present and future of surface plasmon resonance biosensors
    • Homola J. Present and future of surface plasmon resonance biosensors. Anal. Bioanal. Chem. 2003, 377:528-539.
    • (2003) Anal. Bioanal. Chem. , vol.377 , pp. 528-539
    • Homola, J.1
  • 19
    • 40449111291 scopus 로고    scopus 로고
    • Surface plasmon resonance sensors for detection of chemical and biological species
    • Homola J. Surface plasmon resonance sensors for detection of chemical and biological species. Chem. Rev. 2008, 108:462-493.
    • (2008) Chem. Rev. , vol.108 , pp. 462-493
    • Homola, J.1
  • 20
    • 84934441970 scopus 로고    scopus 로고
    • Exploring the complement interaction network using surface plasmon resonance
    • Ricklin D., Lambris J.D. Exploring the complement interaction network using surface plasmon resonance. Adv. Exp. Med. Biol. 2007, 598:260-278.
    • (2007) Adv. Exp. Med. Biol. , vol.598 , pp. 260-278
    • Ricklin, D.1    Lambris, J.D.2
  • 23
    • 34250515667 scopus 로고
    • Excitation of nonradiative surface plasma waves in silver by the method of frustrated total reflection
    • Otto A. Excitation of nonradiative surface plasma waves in silver by the method of frustrated total reflection. Z. Phys. 1968, 216:398-410.
    • (1968) Z. Phys. , vol.216 , pp. 398-410
    • Otto, A.1
  • 24
    • 28044445190 scopus 로고
    • The determination of the optical constants of metals by excitation of surface plasmons
    • Kretchmann E. The determination of the optical constants of metals by excitation of surface plasmons. Z. Phys. 1971, 241:313-324.
    • (1971) Z. Phys. , vol.241 , pp. 313-324
    • Kretchmann, E.1
  • 26
    • 0001383816 scopus 로고
    • Polymer thin films and interfaces characterized with evanescent light
    • Knoll W. Polymer thin films and interfaces characterized with evanescent light. Makromol. Chem. 1991, 192:2827-2856.
    • (1991) Makromol. Chem. , vol.192 , pp. 2827-2856
    • Knoll, W.1
  • 27
    • 13844281513 scopus 로고    scopus 로고
    • Direct optical sensors: principles and selected applications
    • Gauglitz G. Direct optical sensors: principles and selected applications. Anal. Bioanal. Chem. 2005, 381:141-155.
    • (2005) Anal. Bioanal. Chem. , vol.381 , pp. 141-155
    • Gauglitz, G.1
  • 28
    • 78650225822 scopus 로고    scopus 로고
    • Direct optical detection in bioanalysis: an update
    • Gauglitz G. Direct optical detection in bioanalysis: an update. Anal. Bioanal. Chem. 2010, 398:2363-2372.
    • (2010) Anal. Bioanal. Chem. , vol.398 , pp. 2363-2372
    • Gauglitz, G.1
  • 29
    • 0014489983 scopus 로고
    • Identification of rapid changes at plasma-solid interfaces
    • Vroman L., Adams A.L. Identification of rapid changes at plasma-solid interfaces. J. Biomed. Mater. Res. 1969, 3:43-67.
    • (1969) J. Biomed. Mater. Res. , vol.3 , pp. 43-67
    • Vroman, L.1    Adams, A.L.2
  • 30
    • 0023398010 scopus 로고
    • Competition between adsorbed fibrinogen and high-molecular-weight kininogen on solid surfaces incubated in human plasma (the Vroman effect): influence of solid surface wettability
    • Elwing H., Askendal A., Lundström I. Competition between adsorbed fibrinogen and high-molecular-weight kininogen on solid surfaces incubated in human plasma (the Vroman effect): influence of solid surface wettability. J. Biomed. Mater. Res. 1987, 21:1023-1028.
    • (1987) J. Biomed. Mater. Res. , vol.21 , pp. 1023-1028
    • Elwing, H.1    Askendal, A.2    Lundström, I.3
  • 32
    • 0031249906 scopus 로고    scopus 로고
    • In vitro plasma protein adsorption on ω-functionalized alkanethiolate self-assembled monolayers
    • Lestelius M., Liedberg B., Tengvall P. In vitro plasma protein adsorption on ω-functionalized alkanethiolate self-assembled monolayers. Langmuir 1997, 13:5900-5908.
