메뉴 건너뛰기




Volumn 21, Issue 12, 2010, Pages 2153-2163

Effects of charge on antibody tissue distribution and pharmacokinetics

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN-ANTIBODY REACTIONS; ANTIGENS; BLOOD; CHEMICAL MODIFICATION; CYTOLOGY; ELECTROSTATICS; PHARMACOKINETICS; TISSUE;

EID: 78650394814     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc100261d     Document Type: Review
Times cited : (321)

References (108)
  • 1
    • 9444260479 scopus 로고    scopus 로고
    • Biological impediments to monoclonal antibody-based cancer immunotherapy
    • Christiansen, J. and Rajasekaran, A. K. (2004) Biological impediments to monoclonal antibody-based cancer immunotherapy Mol. Cancer Ther. 3, 1493-501
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 1493-1501
    • Christiansen, J.1    Rajasekaran, A.K.2
  • 2
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler, G. and Milstein, C. (1975) Continuous cultures of fused cells secreting antibody of predefined specificity Nature 256, 495-7
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 4
    • 54249138516 scopus 로고    scopus 로고
    • Monoclonal antibody pharmacokinetics and pharmacodynamics
    • Wang, W., Wang, E. Q., and Balthasar, J. P. (2008) Monoclonal antibody pharmacokinetics and pharmacodynamics Clin. Pharmacol. Ther. 84, 548-58
    • (2008) Clin. Pharmacol. Ther. , vol.84 , pp. 548-558
    • Wang, W.1    Wang, E.Q.2    Balthasar, J.P.3
  • 5
    • 33646901012 scopus 로고    scopus 로고
    • Target-mediated drug disposition and dynamics
    • Mager, D. E. (2006) Target-mediated drug disposition and dynamics Biochem. Pharmacol. 72, 1-10
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 1-10
    • Mager, D.E.1
  • 6
    • 67649207267 scopus 로고    scopus 로고
    • Engineering human IgG1 affinity to human neonatal Fc receptor: Impact of affinity improvement on pharmacokinetics in primates
    • Yeung, Y. A., Leabman, M. K., Marvin, J. S., Qiu, J., Adams, C. W., Lien, S., Starovasnik, M. A., and Lowman, H. B. (2009) Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates J. Immunol. 182, 7663-71
    • (2009) J. Immunol. , vol.182 , pp. 7663-7671
    • Yeung, Y.A.1    Leabman, M.K.2    Marvin, J.S.3    Qiu, J.4    Adams, C.W.5    Lien, S.6    Starovasnik, M.A.7    Lowman, H.B.8
  • 7
    • 33846215917 scopus 로고    scopus 로고
    • Antibody constructs in cancer therapy: Protein engineering strategies to improve exposure in solid tumors
    • Beckman, R. A., Weiner, L. M., and Davis, H. M. (2007) Antibody constructs in cancer therapy: protein engineering strategies to improve exposure in solid tumors Cancer 109, 170-9
    • (2007) Cancer , vol.109 , pp. 170-179
    • Beckman, R.A.1    Weiner, L.M.2    Davis, H.M.3
  • 9
    • 78650375670 scopus 로고
    • Electric charge of antibodies
    • Olitzki, L. (1933) Electric charge of antibodies J. Immunol. 24, 505-512
    • (1933) J. Immunol. , vol.24 , pp. 505-512
    • Olitzki, L.1
  • 10
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • Roopenian, D. C. and Akilesh, S. (2007) FcRn: the neonatal Fc receptor comes of age Nat. Rev. Immunol. 7, 715-25
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 12
    • 0031757878 scopus 로고    scopus 로고
    • Dynamics of protein-protein docking: Cytochrome c and cytochrome c peroxidase revisited
    • Castro, G., Boswell, C. A., and Northrup, S. H. (1998) Dynamics of protein-protein docking: cytochrome c and cytochrome c peroxidase revisited J. Biomol. Struct. Dyn. 16, 413-24
    • (1998) J. Biomol. Struct. Dyn. , vol.16 , pp. 413-424
    • Castro, G.1    Boswell, C.A.2    Northrup, S.H.3
  • 13
    • 33644619972 scopus 로고    scopus 로고
    • Heterogeneity of recombinant antibodies: Linking structure to function
    • Harris, R. J. (2005) Heterogeneity of recombinant antibodies: linking structure to function Dev. Biol. (Basel) 122, 117-27
    • (2005) Dev. Biol. (Basel) , vol.122 , pp. 117-127
    • Harris, R.J.1
  • 14
    • 77956873702 scopus 로고    scopus 로고
    • Pharmacokinetic, pharmacodynamic and immunogenicity comparability assessment strategies for monoclonal antibodies
    • Putnam, W. S., Prabhu, S., Zheng, Y., Subramanyam, M., and Wang, Y. M. C. (2010) Pharmacokinetic, pharmacodynamic and immunogenicity comparability assessment strategies for monoclonal antibodies Trends Biotechnol. 28, 509-516
    • (2010) Trends Biotechnol. , vol.28 , pp. 509-516
    • Putnam, W.S.1    Prabhu, S.2    Zheng, Y.3    Subramanyam, M.4    Wang, Y.M.C.5
  • 15
    • 60849102492 scopus 로고    scopus 로고
    • Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods
    • Vlasak, J. and Ionescu, R. (2008) Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods Curr. Pharm. Biotechnol. 9, 468-81
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 468-481
    • Vlasak, J.1    Ionescu, R.2
  • 18
    • 34848813590 scopus 로고    scopus 로고
