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Volumn 29, Issue 3, 1998, Pages 273-289

Receptor-mediated targeted drug or toxin delivery

Author keywords

Endocytosis; Endosomal compartment; HPMA; Ligand; Lysosomes; Monoclonal antibodies; Polymeric carrier; Receptors; Side toxicity; Surface antigens; Targeted chemotherapy

Indexed keywords

ANTIGENS; CELLS; DRUG THERAPY; ENZYMES; MONOCLONAL ANTIBODIES; ONCOLOGY; POLYACRYLATES; TOXICITY;

EID: 0345404305     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-409X(97)00084-7     Document Type: Review
Times cited : (80)

References (145)
  • 1
    • 0006496113 scopus 로고
    • Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles
    • B.M.F. Pearse, Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles, Proc. Natl. Acad. Sci. USA 73 (1976) 1255-1259.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1255-1259
    • Pearse, B.M.F.1
  • 2
    • 0018827560 scopus 로고
    • Three-dimensional visualization of coated vesicle formation in fibroblasts
    • J. Heuser, L. Evans, Three-dimensional visualization of coated vesicle formation in fibroblasts, J. Cell. Biol. 84 (1980) 560-583.
    • (1980) J. Cell. Biol. , vol.84 , pp. 560-583
    • Heuser, J.1    Evans, L.2
  • 3
    • 0021947313 scopus 로고
    • Assembled and unassembled pools of clathrin: A quantitative study using an enzyme immunoassay
    • B. Goud, C. Huet, D. Louvard, Assembled and unassembled pools of clathrin: a quantitative study using an enzyme immunoassay, J. Cell. Biol. 100 (1985) 521-527.
    • (1985) J. Cell. Biol. , vol.100 , pp. 521-527
    • Goud, B.1    Huet, C.2    Louvard, D.3
  • 4
    • 0020601856 scopus 로고
    • Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells
    • C.R. Hopkins, I.S. Trowbridge, Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells, J. Cell. Biol. 97 (1983) 508-521.
    • (1983) J. Cell. Biol. , vol.97 , pp. 508-521
    • Hopkins, C.R.1    Trowbridge, I.S.2
  • 6
    • 0018927306 scopus 로고
    • The receptosome: An intermediate organelle of receptor-mediated endocytosis in cultured fibroblasts
    • M.C. Willingham, I. Pastan, The receptosome: an intermediate organelle of receptor-mediated endocytosis in cultured fibroblasts, Cell 21 (1980) 67-77.
    • (1980) Cell , vol.21 , pp. 67-77
    • Willingham, M.C.1    Pastan, I.2
  • 8
    • 0020324578 scopus 로고
    • The transit of epidermal growth factor through coated pits of the Golgi system
    • M.C. Willingham, I. Pastan, The transit of epidermal growth factor through coated pits of the Golgi system, J. Cell. Biol. 94 (1982) 207-212.
    • (1982) J. Cell. Biol. , vol.94 , pp. 207-212
    • Willingham, M.C.1    Pastan, I.2
  • 9
    • 0020685762 scopus 로고
    • Intracellular site of asialoglycoprotein receptor-ligand uncoupling:double-label immunoelectron microcsopy during receptor-mediated endocytosis
    • H.J. Geuze, J.W. Slot, G.J. Strous, H.F. Lodish, A.L. Schwartz, Intracellular site of asialoglycoprotein receptor-ligand uncoupling:double-label immunoelectron microcsopy during receptor-mediated endocytosis, Cell 32 (1983) 277-287.
    • (1983) Cell , vol.32 , pp. 277-287
    • Geuze, H.J.1    Slot, J.W.2    Strous, G.J.3    Lodish, H.F.4    Schwartz, A.L.5
  • 11
    • 0022481626 scopus 로고
    • Receptor-mediated endocytosis
    • P. Stahl, A.L. Schwartz, Receptor-mediated endocytosis, J. Clin. Invest. 77 (1986) 657-662.
    • (1986) J. Clin. Invest. , vol.77 , pp. 657-662
    • Stahl, P.1    Schwartz, A.L.2
  • 12
    • 0021018412 scopus 로고
    • Prelysosomal divergence of transferrin and epidermal growth factor during receptor-mediated endocytosis
    • R.B. Dickson, J.A. Hanover, M.C. Willingham, I. Pastan, Prelysosomal divergence of transferrin and epidermal growth factor during receptor-mediated endocytosis, Biochemistry 22 (1983) 5667-5674.
    • (1983) Biochemistry , vol.22 , pp. 5667-5674
    • Dickson, R.B.1    Hanover, J.A.2    Willingham, M.C.3    Pastan, I.4
  • 13
    • 0021844413 scopus 로고
    • Uptake and transport of mannosylated ligands by alveolar macrophages. Studies on ATP-dependent receptor-ligand dissociation
    • T. Wileman, R. Boshans, P. Stahl, Uptake and transport of mannosylated ligands by alveolar macrophages. Studies on ATP-dependent receptor-ligand dissociation, J. Biol. Chem. 260 (1985) 7387-7393.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7387-7393
    • Wileman, T.1    Boshans, R.2    Stahl, P.3
  • 14
    • 0020724143 scopus 로고
    • Recycling receptors: The round-trip itinerary of migrant membrane proteins
    • M.S. Brown, R.G.W. Anderson, J.L. Goldstein, Recycling receptors: the round-trip itinerary of migrant membrane proteins, Cell 32 (1983) 663-667.
    • (1983) Cell , vol.32 , pp. 663-667
    • Brown, M.S.1    Anderson, R.G.W.2    Goldstein, J.L.3
  • 15
    • 0021220948 scopus 로고
    • Internalization and degradation of macrophage Fc receptors bound to polyvalent immune complexes
    • I.S. Mellman, H. Plutner, Internalization and degradation of macrophage Fc receptors bound to polyvalent immune complexes, J. Cell. Biol. 98 (1984) 1170-1177.
    • (1984) J. Cell. Biol. , vol.98 , pp. 1170-1177
    • Mellman, I.S.1    Plutner, H.2
  • 16
    • 0002400525 scopus 로고
    • Entry of polypeptide toxins into mammalian cells
    • I. Pastan, M.C. Wellingham, (Eds.), Plenum Press, New York
    • S. Olsnes, K. Sandvig, Entry of polypeptide toxins into mammalian cells, in: I. Pastan, M.C. Wellingham, (Eds.), Endocytosis, Plenum Press, New York, 1985, pp. 195-234.
    • (1985) Endocytosis , pp. 195-234
    • Olsnes, S.1    Sandvig, K.2
  • 17
    • 0021958570 scopus 로고
    • Drug-induced endocytosis of neonatal erythrocytes
    • L.M. Matovcik, I.G. Junga, S.L. Schrier, Drug-induced endocytosis of neonatal erythrocytes, Blood 65 (1985) 1056-1063.
    • (1985) Blood , vol.65 , pp. 1056-1063
    • Matovcik, L.M.1    Junga, I.G.2    Schrier, S.L.3
  • 18
    • 0014680926 scopus 로고
    • Membrane alterations in hemolysis: Internalization of plasmalemma induced by primaquine
    • F.L. Ginn, P. Hochstein, B.F. Trump, Membrane alterations in hemolysis: internalization of plasmalemma induced by primaquine, Science 164 (1969) 843-845.