    • (1997) Langmuir , vol.13 , pp. 5900-5908
    • Lestelius, M.1    Liedberg, B.2    Tengvall, P.3
  • 33
    • 0022461272 scopus 로고
    • Complement deposition from human sera on silicon surfaces studied in situ ellipsometry: the influence of surface wettability
    • Elwing H., Ivarsson B., Lundström I. Complement deposition from human sera on silicon surfaces studied in situ ellipsometry: the influence of surface wettability. Eur. J. Biochem. 1986, 156:359-365.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 359-365
    • Elwing, H.1    Ivarsson, B.2    Lundström, I.3
  • 34
    • 0030152312 scopus 로고    scopus 로고
    • Complement activation by 3-mercapto-1,2-propanediol immobilized on gold surfaces
    • Tengvall P., Askendal A., Lundström I. Complement activation by 3-mercapto-1,2-propanediol immobilized on gold surfaces. Biomaterials 1996, 17:1001-1007.
    • (1996) Biomaterials , vol.17 , pp. 1001-1007
    • Tengvall, P.1    Askendal, A.2    Lundström, I.3
  • 35
    • 0030130807 scopus 로고    scopus 로고
    • Complement activation on thiol-modified gold surfaces
    • Liu L., Elwing H. Complement activation on thiol-modified gold surfaces. J. Biomed. Mater. Res. 1996, 30:535-541.
    • (1996) J. Biomed. Mater. Res. , vol.30 , pp. 535-541
    • Liu, L.1    Elwing, H.2
  • 36
    • 0030199893 scopus 로고    scopus 로고
    • Complement activation by IgG immobilized on methylated silicon
    • Tengvall P., Askendal A., Lundström I. Complement activation by IgG immobilized on methylated silicon. J. Biomed. Mater. Res. 1996, 31:305-312.
    • (1996) J. Biomed. Mater. Res. , vol.31 , pp. 305-312
    • Tengvall, P.1    Askendal, A.2    Lundström, I.3
  • 37
    • 0031127587 scopus 로고    scopus 로고
    • Temporal studies on the deposition of complement on human colostrum IgA and serum IgG immobilized on methylated silicon
    • Tengvall P., Askendal A., Lundström I. Temporal studies on the deposition of complement on human colostrum IgA and serum IgG immobilized on methylated silicon. J. Biomed. Mater. Res. 1997, 35:81-92.
    • (1997) J. Biomed. Mater. Res. , vol.35 , pp. 81-92
    • Tengvall, P.1    Askendal, A.2    Lundström, I.3
  • 38
    • 0032144460 scopus 로고    scopus 로고
    • Complement activation and inflammation triggered by model biomaterial surfaces
    • Tang L., Liu L., Elwing H.B. Complement activation and inflammation triggered by model biomaterial surfaces. J. Biomed. Mater. Res. 1998, 41:333-341.
    • (1998) J. Biomed. Mater. Res. , vol.41 , pp. 333-341
    • Tang, L.1    Liu, L.2    Elwing, H.B.3
  • 39
    • 0035864104 scopus 로고    scopus 로고
    • Ellipsometric in vitro studies on the activation of complement by human immunoglobulins M and G after adsorption to methylated silicon
    • Tengvall P., Askendal A., Lundström I. Ellipsometric in vitro studies on the activation of complement by human immunoglobulins M and G after adsorption to methylated silicon. Colloids Surf. B 2001, 20:51-62.
    • (2001) Colloids Surf. B , vol.20 , pp. 51-62
    • Tengvall, P.1    Askendal, A.2    Lundström, I.3
  • 40
    • 0037082746 scopus 로고    scopus 로고
    • On the binding of complement to solid artificial surfaces in vitro
    • Wetterö J., Askendal A., Bengtsson T., Tengvall P. On the binding of complement to solid artificial surfaces in vitro. Biomaterials 2002, 23:981-991.
    • (2002) Biomaterials , vol.23 , pp. 981-991
    • Wetterö, J.1    Askendal, A.2    Bengtsson, T.3    Tengvall, P.4
  • 41
    • 0036604084 scopus 로고    scopus 로고
    • C3 adsorbed to a polymer surface can form an initiating alternative pathway convertase
    • Andersson J., Ekdahl K.N., Larsson R., Nilsson U.R., Nilsson B. C3 adsorbed to a polymer surface can form an initiating alternative pathway convertase. J. Immunol. 2002, 168:5786-5791.
    • (2002) J. Immunol. , vol.168 , pp. 5786-5791
    • Andersson, J.1    Ekdahl, K.N.2    Larsson, R.3    Nilsson, U.R.4    Nilsson, B.5
  • 42
    • 7444238105 scopus 로고    scopus 로고
    • Binding of C3 fragments on top of adsorbed plasma proteins during complement activation on a model biomaterial surface
    • Andersson J., Ekdahl K.N., Lambris J.D., Nilsson B. Binding of C3 fragments on top of adsorbed plasma proteins during complement activation on a model biomaterial surface. Biomaterials 2005, 26:1477-1485.