    • Development of radioimmunotherapeutic and diagnostic antibodies: An inside-out view
    • Boswell, C. A. and Brechbiel, M. W. (2007) Development of radioimmunotherapeutic and diagnostic antibodies: an inside-out view Nucl. Med. Biol. 34, 757-78
    • (2007) Nucl. Med. Biol. , vol.34 , pp. 757-778
    • Boswell, C.A.1    Brechbiel, M.W.2
  • 19
    • 49449114385 scopus 로고    scopus 로고
    • Antibody-drug conjugates ace the tolerability test
    • Damle, N. K. (2008) Antibody-drug conjugates ace the tolerability test Nat. Biotechnol. 26, 884-5
    • (2008) Nat. Biotechnol. , vol.26 , pp. 884-885
    • Damle, N.K.1
  • 20
    • 0038500962 scopus 로고    scopus 로고
    • Interactions of diethylenetriaminepentaacetic acid (dtpa) and triethylenetetraaminehexaacetic acid (ttha) with major components of natural waters
    • De Stefano, C., Gianguzza, A., Piazzese, D., and Sammartano, S. (2003) Interactions of diethylenetriaminepentaacetic acid (dtpa) and triethylenetetraaminehexaacetic acid (ttha) with major components of natural waters Anal. Bioanal. Chem. 375, 956-67
    • (2003) Anal. Bioanal. Chem. , vol.375 , pp. 956-967
    • De Stefano, C.1    Gianguzza, A.2    Piazzese, D.3    Sammartano, S.4
  • 21
    • 0032650747 scopus 로고    scopus 로고
    • 2 (n = 2-10) in NaCl aqueous solution at different ionic strengths
    • 2 (n = 2-10) in NaCl aqueous solution at different ionic strengths J. Chem. Eng. Data 44, 735-738
    • (1999) J. Chem. Eng. Data , vol.44 , pp. 735-738
    • Cascio, S.1    De Robertis, A.2    Foti, C.3
  • 22
    • 0032440019 scopus 로고    scopus 로고
    • Improving monoclonal antibody pharmacokinetics via chemical modification
    • Sharifi, J., Khawli, L. A., Hornick, J. L., and Epstein, A. L. (1998) Improving monoclonal antibody pharmacokinetics via chemical modification Q. J. Nucl. Med. 42, 242-9
    • (1998) Q. J. Nucl. Med. , vol.42 , pp. 242-249
    • Sharifi, J.1    Khawli, L.A.2    Hornick, J.L.3    Epstein, A.L.4
  • 24
    • 0032904706 scopus 로고    scopus 로고
    • Pharmacokinetics and organ distribution of cationized colchicine-specific IgG and Fab fragments in rat
    • Hong, G., Bazin-Redureau, M. I., and Scherrmann, J. M. (1999) Pharmacokinetics and organ distribution of cationized colchicine-specific IgG and Fab fragments in rat J. Pharm. Sci. 88, 147-53
    • (1999) J. Pharm. Sci. , vol.88 , pp. 147-153
    • Hong, G.1    Bazin-Redureau, M.I.2    Scherrmann, J.M.3
  • 25
    • 0029092948 scopus 로고
    • 125I-labeled cationized monoclonal antibody against β-amyloid in mouse and dog
    • 125I-labeled cationized monoclonal antibody against β-amyloid in mouse and dog Drug Delivery 2, 128-135
    • (1995) Drug Delivery , vol.2 , pp. 128-135
    • Bickel, U.1    Lee, V.M.Y.2    Pardridge, W.M.3
  • 26
    • 0029873942 scopus 로고    scopus 로고
    • Cationized hyperimmune immunoglobulins: Pharmacokinetics, toxicity evaluation and treatment of human immunodeficiency virus-infected human-peripheral blood lymphocytes-severe combined immune deficiency mice
    • Pardridge, W. M., Kang, Y. S., Diagne, A., and Zack, J. A. (1996) Cationized hyperimmune immunoglobulins: pharmacokinetics, toxicity evaluation and treatment of human immunodeficiency virus-infected human-peripheral blood lymphocytes-severe combined immune deficiency mice J. Pharmacol. Exp. Ther. 276, 246-52
    • (1996) J. Pharmacol. Exp. Ther. , vol.276 , pp. 246-252
    • Pardridge, W.M.1    Kang, Y.S.2    Diagne, A.3    Zack, J.A.4
  • 27
    • 0029115713 scopus 로고
    • Enhanced cellular uptake and in vivo biodistribution of a monoclonal antibody following cationization
    • Pardridge, W. M., Kang, Y. S., Yang, J., and Buciak, J. L. (1995) Enhanced cellular uptake and in vivo biodistribution of a monoclonal antibody following cationization J. Pharm. Sci. 84, 943-8
    • (1995) J. Pharm. Sci. , vol.84 , pp. 943-948
    • Pardridge, W.M.1    Kang, Y.S.2    Yang, J.3    Buciak, J.L.4
  • 28
    • 0031869867 scopus 로고    scopus 로고
    • Enhanced endocytosis in cultured human breast carcinoma cells and in vivo biodistribution in rats of a humanized monoclonal antibody after cationization of the protein
    • Pardridge, W. M., Buciak, J., Yang, J., and Wu, D. (1998) Enhanced endocytosis in cultured human breast carcinoma cells and in vivo biodistribution in rats of a humanized monoclonal antibody after cationization of the protein J. Pharmacol. Exp. Ther. 286, 548-54
    • (1998) J. Pharmacol. Exp. Ther. , vol.286 , pp. 548-554
    • Pardridge, W.M.1    Buciak, J.2    Yang, J.3    Wu, D.4
  • 29
    • 0034114282 scopus 로고    scopus 로고
    • Vascular permeability in a human tumour xenograft: Molecular charge dependence
    • Dellian, M., Yuan, F., Trubetskoy, V. S., Torchilin, V. P., and Jain, R. K. (2000) Vascular permeability in a human tumour xenograft: molecular charge dependence Br. J. Cancer 82, 1513-8
