메뉴 건너뛰기




Volumn 1830, Issue 12, 2013, Pages 5526-5534

Albumin as a versatile platform for drug half-life extension

Author keywords

Albumin; Animal models; FcRn; Half life; Pharmacokinetics; Protein drug

Indexed keywords


EID: 84885370061     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.04.023     Document Type: Review
Times cited : (397)

References (106)
  • 1
    • 82755197856 scopus 로고    scopus 로고
    • Strategies for extended serum half-life of protein therapeutics
    • R.E. Kontermann Strategies for extended serum half-life of protein therapeutics Curr. Opin. Biotechnol. 22 2011 1 9
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 1-9
    • Kontermann, R.E.1
  • 2
    • 0003626648 scopus 로고    scopus 로고
    • Academic Press Inc. USA
    • T. Peters Jr. All About Albumin 1996 Academic Press Inc. USA 223 234
    • (1996) All about Albumin , pp. 223-234
    • Peters, Jr.T.1
  • 3
    • 33745508741 scopus 로고    scopus 로고
    • Perspective - FcRn transports albumin: Relevance to immunology and medicine
    • DOI 10.1016/j.it.2006.05.004, PII S1471490606001463
    • C.L. Anderson, C. Chadhury, J. Kim, C.L. Bronson, M.A. Wani, and S. Mohanty Perspective - FcRn transports albumin: relevance to immunology and medicine Trends Immunol. 27 2006 343 348 (Pubitemid 43963476)
    • (2006) Trends in Immunology , vol.27 , Issue.7 , pp. 343-348
    • Anderson, C.L.1    Chaudhury, C.2    Kim, J.3    Bronson, C.L.4    Wani, M.A.5    Mohanty, S.6
  • 4
    • 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
    • DOI 10.1016/j.clim.2006.09.001, PII S1521661606008722
    • 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 2007 146 155 (Pubitemid 46073892)
    • (2007) Clinical Immunology , vol.122 , Issue.2 , pp. 146-155
    • Kim, J.1    Hayton, W.L.2    Robinson, J.M.3    Anderson, C.L.4
  • 6
    • 0026493761 scopus 로고
    • Preferential interaction of albumin-binding proteins, gp30 and gp18, with conformationally modified albumins
    • J. Schnitzer, A. Sung, R. Horvat, and J. Bravo Preferential interaction of albumin-binding proteins, gp30 and gp18, with conformationally modified albumins J. Biol. Chem. 267 1992 24544 24553
    • (1992) J. Biol. Chem. , vol.267 , pp. 24544-24553
    • Schnitzer, J.1    Sung, A.2    Horvat, R.3    Bravo, J.4
  • 7
    • 0027478043 scopus 로고
    • High affinity binding, endocytosis and degradation of conformationally modified albumins
    • J. Schnitzer, and J. Bravo High affinity binding, endocytosis and degradation of conformationally modified albumins J. Biol. Chem. 268 1993 7562 7570
    • (1993) J. Biol. Chem. , vol.268 , pp. 7562-7570
    • Schnitzer, J.1    Bravo, J.2
  • 8
    • 0027931859 scopus 로고
    • Albondin-mediated capillary permeability to albumin
    • J. Schnitzer, and P. Oh Albondin-mediated capillary permeability to albumin J. Biol. Chem. 269 1994 6072 6082
    • (1994) J. Biol. Chem. , vol.269 , pp. 6072-6082
    • Schnitzer, J.1    Oh, P.2
  • 9
    • 0036192011 scopus 로고    scopus 로고
    • Vesicle formation and trafficking in endothelial cells and regulation of endothelial barrier function
    • DOI 10.1007/s00418-001-0367-x
    • R. Minshall, C. Tiruppathi, S.M. Vogel, and A.B. Malik Vesicle formation and trafficking in endothelial cells and regulation of endothelial barrier function Histochem. Cell Biol. 117 2002 105 112 (Pubitemid 34185616)
    • (2002) Histochemistry and Cell Biology , vol.117 , Issue.2 , pp. 105-112
    • Minshall, R.D.1    Tiruppathi, C.2    Vogel, S.M.3    Malik, A.B.4
  • 10
    • 84885386501 scopus 로고    scopus 로고
