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Volumn 117, Issue 1, 2011, Pages 290-298

Zymogen-like factor Xa variants restore thrombin generation and effectively bypass the intrinsic pathway in vitro

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN III; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5A; ENZYME PRECURSOR; MUTANT PROTEIN; THROMBIN; TISSUE FACTOR PATHWAY INHIBITOR;

EID: 78650988916     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-08-300756     Document Type: Article
Times cited : (68)

References (52)
  • 1
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann KG, Nesheim ME, Church WR, Haley PE, Krishnaswamy S. Surface dependent reactions of the vitamin K-dependent enzyme complexes. Blood. 1990;76(1):1-16. (Pubitemid 20220784)
    • (1990) Blood , vol.76 , Issue.1 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, K.R.3    Haley, P.4    Krishnaswamy, S.5
  • 2
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human alpha-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W, Mayr I, Bauman Y, et al. The refined 1.9 Å crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Trp insertion segment. EMBO J. 1989;8(11):3467-3475. (Pubitemid 19273577)
    • (1989) EMBO Journal , vol.8 , Issue.11 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 3
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan AM, James MNG. Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Prot Sci. 1998;7(4):815-836.
    • (1998) Prot Sci , vol.7 , Issue.4 , pp. 815-836
    • Khan, A.M.1    James, M.N.G.2
  • 4
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R, Bode W. Structural basis of the activation and action of trypsin. Acc Chem Res. 1978;11114-11122.
    • (1978) Acc Chem Res , pp. 11114-11122
    • Huber, R.1    Bode, W.2
  • 5
    • 0037020083 scopus 로고    scopus 로고
    • Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site
    • Camire RM. Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site. J Biol Chem. 2002;277(40):37863-37870.
    • (2002) J Biol Chem , vol.277 , Issue.40 , pp. 37863-37870
    • Camire, R.M.1
  • 6
    • 49649122047 scopus 로고    scopus 로고
    • The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly
    • Toso R, Zhu H, Camire RM. The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly. J Biol Chem. 2008;283(27):18627-18635.
    • (2008) J Biol Chem , vol.283 , Issue.27 , pp. 18627-18635
    • Toso, R.1    Zhu, H.2    Camire, R.M.3
  • 7
    • 0021046120 scopus 로고
    • The factor Xa-catalyzed activation of factor V
    • Foster WB, Nesheim ME, Mann KG. The factor Xa-catalyzed activation of factor V. J Biol Chem. 1983;258(22):13970-13977.
    • (1983) J Biol Chem , vol.258 , Issue.22 , pp. 13970-13977
    • Foster, W.B.1    Nesheim, M.E.2    Mann, K.G.3
  • 8
    • 0022454539 scopus 로고
    • Proteolytic processing of human FVIII. Correlation of specific cleavages by thrombin FXa and activated protein C with activation and inactivation of Factor VIII coagulant activity
    • Eaton D, Rodriguez H, Vehar G. Proteolytic processing of human FVIII. Correlation of specific cleavages by thrombin FXa 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.3
  • 9
    • 0030068977 scopus 로고    scopus 로고
    • Kinetics of human factor VII activation
    • Butenas S, Mann KG. Kinetics of human factor VII activation. Biochemistry. 1996;35(6):1904-1910.
    • (1996) Biochemistry , vol.35 , Issue.6 , pp. 1904-1910
    • Butenas, S.1    Mann, K.G.2
  • 10
    • 52949084684 scopus 로고    scopus 로고
    • Factor Xa: At the crossroads between coagulation and signaling in physiology and disease
    • Borensztajn K, Peppelenbosch MP, Spek CA. Factor Xa: at the crossroads between coagulation and signaling in physiology and disease. Trends Mol Med. 2008;14(10):429-440.
    • (2008) Trends Mol Med , vol.14 , Issue.10 , pp. 429-440
    • Borensztajn, K.1    Peppelenbosch, M.P.2    Spek, C.A.3
  • 11
    • 0028932993 scopus 로고
    • Tissue factor pathway inhibitor and the revised theory of coagulation
    • Broze GJ Jr. Tissue factor pathway inhibitor and the revised theory of coagulation. Annu Rev Med. 1995;46103-46112.
    • (1995) Annu Rev Med , pp. 46103-46112
    • Broze Jr., G.J.1
  • 12
    • 0031455114 scopus 로고    scopus 로고
    • Antithrombin. A bloody important serpin
    • Bjork I, Olson ST. Antithrombin. A bloody important serpin. Adv Exp Med Biol. 1997;42517-42533.