    • (1969) Science , vol.164 , pp. 843-845
    • Ginn, F.L.1    Hochstein, P.2    Trump, B.F.3
  • 19
    • 0023611524 scopus 로고
    • Drug-induced endocytosis and entrapment in red cells and ghosts
    • S.L. Schrier, Drug-induced endocytosis and entrapment in red cells and ghosts, Methods. Enyzmol. 149 (1987) 260-270.
    • (1987) Methods. Enyzmol. , vol.149 , pp. 260-270
    • Schrier, S.L.1
  • 20
    • 0015362501 scopus 로고
    • Drug-induced erythrocyte membrane internalization
    • I. Ben-Bassat, K.G. Bensch, S.L. Schrier, Drug-induced erythrocyte membrane internalization, J. Clin. Invest. 51 (1972) 1833-1844.
    • (1972) J. Clin. Invest. , vol.51 , pp. 1833-1844
    • Ben-Bassat, I.1    Bensch, K.G.2    Schrier, S.L.3
  • 21
    • 0017350046 scopus 로고
    • Response of cultured cells to the exotoxins of Pseudomonas aeruginosa and Corynebacterium diphtheria: Differential toxicity
    • J.L. Middlebrook, R.B. Dorland, Response of cultured cells to the exotoxins of Pseudomonas aeruginosa and Corynebacterium diphtheria: differential toxicity, Can. J. Microbiol. 23 (1977) 183-189.
    • (1977) Can. J. Microbiol. , vol.23 , pp. 183-189
    • Middlebrook, J.L.1    Dorland, R.B.2
  • 22
    • 0021354472 scopus 로고
    • Controlled biodegradability of polymers - Key to drug delivery systems
    • J. Kopeček, Controlled biodegradability of polymers - key to drug delivery systems, J. Biomaterials 5 (1984) 19-25.
    • (1984) J. Biomaterials , vol.5 , pp. 19-25
    • Kopeček, J.1
  • 24
    • 0025099302 scopus 로고
    • The potential of water-soluble polymeric carriers in targeted and site-specific drug delivery
    • J. Kopeček, The potential of water-soluble polymeric carriers in targeted and site-specific drug delivery, J. Control. Release 11 (1990) 279-290.
    • (1990) J. Control. Release , vol.11 , pp. 279-290
    • Kopeček, J.1
  • 25
    • 0026757191 scopus 로고
    • Drug-polymer conjugates: Potential for improved chemotherapy
    • R. Duncan, Drug-polymer conjugates: potential for improved chemotherapy, Anti-Cancer Drugs 3 (1992) 175-210.
    • (1992) Anti-Cancer Drugs , vol.3 , pp. 175-210
    • Duncan, R.1
  • 27
    • 0029451952 scopus 로고
    • Antibody-targeted polymer bound drugs
    • B. Říhová, Antibody-targeted polymer bound drugs, Folia Microbiol. 40 (1995) 367-384.
    • (1995) Folia Microbiol. , vol.40 , pp. 367-384
    • Říhová, B.1
  • 28
    • 0024282306 scopus 로고
    • Evidence for targeted gene delivery to Hep G2 hepatoma cells in vitro
    • G.Y. Wu, C.H. Wu, Evidence for targeted gene delivery to Hep G2 hepatoma cells in vitro, Biochemistry 27 (1988) 887-892.
    • (1988) Biochemistry , vol.27 , pp. 887-892
    • Wu, G.Y.1    Wu, C.H.2
  • 29
    • 0026502766 scopus 로고
    • Hepatocyte-directed gene transfer in vivo leads to transient improvement of hypercholesterolemia in low density lipoprotein receptor-deficient rabbits
    • J.M. Wilson, M. Grossman, C.H. Wu, N.R. Chowdhury, G.Y. Wu, J.R. Chowdhury, Hepatocyte-directed gene transfer in vivo leads to transient improvement of hypercholesterolemia in low density lipoprotein receptor-deficient rabbits, J. Biol. Chem. 267 (1992) 963-967.
    • (1992) J. Biol. Chem. , vol.267 , pp. 963-967
    • Wilson, J.M.1    Grossman, M.2    Wu, C.H.3    Chowdhury, N.R.4    Wu, G.Y.5    Chowdhury, J.R.6
  • 30
    • 0028430957 scopus 로고
    • Folate receptor mediated DNA delivery into tumor cells: Potosomal disruption results in enhanced gene expression
    • S. Gottschalk, R.J. Cristiano, L.C. Smith, S.L.C. Woo, Folate receptor mediated DNA delivery into tumor cells: potosomal disruption results in enhanced gene expression, Gene Ther. 1 (1994) 185-191.
    • (1994) Gene Ther. , vol.1 , pp. 185-191
    • Gottschalk, S.1    Cristiano, R.J.2    Smith, L.C.3    Woo, S.L.C.4
  • 31
    • 0028223310 scopus 로고
    • Gene transfer in vivo: Sustained expression and regulation of genes introduced into the liver by receptor-targeted uptake
    • J.C. Perales, T. Ferkol, H. Beegen, O.D. Ratnoff, R.W. Hanson, Gene transfer in vivo: sustained expression and regulation of genes introduced into the liver by receptor-targeted uptake, Proc. Natl. Acad. Sci. USA 91 (1994) 4086-4090.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4086-4090
    • Perales, J.C.1    Ferkol, T.2    Beegen, H.3    Ratnoff, O.D.4    Hanson, R.W.5
  • 32
    • 0030002508 scopus 로고    scopus 로고
    • Controllable gene therapy. Pharmaceutics of non-viral gene delivery systems
    • E. Tomlinson, A.P. Rolland, Controllable gene therapy. Pharmaceutics of non-viral gene delivery systems, J. Control. Release 39 (1996) 357-372.
    • (1996) J. Control. Release , vol.39 , pp. 357-372
    • Tomlinson, E.1    Rolland, A.P.2
  • 33
    • 0028052170 scopus 로고
    • Targeted gene delivery to alveolar macropohages via Fc receptor-mediated endocytosis
    • Y. Rojanasakul, L.Y. Wang, C.J. Malanga, J.K.H. Ma, J. Liaw, Targeted gene delivery to alveolar macropohages via Fc receptor-mediated endocytosis, Pharmaceutical Res. 11 (1994) 1731-1736.
    • (1994) Pharmaceutical Res. , vol.11 , pp. 1731-1736
    • Rojanasakul, Y.1    Wang, L.Y.2    Malanga, C.J.3    Ma, J.K.H.4    Liaw, J.5
  • 35
    • 0018746767 scopus 로고
    • Coated pits, coated vesicles, and receptor-mediated endocytosis
    • J.L. Goldstein, R.G.W. Anderson, M.S. Brown, Coated pits, coated vesicles, and receptor-mediated endocytosis, Nature (Lond.) 279 (1979) 679-685.
    • (1979) Nature (Lond.) , vol.279 , pp. 679-685
    • Goldstein, J.L.1    Anderson, R.G.W.2    Brown, M.S.3
  • 38
    • 0024454711 scopus 로고
    • Intracellular pathways and mechanisms of sorting in receptor-mediated endocytosis
    • V.L. Shepherd, Intracellular pathways and mechanisms of sorting in receptor-mediated endocytosis, Trends Pharmacol. Sci. 10 (1989) 458-462.
