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Volumn 24, Issue 4, 2009, Pages 318-332

The versatile MHC class I-related FcRn protects IgG and albumin from degradation: Implications for development of new diagnostics and therapeutics

Author keywords

Albumin; Albumin targeting; Genetic fusion; Half life; IgG; Neonatal Fc receptor (FcRn); pH dependent; Recycling

Indexed keywords

ALBUMIN; FC RECEPTOR; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; METHOTREXATE;

EID: 70350438004     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.2133/dmpk.24.318     Document Type: Conference Paper
Times cited : (109)

References (160)
  • 2
    • 0036599564 scopus 로고    scopus 로고
    • Practical aspects of the ligand-binding and enzymatic properties of human serum albumin
    • Kragh-Hansen, U., Chuang, V. T. and Otagiri, M.: Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol. Pharm. Bull., 25: 695-704 (2002).
    • (2002) Biol. Pharm. Bull , vol.25 , pp. 695-704
    • Kragh-Hansen, U.1    Chuang, V.T.2    Otagiri, M.3
  • 3
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M. and Carter, D. C.: Atomic structure and chemistry of human serum albumin. Nature, 358: 209-215 (1992).
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 5
    • 0032720125 scopus 로고    scopus 로고
    • Fatty acid binding to human serum albumin: New insights from crystallographic studies
    • Curry, S., Brick, P. and Franks, N. P.: Fatty acid binding to human serum albumin: new insights from crystallographic studies. Biochim. Biophys. Acta., 1441:, 131-140 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 131-140
    • Curry, S.1    Brick, P.2    Franks, N.P.3
  • 6
    • 0034634370 scopus 로고    scopus 로고
    • Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin
    • Bhattacharya, A. A., Grune, T. and Curry, S.: Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J. Mol. Biol., 303:, 721-732 (2000).
    • (2000) J. Mol. Biol , vol.303 , pp. 721-732
    • Bhattacharya, A.A.1    Grune, T.2    Curry, S.3
  • 7
    • 0014450553 scopus 로고
    • Metabolism of immunoglobulins
    • Waldmann, T. A. and Strober, W.: Metabolism of immunoglobulins. Prog. Allergy., 13: 1-110 (1969).
    • (1969) Prog. Allergy , vol.13 , pp. 1-110
    • Waldmann, T.A.1    Strober, W.2
  • 8
    • 0015327927 scopus 로고
    • The catabolism of human G immunoglobulins of different heavy chain subclasses. 3. The catabolism of heavy chain disease proteins and of Fc fragments of myeloma proteins
    • Spiegelberg, H. L. and Fishkin, B. G.: The catabolism of human G immunoglobulins of different heavy chain subclasses. 3. The catabolism of heavy chain disease proteins and of Fc fragments of myeloma proteins. Clin. Exp. Immunol., 10: 599-607 (1972).
    • (1972) Clin. Exp. Immunol , vol.10 , pp. 599-607
    • Spiegelberg, H.L.1    Fishkin, B.G.2
  • 10
    • 0037415556 scopus 로고    scopus 로고
    • The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan
    • Chaudhury, C., Mehnaz, S., Robinson, J. M., Hayton, W. L., Pearl, D. K., Roopenian, D. C. and Anderson, C. L.: The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan. J. Exp. Med., 197: 315-322 (2003).
    • (2003) J. Exp. Med , vol.197 , pp. 315-322
    • Chaudhury, C.1    Mehnaz, S.2    Robinson, J.M.3    Hayton, W.L.4    Pearl, D.K.5    Roopenian, D.C.6    Anderson, C.L.7
  • 11
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class I- related receptor FcRn
    • Ghetie, V. and Ward, E. S.: Multiple roles for the major histocompatibility complex class I- related receptor FcRn. Annu. Rev. Immunol., 18: 739-766 (2000).
    • (2000) Annu. Rev. Immunol , vol.18 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 12
    • 0014022299 scopus 로고
    • The transmission of immunity from mother to young and the catabolism of immunoglobulins
    • Brambell, F. W.: The transmission of immunity from mother to young and the catabolism of immunoglobulins. Lancet, 2: 1087-1093 (1966).
    • (1966) Lancet , vol.2 , pp. 1087-1093
    • Brambell, F.W.1
  • 13
    • 0342771300 scopus 로고
    • The relative transmission of the fractions of papain hydrolyzed homologous gamma-globulin from the uterine cavity to the foetal circulation in the rabbit
    • Brambell, F. W., Hemmings, W. A., Oakley, C. L. and Porter, R. R.: The relative transmission of the fractions of papain hydrolyzed homologous gamma-globulin from the uterine cavity to the foetal circulation in the rabbit. Proc. R. Soc. Lond. B. Biol. Sci., 151: 478-482 (1960).
    • (1960) Proc. R. Soc. Lond. B. Biol. Sci , vol.151 , pp. 478-482
    • Brambell, F.W.1    Hemmings, W.A.2    Oakley, C.L.3    Porter, R.R.4
  • 14
    • 0013672239 scopus 로고
    • Prenatal and postnatal transmission of passive immunity to young rats
    • Halliday, R.: Prenatal and postnatal transmission of passive immunity to young rats. Proc. R. Soc. Lond. B. Biol. Sci., 144: 427-430 (1955).
    • (1955) Proc. R. Soc. Lond. B. Biol. Sci , vol.144 , pp. 427-430
    • Halliday, R.1
  • 15
    • 0013659206 scopus 로고
    • The absorption of antibodies from immune sera by the gut of the young rat
    • Halliday, R.: The absorption of antibodies from immune sera by the gut of the young rat. Proc. R. Soc. Lond. B. Biol. Sci., 143: 408-413 (1955).
    • (1955) Proc. R. Soc. Lond. B. Biol. Sci , vol.143 , pp. 408-413
    • Halliday, R.1
  • 16
    • 0014018740 scopus 로고
    • Studies in vitro of the passage of serum proteins across the intestinal wall of young rats
    • Bamford, D. R.: Studies in vitro of the passage of serum proteins across the intestinal wall of young rats. Proc. R. Soc. Lond. B. Biol. Sci., 166: 30-45 (1966).
    • (1966) Proc. R. Soc. Lond. B. Biol. Sci , vol.166 , pp. 30-45
    • Bamford, D.R.1
  • 17
    • 0010729381 scopus 로고
    • Factors Controlling Serum Gamma-Globulin Concentration
    • Fahey, J. L. and Robinson, A. G.: Factors Controlling Serum Gamma-Globulin Concentration. J. Exp. Med., 118: 845-868 (1963).
    • (1963) J. Exp. Med , vol.118 , pp. 845-868
    • Fahey, J.L.1    Robinson, A.G.2
  • 18
    • 0000146003 scopus 로고
    • A Theoretical Model Of Gamma-Globulin Catabolism
    • Brambell, F. W., Hemmings, W. A. and Morris, I. G.: A Theoretical Model Of Gamma-Globulin Catabolism. Nature, 203: 1352-1354 (1964).
