메뉴 건너뛰기




Volumn 43, Issue 2-3, 2000, Pages 101-164

Endogenous carriers and ligands in non-immunogenic site-specific drug delivery

Author keywords

Bio ligand; Endogenous; Receptor; Serum component; Site specificity; Targeting

Indexed keywords

CYTOLOGY; IMMUNOLOGY;

EID: 0034734960     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-409X(00)00067-3     Document Type: Article
Times cited : (87)

References (277)
  • 1
    • 0026541171 scopus 로고
    • Serum opsonins and liposomes: Their interaction and opsonophagocytosis
    • Patel H.M. Serum opsonins and liposomes: their interaction and opsonophagocytosis. Crit. Rev. Ther. Drug Carrier Syst. 9:1992;39-90.
    • (1992) Crit. Rev. Ther. Drug Carrier Syst. , vol.9 , pp. 39-90
    • Patel, H.M.1
  • 2
    • 0032496713 scopus 로고    scopus 로고
    • Serum-mediated recognition of liposomes by phagocytic cells of the reticuloendothelial system - The concept of tissue specificity
    • Moghimi S.M., Patel H.M. Serum-mediated recognition of liposomes by phagocytic cells of the reticuloendothelial system - the concept of tissue specificity. Adv. Drug Deliv. Rev. 32:1998;45-60.
    • (1998) Adv. Drug Deliv. Rev. , vol.32 , pp. 45-60
    • Moghimi, S.M.1    Patel, H.M.2
  • 3
    • 0032883199 scopus 로고    scopus 로고
    • Mechanism of hepatic disposition of polystyrene microspheres in rats: Effects of serum depend on the size of microspheres
    • Ogawara K., Yoshida M., Kubo J., Mnishikawa M., Takakura Y., Hashida M., Higaki K., Kimura T. Mechanism of hepatic disposition of polystyrene microspheres in rats: effects of serum depend on the size of microspheres. J. Control. Release. 61:1999;241-250.
    • (1999) J. Control. Release , vol.61 , pp. 241-250
    • Ogawara, K.1    Yoshida, M.2    Kubo, J.3    Mnishikawa, M.4    Takakura, Y.5    Hashida, M.6    Higaki, K.7    Kimura, T.8
  • 5
    • 0022977108 scopus 로고
    • Regulation of interleukin-2 receptor expression and receptor release
    • Diamantstein T., Osawa H., Mouzaki A., Josimovic A.O. Regulation of interleukin-2 receptor expression and receptor release. Mol. Immunol. 23:1986;1165-1167.
    • (1986) Mol. Immunol. , vol.23 , pp. 1165-1167
    • Diamantstein, T.1    Osawa, H.2    Mouzaki, A.3    Josimovic, A.O.4
  • 6
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown M.S., Goldstein J.L. A receptor-mediated pathway for cholesterol homeostasis. Science. 232:1986;34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 7
    • 0028416238 scopus 로고
    • Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis
    • Wagner E., Curiel D., Cotton M. Delivery of drugs, proteins and genes into cells using transferrin as a ligand for receptor-mediated endocytosis. Adv. Drug Deliv. Rev. 14:1994;113-135.
    • (1994) Adv. Drug Deliv. Rev. , vol.14 , pp. 113-135
    • Wagner, E.1    Curiel, D.2    Cotton, M.3
  • 8
    • 0028069487 scopus 로고
    • In vitro and in vivo evidence for the role of HDL in reverse cholesterol transport
    • Pieters M.N., Schouten D., Van Berkel Th.J. In vitro and in vivo evidence for the role of HDL in reverse cholesterol transport. Biochim. Biophys. Acta. 1225:1994;125-134.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 125-134
    • Pieters, M.N.1    Schouten, D.2    Van Berkel, T.J.3
  • 10
    • 0028416237 scopus 로고
    • Targeting of drugs to various blood cell using (neo)-glycoproteins, antibodies and other protein carriers
    • Molema G., Meijer D.K.F. Targeting of drugs to various blood cell using (neo)-glycoproteins, antibodies and other protein carriers. Adv. Drug Deliv. Rev. 14:1994;25-50.
    • (1994) Adv. Drug Deliv. Rev. , vol.14 , pp. 25-50
    • Molema, G.1    Meijer, D.K.F.2
  • 11
    • 0031054009 scopus 로고    scopus 로고
    • Utilization of endogenous cellular transport system for the delivery of therapeutic across the blood-brain barrier
    • Friden P.M. Utilization of endogenous cellular transport system for the delivery of therapeutic across the blood-brain barrier. J. Control. Release. 46:1996;117-128.
    • (1996) J. Control. Release , vol.46 , pp. 117-128
    • Friden, P.M.1
  • 13
    • 0020583164 scopus 로고
    • Inhibition of phagocytosis by erythrocyte membrane sialoglycoprotein on target liposomes
    • Utsumi S., Shinomiya H., Minami J., Sonoda S. Inhibition of phagocytosis by erythrocyte membrane sialoglycoprotein on target liposomes. Immunology. 49:1983;113-120.
    • (1983) Immunology , vol.49 , pp. 113-120
    • Utsumi, S.1    Shinomiya, H.2    Minami, J.3    Sonoda, S.4
  • 15
    • 0342548967 scopus 로고    scopus 로고
    • S.P. Vyas, & V.K. Dixit. New Delhi: CBS
    • Vyas S.P., Dixit V.K. Pharmaceutical Biotechnology. 1st Edition:1998;395-396 CBS, New Delhi.
    • (1998) Pharmaceutical Biotechnology 1st Edition , pp. 395-396
  • 16
    • 0025096258 scopus 로고
    • Native and modified lipoproteins as drug delivery systems
    • Bijsterbosch M.K., van Berkel T.J. Native and modified lipoproteins as drug delivery systems. Adv. Drug Deliv. Rev. 5:1990;231-251.
    • (1990) Adv. Drug Deliv. Rev. , vol.5 , pp. 231-251
    • Bijsterbosch, M.K.1    Van Berkel, T.J.2
  • 17
    • 0030046514 scopus 로고    scopus 로고
    • Endocytosis of GPI-linked membrane folate receptor-alpha
    • Rijnboutt S., Jansen G., Strous G.J. Endocytosis of GPI-linked membrane folate receptor-alpha. J. Cell Biol. 132:1996;35.
    • (1996) J. Cell Biol. , vol.132 , pp. 35
    • Rijnboutt, S.1    Jansen, G.2    Strous, G.J.3
  • 18
    • 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. 142:1991;149-158.
    • (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
  • 19
    • 0026118420 scopus 로고
    • Protein-surface interactions in the presence of polyethylene oxide. II. Effect of protein size
    • Jeon S.I., Lee J.H., Andrade J.D. Protein-surface interactions in the presence of polyethylene oxide. II. Effect of protein size. J. Colloid Interface Sci. 142:1991;159-166.
    • (1991) J. Colloid Interface Sci. , vol.142 , pp. 159-166
    • Jeon, S.I.1    Lee, J.H.2    Andrade, J.D.3
  • 20
    • 0025759230 scopus 로고
    • Use of an anti-horseradish peroxidase antibody gold complex in the ABC technique
    • Gee B., Warhol M.J., Roth J. Use of an anti-horseradish peroxidase antibody gold complex in the ABC technique. J. Histochem. Cytochem. 39:1991;863-867.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 863-867
    • Gee, B.1    Warhol, M.J.2    Roth, J.3
  • 21
    • 0029964003 scopus 로고    scopus 로고
    • Cells involved in removing liposomes from the blood circulation: Why are they so special?
    • Scherphof G.L., Crommellin D.J.A. Cells involved in removing liposomes from the blood circulation: why are they so special? J. Liposome Res. 6:1996;19-31.
    • (1996) J. Liposome Res. , vol.6 , pp. 19-31
    • Scherphof, G.L.1    Crommellin, D.J.A.2
  • 22
    • 0032937301 scopus 로고    scopus 로고
    • In vitro binding of HAS, IgG and HDL on liposomes of different composition and its correlation with the BLOOD/RES ratio of liposomes
    • Panagi Z., Avgoustakis K., Evangelatos G., Ithakissios D.S. In vitro binding of HAS, IgG and HDL on liposomes of different composition and its correlation with the BLOOD/RES ratio of liposomes. Int. J. Pharm. 176:1999;203-207.
    • (1999) Int. J. Pharm. , vol.176 , pp. 203-207
    • Panagi, Z.1    Avgoustakis, K.2    Evangelatos, G.3    Ithakissios, D.S.4
  • 23
    • 0020420111 scopus 로고
    • Particle-size inter-conversion of human low-density lipoproteins during incubation of plasma with phosphatidylcholine vesicles
    • Shahrokh Z., Nichols A.V. Particle-size inter-conversion of human low-density lipoproteins during incubation of plasma with phosphatidylcholine vesicles. Biochem. Biophys. Res. Commun. 108:1982;888.
    • (1982) Biochem. Biophys. Res. Commun. , vol.108 , pp. 888
    • Shahrokh, Z.1    Nichols, A.V.2
  • 24
    • 0025325963 scopus 로고
    • Serum-induced leakage of negatively charged liposomes at nanomolar lipid concentrations
    • Comisky S.J., Heath T.D. Serum-induced leakage of negatively charged liposomes at nanomolar lipid concentrations. Biochemistry. 29:1990;3636.
    • (1990) Biochemistry , vol.29 , pp. 3636
    • Comisky, S.J.1    Heath, T.D.2
  • 25
    • 0022725695 scopus 로고
    • Interaction of liposomes with serum proteins
    • Bonte F., Juliano R.L. Interaction of liposomes with serum proteins. Chem. Phys. Lipids. 40:1986;359-372.
    • (1986) Chem. Phys. Lipids , vol.40 , pp. 359-372
    • Bonte, F.1    Juliano, R.L.2
  • 26
    • 0022928009 scopus 로고
    • Opsonins and dysopsonins: An overview
    • Absolom D.R. Opsonins and dysopsonins: an overview. Methods Enzymol. 132:1986;281-318.
    • (1986) Methods Enzymol. , vol.132 , pp. 281-318
    • Absolom, D.R.1
  • 27
    • 0024423093 scopus 로고
    • Differential properties of organ-specific serum opsonins for liver and spleen macrophages
    • Moghimi S.M., Patel H.M. Differential properties of organ-specific serum opsonins for liver and spleen macrophages. Biochim. Biophys. Acta. 984:1989;379-383.
    • (1989) Biochim. Biophys. Acta , vol.984 , pp. 379-383
    • Moghimi, S.M.1    Patel, H.M.2
  • 28
    • 0003652832 scopus 로고
    • Monolithiac albumin particles as drug carrier systems
    • L. Illum, & S.S. Davis. Bristol: Wright
    • Tomlinson E., Burger J.J. Monolithiac albumin particles as drug carrier systems. Illum L., Davis S.S. Polymers in Controlled Drug Delivery. 1987;25-48 Wright, Bristol.
    • (1987) Polymers in Controlled Drug Delivery , pp. 25-48
    • Tomlinson, E.1    Burger, J.J.2
  • 29
    • 0027491769 scopus 로고
    • Coating particles with a block co-polymer (poloxamine-908) suppresses opsonization but permits the activity of dysopsonins in the serum
    • Moghimi S.M., Muir I.S., Illum L., Davis S.S., Kolb-Bachofen V. Coating particles with a block co-polymer (poloxamine-908) suppresses opsonization but permits the activity of dysopsonins in the serum. Biochim. Biophys. Acta. 1179:1993;157-165.
    • (1993) Biochim. Biophys. Acta , vol.1179 , pp. 157-165
    • Moghimi, S.M.1    Muir, I.S.2    Illum, L.3    Davis, S.S.4    Kolb-Bachofen, V.5
  • 30
    • 0024557781 scopus 로고
    • Effect of apo-lipoproteins A-IV and A-I on the uptake of phospholipid liposomes by hepatocytes
    • Bisgaier C.L., Siebenkas M.V., Williams K.J. Effect of apo-lipoproteins A-IV and A-I on the uptake of phospholipid liposomes by hepatocytes. J. Biol. Chem. 264:1989;862.
    • (1989) J. Biol. Chem. , vol.264 , pp. 862
    • Bisgaier, C.L.1    Siebenkas, M.V.2    Williams, K.J.3
  • 31
    • 0019836446 scopus 로고
    • Tuftsin, Thr-Lys-Pro-Arg. Anatomy of an immunologically active peptide
    • Fridkin M., Gottlieb P. Tuftsin, Thr-Lys-Pro-Arg. Anatomy of an immunologically active peptide. Mol. Cell. Biochem. 41:1981;73-97.
    • (1981) Mol. Cell. Biochem. , vol.41 , pp. 73-97
    • Fridkin, M.1    Gottlieb, P.2
  • 32
    • 0028241288 scopus 로고
    • Opsonic effect of globulins on phagocytosis of liposomes by bone marrow cells
    • Bumrah R., Patel H.M. Opsonic effect of globulins on phagocytosis of liposomes by bone marrow cells. Biochem. Soc. Trans. 22:1994;86S.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 86S
    • Bumrah, R.1    Patel, H.M.2
  • 34
    • 0031051814 scopus 로고    scopus 로고
    • Influence of fluorescent labelling of polystyrene particles on phagocytic uptake, surface hydrophilicity, and plasma protein adsorption
    • Muller R.H., Ruhl D., Luck M., Paulke B.R. Influence of fluorescent labelling of polystyrene particles on phagocytic uptake, surface hydrophilicity, and plasma protein adsorption. Pharm. Res. 14:1997;18-24.
    • (1997) Pharm. Res. , vol.14 , pp. 18-24
    • Muller, R.H.1    Ruhl, D.2    Luck, M.3    Paulke, B.R.4
  • 37
    • 0032485414 scopus 로고    scopus 로고
    • Analysis of plasma protein adsorption on polymeric nanoparticles with different surface characteristics
    • Luck M., Paulke B.R., Sebroder W., Blunk T., Muller R.H. Analysis of plasma protein adsorption on polymeric nanoparticles with different surface characteristics. J. Biomed. Mater. Res. 39:1998;478-485.
