메뉴 건너뛰기




Volumn 130, Issue 23, 2017, Pages 2463-2468

Emicizumab, a bispecific antibody recognizing coagulation factors IX and X: How does it actually compare to factor VIII?

Author keywords

[No Author keywords available]

Indexed keywords

BISPECIFIC ANTIBODY; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 9; EMICIZUMAB; ENZYME PRECURSOR; BLOOD CLOTTING FACTOR 13A; MONOCLONAL ANTIBODY; MULTIPROTEIN COMPLEX; PROTEIN BINDING;

EID: 85037622811     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2017-08-801662     Document Type: Review
Times cited : (212)

References (55)
  • 1
    • 0026635406 scopus 로고
    • Twenty-five years’ experience of prophylactic treatment in severe haemophilia A and B
    • Nilsson IM, Berntorp E, Löfqvist T, Pettersson H. Twenty-five years’ experience of prophylactic treatment in severe haemophilia A and B. J Intern Med. 1992;232(1):25-32.
    • (1992) J Intern Med , vol.232 , Issue.1 , pp. 25-32
    • Nilsson, I.M.1    Berntorp, E.2    Löfqvist, T.3    Pettersson, H.4
  • 2
    • 34547757915 scopus 로고    scopus 로고
    • Prophylaxis versus episodic treatment to prevent joint disease in boys with severe hemophilia
    • Manco-Johnson MJ, Abshire TC, Shapiro AD, et al. Prophylaxis versus episodic treatment to prevent joint disease in boys with severe hemophilia. N Engl J Med. 2007;357(6):535-544.
    • (2007) N Engl J Med , vol.357 , Issue.6 , pp. 535-544
    • Manco-Johnson, M.J.1    Abshire, T.C.2    Shapiro, A.D.3
  • 3
    • 84872450786 scopus 로고    scopus 로고
    • Factor VIII products and inhibitor development in severe hemophilia A
    • Gouw SC, van der Bom JG, Ljung R, et al. PedNet and RODIN Study Group. Factor VIII products and inhibitor development in severe hemophilia A. N Engl J Med. 2013;368(3):231-239.
    • (2013) N Engl J Med , vol.368 , Issue.3 , pp. 231-239
    • Gouw, S.C.1    Van Der Bom, J.G.2    Ljung, R.3
  • 4
    • 84914140043 scopus 로고    scopus 로고
    • FranceCoag Network. Recombinant factor VIII products and inhibitor development in previously untreated boys with severe hemophilia A
    • Calvez T, Chambost H, Claeyssens-Donadel S, et al. FranceCoag Network. Recombinant factor VIII products and inhibitor development in previously untreated boys with severe hemophilia A. Blood. 2014;124(23):3398-3408.
    • (2014) Blood , vol.124 , Issue.23 , pp. 3398-3408
    • Calvez, T.1    Chambost, H.2    Claeyssens-Donadel, S.3
  • 5
    • 84971222569 scopus 로고    scopus 로고
    • A Randomized Trial of Factor VIII and Neutralizing Antibodies in Hemophilia A
    • Peyvandi F, Mannucci PM, Garagiola I, et al. A Randomized Trial of Factor VIII and Neutralizing Antibodies in Hemophilia A. N Engl J Med. 2016; 374(21):2054-2064.
    • (2016) N Engl J Med , vol.374 , Issue.21 , pp. 2054-2064
    • Peyvandi, F.1    Mannucci, P.M.2    Garagiola, I.3
  • 6
    • 84887363261 scopus 로고    scopus 로고
    • Factor VIII gene (F8) mutation and risk of inhibitor development in nonsevere hemophilia A
    • Eckhardt CL, van Velzen AS, Peters M, et al. INSIGHT Study Group. Factor VIII gene (F8) mutation and risk of inhibitor development in nonsevere hemophilia A. Blood. 2013;122(11): 1954-1962.
