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Volumn 12, Issue SUPPL. 3, 2006, Pages 42-51

Strategies towards a longer acting factor VIII

Author keywords

Bioengineering; Clearance; Factor VIII; Half life; Polyethylene glycol; Polysialic acids

Indexed keywords

ADENOSINE DEAMINASE; ALPHA2B INTERFERON; ANTINEOPLASTIC AGENT; ASPARAGINASE; ASPARAGINASE MACROGOL; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 8A; DISTEAROYLPHOSPHATIDYLETHANOLAMINE; DOXORUBICIN; GRANULOCYTE COLONY STIMULATING FACTOR; GROWTH HORMONE; HEMOSTATIC AGENT; INSULIN; LIPOSOME; LOW DENSITY LIPOPROTEIN RECEPTOR; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; MACROGOL; PEGINTERFERON; PEGYLATED ADENOSINE DEAMINASE; PEGYLATED BLOOD CLOTTING FACTOR 8; PEGYLATED GRANULOCYTE COLONY STIMULATING FACTOR; PEGYLATED GROWTH HORMONE; PEGYLATED LIPOSOMAL BLOOD CLOTTING FACTOR 8; POLYSIALIC ACID; RECOMBINANT BLOOD CLOTTING FACTOR 8; UNCLASSIFIED DRUG;

EID: 33646147385     PISSN: 13518216     EISSN: 13652516     Source Type: Journal    
DOI: 10.1111/j.1365-2516.2006.01260.x     Document Type: Article
Times cited : (42)

References (60)
  • 1
    • 11044233673 scopus 로고    scopus 로고
    • Comprehensive care for haemophilia around the world
    • Evatt BL, Black C, Batorova A et al. Comprehensive care for haemophilia around the world. Haemophilia 2004; 10 (Suppl. 4): 9-13.
    • (2004) Haemophilia , vol.10 , Issue.SUPPL. 4 , pp. 9-13
    • Evatt, B.L.1    Black, C.2    Batorova, A.3
  • 2
    • 11044229599 scopus 로고    scopus 로고
    • Towards the goal of prophylaxis: Experience and treatment strategies from Sweden, France and Hungary
    • Petrini P, Chambost H, Nemes L. Towards the goal of prophylaxis: experience and treatment strategies from Sweden, France and Hungary. Haemophilia 2004; 10 (Suppl. 4): 94-6.
    • (2004) Haemophilia , vol.10 , Issue.SUPPL. 4 , pp. 94-96
    • Petrini, P.1    Chambost, H.2    Nemes, L.3
  • 3
    • 11044235064 scopus 로고    scopus 로고
    • Utilization of care in haemophilia: A resource-based method for cost analysis from the Haemophilia Utilization Group Study (HUGS)
    • Globe DR, Curtis RG, Koerper MA. Utilization of care in haemophilia: A resource-based method for cost analysis from the Haemophilia Utilization Group Study (HUGS). Haemophilia 2004; 10 (Suppl. 1): 63-70.
    • (2004) Haemophilia , vol.10 , Issue.SUPPL. 1 , pp. 63-70
    • Globe, D.R.1    Curtis, R.G.2    Koerper, M.A.3
  • 4
    • 11044234586 scopus 로고    scopus 로고
    • WFH: Back to the future
    • O'Mahony B. WFH: Back to the future. Haemophilia 2004; 10 (Suppl. 4): 1-8.
    • (2004) Haemophilia , vol.10 , Issue.SUPPL. 4 , pp. 1-8
    • O'Mahony, B.1
  • 5
    • 0034913232 scopus 로고    scopus 로고
    • Barriers to compliance with prophylaxis therapy in haemophilia
    • Hacker MR, Geraghty S, Manco-Johnson M. Barriers to compliance with prophylaxis therapy in haemophilia. Haemophilia 2001; 7: 392-6.
    • (2001) Haemophilia , vol.7 , pp. 392-396
    • Hacker, M.R.1    Geraghty, S.2    Manco-Johnson, M.3
  • 6
    • 11044219714 scopus 로고    scopus 로고
    • Optimizing factor prophylaxis for the haemophilia population: Where do we stand?
    • Blanchette VS, Manco-Johnson M, Santagostino E, Ljung R. Optimizing factor prophylaxis for the haemophilia population: Where do we stand? Haemophilia 2004; 10 (Suppl. 4): 97-104.