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 458-462
    • Shepherd, V.L.1
  • 39
    • 0005106988 scopus 로고
    • Selective endocytosis
    • J.R. Robinson, V.H. Lee, (Eds.), New York, Marcel Dekker
    • R. Duncan, Selective endocytosis, in: J.R. Robinson, V.H. Lee, (Eds.), Sustained and Controlled Drug Delivery Systems, New York, Marcel Dekker, 1987, pp. 581-621.
    • (1987) Sustained and Controlled Drug Delivery Systems , pp. 581-621
    • Duncan, R.1
  • 40
    • 0024147194 scopus 로고
    • How protein toxins enter and kill cells
    • A.E. Frankel (Ed.), Boston, Kluwer Academic Publishers
    • S. Olsnes, K. Sandvig, How protein toxins enter and kill cells, in: A.E. Frankel (Ed.), Immunotoxins, Boston, Kluwer Academic Publishers, 1988, pp. 39-73.
    • (1988) Immunotoxins , pp. 39-73
    • Olsnes, S.1    Sandvig, K.2
  • 41
    • 0024227006 scopus 로고
    • Ricin A-chain containing immunotoxins directed against different epitopes on the CD2 molecule differ in their ability to kill normal and malignant T cells
    • O.W. Press, J.P. Martin, P.E. Thorpe, E.S. Vitetta, Ricin A-chain containing immunotoxins directed against different epitopes on the CD2 molecule differ in their ability to kill normal and malignant T cells, J. Immunol. 141 (1988) 4410-4417.
    • (1988) J. Immunol. , vol.141 , pp. 4410-4417
    • Press, O.W.1    Martin, J.P.2    Thorpe, P.E.3    Vitetta, E.S.4
  • 42
    • 0029934710 scopus 로고    scopus 로고
    • Kinetic analysis of receptor-mediated endocytosis (RME) of proteins and peptides: Use of RME as a drug delivery system
    • Y. Kato, T. Seita, T. Kuwabara, Y. Sugiyama, 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
  • 43
    • 0018958518 scopus 로고
    • The galactose-specific recognition system of mammalian liver: The route of ligand internalization in rat hepatocytes
    • D.A. Wall, G. Wilson, A.L. Hubbard, The galactose-specific recognition system of mammalian liver: the route of ligand internalization in rat hepatocytes, Cell 21 (1980) 79-93.
    • (1980) Cell , vol.21 , pp. 79-93
    • Wall, D.A.1    Wilson, G.2    Hubbard, A.L.3
  • 44
    • 0021972989 scopus 로고
    • Acetaminophen hepatotoxicity and targeted rescue: A model for specific chemotherapy of hepatocellular carcinoma
    • G.Y. Wu, C.H. Wu, M.I. Rubin, Acetaminophen hepatotoxicity and targeted rescue: a model for specific chemotherapy of hepatocellular carcinoma, Hepatology 5 (1985) 709-713.
    • (1985) Hepatology , vol.5 , pp. 709-713
    • Wu, G.Y.1    Wu, C.H.2    Rubin, M.I.3
  • 45
    • 0023633667 scopus 로고
    • Some perspectives on targeted delivery with prodrugs
    • A.A. Sinkula, Some perspectives on targeted delivery with prodrugs, Ann. New York Acad. Sci. 507 (1987) 281-288.
    • (1987) Ann. New York Acad. Sci. , vol.507 , pp. 281-288
    • Sinkula, A.A.1
  • 48
    • 0021024586 scopus 로고
    • Site-specific (targeted) drug delivery in cancer therapy
    • G. Poste, R. Kirsch, Site-specific (targeted) drug delivery in cancer therapy, Biotechnology 1 (1983) 869-878.
    • (1983) Biotechnology , vol.1 , pp. 869-878
    • Poste, G.1    Kirsch, R.2
  • 49
    • 0026773763 scopus 로고
    • Intracellular catabolism of radiolabeled anti-Ţ antibodies by malignant B-cells
    • F. Geissler, S.K. Anderson, P. Venkatesan, O. Press, Intracellular catabolism of radiolabeled anti-Ţ antibodies by malignant B-cells, Cancer Res. 52 (1992) 2907-2915.
    • (1992) Cancer Res. , vol.52 , pp. 2907-2915
    • Geissler, F.1    Anderson, S.K.2    Venkatesan, P.3    Press, O.4
  • 51
    • 0025861068 scopus 로고
    • The effect of ricin B chain on the intracellular trafficking of an a chain immunotoxin
    • J. Timar, D.P. McIntosh, R. Henry, A.J. Cumber, G.D. Parnell, A.J. Davies, The effect of ricin B chain on the intracellular trafficking of an A chain immunotoxin, Br. J. Cancer 64 (1991) 655-662.
    • (1991) Br. J. Cancer , vol.64 , pp. 655-662
    • Timar, J.1    McIntosh, D.P.2    Henry, R.3    Cumber, A.J.4    Parnell, G.D.5    Davies, A.J.6
  • 52
    • 0029975193 scopus 로고    scopus 로고
    • Physiologic-based strategies for protein drug delivery to the brain
    • W.M. Pardridge, Physiologic-based strategies for protein drug delivery to the brain, J. Control. Release 39 (1996) 281-286.
    • (1996) J. Control. Release , vol.39 , pp. 281-286
    • Pardridge, W.M.1
  • 54
    • 0023911890 scopus 로고
    • Endocytosis and degradation of murine anti-human CD3 monoclonal antibodies by normal and malignant T-lymphocytes
    • O.W. Press, J.A. Hansen, A. Farr, P.J. Martin, Endocytosis and degradation of murine anti-human CD3 monoclonal antibodies by normal and malignant T-lymphocytes, Cancer Res. 48 (1988) 2249-2257.
    • (1988) Cancer Res. , vol.48 , pp. 2249-2257
    • Press, O.W.1    Hansen, J.A.2    Farr, A.3    Martin, P.J.4
  • 55
    • 0021955656 scopus 로고
    • In vivo administration of lymphocyte-specific monoclonal antibodies in nonhuman primates. I.Effects of anti-T11 antibodies on the circulating T cell pool
    • N.L. Letvin, J. Ritz, L.J. Guida, J.M. Yetz, J.M. Lambert, E.L. Reiherz, S.F. Schlossman, In vivo administration of lymphocyte-specific monoclonal antibodies in nonhuman primates. I.Effects of anti-T11 antibodies on the circulating T cell pool, Blood 66 (1985) 961-966.
    • (1985) Blood , vol.66 , pp. 961-966
    • Letvin, N.L.1    Ritz, J.2    Guida, L.J.3    Yetz, J.M.4    Lambert, J.M.5    Reiherz, E.L.6    Schlossman, S.F.7
  • 57
    • 0025309130 scopus 로고
    • Comparison of in vitro cell binding characteristics of four monoclonal antibodies and their individual tumor localization properties in mice
    • S.M. Andrew, R.W. Johnstone, S.M. Russell, I.F.C. McKenzie, G.A. Pietersz, Comparison of in vitro cell binding characteristics of four monoclonal antibodies and their individual tumor localization properties in mice, Cancer Res. 50 (1990) 4423-4428.