    • (2013) Blood , vol.122 , Issue.11 , pp. 1954-1962
    • Eckhardt, C.L.1    Van Velzen, A.S.2    Peters, M.3
  • 7
    • 84934783767 scopus 로고    scopus 로고
    • INSIGHT study group. Inhibitors in nonsevere haemophilia A: Outcome and eradication strategies
    • van Velzen AS, Eckhardt CL, Hart DP, et al. INSIGHT study group. Inhibitors in nonsevere haemophilia A: outcome and eradication strategies. Thromb Haemost. 2015;114(1):46-55.
    • (2015) Thromb Haemost , vol.114 , Issue.1 , pp. 46-55
    • Van Velzen, A.S.1    Eckhardt, C.L.2    Hart, D.P.3
  • 8
    • 84893123337 scopus 로고    scopus 로고
    • A-LONG Investigators. Phase 3 study of recombinant factor VIII Fc fusion protein in severe hemophilia A
    • Mahlangu J, Powell JS, Ragni MV, et al. A-LONG Investigators. Phase 3 study of recombinant factor VIII Fc fusion protein in severe hemophilia A. Blood. 2014;123(3):317-325.
    • (2014) Blood , vol.123 , Issue.3 , pp. 317-325
    • Mahlangu, J.1    Powell, J.S.2    Ragni, M.V.3
  • 9
    • 84942546645 scopus 로고    scopus 로고
    • Pegylated, full-length, recombinant factor VIII for prophylactic and on-demand treatment of severe hemophilia A
    • Konkle BA, Stasyshyn O, Chowdary P, et al. Pegylated, full-length, recombinant factor VIII for prophylactic and on-demand treatment of severe hemophilia A. Blood. 2015;126(9):1078-1085.
    • (2015) Blood , vol.126 , Issue.9 , pp. 1078-1085
    • Konkle, B.A.1    Stasyshyn, O.2    Chowdary, P.3
  • 10
    • 84928764693 scopus 로고    scopus 로고
    • Safety and pharmacokinetics of anti-TFPI antibody (concizumab) in healthy volunteers and patients with hemophilia: A randomized first human dose trial
    • Chowdary P, Lethagen S, Friedrich U, et al. Safety and pharmacokinetics of anti-TFPI antibody (concizumab) in healthy volunteers and patients with hemophilia: a randomized first human dose trial. J Thromb Haemost. 2015;13(5): 743-754.
    • (2015) J Thromb Haemost , vol.13 , Issue.5 , pp. 743-754
    • Chowdary, P.1    Lethagen, S.2    Friedrich, U.3
  • 11
    • 84937764228 scopus 로고    scopus 로고
    • An RNAi therapeutic targeting antithrombin to rebalance the coagulation system and promote hemostasis in hemophilia
    • Sehgal A, Barros S, Ivanciu L, et al. An RNAi therapeutic targeting antithrombin to rebalance the coagulation system and promote hemostasis in hemophilia. Nat Med. 2015;21(5):492-497.
    • (2015) Nat Med , vol.21 , Issue.5 , pp. 492-497
    • Sehgal, A.1    Barros, S.2    Ivanciu, L.3
  • 12
    • 84870302675 scopus 로고    scopus 로고
    • A bispecific antibody to factors IXa and X restores factor VIII hemostatic activity in a hemophilia A model
    • Kitazawa T, Igawa T, Sampei Z, et al. A bispecific antibody to factors IXa and X restores factor VIII hemostatic activity in a hemophilia A model. Nat Med. 2012;18(10):1570-1574.
    • (2012) Nat Med , vol.18 , Issue.10 , pp. 1570-1574
    • Kitazawa, T.1    Igawa, T.2    Sampei, Z.3
  • 13
    • 84911438456 scopus 로고    scopus 로고
    • Anti-factor IXa/X bispecific antibody ACE910 prevents joint bleeds in a long-term primate model of acquired hemophilia A
    • Muto A, Yoshihashi K, Takeda M, et al. Anti-factor IXa/X bispecific antibody ACE910 prevents joint bleeds in a long-term primate model of acquired hemophilia A. Blood. 2014;124(20):3165-3171.