    • (2000) Br. J. Cancer , vol.82 , pp. 1513-1518
    • Dellian, M.1    Yuan, F.2    Trubetskoy, V.S.3    Torchilin, V.P.4    Jain, R.K.5
  • 30
    • 0037908924 scopus 로고    scopus 로고
    • Monoclonal antibody radiopharmaceuticals: Cationization, pegylation, radiometal chelation, pharmacokinetics, and tumor imaging
    • Lee, H. J. and Pardridge, W. M. (2003) Monoclonal antibody radiopharmaceuticals: cationization, pegylation, radiometal chelation, pharmacokinetics, and tumor imaging Bioconjugate Chem. 14, 546-53
    • (2003) Bioconjugate Chem. , vol.14 , pp. 546-553
    • Lee, H.J.1    Pardridge, W.M.2
  • 31
    • 0021949366 scopus 로고
    • Endocytic uptake, transport, and catabolism of proteins by epithelial cells
    • Wall, D. A. and Maack, T. (1985) Endocytic uptake, transport, and catabolism of proteins by epithelial cells Am. J. Physiol. 248, C12-20
    • (1985) Am. J. Physiol. , vol.248 , pp. 12-20
    • Wall, D.A.1    Maack, T.2
  • 32
    • 0005849853 scopus 로고
    • Degradation of cationized low density lipoprotein and regulation of cholesterol metabolism in homozygous familial hypercholesterolemia fibroblasts
    • Basu, S. K., Goldstein, J. L., Anderson, G. W., and Brown, M. S. (1976) Degradation of cationized low density lipoprotein and regulation of cholesterol metabolism in homozygous familial hypercholesterolemia fibroblasts Proc. Natl. Acad. Sci. U.S.A. 73, 3178-82
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 3178-3182
    • Basu, S.K.1    Goldstein, J.L.2    Anderson, G.W.3    Brown, M.S.4
  • 33
    • 0011766331 scopus 로고
    • Conjugation of poly-L-lysine to albumin and horseradish peroxidase: A novel method of enhancing the cellular uptake of proteins
    • Shen, W. C. and Ryser, H. J. (1978) Conjugation of poly-L-lysine to albumin and horseradish peroxidase: a novel method of enhancing the cellular uptake of proteins Proc. Natl. Acad. Sci. U.S.A. 75, 1872-6
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 1872-1876
    • Shen, W.C.1    Ryser, H.J.2
  • 34
    • 0024390069 scopus 로고
    • Ultracytochemical characterization of anionic sites in the wall of brain capillaries
    • Vorbrodt, A. W. (1989) Ultracytochemical characterization of anionic sites in the wall of brain capillaries J. Neurocytol. 18, 359-68
    • (1989) J. Neurocytol. , vol.18 , pp. 359-368
    • Vorbrodt, A.W.1
  • 35
    • 0028091458 scopus 로고
    • Cationization of a monoclonal antibody to the human immunodeficiency virus REV protein enhances cellular uptake but does not impair antigen binding of the antibody
    • Pardridge, W. M., Bickel, U., Buciak, J., Yang, J., Diagne, A., and Aepinus, C. (1994) Cationization of a monoclonal antibody to the human immunodeficiency virus REV protein enhances cellular uptake but does not impair antigen binding of the antibody Immunol. Lett. 42, 191-5
    • (1994) Immunol. Lett. , vol.42 , pp. 191-195
    • Pardridge, W.M.1    Bickel, U.2    Buciak, J.3    Yang, J.4    Diagne, A.5    Aepinus, C.6
  • 36
    • 0001120209 scopus 로고
    • Blood-brain barrier transport of cationized immunoglobulin G: Enhanced delivery compared to native protein
    • Triguero, D., Buciak, J. B., Yang, J., and Pardridge, W. M. (1989) Blood-brain barrier transport of cationized immunoglobulin G: enhanced delivery compared to native protein Proc. Natl. Acad. Sci. U.S.A. 86, 4761-5
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 4761-4765
    • Triguero, D.1    Buciak, J.B.2    Yang, J.3    Pardridge, W.M.4
  • 37
    • 0027423126 scopus 로고
    • Activation of human platelets by immune complexes prepared with cationized human IgG
    • Schattner, M., Lazzari, M., Trevani, A. S., Malchiodi, E., Kempfer, A. C., Isturiz, M. A., and Geffner, J. R. (1993) Activation of human platelets by immune complexes prepared with cationized human IgG Blood 82, 3045-51 (Pubitemid 23334931)
    • (1993) Blood , vol.82 , Issue.10 , pp. 3045-3051
    • Schattner, M.1    Lazzari, M.2    Trevani, A.S.3    Malchiodi, E.4    Kempfer, A.C.5    Isturiz, M.A.6    Geffner, J.R.7
  • 38
    • 0018841815 scopus 로고
    • Determination of net ionic charge on Tc-99m DTPA and Tc-99m EDTA by a column ion-exchange method
    • Russell, C. D., Crittenden, R. C., and Cash, A. G. (1980) Determination of net ionic charge on Tc-99m DTPA and Tc-99m EDTA by a column ion-exchange method J. Nucl. Med. 21, 354-60
    • (1980) J. Nucl. Med. , vol.21 , pp. 354-360
    • Russell, C.D.1    Crittenden, R.C.2    Cash, A.G.3
  • 39
    • 1542328068 scopus 로고    scopus 로고
    • Comparative in vivo stability of copper-64-labeled cross-bridged and conventional tetraazamacrocyclic complexes
    • Boswell, C. A., Sun, X., Niu, W., Weisman, G. R., Wong, E. H., Rheingold, A. L., and Anderson, C. J. (2004) Comparative in vivo stability of copper-64-labeled cross-bridged and conventional tetraazamacrocyclic complexes J. Med. Chem. 47, 1465-74
