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Volumn 161, Issue , 2016, Pages 22-39

A comprehensive review of the neonatal Fc receptor and its application in drug delivery

Author keywords

Albumin; Drug delivery; FcRn; IgG; Recycling; Transcytosis

Indexed keywords

ALBUMIN; FC RECEPTOR; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; ALBUMINOID; FC RECEPTOR, NEONATAL; HLA ANTIGEN CLASS 1;

EID: 84962069586     PISSN: 01637258     EISSN: 1879016X     Source Type: Journal    
DOI: 10.1016/j.pharmthera.2016.03.007     Document Type: Review
Times cited : (98)

References (234)
  • 1
    • 84924528149 scopus 로고    scopus 로고
    • The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinity
    • Y.N. Abdiche, Y.A. Yeung, J. Chaparro-riggers, I. Barman, P. Strop, S.M. Chin, and et al. The neonatal Fc receptor (FcRn) binds independently to both sites of the IgG homodimer with identical affinity MAbs 7 2 2015 331 343
    • (2015) MAbs , vol.7 , Issue.2 , pp. 331-343
    • Abdiche, Y.N.1    Yeung, Y.A.2    Chaparro-Riggers, J.3    Barman, I.4    Strop, P.5    Chin, S.M.6
  • 2
    • 80052642324 scopus 로고    scopus 로고
    • Rab GTPases as regulators of endocytosis, targets of disease and therapeutic opportunities
    • J.O. Agola, P.A. Jim, H.H. Ward, S. Basuray, and A. Wandinger-Ness Rab GTPases as regulators of endocytosis, targets of disease and therapeutic opportunities Clin Genet 80 4 2011 305 318
    • (2011) Clin Genet , vol.80 , Issue.4 , pp. 305-318
    • Agola, J.O.1    Jim, P.A.2    Ward, H.H.3    Basuray, S.4    Wandinger-Ness, A.5
  • 3
    • 39549088649 scopus 로고    scopus 로고
    • Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism
    • S. Akilesh, G.J. Christianson, D.C. Roopenian, and A.S. Shaw Neonatal FcR expression in bone marrow-derived cells functions to protect serum IgG from catabolism J Immunol 179 7 2007 4580 4588
    • (2007) J Immunol , vol.179 , Issue.7 , pp. 4580-4588
    • Akilesh, S.1    Christianson, G.J.2    Roopenian, D.C.3    Shaw, A.S.4
  • 5
    • 78149299782 scopus 로고    scopus 로고
    • Cubilin is essential for albumin reabsorption in the renal proximal tubule
    • S. Amsellem, J. Gburek, G. Hamard, R. Nielsen, T.E. Willnow, O. Devuyst, and et al. Cubilin is essential for albumin reabsorption in the renal proximal tubule J Am Soc Nephrol 21 11 2010 1859 1867
    • (2010) J Am Soc Nephrol , vol.21 , Issue.11 , pp. 1859-1867
    • Amsellem, S.1    Gburek, J.2    Hamard, G.3    Nielsen, R.4    Willnow, T.E.5    Devuyst, O.6
  • 6
    • 70350438004 scopus 로고    scopus 로고
    • The versatile MHC class I-related FcRn protects IgG and albumin from degradation: Implications for development of new diagnostics and therapeutics
    • J.T. Andersen, and I. Sandlie The versatile MHC class I-related FcRn protects IgG and albumin from degradation: Implications for development of new diagnostics and therapeutics Drug Metab Pharmacokinet 24 4 2009 318 332
    • (2009) Drug Metab Pharmacokinet , vol.24 , Issue.4 , pp. 318-332
    • Andersen, J.T.1    Sandlie, I.2
  • 7
    • 76749138019 scopus 로고    scopus 로고
    • FcRn binding properties of an abnormal truncated analbuminemic albumin variant
    • J.T. Andersen, M.B. Daba, and I. Sandlie FcRn binding properties of an abnormal truncated analbuminemic albumin variant Clin Biochem 43 4-5 2010 367 372
    • (2010) Clin Biochem , vol.43 , Issue.4-5 , pp. 367-372
    • Andersen, J.T.1    Daba, M.B.2    Sandlie, I.3
  • 8
    • 84856726736 scopus 로고    scopus 로고
    • Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor
    • J.T. Andersen, B. Dalhus, J. Cameron, M.B. Daba, A. Plumridge, L. Evans, and et al. Structure-based mutagenesis reveals the albumin-binding site of the neonatal Fc receptor Nat Commun 3 2012 610
    • (2012) Nat Commun , vol.3 , pp. 610
    • Andersen, J.T.1    Dalhus, B.2    Cameron, J.3    Daba, M.B.4    Plumridge, A.5    Evans, L.6
  • 9
    • 84900437074 scopus 로고    scopus 로고
    • Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding
    • J.T. Andersen, B. Dalhus, D. Viuff, B.T. Ravn, K.S. Gunnarsen, A. Plumridge, and et al. Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding J Biol Chem 289 19 2014 13492 13502
    • (2014) J Biol Chem , vol.289 , Issue.19 , pp. 13492-13502
    • Andersen, J.T.1    Dalhus, B.2    Viuff, D.3    Ravn, B.T.4    Gunnarsen, K.S.5    Plumridge, A.6
  • 10
    • 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
    • J.T. Andersen, J. Dee Qian, and I. Sandlie 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 11 2006 3044 3051
    • (2006) Eur J Immunol , vol.36 , Issue.11 , pp. 3044-3051
    • Andersen, J.T.1    Dee Qian, J.2    Sandlie, I.3
  • 13
    • 81055141343 scopus 로고    scopus 로고
    • Intracellular neutralization of viral infection in polarized epithelial cells by neonatal Fc receptor (FcRn)-mediated IgG transport
    • Y. Bai, L. Ye, D.B. Tesar, H. Song, D. Zhao, P.J. Bjorkman, and et al. Intracellular neutralization of viral infection in polarized epithelial cells by neonatal Fc receptor (FcRn)-mediated IgG transport Proc Natl Acad Sci U S A 108 45 2011 18406 18411
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.45 , pp. 18406-18411
    • Bai, Y.1    Ye, L.2    Tesar, D.B.3    Song, H.4    Zhao, D.5    Bjorkman, P.J.6
  • 14
    • 79959946173 scopus 로고    scopus 로고
    • Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune complexes by CD8-CD11b + dendritic cells
    • K. Baker, S.-W. Qiao, T.T. Kuo, V.G. Aveson, B. Platzer, J.-T. Andersen, and et al. Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune complexes by CD8-CD11b + dendritic cells Proc Natl Acad Sci U S A 108 24 2011 9927 9932
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.24 , pp. 9927-9932
    • Baker, K.1    Qiao, S.-W.2    Kuo, T.T.3    Aveson, V.G.4    Platzer, B.5    Andersen, J.-T.6
  • 15
    • 70349275220 scopus 로고    scopus 로고
    • Immune and non-immune functions of the (not so) neonatal Fc receptor, FcRn
    • K. Baker, S.-W. Qiao, T. Kuo, K. Kobayashi, M. Yoshida, W.I. Lencer, and et al. Immune and non-immune functions of the (not so) neonatal Fc receptor, FcRn Semin Immunopathol 31 2 2009 223 236
    • (2009) Semin Immunopathol , vol.31 , Issue.2 , pp. 223-236
    • Baker, K.1    Qiao, S.-W.2    Kuo, T.3    Kobayashi, K.4    Yoshida, M.5    Lencer, W.I.6
  • 16
    • 84890149954 scopus 로고    scopus 로고
    • Neonatal Fc receptor expression in dendritic cells mediates protective immunity against colorectal cancer
    • K. Baker, T. Rath, M.B. Flak, J.C. Arthur, Z. Chen, J.N. Glickman, and et al. Neonatal Fc receptor expression in dendritic cells mediates protective immunity against colorectal cancer Immunity 39 6 2013 1095 1107
    • (2013) Immunity , vol.39 , Issue.6 , pp. 1095-1107
    • Baker, K.1    Rath, T.2    Flak, M.B.3    Arthur, J.C.4    Chen, Z.5    Glickman, J.N.6
  • 18
    • 0015062163 scopus 로고
    • Albumin metabolism in rheumatoid arthritis
    • F.C. Ballantyne, A. Fleck, and W.C. Dick Albumin metabolism in rheumatoid arthritis Ann Rheum Dis 30 3 1971 265 270
    • (1971) Ann Rheum Dis , vol.30 , Issue.3 , pp. 265-270
    • Ballantyne, F.C.1    Fleck, A.2    Dick, W.C.3
  • 19
    • 0014018740 scopus 로고
    • Studies in vitro of the passage of serum proteins across the intestinal wall of young rats
    • D.R. Bamford Studies in vitro of the passage of serum proteins across the intestinal wall of young rats Proc R Soc Lond Ser B Biol Sci 166 1002 1966 30 45
    • (1966) Proc R Soc Lond ser B Biol Sci , vol.166 , Issue.1002 , pp. 30-45
    • Bamford, D.R.1
  • 20
    • 80052569742 scopus 로고    scopus 로고
    • Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies
    • A. Beck, and J.M. Reichert Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies MAbs 3 5 2011 415 416
    • (2011) MAbs , vol.3 , Issue.5 , pp. 415-416
    • Beck, A.1    Reichert, J.M.2
  • 21
    • 83655183013 scopus 로고    scopus 로고
    • Neonatal Fc receptor for IgG (FcRn) expressed in the gastric epithelium regulates bacterial infection in mice
    • Y. Ben Suleiman, M. Yoshida, S. Nishiumi, H. Tanaka, T. Mimura, K. Nobutani, and et al. Neonatal Fc receptor for IgG (FcRn) expressed in the gastric epithelium regulates bacterial infection in mice Mucosal Immunol 5 1 2012 87 98
    • (2012) Mucosal Immunol , vol.5 , Issue.1 , pp. 87-98
    • Ben Suleiman, Y.1    Yoshida, M.2    Nishiumi, S.3    Tanaka, H.4    Mimura, T.5    Nobutani, K.6
  • 22
    • 84931274576 scopus 로고    scopus 로고
    • The role of albumin receptors in regulation of albumin homeostasis: Implications for drug delivery
    • M. Bern, K.M.K. Sand, J. Nilsen, I. Sandlie, and J.T. Andersen The role of albumin receptors in regulation of albumin homeostasis: Implications for drug delivery J Control Release 211 2015 144 162
    • (2015) J Control Release , vol.211 , pp. 144-162
    • Bern, M.1    Sand, K.M.K.2    Nilsen, J.3    Sandlie, I.4    Andersen, J.T.5
  • 23
    • 3042795848 scopus 로고    scopus 로고
    • Pulmonary delivery of an erythropoietin Fc fusion protein in non-human primates through an immunoglobulin transport pathway
    • A.J. Bitonti, J.A. Dumont, S.C. Low, R.T. Peters, K.E. Kropp, V.J. Palombella, and et al. Pulmonary delivery of an erythropoietin Fc fusion protein in non-human primates through an immunoglobulin transport pathway Proc Natl Acad Sci U S A 101 26 2004 9763 9768
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.26 , pp. 9763-9768
    • Bitonti, A.J.1    Dumont, J.A.2    Low, S.C.3    Peters, R.T.4    Kropp, K.E.5    Palombella, V.J.6
  • 24
    • 0031685365 scopus 로고    scopus 로고
    • Functional expression of the MHC class I-related receptor, FcRn, in endothelial cells of mice
    • J. Borvak, J. Richardson, C. Medesan, F. Antohe, C. Radu, M. Simionescu, and et al. Functional expression of the MHC class I-related receptor, FcRn, in endothelial cells of mice Int Immunol 10 9 1998 1289 1298
    • (1998) Int Immunol , vol.10 , Issue.9 , pp. 1289-1298
    • Borvak, J.1    Richardson, J.2    Medesan, C.3    Antohe, F.4    Radu, C.5    Simionescu, M.6
  • 25
    • 0022391685 scopus 로고
    • Transcytosis and paracellular movements of horseradish peroxidase across liver parenchymal tissue from blood to bile
    • P.O. Box, and B. Birmingham Transcytosis and paracellular movements of horseradish peroxidase across liver parenchymal tissue from blood to bile Biochem J 229 1985 529 537
    • (1985) Biochem J , vol.229 , pp. 529-537
    • Box, P.O.1    Birmingham, B.2
  • 26
    • 0014489153 scopus 로고
    • The transmission of immune globulins from the mother to the foetal and newborn young
    • F.W. Brambell The transmission of immune globulins from the mother to the foetal and newborn young Proc Nutr Soc 28 1 1969 35 41
    • (1969) Proc Nutr Soc , vol.28 , Issue.1 , pp. 35-41
    • Brambell, F.W.1
  • 27
    • 0000146003 scopus 로고
    • A theoretical model of gamma-globulin catabolism
    • F.W. Brambell, W.A. Hemmings, and I.G. Morris A theoretical model of gamma-globulin catabolism Nature 203 1964 1352 1354
    • (1964) Nature , vol.203 , pp. 1352-1354
    • Brambell, F.W.1    Hemmings, W.A.2    Morris, I.G.3
  • 28
    • 0028837083 scopus 로고
    • Recent advances on the use of biodegradable microparticles and nanoparticles in controlled drug delivery
    • L. Brannon-Peppas Recent advances on the use of biodegradable microparticles and nanoparticles in controlled drug delivery Int J Pharm 116 1 1995 1 9
    • (1995) Int J Pharm , vol.116 , Issue.1 , pp. 1-9
    • Brannon-Peppas, L.1
  • 30
    • 84859158304 scopus 로고    scopus 로고
    • Two different dosing regimens of human recombinant erythropoietin beta during preoperative autologous blood donation in patients having hip arthroplasty
    • M. Buljan, D. Nemet, B. Golubic-Cepulic, G. Bicanic, B. Tripkovic, and D. Delimar Two different dosing regimens of human recombinant erythropoietin beta during preoperative autologous blood donation in patients having hip arthroplasty Int Orthop 36 4 2012 703 709
    • (2012) Int Orthop , vol.36 , Issue.4 , pp. 703-709
    • Buljan, M.1    Nemet, D.2    Golubic-Cepulic, B.3    Bicanic, G.4    Tripkovic, B.5    Delimar, D.6
  • 31
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • W.P. Burmeister, A.H. Huber, and P.J. Bjorkman Crystal structure of the complex of rat neonatal Fc receptor with Fc Nature 372 6504 1994 379 383
    • (1994) Nature , vol.372 , Issue.6504 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 34
    • 84958543989 scopus 로고    scopus 로고
    • FcRn: From molecular interactions to regulation of IgG pharmacokinetics and functions
    • D.K. Challa, R. Velmurugan, R.J. Ober, and E. Sally Ward FcRn: From molecular interactions to regulation of IgG pharmacokinetics and functions Curr Top Microbiol Immunol 382 2014 249 272
    • (2014) Curr Top Microbiol Immunol , vol.382 , pp. 249-272
    • Challa, D.K.1    Velmurugan, R.2    Ober, R.J.3    Sally Ward, E.4
  • 36
    • 0037415556 scopus 로고    scopus 로고
    • The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan
    • C. Chaudhury, S. Mehnaz, J.M. Robinson, W.L. Hayton, D.K. Pearl, D.C. Roopenian, and et al. The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan J Exp Med 197 3 2003 315 322
    • (2003) J Exp Med , vol.197 , Issue.3 , 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
  • 37
    • 84869147336 scopus 로고    scopus 로고
    • Evaluation of a catenary PBPK model for predicting the in vivo disposition of mAbs engineered for high-affinity binding to FcRn
    • Y. Chen, and J.P. Balthasar Evaluation of a catenary PBPK model for predicting the in vivo disposition of mAbs engineered for high-affinity binding to FcRn AAPS J 14 4 2012 850 859
    • (2012) AAPS J , vol.14 , Issue.4 , pp. 850-859
    • Chen, Y.1    Balthasar, J.P.2
  • 38
    • 0344851751 scopus 로고    scopus 로고
    • The MHC class I related Fc receptor, FcRn, is expressed in the epithelial cells of the human mammary gland
    • P. Cianga, C. Cianga, L. Cozma, E.S. Ward, and E. Carasevici The MHC class I related Fc receptor, FcRn, is expressed in the epithelial cells of the human mammary gland Hum Immunol 64 12 2003 1152 1159
    • (2003) Hum Immunol , vol.64 , Issue.12 , pp. 1152-1159
    • Cianga, P.1    Cianga, C.2    Cozma, L.3    Ward, E.S.4    Carasevici, E.5
  • 40
    • 0032767535 scopus 로고    scopus 로고
    • Identification and function of neonatal Fc receptor in mammary gland of lactating mice
    • P. Cianga, C. Medesan, J.A. Richardson, V. Ghetie, and E.S. Ward Identification and function of neonatal Fc receptor in mammary gland of lactating mice Eur J Immunol 29 8 1999 2515 2523
    • (1999) Eur J Immunol , vol.29 , Issue.8 , pp. 2515-2523
    • Cianga, P.1    Medesan, C.2    Richardson, J.A.3    Ghetie, V.4    Ward, E.S.5
  • 41
    • 84892990008 scopus 로고    scopus 로고
    • Nanoparticle albumin bound paclitaxel in the treatment of human cancer: Nanodelivery reaches prime-time?