    • (2004) Haemophilia , vol.10 , Issue.SUPPL. 4 , pp. 97-104
    • Blanchette, V.S.1    Manco-Johnson, M.2    Santagostino, E.3    Ljung, R.4
  • 7
    • 0043261498 scopus 로고    scopus 로고
    • Pegylation: Engineering improved biopharmaceuticals for oncology
    • Molineux G. Pegylation: Engineering improved biopharmaceuticals for oncology. Pharmacotherapy 2003; 23: 3S-8S.
    • (2003) Pharmacotherapy , vol.23
    • Molineux, G.1
  • 8
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski A, van Es T, Palczuk NC, Davis FF. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J Biol Chem 1977; 252: 3578-81.
    • (1977) J Biol Chem , vol.252 , pp. 3578-3581
    • Abuchowski, A.1    van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 9
    • 0017388651 scopus 로고
    • Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase
    • Abuchowski A, McCoy JR, Palczuk NC et al. Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J Biol Chem 1977; 252: 3582-6.
    • (1977) J Biol Chem , vol.252 , pp. 3582-3586
    • Abuchowski, A.1    McCoy, J.R.2    Palczuk, N.C.3
  • 11
    • 0035216905 scopus 로고    scopus 로고
    • Peginterferon alfa-2a (40 kDa) monotherapy: A novel agent for chronic hepatitis C therapy
    • Zeuzem S, Heathcote JE, Martin N et al. Peginterferon alfa-2a (40 kDa) monotherapy: A novel agent for chronic hepatitis C therapy. Expert Opin Investig Drugs 2001; 10: 2201-13.
    • (2001) Expert Opin Investig Drugs , vol.10 , pp. 2201-2213
    • Zeuzem, S.1    Heathcote, J.E.2    Martin, N.3
  • 12
    • 0022908309 scopus 로고
    • Characterization of polyethylene glycol-modified L -asparaginase from Escherichia coli and its application to therapy of leukemia
    • Yoshimoto T, Nishimura H, Saito Y et al. Characterization of polyethylene glycol-modified L -asparaginase from Escherichia coli and its application to therapy of leukemia. Jpn J Cancer Res 1986; 77: 1264-70.
    • (1986) Jpn J Cancer Res , vol.77 , pp. 1264-1270
    • Yoshimoto, T.1    Nishimura, H.2    Saito, Y.3
  • 13
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • Veronese FM, Pasut G. PEGylation, successful approach to drug delivery. Drug Discov Today 2005; 10: 1451-8.
    • (2005) Drug Discov Today , vol.10 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 14
    • 0035086519 scopus 로고    scopus 로고
    • Rational design of a potent, long-lasting form of interferon: A 40 kDa branched polyethylene glycol-conjugated interferon alpha-2a for the treatment of hepatitis C
    • Bailon P, Palleroni A, Schaffer CA et al. Rational design of a potent, long-lasting form of interferon: A 40 kDa branched polyethylene glycol-conjugated interferon alpha-2a for the treatment of hepatitis C. Bioconjug Chem 2001; 12: 195-202.
    • (2001) Bioconjug Chem , vol.12 , pp. 195-202
    • Bailon, P.1    Palleroni, A.2    Schaffer, C.A.3
  • 15
    • 0017754787 scopus 로고
    • Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand's disease
    • Weiss HJ, Sussman II, Hoyer LW. Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand's disease. J Clin Invest 1977; 60: 390-404.
    • (1977) J Clin Invest , vol.60 , pp. 390-404
    • Weiss, H.J.1    Sussman, I.I.2    Hoyer, L.W.3
  • 16
    • 0034774812 scopus 로고    scopus 로고
    • Catabolism of the coagulation factor VIII: Can we prolong lifetime of fVIII in circulation?
    • Ananyeva NM, Kouiavskaia DV, Shima M, Saenko EL. Catabolism of the coagulation factor VIII: Can we prolong lifetime of fVIII in circulation? Trends Cardiovasc Med 2001; 11: 251-7.
    • (2001) Trends Cardiovasc Med , vol.11 , pp. 251-257
    • Ananyeva, N.M.1    Kouiavskaia, D.V.2    Shima, M.3    Saenko, E.L.4
  • 17
    • 0020043657 scopus 로고
    • Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein
    • Fass DN, Knutson GJ, Katzmann JA. Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein. Blood 1982; 59: 594-600.