    • (1990) Cancer Res. , vol.50 , pp. 4423-4428
    • Andrew, S.M.1    Johnstone, R.W.2    Russell, S.M.3    McKenzie, I.F.C.4    Pietersz, G.A.5
  • 59
    • 0025122427 scopus 로고
    • Evaluation of ricin a chain-containing immunotoxins directed against the CD30 antigen as potential reagents for the treatment of Hodgkin's disease
    • A. Engert, F. Burrows, W. Jung, P.L. Tazzari, H. Stein, M. Pfreundschuh, V. Diehl, P. Thorpe, Evaluation of ricin A chain-containing immunotoxins directed against the CD30 antigen as potential reagents for the treatment of Hodgkin's disease, Cancer Res. 50 (1990) 84-88.
    • (1990) Cancer Res. , vol.50 , pp. 84-88
    • Engert, A.1    Burrows, F.2    Jung, W.3    Tazzari, P.L.4    Stein, H.5    Pfreundschuh, M.6    Diehl, V.7    Thorpe, P.8
  • 60
    • 0026705890 scopus 로고
    • Effect of bivalent interaction upon apparent antibody affinity: Experimental confirmation of theory using fluorescence photobleaching and implication for antibody binding assays
    • E.N. Kaufman, R.K. Jain, Effect of bivalent interaction upon apparent antibody affinity: experimental confirmation of theory using fluorescence photobleaching and implication for antibody binding assays, Cancer Res. 52 (1992) 4157-4167.
    • (1992) Cancer Res. , vol.52 , pp. 4157-4167
    • Kaufman, E.N.1    Jain, R.K.2
  • 61
    • 0027366723 scopus 로고
    • Re-evaluation of the concept of functional affinity as applied to bivalent antibody binding to cell surface antigens
    • G.L. Ong, M.J. Mattes, Re-evaluation of the concept of functional affinity as applied to bivalent antibody binding to cell surface antigens, Mol. Immunol. 30 (1993) 1455-1462.
    • (1993) Mol. Immunol. , vol.30 , pp. 1455-1462
    • Ong, G.L.1    Mattes, M.J.2
  • 62
    • 0020571717 scopus 로고
    • Monoclonal antibodies to carcinoembryonic antigen:ionic strength as a factor in the selection of antibodies for immunoscintigraphy
    • C.M. Haskell, F. Buchegger, M. Schreyer, S. Carrel, J.-P. Mach, Monoclonal antibodies to carcinoembryonic antigen:ionic strength as a factor in the selection of antibodies for immunoscintigraphy, Cancer Res. 43 (1983) 3857-3864.
    • (1983) Cancer Res. , vol.43 , pp. 3857-3864
    • Haskell, C.M.1    Buchegger, F.2    Schreyer, M.3    Carrel, S.4    Mach, J.-P.5
  • 63
    • 0029586287 scopus 로고
    • Tumor targeting of the anti-ovarian carcinoma x anti-CD3/TCR bispecific monoclonal antibody OC/TR and its parental MOv18 antibody in experimental ovarian cancer
    • O.C. Boerman, J.G. Tibben, L.F.A.G. Massuger, R.A.M.J. Claessens, F.H.M. Corstens, Tumor targeting of the anti-ovarian carcinoma x anti-CD3/TCR bispecific monoclonal antibody OC/TR and its parental MOv18 antibody in experimental ovarian cancer, Anticancer Res. 15 (1995) 2169-2174.
    • (1995) Anticancer Res. , vol.15 , pp. 2169-2174
    • Boerman, O.C.1    Tibben, J.G.2    Massuger, L.F.A.G.3    Claessens, R.A.M.J.4    Corstens, F.H.M.5
  • 64
    • 0022395325 scopus 로고
    • Immunoreactivity of monoclonal anti-melanoma antibodies in relation to the amount of radioactive iodine substituted to the antibody molecules
    • S. Matzku, H. Kirchgessner, W.G. Dippold, J. Bruggen, Immunoreactivity of monoclonal anti-melanoma antibodies in relation to the amount of radioactive iodine substituted to the antibody molecules, Eur. J. Nucl. Med. 11 (1985) 260-264.
    • (1985) Eur. J. Nucl. Med. , vol.11 , pp. 260-264
    • Matzku, S.1    Kirchgessner, H.2    Dippold, W.G.3    Bruggen, J.4
  • 65
    • 0022870818 scopus 로고
    • Selective killing of normal and neoplastic human B cells with anti-CD19- And anti-CD22-ricin a chain immunotoxins
    • R.D. May, E.S. Vitetta, G. Moldenhauer, B. Dorken, Selective killing of normal and neoplastic human B cells with anti-CD19- and anti-CD22-ricin A chain immunotoxins, Cancer Drug Delivery 3 (1986) 261-272.
    • (1986) Cancer Drug Delivery , vol.3 , pp. 261-272
    • May, R.D.1    Vitetta, E.S.2    Moldenhauer, G.3    Dorken, B.4
  • 67
    • 0342337058 scopus 로고
    • Receptor-mediated hepatic clearance of peptide hormones
    • D.D. Breimer, D.J.A. Crommelin, K.K. Midha (Eds.), Amsterdam Medical Press, Noordwijk
    • Y. Sugiyama, H. Sato, S. Yanai, D.C. Kim, S. Miyauchi, Y. Sawada, T. Iga, M. Hanano, Receptor-mediated hepatic clearance of peptide hormones, in: D.D. Breimer, D.J.A. Crommelin, K.K. Midha (Eds.), Topics in Pharmaceutical Sciences 1989, Amsterdam Medical Press, Noordwijk, 1989, pp.429-443.
    • (1989) Topics in Pharmaceutical Sciences 1989 , pp. 429-443
    • Sugiyama, Y.1    Sato, H.2    Yanai, S.3    Kim, D.C.4    Miyauchi, S.5    Sawada, Y.6    Iga, T.7    Hanano, M.8
  • 68
    • 0024996478 scopus 로고
    • Receptor-mediated disposition of polypeptides: Kinetic analysis of the transport of epidermal growth factor using in vitro, isolated perfused organs, and in vivo system
    • Y. Sugiyama, D.C. Kim, H. Sato, S. Yanai, H. Satoh, T. Iga, M. Hanano, Receptor-mediated disposition of polypeptides: kinetic analysis of the transport of epidermal growth factor using in vitro, isolated perfused organs, and in vivo system, J. Control. Release 13 (1990) 157-174.
    • (1990) J. Control. Release , vol.13 , pp. 157-174
    • Sugiyama, Y.1    Kim, D.C.2    Sato, H.3    Yanai, S.4    Satoh, H.5    Iga, T.6    Hanano, M.7
  • 69
    • 0024341614 scopus 로고
    • Endocytosis and degradation of monoclonal antibodies targeting human B-cell malignancies
    • O.W. Press, A.G. Farr, K.I. Borroz, S.K. Anderson, P.J. Martin, Endocytosis and degradation of monoclonal antibodies targeting human B-cell malignancies, Cancer Res. 49 (1989) 4906-4912.
    • (1989) Cancer Res. , vol.49 , pp. 4906-4912
    • Press, O.W.1    Farr, A.G.2    Borroz, K.I.3    Anderson, S.K.4    Martin, P.J.5
  • 70
    • 0040985974 scopus 로고
    • Internalization of lymphocyte membrane components
    • B. Pernis, Internalization of lymphocyte membrane components, Immunol. Today 6 (1985) 45-49.