    • (1998) J. Biomed. Mater. Res. , vol.39 , pp. 478-485
    • Luck, M.1    Paulke, B.R.2    Sebroder, W.3    Blunk, T.4    Muller, R.H.5
  • 38
    • 0344500892 scopus 로고    scopus 로고
    • Complement activation by model drug carriers for intravenous application: Determination by two-dimensional electrophoresis
    • Luck M., Schroder W., Paulke B.R., Blunk T., Muller R.H. Complement activation by model drug carriers for intravenous application: determination by two-dimensional electrophoresis. Biomaterials. 20:1999;2063-2068.
    • (1999) Biomaterials , vol.20 , pp. 2063-2068
    • Luck, M.1    Schroder, W.2    Paulke, B.R.3    Blunk, T.4    Muller, R.H.5
  • 39
    • 0021455525 scopus 로고
    • Equilibrium adsorption of human serum albumin and human fibrinogen on hydrophobic and hydrophilic surfaces
    • Brynda E., Cepalova N.A., Stol M. Equilibrium adsorption of human serum albumin and human fibrinogen on hydrophobic and hydrophilic surfaces. Biomed. Mater. Res. 18:1984;685-693.
    • (1984) Biomed. Mater. Res. , vol.18 , pp. 685-693
    • Brynda, E.1    Cepalova, N.A.2    Stol, M.3
  • 40
    • 0032845157 scopus 로고    scopus 로고
    • Interaction of polystyrene microspheres with liver cells: Roles of membrane receptors and serum proteins
    • Ogawara K., Yoshida M., Takakura Y., Hashida M., Higaki K., Kimura T. Interaction of polystyrene microspheres with liver cells: roles of membrane receptors and serum proteins. Biochim. Biophys. Acta. 1472:1999;165-172.
    • (1999) Biochim. Biophys. Acta , vol.1472 , pp. 165-172
    • Ogawara, K.1    Yoshida, M.2    Takakura, Y.3    Hashida, M.4    Higaki, K.5    Kimura, T.6
  • 41
    • 0030874980 scopus 로고    scopus 로고
    • Recent developments in medical applications of liposomes: Sterically stabilized liposomes in cancer therapy and gene delivery in vivo
    • Lasic D.D. Recent developments in medical applications of liposomes: sterically stabilized liposomes in cancer therapy and gene delivery in vivo. J. Control. Release. 48:1997;203.
    • (1997) J. Control. Release , vol.48 , pp. 203
    • Lasic, D.D.1
  • 42
    • 0032496677 scopus 로고    scopus 로고
    • Receptor versus non-receptor mediated clearance of liposomes
    • Scherphof G.L., Kamps J.A.A.M. Receptor versus non-receptor mediated clearance of liposomes. Adv. Drug Deliv. Rev. 32:1998;81-97.
    • (1998) Adv. Drug Deliv. Rev. , vol.32 , pp. 81-97
    • Scherphof, G.L.1    Kamps, J.A.A.M.2
  • 43
    • 0032439486 scopus 로고    scopus 로고
    • Folate-mediated targeting of therapeutic and imaging agents to cancers
    • Reddy J.A., Low P.S. Folate-mediated targeting of therapeutic and imaging agents to cancers. Crit. Rev. Ther. Drug Carrier Syst. 15:1998;587-627.
    • (1998) Crit. Rev. Ther. Drug Carrier Syst. , vol.15 , pp. 587-627
    • Reddy, J.A.1    Low, P.S.2
  • 44
    • 0031786789 scopus 로고    scopus 로고
    • TNF-related ligands and their receptors
    • Orlinick J.R., Chao M.V. TNF-related ligands and their receptors. Cell. Signal. 10:1998;543-551.
    • (1998) Cell. Signal. , vol.10 , pp. 543-551
    • Orlinick, J.R.1    Chao, M.V.2
  • 45
    • 0032985063 scopus 로고    scopus 로고
    • Transferrin as a targeting ligand for liposomes and anti-cancer drugs
    • Singh M. Transferrin as a targeting ligand for liposomes and anti-cancer drugs. Curr. Pharm. Des. 5:1999;443-451.
    • (1999) Curr. Pharm. Des. , vol.5 , pp. 443-451
    • Singh, M.1
  • 46
    • 0032998460 scopus 로고    scopus 로고
    • Binding of EGF peptide and EGF receptor antibodies and its fragments in different tumor models
    • Senekowitsch-Schmidtke R. Binding of EGF peptide and EGF receptor antibodies and its fragments in different tumor models. Hybridoma. 18:1999;29-35.
    • (1999) Hybridoma , vol.18 , pp. 29-35
    • Senekowitsch-Schmidtke, R.1
  • 47
    • 0028803615 scopus 로고
    • Receptor cell biology: Receptor-mediated endocytosis
    • Schwartz A.L. Receptor cell biology: receptor-mediated endocytosis. Paediatr. Res. 38:1995;835.
    • (1995) Paediatr. Res. , vol.38 , pp. 835
    • Schwartz, A.L.1
  • 48
    • 0031039539 scopus 로고    scopus 로고
    • Targeted delivery of drugs and proteins to the liver via receptor mediated endocytosis
    • Hasida M., Hirabyayashi H., Nishikawa M., Takakura Y. Targeted delivery of drugs and proteins to the liver via receptor mediated endocytosis. J. Control. Release. 46:1997;129-137.
    • (1997) J. Control. Release , vol.46 , pp. 129-137
    • Hasida, M.1    Hirabyayashi, H.2    Nishikawa, M.3    Takakura, Y.4
  • 49
    • 0345404305 scopus 로고    scopus 로고
    • Receptor-mediated targeted drug or toxin delivery
    • Rihova B. Receptor-mediated targeted drug or toxin delivery. Adv. Drug Deliv. Rev. 29:1998;273-289.
    • (1998) Adv. Drug Deliv. Rev. , vol.29 , pp. 273-289
    • Rihova, B.1
  • 50
    • 0032472885 scopus 로고    scopus 로고
    • Receptor-mediated delivery of foreign genes to hepatocytes
    • Wu G.Y., Wu C.H. Receptor-mediated delivery of foreign genes to hepatocytes. Adv. Drug Deliv. Rev. 29:1998;243-248.
    • (1998) Adv. Drug Deliv. Rev. , vol.29 , pp. 243-248
    • Wu, G.Y.1    Wu, C.H.2
  • 51
    • 0028202474 scopus 로고
    • Transepithelial transport of immunoglobulins
    • Mostov K.E. Transepithelial transport of immunoglobulins. Annu. Rev. Immunol. 12:1994;63-84.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 63-84
    • Mostov, K.E.1
  • 52
    • 0029240448 scopus 로고
    • Regulation of protein traffic in polarized epithelial cells
    • Mostov K.E., Cardone M.H. Regulation of protein traffic in polarized epithelial cells. BioEssays. 17:1995;129-138.
    • (1995) BioEssays , vol.17 , pp. 129-138
    • Mostov, K.E.1    Cardone, M.H.2
  • 53
    • 0027365343 scopus 로고
    • Gene transfer into respiratory epithelial cells by targeting the polymeric immunoglobulin receptor
    • Ferkol T., Kaetzel C.S., Davis P.B. Gene transfer into respiratory epithelial cells by targeting the polymeric immunoglobulin receptor. J. Clin. Invest. 92:1993;2394-2400.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2394-2400
    • Ferkol, T.1    Kaetzel, C.S.2    Davis, P.B.3
  • 54
    • 0029098999 scopus 로고
    • Identification and characterization of a novel protein (p. 137) which transcytoses bidirectionally in Caco-2 cells
    • Ellis J.A., Luzio J.P. Identification and characterization of a novel protein (p. 137) which transcytoses bidirectionally in Caco-2 cells. J. Biol. Chem. 270:1995;20717.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20717
    • Ellis, J.A.1    Luzio, J.P.2
  • 55
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson M.S. The role of clathrin, adaptors and dynamin in endocytosis. Curr. Opin. Cell Biol. 6:1994;538-544.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 56
    • 0027333415 scopus 로고
    • Signal-dependent membrane protein trafficking in the endocytic pathway
    • Trowbridge L.S., Collawan J.F., Hopkins C.R. Signal-dependent membrane protein trafficking in the endocytic pathway. Annu. Rev. Cell Biol. 9:1993;129-161.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 129-161
    • Trowbridge, L.S.1    Collawan, J.F.2    Hopkins, C.R.3
  • 57
    • 0029117498 scopus 로고
    • The emergence of clathrin-independent pinocytic pathways
    • Lamaze C., Schmid S.L. The emergence of clathrin-independent pinocytic pathways. Curr. Opin. Cell Biol. 7:1995;573-580.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 573-580
    • Lamaze, C.1    Schmid, S.L.2
  • 58
    • 0027415690 scopus 로고
    • Potocytosis of small molecules and ions by caveolae
    • Anderson R.G.W. Potocytosis of small molecules and ions by caveolae. Trends Cell Biol. 3:1993;69-72.
    • (1993) Trends Cell Biol. , vol.3 , pp. 69-72
    • Anderson, R.G.W.1
  • 60
    • 0028875216 scopus 로고
    • Cytoplasmic coat proteins involved in endosome function
    • Whitney J.A., Gomez M., Sheff D., Kreis T.E., Mellman I. Cytoplasmic coat proteins involved in endosome function. Cell. 83:1995;703-713.
    • (1995) Cell , vol.83 , pp. 703-713
    • Whitney, J.A.1    Gomez, M.2    Sheff, D.3    Kreis, T.E.4    Mellman, I.5
  • 61
    • 0024517745 scopus 로고
    • Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro
    • Gruenberg J., Griffiths G., Howell K.E. Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro. J. Cell Biol. 108:1989;1301.
    • (1989) J. Cell Biol. , vol.108 , pp. 1301
    • Gruenberg, J.1    Griffiths, G.2    Howell, K.E.3
  • 63
    • 0029934710 scopus 로고    scopus 로고
    • Kinetic analysis of receptor-mediated endocytosis (RME) of proteins and peptides: Use of RME as a drug delivery system
    • Kato Y., Seita T., Kuwabara T., Sugiyama Y. Kinetic analysis of receptor-mediated endocytosis (RME) of proteins and peptides: use of RME as a drug delivery system. J. Control. Release. 39:1996;191-200.
    • (1996) J. Control. Release , vol.39 , pp. 191-200
    • Kato, Y.1    Seita, T.2    Kuwabara, T.3    Sugiyama, Y.4
  • 64
    • 0024465916 scopus 로고
    • Monensin and chloroquine inhibit transfer to lysosomes of endocytosed macromolecules in cultured mouse peritoneal macrophages
    • Stenseth K., Thyberg P. Monensin and chloroquine inhibit transfer to lysosomes of endocytosed macromolecules in cultured mouse peritoneal macrophages. Eur. J. Cell Biol. 49:1989;326.
    • (1989) Eur. J. Cell Biol. , vol.49 , pp. 326
    • Stenseth, K.1    Thyberg, P.2
  • 65
    • 0021356320 scopus 로고
    • The entry of enveloped viruses into cells by endocytosis
    • Marsh M. The entry of enveloped viruses into cells by endocytosis. Biochim. J. 218:1984;110.
    • (1984) Biochim. J. , vol.218 , pp. 110
    • Marsh, M.1
  • 66
    • 0021231875 scopus 로고
    • Pseudomonas exotoxin-anti TAC: Cell specific immunotoxin active against cells expressing the human T-cell growth factor receptor
    • FitzGerald D.J., Waldmann T.A., Willingham M.C., Pastan I. Pseudomonas exotoxin-anti TAC: cell specific immunotoxin active against cells expressing the human T-cell growth factor receptor. J. Clin. Invest. 74:1984;966.
    • (1984) J. Clin. Invest. , vol.74 , pp. 966
    • Fitzgerald, D.J.1    Waldmann, T.A.2    Willingham, M.C.3    Pastan, I.4
  • 67
    • 0032472798 scopus 로고    scopus 로고
    • Molecular motors and their role in membrane traffic
    • Hamm-Alvarez S.F. Molecular motors and their role in membrane traffic. Adv. Drug Deliv. Rev. 29:1998;229-242.
    • (1998) Adv. Drug Deliv. Rev. , vol.29 , pp. 229-242
    • Hamm-Alvarez, S.F.1
  • 68
    • 0028942256 scopus 로고
    • Actin- And microtubule-dependent organelle motors: Inter-relationships between the two motility systems
    • Langford G.M. Actin- and microtubule-dependent organelle motors: inter-relationships between the two motility systems. Curr. Opin. Cell Biol. 7:1995;82.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82
    • Langford, G.M.1
  • 69
    • 0028062850 scopus 로고
    • Insulin fragments as a carrier for peptide delivery across the blood brain barrier
    • Fukuta M., Okada H., Linuma S., Yanai S., Toguchi H. Insulin fragments as a carrier for peptide delivery across the blood brain barrier. Pharm. Res. 11:1994;1681.
    • (1994) Pharm. Res. , vol.11 , pp. 1681
    • Fukuta, M.1    Okada, H.2    Linuma, S.3    Yanai, S.4    Toguchi, H.5
  • 73
    • 0028386492 scopus 로고
    • Low-density lipoprotein as a vehicle for targeting anti-tumor compounds to cancer cells
    • Firestone R.A. Low-density lipoprotein as a vehicle for targeting anti-tumor compounds to cancer cells. Bioconjugate Chem. 5:1994;105-113.
    • (1994) Bioconjugate Chem. , vol.5 , pp. 105-113
    • Firestone, R.A.1
  • 74
    • 0027742959 scopus 로고
    • Structure-function studies on selectins carbohydrate ligands. Modification to fucose, sialic acid and sulfate as a sialic acid replacement
    • Brandley B.K., Kiso M., Abbas S., Nicard P., Srivastava O., Foxall C., Oda Y., Hasegawa A. Structure-function studies on selectins carbohydrate ligands. Modification to fucose, sialic acid and sulfate as a sialic acid replacement. Glycobiology. 3:1993;633-639.