    • (2004) J. Med. Chem. , vol.47 , pp. 1465-1474
    • Boswell, C.A.1    Sun, X.2    Niu, W.3    Weisman, G.R.4    Wong, E.H.5    Rheingold, A.L.6    Anderson, C.J.7
  • 40
    • 0038752102 scopus 로고    scopus 로고
    • Polyclonal antibodies to xenogeneic endothelial cells induce apoptosis and block support of tumor growth in mice
    • Scappaticci, F. A., Contreras, A., Boswell, C. A., Lewis, J. S., and Nolan, G. (2003) Polyclonal antibodies to xenogeneic endothelial cells induce apoptosis and block support of tumor growth in mice Vaccine 21, 2667-77
    • (2003) Vaccine , vol.21 , pp. 2667-2677
    • Scappaticci, F.A.1    Contreras, A.2    Boswell, C.A.3    Lewis, J.S.4    Nolan, G.5
  • 41
    • 33845644587 scopus 로고    scopus 로고
    • Effect of succinylation of antibodies on their conformation and interaction with the antigen
    • Ali, J. and Younus, H. (2006) Effect of succinylation of antibodies on their conformation and interaction with the antigen Biochemistry (Mosc.) 71, 1336-40
    • (2006) Biochemistry (Mosc.) , vol.71 , pp. 1336-1340
    • Ali, J.1    Younus, H.2
  • 43
    • 33745834770 scopus 로고    scopus 로고
    • Validation of a novel CHX-A" derivative suitable for peptide conjugation: Small animal PET/CT imaging using yttrium-86-CHX-A"-octreotide
    • Clifford, T., Boswell, C. A., Biddlecombe, G. B., Lewis, J. S., and Brechbiel, M. W. (2006) Validation of a novel CHX-A" derivative suitable for peptide conjugation: small animal PET/CT imaging using yttrium-86-CHX- A"-octreotide J. Med. Chem. 49, 4297-304
    • (2006) J. Med. Chem. , vol.49 , pp. 4297-4304
    • Clifford, T.1    Boswell, C.A.2    Biddlecombe, G.B.3    Lewis, J.S.4    Brechbiel, M.W.5
  • 44
    • 0027255595 scopus 로고
    • Quality control of protein and peptide drugs: Monoclonal antibodies and some biological response modifiers derived by recombinant DNA technology
    • Geerligs, I. E. J., Beijnen, J. H., Bekers, O., and Underberg, W. J. M. (1993) Quality control of protein and peptide drugs: Monoclonal antibodies and some biological response modifiers derived by recombinant DNA technology Drug Dev. Ind. Pharm. 19, 33-84
    • (1993) Drug Dev. Ind. Pharm. , vol.19 , pp. 33-84
    • Geerligs, I.E.J.1    Beijnen, J.H.2    Bekers, O.3    Underberg, W.J.M.4
  • 46
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • Varki, A. (2008) Sialic acids in human health and disease Trends Mol. Med. 14, 351-60
    • (2008) Trends Mol. Med. , vol.14 , pp. 351-360
    • Varki, A.1
  • 47
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • Belting, M. (2003) Heparan sulfate proteoglycan as a plasma membrane carrier Trends Biochem. Sci. 28, 145-51
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 145-151
    • Belting, M.1
  • 48
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and many functions
    • Hardingham, T. E. and Fosang, A. J. (1992) Proteoglycans: many forms and many functions Faseb J. 6, 861-70
    • (1992) Faseb J. , vol.6 , pp. 861-670
    • Hardingham, T.E.1    Fosang, A.J.2
  • 50
    • 46149103169 scopus 로고    scopus 로고
    • The role of the extracellular matrix in tissue distribution of macromolecules in normal and pathological tissues: Potential therapeutic consequences
    • Wiig, H., Gyenge, C., Iversen, P. O., Gullberg, D., and Tenstad, O. (2008) The role of the extracellular matrix in tissue distribution of macromolecules in normal and pathological tissues: potential therapeutic consequences Microcirculation 15, 283-96
    • (2008) Microcirculation , vol.15 , pp. 283-296
    • Wiig, H.1    Gyenge, C.2    Iversen, P.O.3    Gullberg, D.4    Tenstad, O.5
  • 51
    • 0029998012 scopus 로고    scopus 로고
    • Modification of antibody isoelectric point affects biodistribution of 111-indium-labeled antibody
    • Gangopadhyay, A., Petrick, A. T., and Thomas, P. (1996) Modification of antibody isoelectric point affects biodistribution of 111-indium-labeled antibody Nucl. Med. Biol. 23, 257-61
    • (1996) Nucl. Med. Biol. , vol.23 , pp. 257-261
    • Gangopadhyay, A.1    Petrick, A.T.2    Thomas, P.3
  • 53
    • 0036226357 scopus 로고    scopus 로고
    • Pharmacokinetic analysis of in vivo disposition of succinylated proteins targeted to liver nonparenchymal cells via scavenger receptors: Importance of molecular size and negative charge density for in vivo recognition by receptors
    • Yamasaki, Y., Sumimoto, K., Nishikawa, M., Yamashita, F., Yamaoka, K., Hashida, M., and Takakura, Y. (2002) Pharmacokinetic analysis of in vivo disposition of succinylated proteins targeted to liver nonparenchymal cells via scavenger receptors: importance of molecular size and negative charge density for in vivo recognition by receptors J. Pharmacol. Exp. Ther. 301, 467-77
    • (2002) J. Pharmacol. Exp. Ther. , vol.301 , pp. 467-477