    • (2014) Blood , vol.124 , Issue.20 , pp. 3165-3171
    • Muto, A.1    Yoshihashi, K.2    Takeda, M.3
  • 14
    • 84963623112 scopus 로고    scopus 로고
    • A first-inhuman phase 1 study of ACE910, a novel factor VIII-mimetic bispecific antibody, in healthy subjects
    • Uchida N, Sambe T, Yoneyama K, et al. A first-inhuman phase 1 study of ACE910, a novel factor VIII-mimetic bispecific antibody, in healthy subjects. Blood. 2016;127(13):1633-1641.
    • (2016) Blood , vol.127 , Issue.13 , pp. 1633-1641
    • Uchida, N.1    Sambe, T.2    Yoneyama, K.3
  • 15
    • 84971325206 scopus 로고    scopus 로고
    • Factor VIII-mimetic function of humanized bispecific antibody in hemophilia A
    • Shima M, Hanabusa H, Taki M, et al. Factor VIII-mimetic function of humanized bispecific antibody in hemophilia A. N Engl J Med. 2016;374(21): 2044-2053.
    • (2016) N Engl J Med , vol.374 , Issue.21 , pp. 2044-2053
    • Shima, M.1    Hanabusa, H.2    Taki, M.3
  • 16
    • 85028497303 scopus 로고    scopus 로고
    • Emicizumab prophylaxis in hemophilia A with inhibitors
    • Oldenburg J, Mahlangu JN, Kim B, et al. Emicizumab prophylaxis in hemophilia A with inhibitors. N Engl J Med. 2017;377(9):809-818.
    • (2017) N Engl J Med , vol.377 , Issue.9 , pp. 809-818
    • Oldenburg, J.1    Mahlangu, J.N.2    Kim, B.3
  • 17
    • 0022363126 scopus 로고
    • Purification of human factor VIII: C and its characterization by Western blotting using monoclonal antibodies
    • Rotblat F, O’Brien DP, O’Brien FJ, Goodall AH, Tuddenham EG. Purification of human factor VIII: C and its characterization by Western blotting using monoclonal antibodies. Biochemistry. 1985; 24(16):4294-4300.
    • (1985) Biochemistry , vol.24 , Issue.16 , pp. 4294-4300
    • Rotblat, F.1    O’Brien, D.P.2    O’Brien, F.J.3    Goodall, A.H.4    Tuddenham, E.G.5
  • 18
    • 0000640811 scopus 로고
    • Isolation and characterization of human factor VIII: Molecular forms in commercial factor VIII concentrate, cryoprecipitate, and plasma
    • Andersson LO, Forsman N, Huang K, et al. Isolation and characterization of human factor VIII: molecular forms in commercial factor VIII concentrate, cryoprecipitate, and plasma. Proc Natl Acad Sci USA. 1986;83(9):2979-2983.
    • (1986) Proc Natl Acad Sci USA , vol.83 , Issue.9 , pp. 2979-2983
    • Andersson, L.O.1    Forsman, N.2    Huang, K.3
  • 19
    • 0023918719 scopus 로고
    • Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells
    • Kaufman RJ, Wasley LC, Dorner AJ. Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells. J Biol Chem. 1988;263(13):6352-6362.
    • (1988) J Biol Chem , vol.263 , Issue.13 , pp. 6352-6362
    • Kaufman, R.J.1    Wasley, L.C.2    Dorner, A.J.3
  • 20
    • 84992390506 scopus 로고    scopus 로고
    • Life in the shadow of a dominant partner: The FVIII-VWF association and its clinical implications for hemophilia A
    • Pipe SW, Montgomery RR, Pratt KP, Lenting PJ, Lillicrap D. Life in the shadow of a dominant partner: the FVIII-VWF association and its clinical implications for hemophilia A. Blood. 2016; 128(16):2007-2016.
    • (2016) Blood , vol.128 , Issue.16 , pp. 2007-2016
    • Pipe, S.W.1    Montgomery, R.R.2    Pratt, K.P.3    Lenting, P.J.4    Lillicrap, D.5
  • 21
    • 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(2):505-512.
    • (1986) Biochemistry , vol.25 , Issue.2 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 22
    • 0025924755 scopus 로고
    • Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor
    • Leyte A, van Schijndel HB, Niehrs C, et al. Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor. J Biol Chem. 1991; 266(2):740-746.