    • Targeting endothelial cell surface receptors: Novel mechanisms of microvascular endothelial barrier transport
    • A.B. Malik Targeting endothelial cell surface receptors: novel mechanisms of microvascular endothelial barrier transport J. Med. Sci. 2 2009 13 17
    • (2009) J. Med. Sci. , vol.2 , pp. 13-17
    • Malik, A.B.1
  • 11
    • 0027160698 scopus 로고
    • Plasmalemmal vesicles represent the large pore system of continuous microvascular endothelium
    • D. Predescu, and G.E. Palade Plasmalemmal vesicles represent the large pore system of continuous microvascular endothelium Am. J. Physiol. 265 1993 H725 H733
    • (1993) Am. J. Physiol. , vol.265
    • Predescu, D.1    Palade, G.E.2
  • 12
    • 15544373016 scopus 로고    scopus 로고
    • Renal tubules albumin transport
    • M. Gekle Renal tubules albumin transport Annu. Rev. Physiol. 67 2005 573 594
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 573-594
    • Gekle, M.1
  • 13
    • 42149122041 scopus 로고    scopus 로고
    • Properties of the glomerular barrier and mechanisms of proteinuria
    • DOI 10.1152/physrev.00055.2006
    • B. Haraldsson, J. Nystrom, and W.M. Deen Properties of the glomerular barrier and mechanisms of proteinuria Physiol. Rev. 88 2008 451 487 (Pubitemid 351522745)
    • (2008) Physiological Reviews , vol.88 , Issue.2 , pp. 451-487
    • Haraldsson, B.1    Nystrom, J.2    Deen, W.M.3
  • 15
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • DOI 10.1038/nri2155, PII NRI2155
    • D.C. Roopenian, and S. Akilesh FcRn: the neonatal Fc receptor comes of age Nat. Rev. Immunol. 7 2007 715 725 (Pubitemid 47327396)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.9 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 16
    • 82455199172 scopus 로고    scopus 로고
    • Selective albuminuria via podocyte albumin transport in puromycin nephrotic rats is attenuated by an inhibitor of NADPH oxidase
    • S. Kinugasa, A. Tojo, T. Sakai, H. Tsumura, M. Takahashi, Y. Hirata, and T. Fujita Selective albuminuria via podocyte albumin transport in puromycin nephrotic rats is attenuated by an inhibitor of NADPH oxidase Kidney Int. 80 2011 1328 1338
    • (2011) Kidney Int. , vol.80 , pp. 1328-1338
    • Kinugasa, S.1    Tojo, A.2    Sakai, T.3    Tsumura, H.4    Takahashi, M.5    Hirata, Y.6    Fujita, T.7
  • 18
    • 70349567495 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis in renal proximal tubule
    • E.I. Christensen, P.J. Verroust, and R. Nielson Receptor-mediated endocytosis in renal proximal tubule Pflugers Arch. 458 2009 1039 1048
    • (2009) Pflugers Arch. , vol.458 , pp. 1039-1048
    • Christensen, E.I.1    Verroust, P.J.2    Nielson, R.3
  • 19
    • 0024529856 scopus 로고
    • An Fc receptor structurally related to MHC class I antigens
    • DOI 10.1038/337184a0
    • N.E. Simister, and K.E. Mostov An Fc receptor structurally related to MHC class I antigens Nature 337 1989 184 187 (Pubitemid 19025381)
    • (1989) Nature , vol.337 , Issue.6203 , pp. 184-187
    • Simister, N.E.1    Mostov, K.E.2
  • 20
    • 0028051652 scopus 로고
    • Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor
    • W.P. Burmeister, L.N. Gastinel, M.L. Blum, and P.J. Bjorkman Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor Nature 372 1994 336 343
    • (1994) Nature , vol.372 , pp. 336-343
    • Burmeister, W.P.1    Gastinel, L.N.2    Blum, M.L.3    Bjorkman, P.J.4
  • 21
    • 0034663798 scopus 로고    scopus 로고
    • Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor
    • DOI 10.1021/bi000749m