    • Yamasaki, Y.1    Sumimoto, K.2    Nishikawa, M.3    Yamashita, F.4    Yamaoka, K.5    Hashida, M.6    Takakura, Y.7
  • 54
    • 37149051582 scopus 로고    scopus 로고
    • Internalization, intracellular trafficking, and biodistribution of monoclonal antibody 806: A novel anti-epidermal growth factor receptor antibody
    • Perera, R. M., Zoncu, R., Johns, T. G., Pypaert, M., Lee, F. T., Mellman, I., Old, L. J., Toomre, D. K., and Scott, A. M. (2007) Internalization, intracellular trafficking, and biodistribution of monoclonal antibody 806: a novel anti-epidermal growth factor receptor antibody Neoplasia 9, 1099-110
    • (2007) Neoplasia , vol.9 , pp. 1099-1110
    • Perera, R.M.1    Zoncu, R.2    Johns, T.G.3    Pypaert, M.4    Lee, F.T.5    Mellman, I.6    Old, L.J.7    Toomre, D.K.8    Scott, A.M.9
  • 56
    • 0344420226 scopus 로고    scopus 로고
    • Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates
    • Caliceti, P. and Veronese, F. M. (2003) Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates Adv. Drug Delivery Rev. 55, 1261-77
    • (2003) Adv. Drug Delivery Rev. , vol.55 , pp. 1261-1277
    • Caliceti, P.1    Veronese, F.M.2
  • 57
    • 0037124466 scopus 로고    scopus 로고
    • PEGylated antibodies and antibody fragments for improved therapy: A review
    • Chapman, A. P. (2002) PEGylated antibodies and antibody fragments for improved therapy: a review Adv. Drug Delivery Rev. 54, 531-45
    • (2002) Adv. Drug Delivery Rev. , vol.54 , pp. 531-545
    • Chapman, A.P.1
  • 58
    • 0036381439 scopus 로고    scopus 로고
    • Pharmacokinetic characteristics and biodistribution of radioiodinated chimeric TNT-1, -2, and -3 monoclonal antibodies after chemical modification with biotin
    • Khawli, L. A., Mizokami, M. M., Sharifi, J., Hu, P., and Epstein, A. L. (2002) Pharmacokinetic characteristics and biodistribution of radioiodinated chimeric TNT-1, -2, and -3 monoclonal antibodies after chemical modification with biotin Cancer Biother. Radiopharm. 17, 359-70
    • (2002) Cancer Biother. Radiopharm. , vol.17 , pp. 359-370
    • Khawli, L.A.1    Mizokami, M.M.2    Sharifi, J.3    Hu, P.4    Epstein, A.L.5
  • 60
    • 0029776847 scopus 로고    scopus 로고
    • Improved tumor localization and radioimaging with chemically modified monoclonal antibodies
    • Khawli, L. A., Glasky, M. S., Alauddin, M. M., and Epstein, A. L. (1996) Improved tumor localization and radioimaging with chemically modified monoclonal antibodies Cancer Biother. Radiopharm. 11, 203-15
    • (1996) Cancer Biother. Radiopharm. , vol.11 , pp. 203-215
    • Khawli, L.A.1    Glasky, M.S.2    Alauddin, M.M.3    Epstein, A.L.4
  • 61
    • 0029927482 scopus 로고    scopus 로고
    • Abnormally short serum half-lives of IgG in beta 2-microglobulin- deficient mice
    • Ghetie, V., Hubbard, J. G., Kim, J. K., Tsen, M. F., Lee, Y., and Ward, E. S. (1996) Abnormally short serum half-lives of IgG in beta 2-microglobulin-deficient mice Eur. J. Immunol. 26, 690-6
    • (1996) Eur. J. Immunol. , vol.26 , pp. 690-696
    • Ghetie, V.1    Hubbard, J.G.2    Kim, J.K.3    Tsen, M.F.4    Lee, Y.5    Ward, E.S.6
  • 62
    • 0029856774 scopus 로고    scopus 로고
    • Increased clearance of IgG in mice that lack beta 2-microglobulin: Possible protective role of FcRn
    • Israel, E. J., Wilsker, D. F., Hayes, K. C., Schoenfeld, D., and Simister, N. E. (1996) Increased clearance of IgG in mice that lack beta 2-microglobulin: possible protective role of FcRn Immunology 89, 573-8
    • (1996) Immunology , vol.89 , pp. 573-578
    • Israel, E.J.1    Wilsker, D.F.2    Hayes, K.C.3    Schoenfeld, D.4    Simister, N.E.5
  • 63
    • 0029891262 scopus 로고    scopus 로고
    • The protection receptor for IgG catabolism is the beta2-microglobulin- containing neonatal intestinal transport receptor
    • Junghans, R. P. and Anderson, C. L. (1996) The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor Proc. Natl. Acad. Sci. U.S.A. 93, 5512-6
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 64
    • 33845364560 scopus 로고    scopus 로고
    • Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: Potential application in humorally mediated autoimmune disease
    • Petkova, S. B., Akilesh, S., Sproule, T. J., Christianson, G. J., Al Khabbaz, H., Brown, A. C., Presta, L. G., Meng, Y. G., and Roopenian, D. C. (2006) Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: potential application in humorally mediated autoimmune disease Int. Immunol. 18, 1759-69
    • (2006) Int. Immunol. , vol.18 , pp. 1759-1769
    • Petkova, S.B.1    Akilesh, S.2    Sproule, T.J.3    Christianson, G.J.4    Al Khabbaz, H.5    Brown, A.C.6    Presta, L.G.7    Meng, Y.G.8    Roopenian, D.C.9
  • 65
    • 0842304936 scopus 로고    scopus 로고
    • Minimizing the immunogenicity of protein therapeutics
    • Chirino, A. J., Ary, M. L., and Marshall, S. A. (2004) Minimizing the immunogenicity of protein therapeutics Drug Discovery Today 9, 82-90