    • (1964) Nature , vol.203 , pp. 1352-1354
    • Brambell, F.W.1    Hemmings, W.A.2    Morris, I.G.3
  • 19
    • 0024529856 scopus 로고
    • An Fc receptor structurally related to MHC class I antigens
    • Simister, N. E. and Mostov, K. E.: An Fc receptor structurally related to MHC class I antigens. Nature, 337: 184-187 (1989).
    • (1989) Nature , vol.337 , pp. 184-187
    • Simister, N.E.1    Mostov, K.E.2
  • 20
    • 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.: The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor. Proc. Natl. Acad. Sci. USA, 93: 5512-5516 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 21
    • 0030959647 scopus 로고    scopus 로고
    • Ontogenetic development and distribution of antibody transport and Fc receptor mRNA expression in rat intestine
    • Martin, M. G., Wu, S. V. and Walsh, J. H.: Ontogenetic development and distribution of antibody transport and Fc receptor mRNA expression in rat intestine. Dig Dis. Sci., 42: 1062-1069 (1997).
    • (1997) Dig Dis. Sci , vol.42 , pp. 1062-1069
    • Martin, M.G.1    Wu, S.V.2    Walsh, J.H.3
  • 22
    • 0034058526 scopus 로고    scopus 로고
    • Bidirectional transcytosis of IgG by the rat neonatal Fc receptor expressed in a rat kidney cell line: A system to study protein transport across epithelia
    • McCarthy, K. M., Yoong, Y. and Simister, N. E.: Bidirectional transcytosis of IgG by the rat neonatal Fc receptor expressed in a rat kidney cell line: a system to study protein transport across epithelia. J. Cell Sci., 113 (Pt 7): 1277-1285 (2000).
    • (2000) J. Cell Sci , vol.113 , Issue.PART 7 , pp. 1277-1285
    • McCarthy, K.M.1    Yoong, Y.2    Simister, N.E.3
  • 26
    • 39549088649 scopus 로고    scopus 로고
    • Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism
    • Akilesh, S., Christianson, G. J., Roopenian, D. C. and Shaw, A. S.: Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism. J. Immunol., 179: 4580-4588 (2007).
    • (2007) J. Immunol , vol.179 , pp. 4580-4588
    • Akilesh, S.1    Christianson, G.J.2    Roopenian, D.C.3    Shaw, A.S.4
  • 27
    • 0034129672 scopus 로고    scopus 로고
    • The role of the Brambell receptor (FcRB) in liver: Protection of endocytosed immunoglobulin G (IgG) from catabolism in hepatocytes rather than transport of IgG to bile
    • Telleman, P. and Junghans, R. P.: The role of the Brambell receptor (FcRB) in liver: protection of endocytosed immunoglobulin G (IgG) from catabolism in hepatocytes rather than transport of IgG to bile. Immunology, 100: 245-251 (2000).
    • (2000) Immunology , vol.100 , pp. 245-251
    • Telleman, P.1    Junghans, R.P.2
  • 28
    • 0028061347 scopus 로고
    • A major histocompatibility complex class I-like Fc receptor cloned from human placenta: Possible role in transfer of immunoglobulin G from mother to fetus
    • Story, C. M., Mikulska, J. E. and Simister, N. E.: A major histocompatibility complex class I-like Fc receptor cloned from human placenta: possible role in transfer of immunoglobulin G from mother to fetus. J. Exp. Med., 180: 2377-2381 (1994).
    • (1994) J. Exp. Med , vol.180 , pp. 2377-2381
    • Story, C.M.1    Mikulska, J.E.2    Simister, N.E.3
  • 29
    • 0034879134 scopus 로고    scopus 로고
    • The MHC class I-related receptor, FcRn, plays an essential role in the maternofetal transfer of gamma-globulin in humans
    • Firan, M., Bawdon, R., Radu, C., Ober, R. J., Eaken, D., Antohe, F., Ghetie, V. and Ward, E. S.: The MHC class I-related receptor, FcRn, plays an essential role in the maternofetal transfer of gamma-globulin in humans. Int. Immunol., 13: 993-1002 (2001).
    • (2001) Int. Immunol , vol.13 , pp. 993-1002
    • Firan, M.1    Bawdon, R.2    Radu, C.3    Ober, R.J.4    Eaken, D.5    Antohe, F.6    Ghetie, V.7    Ward, E.S.8
  • 31
    • 0026569633 scopus 로고
    • Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules
    • Gastinel, L. N., Simister, N. E. and Bjorkman, P. J.: Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules. Proc. Natl. Acad. Sci. USA, 89: 638-642 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 638-642
    • Gastinel, L.N.1    Simister, N.E.2    Bjorkman, P.J.3
  • 32
    • 0034663798 scopus 로고    scopus 로고
    • Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor
    • West, A. P., Jr. and Bjorkman, P. J.: Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor. Biochemistry, 39: 9698-9708 (2000).
    • (2000) Biochemistry , vol.39 , pp. 9698-9708
    • West Jr., A.P.1    Bjorkman, P.J.2
  • 33
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister, W. P., Huber, A. H. and Bjorkman, P. J.: Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature, 372: 379-383 (1994).
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 34
    • 0028051652 scopus 로고
    • Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor
    • Burmeister, W. P., Gastinel, L. N., Simister, N. E., Blum, M. L. and Bjorkman, P. J.: Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor. Nature, 372: 336-343 (1994).
    • (1994) Nature , vol.372 , pp. 336-343
    • Burmeister, W.P.1    Gastinel, L.N.2    Simister, N.E.3    Blum, M.L.4    Bjorkman, P.J.5
  • 35
    • 0033393536 scopus 로고    scopus 로고
    • Mapping the site on human IgG for binding of the MHC class I-related receptor, FcRn
    • Kim, J. K., Firan, M., Radu, C. G., Kim, C. H., Ghetie, V. and Ward, E. S.: Mapping the site on human IgG for binding of the MHC class I-related receptor, FcRn. Eur. J. Immunol., 29: 2819-2825 (1999).
    • (1999) Eur. J. Immunol , vol.29 , pp. 2819-2825
    • Kim, J.K.1    Firan, M.2    Radu, C.G.3    Kim, C.H.4    Ghetie, V.5    Ward, E.S.6
  • 36
    • 0031093498 scopus 로고    scopus 로고
    • Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1
    • Medesan, C., Matesoi, D., Radu, C., Ghetie, V. and Ward, E. S.: Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1. J. Immunol., 158: 2211-2217 (1997).
    • (1997) J. Immunol , vol.158 , pp. 2211-2217
    • Medesan, C.1    Matesoi, D.2    Radu, C.3    Ghetie, V.4    Ward, E.S.5
  • 37
    • 0030130749 scopus 로고    scopus 로고
    • The stoichiometry and affinity of the interaction of murine Fc fragments with the MHC class I-related receptor, FcRn
    • Popov, S., Hubbard, J. G., Kim, J., Ober, B., Ghetie, V. and Ward, E. S.: The stoichiometry and affinity of the interaction of murine Fc fragments with the MHC class I-related receptor, FcRn. Mol. Immunol., 33: 521-530 (1996).