    • 905091
    • I. Cucinotto, L. Fiorillo, S. Gualtieri, M. Arbitrio, D. Ciliberto, N. Staropoli, and et al. Nanoparticle albumin bound paclitaxel in the treatment of human cancer: Nanodelivery reaches prime-time? J Drug Deliv 2013 905091 2013 10
    • (2013) J Drug Deliv , vol.2013 , pp. 10
    • Cucinotto, I.1    Fiorillo, L.2    Gualtieri, S.3    Arbitrio, M.4    Ciliberto, D.5    Staropoli, N.6
  • 42
    • 84867065769 scopus 로고    scopus 로고
    • Fc-fusion proteins: New developments and future perspectives
    • D.M. Czajkowsky, J. Hu, Z. Shao, and R.J. Pleass Fc-fusion proteins: New developments and future perspectives EMBO Mol Med 4 10 2012 1015 1028
    • (2012) EMBO Mol Med , vol.4 , Issue.10 , pp. 1015-1028
    • Czajkowsky, D.M.1    Hu, J.2    Shao, Z.3    Pleass, R.J.4
  • 43
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn)
    • W.F. Dall'Acqua, P.A. Kiener, and H. Wu Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn) J Biol Chem 281 33 2006 23514 23524
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23514-23524
    • Dall'Acqua, W.F.1    Kiener, P.A.2    Wu, H.3
  • 44
    • 84954225906 scopus 로고    scopus 로고
    • The interplay of non-specific binding, target-mediated clearance and FcRn interactions on the pharmacokinetics of humanized antibodies
    • A. Datta-Mannan, J. Lu, D.R. Witcher, D. Leung, Y. Tang, and V.J. Wroblewski The interplay of non-specific binding, target-mediated clearance and FcRn interactions on the pharmacokinetics of humanized antibodies MAbs 7 6 2015 1084 1093
    • (2015) MAbs , vol.7 , Issue.6 , pp. 1084-1093
    • Datta-Mannan, A.1    Lu, J.2    Witcher, D.R.3    Leung, D.4    Tang, Y.5    Wroblewski, V.J.6
  • 45
    • 84945300064 scopus 로고    scopus 로고
    • Internalization of bevacizumab by retinal endothelial cells and its intracellular fate: Evidence for an involvement of the neonatal Fc receptor
    • H.L. Deissler, G.K. Lang, and G.E. Lang Internalization of bevacizumab by retinal endothelial cells and its intracellular fate: Evidence for an involvement of the neonatal Fc receptor Exp Eye Res 143 2016 49 59
    • (2016) Exp Eye Res , vol.143 , pp. 49-59
    • Deissler, H.L.1    Lang, G.K.2    Lang, G.E.3
  • 46
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • W.L. DeLano, M.H. Ultsch, A.M. de Vos, and J.A. Wells Convergent solutions to binding at a protein-protein interface Science 287 5456 2000 1279 1283
    • (2000) Science , vol.287 , Issue.5456 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 47
    • 34547986066 scopus 로고    scopus 로고
    • "Should I stay or should I go?": Myosin V function in organelle trafficking
    • C. Desnos, S. Huet, and F. Darchen "Should I stay or should I go?": Myosin V function in organelle trafficking Biol Cell 99 8 2007 411 423
    • (2007) Biol Cell , vol.99 , Issue.8 , pp. 411-423
    • Desnos, C.1    Huet, S.2    Darchen, F.3
  • 48
    • 84889828313 scopus 로고    scopus 로고
    • The effect of pH dependence of antibody-antigen interactions on subcellular trafficking dynamics
    • S.C. Devanaboyina, S.M. Lynch, R.J. Ober, S. Ram, D. Kim, A. Puig-Canto, and et al. The effect of pH dependence of antibody-antigen interactions on subcellular trafficking dynamics MAbs 5 6 2013 851 859
    • (2013) MAbs , vol.5 , Issue.6 , pp. 851-859
    • Devanaboyina, S.C.1    Lynch, S.M.2    Ober, R.J.3    Ram, S.4    Kim, D.5    Puig-Canto, A.6
  • 49
    • 84861990084 scopus 로고    scopus 로고
    • Crossing the barrier: Targeting epithelial receptors for enhanced oral vaccine delivery
    • B. Devriendt, B.G. De Geest, B.M. Goddeeris, and E. Cox Crossing the barrier: Targeting epithelial receptors for enhanced oral vaccine delivery J Control Release 160 3 2012 431 439
    • (2012) J Control Release , vol.160 , Issue.3 , pp. 431-439
    • Devriendt, B.1    De Geest, B.G.2    Goddeeris, B.M.3    Cox, E.4
  • 50
    • 0032741975 scopus 로고    scopus 로고
    • Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line
    • B.L. Dickinson, K. Badizadegan, Z. Wu, J.C. Ahouse, X. Zhu, N.E. Simister, and et al. Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line J Clin Invest 104 7 1999 903 911
    • (1999) J Clin Invest , vol.104 , Issue.7 , pp. 903-911
    • Dickinson, B.L.1    Badizadegan, K.2    Wu, Z.3    Ahouse, J.C.4    Zhu, X.5    Simister, N.E.6
  • 51
    • 25844528107 scopus 로고    scopus 로고
    • Delivery of an erythropoietin-Fc fusion protein by inhalation in humans through an immunoglobulin transport pathway
    • J. a Dumont, A.J. Bitonti, D. Clark, S. Evans, M. Pickford, and S.P. Newman Delivery of an erythropoietin-Fc fusion protein by inhalation in humans through an immunoglobulin transport pathway J Aerosol Med 18 3 2005 294 303
    • (2005) J Aerosol Med , vol.18 , Issue.3 , pp. 294-303
    • Dumont, J.A.1    Bitonti, A.J.2    Clark, D.3    Evans, S.4    Pickford, M.5    Newman, S.P.6
  • 52
    • 33744937065 scopus 로고    scopus 로고
    • Monomeric Fc fusions: Impact on pharmacokinetic and biological activity of protein therapeutics
    • J.A. Dumont, S.C. Low, R.T. Peters, and A.J. Bitonti Monomeric Fc fusions: Impact on pharmacokinetic and biological activity of protein therapeutics BioDrugs 20 3 2006 151 160
    • (2006) BioDrugs , vol.20 , Issue.3 , pp. 151-160
    • Dumont, J.A.1    Low, S.C.2    Peters, R.T.3    Bitonti, A.J.4
  • 53
    • 51149085208 scopus 로고    scopus 로고
    • Nature and functions of autoantibodies
    • K. Elkon, and P. Casali Nature and functions of autoantibodies Nat Clin Pract Rheumatol 4 9 2008 491 498
    • (2008) Nat Clin Pract Rheumatol , vol.4 , Issue.9 , pp. 491-498
    • Elkon, K.1    Casali, P.2
  • 54
    • 10044237889 scopus 로고    scopus 로고
    • Control of rHuEPO biological activity: The role of carbohydrate
    • S. Elliott, J. Egrie, J. Browne, T. Lorenzini, L. Busse, N. Rogers, and et al. Control of rHuEPO biological activity: The role of carbohydrate Exp Hematol 32 12 2004 1146 1155
    • (2004) Exp Hematol , vol.32 , Issue.12 , pp. 1146-1155
    • Elliott, S.1    Egrie, J.2    Browne, J.3    Lorenzini, T.4    Busse, L.5    Rogers, N.6
  • 55
    • 12244272391 scopus 로고    scopus 로고
    • Enhancement of therapeutic protein in vivo activities through glycoengineering
    • S. Elliott, T. Lorenzini, S. Asher, K. Aoki, D. Brankow, L. Buck, and et al. Enhancement of therapeutic protein in vivo activities through glycoengineering Nat Biotechnol 21 4 2003 414 421
    • (2003) Nat Biotechnol , vol.21 , Issue.4 , pp. 414-421
    • Elliott, S.1    Lorenzini, T.2    Asher, S.3    Aoki, K.4    Brankow, D.5    Buck, L.6
  • 56
    • 84855850311 scopus 로고    scopus 로고
    • Impact of albumin on drug delivery - New applications on the horizon
    • B. Elsadek, and F. Kratz Impact of albumin on drug delivery - new applications on the horizon J Control Release 157 1 2012 4 28
    • (2012) J Control Release , vol.157 , Issue.1 , pp. 4-28
    • Elsadek, B.1    Kratz, F.2
  • 57
    • 84855813140 scopus 로고    scopus 로고
    • Albumin-based nanoparticles as potential controlled release drug delivery systems
    • A.O. Elzoghby, W.M. Samy, and N.A. Elgindy Albumin-based nanoparticles as potential controlled release drug delivery systems J Control Release Off J Control Release Soc 157 2 2012 168 182
    • (2012) J Control Release off J Control Release Soc , vol.157 , Issue.2 , pp. 168-182
    • Elzoghby, A.O.1    Samy, W.M.2    Elgindy, N.A.3
  • 58
    • 84859719708 scopus 로고    scopus 로고
    • Oral drug delivery with polymeric nanoparticles: The gastrointestinal mucus barriers
    • L.M. Ensign, R. Cone, and J. Hanes Oral drug delivery with polymeric nanoparticles: The gastrointestinal mucus barriers Adv Drug Deliv Rev 64 6 2012 557 570
    • (2012) Adv Drug Deliv Rev , vol.64 , Issue.6 , pp. 557-570
    • Ensign, L.M.1    Cone, R.2    Hanes, J.3
  • 59
    • 84881282394 scopus 로고    scopus 로고
    • Effects of the Fc-III tag on activity and stability of green fluorescent protein and human muscle creatine kinase
    • S. Feng, Y. Gong, G. Adilijiang, and H. Deng Effects of the Fc-III tag on activity and stability of green fluorescent protein and human muscle creatine kinase Protein Sci A Publ Protein Soc A Publ Protein Soc 22 7 2013 1008 1015
    • (2013) Protein Sci A Publ Protein Soc A Publ Protein Soc , vol.22 , Issue.7 , pp. 1008-1015
    • Feng, S.1    Gong, Y.2    Adilijiang, G.3    Deng, H.4
  • 60
    • 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
    • M. Firan, R. Bawdon, C. Radu, R.J. Ober, D. Eaken, F. Antohe, and et al. The MHC class I-related receptor, FcRn, plays an essential role in the maternofetal transfer of gamma-globulin in humans Int Immunol 13 8 2001 993 1002
    • (2001) Int Immunol , vol.13 , Issue.8 , pp. 993-1002
    • Firan, M.1    Bawdon, R.2    Radu, C.3    Ober, R.J.4    Eaken, D.5    Antohe, F.6
  • 61
    • 84952361181 scopus 로고    scopus 로고
    • Enhanced FcRn-dependent transepithelial delivery of IgG by Fc-engineering and polymerization
    • S. Foss, A. Grevys, K.M.K. Sand, M. Bern, P. Blundell, T.E. Michaelsen, and et al. Enhanced FcRn-dependent transepithelial delivery of IgG by Fc-engineering and polymerization J Control Release 223 2016 42 52
    • (2016) J Control Release , vol.223 , pp. 42-52
    • Foss, S.1    Grevys, A.2    Sand, K.M.K.3    Bern, M.4    Blundell, P.5    Michaelsen, T.E.6
  • 62
    • 84945265000 scopus 로고    scopus 로고
    • TRIM21: A cytosolic Fc receptor with broad antibody isotype specificity
    • S. Foss, R. Watkinson, I. Sandlie, L.C. James, and J.T. Andersen TRIM21: A cytosolic Fc receptor with broad antibody isotype specificity Immunol Rev 268 1 2015 328 339
    • (2015) Immunol Rev , vol.268 , Issue.1 , pp. 328-339
    • Foss, S.1    Watkinson, R.2    Sandlie, I.3    James, L.C.4    Andersen, J.T.5
  • 63
    • 1642452656 scopus 로고    scopus 로고
    • Isolation and identification of heterogeneous nuclear ribonucleoproteins (hnRNP) from purified plasma membranes of human tumour cell lines as albumin-binding proteins
    • T. Fritzsche, M. Schnolzer, S. Fiedler, M. Weigand, M. Wiessler, and E. Frei Isolation and identification of heterogeneous nuclear ribonucleoproteins (hnRNP) from purified plasma membranes of human tumour cell lines as albumin-binding proteins Biochem Pharmacol 67 4 2004 655 665
    • (2004) Biochem Pharmacol , vol.67 , Issue.4 , pp. 655-665
    • Fritzsche, T.1    Schnolzer, M.2    Fiedler, S.3    Weigand, M.4    Wiessler, M.5    Frei, E.6
  • 65
    • 73349086530 scopus 로고    scopus 로고
    • Investigation of the influence of FcRn on the distribution of IgG to the brain
    • A. Garg, and J.P. Balthasar Investigation of the influence of FcRn on the distribution of IgG to the brain AAPS J 11 3 2009 553 557
    • (2009) AAPS J , vol.11 , Issue.3 , pp. 553-557
    • Garg, A.1    Balthasar, J.P.2
  • 66
    • 0026569633 scopus 로고
    • Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules
    • L.N. Gastinel, N.E. Simister, and P.J. Bjorkman Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules Proc Natl Acad Sci U S A 89 1992 638 642
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 638-642
    • Gastinel, L.N.1    Simister, N.E.2    Bjorkman, P.J.3
  • 67
    • 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
    • K.E. Getman, and J.P. Balthasar 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 4 2005 718 729
    • (2005) J Pharm Sci , vol.94 , Issue.4 , pp. 718-729
    • Getman, K.E.1    Balthasar, J.P.2
  • 68
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class I-related receptor FcRn
    • V. Ghetie, and E.S. Ward Multiple roles for the major histocompatibility complex class I-related receptor FcRn Annu Rev Immunol 18 2000 739 766
    • (2000) Annu Rev Immunol , vol.18 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 69
    • 0029927482 scopus 로고    scopus 로고
    • Abnormally short serum half-lives of IgG in beta 2-microglobulin-deficient mice
    • V. Ghetie, J.G. Hubbard, J.K. Kim, M.F. Tsen, Y. Lee, and E.S. Ward Abnormally short serum half-lives of IgG in beta 2-microglobulin-deficient mice Eur J Immunol 26 3 1996 690 696
    • (1996) Eur J Immunol , vol.26 , Issue.3 , 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
  • 70
    • 0023679087 scopus 로고
    • Identification of albumin-binding proteins in capillary endothelial cells
    • N. Ghinea, A. Fixman, D. Alexandru, D. Popov, M. Hasu, L. Ghitescu, and et al. Identification of albumin-binding proteins in capillary endothelial cells J Cell Biol 107 1 1988 231 239
    • (1988) J Cell Biol , vol.107 , Issue.1 , pp. 231-239
    • Ghinea, N.1    Fixman, A.2    Alexandru, D.3    Popov, D.4    Hasu, M.5    Ghitescu, L.6
  • 71
    • 0033169980 scopus 로고    scopus 로고
    • IgG binding and expression of its receptor in rat intestine during postnatal development
    • R.K. Gill, S. Mahmood, C.P. Sodhi, J.P. Nagpaul, and A. Mahmood IgG binding and expression of its receptor in rat intestine during postnatal development Indian J Biochem Biophys 36 4 1999 252 257
    • (1999) Indian J Biochem Biophys , vol.36 , Issue.4 , pp. 252-257
    • Gill, R.K.1    Mahmood, S.2    Sodhi, C.P.3    Nagpaul, J.P.4    Mahmood, A.5
  • 72
    • 59449083582 scopus 로고    scopus 로고
    • Neonatal Fc receptor mediates internalization of Fc in transfected human endothelial cells
    • N.A. Goebl, C.M. Babbey, A. Datta-Mannan, D.R. Witcher, V.J. Wroblewski, and K.W. Dunn Neonatal Fc receptor mediates internalization of Fc in transfected human endothelial cells Mol Biol Cell 19 12 2008 5490 5505
    • (2008) Mol Biol Cell , vol.19 , Issue.12 , pp. 5490-5505
    • Goebl, N.A.1    Babbey, C.M.2    Datta-Mannan, A.3    Witcher, D.R.4    Wroblewski, V.J.5    Dunn, K.W.6
  • 73
    • 79960992429 scopus 로고    scopus 로고
    • Shortened engineered human antibody CH2 domains: Increased stability and binding to the human neonatal Fc receptor
    • R. Gong, Y. Wang, Y. Feng, Q. Zhao, and D.S. Dimitrov Shortened engineered human antibody CH2 domains: Increased stability and binding to the human neonatal Fc receptor J Biol Chem 286 31 2011 27288 27293
    • (2011) J Biol Chem , vol.286 , Issue.31 , pp. 27288-27293
    • Gong, R.1    Wang, Y.2    Feng, Y.3    Zhao, Q.4    Dimitrov, D.S.5
  • 74
    • 33745458519 scopus 로고    scopus 로고
    • Albumin-bound paclitaxel: A next-generation taxane
    • W.J. Gradishar Albumin-bound paclitaxel: A next-generation taxane Expert Opin Pharmacother 7 8 2006 1041 1053
    • (2006) Expert Opin Pharmacother , vol.7 , Issue.8 , pp. 1041-1053
    • Gradishar, W.J.1
  • 75
    • 46149113010 scopus 로고    scopus 로고
    • Infused Fc-tagged β-glucuronidase crosses the placenta and produces clearance of storage in utero in mucopolysaccharidosis VII mice
    • J.H. Grubb, C. Vogler, Y. Tan, G.N. Shah, A.F. MacRae, and W.S. Sly Infused Fc-tagged β-glucuronidase crosses the placenta and produces clearance of storage in utero in mucopolysaccharidosis VII mice Proc Natl Acad Sci U S A 105 24 2008 8375 8380
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.24 , 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
  • 76
    • 84355161386 scopus 로고    scopus 로고
    • Walking to work: Roles for class V myosins as cargo transporters
    • J.A. Hammer 3rd, and J.R. Sellers Walking to work: Roles for class V myosins as cargo transporters Nat Rev Mol Cell Biol 13 1 2012 13 26
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.1 , pp. 13-26
    • Hammer, J.A.1    Sellers, J.R.2
  • 77
    • 0015966366 scopus 로고
    • Antibacterial mechanisms of the lower respiratory tract. I. immunoglobulin synthesis and secretion
    • W.L. Hand, and J.R. Cantey Antibacterial mechanisms of the lower respiratory tract. I. immunoglobulin synthesis and secretion J Clin Invest 53 2 1974 354 362
    • (1974) J Clin Invest , vol.53 , Issue.2 , pp. 354-362
    • Hand, W.L.1    Cantey, J.R.2
  • 78
    • 0034023794 scopus 로고    scopus 로고
    • Characterization and localization of the neonatal Fc receptor in adult human kidney
    • J.P. Haymann, J.P. Levraud, S. Bouet, V. Kappes, J. Hagege, G. Nguyen, and et al. Characterization and localization of the neonatal Fc receptor in adult human kidney J Am Soc Nephrol 11 4 2000 632 639
    • (2000) J Am Soc Nephrol , vol.11 , Issue.4 , pp. 632-639
    • Haymann, J.P.1    Levraud, J.P.2    Bouet, S.3    Kappes, V.4    Hagege, J.5    Nguyen, G.6
  • 79
    • 84885377002 scopus 로고    scopus 로고
    • AlbudAb™ technology platform-versatile albumin binding domains for the development of therapeutics with Tunable half-lives
    • Wiley-VCH Verlag GmbH & Co. KGaA
    • C. Herring, and O. Schon AlbudAb™ technology platform-versatile albumin binding domains for the development of therapeutics with Tunable half-lives Therapeutic proteins 2012 Wiley-VCH Verlag GmbH & Co. KGaA 249 268
    • (2012) Therapeutic Proteins , pp. 249-268
    • Herring, C.1    Schon, O.2
  • 80
    • 74549221384 scopus 로고    scopus 로고
    • A phase 2 clinical trial of nab-paclitaxel in previously treated and chemotherapy-naive patients with metastatic melanoma
    • E.M. Hersh, S.J. O'Day, A. Ribas, W.E. Samlowski, M.S. Gordon, D.E. Shechter, and et al. A phase 2 clinical trial of nab-paclitaxel in previously treated and chemotherapy-naive patients with metastatic melanoma Cancer 116 1 2010 155 163
    • (2010) Cancer , vol.116 , Issue.1 , pp. 155-163
    • Hersh, E.M.1    O'Day, S.J.2    Ribas, A.3    Samlowski, W.E.4    Gordon, M.S.5    Shechter, D.E.6
  • 83
    • 33144488817 scopus 로고    scopus 로고
    • Insulin detemir: From concept to clinical experience
    • P. Home, and P. Kurtzhals Insulin detemir: From concept to clinical experience Expert Opin Pharmacother 7 3 2006 325 343
    • (2006) Expert Opin Pharmacother , vol.7 , Issue.3 , pp. 325-343
    • Home, P.1    Kurtzhals, P.2
  • 84
    • 84897015338 scopus 로고    scopus 로고
    • Human and non-human primate intestinal FcRn expression and immunoglobulin G transcytosis
    • P.J. Hornby, P.R. Cooper, C. Kliwinski, E. Ragwan, J.R. Mabus, B. Harman, and et al. Human and non-human primate intestinal FcRn expression and immunoglobulin G transcytosis Pharm Res 31 4 2014 908 922
    • (2014) Pharm Res , vol.31 , Issue.4 , pp. 908-922
    • Hornby, P.J.1    Cooper, P.R.2    Kliwinski, C.3    Ragwan, E.4    Mabus, J.R.5    Harman, B.6
  • 85
    • 70449706366 scopus 로고    scopus 로고
    • Receptor-Fc fusion therapeutics, traps, and MIMETIBODY technology
    • C. Huang Receptor-Fc fusion therapeutics, traps, and MIMETIBODY technology Curr Opin Biotechnol 20 6 2009 692 699
    • (2009) Curr Opin Biotechnol , vol.20 , Issue.6 , pp. 692-699
    • Huang, C.1
  • 86
    • 0034655265 scopus 로고    scopus 로고
    • Mapping of the C1q binding site on Rituxan, a chimeric antibody with a human IgG1 Fc
    • E.E. Idusogie, L.G. Presta, H. Gazzano-Santoro, K. Totpal, P.Y. Wong, M. Ultsch, and et al. Mapping of the C1q binding site on Rituxan, a chimeric antibody with a human IgG1 Fc J Immunol 164 8 2000 4178 4184
    • (2000) J Immunol , vol.164 , Issue.8 , pp. 4178-4184
    • Idusogie, E.E.1    Presta, L.G.2    Gazzano-Santoro, H.3    Totpal, K.4    Wong, P.Y.5    Ultsch, M.6
  • 87
    • 84877147797 scopus 로고    scopus 로고
    • Engineered monoclonal antibody with novel antigen-sweeping activity in vivo
    • T. Igawa, A. Maeda, K. Haraya, T. Tachibana, Y. Iwayanagi, F. Mimoto, and et al. Engineered monoclonal antibody with novel antigen-sweeping activity in vivo PLoS One 8 5 2013 e63236
    • (2013) PLoS One , vol.8 , Issue.5
    • Igawa, T.1    Maeda, A.2    Haraya, K.3    Tachibana, T.4    Iwayanagi, Y.5    Mimoto, F.6
  • 88
    • 0028980061 scopus 로고
    • Requirement for a beta 2-microglobulin-associated Fc receptor for acquisition of maternal IgG by fetal and neonatal mice
    • E.J. Israel, V.K. Patel, S.F. Taylor, A. Marshak-Rothstein, and N.E. Simister Requirement for a beta 2-microglobulin-associated Fc receptor for acquisition of maternal IgG by fetal and neonatal mice J Immunol 154 12 1995 6246 6251
    • (1995) J Immunol , vol.154 , Issue.12 , pp. 6246-6251
    • Israel, E.J.1    Patel, V.K.2    Taylor, S.F.3    Marshak-Rothstein, A.4    Simister, N.E.5
  • 89
    • 0030880901 scopus 로고    scopus 로고
    • Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells
    • E.J. Israel, S. Taylor, Z. Wu, E. Mizoguchi, R.S. Blumberg, A. Bhan, and et al. Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells Immunology 92 1997 69 74
    • (1997) Immunology , vol.92 , pp. 69-74
    • Israel, E.J.1    Taylor, S.2    Wu, Z.3    Mizoguchi, E.4    Blumberg, R.S.5    Bhan, A.6
  • 90
    • 34848838291 scopus 로고    scopus 로고
    • Improved tumor imaging and therapy via i.v. IgG-mediated time-sequential modulation of neonatal Fc receptor
    • J.S. Jaggi, J.A. Carrasquillo, S.V. Seshan, P. Zanzonico, E. Henke, A. Nagel, and et al. Improved tumor imaging and therapy via i.v. IgG-mediated time-sequential modulation of neonatal Fc receptor J Clin Invest 117 9 2007 2422 2430
    • (2007) J Clin Invest , vol.117 , Issue.9 , pp. 2422-2430
    • Jaggi, J.S.1    Carrasquillo, J.A.2    Seshan, S.V.3    Zanzonico, P.4    Henke, E.5    Nagel, A.6
  • 91
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • R. Jahn, T. Lang, and T.C. Südhof Membrane fusion Cell 112 4 2003 519 533
    • (2003) Cell , vol.112 , Issue.4 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Südhof, T.C.3
  • 93
    • 47649128420 scopus 로고    scopus 로고
    • Engineering of a femtomolar affinity binding protein to human serum albumin
    • A. Jonsson, J. Dogan, N. Herne, L. Abrahmsen, and P.-A. Nygren Engineering of a femtomolar affinity binding protein to human serum albumin Protein Eng Des Sel 21 8 2008 515 527
    • (2008) Protein Eng des Sel , vol.21 , Issue.8 , pp. 515-527
    • Jonsson, A.1    Dogan, J.2    Herne, N.3    Abrahmsen, L.4    Nygren, P.-A.5
  • 94
    • 36348966705 scopus 로고    scopus 로고
    • Cellular protection by erythropoietin: New therapeutic implications?