    • (2005) Biomaterials , vol.26 , pp. 1477-1485
    • Andersson, J.1    Ekdahl, K.N.2    Lambris, J.D.3    Nilsson, B.4
  • 43
    • 10644221291 scopus 로고    scopus 로고
    • Immune complement activation on polystyrene and silicon dioxide surfaces: impact of reversible IgG adsorption
    • Sellborn A., Andersson M., Hedlund J., Andersson J., Berglin M., Elwing H. Immune complement activation on polystyrene and silicon dioxide surfaces: impact of reversible IgG adsorption. Mol. Immunol. 2005, 42:569-574.
    • (2005) Mol. Immunol. , vol.42 , pp. 569-574
    • Sellborn, A.1    Andersson, M.2    Hedlund, J.3    Andersson, J.4    Berglin, M.5    Elwing, H.6
  • 44
    • 0035894177 scopus 로고    scopus 로고
    • Variations in coupled water, viscoelastic properties, and film thickness of a Mefp-1 protein film during adsorption and cross-linking: a quartz crystal microbalance with dissipation monitoring, ellipsometry, and surface plasmon resonance study
    • Höök F., Kasemo B., Nylander T., Fant C., Sott K., Elwing H. Variations in coupled water, viscoelastic properties, and film thickness of a Mefp-1 protein film during adsorption and cross-linking: a quartz crystal microbalance with dissipation monitoring, ellipsometry, and surface plasmon resonance study. Anal. Chem. 2001, 73:5796-5804.
    • (2001) Anal. Chem. , vol.73 , pp. 5796-5804
    • Höök, F.1    Kasemo, B.2    Nylander, T.3    Fant, C.4    Sott, K.5    Elwing, H.6
  • 45
    • 10644245241 scopus 로고    scopus 로고
    • Simultaneous SPR and QCM-D monitoring measurements of biomolecular adsorption events involving structural transformations and variations in coupled water
    • Reimhult E., Larsson C., Kasemo B., Höök F. Simultaneous SPR and QCM-D monitoring measurements of biomolecular adsorption events involving structural transformations and variations in coupled water. Anal. Chem. 2004, 76:7211-7220.
    • (2004) Anal. Chem. , vol.76 , pp. 7211-7220
    • Reimhult, E.1    Larsson, C.2    Kasemo, B.3    Höök, F.4
  • 46
    • 0345979435 scopus 로고    scopus 로고
    • Formation and structure of self-assembled monolayers
    • Ulman A. Formation and structure of self-assembled monolayers. Chem. Rev. 1996, 96:1533-1554.
    • (1996) Chem. Rev. , vol.96 , pp. 1533-1554
    • Ulman, A.1
  • 47
    • 0032799596 scopus 로고    scopus 로고
    • The interaction of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver
    • Ostuni E., Yan L., Whitesides G.M. The interaction of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver. Colloids Surf. B 1999, 15:3-30.
    • (1999) Colloids Surf. B , vol.15 , pp. 3-30
    • Ostuni, E.1    Yan, L.2    Whitesides, G.M.3
  • 48
    • 18044398972 scopus 로고    scopus 로고
    • Self-assembled monolayers of thiolates on metals as a form of nanotechnology
    • Love J.C., Estroff L.A., Kriebel J.K., Nuzzo R.G., Whitesides G.M. Self-assembled monolayers of thiolates on metals as a form of nanotechnology. Chem. Rev. 2005, 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
  • 49
    • 25844504608 scopus 로고    scopus 로고
    • Self-assembled monolayers and polymer brushes in biotechnology: current applications and future perspectives
    • Senaratne W., Andruzzi L., Ober C.K. Self-assembled monolayers and polymer brushes in biotechnology: current applications and future perspectives. Biomacromolecules 2005, 6:2427-2448.