    • A.P. West Jr., and P.J. Bjorkman Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor Biochemistry 39 2000 9698 9708 (Pubitemid 30626819)
    • (2000) Biochemistry , vol.39 , Issue.32 , pp. 9698-9708
    • West Jr., A.P.1    Bjorkman, P.J.2
  • 22
    • 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
  • 23
    • 77956242476 scopus 로고    scopus 로고
    • X-ray crystal structures of monomeric and dimeric peptide inhibitors in complex with the human neonatal Fc receptor
    • 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 2010 27694 27701
    • (2010) FcRn J. Biol. Chem. , vol.285 , pp. 27694-27701
    • Mezo, A.R.1    Sridhar, V.2    Badger, J.3    Sakorafas, P.4    Nienaber, V.5
  • 24
    • 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
    • DOI 10.1002/eji.200636556
    • 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 2006 3044 3051 (Pubitemid 44782576)
    • (2006) European Journal of Immunology , vol.36 , Issue.11 , pp. 3044-3051
    • Andersen, J.T.1    Qian, J.D.2    Sandlie, I.3
  • 26
  • 27
    • 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 1996 5512 5516
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 5512-5516
    • Junghans, R.P.1    Anderson, C.L.2
  • 28
    • 69949115639 scopus 로고    scopus 로고
    • Chapter 4: Multitasking by exploitation of intracellular transport functions the many faces of FcRn
    • E.S. Ward, and R.J. Ober Chapter 4: Multitasking by exploitation of intracellular transport functions the many faces of FcRn Adv. Immunol. 103 2009 77 115
    • (2009) Adv. Immunol. , vol.103 , pp. 77-115
    • Ward, E.S.1    Ober, R.J.2
  • 30
    • 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 2009 2788 2793
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 2788-2793
    • Montoyo, H.P.1    Vaccaro, C.2    Hafner, M.3    Ober, R.J.4    Mueller, W.5    Ward, E.S.6
  • 32
    • 0025666296 scopus 로고
    • Familial hypercatabolic hypoproteinemia. A disorder of endogenous catabolism of albumin and immunoglobulin
    • T.A. Waldmann, and W.D. Terry Familial hypercatabolic hypoproteinemia. A disorder of endogenous catabolism of albumin and immunoglobulin J. Clin. Invest. 86 1990 2093 2098
    • (1990) J. Clin. Invest. , vol.86 , pp. 2093-2098
    • Waldmann, T.A.1    Terry, W.D.2
  • 33
    • 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 1976 666 669
    • (1976) J. Cell Biol. , vol.71 , pp. 666-669
    • Rodewald, R.1
  • 34
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • DOI 10.1038/372379a0
    • W.P. Burmeister, A.H. Huber, and P.J. Bjorkman Crystal structure of the complex of rat neonatal Fc receptor with Fc Nature 372 1994 379 383 (Pubitemid 24363442)
    • (1994) Nature , vol.372 , Issue.6504 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 35
    • 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 1997 2211 2217 (Pubitemid 127470004)
    • (1997) Journal of Immunology , vol.158 , Issue.5 , pp. 2211-2217
    • Medesan, C.1    Matesoi, D.2    Radu, C.3    Ghetie, V.4    Ward, E.S.5
  • 42
    • 0142138645 scopus 로고    scopus 로고
    • The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants
    • DOI 10.1016/j.bbagen.2003.08.001
    • K. Nakajou, H. Watanabe, U. Kragh-Hansen, T. Maruyama, and M. Otagiri The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants Biochim. Biophys. Acta 1623 2003 88 97 (Pubitemid 37315665)
    • (2003) Biochimica et Biophysica Acta - General Subjects , vol.1623 , Issue.2-3 , pp. 88-97
    • Nakajou, K.1    Watanabe, H.2    Kragh-Hansen, U.3    Maruyama, T.4    Otagiri, M.5
  • 45
    • 0034666718 scopus 로고    scopus 로고
    • Modulation of clearance of recombinant serum albumin by either glycosylation or truncation