    • (1982) Blood , vol.59 , pp. 594-600
    • Fass, D.N.1    Knutson, G.J.2    Katzmann, J.A.3
  • 18
    • 0022445266 scopus 로고
    • The size of human factor VIII heterodimers and the effects produced by thrombin
    • Fay PJ, Anderson MT, Chavin SI, Marder VJ. The size of human factor VIII heterodimers and the effects produced by thrombin. Biochim Biophys Acta 1986; 871: 268-78.
    • (1986) Biochim Biophys Acta , vol.871 , pp. 268-278
    • Fay, P.J.1    Anderson, M.T.2    Chavin, S.I.3    Marder, V.J.4
  • 19
    • 0028358217 scopus 로고
    • Copper-atom identification in the active and inactive forms of plasma-derived FVIII and recombinant FVIII-delta II
    • Bihoreau N, Pin S, de Kersabiec AM et al. Copper-atom identification in the active and inactive forms of plasma-derived FVIII and recombinant FVIII-delta II. Eur J Biochem 1994; 222: 41-8.
    • (1994) Eur J Biochem , vol.222 , pp. 41-48
    • Bihoreau, N.1    Pin, S.2    de Kersabiec, A.M.3
  • 20
    • 0022454539 scopus 로고
    • Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity
    • Eaton D, Rodriguez H, Vehar GA. Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity. Biochemistry 1986; 25: 505-12.
    • (1986) Biochemistry , vol.25 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 21
    • 0029919613 scopus 로고    scopus 로고
    • Model for the factor VIIIa-dependent decay of the intrinsic factor Xase. Role of subunit dissociation and factor IXa-catalyzed proteolysis
    • Fay PJ, Beattie TL, Regan LM et al. Model for the factor VIIIa-dependent decay of the intrinsic factor Xase. Role of subunit dissociation and factor IXa-catalyzed proteolysis. J Biol Chem 1996; 271: 6027-32.
    • (1996) J Biol Chem , vol.271 , pp. 6027-6032
    • Fay, P.J.1    Beattie, T.L.2    Regan, L.M.3
  • 22
    • 0026708655 scopus 로고
    • Characterization of the interaction between the A2 subunit and A1/ A3-C1-C2 dimer in human factor VIIIa
    • Fay PJ, Smudzin TM. Characterization of the interaction between the A2 subunit and A1/A3-C1-C2 dimer in human factor VIIIa. J Biol Chem 1992; 267: 13246-50.
    • (1992) J Biol Chem , vol.267 , pp. 13246-13250
    • Fay, P.J.1    Smudzin, T.M.2
  • 23
    • 0343963682 scopus 로고    scopus 로고
    • B-Domain deleted recombinant coagulation factor VIII modified with monomethoxy polyethylene glycol
    • Rostin J, Smeds AL, Akerblom E. B-Domain deleted recombinant coagulation factor VIII modified with monomethoxy polyethylene glycol. Bioconjug Chem 2000; 11: 387-96.
    • (2000) Bioconjug Chem , vol.11 , pp. 387-396
    • Rostin, J.1    Smeds, A.L.2    Akerblom, E.3
  • 24
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: A review of problems and solutions
    • Veronese FM. Peptide and protein PEGylation: A review of problems and solutions. Biomaterials 2001; 22: 405-17.
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 25
    • 33646145684 scopus 로고    scopus 로고
    • Structural and functional role of the factor VIII B domain
    • Pipe SW, Kaufman RJ. Structural and functional role of the factor VIII B domain. Haematologica 2004; 89: 8-13.
    • (2004) Haematologica , vol.89 , pp. 8-13
    • Pipe, S.W.1    Kaufman, R.J.2
  • 26
    • 1942521325 scopus 로고    scopus 로고
    • Bioengineering of coagulation factor VIII for improved secretion
    • Miao HZ, Sirachainan N, Palmer L et al. Bioengineering of coagulation factor VIII for improved secretion. Blood 2004; 103: 3412-19.
    • (2004) Blood , vol.103 , pp. 3412-3419
    • Miao, H.Z.1    Sirachainan, N.2    Palmer, L.3
  • 27
    • 33646155895 scopus 로고    scopus 로고
    • Baxter announces collaborations to develop longer acting forms of blood clotting factors
    • Baxter International, Inc. Published online at Accessed 7 January
    • Baxter International, Inc. Baxter announces collaborations to develop longer acting forms of blood clotting factors. Published online at http://www.baxter.com/about_baxter/news_room/news_releases/2005/ 09-29-05-collaboration.html. Accessed 7 January, 2006.