    • (1985) Immunol. Today , vol.6 , pp. 45-49
    • Pernis, B.1
  • 72
    • 0023574012 scopus 로고
    • Selective in vivo antitumor effects of monoclonal anti-I-A antibody on B cell lymphoma
    • S.H. Bridges, A.M. Kruisbeek, D.L. Longo, Selective in vivo antitumor effects of monoclonal anti-I-A antibody on B cell lymphoma, J. Immunol. 139 (1987) 4242-4249.
    • (1987) J. Immunol. , vol.139 , pp. 4242-4249
    • Bridges, S.H.1    Kruisbeek, A.M.2    Longo, D.L.3
  • 74
    • 3643074049 scopus 로고
    • Endocytosis of the membrane immunoglobulins of mouse spleen B-cells: A quantitative study of its rate, amount, and sensitivity to physiological, physical, and cross-linking agents
    • P. Metezeau, I. Elguindi, M.E. Goldberg, Endocytosis of the membrane immunoglobulins of mouse spleen B-cells: a quantitative study of its rate, amount, and sensitivity to physiological, physical, and cross-linking agents, EMBO J. 3 (1984) 2235-2242.
    • (1984) EMBO J. , vol.3 , pp. 2235-2242
    • Metezeau, P.1    Elguindi, I.2    Goldberg, M.E.3
  • 76
    • 0021678752 scopus 로고
    • Acidification of internalized Class I major histocompatibility complex antigen by T-lymphoblasts
    • R.F. Murphy, D.B. Tse, C.R. Cantor, B. Pernis, Acidification of internalized Class I major histocompatibility complex antigen by T-lymphoblasts, Cell Immunol. 88 (1984) 336-342.
    • (1984) Cell Immunol. , vol.88 , pp. 336-342
    • Murphy, R.F.1    Tse, D.B.2    Cantor, C.R.3    Pernis, B.4
  • 77
    • 0005595441 scopus 로고
    • Role of endocytosis and receptor recycling in ligand-toxin and antibody-toxin conjugate activity
    • C.-W. Vogel (Ed.), Oxford University Press, Oxford
    • R. Youle, D. Neville, Role of endocytosis and receptor recycling in ligand-toxin and antibody-toxin conjugate activity, in: C.-W. Vogel (Ed.), Immunoconjugates, Oxford University Press, Oxford, 1987, p. 153.
    • (1987) Immunoconjugates , pp. 153
    • Youle, R.1    Neville, D.2
  • 78
    • 0021271357 scopus 로고
    • Tyrosinamide residues enhance pinocytic capture of N-(2-hydroxypropyl)methacrylamide copolymers
    • R. Duncan, H. Cable, P. Rejmanová, J. Kopeček, J.B. Lloyd, Tyrosinamide residues enhance pinocytic capture of N-(2-hydroxypropyl)methacrylamide copolymers, Biochim. Biophys. Acta 799 (1984) 1-8.
    • (1984) Biochim. Biophys. Acta , vol.799 , pp. 1-8
    • Duncan, R.1    Cable, H.2    Rejmanová, P.3    Kopeček, J.4    Lloyd, J.B.5
  • 79
    • 0027253329 scopus 로고
    • 6 toward human hepatocarcinoma cell line (PLC/PRF/5) targeted with galactosamine and to mouse splenocytes targeted with anti-Thy-1.2 antibodies
    • 6 toward human hepatocarcinoma cell line (PLC/PRF/5) targeted with galactosamine and to mouse splenocytes targeted with anti-Thy-1.2 antibodies, J. Control. Release 25 (1993) 71-87.
    • (1993) J. Control. Release , vol.25 , pp. 71-87
    • Říhová, B.1    Krinick, N.2    Kopeček, J.3
  • 83
    • 0025282386 scopus 로고
    • Partial characterization of mechanism of insulin accumulation in H35 hepatoma cell nuclei
    • R.M. Smith, L. Jarett, Partial characterization of mechanism of insulin accumulation in H35 hepatoma cell nuclei, Diabetes 39 (1990) 683-689.
    • (1990) Diabetes , vol.39 , pp. 683-689
    • Smith, R.M.1    Jarett, L.2
  • 84
    • 0028071526 scopus 로고
    • Nuclear signaling pathway for polypeptide ligands and their membrane-receptors
    • D.A. Jans, Nuclear signaling pathway for polypeptide ligands and their membrane-receptors, FASEB J. 8 (1994) 841-847.
    • (1994) FASEB J. , vol.8 , pp. 841-847
    • Jans, D.A.1
  • 85
    • 0022550409 scopus 로고
    • Evidence that pinocytosis in lymphoid cells has a low capacity
    • V.S. Goldmacher, N.L. Tinnel, B.C. Nelson, Evidence that pinocytosis in lymphoid cells has a low capacity, J. Cell. Biol. 102 (1986) 1312-1319.
    • (1986) J. Cell. Biol. , vol.102 , pp. 1312-1319
    • Goldmacher, V.S.1    Tinnel, N.L.2    Nelson, B.C.3
  • 87
    • 0028863458 scopus 로고
    • Intracellular uptake and catabolism of anti-IgM antibodies and bi-specific antibody-targeted hapten by B-lymphoma cells
    • C. Manetti, J.M. Le Doussal, E. Rouvier, A. Gruaz-Guyon, J. Barbet, Intracellular uptake and catabolism of anti-IgM antibodies and bi-specific antibody-targeted hapten by B-lymphoma cells, Int. J. Cancer 63 (1995) 250-256.
    • (1995) Int. J. Cancer , vol.63 , pp. 250-256
    • Manetti, C.1    Le Doussal, J.M.2    Rouvier, E.3    Gruaz-Guyon, A.4    Barbet, J.5
  • 89
    • 0025882501 scopus 로고
    • Targeting behavior of rat monoclonal IgG antibodies in vivo: Role of antibody isotype, specificity and the target cell antigen density
    • N. Yousaf, J.C. Howard, B.D. Williams, Targeting behavior of rat monoclonal IgG antibodies in vivo: role of antibody isotype, specificity and the target cell antigen density, Eur. J. Immunol. 21 (1991) 943-950.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 943-950
    • Yousaf, N.1    Howard, J.C.2    Williams, B.D.3
  • 90
    • 0018949401 scopus 로고
    • Characterization of a human B lymphocyte-specific antigen
    • P. Stashenko, L.M. Nadler, R. Hardy, S.F. Schlossman, Characterization of a human B lymphocyte-specific antigen, J. Immunol. 125 (1980) 1678-1685.
    • (1980) J. Immunol. , vol.125 , pp. 1678-1685
    • Stashenko, P.1    Nadler, L.M.2    Hardy, R.3    Schlossman, S.F.4
  • 91
    • 0022508408 scopus 로고
    • Exposure of K 562 cells to anti-receptor monoclonal antibody OKT9 results in rapid redistribution and enhanced degradation of the transferrin receptor
    • A. Weissman, R.D. Klausner, K. Rao, J.B. Harford, Exposure of K 562 cells to anti-receptor monoclonal antibody OKT9 results in rapid redistribution and enhanced degradation of the transferrin receptor, J. Cell. Biol. 102 (1986) 951-958.
    • (1986) J. Cell. Biol. , vol.102 , pp. 951-958
    • Weissman, A.1    Klausner, R.D.2    Rao, K.3    Harford, J.B.4
  • 92
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • K.W. Dunn, T.E. McGraw, F.R. Maxfield, Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome, J. Cell. Biol. 109 (1989) 3303-3314.