    • (2005) Biomacromolecules , vol.6 , pp. 2427-2448
    • Senaratne, W.1    Andruzzi, L.2    Ober, C.K.3
  • 50
    • 33845281250 scopus 로고
    • Fundamental studies of the chemisorption of organosulfur compounds on Au(111). Implications for molecular self-assembly on gold surfaces
    • Nuzzo R.G., Zegarski B.R., Dubois L.H. Fundamental studies of the chemisorption of organosulfur compounds on Au(111). Implications for molecular self-assembly on gold surfaces. J. Am. Chem. Soc. 1987, 109:733-740.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 733-740
    • Nuzzo, R.G.1    Zegarski, B.R.2    Dubois, L.H.3
  • 51
    • 0025366704 scopus 로고
    • Fundamental studies of microscopic wetting on organic surfaces. 1. Formation and structural characterization of a self-consistent series of polyfunctional organic monolayers
    • Nuzzo R.G., Dubois L.H., Allara D.L. Fundamental studies of microscopic wetting on organic surfaces. 1. Formation and structural characterization of a self-consistent series of polyfunctional organic monolayers. J. Am. Chem. Soc. 1990, 112:558-569.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 558-569
    • Nuzzo, R.G.1    Dubois, L.H.2    Allara, D.L.3
  • 52
    • 0006163257 scopus 로고
    • Spontaneously organized molecular assemblies. 4. Structural characterization of n-alkyl thiol monolayers on gold by optical ellipsometry, infrared spectroscopy, and electrochemistry
    • Porter M.D., Bright T.B., Allara D.L., Chidsey C.E.D. Spontaneously organized molecular assemblies. 4. Structural characterization of n-alkyl thiol monolayers on gold by optical ellipsometry, infrared spectroscopy, and electrochemistry. J. Am. Chem. Soc. 1987, 109:3559-3568.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3559-3568
    • Porter, M.D.1    Bright, T.B.2    Allara, D.L.3    Chidsey, C.E.D.4
  • 53
    • 25744449978 scopus 로고
    • Structures of self-assembled monolayer films of organosulfur compounds adsorbed on gold single crystals: electron diffraction studies
    • Strong L., Whitesides G.M. Structures of self-assembled monolayer films of organosulfur compounds adsorbed on gold single crystals: electron diffraction studies. Langmuir 1988, 4:546-558.
    • (1988) Langmuir , vol.4 , pp. 546-558
    • Strong, L.1    Whitesides, G.M.2
  • 54
    • 0344738717 scopus 로고    scopus 로고
    • Deposition of complement protein C3b on mixed self-assembled monolayers carrying surface hydroxyl and methyl groups studied by surface plasmon resonance
    • Hirata I., Hioki Y., Toda M., Kitazawa T., Murakami Y., Kitano E., Kitamura H., Ikada Y., Iwata H. Deposition of complement protein C3b on mixed self-assembled monolayers carrying surface hydroxyl and methyl groups studied by surface plasmon resonance. J. Biomed. Mater. Res. 2003, 66A:669-676.
    • (2003) J. Biomed. Mater. Res. , vol.66 A , pp. 669-676
    • Hirata, I.1    Hioki, Y.2    Toda, M.3    Kitazawa, T.4    Murakami, Y.5    Kitano, E.6    Kitamura, H.7    Ikada, Y.8    Iwata, H.9
  • 55
    • 33845184543 scopus 로고
    • Formation of monolayers by the coadsorption of thiols on gold: variation in the head group, tail group, and solvent
    • Bain C.D., Evall J., Whitesides G.M. Formation of monolayers by the coadsorption of thiols on gold: variation in the head group, tail group, and solvent. J. Am. Chem. Soc. 1989, 111:7155-7164.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7155-7164
    • Bain, C.D.1    Evall, J.2    Whitesides, G.M.3
  • 56
    • 34247131744 scopus 로고    scopus 로고
    • Effect of wettability and surface functional groups on protein adsorption and cell adhesion using well-defined mixed self-assembled monolayers
    • Arima Y., Iwata H. Effect of wettability and surface functional groups on protein adsorption and cell adhesion using well-defined mixed self-assembled monolayers. Biomaterials 2007, 28:3074-3082.
    • (2007) Biomaterials , vol.28 , pp. 3074-3082
    • Arima, Y.1    Iwata, H.2
  • 58
    • 13244272160 scopus 로고    scopus 로고
    • Protein resistance of surfaces prepared by sorption of end-thiolated poly(ethylene glycol) to gold: effect of surface chain density
    • Unsworth L.D., Sheardown H., Brash J.L. Protein resistance of surfaces prepared by sorption of end-thiolated poly(ethylene glycol) to gold: effect of surface chain density. Langmuir 2005, 21:1036-1041.
    • (2005) Langmuir , vol.21 , pp. 1036-1041
    • Unsworth, L.D.1    Sheardown, H.2    Brash, J.L.3
  • 59
    • 0034939970 scopus 로고    scopus 로고
    • Modification of gold surface by grafting of poly(ethylene glycol) for reduction in protein adsorption and platelet adhesion
    • Zhang F., Kang E.T., Neoh K.G., Huang W. Modification of gold surface by grafting of poly(ethylene glycol) for reduction in protein adsorption and platelet adhesion. J. Biomater. Sci. Polymer Ed. 2001, 12:515-531.