    • (2004) Drug Discovery Today , vol.9 , pp. 82-90
    • Chirino, A.J.1    Ary, M.L.2    Marshall, S.A.3
  • 66
    • 17644378667 scopus 로고    scopus 로고
    • Immunogenicity of engineered antibodies
    • Hwang, W. Y. and Foote, J. (2005) Immunogenicity of engineered antibodies Methods 36, 3-10
    • (2005) Methods , vol.36 , pp. 3-10
    • Hwang, W.Y.1    Foote, J.2
  • 67
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • Carter, P. J. (2006) Potent antibody therapeutics by design Nat. Rev. Immunol. 6, 343-57
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 343-357
    • Carter, P.J.1
  • 68
    • 0038476357 scopus 로고    scopus 로고
    • Immunogenicity of therapeutic monoclonal antibodies
    • Pendley, C., Schantz, A., and Wagner, C. (2003) Immunogenicity of therapeutic monoclonal antibodies Curr. Opin. Mol. Ther. 5, 172-9
    • (2003) Curr. Opin. Mol. Ther. , vol.5 , pp. 172-179
    • Pendley, C.1    Schantz, A.2    Wagner, C.3
  • 69
    • 43149096699 scopus 로고    scopus 로고
    • Immunogenicity of iodine 131 chimeric tumor necrosis therapy monoclonal antibody in advanced lung cancer patients
    • Wang, H., Cao, C., Li, B., Chen, S., Yin, J., Shi, J., Ye, D., Tao, Q., Hu, P., Epstein, A., and Ju, D. (2008) Immunogenicity of iodine 131 chimeric tumor necrosis therapy monoclonal antibody in advanced lung cancer patients Cancer Immunol. Immunother. 57, 677-84
    • (2008) Cancer Immunol. Immunother. , vol.57 , pp. 677-684
    • Wang, H.1    Cao, C.2    Li, B.3    Chen, S.4    Yin, J.5    Shi, J.6    Ye, D.7    Tao, Q.8    Hu, P.9    Epstein, A.10    Ju, D.11
  • 70
    • 3242708910 scopus 로고    scopus 로고
    • Monte Carlo simulations of antibody adsorption and orientation on charged surfaces
    • Zhou, J., Tsao, H. K., Sheng, Y. J., and Jiang, S. (2004) Monte Carlo simulations of antibody adsorption and orientation on charged surfaces J. Chem. Phys. 121, 1050-7
    • (2004) J. Chem. Phys. , vol.121 , pp. 1050-1057
    • Zhou, J.1    Tsao, H.K.2    Sheng, Y.J.3    Jiang, S.4
  • 71
    • 0033953746 scopus 로고    scopus 로고
    • Single amino acid substitution in the Fc region of chimeric TNT-3 antibody accelerates clearance and improves immunoscintigraphy of solid tumors
    • Hornick, J. L., Sharifi, J., Khawli, L. A., Hu, P., Bai, W. G., Alauddin, M. M., Mizokami, M. M., and Epstein, A. L. (2000) Single amino acid substitution in the Fc region of chimeric TNT-3 antibody accelerates clearance and improves immunoscintigraphy of solid tumors J. Nucl. Med. 41, 355-62
    • (2000) J. Nucl. Med. , vol.41 , pp. 355-362
    • Hornick, J.L.1    Sharifi, J.2    Khawli, L.A.3    Hu, P.4    Bai, W.G.5    Alauddin, M.M.6    Mizokami, M.M.7    Epstein, A.L.8
  • 72
    • 0030881215 scopus 로고    scopus 로고
    • Electric charge influence of dextran derivatives on their tumor accumulation after intravenous injection
    • Tabata, Y., Kawai, T., Murakami, Y., and Ikada, Y. (1997) Electric charge influence of dextran derivatives on their tumor accumulation after intravenous injection Drug Delivery 4, 213-221
    • (1997) Drug Delivery , vol.4 , pp. 213-221
    • Tabata, Y.1    Kawai, T.2    Murakami, Y.3    Ikada, Y.4
  • 73
    • 0029150245 scopus 로고
    • Vascular permeability in a human tumor xenograft: Molecular size dependence and cutoff size
    • Yuan, F., Dellian, M., Fukumura, D., Leunig, M., Berk, D. A., Torchilin, V. P., and Jain, R. K. (1995) Vascular permeability in a human tumor xenograft: molecular size dependence and cutoff size Cancer Res. 55, 3752-6
    • (1995) Cancer Res. , vol.55 , pp. 3752-3756
    • Yuan, F.1    Dellian, M.2    Fukumura, D.3    Leunig, M.4    Berk, D.A.5    Torchilin, V.P.6    Jain, R.K.7
  • 74
    • 42149122041 scopus 로고    scopus 로고
    • Properties of the glomerular barrier and mechanisms of proteinuria
    • Haraldsson, B., Nystrom, J., and Deen, W. M. (2008) Properties of the glomerular barrier and mechanisms of proteinuria Physiol. Rev. 88, 451-87
    • (2008) Physiol. Rev. , vol.88 , pp. 451-487
    • Haraldsson, B.1    Nystrom, J.2    Deen, W.M.3
  • 78
    • 24744450185 scopus 로고    scopus 로고
    • Penetratin improves tumor retention of single-chain antibodies: A novel step toward optimization of radioimmunotherapy of solid tumors
    • Jain, M., Chauhan, S. C., Singh, A. P., Venkatraman, G., Colcher, D., and Batra, S. K. (2005) Penetratin improves tumor retention of single-chain antibodies: a novel step toward optimization of radioimmunotherapy of solid tumors Cancer Res. 65, 7840-6
    • (2005) Cancer Res. , vol.65 , pp. 7840-7846
    • Jain, M.1    Chauhan, S.C.2    Singh, A.P.3    Venkatraman, G.4    Colcher, D.5    Batra, S.K.6
  • 79
    • 0036891467 scopus 로고    scopus 로고
    • An antibody-calmodulin fusion protein reveals a functional dependence between macromolecular isoelectric point and tumor targeting performance