    • (2006)
  • 28
    • 0344420226 scopus 로고    scopus 로고
    • Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates
    • Caliceti P, Veronese FM. Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates. Adv Drug Deliv Rev 2003; 55: 1261-77.
    • (2003) Adv Drug Deliv Rev , vol.55 , pp. 1261-1277
    • Caliceti, P.1    Veronese, F.M.2
  • 29
    • 23444455640 scopus 로고    scopus 로고
    • Improving the therapeutic efficacy of peptides and proteins: A role for polysialic acids
    • Gregoriadis G, Jain S, Papaioannou I, Laing P. Improving the therapeutic efficacy of peptides and proteins: A role for polysialic acids. Int J Pharm 2005; 300: 125-30.
    • (2005) Int J Pharm , vol.300 , pp. 125-130
    • Gregoriadis, G.1    Jain, S.2    Papaioannou, I.3    Laing, P.4
  • 30
    • 17644391325 scopus 로고    scopus 로고
    • Liposomal drug delivery systems - Clinical applications
    • Goyal P, Goyal K, Vijaya Kumar SG et al. Liposomal drug delivery systems - clinical applications. Acta Pharm 2005; 55: 1-25.
    • (2005) Acta Pharm , vol.55 , pp. 1-25
    • Goyal, P.1    Goyal, K.2    Vijaya Kumar, S.G.3
  • 31
    • 0035005359 scopus 로고    scopus 로고
    • Pegylated liposomal doxorubicin: Metamorphosis of an old drug into a new form of chemotherapy
    • Gabizon AA. Pegylated liposomal doxorubicin: Metamorphosis of an old drug into a new form of chemotherapy. Cancer Invest 2001; 19: 424-36.
    • (2001) Cancer Invest , vol.19 , pp. 424-436
    • Gabizon, A.A.1
  • 32
    • 0028016169 scopus 로고
    • Delivery of cytokines by liposomes. II. Interleukin-2 encapsulated in long-circulating sterically stabilized liposomes: Immunomodulatory and anti-tumor activity in mice
    • Kedar E, Braun E, Rutkowski Y et al. Delivery of cytokines by liposomes. II. Interleukin-2 encapsulated in long-circulating sterically stabilized liposomes: Immunomodulatory and anti-tumor activity in mice. J Immunother Emphasis Tumor Immunol 1994; 16: 115-24.
    • (1994) J Immunother Emphasis Tumor Immunol , vol.16 , pp. 115-124
    • Kedar, E.1    Braun, E.2    Rutkowski, Y.3
  • 33
    • 20444503381 scopus 로고    scopus 로고
    • Factor VIII efficient and specific non-covalent binding to PEGylated liposomes enables prolongation of its circulation time and haemostatic efficacy
    • Baru M, Carmel-Goren L, Barenholz Y et al. Factor VIII efficient and specific non-covalent binding to PEGylated liposomes enables prolongation of its circulation time and haemostatic efficacy. Thromb Haemost 2005; 93: 1061-8.
    • (2005) Thromb Haemost , vol.93 , pp. 1061-1068
    • Baru, M.1    Carmel-Goren, L.2    Barenholz, Y.3
  • 34
    • 33646128656 scopus 로고    scopus 로고
    • Bayer completes investigational new drug filing with FDA for longer-acting Kogenate® product
    • Bayer HealthCare. Published online at Accessed 7 January
    • Bayer HealthCare. Bayer completes investigational new drug filing with FDA for longer-acting Kogenate® product. Published online at http://www.bayerhealthcare.com/401.0.html?&L=2&tx_ ttnews[pointer]=4&tx_ttnews[tt_news]=228&tx_ ttnews[backPid]=30&cHash=63f91fd197
    • (2006)
  • 35
    • 0030835335 scopus 로고    scopus 로고
    • Polysialylated asparaginase: Preparation, activity and pharmacokinetics
    • Fernandes AI, Gregoriadis G. Polysialylated asparaginase: Preparation, activity and pharmacokinetics. Biochim Biophys Acta 1997; 1341: 26-34.