    • (2001) J. Biomater. Sci. Polymer Ed. , vol.12 , pp. 515-531
    • Zhang, F.1    Kang, E.T.2    Neoh, K.G.3    Huang, W.4
  • 61
    • 77954387024 scopus 로고    scopus 로고
    • Effect of swelling of poly(vinyl alcohol) layers on complement activation
    • Arima Y., Kawagoe M., Furuta M., Toda M., Iwata H. Effect of swelling of poly(vinyl alcohol) layers on complement activation. Biomaterials 2010, 31:6926-6933.
    • (2010) Biomaterials , vol.31 , pp. 6926-6933
    • Arima, Y.1    Kawagoe, M.2    Furuta, M.3    Toda, M.4    Iwata, H.5
  • 62
    • 66749098938 scopus 로고    scopus 로고
    • Adsorption of pluronic F-127 on surfaces with different hydrophobicities probed by quartz crystal microbalance with dissipation
    • Nejadnik M.R., Olsson A.L.J., Sharma P.K., van der Mei H.C., Norde W., Busscher H.J. Adsorption of pluronic F-127 on surfaces with different hydrophobicities probed by quartz crystal microbalance with dissipation. Langmuir 2009, 25:6245-6249.
    • (2009) Langmuir , vol.25 , pp. 6245-6249
    • Nejadnik, M.R.1    Olsson, A.L.J.2    Sharma, P.K.3    van der Mei, H.C.4    Norde, W.5    Busscher, H.J.6
  • 63
    • 0027559885 scopus 로고
    • Principles of biosensing with an extended coupling matrix and surface plasmon resonance
    • Liedberg B., Lundström I., Stenberg E. Principles of biosensing with an extended coupling matrix and surface plasmon resonance. Sens. Actuators B 1993, 11:63-72.
    • (1993) Sens. Actuators B , vol.11 , pp. 63-72
    • Liedberg, B.1    Lundström, I.2    Stenberg, E.3
  • 64
    • 4143064685 scopus 로고    scopus 로고
    • Simple method for preparation of ultra-thin poly(N-isopropylacrylamide) hydrogel layers and characterization of their thermo-responsive properties
    • Hirata I., Okazaki M., Iwata H. Simple method for preparation of ultra-thin poly(N-isopropylacrylamide) hydrogel layers and characterization of their thermo-responsive properties. Polymer 2004, 45:5569-5578.
    • (2004) Polymer , vol.45 , pp. 5569-5578
    • Hirata, I.1    Okazaki, M.2    Iwata, H.3
  • 65
    • 33646359426 scopus 로고    scopus 로고
    • Formation of solid-supported lipid bilayer: an integrated view
    • Richter R.P., Bérat R., Brisson A.R. Formation of solid-supported lipid bilayer: an integrated view. Langmuir 2006, 22:3497-3505.
    • (2006) Langmuir , vol.22 , pp. 3497-3505
    • Richter, R.P.1    Bérat, R.2    Brisson, A.R.3
  • 66
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • Tanaka M., Sachmann E. Polymer-supported membranes as models of the cell surface. Nature 2005, 437:656-663.
    • (2005) Nature , vol.437 , pp. 656-663
    • Tanaka, M.1    Sachmann, E.2
  • 68
  • 69
    • 77955917251 scopus 로고    scopus 로고
    • Complement activation on degraded polyethylene glycol-covered surface
    • Toda M., Arima Y., Iwata H. Complement activation on degraded polyethylene glycol-covered surface. Acta Biomater. 2010, 6:2642-2649.
    • (2010) Acta Biomater. , vol.6 , pp. 2642-2649
    • Toda, M.1    Arima, Y.2    Iwata, H.3
  • 70
    • 77953718601 scopus 로고    scopus 로고
    • Effects of hydrophobicity and electrostatic charge on complement activation by amino groups
    • Toda M., Iwata H. Effects of hydrophobicity and electrostatic charge on complement activation by amino groups. ACS Appl. Mater. Interfaces 2010, 2:1107-1113.
    • (2010) ACS Appl. Mater. Interfaces , vol.2 , pp. 1107-1113
    • Toda, M.1    Iwata, H.2
  • 71
    • 0037210289 scopus 로고    scopus 로고
    • Compstatin, a peptide inhibitor of complement, exhibits species-specific binding to complement component C3
    • Sahu A., Morikis D., Lambris J.D. Compstatin, a peptide inhibitor of complement, exhibits species-specific binding to complement component C3. Mol. Immunol. 2003, 39:557-566.
    • (2003) Mol. Immunol. , vol.39 , pp. 557-566
    • Sahu, A.1    Morikis, D.2    Lambris, J.D.3
  • 72
    • 0032170593 scopus 로고    scopus 로고
    • Compstatin inhibits complement and cellular activation in whole blood in two models of extracorporeal circulation
    • Nilsson B., Larsson R., Hong J., Elgue G., Ekdahl K.N., Sahu A., Lambris J.D. Compstatin inhibits complement and cellular activation in whole blood in two models of extracorporeal circulation. Blood 1998, 92:1661-1667.