    • (1989) J. Cell. Biol. , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 93
    • 0024309206 scopus 로고
    • Effect of galactose on interaction of N-(2-hydroxypropyl)methacrylamide copolymers with hepatoma cells in culture: Preliminary application to an anticancer agent, daunomycin
    • K.B. O'Hare, I.C. Hume, L. Scarlett, V. Chytrý, P. Kopeèková, J. Kopecek, J. Duncan, Effect of galactose on interaction of N-(2-hydroxypropyl)methacrylamide copolymers with hepatoma cells in culture: preliminary application to an anticancer agent, daunomycin, Hepatology 10 (1989) 207-214.
    • (1989) Hepatology , vol.10 , pp. 207-214
    • O'Hare, K.B.1    Hume, I.C.2    Scarlett, L.3    Chytrý, V.4    Kopeèková, P.5    Kopecek, J.6    Duncan, J.7
  • 94
    • 0022460432 scopus 로고
    • Evaluation of ricin a chain immunotoxins directed against human T cells
    • O. Press, E. Vitetta, A. Farr, J. Hansen, P. Martin, Evaluation of ricin A chain immunotoxins directed against human T cells, Cell. Immunol. 102 (1986) 10-20.
    • (1986) Cell. Immunol. , vol.102 , pp. 10-20
    • Press, O.1    Vitetta, E.2    Farr, A.3    Hansen, J.4    Martin, P.5
  • 95
    • 0019121477 scopus 로고
    • Epidermal growth factor-toxin a chain conjugates: EGF-ricin a is a potent toxin while EGF-diphtheria fragment a is nontoxic
    • D.B. Cawley, H.R. Herschman, D.G. Gilliland, R.J. Collier, Epidermal growth factor-toxin A chain conjugates: EGF-ricin A is a potent toxin while EGF-diphtheria fragment A is nontoxic, Cell 22 (1980) 563-570.
    • (1980) Cell , vol.22 , pp. 563-570
    • Cawley, D.B.1    Herschman, H.R.2    Gilliland, D.G.3    Collier, R.J.4
  • 96
    • 0022355089 scopus 로고
    • Purified immunotoxins that are reactive with human lymphoid cells. Monoclonal antibodies conjugated to the ribosome-inactivating proteins gelonin and the pokeweed antiviral proteins
    • J.M. Lambert, P.D. Senter, A. Yau-Young, W.A. Blatter, V.S. Goldmacher, Purified immunotoxins that are reactive with human lymphoid cells. Monoclonal antibodies conjugated to the ribosome-inactivating proteins gelonin and the pokeweed antiviral proteins, J. Biol. Chem. 260 (1985) 12035-12041.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12035-12041
    • Lambert, J.M.1    Senter, P.D.2    Yau-Young, A.3    Blatter, W.A.4    Goldmacher, V.S.5
  • 97
    • 0023616248 scopus 로고
    • Comparison of two anti-Thy 1.1-abrin A-chain immunotoxins prepared with different cross-linking agents: Antitumor effects, in vivo fate, and tumor cell mutants
    • P.E. Thorpe, D.C. Blakey, A.N. Brown, P. Knowles, R.E. Knyba, P.M. Wallace, G.J. Watson, E.J. Wawrzynczak, Comparison of two anti-Thy 1.1-abrin A-chain immunotoxins prepared with different cross-linking agents: antitumor effects, in vivo fate, and tumor cell mutants, J. Natl. Cancer Inst. 79 (1987) 1101-1112.
    • (1987) J. Natl. Cancer Inst. , vol.79 , pp. 1101-1112
    • Thorpe, P.E.1    Blakey, D.C.2    Brown, A.N.3    Knowles, P.4    Knyba, R.E.5    Wallace, P.M.6    Watson, G.J.7    Wawrzynczak, E.J.8
  • 99
    • 0021996468 scopus 로고
    • Endocytosis of an antibody ricin a chain conjugate (immuno-A-toxin) absorbed on colloidal gold. Effects of ammonium chloride and monensin
    • D. Carriere, P. Casellas, G. Richer, P. Gros, J.K. Jansen, Endocytosis of an antibody ricin A chain conjugate (immuno-A-toxin) absorbed on colloidal gold. Effects of ammonium chloride and monensin, Exp. Cell. Res. 156 (1985) 327-340.
    • (1985) Exp. Cell. Res. , vol.156 , pp. 327-340
    • Carriere, D.1    Casellas, P.2    Richer, G.3    Gros, P.4    Jansen, J.K.5
  • 101
    • 0024469053 scopus 로고
    • Anticancer agents coupled to N-(2-hydroxypropyl)methacrylamide copolymers. 3. Evaluation of adriamycin conjugates against mouse leukaemia L1210 in vivo
    • R. Duncan, I.C. Hume, P. Kopečková, K. Ulbrich, J. Strohalm, J. Kopeček, Anticancer agents coupled to N-(2-hydroxypropyl)methacrylamide copolymers. 3. Evaluation of adriamycin conjugates against mouse leukaemia L1210 in vivo, J. Control. Release 10 (1989) 51-63.
    • (1989) J. Control. Release , vol.10 , pp. 51-63
    • Duncan, R.1    Hume, I.C.2    Kopečková, P.3    Ulbrich, K.4    Strohalm, J.5    Kopeček, J.6
  • 102
    • 0020021127 scopus 로고
    • Carbohydrate recognition systems of the liver
    • G. Ashwell, J. Harford, Carbohydrate recognition systems of the liver, Annu. Rev. Biochem. 51 (1982) 531-554.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 104
    • 0025855856 scopus 로고
    • Comparison of the liver subcellular distribution of free daunomycin and that bound to galactosamine targeted N-(2-hydropxypropyl)-methacrylamide copolymers following intravenous administration in the rat
    • S.R. Wedge, R. Duncan, P. Kopečková, Comparison of the liver subcellular distribution of free daunomycin and that bound to galactosamine targeted N-(2-hydropxypropyl)-methacrylamide copolymers following intravenous administration in the rat, Br. J. Cancer 63 (1991) 546-549.
    • (1991) Br. J. Cancer , vol.63 , pp. 546-549
    • Wedge, S.R.1    Duncan, R.2    Kopečková, P.3
  • 105
    • 0022630373 scopus 로고
    • Immunotoxins show rapid entry of diphtheria toxin but not ricin via the T3 antigen
    • R.J. Youle, F.M. Uckun, D.A. Vallera, M. Colombatti, Immunotoxins show rapid entry of diphtheria toxin but not ricin via the T3 antigen, J. Immunol. 136 (1986) 93-98.
    • (1986) J. Immunol. , vol.136 , pp. 93-98
    • Youle, R.J.1    Uckun, F.M.2    Vallera, D.A.3    Colombatti, M.4
  • 107
    • 0019990986 scopus 로고
    • Differential endocytosis of T and B lymphocyte surface molecules evaluated with antibody-bearing fluorescent liposomes containing methotrexate
    • P. Machy, J. Barbet, L.D. Leserman, Differential endocytosis of T and B lymphocyte surface molecules evaluated with antibody-bearing fluorescent liposomes containing methotrexate, Proc. Natl. Acad. Sci. USA 79 (1982) 4148-4152.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4148-4152
    • Machy, P.1    Barbet, J.2    Leserman, L.D.3
  • 108
    • 0026040618 scopus 로고
    • Intracellular catabolism of radiolabeled anti-CD3 antibodies by leukemic T cells
    • F. Geissler, S.K. Anderson, O.W. Press, Intracellular catabolism of radiolabeled anti-CD3 antibodies by leukemic T cells, Cell. Immunol. 137 (1991) 96-110.