    • DOI 10.1016/S0049-3848(00)00286-3, PII S0049384800002863
    • W.P. Sheffield, J.A. Marques, V. Bhakta, and I.J. Smith Modulation of clearance of recombinant serum albumin by either glycosylation or truncation Thromb. Res. 99 2000 613 621 (Pubitemid 30642743)
    • (2000) Thrombosis Research , vol.99 , Issue.6 , pp. 613-621
    • Sheffield, W.P.1    Marques, J.A.2    Bhakta, V.3    Smith, I.J.4
  • 47
    • 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 2010 367 372
    • (2010) Clin. Biochem. , vol.43 , pp. 367-372
    • Andersen, J.T.1    Daba, M.B.2    Sandlie, I.3
  • 48
    • 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 2001 1551 1559 (Pubitemid 33133882)
    • (2001) International Immunology , vol.13 , Issue.12 , pp. 1551-1559
    • Ober, R.J.1    Radu, C.G.2    Ghetie, V.3    Ward, E.S.4
  • 49
    • 77951156788 scopus 로고    scopus 로고
    • Cross-species binding analyses of mouse and human neonatal Fc receptor show dramatic differences in immunoglobulin G and albumin binding
    • J.T. Andersen, M.B. Daba, G. Berntzen, T.E. Michaelsen, and I. Sandlie Cross-species binding analyses of mouse and human neonatal Fc receptor show dramatic differences in immunoglobulin G and albumin binding J. Biol. Chem. 285 2010 4826 4836
    • (2010) J. Biol. Chem. , vol.285 , pp. 4826-4836
    • Andersen, J.T.1    Daba, M.B.2    Berntzen, G.3    Michaelsen, T.E.4    Sandlie, I.5
  • 50
    • 70350438004 scopus 로고    scopus 로고
    • Extending half-life by indirect targeting of the Neonatal Fc Receptor (FcRn) using a minimal albumin binding domain
    • J.T. Andersen, and I. Sandlie Extending half-life by indirect targeting of the Neonatal Fc Receptor (FcRn) using a minimal albumin binding domain Drug Metab. Pharmacokinet. 24 2009 318 332
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 318-332
    • Andersen, J.T.1    Sandlie, I.2
  • 52
    • 0036826998 scopus 로고    scopus 로고
    • Albugranin™, a recombinant human granulocyte colony stimulating factor (G-CSF) genetically fused to recombinant human albumin induces prolonged myelopoietic effects in mice and monkeys
    • DOI 10.1023/A:1020917732218
    • W. Halpern, T.A. Riccobene, H. Agostini, K. Baker, D. Stolow, M.L. Gu, J. Hirsch, A. Mahoney, J. Carrell, E. Boyd, and K. Grzegorzewski Albugranin™, a recombinant human granulocyte colony stimulating factor (G-CSF) genetically fused to recombinant human albumin induces prolonged myelopoietic effects in mice and monkeys Pharm. Res. 19 2002 1720 1729 (Pubitemid 35305525)
    • (2002) Pharmaceutical Research , vol.19 , Issue.11 , pp. 1720-1729
    • Halpern, W.1    Riccobene, T.A.2    Agostini, H.3    Baker, K.4    Stolow, D.5    Gu, M.-L.6    Hirsch, J.7    Mahoney, A.8    Carrell, J.9    Boyd, E.10    Grzegorzewski, K.J.11
  • 53
    • 36849040529 scopus 로고    scopus 로고
    • Albinterferon α-2b: A genetic fusion protein for the treatment of chronic hepatitis C
    • DOI 10.1038/nbt1364, PII NBT1364
    • G.M. Subramanian, M. Fiscella, A. Lamouse-Smith, S. Zeuzem, and J.G. McHutchison Albinterferon alpha-2b: a genetic fusion protein for the treatment of chronic hepatitis C Nat. Biotechnol. 25 2007 1411 1419 (Pubitemid 350233139)
    • (2007) Nature Biotechnology , vol.25 , Issue.12 , pp. 1411-1419
    • Subramanian, G.M.1    Fiscella, M.2    Lamouse-Smith, A.3    Zeuzem, S.4    McHutchison, J.G.5
  • 55
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • DOI 10.1038/1869
    • S. Curry, H. Mandelkow, P. Brick, and N. Franks Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites Nat. Struct. Biol. 5 1998 827 835 (Pubitemid 28402087)