    • (1998) Blood , vol.92 , pp. 1661-1667
    • Nilsson, B.1    Larsson, R.2    Hong, J.3    Elgue, G.4    Ekdahl, K.N.5    Sahu, A.6    Lambris, J.D.7
  • 73
    • 0030013492 scopus 로고    scopus 로고
    • Inhibition of human complement by a C3-binding peptide isolated from a phage-displayed random peptide library
    • Sahu A., Kay B.K., Lambris J.D. Inhibition of human complement by a C3-binding peptide isolated from a phage-displayed random peptide library. J. Immunol. 1996, 157:884-891.
    • (1996) J. Immunol. , vol.157 , pp. 884-891
    • Sahu, A.1    Kay, B.K.2    Lambris, J.D.3
  • 74
    • 0034874856 scopus 로고    scopus 로고
    • Deposition of C3b/iC3b leads to the concealment of antigens, immunoglobulins and bound C1q in complement-activating immune complexes
    • Nilsson U.R. Deposition of C3b/iC3b leads to the concealment of antigens, immunoglobulins and bound C1q in complement-activating immune complexes. Mol. Immunol. 2001, 38:151-160.
    • (2001) Mol. Immunol. , vol.38 , pp. 151-160
    • Nilsson, U.R.1
  • 75
    • 33645815708 scopus 로고    scopus 로고
    • Injection of PEGylated liposomes in rats elicits PEG-specific IgM, which is responsible for rapid elimination of a second dose of PEGylated liposomes
    • Ishida T., Ichihara M., Wang X., Yamamoto K., Kimura J., Majima E., Kiwada H. Injection of PEGylated liposomes in rats elicits PEG-specific IgM, which is responsible for rapid elimination of a second dose of PEGylated liposomes. J. Control. Release 2006, 112:15-25.
    • (2006) J. Control. Release , vol.112 , pp. 15-25
    • Ishida, T.1    Ichihara, M.2    Wang, X.3    Yamamoto, K.4    Kimura, J.5    Majima, E.6    Kiwada, H.7
  • 76
    • 0018935575 scopus 로고
    • Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement
    • Pangburn M.K., Muller-Eberhard H.J. Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement. J. Exp. Med. 1980, 152:1102-1114.
    • (1980) J. Exp. Med. , vol.152 , pp. 1102-1114
    • Pangburn, M.K.1    Muller-Eberhard, H.J.2
  • 77
    • 0020974251 scopus 로고
    • The covalent binding reaction of C3 and C4
    • Law S.K.A. The covalent binding reaction of C3 and C4. Ann. NY Acad. Sci. 1983, 421:246-258.
    • (1983) Ann. NY Acad. Sci. , vol.421 , pp. 246-258
    • Law, S.K.A.1
  • 78
    • 0020974254 scopus 로고
    • Autolytic fragmentation of complement components C3 and C4 and its relationship to covalent binding activity
    • Sim R.B., Sim E. Autolytic fragmentation of complement components C3 and C4 and its relationship to covalent binding activity. Ann. NY Acad. Sci. 1983, 421:259-276.
    • (1983) Ann. NY Acad. Sci. , vol.421 , pp. 259-276
    • Sim, R.B.1    Sim, E.2
  • 79
    • 0026124772 scopus 로고
    • The therapeutic values of poly(ethylene glycol)-modified proteins
    • Nucci M.L., Shorr D., Abuchowski A. The therapeutic values of poly(ethylene glycol)-modified proteins. Adv. Drug Deliv. Rev. 1991, 6:133-151.
    • (1991) Adv. Drug Deliv. Rev. , vol.6 , pp. 133-151
    • Nucci, M.L.1    Shorr, D.2    Abuchowski, A.3
  • 80
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris J.M., Chess R.B. Effect of PEGylation on pharmaceuticals. Nat. Rev. Drug Discov. 2003, 2:214-221.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 81
    • 0038387390 scopus 로고    scopus 로고
    • The dawning era of polymer therapeutics
    • Duncan R. The dawning era of polymer therapeutics. Nat. Rev. Drug Discov. 2003, 2:347-360.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 347-360
    • Duncan, R.1
  • 83
    • 0009884148 scopus 로고    scopus 로고
    • Liposomal and lipid-based formulations of amphotericin B
    • de Marie S. Liposomal and lipid-based formulations of amphotericin B. Leukemia 1996, 10:S93-S96.