    • (1996) Mol. Immunol , vol.33 , pp. 521-530
    • Popov, S.1    Hubbard, J.G.2    Kim, J.3    Ober, B.4    Ghetie, V.5    Ward, E.S.6
  • 38
    • 0028808880 scopus 로고
    • Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants
    • Raghavan, M., Bonagura, V. R., Morrison, S. L. and Bjorkman, P. J.: Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants. Biochemistry, 34: 14649-14657 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14649-14657
    • Raghavan, M.1    Bonagura, V.R.2    Morrison, S.L.3    Bjorkman, P.J.4
  • 39
    • 0028467948 scopus 로고
    • Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand
    • Raghavan, M., Chen, M. Y., Gastinel, L. N. and Bjorkman, P. J.: Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand. Immunity, 1: 303-315 (1994).
    • (1994) Immunity , vol.1 , pp. 303-315
    • Raghavan, M.1    Chen, M.Y.2    Gastinel, L.N.3    Bjorkman, P.J.4
  • 40
    • 0027249327 scopus 로고
    • The class I major histocompatibility complex related Fc receptor shows pH-dependent stability differences correlating with immunoglobulin binding and release
    • Raghavan, M., Gastinel, L. N. and Bjorkman, P. J.: The class I major histocompatibility complex related Fc receptor shows pH-dependent stability differences correlating with immunoglobulin binding and release. Biochemistry, 32: 8654-8660 (1993).
    • (1993) Biochemistry , vol.32 , pp. 8654-8660
    • Raghavan, M.1    Gastinel, L.N.2    Bjorkman, P.J.3
  • 41
    • 0032518373 scopus 로고    scopus 로고
    • Structural basis of pH-dependent antibody binding by the neonatal Fc receptor
    • Vaughn, D. E. and Bjorkman, P. J.: Structural basis of pH-dependent antibody binding by the neonatal Fc receptor. Structure, 6: 63-73 (1998).
    • (1998) Structure , vol.6 , pp. 63-73
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 43
    • 33751211517 scopus 로고    scopus 로고
    • The conserved histidine 166 residue of the human neonatal Fc receptor heavy chain is critical for the pH-dependent binding to albumin
    • Andersen, J. T., Dee Qian, J. and Sandlie, I.: The conserved histidine 166 residue of the human neonatal Fc receptor heavy chain is critical for the pH-dependent binding to albumin. Eur. J. Immunol., 36: 3044-3051 (2006).
    • (2006) Eur. J. Immunol , vol.36 , pp. 3044-3051
    • Andersen, J.T.1    Dee Qian, J.2    Sandlie, I.3
  • 49
    • 0842343448 scopus 로고    scopus 로고
    • Visualizing the site and dynamics of IgG salvage by the MHC class I-related receptor, FcRn
    • Ober, R. J., Martinez, C., Vaccaro, C., Zhou, J. and Ward, E. S.: Visualizing the site and dynamics of IgG salvage by the MHC class I-related receptor, FcRn. J. Immunol., 172: 2021-2029 (2004).
    • (2004) J. Immunol , vol.172 , pp. 2021-2029
    • Ober, R.J.1    Martinez, C.2    Vaccaro, C.3    Zhou, J.4    Ward, E.S.5
  • 50
    • 3343010237 scopus 로고    scopus 로고
    • Exocytosis of IgG as mediated by the receptor, FcRn: An analysis at the single-molecule level
    • Ober, R. J., Martinez, C., Lai, X., Zhou, J. andWard, E. S.: Exocytosis of IgG as mediated by the receptor, FcRn: an analysis at the single-molecule level. Proc. Natl. Acad. Sci. USA, 101: 11076-11081 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11076-11081
    • Ober, R.J.1    Martinez, C.2    Lai, X.3    Zhou, J.4    andWard, E.S.5
  • 51
    • 62449200475 scopus 로고    scopus 로고
    • Conditional deletion of the MHC class I-related receptor FcRn reveals the sites of IgG homeostasis in mice
    • Montoyo, H. P., Vaccaro, C., Hafner, M., Ober, R. J., Mueller, W. and Ward, E. S.: Conditional deletion of the MHC class I-related receptor FcRn reveals the sites of IgG homeostasis in mice. Proc. Natl. Acad. Sci. USA, 106: 2788-2793 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2788-2793
    • Montoyo, H.P.1    Vaccaro, C.2    Hafner, M.3    Ober, R.J.4    Mueller, W.5    Ward, E.S.6
  • 54
    • 2942516894 scopus 로고    scopus 로고
    • Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells
    • Yoshida, M., Claypool, S. M., Wagner, J. S., Mizoguchi, E., Mizoguchi, A., Roopenian, D. C., Lencer, W. I. and Blumberg, R. S.: Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells. Immunity, 20: 769-783 (2004).
    • (2004) Immunity , vol.20 , pp. 769-783
    • Yoshida, M.1    Claypool, S.M.2    Wagner, J.S.3    Mizoguchi, E.4    Mizoguchi, A.5    Roopenian, D.C.6    Lencer, W.I.7    Blumberg, R.S.8
  • 55
    • 0037025895 scopus 로고    scopus 로고
    • Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: Functional expression of FcRn in the mammalian lung
    • Spiekermann, G. M., Finn, P. W., Ward, E. S., Dumont, J., Dickinson, B. L., Blumberg, R. S. and Lencer, W. I.: Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: functional expression of FcRn in the mammalian lung. J. Exp. Med., 196: 303-310 (2002).
    • (2002) J. Exp. Med , vol.196 , pp. 303-310
    • Spiekermann, G.M.1    Finn, P.W.2    Ward, E.S.3    Dumont, J.4    Dickinson, B.L.5    Blumberg, R.S.6    Lencer, W.I.7
  • 57
    • 25844528107 scopus 로고    scopus 로고
    • Delivery of an erythropoietin-Fc fusion protein by inhalation in humans through an immunoglobulin transport pathway
    • Dumont, J. A., Bitonti, A. J., Clark, D., Evans, S., Pickford, M. and Newman, S. P.: Delivery of an erythropoietin-Fc fusion protein by inhalation in humans through an immunoglobulin transport pathway. J. Aerosol. Med., 18: 294-303 (2005).
    • (2005) J. Aerosol. Med , vol.18 , pp. 294-303
    • Dumont, J.A.1    Bitonti, A.J.2    Clark, D.3    Evans, S.4    Pickford, M.5    Newman, S.P.6
  • 59
    • 0029842013 scopus 로고    scopus 로고
    • Localization of the site of the IgG molecule that regulates maternofetal transmission in mice
    • Medesan, C., Radu, C., Kim, J. K., Ghetie, V. and Ward, E. S.: Localization of the site of the IgG molecule that regulates maternofetal transmission in mice. Eur. J. Immunol., 26: 2533-2536 (1996).