    • (1998) Nature Structural Biology , vol.5 , Issue.9 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 56
    • 33144488817 scopus 로고    scopus 로고
    • Insulin detemir: From concept to clinical experience
    • DOI 10.1517/14656566.7.3.325
    • P. Home, and P. Kurtzhals Insulin detemir: from concept to clinical experience Expert Opin. Pharmacother. 7 2006 325 343 (Pubitemid 43263250)
    • (2006) Expert Opinion on Pharmacotherapy , vol.7 , Issue.3 , pp. 325-343
    • Home, P.1    Kurtzhals, P.2
  • 57
    • 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 2012 4 28
    • (2012) J. Control. Release , vol.157 , pp. 4-28
    • Elsadek, B.1    Kratz, F.2
  • 58
    • 72449130972 scopus 로고    scopus 로고
    • New strategy for the extension of the serum half-life of antibody fragments
    • S. Trüssel, C. Dumelin, K. Frey, A. Villa, F. Buller, and D. Neri New strategy for the extension of the serum half-life of antibody fragments Bioconjug. Chem. 20 2009 2286 2292
    • (2009) Bioconjug. Chem. , vol.20 , pp. 2286-2292
    • Trüssel, S.1    Dumelin, C.2    Frey, K.3    Villa, A.4    Buller, F.5    Neri, D.6
  • 63
    • 53349171633 scopus 로고    scopus 로고
    • Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: Taking advantage of modular Nanobody technology
    • B.M. Tijink, T. Laeremans, M. Budde, M. Stigter-van Walsum, T. Dreier, H.J. de Haard, C.R. Leemans, and G.A. van Dongen Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: taking advantage of modular Nanobody technology Mol. Cancer Ther. 7 2008 2288 2297
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2288-2297
    • Tijink, B.M.1    Laeremans, T.2    Budde, M.3    Stigter-Van Walsum, M.4    Dreier, T.5    De Haard, H.J.6    Leemans, C.R.7    Van Dongen, G.A.8
  • 65
    • 78650468405 scopus 로고    scopus 로고
    • Adnectins: Engineered target-binding protein therapeutics
    • D. Lipovšek Adnectins: engineered target-binding protein therapeutics Protein Eng. Des. Sel. 24 2011 3 9
    • (2011) Protein Eng. Des. Sel. , vol.24 , pp. 3-9
    • Lipovšek, D.1
  • 66
    • 84885377002 scopus 로고    scopus 로고
    • AlbudAb™ technology platform: Versatile albumin binding domains for the development of therapeutics with tunable half-lives
    • R. Kontermann, Wiley-VCH Verlag & Co. KGaA
    • C. Herring, and O. Schon AlbudAb™ technology platform: versatile albumin binding domains for the development of therapeutics with tunable half-lives R. Kontermann, Therapeutic Proteins: Strategies to Modulate their Plasma Half-lives 2012 Wiley-VCH Verlag & Co. KGaA 249 268
    • (2012) Therapeutic Proteins: Strategies to Modulate Their Plasma Half-lives , pp. 249-268
    • Herring, C.1    Schon, O.2
  • 67
    • 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 2008 171 183
    • (2008) J. Control. Release , vol.132 , pp. 171-183
    • Kratz, F.1
  • 71
    • 41349098117 scopus 로고    scopus 로고
    • An albumin-exendin-4 conjugate engages central and peripheral circuits regulating murine energy and glucose homeostasis
    • DOI 10.1053/j.gastro.2008.01.017, PII S0016508508000565
    • L.L. Baggio, Q. Huang, X. Cao, and D.J. Drucker An albumin-exendin-4 conjugate engages central and peripheral circuits regulating murine energy and glucose homeostasis Gastroenterology 134 2008 1137 1147 (Pubitemid 351451971)
    • (2008) Gastroenterology , vol.134 , Issue.4 , pp. 1137-1147
    • Baggio, L.L.1    Huang, Q.2    Cao, X.3    Drucker, D.J.4
  • 74
    • 70349664297 scopus 로고    scopus 로고