    • (1996) Leukemia , vol.10
    • de Marie, S.1
  • 84
    • 0030696871 scopus 로고    scopus 로고
    • Safety aspects of pegylated liposomal doxorubicin in patients with cancer
    • Alberts D.S., Garcia D.J. Safety aspects of pegylated liposomal doxorubicin in patients with cancer. Drugs 1997, S4:30-45.
    • (1997) Drugs , vol.S4 , pp. 30-45
    • Alberts, D.S.1    Garcia, D.J.2
  • 85
    • 0031886983 scopus 로고    scopus 로고
    • Doxil
    • Skubitz K.M., Skubitz A.P. Mechanism of transient dyspnea induced by pegylated-liposomal doxorubicin. Anticancer Drugs 1998, 9:45-50.
    • (1998) Anticancer Drugs , vol.9 , pp. 45-50
    • Skubitz, K.M.1    Skubitz, A.P.2
  • 87
    • 0141927263 scopus 로고    scopus 로고
    • Stealth liposomes and long circulating nanoparticles: critical issues in pharmacokinetics, opsonization and protein-binding properties
    • Moghimi S.M., Szebeni J. Stealth liposomes and long circulating nanoparticles: critical issues in pharmacokinetics, opsonization and protein-binding properties. Prog. Lipid Res. 2003, 42:463-478.
    • (2003) Prog. Lipid Res. , vol.42 , pp. 463-478
    • Moghimi, S.M.1    Szebeni, J.2
  • 89
    • 33646384586 scopus 로고    scopus 로고
    • Parameters influencing the stealthiness of colloidal drug delivery system
    • Vonarbourg A., Passirani C., Saulnier P., Benoit J.P. Parameters influencing the stealthiness of colloidal drug delivery system. Biomaterials 2006, 27:4356-4373.
    • (2006) Biomaterials , vol.27 , pp. 4356-4373
    • Vonarbourg, A.1    Passirani, C.2    Saulnier, P.3    Benoit, J.P.4
  • 90
    • 36048980533 scopus 로고    scopus 로고
    • Complement activation on surfaces modified with ethylene glycol units
    • Arima Y., Toda M., Iwata H. Complement activation on surfaces modified with ethylene glycol units. Biomaterials 2008, 29:551-560.
    • (2008) Biomaterials , vol.29 , pp. 551-560
    • Arima, Y.1    Toda, M.2    Iwata, H.3
  • 91
    • 0002754017 scopus 로고
    • Formation of self-assembled monolayers by chemisorption of derivatives of oligo(ethylene glycol) of structure HS(CH2)11OCH2CH2)mOH on gold
    • Pale-Grosdemange C., Simon E.S., Prime K.L., Whitesides G.M. Formation of self-assembled monolayers by chemisorption of derivatives of oligo(ethylene glycol) of structure HS(CH2)11OCH2CH2)mOH on gold. J. Am. Chem. Soc. 1991, 113:12-20.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 12-20
    • Pale-Grosdemange, C.1    Simon, E.S.2    Prime, K.L.3    Whitesides, G.M.4
  • 92
    • 12044254336 scopus 로고
    • Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide): A model system using self-assembled monolayers
    • Prime K.L., Whitesides G.M. Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide): A model system using self-assembled monolayers. J. Am. Chem. Soc. 1993, 115:10714-10721.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 10714-10721
    • Prime, K.L.1    Whitesides, G.M.2
  • 93
    • 28844488494 scopus 로고    scopus 로고
    • Opsonization, biodistribution, and pharmacokinetics of polymeric nanoparticles
    • Owens D.E., Peppas N.A. Opsonization, biodistribution, and pharmacokinetics of polymeric nanoparticles. Int. J. Pharm. 2006, 307:93-102.
    • (2006) Int. J. Pharm. , vol.307 , pp. 93-102
    • Owens, D.E.1    Peppas, N.A.2
  • 94
    • 3042857054 scopus 로고    scopus 로고
    • A 13C NMR study of the products and mechanism of the thermal oxidative degradation of poly(ethylene oxide)
    • Mkhatresh O.A., Heatley F. A 13C NMR study of the products and mechanism of the thermal oxidative degradation of poly(ethylene oxide). Macromol. Chem. Phys. 2002, 203:2273-2280.
    • (2002) Macromol. Chem. Phys. , vol.203 , pp. 2273-2280
    • Mkhatresh, O.A.1    Heatley, F.2
  • 95
    • 0028303633 scopus 로고
    • Human complement activation by polygeline and dextran 70
    • Videm V., Mollens T.E. Human complement activation by polygeline and dextran 70. Scand. J. Immunol. 1994, 39:314-320.