    • M. Joyeux-Faure Cellular protection by erythropoietin: New therapeutic implications? J Pharmacol Exp Ther 323 3 2007 759 762
    • (2007) J Pharmacol Exp Ther , vol.323 , Issue.3 , pp. 759-762
    • Joyeux-Faure, M.1
  • 95
    • 0029891262 scopus 로고    scopus 로고
    • The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor
    • R.P. Junghans, and C.L. Anderson The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor Proc Natl Acad Sci U S A 93 11 1996 5512 5516
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.11 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 98
    • 0033393536 scopus 로고    scopus 로고
    • Mapping the site on human IgG for binding of the MHC class I-related receptor, FcRn
    • J.K. Kim, M. Firan, C.G. Radu, C.H. Kim, V. Ghetie, and E.S. Ward Mapping the site on human IgG for binding of the MHC class I-related receptor, FcRn Eur J Immunol 29 9 1999 2819 2825
    • (1999) Eur J Immunol , vol.29 , Issue.9 , 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
  • 99
    • 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
    • J. Kim, W.L. Hayton, J.M. Robinson, and C.L. Anderson Kinetics of FcRn-mediated recycling of IgG and albumin in human: Pathophysiology and therapeutic implications using a simplified mechanism-based model Clin Immunol 122 2 2007 146 155
    • (2007) Clin Immunol , vol.122 , Issue.2 , pp. 146-155
    • Kim, J.1    Hayton, W.L.2    Robinson, J.M.3    Anderson, C.L.4
  • 100
    • 0028021594 scopus 로고
    • Localization of the site of the murine IgG1 molecule that is involved in binding to the murine intestinal Fc receptor
    • J.K. Kim, M.F. Tsen, V. Ghetie, and E.S. Ward Localization of the site of the murine IgG1 molecule that is involved in binding to the murine intestinal Fc receptor Eur J Immunol 24 10 1994 2429 2434
    • (1994) Eur J Immunol , vol.24 , Issue.10 , pp. 2429-2434
    • Kim, J.K.1    Tsen, M.F.2    Ghetie, V.3    Ward, E.S.4
  • 101
    • 0028170522 scopus 로고
    • Catabolism of the murine IgG1 molecule: Evidence that both CH2-CH3 domain interfaces are required for persistence of IgG1 in the circulation of mice
    • J.K. Kim, M.F. Tsen, V. Ghetie, and E.S. Ward Catabolism of the murine IgG1 molecule: Evidence that both CH2-CH3 domain interfaces are required for persistence of IgG1 in the circulation of mice Scand J Immunol 40 4 1994 457 465
    • (1994) Scand J Immunol , vol.40 , Issue.4 , pp. 457-465
    • Kim, J.K.1    Tsen, M.F.2    Ghetie, V.3    Ward, E.S.4
  • 102
    • 0028220297 scopus 로고
    • Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis
    • J.K. Kim, M.F. Tsen, V. Ghetie, and E.S. Ward Identifying amino acid residues that influence plasma clearance of murine IgG1 fragments by site-directed mutagenesis Eur J Immunol 24 3 1994 542 548
    • (1994) Eur J Immunol , vol.24 , Issue.3 , pp. 542-548
    • Kim, J.K.1    Tsen, M.F.2    Ghetie, V.3    Ward, E.S.4
  • 104
    • 25144496461 scopus 로고    scopus 로고
    • Transport of IgG across the blood-luminal barrier of the male reproductive tract of the rat and the effect of estradiol administration on reabsorption of fluid and IgG by the epididymal ducts
    • R.A. Knee, D.K. Hickey, K.W. Beagley, and R.C. Jones Transport of IgG across the blood-luminal barrier of the male reproductive tract of the rat and the effect of estradiol administration on reabsorption of fluid and IgG by the epididymal ducts Biol Reprod 73 4 2005 688 694
    • (2005) Biol Reprod , vol.73 , Issue.4 , pp. 688-694
    • Knee, R.A.1    Hickey, D.K.2    Beagley, K.W.3    Jones, R.C.4
  • 105
    • 84907983318 scopus 로고    scopus 로고
    • Enhanced neonatal Fc receptor function improves protection against primate SHIV infection
    • S.-Y. Ko, A. Pegu, R.S. Rudicell, Z.-Y. Yang, M.G. Joyce, X. Chen, and et al. Enhanced neonatal Fc receptor function improves protection against primate SHIV infection Nature 514 7524 2014 642 645
    • (2014) Nature , vol.514 , Issue.7524 , pp. 642-645
    • Ko, S.-Y.1    Pegu, A.2    Rudicell, R.S.3    Yang, Z.-Y.4    Joyce, M.G.5    Chen, X.6
  • 106
    • 79953798396 scopus 로고    scopus 로고
    • A phase II trial of nab-paclitaxel (ABI-007) and carboplatin in patients with unresectable stage IV melanoma: A North Central Cancer Treatment Group Study, N057E(1)
    • L.A. Kottschade, V.J. Suman, T. Amatruda 3rd, R.R. McWilliams, B.I. Mattar, D.A. Nikcevich, and et al. A phase II trial of nab-paclitaxel (ABI-007) and carboplatin in patients with unresectable stage IV melanoma: A North Central Cancer Treatment Group Study, N057E(1) Cancer 117 8 2011 1704 1710
    • (2011) Cancer1 , vol.117 , Issue.8 , pp. 1704-1710
    • Kottschade, L.A.1    Suman, V.J.2    Amatruda, T.3    McWilliams, R.R.4    Mattar, B.I.5    Nikcevich, D.A.6
  • 107
    • 84872956413 scopus 로고    scopus 로고
    • A randomized phase 2 study of temozolomide and bevacizumab or nab-paclitaxel, carboplatin, and bevacizumab in patients with unresectable stage IV melanoma: A North Central Cancer Treatment Group Study, N0775
    • L.A. Kottschade, V.J. Suman, D.G. Perez, R.R. McWilliams, J.S. Kaur, T.T. Amatruda 3rd, and et al. A randomized phase 2 study of temozolomide and bevacizumab or nab-paclitaxel, carboplatin, and bevacizumab in patients with unresectable stage IV melanoma: A North Central Cancer Treatment Group Study, N0775 Cancer 119 3 2013 586 592
    • (2013) Cancer , vol.119 , Issue.3 , pp. 586-592
    • Kottschade, L.A.1    Suman, V.J.2    Perez, D.G.3    McWilliams, R.R.4    Kaur, J.S.5    Amatruda, T.T.6
  • 108
    • 56949084877 scopus 로고    scopus 로고
    • Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles
    • F. Kratz Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles J Control Release 132 3 2008 171 183
    • (2008) J Control Release , vol.132 , Issue.3 , pp. 171-183
    • Kratz, F.1
  • 109
    • 84906783332 scopus 로고    scopus 로고
    • A clinical update of using albumin as a drug vehicle - A commentary
    • F. Kratz A clinical update of using albumin as a drug vehicle - A commentary J Control Release 190 2014 331 336
    • (2014) J Control Release , vol.190 , pp. 331-336
    • Kratz, F.1
  • 110
    • 80052598705 scopus 로고    scopus 로고
    • Neonatal Fc receptor and IgG-based therapeutics
    • T.T. Kuo, and V.G. Aveson Neonatal Fc receptor and IgG-based therapeutics MAbs 3 5 2011 422 430
    • (2011) MAbs , vol.3 , Issue.5 , pp. 422-430
    • Kuo, T.T.1    Aveson, V.G.2
  • 112
    • 0030587958 scopus 로고    scopus 로고
    • Isolation from human placenta of the IgG transporter, FcRn, and localization to the syncytiotrophoblast: Implications for maternal-fetal antibody transport
    • J.L. Leach, D.D. Sedmak, J.M. Osborne, B. Rahill, M.D. Lairmore, and C.L. Anderson Isolation from human placenta of the IgG transporter, FcRn, and localization to the syncytiotrophoblast: Implications for maternal-fetal antibody transport J Immunol 157 8 1996 3317 3322
    • (1996) J Immunol , vol.157 , Issue.8 , pp. 3317-3322
    • Leach, J.L.1    Sedmak, D.D.2    Osborne, J.M.3    Rahill, B.4    Lairmore, M.D.5    Anderson, C.L.6
  • 114
    • 84949319141 scopus 로고    scopus 로고
    • Diabetes at the crossroads: Relevance of disease classification to pathophysiology and treatment
    • R.D. Leslie, J. Palmer, N.C. Schloot, and A. Lernmark Diabetes at the crossroads: Relevance of disease classification to pathophysiology and treatment Diabetologia 59 1 2015 13 20
    • (2015) Diabetologia , vol.59 , Issue.1 , pp. 13-20
    • Leslie, R.D.1    Palmer, J.2    Schloot, N.C.3    Lernmark, A.4
  • 115
    • 79952724131 scopus 로고    scopus 로고
    • Transfer of IgG in the female genital tract by MHC class I-related neonatal Fc receptor (FcRn) confers protective immunity to vaginal infection
    • Z. Li, S. Palaniyandi, R. Zeng, W. Tuo, D.C. Roopenian, and X. Zhu Transfer of IgG in the female genital tract by MHC class I-related neonatal Fc receptor (FcRn) confers protective immunity to vaginal infection Proc Natl Acad Sci U S A 108 11 2011 4388 4393
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.11 , pp. 4388-4393
    • Li, Z.1    Palaniyandi, S.2    Zeng, R.3    Tuo, W.4    Roopenian, D.C.5    Zhu, X.6
  • 116
    • 31044440897 scopus 로고    scopus 로고
    • Complete FcRn dependence for intravenous Ig therapy in autoimmune skin blistering diseases
    • N. Li, M. Zhao, J. Hilario-Vargas, P. Prisayanh, S. Warren, L.A. Diaz, and et al. Complete FcRn dependence for intravenous Ig therapy in autoimmune skin blistering diseases J Clin Invest 115 12 2005 3440 3450
    • (2005) J Clin Invest , vol.115 , Issue.12 , pp. 3440-3450
    • Li, N.1    Zhao, M.2    Hilario-Vargas, J.3    Prisayanh, P.4    Warren, S.5    Diaz, L.A.6
  • 117
    • 0020686787 scopus 로고
    • Plasmapheresis in clinical medicine
    • C. Linker Plasmapheresis in clinical medicine West J Med 138 1 1983 60 69
    • (1983) West J Med , vol.138 , Issue.1 , pp. 60-69
    • Linker, C.1
  • 118
    • 34247094345 scopus 로고    scopus 로고
    • Amelioration of experimental autoimmune myasthenia gravis in rats by neonatal FcR blockade
    • L. Liu, A.M. Garcia, H. Santoro, Y. Zhang, K. McDonnell, J. Dumont, and et al. Amelioration of experimental autoimmune myasthenia gravis in rats by neonatal FcR blockade J Immunol 178 8 2007 5390 5398
    • (2007) J Immunol , vol.178 , Issue.8 , pp. 5390-5398
    • Liu, L.1    Garcia, A.M.2    Santoro, H.3    Zhang, Y.4    McDonnell, K.5    Dumont, J.6
  • 119
    • 79955024081 scopus 로고    scopus 로고
    • The neonatal FcR-mediated presentation of immune-complexed antigen is associated with endosomal and phagosomal pH and antigen stability in macrophages and dendritic cells
    • X. Liu, L. Lu, Z. Yang, S. Palaniyandi, R. Zeng, L.-Y. Gao, and et al. The neonatal FcR-mediated presentation of immune-complexed antigen is associated with endosomal and phagosomal pH and antigen stability in macrophages and dendritic cells J Immunol 186 8 2011 4674 4686
    • (2011) J Immunol , vol.186 , Issue.8 , pp. 4674-4686
    • Liu, X.1    Lu, L.2    Yang, Z.3    Palaniyandi, S.4    Zeng, R.5    Gao, L.-Y.6
  • 120
    • 52549110350 scopus 로고    scopus 로고
    • Myosins in the secretory pathway: Tethers or transporters?