    • (1996) Eur. J. Immunol , vol.26 , pp. 2533-2536
    • Medesan, C.1    Radu, C.2    Kim, J.K.3    Ghetie, V.4    Ward, E.S.5
  • 60
    • 46149113010 scopus 로고    scopus 로고
    • Infused Fc-tagged beta-glucuronidase crosses the placenta and produces clearance of storage in utero in mucopolysaccharidosis VII mice
    • Grubb, J. H., Vogler, C., Tan, Y., Shah, G. N., MacRae, A. F. and Sly, W. S.: Infused Fc-tagged beta-glucuronidase crosses the placenta and produces clearance of storage in utero in mucopolysaccharidosis VII mice. Proc. Natl. Acad. Sci. USA, 105: 8375-8380 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8375-8380
    • Grubb, J.H.1    Vogler, C.2    Tan, Y.3    Shah, G.N.4    MacRae, A.F.5    Sly, W.S.6
  • 62
    • 33846708242 scopus 로고    scopus 로고
    • Radioiodinated versus radiometal-labeled anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments: Optimal pharmacokinetics for therapy
    • Kenanova, V., Olafsen, T., Williams, L. E., Ruel, N. H., Longmate, J., Yazaki, P. J., Shively, J. E., Colcher, D., Raubitschek, A. A. and Wu, A. M.: Radioiodinated versus radiometal-labeled anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments: optimal pharmacokinetics for therapy. Cancer Res., 67: 718-726 (2007).
    • (2007) Cancer Res , vol.67 , pp. 718-726
    • Kenanova, V.1    Olafsen, T.2    Williams, L.E.3    Ruel, N.H.4    Longmate, J.5    Yazaki, P.J.6    Shively, J.E.7    Colcher, D.8    Raubitschek, A.A.9    Wu, A.M.10
  • 64
    • 33846050957 scopus 로고    scopus 로고
    • Kinetics of FcRn-mediated recycling of IgG and albumin in human: Pathophysiology and therapeutic implications using a simplified mechanism-based model
    • Kim, J., Hayton, W. L., Robinson, J. M. and Anderson, C. L.: Kinetics of FcRn-mediated recycling of IgG and albumin in human: pathophysiology and therapeutic implications using a simplified mechanism-based model. Clin. Immunol., 122: 146-155 (2007).
    • (2007) Clin. Immunol , vol.122 , pp. 146-155
    • Kim, J.1    Hayton, W.L.2    Robinson, J.M.3    Anderson, C.L.4
  • 65
    • 0035210960 scopus 로고    scopus 로고
    • Differences in promiscuity for antibody-FcRn interactions across species: Implications for therapeutic antibodies
    • Ober, R. J., Radu, C. G., Ghetie, V. and Ward, E. S.: Differences in promiscuity for antibody-FcRn interactions across species: implications for therapeutic antibodies. Int. Immunol., 13: 1551-1559 (2001).
    • (2001) Int. Immunol , vol.13 , pp. 1551-1559
    • Ober, R.J.1    Radu, C.G.2    Ghetie, V.3    Ward, E.S.4
  • 67
    • 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.: 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: 1759-1769 (2006).
    • (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
  • 68
    • 49149111627 scopus 로고    scopus 로고
    • Mutations and polymorphisms of the gene of the major human blood protein, serum albumin
    • Minchiotti, L., Galliano, M., Kragh-Hansen, U. and Peters, T., Jr.: Mutations and polymorphisms of the gene of the major human blood protein, serum albumin. Hum. Mutat., 29: 1007-1016 (2008).
    • (2008) Hum. Mutat , vol.29 , pp. 1007-1016
    • Minchiotti, L.1    Galliano, M.2    Kragh-Hansen, U.3    Peters Jr., T.4
  • 69
    • 36649020460 scopus 로고    scopus 로고
    • A Receptor-Mediated Mechanism to Support Clinical Observation of Altered Albumin Variants
    • Andersen, J. T. and Sandlie, I.: A Receptor-Mediated Mechanism to Support Clinical Observation of Altered Albumin Variants. Clinical Chemistry, 53: 2216 (2007).
    • (2007) Clinical Chemistry , vol.53 , pp. 2216
    • Andersen, J.T.1    Sandlie, I.2
  • 70
    • 30744451910 scopus 로고    scopus 로고
    • Purification, properties and extended solution structure of the complex formed between human immunoglobulin A1 and human serum albumin by scattering and ultracentrifugation
    • Almogren, A., Furtado, P. B., Sun, Z., Perkins, S. J. and Kerr, M. A.: Purification, properties and extended solution structure of the complex formed between human immunoglobulin A1 and human serum albumin by scattering and ultracentrifugation. J. Mol. Biol., 356: 413-431 (2006).
    • (2006) J. Mol. Biol , vol.356 , pp. 413-431
    • Almogren, A.1    Furtado, P.B.2    Sun, Z.3    Perkins, S.J.4    Kerr, M.A.5
  • 71
    • 0023214577 scopus 로고
    • Complexes of albumin and alpha 1-antitrypsin with Fc-fragment of IgA monomer are disulfide-bound to penultimate C-terminal cysteine in the C alpha 3-domain
    • Vaerman, J. P., Hagiwara, K., Kobayashi, K. and Rits, M.: Complexes of albumin and alpha 1-antitrypsin with Fc-fragment of IgA monomer are disulfide-bound to penultimate C-terminal cysteine in the C alpha 3-domain. Immunol. Lett., 15: 67-72 (1987).
    • (1987) Immunol. Lett , vol.15 , pp. 67-72
    • Vaerman, J.P.1    Hagiwara, K.2    Kobayashi, K.3    Rits, M.4
  • 72
    • 0017687263 scopus 로고
    • Properties of IgA myeloma proteins isolated rom sera of patients with the hyperviscosity syndrome
    • Mestecky, J., Hammack, W. J., Kulhavy, R., Wright, G. P. and Tomana, M.: Properties of IgA myeloma proteins isolated rom sera of patients with the hyperviscosity syndrome. J. Lab. Clin. Med., 89: 919-927 (1977).
    • (1977) J. Lab. Clin. Med , vol.89 , pp. 919-927
    • Mestecky, J.1    Hammack, W.J.2    Kulhavy, R.3    Wright, G.P.4    Tomana, M.5
  • 73
    • 0036079202 scopus 로고    scopus 로고
    • Expression of the neonatal Fc receptor (FcRn) at the blood-brain barrier
    • Schlachetzki, F., Zhu, C. and Pardridge, W. M.: Expression of the neonatal Fc receptor (FcRn) at the blood-brain barrier. J. Neurochem, 81: 203-206 (2002).
    • (2002) J. Neurochem , vol.81 , pp. 203-206
    • Schlachetzki, F.1    Zhu, C.2    Pardridge, W.M.3
  • 74
    • 2342471420 scopus 로고    scopus 로고
    • The blood-brain barrier: An overview: structure, regulation, and clinical implications
    • Ballabh, P., Braun, A. and Nedergaard, M.: The blood-brain barrier: an overview: structure, regulation, and clinical implications. Neurobiol. Dis., 16: 1-13 (2004).
    • (2004) Neurobiol. Dis , vol.16 , pp. 1-13
    • Ballabh, P.1    Braun, A.2    Nedergaard, M.3
  • 75
    • 0035283233 scopus 로고    scopus 로고
    • Mediated efflux of IgG molecules from brain to blood across the blood-brain barrier
    • Zhang, Y. and Pardridge, W. M.: Mediated efflux of IgG molecules from brain to blood across the blood-brain barrier. J. Neuroimmunol, 114: 168-172 (2001).