    • (1991) J Biol Chem , vol.266 , Issue.2 , pp. 740-746
    • Leyte, A.1    Van Schijndel, H.B.2    Niehrs, C.3
  • 23
    • 0032402122 scopus 로고    scopus 로고
    • The life cycle of coagulation factor VIII in view of its structure and function
    • Lenting PJ, van Mourik JA, Mertens K. The life cycle of coagulation factor VIII in view of its structure and function. Blood. 1998;92(11): 3983-3996.
    • (1998) Blood , vol.92 , Issue.11 , pp. 3983-3996
    • Lenting, P.J.1    Van Mourik, J.A.2    Mertens, K.3
  • 24
    • 0020048708 scopus 로고
    • Activation of human coagulation factor VIII by activated factor X, the common product of the intrinsic and the extrinsic pathway of blood coagulation
    • Mertens K, Bertina RM. Activation of human coagulation factor VIII by activated factor X, the common product of the intrinsic and the extrinsic pathway of blood coagulation. Thromb Haemost. 1982;47(2):96-100.
    • (1982) Thromb Haemost , vol.47 , Issue.2 , pp. 96-100
    • Mertens, K.1    Bertina, R.M.2
  • 25
    • 85030647109 scopus 로고    scopus 로고
    • Selective factor VIII activation by the tissue factor-factor VIIa-factor Xa complex
    • Kamikubo Y, Mendolicchio GL, Zampolli A, et al. Selective factor VIII activation by the tissue factor-factor VIIa-factor Xa complex. Blood. 2017; 130(14):1661-1670.
    • (2017) Blood , vol.130 , Issue.14 , pp. 1661-1670
    • Kamikubo, Y.1    Mendolicchio, G.L.2    Zampolli, A.3
  • 27
    • 0032722436 scopus 로고    scopus 로고
    • Factor VIII-factor IX interactions: Molecular sites involved in enzyme-cofactor complex assembly
    • Mertens K, Celie PH, Kolkman JA, Lenting PJ. Factor VIII-factor IX interactions: molecular sites involved in enzyme-cofactor complex assembly. Thromb Haemost. 1999;82(2):209-217.
    • (1999) Thromb Haemost , vol.82 , Issue.2 , pp. 209-217
    • Mertens, K.1    Celie, P.H.2    Kolkman, J.A.3    Lenting, P.J.4
  • 28
    • 0029027015 scopus 로고
    • Binding of blood coagulation factor VIII and its light chain to phosphatidylserine/phosphatidylcholine bilayers as measured by ellipsometry
    • Spaargaren J, Giesen PL, Janssen MP, Voorberg J, Willems GM, van Mourik JA. Binding of blood coagulation factor VIII and its light chain to phosphatidylserine/phosphatidylcholine bilayers as measured by ellipsometry. Biochem J. 1995; 310(Pt 2):539-545.
    • (1995) Biochem J , vol.310 , pp. 539-545
    • Spaargaren, J.1    Giesen, P.L.2    Janssen, M.P.3    Voorberg, J.4    Willems, G.M.5    Van Mourik, J.A.6
  • 29
    • 0021702091 scopus 로고
    • Binding of human blood-coagulation Factors IXa and X to phospholipid membranes
    • Mertens K, Cupers R, Van Wijngaarden A, Bertina RM. Binding of human blood-coagulation Factors IXa and X to phospholipid membranes. Biochem J. 1984;223(3):599-605.
    • (1984) Biochem J , vol.223 , Issue.3 , pp. 599-605
    • Mertens, K.1    Cupers, R.2    Van Wijngaarden, A.3    Bertina, R.M.4
  • 30
    • 0028239173 scopus 로고
    • Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII
    • Lenting PJ, Donath MJ, van Mourik JA, Mertens K. Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII. J Biol Chem. 1994;269(10):7150-7155.
    • (1994) J Biol Chem , vol.269 , Issue.10 , pp. 7150-7155
    • Lenting, P.J.1    Donath, M.J.2    Van Mourik, J.A.3    Mertens, K.4
  • 31
    • 0026785721 scopus 로고
    • Binding of factor VIIIa and factor VIII to factor IXa on phospholipid vesicles
    • Duffy EJ, Parker ET, Mutucumarana VP, Johnson AE, Lollar P. Binding of factor VIIIa and factor VIII to factor IXa on phospholipid vesicles. J Biol Chem. 1992;267(24):17006-17011.