    • S. Loubery, and E. Coudrier Myosins in the secretory pathway: Tethers or transporters? Cell Mol Life Sci 65 18 2008 2790 2800
    • (2008) Cell Mol Life Sci , vol.65 , Issue.18 , pp. 2790-2800
    • Loubery, S.1    Coudrier, E.2
  • 121
    • 21644443969 scopus 로고    scopus 로고
    • Oral and pulmonary delivery of FSH-Fc fusion proteins via neonatal Fc receptor-mediated transcytosis
    • S.C. Low, S.L. Nunes, A.J. Bitonti, and J.A. Dumont Oral and pulmonary delivery of FSH-Fc fusion proteins via neonatal Fc receptor-mediated transcytosis Hum Reprod 20 7 2005 1805 1813
    • (2005) Hum Reprod , vol.20 , Issue.7 , pp. 1805-1813
    • Low, S.C.1    Nunes, S.L.2    Bitonti, A.J.3    Dumont, J.A.4
  • 122
    • 84870917147 scopus 로고    scopus 로고
    • Methamphetamine-induced nitric oxide promotes vesicular transport in blood-brain barrier endothelial cells
    • T. Martins, T. Burgoyne, B.-A. Kenny, N. Hudson, C.E. Futter, A.F. Ambrósio, and et al. Methamphetamine-induced nitric oxide promotes vesicular transport in blood-brain barrier endothelial cells Neuropharmacology 65 2013 74 82
    • (2013) Neuropharmacology , vol.65 , pp. 74-82
    • Martins, T.1    Burgoyne, T.2    Kenny, B.-A.3    Hudson, N.4    Futter, C.E.5    Ambrósio, A.F.6
  • 123
    • 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
    • K.M. McCarthy, Y. Yoong, and N.E. Simister 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 2000 1277 1285
    • (2000) J Cell Sci , vol.113 , pp. 1277-1285
    • McCarthy, K.M.1    Yoong, Y.2    Simister, N.E.3
  • 124
    • 0031093498 scopus 로고    scopus 로고
    • Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1
    • C. Medesan, D. Matesoi, C. Radu, V. Ghetie, and E.S. Ward Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1 J Immunol 158 5 1997 2211 2217
    • (1997) J Immunol , vol.158 , Issue.5 , pp. 2211-2217
    • Medesan, C.1    Matesoi, D.2    Radu, C.3    Ghetie, V.4    Ward, E.S.5
  • 125
    • 84906519506 scopus 로고    scopus 로고
    • Unraveling the mysteries of serum albumin - More than just a serum protein
    • A.M. Merlot, D.S. Kalinowski, and D.R. Richardson Unraveling the mysteries of serum albumin - more than just a serum protein Front Physiol 5 2014 299
    • (2014) Front Physiol , vol.5 , pp. 299
    • Merlot, A.M.1    Kalinowski, D.S.2    Richardson, D.R.3
  • 127
    • 77956242476 scopus 로고    scopus 로고
    • X-ray crystal structures of monomeric and dimeric peptide inhibitors in complex with the human neonatal Fc receptor, FcRn
    • A.R. Mezo, V. Sridhar, J. Badger, P. Sakorafas, and V. Nienaber X-ray crystal structures of monomeric and dimeric peptide inhibitors in complex with the human neonatal Fc receptor, FcRn J Biol Chem 285 36 2010 27694 27701
    • (2010) J Biol Chem , vol.285 , Issue.36 , pp. 27694-27701
    • Mezo, A.R.1    Sridhar, V.2    Badger, J.3    Sakorafas, P.4    Nienaber, V.5
  • 128
    • 0036059819 scopus 로고    scopus 로고
    • Mosaic organization of the endocytic pathway
    • M. Miaczynska, and M. Zerial Mosaic organization of the endocytic pathway Exp Cell Res 272 1 2002 8 14
    • (2002) Exp Cell Res , vol.272 , Issue.1 , pp. 8-14
    • Miaczynska, M.1    Zerial, M.2
  • 129
    • 66149129222 scopus 로고    scopus 로고
    • Albumin-bound formulation of paclitaxel (Abraxane® ABI-007) in the treatment of breast cancer
    • E. Miele, G.P. Spinelli, E. Miele, F. Tomao, and S. Tomao Albumin-bound formulation of paclitaxel (Abraxane® ABI-007) in the treatment of breast cancer Int J Nanomedicine 4 1 2009 99 105
    • (2009) Int J Nanomedicine , vol.4 , Issue.1 , pp. 99-105
    • Miele, E.1    Spinelli, G.P.2    Miele, E.3    Tomao, F.4    Tomao, S.5
  • 130
    • 6444242809 scopus 로고    scopus 로고
    • Albumin transcytosis across the epithelium of the lactating mouse mammary gland
    • J. Monks, and M.C. Neville Albumin transcytosis across the epithelium of the lactating mouse mammary gland J Physiol 560 Pt 1 2004 267 280
    • (2004) J Physiol , vol.560 , pp. 267-280
    • Monks, J.1    Neville, M.C.2
  • 131
    • 62449200475 scopus 로고    scopus 로고
    • Conditional deletion of the MHC class I-related receptor FcRn reveals the sites of IgG homeostasis in mice
    • H.P. Montoyo, C. Vaccaro, M. Hafner, R.J. Ober, W. Mueller, and E.S. Ward Conditional deletion of the MHC class I-related receptor FcRn reveals the sites of IgG homeostasis in mice Proc Natl Acad Sci U S A 106 8 2009 2788 2793
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.8 , pp. 2788-2793
    • Montoyo, H.P.1    Vaccaro, C.2    Hafner, M.3    Ober, R.J.4    Mueller, W.5    Ward, E.S.6
  • 132
    • 0031718315 scopus 로고    scopus 로고
    • Soluble tumor necrosis factor receptor (p75) fusion protein (ENBREL) as a therapy for rheumatoid arthritis
    • L.W. Moreland Soluble tumor necrosis factor receptor (p75) fusion protein (ENBREL) as a therapy for rheumatoid arthritis Rheum Dis Clin N Am 24 3 1998 579 591
    • (1998) Rheum Dis Clin N Am , vol.24 , Issue.3 , pp. 579-591
    • Moreland, L.W.1
  • 133
    • 84990306240 scopus 로고    scopus 로고
    • Artificial affinity proteins as ligands of immunoglobulins
    • B. Mouratou, G. Béhar, and F. Pecorari Artificial affinity proteins as ligands of immunoglobulins Biomolecules 5 1 2015 60 75
    • (2015) Biomolecules , vol.5 , Issue.1 , pp. 60-75
    • Mouratou, B.1    Béhar, G.2    Pecorari, F.3
  • 134
    • 77951621649 scopus 로고    scopus 로고
    • The transfer of maternal antigen-specific IgG regulates the development of allergic airway inflammation early in life in an FcRn-dependent manner
    • K. Nakata, K. Kobayashi, Y. Ishikawa, M. Yamamoto, Y. Funada, Y. Kotani, and et al. The transfer of maternal antigen-specific IgG regulates the development of allergic airway inflammation early in life in an FcRn-dependent manner Biochem Biophys Res Commun 395 2 2010 238 243
    • (2010) Biochem Biophys Res Commun , vol.395 , Issue.2 , pp. 238-243
    • Nakata, K.1    Kobayashi, K.2    Ishikawa, Y.3    Yamamoto, M.4    Funada, Y.5    Kotani, Y.6
  • 135
    • 84903779367 scopus 로고    scopus 로고
    • Characterization and screening of IgG binding to the neonatal Fc receptor
    • T. Neuber, K. Frese, J. Jaehrling, S. Jäger, D. Daubert, K. Felderer, and et al. Characterization and screening of IgG binding to the neonatal Fc receptor MAbs 6 4 2014 928 942
    • (2014) MAbs , vol.6 , Issue.4 , pp. 928-942
    • Neuber, T.1    Frese, K.2    Jaehrling, J.3    Jäger, S.4    Daubert, D.5    Felderer, K.6
  • 136
    • 33745712861 scopus 로고    scopus 로고
    • The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin
    • A. Nguyen, A.E. Reyes 2nd, M. Zhang, P. McDonald, W.L.T. Wong, L.A. Damico, and et al. The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin Protein Eng Des Sel 19 7 2006 291 297
    • (2006) Protein Eng des Sel , vol.19 , Issue.7 , pp. 291-297
    • Nguyen, A.1    Reyes, A.E.2    Zhang, M.3    McDonald, P.4    Wong, W.L.T.5    Damico, L.A.6
  • 137
    • 0024982210 scopus 로고
    • Serum albumin metabolism in rheumatic diseases: Relationship to corticosteroids and peptic ulcer
    • Y. Niwa, A. Iio, G. Niwa, T. Sakane, T. Tsunematsu, and T. Kanoh Serum albumin metabolism in rheumatic diseases: Relationship to corticosteroids and peptic ulcer J Clin Lab Immunol 31 1 1990 11 16
    • (1990) J Clin Lab Immunol , vol.31 , Issue.1 , pp. 11-16
    • Niwa, Y.1    Iio, A.2    Niwa, G.3    Sakane, T.4    Tsunematsu, T.5    Kanoh, T.6
  • 138
    • 3343010237 scopus 로고    scopus 로고
    • Exocytosis of IgG as mediated by the receptor, FcRn: An analysis at the single-molecule level
    • R.J. Ober, C. Martinez, X. Lai, J. Zhou, and E.S. Ward Exocytosis of IgG as mediated by the receptor, FcRn: An analysis at the single-molecule level Proc Natl Acad Sci U S A 101 30 2004 11076 11081
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.30 , pp. 11076-11081
    • Ober, R.J.1    Martinez, C.2    Lai, X.3    Zhou, J.4    Ward, E.S.5
  • 139
    • 0842343448 scopus 로고    scopus 로고
    • Visualizing the site and dynamics of IgG salvage by the MHC class I-related receptor, FcRn
    • R.J. Ober, C. Martinez, C. Vaccaro, J. Zhou, and E.S. Ward Visualizing the site and dynamics of IgG salvage by the MHC class I-related receptor, FcRn J Immunol 172 4 2004 2021 2029
    • (2004) J Immunol , vol.172 , Issue.4 , pp. 2021-2029
    • Ober, R.J.1    Martinez, C.2    Vaccaro, C.3    Zhou, J.4    Ward, E.S.5
  • 140
    • 0035210960 scopus 로고    scopus 로고
    • Differences in promiscuity for antibody-FcRn interactions across species: Implications for therapeutic antibodies
    • R.J. Ober, C.G. Radu, V. Ghetie, and E.S. Ward Differences in promiscuity for antibody-FcRn interactions across species: Implications for therapeutic antibodies Int Immunol 13 12 2001 1551 1559
    • (2001) Int Immunol , vol.13 , Issue.12 , pp. 1551-1559
    • Ober, R.J.1    Radu, C.G.2    Ghetie, V.3    Ward, E.S.4
  • 141
    • 84896265417 scopus 로고    scopus 로고
    • Structural insights into neonatal Fc receptor-based recycling mechanisms
    • V. Oganesyan, M.M. Damschroder, K.E. Cook, Q. Li, C. Gao, H. Wu, and et al. Structural insights into neonatal Fc receptor-based recycling mechanisms J Biol Chem 289 11 2014 7812 7824
    • (2014) J Biol Chem , vol.289 , Issue.11 , pp. 7812-7824
    • Oganesyan, V.1    Damschroder, M.M.2    Cook, K.E.3    Li, Q.4    Gao, C.5    Wu, H.6
  • 143
    • 0038555755 scopus 로고    scopus 로고
    • Biopolymer albumin for diagnosis and in drug delivery
    • G.V. Patil Biopolymer albumin for diagnosis and in drug delivery Drug Dev Res 58 3 2003 219 247
    • (2003) Drug Dev Res , vol.58 , Issue.3 , pp. 219-247
    • Patil, G.V.1
  • 144
    • 77952303814 scopus 로고    scopus 로고
    • Production of recombinant human erythropoietin/Fc fusion protein by genetically manipulated chickens
    • C.A. Penno, Y. Kawabe, A. Ito, and M. Kamihira Production of recombinant human erythropoietin/Fc fusion protein by genetically manipulated chickens Transgenic Res 19 2010 187 195
    • (2010) Transgenic Res , vol.19 , pp. 187-195
    • Penno, C.A.1    Kawabe, Y.2    Ito, A.3    Kamihira, M.4
  • 145
    • 84928394450 scopus 로고    scopus 로고
    • Dissecting stromal-epithelial interactions in a 3D in vitro cellularized intestinal model for permeability studies
    • C. Pereira, F. Araújo, C.C. Barrias, P.L. Granja, and B. Sarmento Dissecting stromal-epithelial interactions in a 3D in vitro cellularized intestinal model for permeability studies Biomaterials 56 2015 36 45
    • (2015) Biomaterials , vol.56 , pp. 36-45
    • Pereira, C.1    Araújo, F.2    Barrias, C.C.3    Granja, P.L.4    Sarmento, B.5
  • 146
    • 0003626648 scopus 로고
    • 4 - Genetics: The albumin gene
    • T.B.T.-A.A.A. Peters, Academic Press San Diego
    • T. Peters Jr. 4 - Genetics: The albumin gene T.B.T.-A.A.A. Peters, All about albumin 1995 Academic Press San Diego 133 187
    • (1995) All about Albumin , pp. 133-187
    • Peters, T.1
  • 147
    • 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
    • S.B. Petkova, S. Akilesh, T.J. Sproule, G.J. Christianson, H. Al Khabbaz, A.C. Brown, and et al. 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 12 2006 1759 1769
    • (2006) Int Immunol , vol.18 , Issue.12 , 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
  • 148
    • 77952168147 scopus 로고    scopus 로고
    • Targeted delivery for breast cancer therapy: The history of nanoparticle-albumin-bound paclitaxel
    • F. Petrelli, K. Borgonovo, and S. Barni Targeted delivery for breast cancer therapy: The history of nanoparticle-albumin-bound paclitaxel Expert Opin Pharmacother 11 8 2010 1413 1432
    • (2010) Expert Opin Pharmacother , vol.11 , Issue.8 , pp. 1413-1432