    • (2001) J. Neuroimmunol , vol.114 , pp. 168-172
    • Zhang, Y.1    Pardridge, W.M.2
  • 76
    • 30844472909 scopus 로고    scopus 로고
    • IgG-assisted age-dependent clearance of Alzheimer's amyloid beta peptide by the blood-brain barrier neonatal Fc receptor
    • Deane, R., Sagare, A., Hamm, K., Parisi, M., LaRue, B., Guo, H., Wu, Z., Holtzman, D. M. and Zlokovic, B. V.: IgG-assisted age-dependent clearance of Alzheimer's amyloid beta peptide by the blood-brain barrier neonatal Fc receptor. J. Neurosci., 25: 11495-11503 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 11495-11503
    • Deane, R.1    Sagare, A.2    Hamm, K.3    Parisi, M.4    LaRue, B.5    Guo, H.6    Wu, Z.7    Holtzman, D.M.8    Zlokovic, B.V.9
  • 77
    • 33745107170 scopus 로고    scopus 로고
    • Strategies to improve plasma half life time of peptide and protein drugs
    • Werle, M. and Bernkop-Schnurch, A.: Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids, 30: 351-367 (2006).
    • (2006) Amino Acids , vol.30 , pp. 351-367
    • Werle, M.1    Bernkop-Schnurch, A.2
  • 78
    • 54849425126 scopus 로고    scopus 로고
    • Discovering and improving novel peptide therapeutics
    • McGregor, D. P.: Discovering and improving novel peptide therapeutics. Curr. Opin. Pharmacol., 8: 616-619 (2008).
    • (2008) Curr. Opin. Pharmacol , vol.8 , pp. 616-619
    • McGregor, D.P.1
  • 79
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler, G. and Milstein, C.: Continuous cultures of fused cells secreting antibody of predefined specificity. Nature, 256: 495-497 (1975).
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 80
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • Hoogenboom, H. R.: Selecting and screening recombinant antibody libraries. Nat. Biotechnol., 23: 1105-1116 (2005).
    • (2005) Nat. Biotechnol , vol.23 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 81
    • 0037264969 scopus 로고    scopus 로고
    • Therapeutic antibodies for human diseases at the dawn of the twenty-first century
    • Brekke, O. H. and Sandlie, I.: Therapeutic antibodies for human diseases at the dawn of the twenty-first century. Nat. Rev. Drug Discov., 2: 52-62 (2003).
    • (2003) Nat. Rev. Drug Discov , vol.2 , pp. 52-62
    • Brekke, O.H.1    Sandlie, I.2
  • 82
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: Prospects and challenges for immunoconjugates
    • Wu, A. M. and Senter, P. D.: Arming antibodies: prospects and challenges for immunoconjugates. Nat. Biotechnol., 23: 1137-1146 (2005).
    • (2005) Nat. Biotechnol , vol.23 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 83
    • 0034873973 scopus 로고    scopus 로고
    • Monoclonal antibodies in the clinic
    • Reichert, J. M.: Monoclonal antibodies in the clinic. Nat. Biotechnol., 19: 819-822 (2001).
    • (2001) Nat. Biotechnol , vol.19 , pp. 819-822
    • Reichert, J.M.1
  • 84
    • 0021713342 scopus 로고
    • Production of functional chimaeric mouse/human antibody
    • Boulianne, G. L., Hozumi, N. and Shulman, M. J.: Production of functional chimaeric mouse/human antibody. Nature, 312: 643-646 (1984).
    • (1984) Nature , vol.312 , pp. 643-646
    • Boulianne, G.L.1    Hozumi, N.2    Shulman, M.J.3
  • 85
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones, P. T., Dear, P. H., Foote, J., Neuberger, M. S. and Winter, G.: Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature, 321: 522-525 (1986).
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 86
    • 11844275385 scopus 로고    scopus 로고
    • Conferring the binding properties of the mouse MHC class I-related receptor, FcRn, onto the human ortholog by sequential rounds of site-directed mutagenesis
    • Zhou, J., Mateos, F., Ober, R. J. and Ward, E. S.: Conferring the binding properties of the mouse MHC class I-related receptor, FcRn, onto the human ortholog by sequential rounds of site-directed mutagenesis. J. Mol. Biol., 345: 1071-1081 (2005).
    • (2005) J. Mol. Biol , vol.345 , pp. 1071-1081
    • Zhou, J.1    Mateos, F.2    Ober, R.J.3    Ward, E.S.4
  • 87
    • 38549161562 scopus 로고    scopus 로고
    • Fc-based cytokines: Prospects for engineering superior therapeutics
    • Jazayeri, J. A. and Carroll, G. J.: Fc-based cytokines: prospects for engineering superior therapeutics. BioDrugs, 22: 11-26 (2008).
    • (2008) BioDrugs , vol.22 , pp. 11-26
    • Jazayeri, J.A.1    Carroll, G.J.2
  • 88
    • 33744937065 scopus 로고    scopus 로고
    • Monomeric Fc fusions: Impact on pharmacokinetic and biological activity of protein therapeutics
    • Dumont, J. A., Low, S. C., Peters, R. T. and Bitonti, A. J.: Monomeric Fc fusions: impact on pharmacokinetic and biological activity of protein therapeutics. BioDrugs, 20: 151-160 (2006).
    • (2006) BioDrugs , vol.20 , pp. 151-160
    • Dumont, J.A.1    Low, S.C.2    Peters, R.T.3    Bitonti, A.J.4
  • 90
    • 0033012077 scopus 로고    scopus 로고
    • Etanercept, a novel drug for the treatment of patients with severe, active rheumatoid arthritis
    • discussion 71-72
    • Goldenberg, M. M.: Etanercept, a novel drug for the treatment of patients with severe, active rheumatoid arthritis. Clin. Ther., 21: 75-87; discussion 71-72 (1999).
    • (1999) Clin. Ther , vol.21 , pp. 75-87
    • Goldenberg, M.M.1
  • 91
    • 27144465484 scopus 로고    scopus 로고
    • Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels
    • Vaccaro, C., Zhou, J., Ober, R. J. and Ward, E. S.: Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels. Nat. Biotechnol., 23: 1283-1288 (2005).
    • (2005) Nat. Biotechnol , vol.23 , pp. 1283-1288
    • Vaccaro, C.1    Zhou, J.2    Ober, R.J.3    Ward, E.S.4
  • 92
    • 33845484193 scopus 로고    scopus 로고
    • Divergent activities of an engineered antibody in murine and human systems have implications for therapeutic antibodies
    • Vaccaro, C., Bawdon, R., Wanjie, S., Ober, R. J. and Ward, E. S.: Divergent activities of an engineered antibody in murine and human systems have implications for therapeutic antibodies. Proc. Natl. Acad. Sci. USA, 103: 18709-18714 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18709-18714
    • Vaccaro, C.1    Bawdon, R.2    Wanjie, S.3    Ober, R.J.4    Ward, E.S.5
  • 93
    • 71849083999 scopus 로고    scopus 로고
    • Targeting the neonatal fc receptor for antigen delivery using engineered fc fragments
    • Mi, W., Wanjie, S., Lo, S. T., Gan, Z., Pickl-Herk, B., Ober, R. J. and Ward, E. S.: Targeting the neonatal fc receptor for antigen delivery using engineered fc fragments. J. Immunol., 181: 7550-7561 (2008).