    • (1994) Scand. J. Immunol. , vol.39 , pp. 314-320
    • Videm, V.1    Mollens, T.E.2
  • 96
    • 0023694079 scopus 로고
    • The ability of Sephadex to activate human-complement is suppressed in specifically substituted functional sephadex derivatives
    • Carreno M.P., Labarre D., Jozefowicz M., Kazatchkine M.D. The ability of Sephadex to activate human-complement is suppressed in specifically substituted functional sephadex derivatives. Mol. Immunol. 1988, 5:165-171.
    • (1988) Mol. Immunol. , vol.5 , pp. 165-171
    • Carreno, M.P.1    Labarre, D.2    Jozefowicz, M.3    Kazatchkine, M.D.4
  • 97
    • 0032536028 scopus 로고    scopus 로고
    • Interactions of nanoparticles bearing heparin or dextran covalently bound to poly(methyl methacrylate) with the complement system
    • Passirani C., Barratt G., Devissaguet J.P., Labarre D. Interactions of nanoparticles bearing heparin or dextran covalently bound to poly(methyl methacrylate) with the complement system. Life Sci. 1998, 62:775-785.
    • (1998) Life Sci. , vol.62 , pp. 775-785
    • Passirani, C.1    Barratt, G.2    Devissaguet, J.P.3    Labarre, D.4
  • 98
    • 0030849130 scopus 로고    scopus 로고
    • Complement concumption by poly(ethylene glycol) in different conformations chemically coupled to poly(isobutyl 2-cyanoacrylate) nanoparticles
    • Peracchia M.T., Vauthier C., Passirani C., Couvreur P., Labarre D. Complement concumption by poly(ethylene glycol) in different conformations chemically coupled to poly(isobutyl 2-cyanoacrylate) nanoparticles. Life Sci. 1997, 61:749-761.
    • (1997) Life Sci. , vol.61 , pp. 749-761
    • Peracchia, M.T.1    Vauthier, C.2    Passirani, C.3    Couvreur, P.4    Labarre, D.5
  • 99
    • 78649538085 scopus 로고    scopus 로고
    • Distinct polymer architecture mediates switching of complement activation pathways at the nanosphere-serum interface: implications for stealth nanoparticle engineering
    • Hamad I., Al-Hanbali O., Hunter A.C., Rutt K.J., Andresen T.L., Moghimi S.M. Distinct polymer architecture mediates switching of complement activation pathways at the nanosphere-serum interface: implications for stealth nanoparticle engineering. ACS Nano 2010, 4:6629-6638.
    • (2010) ACS Nano , vol.4 , pp. 6629-6638
    • Hamad, I.1    Al-Hanbali, O.2    Hunter, A.C.3    Rutt, K.J.4    Andresen, T.L.5    Moghimi, S.M.6
  • 101
    • 33750859976 scopus 로고    scopus 로고
    • Structure of C3b reveals conformational changes that underlie complement activity
    • Janssen B.J.C., Christodoulidou A., McCarthy A., Lambris J.D., Gros P. Structure of C3b reveals conformational changes that underlie complement activity. Nature 2006, 444:213-216.
    • (2006) Nature , vol.444 , pp. 213-216
    • Janssen, B.J.C.1    Christodoulidou, A.2    McCarthy, A.3    Lambris, J.D.4    Gros, P.5
  • 103
    • 58849109079 scopus 로고    scopus 로고
    • 3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase
    • Torreira E., Tortajada A., Montes T., de Córdoba S.R., Llorca O. 3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase. Proc. Natl. Acad. Sci. USA 2009, 106:882-887.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 882-887
    • Torreira, E.1    Tortajada, A.2    Montes, T.3    de Córdoba, S.R.4    Llorca, O.5
  • 104
    • 67649230210 scopus 로고    scopus 로고
    • Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
    • Wu J., Wu Y.Q., Ricklin D., Janssen B.J.C., Lambris J.D., Gros P. Structure of complement fragment C3b-factor H and implications for host protection by complement regulators. Nat. Immunol. 2009, 10:728-733.
    • (2009) Nat. Immunol. , vol.10 , pp. 728-733
    • Wu, J.1    Wu, Y.Q.2    Ricklin, D.3    Janssen, B.J.C.4    Lambris, J.D.5    Gros, P.6
  • 105
    • 78650638514 scopus 로고    scopus 로고
    • Structures of C3b in complex with factors B and D give insight into complement convertase formation
    • Forneris F., Ricklin D., Wu J., Tzekou A., Wallace R.S., Lambris J.D., Gros P. Structures of C3b in complex with factors B and D give insight into complement convertase formation. Science 2010, 330:1816-1820.
    • (2010) Science , vol.330 , pp. 1816-1820
    • Forneris, F.1    Ricklin, D.2    Wu, J.3    Tzekou, A.4    Wallace, R.S.5    Lambris, J.D.6    Gros, P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.