    • Petrelli, F.1    Borgonovo, K.2    Barni, S.3
  • 149
    • 84882799443 scopus 로고    scopus 로고
    • A novel hypothesis for an alkaline phosphatase "rescue" mechanism in the hepatic acute phase immune response
    • A.F. Pike, N.I. Kramer, B.J. Blaauboer, W. Seinen, and R. Brands A novel hypothesis for an alkaline phosphatase "rescue" mechanism in the hepatic acute phase immune response Biochim Biophys Acta Mol basis Dis 1832 12 2013 2044 2056
    • (2013) Biochim Biophys Acta Mol Basis Dis , vol.1832 , Issue.12 , pp. 2044-2056
    • Pike, A.F.1    Kramer, N.I.2    Blaauboer, B.J.3    Seinen, W.4    Brands, R.5
  • 150
    • 0031280052 scopus 로고    scopus 로고
    • Rigidification of the alpha2 helix of an MHC class I molecule by a valine to proline mutation in position 165 does not prevent peptide-specific antigen presentation
    • D. Plaksin, K. Polakova, M.G. Mage, and D.H. Margulies Rigidification of the alpha2 helix of an MHC class I molecule by a valine to proline mutation in position 165 does not prevent peptide-specific antigen presentation J Immunol 159 9 1997 4408 4414
    • (1997) J Immunol , vol.159 , Issue.9 , pp. 4408-4414
    • Plaksin, D.1    Polakova, K.2    Mage, M.G.3    Margulies, D.H.4
  • 151
    • 0030130749 scopus 로고    scopus 로고
    • The stoichiometry and affinity of the interaction of murine Fc fragments with the MHC class I-related receptor, FcRn
    • S. Popov, J.G. Hubbard, J. Kim, B. Ober, V. Ghetie, and E.S. Ward The stoichiometry and affinity of the interaction of murine Fc fragments with the MHC class I-related receptor, FcRn Mol Immunol 33 6 1996 521 530
    • (1996) Mol Immunol , vol.33 , Issue.6 , pp. 521-530
    • Popov, S.1    Hubbard, J.G.2    Kim, J.3    Ober, B.4    Ghetie, V.5    Ward, E.S.6
  • 153
    • 34347209969 scopus 로고    scopus 로고
    • Elucidation of intracellular recycling pathways leading to exocytosis of the Fc receptor, FcRn, by using multifocal plane microscopy
    • P. Prabhat, Z. Gan, J. Chao, S. Ram, C. Vaccaro, S. Gibbons, and et al. Elucidation of intracellular recycling pathways leading to exocytosis of the Fc receptor, FcRn, by using multifocal plane microscopy Proc Natl Acad Sci U S A 104 14 2007 5889 5894
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.14 , pp. 5889-5894
    • Prabhat, P.1    Gan, Z.2    Chao, J.3    Ram, S.4    Vaccaro, C.5    Gibbons, S.6
  • 154
    • 84890028543 scopus 로고    scopus 로고
    • Transepithelial transport of Fc-targeted nanoparticles by the neonatal Fc receptor for oral delivery
    • E.M. Pridgen, F. Alexis, T.T. Kuo, E. Levy-Nissenbaum, R. Karnik, R.S. Blumberg, and et al. Transepithelial transport of Fc-targeted nanoparticles by the neonatal Fc receptor for oral delivery Sci Transl Med 5 2013 213ra167
    • (2013) Sci Transl Med , vol.5
    • Pridgen, E.M.1    Alexis, F.2    Kuo, T.T.3    Levy-Nissenbaum, E.4    Karnik, R.5    Blumberg, R.S.6
  • 155
    • 84891627700 scopus 로고    scopus 로고
    • Humanized FcRn mouse models for evaluating pharmacokinetics of human IgG antibodies
    • G. Proetzel, and D.C. Roopenian Humanized FcRn mouse models for evaluating pharmacokinetics of human IgG antibodies Methods 65 1 2014 148 153
    • (2014) Methods , vol.65 , Issue.1 , pp. 148-153
    • Proetzel, G.1    Roopenian, D.C.2
  • 156
    • 84897037852 scopus 로고    scopus 로고
    • Genetically engineered humanized mouse models for preclinical antibody studies
    • G. Proetzel, M.V. Wiles, and D.C. Roopenian Genetically engineered humanized mouse models for preclinical antibody studies BioDrugs 28 2 2014 171 180
    • (2014) BioDrugs , vol.28 , Issue.2 , pp. 171-180
    • Proetzel, G.1    Wiles, M.V.2    Roopenian, D.C.3
  • 157
    • 0028808880 scopus 로고
    • Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants
    • M. Raghavan, V.R. Bonagura, S.L. Morrison, and P.J. Bjorkman Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants Biochemistry 34 45 1995 14649 14657
    • (1995) Biochemistry , vol.34 , Issue.45 , pp. 14649-14657
    • Raghavan, M.1    Bonagura, V.R.2    Morrison, S.L.3    Bjorkman, P.J.4
  • 158
    • 0028467948 scopus 로고
    • Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand
    • M. Raghavan, M.Y. Chen, L.N. Gastinel, and P.J. Bjorkman Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand Immunity 1 4 1994 303 315
    • (1994) Immunity , vol.1 , Issue.4 , pp. 303-315
    • Raghavan, M.1    Chen, M.Y.2    Gastinel, L.N.3    Bjorkman, P.J.4
  • 159
    • 0027249327 scopus 로고
    • The class I major histocompatibility complex related Fc receptor shows pH-dependent stability differences correlating with immunoglobulin binding and release
    • M. Raghavan, L.N. Gastinel, and P.J. Bjorkman The class I major histocompatibility complex related Fc receptor shows pH-dependent stability differences correlating with immunoglobulin binding and release Biochemistry 32 33 1993 8654 8660
    • (1993) Biochemistry , vol.32 , Issue.33 , pp. 8654-8660
    • Raghavan, M.1    Gastinel, L.N.2    Bjorkman, P.J.3
  • 160
    • 84932132043 scopus 로고    scopus 로고
    • Fc-fusion proteins and FcRn: Structural insights for longer-lasting and more effective therapeutics
    • T. Rath, K. Baker, J.a. Dumont, R.T. Peters, H. Jiang, S.-W. Qiao, and et al. Fc-fusion proteins and FcRn: Structural insights for longer-lasting and more effective therapeutics Crit Rev Biotechnol 35 2 2015 235 254
    • (2015) Crit Rev Biotechnol , vol.35 , Issue.2 , pp. 235-254
    • Rath, T.1    Baker, K.2    Dumont, J.A.3    Peters, R.T.4    Jiang, H.5    Qiao, S.-W.6
  • 161
    • 84919496171 scopus 로고    scopus 로고
    • Regulation of immune responses by the neonatal Fc receptor and its therapeutic implications
    • T. Rath, K. Baker, M. Pyzik, and R.S. Blumberg Regulation of immune responses by the neonatal Fc receptor and its therapeutic implications Front Immunol 5 2014
    • (2014) Front Immunol , vol.5
    • Rath, T.1    Baker, K.2    Pyzik, M.3    Blumberg, R.S.4
  • 163
    • 0025134727 scopus 로고
    • Isolation and characterization of the Fc receptor from the fetal yolk sac of the rat
    • D.M. Roberts, M. Guenthert, and R. Rodewald Isolation and characterization of the Fc receptor from the fetal yolk sac of the rat J Cell Biol 111 5 I 1990 1867 1876
    • (1990) J Cell Biol , vol.111 , Issue.5 I , pp. 1867-1876
    • Roberts, D.M.1    Guenthert, M.2    Rodewald, R.3
  • 164
    • 0017166982 scopus 로고
    • PH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat
    • R. Rodewald pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat J Cell Biol 71 2 1976 666 669
    • (1976) J Cell Biol , vol.71 , Issue.2 , pp. 666-669
    • Rodewald, R.1
  • 165
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • D.C. Roopenian, and S. Akilesh FcRn: The neonatal Fc receptor comes of age Nat Rev Immunol 7 August 2007 715 725
    • (2007) Nat Rev Immunol , vol.7 , Issue.August , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 166
    • 0037379288 scopus 로고    scopus 로고
    • The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs
    • D.C. Roopenian, G.J. Christianson, T.J. Sproule, A.C. Brown, S. Akilesh, N. Jung, and et al. The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs J Immunol 170 7 2003 3528 3533
    • (2003) J Immunol , vol.170 , Issue.7 , pp. 3528-3533
    • Roopenian, D.C.1    Christianson, G.J.2    Sproule, T.J.3    Brown, A.C.4    Akilesh, S.5    Jung, N.6
  • 167
    • 84924619421 scopus 로고    scopus 로고
    • Albumin-deficient mouse models for studying metabolism of human albumin and pharmacokinetics of albumin-based drugs
    • D.C. Roopenian, B.E. Low, G.J. Christianson, G. Proetzel, T.J. Sproule, and M.V. Wiles Albumin-deficient mouse models for studying metabolism of human albumin and pharmacokinetics of albumin-based drugs MAbs 7 2 2015 344 351
    • (2015) MAbs , vol.7 , Issue.2 , pp. 344-351
    • Roopenian, D.C.1    Low, B.E.2    Christianson, G.J.3    Proetzel, G.4    Sproule, T.J.5    Wiles, M.V.6
  • 168
    • 84929465177 scopus 로고    scopus 로고
    • Post-translational modification of a chimeric EPO-Fc hormone is more important than its molecular size in defining its in vivo hematopoietic activity
    • E.R. Salgado, R. Montesino, S.P. Jimenez, M. Gonzalez, F. Hugues, O.I. Cabezas, and et al. Post-translational modification of a chimeric EPO-Fc hormone is more important than its molecular size in defining its in vivo hematopoietic activity Biochim Biophys Acta 1850 9 2015 1685 1693
    • (2015) Biochim Biophys Acta , vol.1850 , Issue.9 , pp. 1685-1693
    • Salgado, E.R.1    Montesino, R.2    Jimenez, S.P.3    Gonzalez, M.4    Hugues, F.5    Cabezas, O.I.6
  • 169
    • 0039643451 scopus 로고    scopus 로고
    • Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand
    • L.M. Sánchez, D.M. Penny, and P.J. Bjorkman Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand Biochemistry 38 29 1999 9471 9476
    • (1999) Biochemistry , vol.38 , Issue.29 , pp. 9471-9476
    • Sánchez, L.M.1    Penny, D.M.2    Bjorkman, P.J.3
  • 170
    • 84926670297 scopus 로고    scopus 로고
    • Unraveling the interaction between FcRn and albumin: Opportunities for design of albumin-based therapeutics
    • K.M.K. Sand, M. Bern, J. Nilsen, H.T. Noordzij, I. Sandlie, and J.T. Andersen Unraveling the interaction between FcRn and albumin: Opportunities for design of albumin-based therapeutics Front Immunol 5 January 2015 1 21
    • (2015) Front Immunol , vol.5 , Issue.January , pp. 1-21
    • Sand, K.M.K.1    Bern, M.2    Nilsen, J.3    Noordzij, H.T.4    Sandlie, I.5    Andersen, J.T.6
  • 171
    • 84902449067 scopus 로고    scopus 로고
    • Dissection of the neonatal Fc receptor (FcRn)-albumin interface using mutagenesis and anti-FcRn albumin-blocking antibodies
    • K.M.K. Sand, B. Dalhus, G.J. Christianson, M. Bern, S. Foss, J. Cameron, and et al. Dissection of the neonatal Fc receptor (FcRn)-albumin interface using mutagenesis and anti-FcRn albumin-blocking antibodies J Biol Chem 289 24 2014 17228 17239
    • (2014) J Biol Chem , vol.289 , Issue.24 , pp. 17228-17239
    • Sand, K.M.K.1    Dalhus, B.2    Christianson, G.J.3    Bern, M.4    Foss, S.5    Cameron, J.6
  • 172
    • 69849108449 scopus 로고    scopus 로고
    • Renal FcRn reclaims albumin but facilitates elimination of IgG
    • M. Sarav, Y. Wang, B.K. Hack, A. Chang, M. Jensen, L. Bao, and et al. Renal FcRn reclaims albumin but facilitates elimination of IgG J Am Soc Nephrol 20 9 2009 1941 1952
    • (2009) J Am Soc Nephrol , vol.20 , Issue.9 , pp. 1941-1952
    • Sarav, M.1    Wang, Y.2    Hack, B.K.3    Chang, A.4    Jensen, M.5    Bao, L.6
  • 173
    • 0036079202 scopus 로고    scopus 로고
    • Expression of the neonatal Fc receptor (FcRn) at the blood-brain barrier
    • F. Schlachetzki, C. Zhu, and W.M. Pardridge Expression of the neonatal Fc receptor (FcRn) at the blood-brain barrier J Neurochem 81 1 2002 203 206
    • (2002) J Neurochem , vol.81 , Issue.1 , pp. 203-206
    • Schlachetzki, F.1    Zhu, C.2    Pardridge, W.M.3
  • 174
    • 84887332244 scopus 로고    scopus 로고
    • Crystal structure of an HSA/FcRn complex reveals recycling by competitive mimicry of HSA ligands at a pH-dependent hydrophobic interface
    • M.M. Schmidt, S.A. Townson, A.J. Andreucci, B.M. King, E.B. Schirmer, A.J. Murillo, and et al. Crystal structure of an HSA/FcRn complex reveals recycling by competitive mimicry of HSA ligands at a pH-dependent hydrophobic interface Structure 21 11 2013 1966 1978
    • (2013) Structure , vol.21 , Issue.11 , pp. 1966-1978
    • Schmidt, M.M.1    Townson, S.A.2    Andreucci, A.J.3    King, B.M.4    Schirmer, E.B.5    Murillo, A.J.6
  • 175
    • 0027080479 scopus 로고