    • (1992) J Biol Chem , vol.267 , Issue.24 , pp. 17006-17011
    • Duffy, E.J.1    Parker, E.T.2    Mutucumarana, V.P.3    Johnson, A.E.4    Lollar, P.5
  • 32
    • 84907480691 scopus 로고    scopus 로고
    • Structural insights into the interaction of blood coagulation co-factor VIIIa with factor IXa: A computational protein-protein docking and molecular dynamics refinement study
    • Venkateswarlu D. Structural insights into the interaction of blood coagulation co-factor VIIIa with factor IXa: a computational protein-protein docking and molecular dynamics refinement study. Biochem Biophys Res Commun. 2014; 452(3):408-414.
    • (2014) Biochem Biophys Res Commun , vol.452 , Issue.3 , pp. 408-414
    • Venkateswarlu, D.1
  • 33
    • 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, O’Brien LM, Kaufman RJ. 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(11):6027-6032.
    • (1996) J Biol Chem , vol.271 , Issue.11 , pp. 6027-6032
    • Fay, P.J.1    Beattie, T.L.2    Regan, L.M.3    O’Brien, L.M.4    Kaufman, R.J.5
  • 34
    • 0032563086 scopus 로고    scopus 로고
    • The A2 subunit of factor VIIIa modulates the active site of factor IXa
    • Fay PJ, Koshibu K. The A2 subunit of factor VIIIa modulates the active site of factor IXa. J Biol Chem. 1998;273(30):19049-19054.
    • (1998) J Biol Chem , vol.273 , Issue.30 , pp. 19049-19054
    • Fay, P.J.1    Koshibu, K.2
  • 35
    • 0033560705 scopus 로고    scopus 로고
    • Regions 301-303 and 333-339 in the catalytic domain of blood coagulation factor IX are factor VIII-interactive sites involved in stimulation of enzyme activity
    • Kolkman JA, Lenting PJ, Mertens K. Regions 301-303 and 333-339 in the catalytic domain of blood coagulation factor IX are factor VIII-interactive sites involved in stimulation of enzyme activity. Biochem J. 1999;339(Pt 2):217-221.
    • (1999) Biochem J , vol.339 , pp. 217-221
    • Kolkman, J.A.1    Lenting, P.J.2    Mertens, K.3
  • 36
    • 0032857459 scopus 로고    scopus 로고
    • Surface loop 199-204 in blood coagulation factor IX is a cofactor-dependent site involved in macromolecular substrate interaction
    • Kolkman JA, Christophe OD, Lenting PJ, Mertens K. Surface loop 199-204 in blood coagulation factor IX is a cofactor-dependent site involved in macromolecular substrate interaction. J Biol Chem. 1999;274(41):29087-29093.
    • (1999) J Biol Chem , vol.274 , Issue.41 , pp. 29087-29093
    • Kolkman, J.A.1    Christophe, O.D.2    Lenting, P.J.3    Mertens, K.4
  • 37
    • 0034720774 scopus 로고    scopus 로고
    • Insertion loop 256-268 in coagulation factor IX restricts enzymatic activity in the absence but not in the presence of factor VIII
    • Kolkman JA, Mertens K. Insertion loop 256-268 in coagulation factor IX restricts enzymatic activity in the absence but not in the presence of factor VIII. Biochemistry. 2000;39(25):7398-7405.
    • (2000) Biochemistry , vol.39 , Issue.25 , pp. 7398-7405
    • Kolkman, J.A.1    Mertens, K.2
  • 38
    • 0031754930 scopus 로고    scopus 로고
    • Interaction of the A1 subunit of factor VIIIa and the serine protease domain of factor X identified by zero-length cross-linking
    • Lapan KA, Fay PJ. Interaction of the A1 subunit of factor VIIIa and the serine protease domain of factor X identified by zero-length cross-linking. Thromb Haemost. 1998;80(3):418-422.