    • (1993) Glycobiology , vol.3 , pp. 633-639
    • Brandley, B.K.1    Kiso, M.2    Abbas, S.3    Nicard, P.4    Srivastava, O.5    Foxall, C.6    Oda, Y.7    Hasegawa, A.8
  • 75
    • 0028418574 scopus 로고
    • Soluble polymers for lectin-mediated targeting
    • Seymour L.W. Soluble polymers for lectin-mediated targeting. Adv. Drug Deliv. Rev. 14:1994;89.
    • (1994) Adv. Drug Deliv. Rev. , vol.14 , pp. 89
    • Seymour, L.W.1
  • 76
    • 0031042534 scopus 로고    scopus 로고
    • Tumor vascular endothelium: Barrier or target in tumor directed drug delivery and immunotherapy
    • Molema G., Lou F., de Leij F.M.H., Meijer D.K.F. Tumor vascular endothelium: barrier or target in tumor directed drug delivery and immunotherapy. Pharm. Res. 14:1997;2-10.
    • (1997) Pharm. Res. , vol.14 , pp. 2-10
    • Molema, G.1    Lou, F.2    De Leij, F.M.H.3    Meijer, D.K.F.4
  • 77
    • 0026711121 scopus 로고
    • Drug targeting for anti-viral agents: Options and limitations
    • Meijer D.K.F., Jansen R.W., Molema G. Drug targeting for anti-viral agents: options and limitations. Antiviral Res. 18:1992;215-258.
    • (1992) Antiviral Res. , vol.18 , pp. 215-258
    • Meijer, D.K.F.1    Jansen, R.W.2    Molema, G.3
  • 78
    • 0025666651 scopus 로고
    • Carbohydrate ligands of the LEC cell adhesion molecules
    • Brandley B.K., Swiedler S.J., Robbins P.W. Carbohydrate ligands of the LEC cell adhesion molecules. Cell. 63:1990;861-863.
    • (1990) Cell , vol.63 , pp. 861-863
    • Brandley, B.K.1    Swiedler, S.J.2    Robbins, P.W.3
  • 79
    • 0027234353 scopus 로고
    • Intercellular immune adhesion molecules in human liver transplants: Overview on expression patterns of leukocyte receptors and ligand molecules
    • Steinhoff G., Behrend M., Schrader B., Pichlmayr R. Intercellular immune adhesion molecules in human liver transplants: overview on expression patterns of leukocyte receptors and ligand molecules. Hepatology. 18:1993;440.
    • (1993) Hepatology , vol.18 , pp. 440
    • Steinhoff, G.1    Behrend, M.2    Schrader, B.3    Pichlmayr, R.4
  • 84
    • 0029973887 scopus 로고    scopus 로고
    • Integrin dependent signal transduction
    • Lafrenie R.M., Yamada K.M. Integrin dependent signal transduction. J. Cell. Biochem. 61:1996;543-544.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 543-544
    • Lafrenie, R.M.1    Yamada, K.M.2
  • 85
    • 0029940091 scopus 로고    scopus 로고
    • The vitronectin receptor (alpha v beta 30) as an example for the role of integrins in T lymphocyte stimulation
    • Halvorson M.J., Coligan J.E., Sturmhofel K. The vitronectin receptor (alpha v beta 30) as an example for the role of integrins in T lymphocyte stimulation. Immunol. Res. 15:1996;16-29.
    • (1996) Immunol. Res. , vol.15 , pp. 16-29
    • Halvorson, M.J.1    Coligan, J.E.2    Sturmhofel, K.3
  • 88
    • 0026445723 scopus 로고
    • Selectins - Interpreters of cell-specific carbohydrate information during inflammation
    • Lasky L.A. Selectins - Interpreters of cell-specific carbohydrate information during inflammation. Science. 258:1992;964-969.
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 89
    • 0027640355 scopus 로고
    • Antigen processing and intracellular traffic of antigen and MHC molecules
    • Harding C.V., Gueze H.J. Antigen processing and intracellular traffic of antigen and MHC molecules. Curr. Opin. Cell Biol. 5:1993;596-605.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 596-605
    • Harding, C.V.1    Gueze, H.J.2
  • 91
    • 0023266203 scopus 로고
    • Regulation of insulin receptor internalization in vascular endothelial cells by insulin and phorbol ester
    • Hachia H.L., Takayama S., White M.F., King G.L. Regulation of insulin receptor internalization in vascular endothelial cells by insulin and phorbol ester. J. Biol. Chem. 262:1987;6417.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6417
    • Hachia, H.L.1    Takayama, S.2    White, M.F.3    King, G.L.4
  • 92
    • 0032482978 scopus 로고    scopus 로고
    • Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice
    • Hiratsuka S., Minowa O., Kuno J., Noda T., Shibuya M. Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice. Proc. Natl. Acad. Sci. USA. 94:1998;9349.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9349
    • Hiratsuka, S.1    Minowa, O.2    Kuno, J.3    Noda, T.4    Shibuya, M.5
  • 93
    • 0025302645 scopus 로고
    • Insulin-sensitive tyrosine kinase: Relationship with in vivo insulin action in humans
    • Nyomba B.L., Ossowski V.M., Bogardus C., Mott D.M. Insulin-sensitive tyrosine kinase: relationship with in vivo insulin action in humans. Am. J. Physiol. 58:1990;E964.
    • (1990) Am. J. Physiol. , vol.58 , pp. 964
    • Nyomba, B.L.1    Ossowski, V.M.2    Bogardus, C.3    Mott, D.M.4
  • 95
    • 0032472884 scopus 로고    scopus 로고
    • The biochemical and physiological characteristics of receptors
    • Feener E.P., King G.L. The biochemical and physiological characteristics of receptors. Adv. Drug Deliv. Rev. 29:1998;197-213.
    • (1998) Adv. Drug Deliv. Rev. , vol.29 , pp. 197-213
    • Feener, E.P.1    King, G.L.2
  • 97
    • 0022556083 scopus 로고
    • Isolation and characterization of apoproteins
    • J.P. Segrest, & J.J. Alka. Orlando, FL: Academic Press
    • McConathy W.J., Alaupovic P. Isolation and characterization of apoproteins. Segrest J.P., Alka J.J. Methods in Enzymology. 1986;128, 297 Academic Press, Orlando, FL.
    • (1986) Methods in Enzymology , pp. 128
    • McConathy, W.J.1    Alaupovic, P.2
  • 99
    • 0031428861 scopus 로고    scopus 로고
    • Lipoproteins: Their potential as endogenous target oriented novel drug delivery system
    • Jaitely V., Kanaujia P., Vyas S.P. Lipoproteins: their potential as endogenous target oriented novel drug delivery system. Indian J. Exp. Biol. 35:1997;212-218.
    • (1997) Indian J. Exp. Biol. , vol.35 , pp. 212-218
    • Jaitely, V.1    Kanaujia, P.2    Vyas, S.P.3
  • 100
    • 0030612230 scopus 로고    scopus 로고
    • Self-assessing supramolecular biovectors: A new dimension in novel drug delivery systems
    • Vyas S.P., Jaitely V., Kanaujia P. Self-assessing supramolecular biovectors: a new dimension in novel drug delivery systems. Pharmazie. 52:1997;259-267.
    • (1997) Pharmazie , vol.52 , pp. 259-267
    • Vyas, S.P.1    Jaitely, V.2    Kanaujia, P.3
  • 101
    • 0026722109 scopus 로고
    • A novel mechanism for achieving transgene persistence in vivo after somatic gene transfer into hepatocytes
    • Wilson J.M., Grossman M., Cabrera J.A., Wu C.H., Wu G.Y. A novel mechanism for achieving transgene persistence in vivo after somatic gene transfer into hepatocytes. J. Biol. Chem. 267:1992;11483.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11483
    • Wilson, J.M.1    Grossman, M.2    Cabrera, J.A.3    Wu, C.H.4    Wu, G.Y.5
  • 102
    • 0026502766 scopus 로고
    • Hepatocyte-directed gene transfer in vivo leads to transient improvement of hepatocholesterolemia in LDL-receptor deficient rabbits
    • Wilson J.M., Grossman M., Wu C.H., Chowdhary N.R., Wu G.Y., Chowdhary J.R. Hepatocyte-directed gene transfer in vivo leads to transient improvement of hepatocholesterolemia in LDL-receptor deficient rabbits. J. Biol. Chem. 267:1992;963.
    • (1992) J. Biol. Chem. , vol.267 , pp. 963
    • Wilson, J.M.1    Grossman, M.2    Wu, C.H.3    Chowdhary, N.R.4    Wu, G.Y.5    Chowdhary, J.R.6
  • 103
    • 0022413777 scopus 로고
    • Specific targeting of HDL to liver hepatocytes by incorporation of a Tris-galactoside terminated cholesterol derivative
    • van Berkel Th.C., Kruij K., Kempen H. Specific targeting of HDL to liver hepatocytes by incorporation of a Tris-galactoside terminated cholesterol derivative. J. Biol. Chem. 260:1985;12203-12207.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12203-12207
    • Van Berkel, T.C.1    Kruij, K.2    Kempen, H.3
  • 104
    • 0027967602 scopus 로고
    • Synthesis of the dioleoyl derivative of iododeoxyuridine and its incorporation into reconstituted high density lipoprotein particles
    • Bijsterbosch M.K., Schouten D., van Berkel Th.J. Synthesis of the dioleoyl derivative of iododeoxyuridine and its incorporation into reconstituted high density lipoprotein particles. Biochemistry. 33:1994;14073-14080.
    • (1994) Biochemistry , vol.33 , pp. 14073-14080
    • Bijsterbosch, M.K.1    Schouten, D.2    Van Berkel, T.J.3
  • 105
    • 0021987742 scopus 로고
    • Uptake of chemically modified low-density lipoproteins in vivo is mediated by specific endothelial cells
    • Pitas R.E., Boyles J., Mahley R.W. Uptake of chemically modified low-density lipoproteins in vivo is mediated by specific endothelial cells. J. Cell Biol. 100:1985;103-117.
    • (1985) J. Cell Biol. , vol.100 , pp. 103-117
    • Pitas, R.E.1    Boyles, J.2    Mahley, R.W.3
  • 107
    • 0024342122 scopus 로고
    • Acetylated low-density lipoproteins: A potential carrier for site-specific delivery of drugs to Kupffer cells
    • Bijsterbosch M.K., Ziere G.L., van Berkel Th.J. Acetylated low-density lipoproteins: a potential carrier for site-specific delivery of drugs to Kupffer cells. Mol. Pharmacol. 36:1989;484-489.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 484-489
    • Bijsterbosch, M.K.1    Ziere, G.L.2    Van Berkel, T.J.3
  • 108
    • 0025219143 scopus 로고
    • Scavenger receptor-mediated uptake and metabolism of lipid vesicles containing acidic phospholipids by mouse peritoneal macrophages
    • Nishikawa K., Arai H., Inoue K. Scavenger receptor-mediated uptake and metabolism of lipid vesicles containing acidic phospholipids by mouse peritoneal macrophages. J. Biol. Chem. 265:1990;5226-5231.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5226-5231
    • Nishikawa, K.1    Arai, H.2    Inoue, K.3
  • 109
    • 0027076731 scopus 로고
    • Role of surface glycolipids natural or synthetic origin on the biodistribution of liposomes
    • Ghosh P.C., Bachawat B.K. Role of surface glycolipids natural or synthetic origin on the biodistribution of liposomes. J. Lipid Res. 2:1992;369.
    • (1992) J. Lipid Res. , vol.2 , pp. 369
    • Ghosh, P.C.1    Bachawat, B.K.2
  • 110
    • 84991429531 scopus 로고
    • Receptor-dependent uptake of macromolecules by specific hepatic cells
    • H.E. Junginger. London: Ellis Horwood
    • Van Berkel Th.J. Receptor-dependent uptake of macromolecules by specific hepatic cells. Junginger H.E. Drug Targeting and Delivery: Concepts in Dosage Form Design. 1992;13-25 Ellis Horwood, London.
    • (1992) Drug Targeting and Delivery: Concepts in Dosage Form Design , pp. 13-25
    • Van Berkel, T.J.1
  • 111
    • 0026688618 scopus 로고
    • Evidence that the scavenger receptor is not involved in the uptake of negatively charged liposomes by cells
    • Lee K.D., Pitas R.E., Papahadjopoulos D. Evidence that the scavenger receptor is not involved in the uptake of negatively charged liposomes by cells. Biochim. Biophys. Acta. 1111:1992;1-6.
    • (1992) Biochim. Biophys. Acta , vol.1111 , pp. 1-6
    • Lee, K.D.1    Pitas, R.E.2    Papahadjopoulos, D.3
  • 112
    • 0028997232 scopus 로고
    • The class B scavenger receptor SR-B1 and CD36 are receptors for anionic phospholipids
    • Rigotti A., Acton S.L., Krieger M. The class B scavenger receptor SR-B1 and CD36 are receptors for anionic phospholipids. J. Biol. Chem. 270:1995;16221-16224.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16221-16224
    • Rigotti, A.1    Acton, S.L.2    Krieger, M.3
  • 113
    • 0030046797 scopus 로고    scopus 로고
    • Identification of scavenger receptor SR-BI as a high density lipoprotein receptor
    • Acton S., Rigotti A., Landschultz K.T., Xu S., Hobbs H.H., Krieger M. Identification of scavenger receptor SR-BI as a high density lipoprotein receptor. Science. 271:1996;518-520.
    • (1996) Science , vol.271 , pp. 518-520
    • Acton, S.1    Rigotti, A.2    Landschultz, K.T.3    Xu, S.4    Hobbs, H.H.5    Krieger, M.6
  • 114
    • 0028929744 scopus 로고
    • A macrophage receptor for oxidized low density lipoprotein distinct from the receptor for acetyl low density lipoprotein: Partial purification and role in recognition of oxidatively damaged cells
    • Ottend E., Parthasarthy S., Sambrano G.R., Ramprasad M.P., Quehenberger O., Kondratenco N., Green S., Steinberg D. A macrophage receptor for oxidized low density lipoprotein distinct from the receptor for acetyl low density lipoprotein: partial purification and role in recognition of oxidatively damaged cells. Proc. Natl. Acad. Sci. USA. 92:1995;1391-1395.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1391-1395
    • Ottend, E.1    Parthasarthy, S.2    Sambrano, G.R.3    Ramprasad, M.P.4    Quehenberger, O.5    Kondratenco, N.6    Green, S.7    Steinberg, D.8
  • 115
    • 0031777742 scopus 로고    scopus 로고
    • Glyoaldehyde-modified low density lipoprotein leads macrophages to foam cells via the macrophage scavenger receptor
    • Jinnouchi Y., Sano H., Negai R., Hakamata H., Kodama T., Suzuki H., Yoshida M., Ueda S., Horiuchi S. Glyoaldehyde-modified low density lipoprotein leads macrophages to foam cells via the macrophage scavenger receptor. J. Biochem. 123:1998;1208-1217.