    • Antibodies to SPARC inhibit albumin binding to SPARC, gp60, and microvascular endothelium
    • J.E. Schnitzer, and P. Oh Antibodies to SPARC inhibit albumin binding to SPARC, gp60, and microvascular endothelium Am J Phys 263 6 Pt 2 1992 H1872 H1879
    • (1992) Am J Phys , vol.263 , Issue.6 , pp. H1872-H1879
    • Schnitzer, J.E.1    Oh, P.2
  • 176
    • 0002820899 scopus 로고
    • Albumin interacts specifically with a 60-kDa microvascular endothelial glycoprotein
    • J.E. Schnitzer, W.W. Carley, and G.E. Palade Albumin interacts specifically with a 60-kDa microvascular endothelial glycoprotein Proc Natl Acad Sci U S A 85 18 1988 6773 6777
    • (1988) Proc Natl Acad Sci U S A , vol.85 , Issue.18 , pp. 6773-6777
    • Schnitzer, J.E.1    Carley, W.W.2    Palade, G.E.3
  • 177
    • 84929190423 scopus 로고    scopus 로고
    • Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics
    • A. Schoch, H. Kettenberger, O. Mundigl, G. Winter, J. Engert, J. Heinrich, and et al. Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics Proc Natl Acad Sci 112 19 2015 5997 6002
    • (2015) Proc Natl Acad Sci , vol.112 , Issue.19 , pp. 5997-6002
    • Schoch, A.1    Kettenberger, H.2    Mundigl, O.3    Winter, G.4    Engert, J.5    Heinrich, J.6
  • 178
    • 0033367382 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of recombinant mouse FcRn with murine IgG1
    • P. Schuck, C.G. Radu, and E.S. Ward Sedimentation equilibrium analysis of recombinant mouse FcRn with murine IgG1 Mol Immunol 36 15-16 1999 1117 1125
    • (1999) Mol Immunol , vol.36 , Issue.15-16 , pp. 1117-1125
    • Schuck, P.1    Radu, C.G.2    Ward, E.S.3
  • 181
    • 79952116455 scopus 로고    scopus 로고
    • Human serum albumin nanoparticles as an efficient noscapine drug delivery system for potential use in breast cancer: Preparation and in vitro analysis
    • S. Sebak, M. Mirzaei, M. Malhotra, A. Kulamarva, and S. Prakash Human serum albumin nanoparticles as an efficient noscapine drug delivery system for potential use in breast cancer: Preparation and in vitro analysis Int J Nanomedicine 5 1 2010 525 532
    • (2010) Int J Nanomedicine , vol.5 , Issue.1 , pp. 525-532
    • Sebak, S.1    Mirzaei, M.2    Malhotra, M.3    Kulamarva, A.4    Prakash, S.5
  • 182
    • 84915818878 scopus 로고    scopus 로고
    • An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein
    • J. Seijsing, M. Lindborg, I. Hoiden-Guthenberg, H. Bonisch, E. Guneriusson, F.Y. Frejd, and et al. An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein Proc Natl Acad Sci U S A 111 48 2014 17110 17115
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.48 , pp. 17110-17115
    • Seijsing, J.1    Lindborg, M.2    Hoiden-Guthenberg, I.3    Bonisch, H.4    Guneriusson, E.5    Frejd, F.Y.6
  • 183
    • 84945471631 scopus 로고    scopus 로고
    • Autoantibodies in autoimmune liver diseases
    • A.G. Sener Autoantibodies in autoimmune liver diseases APMIS 123 11 2015 915 919
    • (2015) APMIS , vol.123 , Issue.11 , pp. 915-919
    • Sener, A.G.1
  • 186
    • 84904543699 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of recombinant human EPO-Fc fusion protein in vivo
    • X. Shi, J. Yang, H. Zhu, L. Ye, M. Feng, J. Li, and et al. Pharmacokinetics and pharmacodynamics of recombinant human EPO-Fc fusion protein in vivo PLoS One 8 8 2013 e72673
    • (2013) PLoS One , vol.8 , Issue.8
    • Shi, X.1    Yang, J.2    Zhu, H.3    Ye, L.4    Feng, M.5    Li, J.6
  • 187
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • R.L. Shields, A.K. Namenuk, K. Hong, Y.G. Meng, J. Rae, J. Briggs, and et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R J Biol Chem 276 9 2001 6591 6604
    • (2001) J Biol Chem , vol.276 , Issue.9 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6
  • 188
    • 0024529856 scopus 로고
    • An Fc receptor structurally related to MHC class I antigens
    • N.E. Simister, and K.E. Mostov An Fc receptor structurally related to MHC class I antigens Nature 337 6203 1989 184 187
    • (1989) Nature , vol.337 , Issue.6203 , pp. 184-187
    • Simister, N.E.1    Mostov, K.E.2
  • 189
    • 0029901782 scopus 로고    scopus 로고
    • An IgG-transporting Fc receptor expressed in the syncytiotrophoblast of human placenta
    • N.E. Simister, C.M. Story, H.L. Chen, and J.S. Hunt An IgG-transporting Fc receptor expressed in the syncytiotrophoblast of human placenta Eur J Immunol 26 7 1996 1527 1531
    • (1996) Eur J Immunol , vol.26 , Issue.7 , pp. 1527-1531
    • Simister, N.E.1    Story, C.M.2    Chen, H.L.3    Hunt, J.S.4
  • 190
    • 84928321728 scopus 로고    scopus 로고
    • Albumin and its application in drug delivery
    • D. Sleep Albumin and its application in drug delivery Expert Opin Drug Deliv 12 5 2015 793 812
    • (2015) Expert Opin Drug Deliv , vol.12 , Issue.5 , pp. 793-812
    • Sleep, D.1
  • 191
    • 84885370061 scopus 로고    scopus 로고
    • Albumin as a versatile platform for drug half-life extension
    • D. Sleep, J. Cameron, and L.R. Evans Albumin as a versatile platform for drug half-life extension Biochim Biophys Acta 1830 12 2013 5526 5534
    • (2013) Biochim Biophys Acta , vol.1830 , Issue.12 , pp. 5526-5534
    • Sleep, D.1    Cameron, J.2    Evans, L.R.3
  • 192
    • 84940955731 scopus 로고    scopus 로고
    • The neonatal Fc receptor, FcRn, as a target for drug delivery and therapy
    • J.T. Sockolosky, and F.C. Szoka The neonatal Fc receptor, FcRn, as a target for drug delivery and therapy Adv Drug Deliv Rev 91 30 2015 109 124
    • (2015) Adv Drug Deliv Rev , vol.91 , Issue.30 , pp. 109-124
    • Sockolosky, J.T.1    Szoka, F.C.2
  • 193
    • 84904816388 scopus 로고    scopus 로고
    • Fusion of a short peptide that binds immunoglobulin G to a recombinant protein substantially increases its plasma half-life in mice
    • J.T. Sockolosky, S. Kivimae, and F.C. Szoka Fusion of a short peptide that binds immunoglobulin G to a recombinant protein substantially increases its plasma half-life in mice PLoS One 9 7 2014 e102566
    • (2014) PLoS One , vol.9 , Issue.7
    • Sockolosky, J.T.1    Kivimae, S.2    Szoka, F.C.3
  • 194
    • 0033981633 scopus 로고    scopus 로고
    • Rab GTPases coordinate endocytosis
    • Somsel Rodman, J., Wandinger-Ness, A., 2000. Rab GTPases coordinate endocytosis. J Cell Sci 113 Pt 2 pp. 183-192.
    • (2000) J Cell Sci , vol.113 , pp. 183-192
    • Somsel Rodman, J.1    Wandinger-Ness, A.2
  • 195
    • 0037025895 scopus 로고    scopus 로고
    • Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: Functional expression of FcRn in the mammalian lung
    • G.M. Spiekermann, P.W. Finn, E.S. Ward, J. Dumont, B.L. Dickinson, R.S. Blumberg, and et al. Receptor-mediated immunoglobulin G transport across mucosal barriers in adult life: Functional expression of FcRn in the mammalian lung J Exp Med 196 3 2002 303 310
    • (2002) J Exp Med , vol.196 , Issue.3 , 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
  • 197
    • 0030842545 scopus 로고    scopus 로고
    • Plasma protein (albumin) catabolism by the tumor itself - Implications for tumor metabolism and the genesis of cachexia
    • G. Stehle, H. Sinn, A. Wunder, H.H. Schrenk, J.C. Stewart, G. Hartung, and et al. Plasma protein (albumin) catabolism by the tumor itself - implications for tumor metabolism and the genesis of cachexia Crit Rev Oncol Hematol 26 2 1997 77 100
    • (1997) Crit Rev Oncol Hematol , vol.26 , Issue.2 , pp. 77-100
    • Stehle, G.1    Sinn, H.2    Wunder, A.3    Schrenk, H.H.4    Stewart, J.C.5    Hartung, G.6
  • 199
    • 84892615437 scopus 로고    scopus 로고
    • Computational design of a pH-sensitive IgG binding protein
    • E.-M. Strauch, S.J. Fleishman, and D. Baker Computational design of a pH-sensitive IgG binding protein Proc Natl Acad Sci U S A 111 2 2014 675 680
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.2 , pp. 675-680
    • Strauch, E.-M.1    Fleishman, S.J.2    Baker, D.3
  • 200
    • 84941423766 scopus 로고    scopus 로고
    • Fusion proteins for half-life extension of biologics as a strategy to make biobetters
    • W.R. Strohl Fusion proteins for half-life extension of biologics as a strategy to make biobetters BioDrugs 29 4 2015 215 239
    • (2015) BioDrugs , vol.29 , Issue.4 , pp. 215-239
    • Strohl, W.R.1
  • 201
    • 84880925050 scopus 로고    scopus 로고
    • The glomerular basement membrane as a barrier to albumin
    • J.H. Suh, and J.H. Miner The glomerular basement membrane as a barrier to albumin Nat Rev Nephrol 9 8 2013 470 477
    • (2013) Nat Rev Nephrol , vol.9 , Issue.8 , pp. 470-477
    • Suh, J.H.1    Miner, J.H.2
  • 202
    • 84855499391 scopus 로고    scopus 로고
    • Trends in the treatment of anemia using recombinant human erythropoietin in patients with HIV infection
    • P.S. Sullivan, D.L. Hanson, J.T. Richardson, and J.T. Brooks Trends in the treatment of anemia using recombinant human erythropoietin in patients with HIV infection Open AIDS J 5 2011 113 118
    • (2011) Open AIDS J , vol.5 , pp. 113-118
    • Sullivan, P.S.1    Hanson, D.L.2    Richardson, J.T.3    Brooks, J.T.4
  • 203
    • 84904120482 scopus 로고    scopus 로고
    • Use of Fc-engineered antibodies as clearing agents to increase contrast during PET
    • R. Swiercz, S. Chiguru, A. Tahmasbi, S.M. Ramezani, G. Hao, D.K. Challa, and et al. Use of Fc-engineered antibodies as clearing agents to increase contrast during PET J Nucl Med 55 7 2014 1204 1207
    • (2014) J Nucl Med , vol.55 , Issue.7 , pp. 1204-1207
    • Swiercz, R.1    Chiguru, S.2    Tahmasbi, A.3    Ramezani, S.M.4    Hao, G.5    Challa, D.K.6
  • 204
    • 84877898507 scopus 로고    scopus 로고
    • Correlations between pharmacokinetics of IgG antibodies in primates vs. FcRn-transgenic mice reveal a rodent model with predictive capabilities
    • S.H. Tam, S.G. McCarthy, K. Brosnan, K.M. Goldberg, and B.J. Scallon Correlations between pharmacokinetics of IgG antibodies in primates vs. FcRn-transgenic mice reveal a rodent model with predictive capabilities MAbs 5 3 2013 397 405
    • (2013) MAbs , vol.5 , Issue.3 , pp. 397-405
    • Tam, S.H.1    McCarthy, S.G.2    Brosnan, K.3    Goldberg, K.M.4    Scallon, B.J.5
  • 205
    • 84958550123 scopus 로고    scopus 로고
    • An update on myasthenia gravis, challenging disease for the dental profession
    • A. Tamburrini, F. Tacconi, A.C. Barlattani, and T. Mineo An update on myasthenia gravis, challenging disease for the dental profession J Oral Sci 57 3 2015 161 168
    • (2015) J Oral Sci , vol.57 , Issue.3 , pp. 161-168
    • Tamburrini, A.1    Tacconi, F.2    Barlattani, A.C.3    Mineo, T.4
  • 206
    • 84897875076 scopus 로고    scopus 로고
    • Distribution of rat neonatal Fc receptor in the principal organs of neonatal and pubertal rats
    • Z. Tian, B.J. Sutton, and X. Zhang Distribution of rat neonatal Fc receptor in the principal organs of neonatal and pubertal rats J Recept Signal Transduct Res 9893 2 2014 1 6
    • (2014) J Recept Signal Transduct Res , vol.9893 , Issue.2 , pp. 1-6
    • Tian, Z.1    Sutton, B.J.2    Zhang, X.3
  • 207
    • 0037817352 scopus 로고    scopus 로고
    • Transcytosis: Crossing cellular barriers
    • P.L. Tuma, and A.L. Hubbard Transcytosis: Crossing cellular barriers Physiol Rev 83 2003 871 932
    • (2003) Physiol Rev , vol.83 , pp. 871-932
    • Tuma, P.L.1    Hubbard, A.L.2
  • 208
    • 66149115113 scopus 로고    scopus 로고
    • The recycling and transcytotic pathways for IgG transport by FcRn are distinct and display an inherent polarity
    • S. Tzaban, R.H. Massol, E. Yen, W. Hamman, S.R. Frank, L.A. Lapierre, and et al. The recycling and transcytotic pathways for IgG transport by FcRn are distinct and display an inherent polarity J Cell Biol 185 4 2009 673 684