    • (1991) Cell. Immunol. , vol.137 , pp. 96-110
    • Geissler, F.1    Anderson, S.K.2    Press, O.W.3
  • 109
    • 0020358718 scopus 로고
    • Studies of the mechanism of cell intoxication by diphtheria toxin fragment A-asialoorosomucoid hybrid toxins
    • T.M. Chang, D.J. Kullberg, Studies of the mechanism of cell intoxication by diphtheria toxin fragment A-asialoorosomucoid hybrid toxins, J. Biol. Chem. 257 (1982) 12563-12572.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12563-12572
    • Chang, T.M.1    Kullberg, D.J.2
  • 110
    • 0020724144 scopus 로고
    • Penetration of Semliki Forest virus from acidic prelysosomal vacuoles
    • M. Marsh, E. Bolzau, A. Helenius, Penetration of Semliki Forest virus from acidic prelysosomal vacuoles, Cell 32 (1983) 931-940.
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 111
    • 0024553578 scopus 로고
    • Antigen processing and intracellular Ia: Possible roles of endocytosis and protein synthesis in Ia function
    • C.V. Harding, E.R. Unanue, Antigen processing and intracellular Ia: possible roles of endocytosis and protein synthesis in Ia function, J. Immunol. 141 (1989) 12-19.
    • (1989) J. Immunol. , vol.141 , pp. 12-19
    • Harding, C.V.1    Unanue, E.R.2
  • 112
    • 0022468419 scopus 로고
    • Transport of macrophage Fc receptors and Fc receptor-bound ligands to lysosomes
    • P. Ukkonen, V. Lewis, M. Marsh, A. Helenius, I. Mellman, Transport of macrophage Fc receptors and Fc receptor-bound ligands to lysosomes, J. Exp. Med. 163 (1986) 952-971.
    • (1986) J. Exp. Med. , vol.163 , pp. 952-971
    • Ukkonen, P.1    Lewis, V.2    Marsh, M.3    Helenius, A.4    Mellman, I.5
  • 115
    • 0025993767 scopus 로고
    • Requirements for the internalization of a murine monoclonal antibody directed against the HER-2/neu gene product c-erbB-2
    • L.A. Maier, F.J. Xu, S. Hester, C.M. Boyer, S. McKenzie, A.M. Bruskin, Y. Argon, R.C. Bast Jr., Requirements for the internalization of a murine monoclonal antibody directed against the HER-2/neu gene product c-erbB-2, Cancer Res. 51 (1991) 5361-5369.
    • (1991) Cancer Res. , vol.51 , pp. 5361-5369
    • Maier, L.A.1    Xu, F.J.2    Hester, S.3    Boyer, C.M.4    McKenzie, S.5    Bruskin, A.M.6    Argon, Y.7    Bast R.C., Jr.8
  • 116
    • 0023906928 scopus 로고
    • Radiohalogenation of a monoclonal antibody using an N-succinimidyl-3-(tri-n-butylstannyl)benzoate intermediate
    • M.R. Zalutsky, A.S. Narula, Radiohalogenation of a monoclonal antibody using an N-succinimidyl-3-(tri-n-butylstannyl)benzoate intermediate, Cancer Res. 48 (1988) 1446-1450.
    • (1988) Cancer Res. , vol.48 , pp. 1446-1450
    • Zalutsky, M.R.1    Narula, A.S.2
  • 118
    • 0024534779 scopus 로고
    • Virus entry into animal cells
    • M. Marsh, A. Helenius, Virus entry into animal cells, Adv. Virus Res. 36 (1989) 107-139.
    • (1989) Adv. Virus Res. , vol.36 , pp. 107-139
    • Marsh, M.1    Helenius, A.2
  • 119
    • 0023918693 scopus 로고
    • Mediation of reduction of spontaneous and experimental pulmonary metastases by ricin A-chain immunotoxin 45-2D9-RTA with potentiation by systemic monensin in mice
    • J.A. Roth, R.S. Ames, K. Fry, H.M. Lee, P.J. Scannon, Mediation of reduction of spontaneous and experimental pulmonary metastases by ricin A-chain immunotoxin 45-2D9-RTA with potentiation by systemic monensin in mice, Cancer Res. 48 (1988) 3496-3501.
    • (1988) Cancer Res. , vol.48 , pp. 3496-3501
    • Roth, J.A.1    Ames, R.S.2    Fry, K.3    Lee, H.M.4    Scannon, P.J.5
  • 120
    • 0026457254 scopus 로고
    • Cytotoxicity of CD3-ricin a chain immunotoxins in relation to cellular uptake and degradation kinetics
    • Y.V. Van Oosterhout, F.W Preijers, H.M. Wessels, T. de Witte, Cytotoxicity of CD3-ricin A chain immunotoxins in relation to cellular uptake and degradation kinetics, Cancer Res. 52 (1992) 5921-5925.
    • (1992) Cancer Res. , vol.52 , pp. 5921-5925
    • Van Oosterhout, Y.V.1    Preijers, F.W.2    Wessels, H.M.3    De Witte, T.4
  • 121
    • 0028096216 scopus 로고
    • Retention of B-cell-specific monoclonal antibodies by human lymphoma cells
    • O.W. Press, J. Howell-Clark, S. Anderson, I. Bernstein, Retention of B-cell-specific monoclonal antibodies by human lymphoma cells, Blood 83 (1994) 1390-1397.
    • (1994) Blood , vol.83 , pp. 1390-1397
    • Press, O.W.1    Howell-Clark, J.2    Anderson, S.3    Bernstein, I.4
  • 123
    • 0023002618 scopus 로고
    • Cloned fragment of diphtheria toxin linked to T cell-specific antibody identifies regions of B chain activity in cell entry
    • M. Colombatti, L. Greenfield, R.J. Youle, Cloned fragment of diphtheria toxin linked to T cell-specific antibody identifies regions of B chain activity in cell entry, J. Biol. Chem. 261 (1986) 3030-3035.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3030-3035
    • Colombatti, M.1    Greenfield, L.2    Youle, R.J.3
  • 124
    • 0020957391 scopus 로고
    • Monensin inhibits intracellular dissociation of asialoglycoproteins from their receptor
    • J. Harford, A.W. Wolkoff, G. Ashwell, R.D. Klausner, Monensin inhibits intracellular dissociation of asialoglycoproteins from their receptor, J. Cell. Biol. 96 (1983) 1824-1828.
    • (1983) J. Cell. Biol. , vol.96 , pp. 1824-1828
    • Harford, J.1    Wolkoff, A.W.2    Ashwell, G.3    Klausner, R.D.4
  • 125
    • 0024465916 scopus 로고
    • Monensin and chloroquine inhibit transfer to lysosomes of endocytosed macromolecules in cultured mouse peritoneal macrophages
    • K. Stenseth, J. Thyberg, Monensin and chloroquine inhibit transfer to lysosomes of endocytosed macromolecules in cultured mouse peritoneal macrophages, Eur. J. Cell Biol. 49 (1989) 326-333.