    • Melkko, S., Halin, C., Borsi, L., Zardi, L., and Neri, D. (2002) An antibody-calmodulin fusion protein reveals a functional dependence between macromolecular isoelectric point and tumor targeting performance Int. J. Radiat. Oncol. Biol. Phys. 54, 1485-90
    • (2002) Int. J. Radiat. Oncol. Biol. Phys. , vol.54 , pp. 1485-1490
    • Melkko, S.1    Halin, C.2    Borsi, L.3    Zardi, L.4    Neri, D.5
  • 80
    • 0028819845 scopus 로고
    • Evidence that cell surface charge reduction modifes capillary red cell velocity-flux relationships in hamster cremaster muscle
    • Vink, H., Wieringa, P. A., and Spaan, J. A. (1995) Evidence that cell surface charge reduction modifes capillary red cell velocity-flux relationships in hamster cremaster muscle J. Physiol. 489 (Pt 1) 193-201
    • (1995) J. Physiol. , vol.489 , Issue.PART 1 , pp. 193-201
    • Vink, H.1    Wieringa, P.A.2    Spaan, J.A.3
  • 81
    • 29244484446 scopus 로고    scopus 로고
    • Effect of hydration on interstitial distribution of charged albumin in rat dermis in vitro
    • Wiig, H., Tenstad, O., and Bert, J. L. (2005) Effect of hydration on interstitial distribution of charged albumin in rat dermis in vitro J. Physiol. 569, 631-41
    • (2005) J. Physiol. , vol.569 , pp. 631-641
    • Wiig, H.1    Tenstad, O.2    Bert, J.L.3
  • 82
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins: The concept of specificity
    • Kreuger, J., Spillmann, D., Li, J. P., and Lindahl, U. (2006) Interactions between heparan sulfate and proteins: the concept of specificity J. Cell Biol. 174, 323-7
    • (2006) J. Cell Biol. , vol.174 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.P.3    Lindahl, U.4
  • 83
    • 0035019594 scopus 로고    scopus 로고
    • Interstitial exclusion of positively and negatively charged IgG in rat skin and muscle
    • Wiig, H. and Tenstad, O. (2001) Interstitial exclusion of positively and negatively charged IgG in rat skin and muscle Am. J. Physiol. Heart Circ. Physiol. 280, H1505-12
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.280 , pp. 1505-1512
    • Wiig, H.1    Tenstad, O.2
  • 84
    • 0242558882 scopus 로고    scopus 로고
    • In vivo determination of steric and electrostatic exclusion of albumin in rat skin and skeletal muscle
    • Gyenge, C. C., Tenstad, O., and Wiig, H. (2003) In vivo determination of steric and electrostatic exclusion of albumin in rat skin and skeletal muscle J. Physiol. 552, 907-16
    • (2003) J. Physiol. , vol.552 , pp. 907-916
    • Gyenge, C.C.1    Tenstad, O.2    Wiig, H.3
  • 85
    • 0347503515 scopus 로고    scopus 로고
    • Intersitial exluded volumes: The effect of charge
    • Taylor, A. E. and Parker, J. C. (2003) Intersitial exluded volumes: the effect of charge J. Physiol. 553, 333
    • (2003) J. Physiol. , vol.553 , pp. 333
    • Taylor, A.E.1    Parker, J.C.2
  • 86
    • 38149079892 scopus 로고    scopus 로고
    • The role of heparan sulfate in the glomerular basement membrane
    • Morita, H., Yoshimura, A., and Kimata, K. (2008) The role of heparan sulfate in the glomerular basement membrane Kidney Int. 73, 247-8
    • (2008) Kidney Int. , vol.73 , pp. 247-248
    • Morita, H.1    Yoshimura, A.2    Kimata, K.3
  • 89
    • 0021685740 scopus 로고
    • Effect of antibody charge and concentration on deposition of antibody to glomerular basement membrane
    • Madaio, M. P., Salant, D. J., Adler, S., Darby, C., and Couser, W. G. (1984) Effect of antibody charge and concentration on deposition of antibody to glomerular basement membrane Kidney Int. 26, 397-403
    • (1984) Kidney Int. , vol.26 , pp. 397-403
    • Madaio, M.P.1    Salant, D.J.2    Adler, S.3    Darby, C.4    Couser, W.G.5
  • 90
    • 4644240493 scopus 로고    scopus 로고
    • Cationic charge-preferential IgG reabsorption in the renal proximal tubules
    • Takahashi, S., Wada, N., Harada, K., and Nagata, M. (2004) Cationic charge-preferential IgG reabsorption in the renal proximal tubules Kidney Int. 66, 1556-60
    • (2004) Kidney Int. , vol.66 , pp. 1556-1560
    • Takahashi, S.1    Wada, N.2    Harada, K.3    Nagata, M.4
  • 91
    • 0020442197 scopus 로고
    • Tissue distribution of intravenously injected dinitrophenylated human serum albumin. Effects of specific IgG and IgA antibodies
    • Skogh, T. (1982) Tissue distribution of intravenously injected dinitrophenylated human serum albumin. Effects of specific IgG and IgA antibodies Scand. J. Immunol. 16, 465-75
    • (1982) Scand. J. Immunol. , vol.16 , pp. 465-475
    • Skogh, T.1
  • 92
    • 0020683086 scopus 로고
    • Physicochemical properties and blood clearance of human serum albumin conjugated to different extents with dinitrophenyl groups
    • Skogh, T., Stendahl, O., Sundqvist, T., and Edebo, L. (1983) Physicochemical properties and blood clearance of human serum albumin conjugated to different extents with dinitrophenyl groups Int. Arch. Allergy Appl. Immunol. 70, 238-44