    • (1997) Adv Exp Med Biol , pp. 42517-42533
    • Bjork, I.1    Olson, S.T.2
  • 13
    • 65349111124 scopus 로고    scopus 로고
    • Overview of inherited hemorrhagic disorders
    • Colman RW, Marder VJ, Clowes AW, et al, eds. Philadelphia, PA: Lippincott Williams and Wilkins
    • Roberts HR, Ma AD. Overview of inherited hemorrhagic disorders. In: Colman RW, Marder VJ, Clowes AW, et al, eds. Hemostasis and Thrombosis: Basic Principles and Clinical Practice. Philadelphia, PA: Lippincott Williams and Wilkins; 2006:877-885.
    • (2006) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 877-885
    • Roberts, H.R.1    Ma, A.D.2
  • 14
    • 58149461069 scopus 로고    scopus 로고
    • Clinical manifestations and therapy of the hemophilias
    • Colman RW, Marder VJ, Clowes AW, et al, eds. Philadelphia, PA: Lippincott Williams and Wilkins
    • Kessler CM, Mariani G. Clinical manifestations and therapy of the hemophilias. In: Colman RW, Marder VJ, Clowes AW, et al, eds. Hemostasis and Thrombosis: Basic Principles and Clinical Practice. Philadelphia, PA: Lippincott Williams and Wilkins; 2006:887-904.
    • (2006) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 887-904
    • Kessler, C.M.1    Mariani, G.2
  • 15
    • 33746021125 scopus 로고    scopus 로고
    • Mechanism of action, development and clinical experience of recombinant FVIIa
    • Hedner U. Mechanism of action, development and clinical experience of recombinant FVIIa. J Biotechnol. 2006;124(4):747-757.
    • (2006) J Biotechnol , vol.124 , Issue.4 , pp. 747-757
    • Hedner, U.1
  • 17
    • 79951933686 scopus 로고    scopus 로고
    • First 20 years with recombinant FVIIa (NovoSeven)
    • published online ahead of print June 29, doi:10.1111/j.1365-2516.2010. 02352.x
    • Hedner U, Lee CA. First 20 years with recombinant FVIIa (NovoSeven) [published online ahead of print June 29, 2010]. Haemophilia. doi:10.1111/j.1365-2516.2010.02352.x.
    • (2010) Haemophilia
    • Hedner, U.1    Lee, C.A.2
  • 18
    • 63049090494 scopus 로고    scopus 로고
    • Differential response to bypassing agents complicates treatment in patients with haemophilia and inhibitors
    • Berntorp E. Differential response to bypassing agents complicates treatment in patients with haemophilia and inhibitors. Haemophilia. 2009;15(1):3-10.
    • (2009) Haemophilia , vol.15 , Issue.1 , pp. 3-10
    • Berntorp, E.1
  • 19
    • 0021233471 scopus 로고
    • Inhibition of human activated Factor X by antithrombin III and alpha 1-proteinase inhibitor in human plasma
    • Gitel SN, Medina VM, Wessler S. Inhibition of human activated Factor X by antithrombin III and alpha 1-proteinase inhibitor in human plasma. J Biol Chem. 1984;259(11):6890-6895.
    • (1984) J Biol Chem , vol.259 , Issue.11 , pp. 6890-6895
    • Gitel, S.N.1    Medina, V.M.2    Wessler, S.3
  • 20
    • 0022970195 scopus 로고
    • Analysis of the generation and inhibition of activated coagulation factor X in pure systems and in human plasma
    • Jesty J. Analysis of the generation and inhibition of activated coagulation factor X in pure systems and in human plasma. J Biol Chem. 1986;261(19):8695-8702.
    • (1986) J Biol Chem , vol.261 , Issue.19 , pp. 8695-8702
    • Jesty, J.1
  • 21
    • 0021703070 scopus 로고
    • Studies of Factors V and VIII:C in an animal model of disseminated intravascular coagulation
    • Giles AR, Nesheim ME, Mann KG. Studies of Factors V and VIII:C in an animal model of disseminated intravascular coagulation. J Clin Invest. 1984;74(6):2219-2225.
    • (1984) J Clin Invest , vol.74 , Issue.6 , pp. 2219-2225
    • Giles, A.R.1    Nesheim, M.E.2    Mann, K.G.3
  • 22
    • 0023720558 scopus 로고
    • A combination of factor Xa and phosphatidylcholine-phosphatidylserine vesicles bypasses factor VIII in vivo
    • Giles AR, Mann KG, Nesheim ME. A combination of factor Xa and phosphatidylcholine-phosphatidylserine vesicles bypasses factor VIII in vivo. Br J Haematol. 1988;69(4):491-497.