    • (1997) Biochim Biophys Acta , vol.1341 , pp. 26-34
    • Fernandes, A.I.1    Gregoriadis, G.2
  • 36
    • 0035901757 scopus 로고    scopus 로고
    • The effect of polysialylation on the immunogenicity and antigenicity of asparaginase: Implication in its pharmacokinetics
    • Fernandes AI, Gregoriadis G. The effect of polysialylation on the immunogenicity and antigenicity of asparaginase: Implication in its pharmacokinetics. Int J Pharm 2001; 217: 215-24.
    • (2001) Int J Pharm , vol.217 , pp. 215-224
    • Fernandes, A.I.1    Gregoriadis, G.2
  • 37
    • 0037757532 scopus 로고    scopus 로고
    • Polysialylated insulin: Synthesis, characterization and biological activity in vivo
    • Jain S, Hreczuk-Hirst DH, McCormack B et al. Polysialylated insulin: synthesis, characterization and biological activity in vivo. Biochim Biophys Acta 2003; 1622: 42-9.
    • (2003) Biochim Biophys Acta , vol.1622 , pp. 42-49
    • Jain, S.1    Hreczuk-Hirst, D.H.2    McCormack, B.3
  • 38
    • 28244484911 scopus 로고    scopus 로고
    • The promise and challenges of bioengineered recombinant clotting factors
    • Pipe SW. The promise and challenges of bioengineered recombinant clotting factors. J Thromb Haemost 2005; 3: 1692-701.
    • (2005) J Thromb Haemost , vol.3 , pp. 1692-1701
    • Pipe, S.W.1
  • 39
    • 0030664471 scopus 로고    scopus 로고
    • Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa
    • Pipe SW, Kaufman RJ. Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa. Proc Natl Acad Sci USA 1997; 94: 11851-6.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11851-11856
    • Pipe, S.W.1    Kaufman, R.J.2
  • 40
    • 33646126658 scopus 로고    scopus 로고
    • The conformation of the factor VIII light chain can modulate von Willebrand factor binding affinity without affecting cofactor activity in vitro and in vivo
    • Pipe SW, Nichols TC, McClintock DWD et al. The conformation of the factor VIII light chain can modulate von Willebrand factor binding affinity without affecting cofactor activity in vitro and in vivo. Blood 1999; 94 (10 Suppl. 1): 453a.
    • (1999) Blood , vol.94 , Issue.10 SUPPL. 1
    • Pipe, S.W.1    Nichols, T.C.2    McClintock, D.W.D.3
  • 41
    • 84868056815 scopus 로고    scopus 로고
    • Inactivation-resistant human coagulation factor VIIIa (IR8) corrects canine hemophilia A coagulopathy
    • (Suppl. Abstracts)
    • Nichols TC, Pipe SW, Kaufman RJ et al. Inactivation-resistant human coagulation factor VIIIa (IR8) corrects canine hemophilia A coagulopathy. Thromb Haemost 1999; 82 (Suppl. Abstracts): 488a.
    • (1999) Thromb Haemost , vol.82
    • Nichols, T.C.1    Pipe, S.W.2    Kaufman, R.J.3
  • 42
    • 11044221450 scopus 로고    scopus 로고
    • Inactivation-resistant factor VIII provides superior hemostasis to wild-type factor VIII in a murine hemophilia A model without increased thrombogenicity
    • Thornburg CD, Palmer L, Miao HZ et al. Inactivation-resistant factor VIII provides superior hemostasis to wild-type factor VIII in a murine hemophilia A model without increased thrombogenicity. Blood 2003; 102: 88a.
    • (2003) Blood , vol.102
    • Thornburg, C.D.1    Palmer, L.2    Miao, H.Z.3
  • 43
    • 0030903424 scopus 로고    scopus 로고
    • A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin
    • Pemberton S, Lindley P, Zaitsev V et al. A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 1997; 89: 2413-21.
    • (1997) Blood , vol.89 , pp. 2413-2421
    • Pemberton, S.1    Lindley, P.2    Zaitsev, V.3
  • 44
    • 0036707993 scopus 로고    scopus 로고
    • Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C
    • Gale AJ, Xu X, Pellequer JL et al. Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C. Protein Sci 2002; 11: 2091-101.