    • (1998) Thromb Haemost , vol.80 , Issue.3 , pp. 418-422
    • Lapan, K.A.1    Fay, P.J.2
  • 39
    • 0031027575 scopus 로고    scopus 로고
    • Localization of a factor X interactive site in the A1 subunit of factor VIIIa
    • Lapan KA, Fay PJ. Localization of a factor X interactive site in the A1 subunit of factor VIIIa. J Biol Chem. 1997;272(4):2082-2088.
    • (1997) J Biol Chem , vol.272 , Issue.4 , pp. 2082-2088
    • Lapan, K.A.1    Fay, P.J.2
  • 40
    • 84856287741 scopus 로고    scopus 로고
    • Factor VIII light chain contains a binding site for factor X that contributes to the catalytic efficiency of factor Xase
    • Takeyama M, Wakabayashi H, Fay PJ. Factor VIII light chain contains a binding site for factor X that contributes to the catalytic efficiency of factor Xase. Biochemistry. 2012;51(3):820-828.
    • (2012) Biochemistry , vol.51 , Issue.3 , pp. 820-828
    • Takeyama, M.1    Wakabayashi, H.2    Fay, P.J.3
  • 41
    • 84874562364 scopus 로고    scopus 로고
    • Identification and multidimensional optimization of an asymmetric bispecific IgG antibody mimicking the function of factor VIII cofactor activity
    • Sampei Z, Igawa T, Soeda T, et al. Identification and multidimensional optimization of an asymmetric bispecific IgG antibody mimicking the function of factor VIII cofactor activity. PLoS One. 2013;8(2):e57479.
    • (2013) PLoS One , vol.8 , Issue.2
    • Sampei, Z.1    Igawa, T.2    Soeda, T.3
  • 42
    • 85021675727 scopus 로고    scopus 로고
    • Factor VIIIa-mimetic cofactor activity of a bispecific antibody to factors IX/IXa and X/Xa, emicizumab, depends on its ability to bridge the antigens
    • Kitazawa T, Esaki K, Tachibana T, et al. Factor VIIIa-mimetic cofactor activity of a bispecific antibody to factors IX/IXa and X/Xa, emicizumab, depends on its ability to bridge the antigens. Thromb Haemost. 2017;117(7):1348-1357.
    • (2017) Thromb Haemost , vol.117 , Issue.7 , pp. 1348-1357
    • Kitazawa, T.1    Esaki, K.2    Tachibana, T.3
  • 43
    • 0018188355 scopus 로고
    • Activation of clotting factors in prothrombin complex concentrates as demonstrated by clotting assays for factors IXa and Xa
    • Elödi S, Váradi K. Activation of clotting factors in prothrombin complex concentrates as demonstrated by clotting assays for factors IXa and Xa. Thromb Res. 1978;12(5):797-807.
    • (1978) Thromb Res , vol.12 , Issue.5 , pp. 797-807
    • Elödi, S.1    Váradi, K.2
  • 44
    • 0018633905 scopus 로고
    • Activated clotting factors in factor IX concentrates
    • Hultin MB. Activated clotting factors in factor IX concentrates. Blood. 1979;54(5):1028-1038.
    • (1979) Blood , vol.54 , Issue.5 , pp. 1028-1038
    • Hultin, M.B.1
  • 45
    • 0021646754 scopus 로고
    • The contribution of Ca21 and phospholipids to the activation of human blood-coagulation factor X by activated factor IX
    • Mertens K, Bertina RM. The contribution of Ca21 and phospholipids to the activation of human blood-coagulation factor X by activated factor IX. Biochem J. 1984;223(3):607-615.
    • (1984) Biochem J , vol.223 , Issue.3 , pp. 607-615
    • Mertens, K.1    Bertina, R.M.2
  • 46
    • 0023821390 scopus 로고
    • The binding of 35S-labeled recombinant factor VIII to activated and unactivated human platelets
    • Nesheim ME, Pittman DD, Wang JH, Slonosky D, Giles AR, Kaufman RJ. The binding of 35S-labeled recombinant factor VIII to activated and unactivated human platelets. J Biol Chem. 1988; 263(31):16467-16470.