    • Potential of albiglutide, a long-acting GLP-1 receptor agonist, in type 2 diabetes: A randomized controlled trial exploring weekly, biweekly, and monthly dosing
    • J. Rosenstock, J. Reusch, M. Bush, F. Yang, and M. Stewart Potential of albiglutide, a long-acting GLP-1 receptor agonist, in type 2 diabetes: a randomized controlled trial exploring weekly, biweekly, and monthly dosing Diabetes Care 32 2009 1880 1886
    • (2009) Diabetes Care , vol.32 , pp. 1880-1886
    • Rosenstock, J.1    Reusch, J.2    Bush, M.3    Yang, F.4    Stewart, M.5
  • 75
    • 21044438330 scopus 로고    scopus 로고
    • AlbuBNP, a recombinant B-type natriuretic peptide and human serum albumin fusion hormone, as a long-term therapy of congestive heart failure
    • DOI 10.1023/B:PHAM.0000048203.30568.81
    • W. Wang, Y. Ou, and Y. Shi AlbuBNP, a recombinant B-type natriuretic peptide and human serum albumin fusion hormone, as a long-term therapy of congestive heart failure Pharm. Res. 21 2004 2105 2111 (Pubitemid 40941232)
    • (2004) Pharmaceutical Research , vol.21 , Issue.11 , pp. 2105-2111
    • Wang, W.1    Ou, Y.2    Shi, Y.3
  • 76
    • 84858336635 scopus 로고    scopus 로고
    • Characterization of a long-acting recombinant human serum albumin-atrial natriuretic factor (ANF) expressed in Pichia pastoris
    • M.K. de Bold, W.P. Sheffield, A. Martinuk, V. Bhakta, L. Eltringham-Smith, and A.J. de Bold Characterization of a long-acting recombinant human serum albumin-atrial natriuretic factor (ANF) expressed in Pichia pastoris Regul. Pept. 175 2012 7 10
    • (2012) Regul. Pept. , vol.175 , pp. 7-10
    • De Bold, M.K.1    Sheffield, W.P.2    Martinuk, A.3    Bhakta, V.4    Eltringham-Smith, L.5    De Bold, A.J.6
  • 80
    • 70449461639 scopus 로고    scopus 로고
    • Genetic fusion to albumin improves the pharmacokinetic properties of factor IX
    • H.J. Metzner, T. Weimer, U. Kronthaler, W. Lang, and S. Schulte Genetic fusion to albumin improves the pharmacokinetic properties of factor IX Thromb. Haemost. 102 2009 634 644
    • (2009) Thromb. Haemost. , vol.102 , pp. 634-644
    • Metzner, H.J.1    Weimer, T.2    Kronthaler, U.3    Lang, W.4    Schulte, S.5
  • 82
    • 0037027919 scopus 로고    scopus 로고
    • Albutropin: A growth hormone-albumin fusion with improved pharmacokinetics and pharmacodynamics in rats and monkeys
    • DOI 10.1016/S0014-2999(02)02644-4, PII S0014299902026444
    • B.L. Osborn, L. Sekut, M. Corcoran, C. Poortman, B. Sturm, G. Chen, D. Mather, H.L. Lin, and T.J. Parry Albutropin: a growth hormone-albumin fusion with improved pharmacokinetics and pharmacodynamics in rats and monkeys Eur. J. Pharmacol. 456 2002 149 158 (Pubitemid 35351748)
    • (2002) European Journal of Pharmacology , vol.456 , Issue.1-3 , pp. 149-158
    • Osborn, B.L.1    Sekut, L.2    Corcoran, M.3    Poortman, C.4    Sturm, B.5    Chen, G.6    Mather, D.7    Lin, H.L.8    Parry, T.J.9
  • 83
    • 0032579311 scopus 로고    scopus 로고
    • Disruption of the Saccharomyces cerevisiae YAP3 gene reduces the proteolytic degradation of secreted recombinant human albumin
    • DOI 10.1002/(SICI)1097-0061(19980130)14:2<161::AID-YEA208>3.0.CO;2- Y
    • S.M. Kerry-Williams, S.C. Gilbert, L.R. Evans, and D.J. Balance Disruption of the Saccharomyces cerevisiae YAP3 gene reduces the proteolytic degradation of secreted recombinant human albumin Yeast 14 1998 161 169 (Pubitemid 28062866)
    • (1998) Yeast , vol.14 , Issue.2 , pp. 161-169
    • Kerry-Williams, S.M.1    Gilbert, S.C.2    Evans, L.R.3    Ballance, D.J.4
  • 86
    • 34250361507 scopus 로고    scopus 로고
    • Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin
    • DOI 10.1074/jbc.M700820200
    • D. Müller, A. Karle, B. Meissburger, I. Höfig, R. Stork, and R.E. Kontermann Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin J. Biol. Chem. 282 2007 12650 12660 (Pubitemid 47100581)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 12650-12660
    • Muller, D.1    Karle, A.2    Meissburger, B.3    Hofig, I.4    Stork, R.5    Kontermann, R.E.6
  • 88
    • 77955418625 scopus 로고    scopus 로고
    • The production, characterisation and enhanced pharmacokinetics of scFv-albumin fusions expressed in Saccharomyces cerevisiae
    • L. Evans, M. Hughes, J. Waters, J. Cameron, N. Dodsworth, D. Tooth, A. Greenfield, and D. Sleep The production, characterisation and enhanced pharmacokinetics of scFv-albumin fusions expressed in Saccharomyces cerevisiae Protein Expr. Purif. 73 2010 113 124
    • (2010) Protein Expr. Purif. , vol.73 , pp. 113-124
    • Evans, L.1    Hughes, M.2    Waters, J.3    Cameron, J.4    Dodsworth, N.5    Tooth, D.6    Greenfield, A.7    Sleep, D.8
  • 90
    • 80052260642 scopus 로고    scopus 로고
    • Albumin fusion of thioredoxin-The production and evaluation of its biological activity for potential therapeutic applications
    • S. Ikuta, V.T. Chuang, Y. Ishima, K. Nakajou, M. Furukawa, H. Watanabe, T. Maruyama, and M. Otagiri Albumin fusion of thioredoxin-the production and evaluation of its biological activity for potential therapeutic applications J. Control. Release 147 2010 17 23
    • (2010) J. Control. Release , vol.147 , pp. 17-23
    • Ikuta, S.1    Chuang, V.T.2    Ishima, Y.3    Nakajou, K.4    Furukawa, M.5    Watanabe, H.6    Maruyama, T.7    Otagiri, M.8
  • 91
  • 95
    • 0035970278 scopus 로고    scopus 로고
    • Yeast 2 μm plasmid copy number is elevated by a mutation in the nuclear gene UBC4
    • DOI 10.1002/yea.679
    • D. Sleep, C. Finnis, A. Turner, and L. Evans Yeast 2 micron plasmid copy number is elevated by a mutation in the nuclear gene UBC4 Yeast 18 2001 403 421 (Pubitemid 32266192)
    • (2001) Yeast , vol.18 , Issue.5 , pp. 403-421
    • Sleep, D.1    Finnis, C.2    Turner, A.3    Evans, L.4
  • 96
    • 67349176115 scopus 로고    scopus 로고
    • Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes
    • B. Ahrén Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes Nat. Rev. Drug Discov. 8 2009 369 385
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 369-385
    • Ahrén, B.1
  • 97
    • 4644230834 scopus 로고    scopus 로고
    • Gut-derived incretin hormones and new therapeutic approaches
    • DOI 10.2337/diacare.27.10.2554
    • Z.T. Bloomgarden Gut-derived incretin hormones and new therapeutic approaches Diabetes Care 27 2004 2554 2559 (Pubitemid 39281420)
    • (2004) Diabetes Care , vol.27 , Issue.10 , pp. 2554-2559
    • Bloomgarden, Z.T.1
  • 98
    • 79953040963 scopus 로고    scopus 로고
    • An overview of once-weekly glucagon-like peptide-1 receptor agonists-available efficacy and safety data and perspectives for the future
    • S. Madsbad, U. Kielgast, M. Asmar, C.F. Deacon, S.S. Torekov, and J.J. Holst An overview of once-weekly glucagon-like peptide-1 receptor agonists-available efficacy and safety data and perspectives for the future Diabetes Obes. Metab. 13 2011 394 407
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 394-407
    • Madsbad, S.1    Kielgast, U.2    Asmar, M.3    Deacon, C.F.4    Torekov, S.S.5    Holst, J.J.6
  • 100
    • 84885374394 scopus 로고    scopus 로고
    • Efficacy and safety of balugrastim compared with pegfilgrastim in patients with breast cancer who are receiving chemotherapy