    • (2002) Protein Sci , vol.11 , pp. 2091-2101
    • Gale, A.J.1    Xu, X.2    Pellequer, J.L.3
  • 45
    • 2342666603 scopus 로고    scopus 로고
    • A novel engineered interdomain disulfide bond stabilizes human blood coagulation factor VIIIa
    • OC094
    • Gale AJ, Pellequer JL, Griffin JH. A novel engineered interdomain disulfide bond stabilizes human blood coagulation factor VIIIa. J Thromb Haemost 2003; 1 (Suppl. 1): OC094.
    • (2003) J Thromb Haemost , vol.1 , Issue.SUPPL. 1
    • Gale, A.J.1    Pellequer, J.L.2    Griffin, J.H.3
  • 46
    • 33646128433 scopus 로고    scopus 로고
    • Whole blood thromboelastogram assays demonstrate prolonged factor VIIIa potency for recombinant disulfide bond-stabilized factor VIII variants
    • Radtke K-P, Chamberlain D, Griffin JH, Gale AJ. Whole blood thromboelastogram assays demonstrate prolonged factor VIIIa potency for recombinant disulfide bond-stabilized factor VIII variants. Blood 2004; 104: 2976a.
    • (2004) Blood , vol.104
    • Radtke, K.-P.1    Chamberlain, D.2    Griffin, J.H.3    Gale, A.J.4
  • 47
    • 0033621486 scopus 로고    scopus 로고
    • Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism
    • Saenko EL, Yakhyaev AV, Mikhailenko I et al. Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism. J Biol Chem 1999; 274: 37685-92.
    • (1999) J Biol Chem , vol.274 , pp. 37685-37692
    • Saenko, E.L.1    Yakhyaev, A.V.2    Mikhailenko, I.3
  • 48
    • 0033588163 scopus 로고    scopus 로고
    • The light chain of factor VIII comprises a binding site for low density lipoprotein receptor-related protein
    • Lenting PJ, Neels JG, van den Berg BM et al. The light chain of factor VIII comprises a binding site for low density lipoprotein receptor-related protein. J Biol Chem 1999; 274: 23734-9.
    • (1999) J Biol Chem , vol.274 , pp. 23734-23739
    • Lenting, P.J.1    Neels, J.G.2    van den Berg, B.M.3
  • 49
    • 0034161385 scopus 로고    scopus 로고
    • Involvement of low-density lipoprotein receptor-related protein (LRP) in the clearance of factor VIII in von Willebrand factor-deficient mice
    • Schwarz HP, Lenting PJ, Binder B et al. Involvement of low-density lipoprotein receptor-related protein (LRP) in the clearance of factor VIII in von Willebrand factor-deficient mice. Blood 2000; 95: 1703-8.
    • (2000) Blood , vol.95 , pp. 1703-1708
    • Schwarz, H.P.1    Lenting, P.J.2    Binder, B.3
  • 50
    • 0034210883 scopus 로고    scopus 로고
    • In vivo inhibition of low density lipoprotein receptor-related protein improves survival of factor VIII in the absence of von Willebrand factor
    • Turecek PL, Schwarz HP, Binder BR. In vivo inhibition of low density lipoprotein receptor-related protein improves survival of factor VIII in the absence of von Willebrand factor. Blood 2000; 95: 3637-8.
    • (2000) Blood , vol.95 , pp. 3637-3638
    • Turecek, P.L.1    Schwarz, H.P.2    Binder, B.R.3
  • 51
    • 0037926885 scopus 로고    scopus 로고
    • Elevated plasma factor VIII in a mouse model of low-density lipoprotein receptor-related protein deficiency
    • Bovenschen N, Herz J, Grimbergen JM et al. Elevated plasma factor VIII in a mouse model of low-density lipoprotein receptor-related protein deficiency. Blood 2003; 101: 3933-9.
    • (2003) Blood , vol.101 , pp. 3933-3939
    • Bovenschen, N.1    Herz, J.2    Grimbergen, J.M.3
  • 52
    • 23044478501 scopus 로고    scopus 로고
    • LDL receptor cooperates with LDL receptor-related protein in regulating plasma levels of coagulation factor VIII in vivo
    • Bovenschen N, Mertens K, Hu L et al. LDL receptor cooperates with LDL receptor-related protein in regulating plasma levels of coagulation factor VIII in vivo. Blood 2005; 106: 906-12.