    • (1988) J Biol Chem , vol.263 , Issue.31 , pp. 16467-16470
    • Nesheim, M.E.1    Pittman, D.D.2    Wang, J.H.3    Slonosky, D.4    Giles, A.R.5    Kaufman, R.J.6
  • 47
    • 84944097506 scopus 로고    scopus 로고
    • Coordinated membrane ballooning and procoagulant spreading in human platelets
    • Agbani EO, van den Bosch MT, Brown E, et al. Coordinated membrane ballooning and procoagulant spreading in human platelets. Circulation. 2015;132(15):1414-1424.
    • (2015) Circulation , vol.132 , Issue.15 , pp. 1414-1424
    • Agbani, E.O.1    Van Den Bosch, M.T.2    Brown, E.3
  • 48
    • 84942513387 scopus 로고    scopus 로고
    • Platelet binding sites for factor VIII in relation to fibrin and phosphatidylserine
    • Gilbert GE, Novakovic VA, Shi J, Rasmussen J, Pipe SW. Platelet binding sites for factor VIII in relation to fibrin and phosphatidylserine. Blood. 2015;126(10):1237-1244.
    • (2015) Blood , vol.126 , Issue.10 , pp. 1237-1244
    • Gilbert, G.E.1    Novakovic, V.A.2    Shi, J.3    Rasmussen, J.4    Pipe, S.W.5
  • 49
    • 0016703241 scopus 로고
    • Inhibition of human factor IXa by human antithrombin
    • Rosenberg JS, McKenna PW, Rosenberg RD. Inhibition of human factor IXa by human antithrombin. J Biol Chem. 1975;250(23): 8883-8888.
    • (1975) J Biol Chem , vol.250 , Issue.23 , pp. 8883-8888
    • Rosenberg, J.S.1    McKenna, P.W.2    Rosenberg, R.D.3
  • 50
    • 0027517128 scopus 로고
    • Protease nexin-2/amyloid beta protein precursor. A tight-binding inhibitor of coagulation factor IXa
    • Schmaier AH, Dahl LD, Rozemuller AJ, et al. Protease nexin-2/amyloid beta protein precursor. A tight-binding inhibitor of coagulation factor IXa. J Clin Invest. 1993;92(5):2540-2545.
    • (1993) J Clin Invest , vol.92 , Issue.5 , pp. 2540-2545
    • Schmaier, A.H.1    Dahl, L.D.2    Rozemuller, A.J.3
  • 51
    • 84963545939 scopus 로고    scopus 로고
    • In vitro characterization of ACE910, a humanized bispecific antibody to factors IXa and X
    • Soeda T, Kitazawa T, Muto A, et al. In vitro characterization of ACE910, a humanized bispecific antibody to factors IXa and X. Haemophilia. 2014;20(suppl 3):77.
    • (2014) Haemophilia , vol.20 , pp. 77
    • Soeda, T.1    Kitazawa, T.2    Muto, A.3
  • 53
    • 0033579442 scopus 로고    scopus 로고
    • Electron crystallography of human blood coagulation factor VIII bound to phospholipid monolayers
    • Stoylova SS, Lenting PJ, Kemball-Cook G, Holzenburg A. Electron crystallography of human blood coagulation factor VIII bound to phospholipid monolayers. J Biol Chem. 1999; 274(51):36573-36578.
    • (1999) J Biol Chem , vol.274 , Issue.51 , pp. 36573-36578
    • Stoylova, S.S.1    Lenting, P.J.2    Kemball-Cook, G.3    Holzenburg, A.4
  • 54
    • 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, Kemball-Cook G, Holzenburg A. 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(4):1215-1223.
    • (2002) Blood , vol.99 , Issue.4 , pp. 1215-1223
    • Stoilova-McPhie, S.1    Villoutreix, B.O.2    Mertens, K.3    Kemball-Cook, G.4    Holzenburg, A.5
  • 55
    • 70449709337 scopus 로고    scopus 로고
    • Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity
    • Meems H, Meijer AB, Cullinan DB, Mertens K, Gilbert GE. Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity. Blood. 2009; 114(18):3938-3946.
    • (2009) Blood , vol.114 , Issue.18 , pp. 3938-3946
    • Meems, H.1    Meijer, A.B.2    Cullinan, D.B.3    Mertens, K.4    Gilbert, G.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.