    • (1998) J. Biochem. , vol.123 , pp. 1208-1217
    • Jinnouchi, Y.1    Sano, H.2    Negai, R.3    Hakamata, H.4    Kodama, T.5    Suzuki, H.6    Yoshida, M.7    Ueda, S.8    Horiuchi, S.9
  • 116
    • 0033521038 scopus 로고    scopus 로고
    • An extrahepatic receptor-associated protein-sensitive mechanism is involved in the metabolism of triglyceride-rich lipoproteins
    • van Vlijmen B.J., Rohlmann A., Page S.T., Bensadoun A., Bos J.S., van Berkel Th.J., Havekes L.M., Herz J. An extrahepatic receptor-associated protein-sensitive mechanism is involved in the metabolism of triglyceride-rich lipoproteins. J. Biol. Chem. 274:1999;35219-35226.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35219-35226
    • Van Vlijmen, B.J.1    Rohlmann, A.2    Page, S.T.3    Bensadoun, A.4    Bos, J.S.5    Van Berkel, T.J.6    Havekes, L.M.7    Herz, J.8
  • 117
    • 0029952026 scopus 로고    scopus 로고
    • Specific targeting of a lipophilic prodrug of iododeoxyuridine to parenchymal liver cells using lactosylated reconstituted high density lipoprotein particles
    • Bijsterbosch M.K., van de Bilt H., van Berkel Th.J. Specific targeting of a lipophilic prodrug of iododeoxyuridine to parenchymal liver cells using lactosylated reconstituted high density lipoprotein particles. Biochem. Pharmacol. 52:1996;113-121.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 113-121
    • Bijsterbosch, M.K.1    Van De Bilt, H.2    Van Berkel, T.J.3
  • 118
    • 0032776231 scopus 로고    scopus 로고
    • Synthesis of a lipophilic prodrug of 9-(2-phosphonylmethoxyethyl)adenine (PMEA) and its incorporation into a hepatocyte-specific lipidic carrier
    • de Vrueh R.L., Rump E.T., Sliedregt L.A., Biessen E.A., van Berkel T.J., Bijsterbosch M.K. Synthesis of a lipophilic prodrug of 9-(2-phosphonylmethoxyethyl)adenine (PMEA) and its incorporation into a hepatocyte-specific lipidic carrier. Pharm. Res. 16:1999;1179-1185.
    • (1999) Pharm. Res. , vol.16 , pp. 1179-1185
    • De Vrueh, R.L.1    Rump, E.T.2    Sliedregt, L.A.3    Biessen, E.A.4    Van Berkel, T.J.5    Bijsterbosch, M.K.6
  • 120
    • 0028153812 scopus 로고
    • Supramolecular biovectors (SMBV): A new family of nanoparticulate drug delivery systems. Synthesis and structural characterization
    • Peyrot M., Sautereau A.M., Rabanel J.M., Nguyen F., Tocanne J.F., Samain D. Supramolecular biovectors (SMBV): a new family of nanoparticulate drug delivery systems. Synthesis and structural characterization. Int. J. Pharm. 102:1994;25-33.
    • (1994) Int. J. Pharm. , vol.102 , pp. 25-33
    • Peyrot, M.1    Sautereau, A.M.2    Rabanel, J.M.3    Nguyen, F.4    Tocanne, J.F.5    Samain, D.6
  • 123
    • 0031944223 scopus 로고    scopus 로고
    • SupraMolecular BioVectors (SMBV) improve antisense inhibition of erbB-2 expression
    • Allal C., Sixou S., Kravtzoff R., Soulet N., Soula G., Favre G. SupraMolecular BioVectors (SMBV) improve antisense inhibition of erbB-2 expression. Br. J. Cancer. 77:1998;1448-1453.
    • (1998) Br. J. Cancer , vol.77 , pp. 1448-1453
    • Allal, C.1    Sixou, S.2    Kravtzoff, R.3    Soulet, N.4    Soula, G.5    Favre, G.6
  • 124
    • 0028116575 scopus 로고
    • Stabilization and enhancement of interleukin-2 in vitro bioactivity by new carriers: Supramolecular biovectors
    • Castignolles N., Betbeder D., Ioualalen K., Merten O., Leclerc C., Samain D., Penn P. Stabilization and enhancement of interleukin-2 in vitro bioactivity by new carriers: supramolecular biovectors. Vaccine. 12:1994;1413-1418.
    • (1994) Vaccine , vol.12 , pp. 1413-1418
    • Castignolles, N.1    Betbeder, D.2    Ioualalen, K.3    Merten, O.4    Leclerc, C.5    Samain, D.6    Penn, P.7
  • 125
    • 0032935589 scopus 로고    scopus 로고
    • Supramolecular biovectors: Development and characterization
    • Jaitely V., Vyas S.P. Supramolecular biovectors: development and characterization. J. Drug Targeting. 6:1999;315-322.
    • (1999) J. Drug Targeting , vol.6 , pp. 315-322
    • Jaitely, V.1    Vyas, S.P.2
  • 126
    • 0025695510 scopus 로고
    • Prolonged serum half-life of antineoplastic drugs by incorporation into low-density lipoproteins
    • de Smidt P.C., Van Berkel Th.J.C. Prolonged serum half-life of antineoplastic drugs by incorporation into low-density lipoproteins. Cancer Res. 50:1990;7476-7482.
    • (1990) Cancer Res. , vol.50 , pp. 7476-7482
    • De Smidt, P.C.1    Van Berkel, T.J.C.2
  • 127
    • 0031925731 scopus 로고    scopus 로고
    • Synthesis of a lipophilic daunorubicin derivative and its incorporation into lipidic carriers developed for LDL receptor-mediated tumor therapy
    • Versluis A.J., Rump E.T., Rensen P.C., Van Berkel Th.J., Bijsterbosch M.K. Synthesis of a lipophilic daunorubicin derivative and its incorporation into lipidic carriers developed for LDL receptor-mediated tumor therapy. Pharm. Res. 15:1998;531-537.
    • (1998) Pharm. Res. , vol.15 , pp. 531-537
    • Versluis, A.J.1    Rump, E.T.2    Rensen, P.C.3    Van Berkel, T.J.4    Bijsterbosch, M.K.5
  • 128
    • 0020490909 scopus 로고
    • Microemulsions of phospholipids and cholesterol esters: Protein free models of low-density lipoprotein
    • Ginsburg G.S., Small D.M., Atkinson D. Microemulsions of phospholipids and cholesterol esters: protein free models of low-density lipoprotein. J. Biol. Chem. 257:1982;8216-8227.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8216-8227
    • Ginsburg, G.S.1    Small, D.M.2    Atkinson, D.3
  • 129
    • 0021183293 scopus 로고
    • Reassembled plasma low-density lipoproteins: Phospholipid-cholesterol ester-apoprotein B complex
    • Ginsburg G.S., Walsh M.T., Small D.M., Atkinson D. Reassembled plasma low-density lipoproteins: phospholipid-cholesterol ester-apoprotein B complex. J. Biol. Chem. 259:1984;6667-6673.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6667-6673
    • Ginsburg, G.S.1    Walsh, M.T.2    Small, D.M.3    Atkinson, D.4
  • 130
    • 0027314402 scopus 로고
    • Conjugation of apolipoprotein B with liposomes and targeting to cells in culture
    • Lundberg B., Hong K., Papahadjopoulos D. Conjugation of apolipoprotein B with liposomes and targeting to cells in culture. Biochim. Biophys. Acta. 1149:1993;305-312.
    • (1993) Biochim. Biophys. Acta , vol.1149 , pp. 305-312
    • Lundberg, B.1    Hong, K.2    Papahadjopoulos, D.3
  • 131
    • 0027176382 scopus 로고
    • Metabolic behavior in rats of a non-protein microemulsion resembling low-density lipoprotein
    • Maranhao R.C., Cesar T.B., Pedroso-Mariani S.R., Hirata M.H., Mesquita C.H. Metabolic behavior in rats of a non-protein microemulsion resembling low-density lipoprotein. Lipids. 28:1993;691-696.
    • (1993) Lipids , vol.28 , pp. 691-696
    • Maranhao, R.C.1    Cesar, T.B.2    Pedroso-Mariani, S.R.3    Hirata, M.H.4    Mesquita, C.H.5
  • 133
    • 0021088896 scopus 로고
    • Effect of negatively charged lipids on phagocytosis of liposomes opsonized by complements
    • Roerdink F., Wassef N.M., Richardson E.C., Alving C.R. Effect of negatively charged lipids on phagocytosis of liposomes opsonized by complements. Biochim. Biophys. Acta. 734:1983;33-39.
    • (1983) Biochim. Biophys. Acta , vol.734 , pp. 33-39
    • Roerdink, F.1    Wassef, N.M.2    Richardson, E.C.3    Alving, C.R.4
  • 134
    • 0020841295 scopus 로고
    • Apolipoprotein B of plasma lipoproteins incorporated in liposomes: Immunological properties and organ distribution when administered to rabbits
    • Klimov A.N., Korovkin B.F., Kuznetsov A.S., Popov I.N. Apolipoprotein B of plasma lipoproteins incorporated in liposomes: immunological properties and organ distribution when administered to rabbits. Byull. Eksp. Biol. Med. 96:1983;47.
    • (1983) Byull. Eksp. Biol. Med. , vol.96 , pp. 47
    • Klimov, A.N.1    Korovkin, B.F.2    Kuznetsov, A.S.3    Popov, I.N.4
  • 135
    • 84993913350 scopus 로고
    • Selective liver targeting of antivirals by recombinant chylomicrons - A new therapeutic approach to hepatitis B
    • Rensen P.C., van Dijk M.C., Havenaar E.C., Bijsterbosch M.K., Kruijt J.K., van Berkel T.J. Selective liver targeting of antivirals by recombinant chylomicrons - a new therapeutic approach to hepatitis B. Nat. Med. 1:1995;221-225.
    • (1995) Nat. Med. , vol.1 , pp. 221-225
    • Rensen, P.C.1    Van Dijk, M.C.2    Havenaar, E.C.3    Bijsterbosch, M.K.4    Kruijt, J.K.5    Van Berkel, T.J.6
  • 136
    • 0031010389 scopus 로고    scopus 로고
    • Particle size determines the specificity of apoE-containing triglyceride-rich emulsions for the LDL-receptor versus hepatic remnant receptors in vivo
    • Rensen P.C., Herijgers N., Netscher M.H., Meskers S.C.J., Van Eck M., van Berkel Th.J. Particle size determines the specificity of apoE-containing triglyceride-rich emulsions for the LDL-receptor versus hepatic remnant receptors in vivo. J. Lipid Res. 38:1997;1070-1084.
    • (1997) J. Lipid Res. , vol.38 , pp. 1070-1084
    • Rensen, P.C.1    Herijgers, N.2    Netscher, M.H.3    Meskers, S.C.J.4    Van Eck, M.5    Van Berkel, T.J.6
  • 137
    • 0030997483 scopus 로고    scopus 로고
    • Human recombinant apolipoprotein E redirects lipopolysaccharide from Kupffer cells to liver parenchymal cells in rats in vivo
    • Rensen P.C., Oosten M., Bilt E., Eck M., Kuiper J., Berkel Th.J. Human recombinant apolipoprotein E redirects lipopolysaccharide from Kupffer cells to liver parenchymal cells in rats in vivo. J. Clin. Invest. 99:1997;2438-2445.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2438-2445
    • Rensen, P.C.1    Oosten, M.2    Bilt, E.3    Eck, M.4    Kuiper, J.5    Berkel, T.J.6
  • 138
    • 0030851111 scopus 로고    scopus 로고
    • Human recombinant apolipoprotein E-enriched liposomes can mimic low density lipoproteins as carriers for the site-specific delivery of antitumor agents
    • Rensen P.C., Schiffelers R.M., Versluis A.J., Bijsterbosch M.K., Meuwissen M.E.M.J., van Berkel Th.J. Human recombinant apolipoprotein E-enriched liposomes can mimic low density lipoproteins as carriers for the site-specific delivery of antitumor agents. Mol. Pharmacol. 52:1997;445-455.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 445-455
    • Rensen, P.C.1    Schiffelers, R.M.2    Versluis, A.J.3    Bijsterbosch, M.K.4    Meuwissen, M.E.M.J.5    Van Berkel, T.J.6
  • 139
    • 0031795075 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-mediated delivery of a lipophilic daunorubicin derivative to B16 tumours in mice using apolipoprotein E-enriched liposomes
    • Versluis A.J., Rensen P.C., Rump E.T., van Berkel Th.J., Bijsterbosch M.K. Low density lipoprotein receptor-mediated delivery of a lipophilic daunorubicin derivative to B16 tumours in mice using apolipoprotein E-enriched liposomes. Br. J. Cancer. 78:1998;1607-1614.
    • (1998) Br. J. Cancer , vol.78 , pp. 1607-1614
    • Versluis, A.J.1    Rensen, P.C.2    Rump, E.T.3    Van Berkel, T.J.4    Bijsterbosch, M.K.5
  • 140
    • 0032893378 scopus 로고    scopus 로고
    • Stable incorporation of a lipophilic daunorubicin prodrug into apolipoprotein E-exposing liposomes induces uptake of prodrug via low-density lipoprotein receptor in vivo
    • Versluis A.J., Rump E.T., Rensen P.C., van Berkel Th.J., Bijsterbosch M.K. Stable incorporation of a lipophilic daunorubicin prodrug into apolipoprotein E-exposing liposomes induces uptake of prodrug via low-density lipoprotein receptor in vivo. J. Pharmacol. Exp. Ther. 289:1999;1-7.