    • (1989) Eur. J. Cell Biol. , vol.49 , pp. 326-333
    • Stenseth, K.1    Thyberg, J.2
  • 126
    • 0022649774 scopus 로고
    • Subcellular characterization of the endocytosis of small oligomers of mouse immunoglobulin G in murine macrophages
    • D.S. Finbloom, Subcellular characterization of the endocytosis of small oligomers of mouse immunoglobulin G in murine macrophages, J. Immunol. 136 (1986) 844-851.
    • (1986) J. Immunol. , vol.136 , pp. 844-851
    • Finbloom, D.S.1
  • 127
    • 0022508337 scopus 로고
    • Targeting, internalization, and cytotoxicity of methotrexate-monoclonal anti-stage-specific embryonic antigen-1 antibody conjugates in cultured F-9 teratocarcinoma cells
    • W.C. Shen, B. Ballou, H.J.-P. Ryser, T.R. Hakala, Targeting, internalization, and cytotoxicity of methotrexate-monoclonal anti-stage-specific embryonic antigen-1 antibody conjugates in cultured F-9 teratocarcinoma cells, Cancer Res. 46 (1986) 3912-3916.
    • (1986) Cancer Res. , vol.46 , pp. 3912-3916
    • Shen, W.C.1    Ballou, B.2    Ryser, H.J.-P.3    Hakala, T.R.4
  • 128
    • 0013538106 scopus 로고
    • Structures and activities of protease inhibitors of microbial origin
    • E. Reich, D.B. Bifkin, E. Shaw (Eds.), New York, Cold Spring Harbor, Cold Spring Harbor Laboratory
    • T. Aoyagi, H. Umezawa, Structures and activities of protease inhibitors of microbial origin, in: E. Reich, D.B. Bifkin, E. Shaw (Eds.), Proteases and Biological Control, New York, Cold Spring Harbor, Cold Spring Harbor Laboratory, 1975, pp. 429-454.
    • (1975) Proteases and Biological Control , pp. 429-454
    • Aoyagi, T.1    Umezawa, H.2
  • 129
    • 85069068487 scopus 로고    scopus 로고
    • unpublished results
    • Říhová et al., unpublished results, 1996
    • (1996)
    • Říhová1
  • 130
    • 0023930539 scopus 로고
    • Antibody-directed affinity therapy applied to the immune system. in vivo effectiveness and limited toxicity of daunomycin conjugated to HPMA copolymers and targeting antibody
    • B. Říhová, P. Kopečková, J. Strohalm, P. Rossmann, V. Větvička, J. Kopeček, Antibody-directed affinity therapy applied to the immune system. In vivo effectiveness and limited toxicity of daunomycin conjugated to HPMA copolymers and targeting antibody, Clin. Immunol. Immunopathol. 46 (1988) 100-114.
    • (1988) Clin. Immunol. Immunopathol. , vol.46 , pp. 100-114
    • Říhová, B.1    Kopečková, P.2    Strohalm, J.3    Rossmann, P.4    Větvička, V.5    Kopeček, J.6
  • 131
    • 0024557322 scopus 로고
    • Preparation and in vitro cytotoxicity of a methotrexate-anti-MM46 monoclonal antibody conjugate via an oligopeptide spacer
    • N. Umemoto, Y. Kato, N. Endo, Y. Takeda, T. Hara, Preparation and in vitro cytotoxicity of a methotrexate-anti-MM46 monoclonal antibody conjugate via an oligopeptide spacer, Int. J. Cancer 43 (1989) 677-684.
    • (1989) Int. J. Cancer , vol.43 , pp. 677-684
    • Umemoto, N.1    Kato, Y.2    Endo, N.3    Takeda, Y.4    Hara, T.5
  • 132
    • 0021356320 scopus 로고
    • The entry of enveloped viruses into cells by endocytosis
    • M. Marsh, The entry of enveloped viruses into cells by endocytosis, Biochem. J. 218 (1984) 1-10.
    • (1984) Biochem. J. , vol.218 , pp. 1-10
    • Marsh, M.1
  • 133
    • 0021231875 scopus 로고
    • Pseudomonas exotoxin-anti-TAC: Cell-specific immunotoxin active against cells expressing the human T-cell growth factor receptor
    • D.J. FitzGerald, T.A. Waldmann, M.C. Willingham, I. Pastan, Pseudomonas exotoxin-anti-TAC: cell-specific immunotoxin active against cells expressing the human T-cell growth factor receptor, J. Clin. Invest. 74 (1984) 966-971.
    • (1984) J. Clin. Invest. , vol.74 , pp. 966-971
    • FitzGerald, D.J.1    Waldmann, T.A.2    Willingham, M.C.3    Pastan, I.4
  • 134
    • 0006096786 scopus 로고
    • Pathway of adenovirus entry into cells
    • A.L. Notkins, M.B.A. Oldstone (Eds.), Springer-Verlag, New York
    • P. Seth, D.J. FitzGerald, M.C. Willingham, I. Pastan, 1986. Pathway of adenovirus entry into cells, in: A.L. Notkins, M.B.A. Oldstone (Eds.), Concepts in Viral Pathogenesis, vol.II, Springer-Verlag, New York, pp. 191-195.
    • (1986) Concepts in Viral Pathogenesis , vol.2 , pp. 191-195
    • Seth, P.1    FitzGerald, D.J.2    Willingham, M.C.3    Pastan, I.4
  • 135
    • 0023257383 scopus 로고
    • Radioimmunodetection and radioimmunotherapy of cutaneous T cell lymphomas using an labeled monoclonal antibody: An Illinois cancer council study
    • S.T. Rosen, A.M. Zimmer, R. Goldman-Leikin, Radioimmunodetection and radioimmunotherapy of cutaneous T cell lymphomas using an labeled monoclonal antibody: an Illinois cancer council study, J. Clin. Oncol. 5 (1987) 562-573.
    • (1987) J. Clin. Oncol. , vol.5 , pp. 562-573
    • Rosen, S.T.1    Zimmer, A.M.2    Goldman-Leikin, R.3
  • 138
    • 0025825174 scopus 로고
    • Phase I-II studies of Yttrium-labeled antiferritin treatment for end-stage Hodgkin's disease, including radiation therapy oncology group 87-01
    • H.M. Vriesendorp, J.M. Herpst, M.A. Germack, J.L. Klein, P.K. Leichner, D.M. Loudsenslager, S.E. Order, Phase I-II studies of Yttrium-labeled antiferritin treatment for end-stage Hodgkin's disease, including radiation therapy oncology group 87-01, J. Clin. Oncol. 9 (1991) 918-928.
    • (1991) J. Clin. Oncol. , vol.9 , pp. 918-928
    • Vriesendorp, H.M.1    Herpst, J.M.2    Germack, M.A.3    Klein, J.L.4    Leichner, P.K.5    Loudsenslager, D.M.6    Order, S.E.7
  • 142
    • 0001095828 scopus 로고
    • 6 conjugates and a preliminary study of their photodynamic effect on mouse splenocytes in vitro
    • 6 conjugates and a preliminary study of their photodynamic effect on mouse splenocytes in vitro, Makromol. Chem. 191 (1990) 839-856.
    • (1990) Makromol. Chem. , vol.191 , pp. 839-856
    • Krinick, N.L.1    Říhová, B.2    Ulbrich, K.3    Kopeček, J.4
  • 144
    • 85069072509 scopus 로고    scopus 로고
    • unpubl. data
    • Št'astný et al., unpubl. data, 1996
    • (1996)
    • Št'astný1


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