    • (2005) Blood , vol.106 , pp. 906-912
    • Bovenschen, N.1    Mertens, K.2    Hu, L.3
  • 53
    • 0034530108 scopus 로고    scopus 로고
    • Interaction between factor VIII and LDL receptor-related protein. Modulation of coagulation?
    • Neels JG, Bovenschen N, van Zonneveld AJ, Lenting PJ. Interaction between factor VIII and LDL receptor-related protein. Modulation of coagulation? Trends Cardiovasc Med 2000; 10: 8-14.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 8-14
    • Neels, J.G.1    Bovenschen, N.2    van Zonneveld, A.J.3    Lenting, P.J.4
  • 54
    • 0035853843 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycans participate in factor VIII catabolism mediated by low density lipoprotein receptor-related protein
    • Sarafanov AG, Ananyeva NM, Shima M, Saenko EL. Cell surface heparan sulfate proteoglycans participate in factor VIII catabolism mediated by low density lipoprotein receptor-related protein. J Biol Chem 2001; 276: 11970-9.
    • (2001) J Biol Chem , vol.276 , pp. 11970-11979
    • Sarafanov, A.G.1    Ananyeva, N.M.2    Shima, M.3    Saenko, E.L.4
  • 55
    • 0037646492 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein and factor IXa share structural requirements for binding to the A3 domain of coagulation factor VIII
    • Bovenschen N, Boertjes RC, Van Stempvoort G et al. Low-density lipoprotein receptor-related protein and factor IXa share structural requirements for binding to the A3 domain of coagulation factor VIII. J Biol Chem 2003; 278: 9370-7.
    • (2003) J Biol Chem , vol.278 , pp. 9370-9377
    • Bovenschen, N.1    Boertjes, R.C.2    Van Stempvoort, G.3
  • 56
    • 0029670912 scopus 로고    scopus 로고
    • The sequence Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX
    • Lenting PJ, van de Loo JW, Donath MJ et al. The sequence Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX. J Biol Chem 1996; 271: 1935-40.
    • (1996) J Biol Chem , vol.271 , pp. 1935-1940
    • Lenting, P.J.1    van de Loo, J.W.2    Donath, M.J.3
  • 57
    • 0034282886 scopus 로고    scopus 로고
    • Sites in the A2 subunit involved in the interfactor VIIIa interaction
    • Koszelak ME, Huggins CF, Fay PJ. Sites in the A2 subunit involved in the interfactor VIIIa interaction. J Biol Chem 2000; 275: 27137-44.
    • (2000) J Biol Chem , vol.275 , pp. 27137-27144
    • Koszelak, M.E.1    Huggins, C.F.2    Fay, P.J.3
  • 58
    • 0037082464 scopus 로고    scopus 로고
    • 3-Dimensional structure of membrane-bound coagulation factor VIII: Modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography
    • Stoilova-McPhie S, Villoutreix BO, Mertens K et al. 3-Dimensional structure of membrane-bound coagulation factor VIII: Modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography. Blood 2002; 99: 1215-23.
    • (2002) Blood , vol.99 , pp. 1215-1223
    • Stoilova-McPhie, S.1    Villoutreix, B.O.2    Mertens, K.3
  • 59
    • 32344444865 scopus 로고    scopus 로고
    • Identification of coagulation factor VIII A2 domain residues forming the binding epitope for low-density lipoprotein receptor-related protein
    • Sarafanov AG, Makogonenko EM, Pechik IV et al. Identification of coagulation factor VIII A2 domain residues forming the binding epitope for low-density lipoprotein receptor-related protein. Biochemistry 2006; 45: 1829-40.
    • (2006) Biochemistry , vol.45 , pp. 1829-1840
    • Sarafanov, A.G.1    Makogonenko, E.M.2    Pechik, I.V.3
  • 60
    • 0038779248 scopus 로고    scopus 로고
    • A survey of factor prophylaxis in boys with haemophilia followed in North American haemophilia treatment centres
    • (discussion, 26)
    • Blanchette VS, McCready M, Achonu C et al. A survey of factor prophylaxis in boys with haemophilia followed in North American haemophilia treatment centres. Haemophilia 2003; 9 (Suppl. 1): 19-26. (discussion, 26).
    • (2003) Haemophilia , vol.9 , Issue.SUPPL. 1 , pp. 19-26
    • Blanchette, V.S.1    McCready, M.2    Achonu, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.