    • (2008) J. Immunol , vol.181 , pp. 7550-7561
    • Mi, W.1    Wanjie, S.2    Lo, S.T.3    Gan, Z.4    Pickl-Herk, B.5    Ober, R.J.6    Ward, E.S.7
  • 98
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn)
    • Dall'Acqua, W. F., Kiener, P. A. and Wu, H.: Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn). J. Biol. Chem., 281: 23514-23524 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 23514-23524
    • Dall'Acqua, W.F.1    Kiener, P.A.2    Wu, H.3
  • 99
    • 33845930317 scopus 로고    scopus 로고
    • Humanized IgG1 variants with differential binding properties to the neonatal Fc receptor: Relationship to pharmacokinetics in mice and primates
    • Datta-Mannan, A., Witcher, D. R., Tang, Y., Watkins, J., Jiang, W. and Wroblewski, V. J.: Humanized IgG1 variants with differential binding properties to the neonatal Fc receptor: relationship to pharmacokinetics in mice and primates. Drug Metab. Dispos., 35: 86-94 (2007).
    • (2007) Drug Metab. Dispos , vol.35 , pp. 86-94
    • Datta-Mannan, A.1    Witcher, D.R.2    Tang, Y.3    Watkins, J.4    Jiang, W.5    Wroblewski, V.J.6
  • 100
    • 33847330766 scopus 로고    scopus 로고
    • Monoclonal antibody clearance. Impact of modulating the interaction of IgG with the neonatal Fc receptor
    • Datta-Mannan, A., Witcher, D. R., Tang, Y., Watkins, J. and Wroblewski, V. J.: Monoclonal antibody clearance. Impact of modulating the interaction of IgG with the neonatal Fc receptor. J. Biol. Chem., 282: 1709-1717 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 1709-1717
    • Datta-Mannan, A.1    Witcher, D.R.2    Tang, Y.3    Watkins, J.4    Wroblewski, V.J.5
  • 101
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • Nimmerjahn, F. and Ravetch, J. V.: Anti-inflammatory actions of intravenous immunoglobulin. Annu. Rev. Immunol., 26: 513-533 (2008).
    • (2008) Annu. Rev. Immunol , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 102
    • 0027731524 scopus 로고
    • Elimination of infectious antigens and increase of IgG catabolism as possible modes of action of IVIg
    • Masson, P. L.: Elimination of infectious antigens and increase of IgG catabolism as possible modes of action of IVIg. J. Autoimmun., 6: 683-689 (1993).
    • (1993) J. Autoimmun , vol.6 , pp. 683-689
    • Masson, P.L.1
  • 106
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • Samuelsson, A., Towers, T. L. and Ravetch, J. V.: Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor. Science, 291: 484-486 (2001).
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 107
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • Anthony, R. M., Wermeling, F., Karlsson, M. C. and Ravetch, J. V.: Identification of a receptor required for the anti-inflammatory activity of IVIG. Proc. Natl. Acad. Sci. USA, 105: 19571-19578 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 108
    • 34247094345 scopus 로고    scopus 로고
    • Amelioration of experimental autoimmune myasthenia gravis in rats by neonatal FcR blockade
    • Liu, L., Garcia, A. M., Santoro, H., Zhang, Y., McDonnell, K., Dumont, J. and Bitonti, A.: Amelioration of experimental autoimmune myasthenia gravis in rats by neonatal FcR blockade. J. Immunol., 178: 5390-5398 (2007).
    • (2007) J. Immunol , vol.178 , pp. 5390-5398
    • Liu, L.1    Garcia, A.M.2    Santoro, H.3    Zhang, Y.4    McDonnell, K.5    Dumont, J.6    Bitonti, A.7
  • 109
    • 17744366208 scopus 로고    scopus 로고
    • Pharmacokinetic effects of 4C9, an anti-FcRn antibody, in rats: Implications for the use of FcRn inhibitors for the treatment of humoral autoimmune and alloimmune conditions
    • Getman, K. E. and Balthasar, J. P.: Pharmacokinetic effects of 4C9, an anti-FcRn antibody, in rats: implications for the use of FcRn inhibitors for the treatment of humoral autoimmune and alloimmune conditions. J. Pharm. Sci., 94: 718-729 (2005).
    • (2005) J. Pharm. Sci , vol.94 , pp. 718-729
    • Getman, K.E.1    Balthasar, J.P.2
  • 111
    • 0033911048 scopus 로고    scopus 로고
    • Prevention of systemic lupus erythematosus in MRL/lpr mice by administration of an immunoglobulin-binding peptide
    • Marino, M., Ruvo, M., De Falco, S. and Fassina, G.: Prevention of systemic lupus erythematosus in MRL/lpr mice by administration of an immunoglobulin-binding peptide. Nat. Biotechnol., 18: 735-739 (2000).
    • (2000) Nat. Biotechnol , vol.18 , pp. 735-739
    • Marino, M.1    Ruvo, M.2    De Falco, S.3    Fassina, G.4
  • 112
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano, W. L., Ultsch, M. H., de Vos, A. M. and Wells, J. A.: Convergent solutions to binding at a protein-protein interface. Science, 287: 1279-1283 (2000).
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 114
    • 30344482513 scopus 로고    scopus 로고
    • Kenanova, V. and Wu, A. M.: Tailoring antibodies for radionuclide delivery. Expert Opin. Drug Deliv., 3: 53-70 (2006).
    • Kenanova, V. and Wu, A. M.: Tailoring antibodies for radionuclide delivery. Expert Opin. Drug Deliv., 3: 53-70 (2006).
  • 116
    • 34447520330 scopus 로고    scopus 로고
    • Anticancer carrier-linked prodrugs in clinical trials
    • Kratz, F., Abu Ajaj, K. and Warnecke, A.: Anticancer carrier-linked prodrugs in clinical trials. Expert Opin. Investig. Drugs, 16: 1037-1058 (2007).
    • (2007) Expert Opin. Investig. Drugs , vol.16 , pp. 1037-1058
    • Kratz, F.1    Abu Ajaj, K.2    Warnecke, A.3
  • 117
    • 0036201980 scopus 로고    scopus 로고
    • A phase II trial of methotrexate-human serum albumin (MTX-HSA) in patients with metastatic renal cell carcinoma who progressed under immunotherapy
    • Vis, A. N., van der Gaast, A., van Rhijn, B. W., Catsburg, T. K., Schmidt, C. and Mickisch, G. H.: A phase II trial of methotrexate-human serum albumin (MTX-HSA) in patients with metastatic renal cell carcinoma who progressed under immunotherapy. Cancer Chemother. Pharmacol., 49: 342-345 (2002).