    • (1999) J. Pharmacol. Exp. Ther. , vol.289 , pp. 1-7
    • Versluis, A.J.1    Rump, E.T.2    Rensen, P.C.3    Van Berkel, T.J.4    Bijsterbosch, M.K.5
  • 141
    • 0027538628 scopus 로고
    • Properties of incorporation, redistribution and integrity of porphyrin-LDL complexes
    • de Smidt P.C., Versluis A.J., van Berkel Th.J. Properties of incorporation, redistribution and integrity of porphyrin-LDL complexes. Biochemistry. 32:1993;2916-2922.
    • (1993) Biochemistry , vol.32 , pp. 2916-2922
    • De Smidt, P.C.1    Versluis, A.J.2    Van Berkel, T.J.3
  • 142
    • 0025738773 scopus 로고
    • Association of antisense oligonucleotides with lipoproteins prolongs the plasma half life and modifies the tissue distribution
    • de Smidt P.C., Le Doan T., De Falco S., van Berkel Th.J. Association of antisense oligonucleotides with lipoproteins prolongs the plasma half life and modifies the tissue distribution. Nucleic Acids Res. 19:1991;4695-4700.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4695-4700
    • De Smidt, P.C.1    Le Doan, T.2    De Falco, S.3    Van Berkel, T.J.4
  • 143
    • 0032919510 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein as a delivery system for photosensitizers: Implications for photodynamic therapy of atherosclerosis
    • de Vries H.E., Moor A.C., Dubbelman T.M., van Berkel Th.J., Kuiper J. Oxidized low-density lipoprotein as a delivery system for photosensitizers: implications for photodynamic therapy of atherosclerosis. J. Pharmacol. Exp. Ther. 289:1999;528-534.
    • (1999) J. Pharmacol. Exp. Ther. , vol.289 , pp. 528-534
    • De Vries, H.E.1    Moor, A.C.2    Dubbelman, T.M.3    Van Berkel, T.J.4    Kuiper, J.5
  • 144
    • 0024328667 scopus 로고
    • The lack of antigenicity of tuftsin: A naturally occurring phagocytosis stimulating tetrapeptide
    • Naim J.O., Hinshaw J.R., van Oss C.J. The lack of antigenicity of tuftsin: a naturally occurring phagocytosis stimulating tetrapeptide. Immunol. Invest. 18:1989;817-824.
    • (1989) Immunol. Invest. , vol.18 , pp. 817-824
    • Naim, J.O.1    Hinshaw, J.R.2    Van Oss, C.J.3
  • 145
    • 0023618431 scopus 로고
    • Tuftsin and tuftsin conjugates potentiate immunogenic processes: Effects and possible mechanisms
    • Dagan S., Tzehoval E., Fridkin M., Feldman M. Tuftsin and tuftsin conjugates potentiate immunogenic processes: effects and possible mechanisms. J. Biol. Response Mod. 6:1987;625-636.
    • (1987) J. Biol. Response Mod. , vol.6 , pp. 625-636
    • Dagan, S.1    Tzehoval, E.2    Fridkin, M.3    Feldman, M.4
  • 146
    • 0023029371 scopus 로고
    • Interactions of tuftsin with bovine serum albumin
    • Bhakuni V., Gupta C.M. Interactions of tuftsin with bovine serum albumin. FEBS Lett. 205:1986;347-350.
    • (1986) FEBS Lett. , vol.205 , pp. 347-350
    • Bhakuni, V.1    Gupta, C.M.2
  • 147
    • 0025945451 scopus 로고
    • The generation of antibody in mice to tuftsin: A naturally occurring phagocytosis stimulating tetrapeptide
    • Naim J.O., van Oss C.J. The generation of antibody in mice to tuftsin: a naturally occurring phagocytosis stimulating tetrapeptide. Immunol. Invest. 20:1991;351-364.
    • (1991) Immunol. Invest. , vol.20 , pp. 351-364
    • Naim, J.O.1    Van Oss, C.J.2
  • 148
    • 0021686817 scopus 로고
    • Specific interactions of liposomes with PMN leukocytes upon incorporating tuftsin in their bilayers
    • Singhal A., Bali A., Jam R.K., Gupta C.M. Specific interactions of liposomes with PMN leukocytes upon incorporating tuftsin in their bilayers. FEBS Lett. 178:1984;109-113.
    • (1984) FEBS Lett. , vol.178 , pp. 109-113
    • Singhal, A.1    Bali, A.2    Jam, R.K.3    Gupta, C.M.4
  • 149
    • 0023019178 scopus 로고
    • Protection of mice against Plasmodium berghei infection by a tuftsin derivative
    • Gupta C.M., Pun A., Jam R.K., Bali A., Anand N. Protection of mice against Plasmodium berghei infection by a tuftsin derivative. FEBS Lett. 205:1986;351-354.
    • (1986) FEBS Lett. , vol.205 , pp. 351-354
    • Gupta, C.M.1    Pun, A.2    Jam, R.K.3    Bali, A.4    Anand, N.5
  • 150
    • 0024602275 scopus 로고
    • Drug targeting in Leishmania donovani infections using tuftsin-bearing liposomes as drug vehicles
    • Guru P.Y., Agrawal A.K., Singhal U.K., Singhal A., Gupta C.M. Drug targeting in Leishmania donovani infections using tuftsin-bearing liposomes as drug vehicles. FEBS Lett. 245:1989;204-208.
    • (1989) FEBS Lett. , vol.245 , pp. 204-208
    • Guru, P.Y.1    Agrawal, A.K.2    Singhal, U.K.3    Singhal, A.4    Gupta, C.M.5
  • 151
    • 0027270325 scopus 로고
    • Tuftsin-bearing liposomes as drug vehicles in the treatment of experimental aspergillosis
    • Owais M., Ahmed I., Krishnakumar B., Jam R.K., Bachhawat B.K., Gupta C.M. Tuftsin-bearing liposomes as drug vehicles in the treatment of experimental aspergillosis. FEBS Lett. 326:1993;56-58.
    • (1993) FEBS Lett. , vol.326 , pp. 56-58
    • Owais, M.1    Ahmed, I.2    Krishnakumar, B.3    Jam, R.K.4    Bachhawat, B.K.5    Gupta, C.M.6
  • 154
    • 0032984483 scopus 로고    scopus 로고
    • Potentiation of immune response against the RESA peptides of Plasmodium falciparum by incorporating a universal T-cell epitope (CS.T3) and an immunomodulator (polytufisin), and delivery through liposomes
    • Kumar P., Biswas S., Rao D.N. Potentiation of immune response against the RESA peptides of Plasmodium falciparum by incorporating a universal T-cell epitope (CS.T3) and an immunomodulator (polytufisin), and delivery through liposomes. Microbiol. Immunol. 43:1999;567-576.
    • (1999) Microbiol. Immunol. , vol.43 , pp. 567-576
    • Kumar, P.1    Biswas, S.2    Rao, D.N.3
  • 155
    • 0032214525 scopus 로고    scopus 로고
    • Surface-modified biodegradable albumin nano- And microspheres. II: Effect of surface charges on in vitro phagocytosis and biodistribution in rats
    • Rosen M., Fischer D., Kissel T. Surface-modified biodegradable albumin nano- and microspheres. II: Effect of surface charges on in vitro phagocytosis and biodistribution in rats. Eur. J. Pharm. Biopharm. 46:1998;255-263.
    • (1998) Eur. J. Pharm. Biopharm. , vol.46 , pp. 255-263
    • Rosen, M.1    Fischer, D.2    Kissel, T.3
  • 156
    • 4243683654 scopus 로고
    • Targeting antineoplastic agents using magnetic albumin microspheres
    • E.P. Goldberg. New York: Wiley
    • Widder K., Marino P., Morris R., Seneyi A. Targeting antineoplastic agents using magnetic albumin microspheres. Goldberg E.P. Targeted Drugs. 1983;153-200 Wiley, New York.
    • (1983) Targeted Drugs , pp. 153-200
    • Widder, K.1    Marino, P.2    Morris, R.3    Seneyi, A.4
  • 159
    • 0031590665 scopus 로고    scopus 로고
    • An immune response to ovalbumin covalently coupled to liposomes is prevented when the liposomes used contain doxorubicin
    • Tardi P.G., Swartz E.N., Harasym T.O., Cullis P.R., Bally M.B. An immune response to ovalbumin covalently coupled to liposomes is prevented when the liposomes used contain doxorubicin. J. Immunol. Methods. 210:1997;137-148.
    • (1997) J. Immunol. Methods , vol.210 , pp. 137-148
    • Tardi, P.G.1    Swartz, E.N.2    Harasym, T.O.3    Cullis, P.R.4    Bally, M.B.5
  • 160
    • 0025914865 scopus 로고
    • Potent in vitro anti-human immunodeficiency virus-1 activity of modified human serum albumins
    • Jansen R.W., Molema G., Pauwels R., Schols D., De Clercq E., Meijer D.K. Potent in vitro anti-human immunodeficiency virus-1 activity of modified human serum albumins. Mol. Pharmacol. 39:1991;818-823.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 818-823
    • Jansen, R.W.1    Molema, G.2    Pauwels, R.3    Schols, D.4    De Clercq, E.5    Meijer, D.K.6
  • 161
    • 0027420931 scopus 로고
    • Pharmacokinetic analysis and cellular distribution of the anti-HIV compound succinylated human serum albumin (Suc-HSA) in vivo and in the isolated perfused rat liver
    • Jansen R.W., Olinga P., Harms G., Meijen D.K. Pharmacokinetic analysis and cellular distribution of the anti-HIV compound succinylated human serum albumin (Suc-HSA) in vivo and in the isolated perfused rat liver. Pharm. Res. 10:1993;1611-1614.
    • (1993) Pharm. Res. , vol.10 , pp. 1611-1614
    • Jansen, R.W.1    Olinga, P.2    Harms, G.3    Meijen, D.K.4
  • 162
    • 0025955532 scopus 로고
    • CD4 peptide-protein conjugates, but not recombinant gp 120 from the human immunodeficiency virus in the presence of serum from AIDS patients
    • Ghetie V., Slaughter C., Wheeler H.T., Uhr J.W., Vietta E.S. CD4 peptide-protein conjugates, but not recombinant gp 120 from the human immunodeficiency virus in the presence of serum from AIDS patients. Proc. Natl. Acad. Sci. USA. 88:1991;5690-5693.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5690-5693
    • Ghetie, V.1    Slaughter, C.2    Wheeler, H.T.3    Uhr, J.W.4    Vietta, E.S.5
  • 163
    • 0026756506 scopus 로고
    • Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp 120
    • Curtis B.M., Scharnowske S., Watson A.J. Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp 120. Proc. Natl. Acad. Sci. USA. 89:1992;8536-8560.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8536-8560
    • Curtis, B.M.1    Scharnowske, S.2    Watson, A.J.3
  • 165
  • 168
    • 0026687453 scopus 로고
    • Coupling of adenovirus to transfenin-polylysine/DNA complexes greatly enhances receptor mediated gene delivery and expression of transfected genes
    • Wagner E., Zatloukal K., Cotton M., Kinlappos H., Mechtler K., Cuniel D.T. Coupling of adenovirus to transfenin-polylysine/DNA complexes greatly enhances receptor mediated gene delivery and expression of transfected genes. Proc. Natl. Acad. Sci. USA. 89:1992;6099-6103.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6099-6103
    • Wagner, E.1    Zatloukal, K.2    Cotton, M.3    Kinlappos, H.4    Mechtler, K.5    Cuniel, D.T.6
  • 169
    • 0029974294 scopus 로고    scopus 로고
    • Synthesis of transferrin-Mitomycin C as a receptor-mediated drug targeting system
    • Tanaka T., Kaneo Y., Miyashita M. Synthesis of transferrin-Mitomycin C as a receptor-mediated drug targeting system. Biol. Pharm. Bull. 19:1996;774-777.
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 774-777
    • Tanaka, T.1    Kaneo, Y.2    Miyashita, M.3
  • 170
    • 0031855445 scopus 로고    scopus 로고
    • Evaluation of the potential of transferrin-adriamycin conjugates in the treatment of bladder cancer
    • Munns J., Yaxley J., Coomen J., Lavin M.F., Gardinger R.A., Watters D. Evaluation of the potential of transferrin-adriamycin conjugates in the treatment of bladder cancer. Br. J. Urol. 82:1998;284-289.
    • (1998) Br. J. Urol. , vol.82 , pp. 284-289
    • Munns, J.1    Yaxley, J.2    Coomen, J.3    Lavin, M.F.4    Gardinger, R.A.5    Watters, D.6
  • 172
    • 0032085308 scopus 로고    scopus 로고
    • Efficiency of targeted gene delivery of ligand-poly-L-lysine hybrids with different crosslinks
    • Uike H., Sakakibara R., Iwanaga K., Ide M., Ishiguro M. Efficiency of targeted gene delivery of ligand-poly-L-lysine hybrids with different crosslinks. Biosci. Biotechnol. Biochem. 62:1998;1247-1252.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1247-1252
    • Uike, H.1    Sakakibara, R.2    Iwanaga, K.3    Ide, M.4    Ishiguro, M.5
  • 174
    • 0024464471 scopus 로고
    • Comparison of anti-Tac and anti-transferrin receptor-conjugated liposomes for specific drug delivery to adult T-cell leukemia
    • Hege K.M., Daleke D.L., Waldmann T.A., Matthay K.K. Comparison of anti-Tac and anti-transferrin receptor-conjugated liposomes for specific drug delivery to adult T-cell leukemia. Blood. 74:1989;2043-2052.
    • (1989) Blood , vol.74 , pp. 2043-2052
    • Hege, K.M.1    Daleke, D.L.2    Waldmann, T.A.3    Matthay, K.K.4
  • 175
    • 0028225380 scopus 로고
    • Coating of liposomes with transferrin: Physicochemical study of the transferrin-lipid system
    • Egea M.A., Garcia M.L., Alsina M.A., Reig F. Coating of liposomes with transferrin: physicochemical study of the transferrin-lipid system. J. Pharm. Sci. 83:1994;169-173.