    • (2009) J Cell Biol , vol.185 , Issue.4 , pp. 673-684
    • Tzaban, S.1    Massol, R.H.2    Yen, E.3    Hamman, W.4    Frank, S.R.5    Lapierre, L.A.6
  • 209
    • 33845484193 scopus 로고    scopus 로고
    • Divergent activities of an engineered antibody in murine and human systems have implications for therapeutic antibodies
    • C. Vaccaro, R. Bawdon, S. Wanjie, R.J. Ober, and E.S. Ward Divergent activities of an engineered antibody in murine and human systems have implications for therapeutic antibodies Proc Natl Acad Sci U S A 103 49 2006 18709 18714
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.49 , pp. 18709-18714
    • Vaccaro, C.1    Bawdon, R.2    Wanjie, S.3    Ober, R.J.4    Ward, E.S.5
  • 210
    • 27144465484 scopus 로고    scopus 로고
    • Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels
    • C. Vaccaro, J. Zhou, R.J. Ober, and E.S. Ward Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels Nat Biotechnol 23 10 2005 1283 1288
    • (2005) Nat Biotechnol , vol.23 , Issue.10 , pp. 1283-1288
    • Vaccaro, C.1    Zhou, J.2    Ober, R.J.3    Ward, E.S.4
  • 211
    • 0032518373 scopus 로고    scopus 로고
    • Structural basis of pH-dependent antibody binding by the neonatal Fc receptor
    • D.E. Vaughn, and P.J. Bjorkman Structural basis of pH-dependent antibody binding by the neonatal Fc receptor Structure 6 1 1998 63 73
    • (1998) Structure , vol.6 , Issue.1 , pp. 63-73
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 213
    • 84938836458 scopus 로고    scopus 로고
    • Erythropoietin protects neuroblastoma cells against etoposide and vincristine by activating ERK and AKT pathways but has no effect in kidney cells
    • M.J. Vazquez-Mellado, C. Aguilar, and L. Rocha-Zavaleta Erythropoietin protects neuroblastoma cells against etoposide and vincristine by activating ERK and AKT pathways but has no effect in kidney cells Life Sci 137 2015 142 149
    • (2015) Life Sci , vol.137 , pp. 142-149
    • Vazquez-Mellado, M.J.1    Aguilar, C.2    Rocha-Zavaleta, L.3
  • 214
    • 84955487504 scopus 로고    scopus 로고
    • Generation of a double transgenic humanized neonatal Fc receptor (FcRn)/albumin mouse to study the pharmacokinetics of albumin-linked drugs
    • D. Viuff, F. Antunes, L. Evans, J. Cameron, H. Dyrnesli, B. Thue Ravn, and et al. Generation of a double transgenic humanized neonatal Fc receptor (FcRn)/albumin mouse to study the pharmacokinetics of albumin-linked drugs J Control Release 223 2016 22 30
    • (2016) J Control Release , vol.223 , pp. 22-30
    • Viuff, D.1    Antunes, F.2    Evans, L.3    Cameron, J.4    Dyrnesli, H.5    Thue Ravn, B.6
  • 215
    • 84859269939 scopus 로고    scopus 로고
    • Fc-mediated transport of nanoparticles across airway epithelial cell layers
    • D. Vllasaliu, C. Alexander, M. Garnett, M. Eaton, and S. Stolnik Fc-mediated transport of nanoparticles across airway epithelial cell layers J Control Release 158 3 2012 479 486
    • (2012) J Control Release , vol.158 , Issue.3 , pp. 479-486
    • Vllasaliu, D.1    Alexander, C.2    Garnett, M.3    Eaton, M.4    Stolnik, S.5
  • 216
    • 84873744195 scopus 로고    scopus 로고
    • Discovery and structure-activity relationships of small molecules that block the human immunoglobulin G-human neonatal Fc receptor (hIgG-hFcRn) protein-protein interaction
    • Z. Wang, C. Fraley, and A.R. Mezo Discovery and structure-activity relationships of small molecules that block the human immunoglobulin G-human neonatal Fc receptor (hIgG-hFcRn) protein-protein interaction Bioorg Med Chem Lett 23 5 2013 1253 1256
    • (2013) Bioorg Med Chem Lett , vol.23 , Issue.5 , pp. 1253-1256
    • Wang, Z.1    Fraley, C.2    Mezo, A.R.3
  • 217
    • 84898433336 scopus 로고    scopus 로고
    • Neonatal Fc receptor (FcRn): A novel target for therapeutic antibodies and antibody engineering
    • Y. Wang, Z. Tian, D. Thirumalai, and X. Zhang Neonatal Fc receptor (FcRn): A novel target for therapeutic antibodies and antibody engineering J Drug Target 22 4 2014 269 278
    • (2014) J Drug Target , vol.22 , Issue.4 , pp. 269-278
    • Wang, Y.1    Tian, Z.2    Thirumalai, D.3    Zhang, X.4
  • 218
    • 69949115639 scopus 로고    scopus 로고
    • Multitasking by exploitation of intracellular transport functions the many faces of FcRn
    • Elsevier Inc. United States
    • E.S. Ward, and R.J. Ober Multitasking by exploitation of intracellular transport functions the many faces of FcRn Advances in immunology 2009 Elsevier Inc. United States 77 115 10.1016/S0065-2776(09)03004-1
    • (2009) Advances in Immunology , pp. 77-115
    • Ward, E.S.1    Ober, R.J.2
  • 219
    • 84879047058 scopus 로고    scopus 로고
    • Modelling the endothelial blood-CNS barriers: A method for the production of robust in vitro models of the rat blood-brain barrier and blood-spinal cord barrier
    • P.M.D. Watson, J.C. Paterson, G. Thom, U. Ginman, S. Lundquist, and C.I. Webster Modelling the endothelial blood-CNS barriers: A method for the production of robust in vitro models of the rat blood-brain barrier and blood-spinal cord barrier BMC Neurosci 14 1 2013 59
    • (2013) BMC Neurosci , vol.14 , Issue.1 , pp. 59
    • Watson, P.M.D.1    Paterson, J.C.2    Thom, G.3    Ginman, U.4    Lundquist, S.5    Webster, C.I.6
  • 220
    • 84881058016 scopus 로고    scopus 로고
    • Multivalent immune complexes divert FcRn to lysosomes by exclusion from recycling sorting tubules
    • A.W. Weflen, N. Baier, Q.-J. Tang, M. Van den Hof, R.S. Blumberg, W.I. Lencer, and et al. Multivalent immune complexes divert FcRn to lysosomes by exclusion from recycling sorting tubules Mol Biol Cell 24 15 2013 2398 2405
    • (2013) Mol Biol Cell , vol.24 , Issue.15 , pp. 2398-2405
    • Weflen, A.W.1    Baier, N.2    Tang, Q.-J.3    Van Den Hof, M.4    Blumberg, R.S.5    Lencer, W.I.6
  • 221
    • 0034663798 scopus 로고    scopus 로고
    • Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor
    • A.P.J. West, and P.J. Bjorkman Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor Biochemistry 39 32 2000 9698 9708
    • (2000) Biochemistry , vol.39 , Issue.32 , pp. 9698-9708
    • West, A.P.J.1    Bjorkman, P.J.2
  • 223
    • 79751497661 scopus 로고    scopus 로고
    • Efficient mucosal vaccination mediated by the neonatal Fc receptor
    • L. Ye, R. Zeng, Y. Bai, D.C. Roopenian, and X. Zhu Efficient mucosal vaccination mediated by the neonatal Fc receptor Nat Biotechnol 29 2 2011 158 163
    • (2011) Nat Biotechnol , vol.29 , Issue.2 , pp. 158-163
    • Ye, L.1    Zeng, R.2    Bai, Y.3    Roopenian, D.C.4    Zhu, X.5
  • 224
    • 77951027408 scopus 로고    scopus 로고
    • A therapeutic anti-VEGF antibody with increased potency independent of pharmacokinetic half-life
    • Y.A. Yeung, X. Wu, A.E. Reyes 2nd, J.-M. Vernes, S. Lien, J. Lowe, and et al. A therapeutic anti-VEGF antibody with increased potency independent of pharmacokinetic half-life Cancer Res 70 8 2010 3269 3277
    • (2010) Cancer Res , vol.70 , Issue.8 , pp. 3269-3277
    • Yeung, Y.A.1    Wu, X.2    Reyes, A.E.3    Vernes, J.-M.4    Lien, S.5    Lowe, J.6
  • 225
    • 84883404242 scopus 로고    scopus 로고
    • Engineered soluble monomeric IgG1 CH3 domain generation, mechanisms of function, and implications for design of biological therapeutics
    • T. Ying, W. Chen, Y. Feng, Y. Wang, R. Gong, and D.S. Dimitrov Engineered soluble monomeric IgG1 CH3 domain generation, mechanisms of function, and implications for design of biological therapeutics J Biol Chem 288 35 2013 25154 25164
    • (2013) J Biol Chem , vol.288 , Issue.35 , pp. 25154-25164
    • Ying, T.1    Chen, W.2    Feng, Y.3    Wang, Y.4    Gong, R.5    Dimitrov, D.S.6
  • 226
    • 84899741811 scopus 로고    scopus 로고
    • Quantitative cumulative biodistribution of antibodies in mice: Effect of modulating binding affinity to the neonatal Fc receptor
    • V. Yip, E. Palma, D.B. Tesar, E.E. Mundo, D. Bumbaca, E.K. Torres, and et al. Quantitative cumulative biodistribution of antibodies in mice: Effect of modulating binding affinity to the neonatal Fc receptor MAbs 6 3 2014 689 696
    • (2014) MAbs , vol.6 , Issue.3 , pp. 689-696
    • Yip, V.1    Palma, E.2    Tesar, D.B.3    Mundo, E.E.4    Bumbaca, D.5    Torres, E.K.6
  • 227
    • 2942516894 scopus 로고    scopus 로고
    • Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells
    • M. Yoshida, S.M. Claypool, J.S. Wagner, E. Mizoguchi, A. Mizoguchi, D.C. Roopenian, and et al. Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells Immunity 20 2004 769 783
    • (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
  • 228
    • 33746684369 scopus 로고    scopus 로고
    • Neonatal Fc receptor for IgG regulates mucosal immune responses to luminal bacteria
    • M. Yoshida, K. Kobayashi, T.T. Kuo, L. Bry, J.N. Glickman, S.M. Claypool, and et al. Neonatal Fc receptor for IgG regulates mucosal immune responses to luminal bacteria J Clin Invest 116 8 2006 2142 2151
    • (2006) J Clin Invest , vol.116 , Issue.8 , pp. 2142-2151
    • Yoshida, M.1    Kobayashi, K.2    Kuo, T.T.3    Bry, L.4    Glickman, J.N.5    Claypool, S.M.6
  • 230
    • 0033802618 scopus 로고    scopus 로고
    • Cubilin- and megalin-mediated uptake of albumin in cultured proximal tubule cells of opossum kidney
    • X.Y. Zhai, R. Nielsen, H. Birn, K. Drumm, S. Mildenberger, R. Freudinger, and et al. Cubilin- and megalin-mediated uptake of albumin in cultured proximal tubule cells of opossum kidney Kidney Int 58 4 2000 1523 1533
    • (2000) Kidney Int , vol.58 , Issue.4 , pp. 1523-1533
    • Zhai, X.Y.1    Nielsen, R.2    Birn, H.3    Drumm, K.4    Mildenberger, S.5    Freudinger, R.6
  • 231
    • 78951478220 scopus 로고    scopus 로고
    • Translational pharmacokinetics and pharmacodynamics of an FcRn-variant anti-CD4 monoclonal antibody from preclinical model to phase I study
    • Y. Zheng, H. Scheerens, J.C.J. Davis, R. Deng, S.K. Fischer, C. Woods, and et al. Translational pharmacokinetics and pharmacodynamics of an FcRn-variant anti-CD4 monoclonal antibody from preclinical model to phase I study Clin Pharmacol Ther 89 2 2011 283 290
    • (2011) Clin Pharmacol Ther , vol.89 , Issue.2 , pp. 283-290
    • Zheng, Y.1    Scheerens, H.2    Davis, J.C.J.3    Deng, R.4    Fischer, S.K.5    Woods, C.6
  • 232
    • 0035284906 scopus 로고    scopus 로고
    • MHC class I-related neonatal Fc receptor for IgG is functionally expressed in monocytes, intestinal macrophages, and dendritic cells
    • X. Zhu, G. Meng, B.L. Dickinson, X. Li, E. Mizoguchi, L. Miao, and et al. MHC class I-related neonatal Fc receptor for IgG is functionally expressed in monocytes, intestinal macrophages, and dendritic cells J Immunol 166 5 2001 3266 3276
    • (2001) J Immunol , vol.166 , Issue.5 , pp. 3266-3276
    • Zhu, X.1    Meng, G.2    Dickinson, B.L.3    Li, X.4    Mizoguchi, E.5    Miao, L.6
  • 233
    • 0025373363 scopus 로고
    • Beta 2-microglobulin deficient mice lack CD4-8 + cytolytic T cells
    • M. Zijlstra, M. Bix, N.E. Simister, J.M. Loring, D.H. Raulet, and R. Jaenisch Beta 2-microglobulin deficient mice lack CD4-8 + cytolytic T cells Nature 344 6268 1990 742 746
    • (1990) Nature , vol.344 , Issue.6268 , pp. 742-746
    • Zijlstra, M.1    Bix, M.2    Simister, N.E.3    Loring, J.M.4    Raulet, D.H.5    Jaenisch, R.6
  • 234
    • 84921743801 scopus 로고    scopus 로고
    • Use of intravenous immunoglobulin in pediatric practice
    • B. Zülfikar, and B. Koç Use of intravenous immunoglobulin in pediatric practice Turkish Arch Pediatr Pediatr Arşivi 49 4 2014 282 288
    • (2014) Turkish Arch Pediatr Pediatr Arşivi , vol.49 , Issue.4 , pp. 282-288
    • Zülfikar, B.1    Koç, B.2


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