    • (2002) Cancer Chemother. Pharmacol , vol.49 , pp. 342-345
    • Vis, A.N.1    van der Gaast, A.2    van Rhijn, B.W.3    Catsburg, T.K.4    Schmidt, C.5    Mickisch, G.H.6
  • 119
    • 33947644300 scopus 로고    scopus 로고
    • Albumin-bound basal insulin analogues (insulin detemir and NN344): Comparable time-action profiles but less variability than insulin glargine in type 2 diabetes
    • Klein, O., Lynge, J., Endahl, L., Damholt, B., Nosek, L. and Heise, T.: Albumin-bound basal insulin analogues (insulin detemir and NN344): comparable time-action profiles but less variability than insulin glargine in type 2 diabetes. Diabetes Obes. Metab., 9: 290-299 (2007).
    • (2007) Diabetes Obes. Metab , vol.9 , pp. 290-299
    • Klein, O.1    Lynge, J.2    Endahl, L.3    Damholt, B.4    Nosek, L.5    Heise, T.6
  • 121
    • 0037420811 scopus 로고    scopus 로고
    • Phosphate ester serum albumin affinity tags greatly improve peptide half-life in vivo
    • Zobel, K., Koehler, M. F., Beresini, M. H., Caris, L. D. and Combs, D.: Phosphate ester serum albumin affinity tags greatly improve peptide half-life in vivo. Bioorg. Med. Chem. Lett., 13: 1513-1515 (2003).
    • (2003) Bioorg. Med. Chem. Lett , vol.13 , pp. 1513-1515
    • Zobel, K.1    Koehler, M.F.2    Beresini, M.H.3    Caris, L.D.4    Combs, D.5
  • 122
    • 33144488817 scopus 로고    scopus 로고
    • Insulin detemir: From concept to clinical experience
    • Home, P. and Kurtzhals, P.: Insulin detemir: from concept to clinical experience. Expert Opin. Pharmacother, 7: 325-343 (2006).
    • (2006) Expert Opin. Pharmacother , vol.7 , pp. 325-343
    • Home, P.1    Kurtzhals, P.2
  • 124
    • 33745458519 scopus 로고    scopus 로고
    • Albumin-bound paclitaxel: A next-generation taxane
    • Gradishar, W. J.: Albumin-bound paclitaxel: a next-generation taxane. Expert Opin. Pharmacother., 7: 1041-1053 (2006).
    • (2006) Expert Opin. Pharmacother , vol.7 , pp. 1041-1053
    • Gradishar, W.J.1
  • 125
    • 32944482677 scopus 로고    scopus 로고
    • Phase III trial of nanoparticle albumin-bound paclitaxel compared with polyethylated castor oil-based paclitaxel in women with breast cancer
    • Gradishar, W. J., Tjulandin, S., Davidson, N., Shaw, H., Desai, N., Bhar, P., Hawkins, M. and O'Shaughnessy, J.: Phase III trial of nanoparticle albumin-bound paclitaxel compared with polyethylated castor oil-based paclitaxel in women with breast cancer. J. Clin. Oncol., 23: 7794-7803 (2005).
    • (2005) J. Clin. Oncol , vol.23 , pp. 7794-7803
    • Gradishar, W.J.1    Tjulandin, S.2    Davidson, N.3    Shaw, H.4    Desai, N.5    Bhar, P.6    Hawkins, M.7    O'Shaughnessy, J.8
  • 126
    • 61649107667 scopus 로고    scopus 로고
    • Phase II trial of weekly nab (nanoparticle albuminbound)-paclitaxel (nab-paclitaxel) (Abraxane) in combination with gemcitabine in patients with metastatic breast cancer (N0531)
    • Roy, V., LaPlant, B. R., Gross, G. G., Bane, C. L. and Palmieri, F. M.: Phase II trial of weekly nab (nanoparticle albuminbound)-paclitaxel (nab-paclitaxel) (Abraxane) in combination with gemcitabine in patients with metastatic breast cancer (N0531). Ann. Oncol., 20: 449-453 (2009).
    • (2009) Ann. Oncol , vol.20 , pp. 449-453
    • Roy, V.1    LaPlant, B.R.2    Gross, G.G.3    Bane, C.L.4    Palmieri, F.M.5
  • 130
    • 0036826998 scopus 로고    scopus 로고
    • Albugranin, a recombinant human granulocyte colony stimulating factor (G-CSF) genetically fused to recombinant human albumin induces prolonged myelopoietic effects in mice and monkeys
    • Halpern, W., Riccobene, T. A., Agostini, H., Baker, K., Stolow, D., Gu, M. L., Hirsch, J., Mahoney, A., Carrell, J., Boyd, E. and Grzegorzewski, K. J.: Albugranin, a recombinant human granulocyte colony stimulating factor (G-CSF) genetically fused to recombinant human albumin induces prolonged myelopoietic effects in mice and monkeys. Pharm. Res., 19: 1720-1729 (2002).
    • (2002) Pharm. Res , vol.19 , pp. 1720-1729
    • Halpern, W.1    Riccobene, T.A.2    Agostini, H.3    Baker, K.4    Stolow, D.5    Gu, M.L.6    Hirsch, J.7    Mahoney, A.8    Carrell, J.9    Boyd, E.10    Grzegorzewski, K.J.11
  • 131
    • 0037027919 scopus 로고    scopus 로고
    • Albutropin: A growth hormone-albumin fusion with improved pharmacokinetics and pharmacodynamics in rats and monkeys
    • Osborn, B. L., Sekut, L., Corcoran, M., Poortman, C., Sturm, B., Chen, G., Mather, D., Lin, H. L. and Parry, T. J.: Albutropin: a growth hormone-albumin fusion with improved pharmacokinetics and pharmacodynamics in rats and monkeys. Eur. J. Pharmacol., 456: 149-158 (2002).
    • (2002) Eur. J. Pharmacol , vol.456 , pp. 149-158
    • Osborn, B.L.1    Sekut, L.2    Corcoran, M.3    Poortman, C.4    Sturm, B.5    Chen, G.6    Mather, D.7    Lin, H.L.8    Parry, T.J.9
  • 133
    • 36849040529 scopus 로고    scopus 로고
    • Albinterferon alpha-2b: A genetic fusion protein for the treatment of chronic hepatitis C
    • Subramanian, G. M., Fiscella, M., Lamouse-Smith, A., Zeuzem, S. and McHutchison, J. G.: Albinterferon alpha-2b: a genetic fusion protein for the treatment of chronic hepatitis C. Nat. Biotechnol., 25: 1411-1419 (2007).
    • (2007) Nat. Biotechnol , vol.25 , pp. 1411-1419
    • Subramanian, G.M.1    Fiscella, M.2    Lamouse-Smith, A.3    Zeuzem, S.4    McHutchison, J.G.5
  • 135
    • 0034324083 scopus 로고    scopus 로고
    • Pegylated interferon-alpha2b: Pharmacokinetics, pharmacodynamics, safety, and preliminary efficacy data. Hepatitis C Intervention Therapy Group
    • Glue, P., Fang, J. W., Rouzier-Panis, R., Raffanel, C., Sabo, R., Gupta, S. K., Salfi, M. and Jacobs, S.: Pegylated interferon-alpha2b: pharmacokinetics, pharmacodynamics, safety, and preliminary efficacy data. Hepatitis C Intervention Therapy Group. Clin. Pharmacol. Ther., 68: 556-567 (2000).