    • (1994) J. Pharm. Sci. , vol.83 , pp. 169-173
    • Egea, M.A.1    Garcia, M.L.2    Alsina, M.A.3    Reig, F.4
  • 176
    • 0032014611 scopus 로고    scopus 로고
    • Transferrin conjugated PEG-liposomes as intracellular targeting carrier for tumor therapy
    • Ishida O., Maruyama K. Transferrin conjugated PEG-liposomes as intracellular targeting carrier for tumor therapy. Nippon Rinsho. 56:1998;657-662.
    • (1998) Nippon Rinsho , vol.56 , pp. 657-662
    • Ishida, O.1    Maruyama, K.2
  • 177
    • 0026480374 scopus 로고
    • Biotin delivery to brain with a covalent conjugate of avidin and a monoclonal antibody to the transferrin receptor
    • Yoshikawa T., Pardridge W.M. Biotin delivery to brain with a covalent conjugate of avidin and a monoclonal antibody to the transferrin receptor. J. Pharmacol. Exp. Ther. 263:1992;897-903.
    • (1992) J. Pharmacol. Exp. Ther. , vol.263 , pp. 897-903
    • Yoshikawa, T.1    Pardridge, W.M.2
  • 178
    • 0030447660 scopus 로고    scopus 로고
    • Brain drug delivery of small molecules using immunoliposomes
    • Huwyler J., Wu D., Pardridge W.M. Brain drug delivery of small molecules using immunoliposomes. Proc. Natl. Acad. Sci. USA. 93:1996;14164-14169.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14164-14169
    • Huwyler, J.1    Wu, D.2    Pardridge, W.M.3
  • 179
    • 0032013311 scopus 로고    scopus 로고
    • Gene delivery into human cancer cells via transferrin receptor
    • Watanabe N., Sato Y., Yamauchi N., Nitsu Y. Gene delivery into human cancer cells via transferrin receptor. Nippon Rinsho. 56:1998;724-730.
    • (1998) Nippon Rinsho , vol.56 , pp. 724-730
    • Watanabe, N.1    Sato, Y.2    Yamauchi, N.3    Nitsu, Y.4
  • 180
    • 0032825682 scopus 로고    scopus 로고
    • An antibody-avidin fusion protein specific for the transferrin receptor serves as a delivery vehicle for effective brain targeting: Initial applications in anti-HIV antisense drug delivery to the brain
    • Penichet M.L., Kang Y.S., Pardridge W.M., Morrison S.L., Shin S.U. An antibody-avidin fusion protein specific for the transferrin receptor serves as a delivery vehicle for effective brain targeting: initial applications in anti-HIV antisense drug delivery to the brain. J. Immunol. 163:1999;4421-4426.
    • (1999) J. Immunol. , vol.163 , pp. 4421-4426
    • Penichet, M.L.1    Kang, Y.S.2    Pardridge, W.M.3    Morrison, S.L.4    Shin, S.U.5
  • 181
    • 0032824986 scopus 로고    scopus 로고
    • Genetically engineered brain drug delivery vectors: Cloning, expression and in vivo application of an anti-transferrin receptor single chain antibody-streptividin fusion gene and protein
    • Li J.Y., Sugimura K., Jboado R., Lee H.J., Zhang C., Duebel S., Pardridge W. Genetically engineered brain drug delivery vectors: cloning, expression and in vivo application of an anti-transferrin receptor single chain antibody-streptividin fusion gene and protein. Protein Eng. 12:1999;787-796.
    • (1999) Protein Eng. , vol.12 , pp. 787-796
    • Li, J.Y.1    Sugimura, K.2    Jboado, R.3    Lee, H.J.4    Zhang, C.5    Duebel, S.6    Pardridge, W.7
  • 182
    • 0028147299 scopus 로고
    • Pharmacokinetics and saturable blood-brain barrier transport of biotin bound to a conjugate of avidin and a monoclonal antibody to the transferrin receptor
    • Kang Y.S., Bickel U., Pardridge W.M. Pharmacokinetics and saturable
    • (1994) Drug Metab. Dispos. , vol.22 , pp. 99-105
    • Kang, Y.S.1    Bickel, U.2    Pardridge, W.M.3
  • 183
    • 0029079310 scopus 로고
    • Vector-mediated delivery of a polyamide (’peptide’) nucleic acid analogue through the blood brain barrier in vivo
    • Pardridge W.M., Boado R.J., Kang Y.S. Vector-mediated delivery of a polyamide (’peptide’) nucleic acid analogue through the blood brain barrier in vivo. Proc. Natl. Acad. Sci. USA. 92:1995;5592.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5592
    • Pardridge, W.M.1    Boado, R.J.2    Kang, Y.S.3
  • 184
    • 0025303751 scopus 로고
    • The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway
    • Rothberg K.G., Ying Y.S., Kolhouse J.F., Kamen B.A., Anderson R.G. The glycophospholipid-linked folate receptor internalizes folate without entering the clathrin-coated pit endocytic pathway. J. Cell Biol. 110:1990;637-649.
    • (1990) J. Cell Biol. , vol.110 , pp. 637-649
    • Rothberg, K.G.1    Ying, Y.S.2    Kolhouse, J.F.3    Kamen, B.A.4    Anderson, R.G.5
  • 185
    • 0027415690 scopus 로고
    • Potocytosis of small molecules and ions by caveolae
    • Anderson R.G.W. Potocytosis of small molecules and ions by caveolae. Trends Cell Biol. 3:1993;69-72.
    • (1993) Trends Cell Biol. , vol.3 , pp. 69-72
    • Anderson, R.G.W.1
  • 187
    • 0030801644 scopus 로고    scopus 로고
    • Clustering of GPI-anchored folate receptor independent of both cross-linking and association with caveolin
    • Wu M., Fan J., Gunning W., Ratnam M. Clustering of GPI-anchored folate receptor independent of both cross-linking and association with caveolin. J. Membr. Biol. 159:1997;137.
    • (1997) J. Membr. Biol. , vol.159 , pp. 137
    • Wu, M.1    Fan, J.2    Gunning, W.3    Ratnam, M.4
  • 188
    • 0028301752 scopus 로고
    • Differentiation regulation of folate receptor isoforms in normal and malignant tissues in vivo and in established cell lines
    • Ross J.F., Chaudhury P.K., Ratnam M. Differentiation regulation of folate receptor isoforms in normal and malignant tissues in vivo and in established cell lines. Cancer. 73:1994;2432-2443.
    • (1994) Cancer , vol.73 , pp. 2432-2443
    • Ross, J.F.1    Chaudhury, P.K.2    Ratnam, M.3
  • 189
    • 0033106119 scopus 로고    scopus 로고
    • Targeting folate receptor with folate linked to the extremities of poly (ethylene glycol)-grafted liposomes: In vivo studies
    • Gabizon A.T., Horowitz D., Goren D., Tzemach D., Mondelbaum-Shavit F., Qazen M.M., Zalipsky S. Targeting folate receptor with folate linked to the extremities of poly (ethylene glycol)-grafted liposomes: in vivo studies. Bioconjugate Chem. 10:1999;289-298.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 289-298
    • Gabizon, A.T.1    Horowitz, D.2    Goren, D.3    Tzemach, D.4    Mondelbaum-Shavit, F.5    Qazen, M.M.6    Zalipsky, S.7
  • 190
    • 0028001056 scopus 로고
    • Delivery of liposomes into cultured KB cells via folate receptor-mediated endocytosis
    • Lee R.J., Low P.S. Delivery of liposomes into cultured KB cells via folate receptor-mediated endocytosis. J. Biol. Chem. 269:1994;3198-3204.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3198-3204
    • Lee, R.J.1    Low, P.S.2
  • 191
    • 0028794831 scopus 로고
    • Folate-mediated tumor-cell targeting of liposome-entrapped doxorubicin in vitro
    • Lee R.J., Low P.S. Folate-mediated tumor-cell targeting of liposome-entrapped doxorubicin in vitro. Biochim. Biophys. Acta. 1233:1995;134-144.
    • (1995) Biochim. Biophys. Acta , vol.1233 , pp. 134-144
    • Lee, R.J.1    Low, P.S.2
  • 192
    • 5244286664 scopus 로고    scopus 로고
    • Peptide-mediated release of folate-targeted liposome contents from endosomal compartments
    • Vogel K., Wang S., Lee R.J., Chemielewski J., Low P.S. Peptide-mediated release of folate-targeted liposome contents from endosomal compartments. J. Am. Chem. Soc. 118:1996;1581.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1581
    • Vogel, K.1    Wang, S.2    Lee, R.J.3    Chemielewski, J.4    Low, P.S.5
  • 193
    • 0024247478 scopus 로고
    • Effect of lipid composition on insulin-mediated fusion of small unilamellar liposomes: A kinetic study
    • Lai J.Y. Effect of lipid composition on insulin-mediated fusion of small unilamellar liposomes: a kinetic study. J. Pharm. Sci. 77:1988;432-437.
    • (1988) J. Pharm. Sci. , vol.77 , pp. 432-437
    • Lai, J.Y.1
  • 194
    • 0020327654 scopus 로고
    • Binding of insulin to external surface of liposomes. Effect of surface curvature, temperature, and lipid composition
    • Weissner J.H., Hwang K.J. Binding of insulin to external surface of liposomes. Effect of surface curvature, temperature, and lipid composition. Biochim. Biophys. Acta. 689:1982;490-498.
    • (1982) Biochim. Biophys. Acta , vol.689 , pp. 490-498
    • Weissner, J.H.1    Hwang, K.J.2
  • 195
    • 0030980576 scopus 로고    scopus 로고
    • Varying effects of cyclodextrin derivatives on aggregation and thermal behavior of insulin in aqueous solution
    • Tokihiro K., Irie T., Uekama K. Varying effects of cyclodextrin derivatives on aggregation and thermal behavior of insulin in aqueous solution. Chem. Pharm. Bull. Tokyo. 45:1997;525-531.
    • (1997) Chem. Pharm. Bull. Tokyo , vol.45 , pp. 525-531
    • Tokihiro, K.1    Irie, T.2    Uekama, K.3
  • 196
    • 0023688019 scopus 로고
    • Interaction of insulin receptors with lipid bilayers and specific and non-specific binding of insulin to supported membranes
    • Sui S.F., Urumow T., Sachmann E. Interaction of insulin receptors with lipid bilayers and specific and non-specific binding of insulin to supported membranes. Biochemistry. 27:1988;7463-7469.
    • (1988) Biochemistry , vol.27 , pp. 7463-7469
    • Sui, S.F.1    Urumow, T.2    Sachmann, E.3
  • 197
    • 0033003033 scopus 로고    scopus 로고
    • Phase behavior and lipid-membrane structure of phospholipid-glycosphingolipid liposomes and the thermal unfolding of insulin
    • Pederson T.B., Frokjaer S., Mouritesen O.G., Jorgensen K. Phase behavior and lipid-membrane structure of phospholipid-glycosphingolipid liposomes and the thermal unfolding of insulin. J. Liposome Res. 9:1999;261-274.
    • (1999) J. Liposome Res. , vol.9 , pp. 261-274
    • Pederson, T.B.1    Frokjaer, S.2    Mouritesen, O.G.3    Jorgensen, K.4
  • 198
    • 0030457349 scopus 로고    scopus 로고
    • Transcellular delivery of an insulin-transferrin conjugate in enterocyte-like Caco-2 cells
    • Shah D., Shen W.C. Transcellular delivery of an insulin-transferrin conjugate in enterocyte-like Caco-2 cells. J. Pharm. Sci. 85:1996;1306-1311.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1306-1311
    • Shah, D.1    Shen, W.C.2
  • 201
    • 0029009048 scopus 로고
    • Human insulin receptor monoclonal antibody undergoes high affinity binding to human brain capillaries in vitro and rapid transcytosis through the blood-brain barrier in vivo in the primate
    • Pardridge W.M., Kang Y.S., Bucialk J.L., Yang J. Human insulin receptor monoclonal antibody undergoes high affinity binding to human brain capillaries in vitro and rapid transcytosis through the blood-brain barrier in vivo in the primate. Pharm. Res. 12:1995;807-816.
    • (1995) Pharm. Res. , vol.12 , pp. 807-816
    • Pardridge, W.M.1    Kang, Y.S.2    Bucialk, J.L.3    Yang, J.4
  • 202
    • 0030930364 scopus 로고    scopus 로고
    • Drug targeting of a peptide radiopharmaceutical through the primate blood-brain barrier in vivo with a monoclonal antibody to the human insulin receptors
    • Wu D., Yang J., Pardridge W.M. Drug targeting of a peptide radiopharmaceutical through the primate blood-brain barrier in vivo with a monoclonal antibody to the human insulin receptors. J. Clin. Invest. 100:1997;1804-1812.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1804-1812
    • Wu, D.1    Yang, J.2    Pardridge, W.M.3
  • 203
    • 0021705725 scopus 로고
    • Characterization of epidermal growth factor receptor gene expression in malignant and normal cell lines
    • Xu Y.H., Richert N., Ito S., Merlino G.T., Pasten I. Characterization of epidermal growth factor receptor gene expression in malignant and normal cell lines. Proc. Natl. Acad. Sci. USA. 81:1984;7308.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7308
    • Xu, Y.H.1    Richert, N.2    Ito, S.3    Merlino, G.T.4    Pasten, I.5
  • 204
    • 0032506793 scopus 로고    scopus 로고
    • Targeted in vivo delivery of therapeutic gene into experimental squamous cell carcinoma using anti-EGF receptor antibody: Immunogen approach
    • Chen J., Gamou S., Takayanagi A., Ohtake Y., Ohtsubo M., Shimizu N. Targeted in vivo delivery of therapeutic gene into experimental squamous cell carcinoma using anti-EGF receptor antibody: immunogen approach. Hum. Gene Ther. 9:1998;2673-2681.