    • (Suppl.; abstr 9125)
    • C.D. Volovat, O. Gladkov, I. Bondarenko, S. Barash, A. Buchner, N. Avisar, and P. Bias Efficacy and safety of balugrastim compared with pegfilgrastim in patients with breast cancer who are receiving chemotherapy J. Clin. Oncol. 30 2012 (Suppl.; abstr 9125)
    • (2012) J. Clin. Oncol. , vol.30
    • Volovat, C.D.1    Gladkov, O.2    Bondarenko, I.3    Barash, S.4    Buchner, A.5    Avisar, N.6    Bias, P.7
  • 101
    • 84859738027 scopus 로고    scopus 로고
    • Selective domain stabilization as a strategy to reduce human serum albumin-human granulocyte colony stimulating factor aggregation rate
    • A.A. Cordes, J.F. Carpenter, and T.W. Randolph Selective domain stabilization as a strategy to reduce human serum albumin-human granulocyte colony stimulating factor aggregation rate J. Pharm. Sci. 101 2012 2009 2016
    • (2012) J. Pharm. Sci. , vol.101 , pp. 2009-2016
    • Cordes, A.A.1    Carpenter, J.F.2    Randolph, T.W.3
  • 102
    • 84857500984 scopus 로고    scopus 로고
    • Selective domain stabilization as a strategy to reduce fusion protein aggregation
    • A.A. Cordes, C.W. Platt, J.F. Carpenter, and T.W. Randolph Selective domain stabilization as a strategy to reduce fusion protein aggregation J. Pharm. Sci. 101 2012 1400 1409
    • (2012) J. Pharm. Sci. , vol.101 , pp. 1400-1409
    • Cordes, A.A.1    Platt, C.W.2    Carpenter, J.F.3    Randolph, T.W.4
  • 104
    • 84865209564 scopus 로고    scopus 로고
    • Improved kinetics of rIX-FP, a recombinant fusion protein linking factor IX with albumin, in cynomolgus monkeys and hemophilia B dogs
    • M.W. Nolte, T.C. Nichols, J. Mueller-Cohrs, E.P. Merricks, I. Pragst, S. Zollner, and G. Dickneite Improved kinetics of rIX-FP, a recombinant fusion protein linking factor IX with albumin, in cynomolgus monkeys and hemophilia B dogs J. Thromb. Haemost. 10 2012 1591 1599
    • (2012) J. Thromb. Haemost. , vol.10 , pp. 1591-1599
    • Nolte, M.W.1    Nichols, T.C.2    Mueller-Cohrs, J.3    Merricks, E.P.4    Pragst, I.5    Zollner, S.6    Dickneite, G.7
  • 105
    • 84866594053 scopus 로고    scopus 로고
    • Safety and pharmacokinetics of a novel recombinant fusion protein linking coagulation factor IX with albumin (rIX-FP) in hemophilia B patients
    • E. Santagostino, C. Negrier, R. Klamroth, A. Tiede, I. Pabinger-Fasching, C. Voigt, I. Jacobs, and M. Morfini Safety and pharmacokinetics of a novel recombinant fusion protein linking coagulation factor IX with albumin (rIX-FP) in hemophilia B patients Blood 120 2012 2405 2411
    • (2012) Blood , vol.120 , pp. 2405-2411
    • Santagostino, E.1    Negrier, C.2    Klamroth, R.3    Tiede, A.4    Pabinger-Fasching, I.5    Voigt, C.6    Jacobs, I.7    Morfini, M.8
  • 106
    • 84863304928 scopus 로고    scopus 로고
    • Anti-carcinoembryonic antigen single-chain variable fragment antibody variants bind mouse and human neonatal Fc receptor with different affinities that reveal distinct cross-species differences in serum half-life
    • J.T. Andersen, S. Foss, V.E. Kenanova, T. Olafsen, I.S. Leikfoss, D.C. Roopenian, A.M. Wu, and I. Sandlie Anti-carcinoembryonic antigen single-chain variable fragment antibody variants bind mouse and human neonatal Fc receptor with different affinities that reveal distinct cross-species differences in serum half-life J. Biol. Chem. 287 2012 22927 22937
    • (2012) J. Biol. Chem. , vol.287 , pp. 22927-22937
    • Andersen, J.T.1    Foss, S.2    Kenanova, V.E.3    Olafsen, T.4    Leikfoss, I.S.5    Roopenian, D.C.6    Wu, A.M.7    Sandlie, I.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.