    • (1983) Int. Arch. Allergy Appl. Immunol. , vol.70 , pp. 238-244
    • Skogh, T.1    Stendahl, O.2    Sundqvist, T.3    Edebo, L.4
  • 93
    • 0021285491 scopus 로고
    • Surface charge distribution on the endothelial cell of liver sinusoids
    • Ghitescu, L. and Fixman, A. (1984) Surface charge distribution on the endothelial cell of liver sinusoids J. Cell Biol. 99, 639-47
    • (1984) J. Cell Biol. , vol.99 , pp. 639-647
    • Ghitescu, L.1    Fixman, A.2
  • 94
    • 0022341955 scopus 로고
    • Plasma-lymph exchange and interstitial distribution volumes of charged macromolecules in the lung
    • Parker, J. C., Gilchrist, S., and Cartledge, J. T. (1985) Plasma-lymph exchange and interstitial distribution volumes of charged macromolecules in the lung J. Appl. Physiol. 59, 1128-36
    • (1985) J. Appl. Physiol. , vol.59 , pp. 1128-1136
    • Parker, J.C.1    Gilchrist, S.2    Cartledge, J.T.3
  • 95
    • 24944584755 scopus 로고    scopus 로고
    • The interstitial distribution of macromolecules in rat tumours is influenced by the negatively charged matrix components
    • Wiig, H., Gyenge, C. C., and Tenstad, O. (2005) The interstitial distribution of macromolecules in rat tumours is influenced by the negatively charged matrix components J. Physiol. 567, 557-67
    • (2005) J. Physiol. , vol.567 , pp. 557-567
    • Wiig, H.1    Gyenge, C.C.2    Tenstad, O.3
  • 100
    • 0026577463 scopus 로고
    • Characterization of humanized anti-tac monoclonal antibody by traditional separation techniques and capillary electrophoresis
    • Costello, M. A., Woititz, C., De Feo, J., Stremlo, D., Wen, L.-F. L., Palling, D. J., Iqbal, K., and Guzman, N. A. (1992) Characterization of humanized anti-tac monoclonal antibody by traditional separation techniques and capillary electrophoresis J. Liquid Chromatogr. 15, 1081-1097
    • (1992) J. Liquid Chromatogr. , vol.15 , pp. 1081-1097
    • Costello, M.A.1    Woititz, C.2    De Feo, J.3    Stremlo, D.4    Wen, L.-F.L.5    Palling, D.J.6    Iqbal, K.7    Guzman, N.A.8
  • 101
    • 0030582305 scopus 로고    scopus 로고
    • Capillary isoelectric focusing and sodium dodecyl sulfate-capillary gel electrophoresis of recombinant humanized monoclonal antibody HER2
    • Hunt, G., Moorhouse, K. G., and Chen, A. B. (1996) Capillary isoelectric focusing and sodium dodecyl sulfate-capillary gel electrophoresis of recombinant humanized monoclonal antibody HER2 J. Chromatogr., A 744, 295-301
    • (1996) J. Chromatogr., A , vol.744 , pp. 295-301
    • Hunt, G.1    Moorhouse, K.G.2    Chen, A.B.3
  • 102
    • 20344369064 scopus 로고    scopus 로고
    • Separation of monoclonal antibody alemtuzumab monomer and dimers using ultrafiltration
    • Wan, Y., Vasan, S., Ghosh, R., Hale, G., and Cui, Z. (2005) Separation of monoclonal antibody alemtuzumab monomer and dimers using ultrafiltration Biotechnol. Bioeng. 90, 422-32
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 422-432
    • Wan, Y.1    Vasan, S.2    Ghosh, R.3    Hale, G.4    Cui, Z.5
  • 103
    • 0033231450 scopus 로고    scopus 로고
    • Characterization of recombinant human monoclonal tissue necrosis factor-alpha antibody using cation-exchange HPLC and capillary isoelectric focusing
    • Santora, L. C., Krull, I. S., and Grant, K. (1999) Characterization of recombinant human monoclonal tissue necrosis factor-alpha antibody using cation-exchange HPLC and capillary isoelectric focusing Anal. Biochem. 275, 98-108
    • (1999) Anal. Biochem. , vol.275 , pp. 98-108
    • Santora, L.C.1    Krull, I.S.2    Grant, K.3
  • 104
    • 38749137344 scopus 로고    scopus 로고
    • Pharmaceutical applications of isoelectric focusing on microchip with imaged UV detection
    • Vlckova, M., Kalman, F., and Schwarz, M. A. (2008) Pharmaceutical applications of isoelectric focusing on microchip with imaged UV detection J. Chromatogr., A 1181, 145-52
    • (2008) J. Chromatogr., A , vol.1181 , pp. 145-152
    • Vlckova, M.1    Kalman, F.2    Schwarz, M.A.3
  • 105
    • 0345426282 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor
    • Moore, J. M., Patapoff, T. W., and Cromwell, M. E. (1999) Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor Biochemistry 38, 13960-7
    • (1999) Biochemistry , vol.38 , pp. 13960-13967
    • Moore, J.M.1    Patapoff, T.W.2    Cromwell, M.E.3
  • 107
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18, 2714-23
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 108
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI: A web-based graphical user interface for CHARMM
    • Jo, S., Kim, T., Iyer, V. G., and Im, W. (2008) CHARMM-GUI: a web-based graphical user interface for CHARMM J. Comput. Chem. 29, 1859-65
    • (2008) J. Comput. Chem. , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.