    • (1998) Hum. Gene Ther. , vol.9 , pp. 2673-2681
    • Chen, J.1    Gamou, S.2    Takayanagi, A.3    Ohtake, Y.4    Ohtsubo, M.5    Shimizu, N.6
  • 205
    • 0028924955 scopus 로고
    • Delivery of antisense oligodeoxyribonucleotides against the human epidermal growth factor receptor into cultured KB cells with liposomes conjugated to folate via polyethylene glycol
    • Wang S., Lee R.J., Cauchon G., Gorenstein D.G., low P.S. Delivery of antisense oligodeoxyribonucleotides against the human epidermal growth factor receptor into cultured KB cells with liposomes conjugated to folate via polyethylene glycol. Proc. Natl. Acad. Sci. USA. 92:1995;3318.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3318
    • Wang, S.1    Lee, R.J.2    Cauchon, G.3    Gorenstein, D.G.4    Low, P.S.5
  • 206
    • 0032894155 scopus 로고    scopus 로고
    • Retention of biologic activity of human epidermal growth factor following conjugation to a blood-brain barrier drug delivery vector via an extended poly(ethylene glycol) linker
    • Deguchi Y., Kurihara A., Pardridge W.M. Retention of biologic activity of human epidermal growth factor following conjugation to a blood-brain barrier drug delivery vector via an extended poly(ethylene glycol) linker. Bioconjugate Chem. 10:1999;32-37.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 32-37
    • Deguchi, Y.1    Kurihara, A.2    Pardridge, W.M.3
  • 207
    • 0033136645 scopus 로고    scopus 로고
    • 111In chelation, conjugation to a blood-brain barrier delivery vector via a biotin-polyethylene linker, pharmacokinetics, and in vivo imaging of experimental brain tumors
    • 111In chelation, conjugation to a blood-brain barrier delivery vector via a biotin-polyethylene linker, pharmacokinetics, and in vivo imaging of experimental brain tumors. Bioconjugate Chem. 10:1999;502-511.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 502-511
    • Kurihara, A.1    Deguchi, Y.2    Pardridge, W.M.3
  • 210
    • 0032010976 scopus 로고    scopus 로고
    • Targeting delivery of therapeutic genes using monoclonal antibody: Immunogene approach
    • Takayanagi A., Chen J., Gamou S., Shimizu N. Targeting delivery of therapeutic genes using monoclonal antibody: immunogene approach. Nippon Rinsho. 56:1998;731-736.
    • (1998) Nippon Rinsho , vol.56 , pp. 731-736
    • Takayanagi, A.1    Chen, J.2    Gamou, S.3    Shimizu, N.4
  • 211
    • 0023103349 scopus 로고
    • Targeting of liposomes to cells bearing nerve growth factor receptors mediated by biotinylated nerve growth factor
    • Rosenberg M.B., Breakfield X.O., Hawrot E. Targeting of liposomes to cells bearing nerve growth factor receptors mediated by biotinylated nerve growth factor. J. Neurochem. 48:1987;865.
    • (1987) J. Neurochem. , vol.48 , pp. 865
    • Rosenberg, M.B.1    Breakfield, X.O.2    Hawrot, E.3
  • 212
    • 0028099338 scopus 로고
    • Cytotoxic effects of alpha- And gamma-interferon and tumor necrosis factor in human bladder tumor cell lines
    • Niell H.B., Mauer A.M., Rademacher D. Cytotoxic effects of alpha- and gamma-interferon and tumor necrosis factor in human bladder tumor cell lines. Urol. Res. 22:1994;247-250.
    • (1994) Urol. Res. , vol.22 , pp. 247-250
    • Niell, H.B.1    Mauer, A.M.2    Rademacher, D.3
  • 213
    • 0029156178 scopus 로고
    • Effect of tumor necrosis factor-alpha and interferon-gamma on the growth of human prostate cancer cell lines
    • Nakajima Y., DelliPizzi A., Mallouh C., Ferreri N.R. Effect of tumor necrosis factor-alpha and interferon-gamma on the growth of human prostate cancer cell lines. Urol. Res. 23:1995;205-210.
    • (1995) Urol. Res. , vol.23 , pp. 205-210
    • Nakajima, Y.1    Dellipizzi, A.2    Mallouh, C.3    Ferreri, N.R.4
  • 215
    • 0032901067 scopus 로고    scopus 로고
    • Targeting of tumor necrosis factor to tumor by use of dextran and metal coordination
    • Tabata Y., Noda Y., Matsui Y., Ikada Y. Targeting of tumor necrosis factor to tumor by use of dextran and metal coordination. J. Control. Release. 59:1999;187-196.
    • (1999) J. Control. Release , vol.59 , pp. 187-196
    • Tabata, Y.1    Noda, Y.2    Matsui, Y.3    Ikada, Y.4
  • 216
    • 0032484237 scopus 로고    scopus 로고
    • Growth factor release from amylopectin hydrogel based on copper coordination
    • Tabata Y., Matsui Y., Ikada Y. Growth factor release from amylopectin hydrogel based on copper coordination. J. Control. Release. 56:1998;135-148.
    • (1998) J. Control. Release , vol.56 , pp. 135-148
    • Tabata, Y.1    Matsui, Y.2    Ikada, Y.3
  • 217
    • 0343854577 scopus 로고    scopus 로고
    • Targeting transcription through nuclear receptors
    • Jones B.B., Petkovich M. Targeting transcription through nuclear receptors. Cancer Res. 2:1996;156-168.
    • (1996) Cancer Res. , vol.2 , pp. 156-168
    • Jones, B.B.1    Petkovich, M.2
  • 219
    • 0020620990 scopus 로고
    • Factors affecting the target site uptake selectivity of estrogen radiopharmaceuticals: Serum binding and endogenous estrogens
    • McElvany K.D., Carlson K.E., Katzenellenbogen J.A., Welch M.J. Factors affecting the target site uptake selectivity of estrogen radiopharmaceuticals: serum binding and endogenous estrogens. J. Steroid Biochem. 18:1983;635-641.
    • (1983) J. Steroid Biochem. , vol.18 , pp. 635-641
    • McElvany, K.D.1    Carlson, K.E.2    Katzenellenbogen, J.A.3    Welch, M.J.4
  • 221
    • 84901966320 scopus 로고
    • Peptides as targets and carriers
    • G. Gregoriadis, J. Senior, & G. Poste. NATO ASI Series. Series A: Life Sciences. London: Plenum press
    • Ringrose P.S., Humphrey M.J. Peptides as targets and carriers. Gregoriadis G., Senior J., Poste G. Targeting of Drugs With Synthetic Systems. NATO ASI Series. Series A: Life Sciences. Vol. 113:1986;65-84 Plenum press, London.
    • (1986) Targeting of Drugs With Synthetic Systems , vol.113 , pp. 65-84
    • Ringrose, P.S.1    Humphrey, M.J.2
  • 223
    • 84910431835 scopus 로고
    • Perspectives in peptide chemistry
    • A.N. Eberle, R. Geiger, & T. Wieland. Basel: Karger
    • Eberle A.N., Kriwaczek V.M., Schulster D. Perspectives in peptide chemistry. Eberle A.N., Geiger R., Wieland T. Peptide Chemistry. 1981;407-422 Karger, Basel.
    • (1981) Peptide Chemistry , pp. 407-422
    • Eberle, A.N.1    Kriwaczek, V.M.2    Schulster, D.3
  • 226
    • 85047671428 scopus 로고    scopus 로고
    • Multivalent ligand system carrying enkephalin and neurotensin coimmobilized on liposomes
    • Zhao J., Kimura S., Imanishi Y. Multivalent ligand system carrying enkephalin and neurotensin coimmobilized on liposomes. J. Pept. Sci. 2:1996;245-251.
    • (1996) J. Pept. Sci. , vol.2 , pp. 245-251
    • Zhao, J.1    Kimura, S.2    Imanishi, Y.3
  • 227
    • 0032895386 scopus 로고    scopus 로고
    • Synthesis of a novel lipopeptide with alpha-melanocyte-stimulating hormone peptide ligand and its effect on liposome stability
    • Ogawa Y., Kawahara H., Yagi N., Kodaka M., Tomohiro T., Okada T., Konakahara T., Okuno H. Synthesis of a novel lipopeptide with alpha-melanocyte-stimulating hormone peptide ligand and its effect on liposome stability. Lipids. 34:1999;387-394.
    • (1999) Lipids , vol.34 , pp. 387-394
    • Ogawa, Y.1    Kawahara, H.2    Yagi, N.3    Kodaka, M.4    Tomohiro, T.5    Okada, T.6    Konakahara, T.7    Okuno, H.8
  • 228
    • 0032952094 scopus 로고    scopus 로고
    • Different kinds of polypeptides and polypeptide-coated nanoparticles are accepted by the selective transcytosis shown in the rabbit nasal mucosa
    • Cremaschi D., Porta C., Ghirardelli R. Different kinds of polypeptides and polypeptide-coated nanoparticles are accepted by the selective transcytosis shown in the rabbit nasal mucosa. Biochim. Biophys. Acta. 1416:1999;31-38.
    • (1999) Biochim. Biophys. Acta , vol.1416 , pp. 31-38
    • Cremaschi, D.1    Porta, C.2    Ghirardelli, R.3
  • 230
    • 0030013876 scopus 로고    scopus 로고
    • Individually distinct Ig homology domains in PECAM-1 regulate homophilic binding and modulate receptor affinity
    • Sun Q.H., De Lisser H.M., Zukowski M.M., Paddock C., Albelda S.M., Newman P.J. Individually distinct Ig homology domains in PECAM-1 regulate homophilic binding and modulate receptor affinity. J. Biol. Chem. 271:1996;11090-11098.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11090-11098
    • Sun, Q.H.1    De Lisser, H.M.2    Zukowski, M.M.3    Paddock, C.4    Albelda, S.M.5    Newman, P.J.6
  • 231
    • 0029900187 scopus 로고    scopus 로고
    • Cadherin/catenin complex: A target for antiinvasive therapy
    • Mareel M., Berx F., Van Roy F., Bracke M. Cadherin/catenin complex: a target for antiinvasive therapy. J. Cell. Biochem. 61:1996;524-530.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 524-530
    • Mareel, M.1    Berx, F.2    Van Roy, F.3    Bracke, M.4
  • 232
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12:1996;697-715.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 234
    • 84907113049 scopus 로고
    • Review: The integrins alpha v beta 3: Angiogenesis and apoptosis
    • Varner J.A., Brooks P.C., Cheresh D.A. Review: the integrins alpha v beta 3: angiogenesis and apoptosis. Cell Adhes. Commun. 3:1995;367-374.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 367-374
    • Varner, J.A.1    Brooks, P.C.2    Cheresh, D.A.3
  • 235
    • 0027433096 scopus 로고
    • High-affinity self-reactive antibodies by design and selection: Targeting the integrin ligand binding site
    • Barbas C.F., Languino L.R., Smith J.W. High-affinity self-reactive antibodies by design and selection: targeting the integrin ligand binding site. Proc. Natl. Acad. Sci. USA. 90:1993;10003-10007.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10003-10007
    • Barbas, C.F.1    Languino, L.R.2    Smith, J.W.3
  • 236
    • 0028981497 scopus 로고
    • An antagonist of integrin alpha v beta 3 prevents maturation of blood vessels during embryo neovascularization
    • Drake C.J., Cheresh D.A., Little C.D. An antagonist of integrin alpha v beta 3 prevents maturation of blood vessels during embryo neovascularization. J. Cell Sci. 108:1995;2655-2661.
    • (1995) J. Cell Sci. , vol.108 , pp. 2655-2661
    • Drake, C.J.1    Cheresh, D.A.2    Little, C.D.3
  • 237
    • 0005189502 scopus 로고    scopus 로고
    • Development of a new angiogenesis-specific liposome particle for use in diagnostic imaging and drug delivery
    • Washington, DC: American Association of Cancer Research
    • Sipkins D.A., Brooks P.C., Cheresh D.A., Li K.P.C., Bednarski M.D. Development of a new angiogenesis-specific liposome particle for use in diagnostic imaging and drug delivery. AACR Proceedings:1996;American Association of Cancer Research, Washington, DC.
    • (1996) AACR Proceedings
    • Sipkins, D.A.1    Brooks, P.C.2    Cheresh, D.A.3    Li, K.P.C.4    Bednarski, M.D.5
  • 238
  • 239
    • 15844388220 scopus 로고    scopus 로고
    • Functional role of sialyl Lewis X and fibronectin-derived RGDS peptide analogue on tumor cell arrest in lungs followed by extravasation
    • Saiki I., Koike C., Obata A., Fuji H., Murata J., Kiso M., Hasegawa A., Komazawa H. Functional role of sialyl Lewis X and fibronectin-derived RGDS peptide analogue on tumor cell arrest in lungs followed by extravasation. Int. J. Cancer. 65:1996;833-839.
    • (1996) Int. J. Cancer , vol.65 , pp. 833-839
    • Saiki, I.1    Koike, C.2    Obata, A.3    Fuji, H.4    Murata, J.5    Kiso, M.6    Hasegawa, A.7    Komazawa, H.8
  • 240
  • 241
    • 0029400887 scopus 로고
    • Peptide attachment to extremities of liposomal grafted PEG chains: Preparation of the long-circulating form of laminin pentapeptide, YIGSR
    • Zalipsky S., Puntambekar B., Boulikas P., Engbers C.M., Woodle M.C. Peptide attachment to extremities of liposomal grafted PEG chains: preparation of the long-circulating form of laminin pentapeptide, YIGSR. Bioconjugate Chem. 6:1995;705-708.
    • (1995) Bioconjugate Chem. , vol.6 , pp. 705-708
    • Zalipsky, S.1    Puntambekar, B.2    Boulikas, P.3    Engbers, C.M.4    Woodle, M.C.5
  • 243
    • 0026763332 scopus 로고
    • The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis (X) oligosaccharide
    • Foxall C., Watson S.R., Dowbenko D., Fennie C., Lasky L.A., Kiso M., Hasegawa A., Asa D. The three members of the selectin receptor family recognize a common carbohydrate epitope, the sialyl Lewis (X) oligosaccharide. J. Cell Biol. 117:1992;895-902.