    • (2000) Clin. Pharmacol. Ther , vol.68 , pp. 556-567
    • Glue, P.1    Fang, J.W.2    Rouzier-Panis, R.3    Raffanel, C.4    Sabo, R.5    Gupta, S.K.6    Salfi, M.7    Jacobs, S.8
  • 137
    • 34250361507 scopus 로고    scopus 로고
    • Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin
    • Muller, D., Karle, A., Meissburger, B., Hofig, I., Stork, R. and Kontermann, R. E.: Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin. J. Biol. Chem., 282: 12650-12660 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 12650-12660
    • Muller, D.1    Karle, A.2    Meissburger, B.3    Hofig, I.4    Stork, R.5    Kontermann, R.E.6
  • 138
    • 34547855838 scopus 로고    scopus 로고
    • Recombinant bispecific antibodies for cellular cancer immunotherapy
    • Muller, D. and Kontermann, R. E.: Recombinant bispecific antibodies for cellular cancer immunotherapy. Curr. Opin. Mol. Ther., 9: 319-326 (2007).
    • (2007) Curr. Opin. Mol. Ther , vol.9 , pp. 319-326
    • Muller, D.1    Kontermann, R.E.2
  • 142
    • 33745712861 scopus 로고    scopus 로고
    • The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin
    • Nguyen, A., Reyes, A. E., 2nd, Zhang, M., McDonald, P., Wong, W. L., Damico, L. A. and Dennis, M. S.: The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin. Protein Eng. Des. Sel., 19: 291-297 (2006).
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 291-297
    • Nguyen, A.1    Reyes 2nd, A.E.2    Zhang, M.3    McDonald, P.4    Wong, W.L.5    Damico, L.A.6    Dennis, M.S.7
  • 144
    • 34547735974 scopus 로고    scopus 로고
    • Fusion of a recombinant antibody fragment with a homo-amino-acid polymer: Effects on biophysical properties and prolonged plasma half-life
    • Schlapschy, M., Theobald, I., Mack, H., Schottelius, M., Wester, H. J. and Skerra, A.: Fusion of a recombinant antibody fragment with a homo-amino-acid polymer: effects on biophysical properties and prolonged plasma half-life. Protein Eng. Des. Sel., 20: 273-284 (2007).
    • (2007) Protein Eng. Des. Sel , vol.20 , pp. 273-284
    • Schlapschy, M.1    Theobald, I.2    Mack, H.3    Schottelius, M.4    Wester, H.J.5    Skerra, A.6
  • 146
    • 0000137374 scopus 로고
    • In vivo stabilization of a human recombinant CD4 derivative by fusion to a serum albumin-binding receptor
    • Chanok, R. M, ed, New York, Cold Spring Harbor Laboratory Press
    • Nygren, P. A., Flodby, P., Andersson, R., Wigzell, H. and Uhlen, M.: In vivo stabilization of a human recombinant CD4 derivative by fusion to a serum albumin-binding receptor. In Chanok, R. M. (ed.): Vaccines 91, Modern Approaches to Vaccine Development, New York, Cold Spring Harbor Laboratory Press, 1991, pp. 363-368.
    • (1991) Vaccines 91, Modern Approaches to Vaccine Development , pp. 363-368
    • Nygren, P.A.1    Flodby, P.2    Andersson, R.3    Wigzell, H.4    Uhlen, M.5
  • 148
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain
    • Nord, K., Gunneriusson, E., Ringdahl, J., Stahl, S., Uhlen, M. and Nygren, P. A.: Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nat. Biotechnol., 15: 772-777 (1997).
    • (1997) Nat. Biotechnol , vol.15 , pp. 772-777
    • Nord, K.1    Gunneriusson, E.2    Ringdahl, J.3    Stahl, S.4    Uhlen, M.5    Nygren, P.A.6
  • 149
    • 36549022608 scopus 로고    scopus 로고
    • A novel tri-functional antibody fusion protein with improved pharmacokinetic properties generated by fusing a bispecific single-chain diabody with an albumin-binding domain from streptococcal protein G
    • Stork, R., Muller, D. and Kontermann, R. E.: A novel tri-functional antibody fusion protein with improved pharmacokinetic properties generated by fusing a bispecific single-chain diabody with an albumin-binding domain from streptococcal protein G. Protein Eng. Des. Sel., 20: 569-576 (2007).
    • (2007) Protein Eng. Des. Sel , vol.20 , pp. 569-576
    • Stork, R.1    Muller, D.2    Kontermann, R.E.3
  • 150
    • 0036145494 scopus 로고    scopus 로고
    • Mutational analysis of the interaction between albumin-binding domain from streptococcal protein G and human serum albumin
    • Linhult, M., Binz, H. K., Uhlen, M. and Hober, S.: Mutational analysis of the interaction between albumin-binding domain from streptococcal protein G and human serum albumin. Protein Sci., 11: 206-213 (2002).
    • (2002) Protein Sci , vol.11 , pp. 206-213
    • Linhult, M.1    Binz, H.K.2    Uhlen, M.3    Hober, S.4
  • 154
    • 0034666718 scopus 로고    scopus 로고
    • Modulation of clearance of recombinant serum albumin by either glycosylation or truncation
    • Sheffield, W. P., Marques, J. A., Bhakta, V. and Smith, I. J.: Modulation of clearance of recombinant serum albumin by either glycosylation or truncation. Thromb Res., 99: 613-621 (2000).
    • (2000) Thromb Res , vol.99 , pp. 613-621
    • Sheffield, W.P.1    Marques, J.A.2    Bhakta, V.3    Smith, I.J.4
  • 155
    • 33947318463 scopus 로고    scopus 로고
    • Affibody molecules: New protein domains for molecular imaging and targeted tumor therapy
    • Nilsson, F.Y. and Tolmachev, V.: Affibody molecules: new protein domains for molecular imaging and targeted tumor therapy. Curr. Opin. Drug Discov. Devel., 10: 167-175 (2007).
    • (2007) Curr. Opin. Drug Discov. Devel , vol.10 , pp. 167-175
    • Nilsson, F.Y.1    Tolmachev, V.2
  • 156
  • 158
    • 21844442380 scopus 로고    scopus 로고
    • Hypercatabolism of IgG in mice with lupus-like syndrome
    • Zhou, J., Pop, L. M. and Ghetie, V.: Hypercatabolism of IgG in mice with lupus-like syndrome. Lupus, 14: 458-466 (2005).
    • (2005) Lupus , vol.14 , pp. 458-466
    • Zhou, J.1    Pop, L.M.2    Ghetie, V.3
  • 159
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 A resolution
    • Sugio, S., Kashima, A., Mochizuki, S., Noda, M. and Kobayashi, K.: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng., 12: 439-446 (1999).
    • (1999) Protein Eng , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5


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