    • (1992) J. Cell Biol. , vol.117 , pp. 895-902
    • Foxall, C.1    Watson, S.R.2    Dowbenko, D.3    Fennie, C.4    Lasky, L.A.5    Kiso, M.6    Hasegawa, A.7    Asa, D.8
  • 244
    • 0029941666 scopus 로고    scopus 로고
    • Liposomal Arg-Gly-Asp analogues effectively inhibit metastatic B16 melanoma colonization in murine lungs
    • Oku N., Tokudome Y., Koike C., Nishikawa N., Mon H., Saiki I., Okada S. Liposomal Arg-Gly-Asp analogues effectively inhibit metastatic B16 melanoma colonization in murine lungs. Life Sci. 58:1996;2263-2270.
    • (1996) Life Sci. , vol.58 , pp. 2263-2270
    • Oku, N.1    Tokudome, Y.2    Koike, C.3    Nishikawa, N.4    Mon, H.5    Saiki, I.6    Okada, S.7
  • 248
    • 0025854021 scopus 로고
    • Priming of in vivo and in vitro anti-human T lymphotropic virus type 1 cellular immunity by virus-related protein constituted into liposomes
    • Noguchi Y., Noguchi T., Sato T., et al. Priming of in vivo and in vitro anti-human T lymphotropic virus type 1 cellular immunity by virus-related protein constituted into liposomes. J. Immunol. 146:1991;3599.
    • (1991) J. Immunol. , vol.146 , pp. 3599
    • Noguchi, Y.1    Noguchi, T.2    Sato, T.3
  • 249
    • 0030823347 scopus 로고    scopus 로고
    • HIV-1 specific cell-mediated immune responses induced by DNA vaccination were enhanced by mannan-coated liposomes and inhibited by anti-interferon-γ-antibody
    • Toda S., Ishii N., Okada E., Kusakabe K.I., Arai H., Hamajima K., Gorai I., Nishioka K. HIV-1 specific cell-mediated immune responses induced by DNA vaccination were enhanced by mannan-coated liposomes and inhibited by anti-interferon-γ-antibody. Immunology. 92:1997;111.
    • (1997) Immunology , vol.92 , pp. 111
    • Toda, S.1    Ishii, N.2    Okada, E.3    Kusakabe, K.I.4    Arai, H.5    Hamajima, K.6    Gorai, I.7    Nishioka, K.8
  • 250
    • 0032435253 scopus 로고    scopus 로고
    • Liposome oligomannose-coated with neoglycolipid, a new candidate for a safe adjuvant for induction of CD8+ cytotoxic T lymphocytes
    • Fukusawa M., Shimizu Y., Shikata K., Nakata M., Sakakibara R., Yamamoto N., Hatanaka M., Mizouchi T. Liposome oligomannose-coated with neoglycolipid, a new candidate for a safe adjuvant for induction of CD8+ cytotoxic T lymphocytes. FEBS Lett. 441:1998;353-356.
    • (1998) FEBS Lett. , vol.441 , pp. 353-356
    • Fukusawa, M.1    Shimizu, Y.2    Shikata, K.3    Nakata, M.4    Sakakibara, R.5    Yamamoto, N.6    Hatanaka, M.7    Mizouchi, T.8
  • 252
    • 0024349214 scopus 로고
    • Antibody-directed liposomes as drug-delivery vehicles
    • Wright S., Huang L. Antibody-directed liposomes as drug-delivery vehicles. Adv. Drug Deliv. Rev. 3:1989;343-389.
    • (1989) Adv. Drug Deliv. Rev. , vol.3 , pp. 343-389
    • Wright, S.1    Huang, L.2
  • 253
    • 0022645637 scopus 로고
    • Targeting of drug loaded immunoliposomes to herpes simplex virus infected corneal cell, and effective means of inhibiting virus replications in vitro
    • Norley S.G., Huang L., Rouse B.T. Targeting of drug loaded immunoliposomes to herpes simplex virus infected corneal cell, and effective means of inhibiting virus replications in vitro. J. Immunol. 136:1986;681-685.
    • (1986) J. Immunol. , vol.136 , pp. 681-685
    • Norley, S.G.1    Huang, L.2    Rouse, B.T.3
  • 254
    • 0028892778 scopus 로고
    • Plug and seal: Prevention of hypoxic cardiocyte death by sealing membrane lesions with antimyosin-liposomes
    • Khaw B.A., Torchilin V.P., Vural I., Narula J. Plug and seal: prevention of hypoxic cardiocyte death by sealing membrane lesions with antimyosin-liposomes. Nat. Med. 1:1995;1195.
    • (1995) Nat. Med. , vol.1 , pp. 1195
    • Khaw, B.A.1    Torchilin, V.P.2    Vural, I.3    Narula, J.4
  • 255
    • 0031149555 scopus 로고    scopus 로고
    • Single-chain Fv/folate conjugates mediate efficient lysis of folate-receptor-positive tumor cells
    • Cho B.K., Roy E.J., Patrik T.A., Kranz D.M. Single-chain Fv/folate conjugates mediate efficient lysis of folate-receptor-positive tumor cells. Bioconjugate Chem. 8:1997;338.
    • (1997) Bioconjugate Chem. , vol.8 , pp. 338
    • Cho, B.K.1    Roy, E.J.2    Patrik, T.A.3    Kranz, D.M.4
  • 257
    • 0029025474 scopus 로고
    • Identification of a monoclonal antibody, TV-1, directed against the basement membrane of tumor vessels, and its use to enhance the delivery of macromolecules to tumors after conjugation with interleukin-2
    • Epstein A.L., Khawli L.A., Hornick J.L., Taylor C.R. Identification of a monoclonal antibody, TV-1, directed against the basement membrane of tumor vessels, and its use to enhance the delivery of macromolecules to tumors after conjugation with interleukin-2. Cancer Res. 55:1995;2673-2680.
    • (1995) Cancer Res. , vol.55 , pp. 2673-2680
    • Epstein, A.L.1    Khawli, L.A.2    Hornick, J.L.3    Taylor, C.R.4
  • 258
    • 0029586752 scopus 로고
    • Potentiation of tumor necrosis factor-mediated cytotoxicity on human myeloid cell lines: Effects of interferons versus dimethylsulphoxide
    • Depraetere S., Joniau M. Potentiation of tumor necrosis factor-mediated cytotoxicity on human myeloid cell lines: effects of interferons versus dimethylsulphoxide. Leuk. Res. 19:1995;803.
    • (1995) Leuk. Res. , vol.19 , pp. 803
    • Depraetere, S.1    Joniau, M.2
  • 259
    • 0030861258 scopus 로고    scopus 로고
    • Factors affecting the in vitro release of recombinant human interferon-gamma (rhIFN-gamma) from PLGA microspheres
    • Yang J., Cleland J.L. Factors affecting the in vitro release of recombinant human interferon-gamma (rhIFN-gamma) from PLGA microspheres. J. Pharm. Sci. 86:1997;908-914.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 908-914
    • Yang, J.1    Cleland, J.L.2
  • 260
    • 0032872359 scopus 로고    scopus 로고
    • Dermal and transdermal delivery of protein pharmaceuticals: Lipid-based delivery systems for interferon alpha
    • Foldvari M., Baca-Estrada M.E., He Z., Hu J., Attah-Poku S., King M. Dermal and transdermal delivery of protein pharmaceuticals: lipid-based delivery systems for interferon alpha. Biotechnol. Appl. Biochem. 30:1999;129-137.
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 129-137
    • Foldvari, M.1    Baca-Estrada, M.E.2    He, Z.3    Hu, J.4    Attah-Poku, S.5    King, M.6
  • 261
    • 0025006429 scopus 로고
    • Preparation of asialofetuin-labeled liposomes with encapsulated human interferon-gamma and their uptake by isolated rat hepatocytes
    • Ishihara H., Hara T., Aramaki Y., Tsuchiya S., Hosoi K. Preparation of asialofetuin-labeled liposomes with encapsulated human interferon-gamma and their uptake by isolated rat hepatocytes. Pharm. Res. 7:1990;542-546.
    • (1990) Pharm. Res. , vol.7 , pp. 542-546
    • Ishihara, H.1    Hara, T.2    Aramaki, Y.3    Tsuchiya, S.4    Hosoi, K.5
  • 262
    • 0025685168 scopus 로고
    • Growth inhibition of glioma cells transfected with the human beta-interferon gene by liposomes coupled with a monoclonal antibody
    • Mizuno M., Yoshida J., Sugita K., Inoue I., Seo H., Hayashi Y., Koshizaka T., Yagi K. Growth inhibition of glioma cells transfected with the human beta-interferon gene by liposomes coupled with a monoclonal antibody. Cancer Res. 50:1990;7826-7829.
    • (1990) Cancer Res. , vol.50 , pp. 7826-7829
    • Mizuno, M.1    Yoshida, J.2    Sugita, K.3    Inoue, I.4    Seo, H.5    Hayashi, Y.6    Koshizaka, T.7    Yagi, K.8
  • 265
    • 0026070075 scopus 로고
    • Interleukin 4 potentiates the antiproliferative effects of tumor necrosis factor on various tumor cell lines
    • Totpal K., Aggarwal B.B. Interleukin 4 potentiates the antiproliferative effects of tumor necrosis factor on various tumor cell lines. Cancer Res. 51:1991;4266-4271.
    • (1991) Cancer Res. , vol.51 , pp. 4266-4271
    • Totpal, K.1    Aggarwal, B.B.2
  • 266
    • 0028305730 scopus 로고
    • Identification of a region within the cytoplasmic domain of the interleukin-6 (IL-6) signal transducer gp 130 important for ligand-induced endocytosis of the IL-6 receptor
    • Dittrich E. Identification of a region within the cytoplasmic domain of the interleukin-6 (IL-6) signal transducer gp 130 important for ligand-induced endocytosis of the IL-6 receptor. J. Biol. Chem. 269:1994;19014-19020.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19014-19020
    • Dittrich, E.1
  • 267
    • 0001365675 scopus 로고
    • Chemical modification of recombinant interleukin-2 by polyethylene glycol increases its potency in murine Meth A sarcoma model
    • Katre N., Knauf M., Laird W. Chemical modification of recombinant interleukin-2 by polyethylene glycol increases its potency in murine Meth A sarcoma model. Proc. Natl. Acad. Sci. USA. 84:1987;1487-1491.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1487-1491
    • Katre, N.1    Knauf, M.2    Laird, W.3
  • 268
    • 0019423170 scopus 로고
    • Entrapment of human leukocyte interferon in the aqueous interstices of liposomes
    • Anderson P., Vilcek J., Weissmann G. Entrapment of human leukocyte interferon in the aqueous interstices of liposomes. Infect. Immun. 31:1981;1099-1103.
    • (1981) Infect. Immun. , vol.31 , pp. 1099-1103
    • Anderson, P.1    Vilcek, J.2    Weissmann, G.3
  • 269
    • 0027372545 scopus 로고
    • Enhancement of anti-tumor activity of recombinant interleukin-2 (rIL-2) by immunocomplexing with a monoclonal antibody against rIL-2
    • Sato J., Hamaguchi N., Doken K., Gotoh K., Ootsu K., Iwasa S., Ogawa Y., Toguchi H. Enhancement of anti-tumor activity of recombinant interleukin-2 (rIL-2) by immunocomplexing with a monoclonal antibody against rIL-2. Biotherapy. 6:1993;225-231.
    • (1993) Biotherapy , vol.6 , pp. 225-231
    • Sato, J.1    Hamaguchi, N.2    Doken, K.3    Gotoh, K.4    Ootsu, K.5    Iwasa, S.6    Ogawa, Y.7    Toguchi, H.8
  • 270
    • 0032012705 scopus 로고    scopus 로고
    • Molecular design of polymer-conjugated cytokines and its application for drug delivery system
    • Tsunoda S., Tsutsumi Y., Mayumi T. Molecular design of polymer-conjugated cytokines and its application for drug delivery system. Nippon Rinsho. 56:1998;573-578.
    • (1998) Nippon Rinsho , vol.56 , pp. 573-578
    • Tsunoda, S.1    Tsutsumi, Y.2    Mayumi, T.3
  • 271
    • 0028242318 scopus 로고
    • Delivery of cytokines by liposomes. I. Preparation and characterization of interleukin-2 encapsulated in long-circulating sterically stabilized liposomes
    • Kedar E., Rutkowski Y., Braun E., Emanuel N., Barenholz Y. Delivery of cytokines by liposomes. I. Preparation and characterization of interleukin-2 encapsulated in long-circulating sterically stabilized liposomes. J. Immunother. Emphasis Tumor Immunol. 16:1994;47-59.
    • (1994) J. Immunother. Emphasis Tumor Immunol. , vol.16 , pp. 47-59
    • Kedar, E.1    Rutkowski, Y.2    Braun, E.3    Emanuel, N.4    Barenholz, Y.5
  • 272
  • 273
    • 0031917397 scopus 로고    scopus 로고
    • Hepatic immunopotentiation by galactose-entrapped liposomal IL-2 compound in the treatment of liver metastases
    • Okuno K., Nakamura K., Tanaka A., Yachi K., Yasutomi M. Hepatic immunopotentiation by galactose-entrapped liposomal IL-2 compound in the treatment of liver metastases. Surg. Today. 28:1998;64-69.
    • (1998) Surg. Today , vol.28 , pp. 64-69
    • Okuno, K.1    Nakamura, K.2    Tanaka, A.3    Yachi, K.4    Yasutomi, M.5
  • 277
    • 0033051399 scopus 로고    scopus 로고
    • Enhanced accumulation of Sialyl Lewis-Carboxymethyl pullulan conjugate in acute inflammatory lesion
    • Horie K., Sakagami M., Kuramochi K., Hanasaki K., Hamana H., Ito T. Enhanced accumulation of Sialyl Lewis-Carboxymethyl pullulan conjugate in acute inflammatory lesion. Pharm. Res. 16:1999;314-320.
    • (1999) Pharm. Res. , vol.16 , pp. 314-320
    • Horie, K.1    Sakagami, M.2    Kuramochi, K.3    Hanasaki, K.4    Hamana, H.5    Ito, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.