    • (1988) Br J Haematol , vol.69 , Issue.4 , pp. 491-497
    • Giles, A.R.1    Mann, K.G.2    Nesheim, M.E.3
  • 23
    • 0021103421 scopus 로고
    • Solution composition dependent variation in extinction coefficients for ρ-nitroaniline
    • Lottenberg R, Jackson CM. Solution composition dependent variation in extinction coefficients for ρ-nitroaniline. Biochim Biophys Acta. 1983;742(3):558-564.
    • (1983) Biochim Biophys Acta , vol.742 , Issue.3 , pp. 558-564
    • Lottenberg, R.1    Jackson, C.M.2
  • 24
    • 0020633335 scopus 로고
    • The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles
    • Higgins DL, Mann KG. The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles. J Biol Chem. 1983;258(10):6503- 6508. (Pubitemid 13106824)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.10 , pp. 6503-6508
    • Higgins, D.L.1    Mann, K.G.2
  • 25
    • 0037135531 scopus 로고    scopus 로고
    • Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase
    • Buddai SK, Toulokhonova L, Bergum PW, Vlasuk GP, Krishnaswamy S. Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase. J Biol Chem. 2002;277(29):26689-26698.
    • (2002) J Biol Chem , vol.277 , Issue.29 , pp. 26689-26698
    • Buddai, S.K.1    Toulokhonova, L.2    Bergum, P.W.3    Vlasuk, G.P.4    Krishnaswamy, S.5
  • 26
    • 0342300993 scopus 로고
    • Isolation of functional human coagulation Factor V by using a hybridoma antibody
    • Katzmann JA, Nesheim ME, Hibbard LS, Mann KG. Isolation of functional human coagulation Factor V by using a hybridoma antibody. Proc Natl Acad Sci U S A. 1981;78(1):162-166.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , Issue.1 , pp. 162-166
    • Katzmann, J.A.1    Nesheim, M.E.2    Hibbard, L.S.3    Mann, K.G.4
  • 27
    • 0017142556 scopus 로고
    • Factor X activating enzyme from Russell's Viper Venom: Isolation and characterization
    • Kisiel W, Hermodson MA, Davie EW. Factor X activating enzyme from Russell's Viper Venom: Isolation and characterization. Biochemistry. 1976;15(22):4901-4906.
    • (1976) Biochemistry , vol.15 , Issue.22 , pp. 4901-4906
    • Kisiel, W.1    Hermodson, M.A.2    Davie, E.W.3
  • 28
    • 2442655492 scopus 로고    scopus 로고
    • Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized
    • Toso R, Camire RM. Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized. J Biol Chem. 2004;279(20):21643-21650.
    • (2004) J Biol Chem , vol.279 , Issue.20 , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 29
    • 0028365639 scopus 로고
    • Factor X-activating glycoprotein of Russell's viper venom. Polypeptide composition and characterization of the carbohydrate moieties
    • Gowda DC, Jackson CM, Davidson EA. Factor X-activating glycoprotein of Russell's viper venom. Polypeptide composition and characterization of the carbohydrate moieties. J Biol Chem. 1994;269(14):10644-10650.
    • (1994) J Biol Chem , vol.269 , Issue.14 , pp. 10644-10650
    • Gowda, D.C.1    Jackson, C.M.2    Davidson, E.A.3
  • 30
    • 0017275076 scopus 로고
    • Prothrombin
    • Mann KG. Prothrombin. Methods Enzymol. 1976;45:123-156.
    • (1976) Methods Enzymol , vol.45 , pp. 123-156
    • Mann, K.G.1
  • 32
    • 0017337301 scopus 로고
    • A comparison of human prothrombin, factor IX (Christmas Factor), factor X (Stuart Factor), and protein S
    • Di Scipio RG, Hermodson MA, Yates SG, Davie EW. A comparison of human prothrombin, factor IX (Christmas Factor), factor X (Stuart Factor), and protein S. Biochemistry. 1977;16(4):698-706.
    • (1977) Biochemistry , vol.16 , Issue.4 , pp. 698-706
    • Di Scipio, R.G.1    Hermodson, M.A.2    Yates, S.G.3    Davie, E.W.4
  • 33
    • 0027498670 scopus 로고
    • Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
    • Lorand L, Mann KG, eds. San Diego, CA: Academic Press
    • Olson ST, Bjork I, Shore JD. Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. In: Lorand L, Mann KG, eds. Methods in Enzymology Part A. San Diego, CA: Academic Press; 1993:525-559.
    • (1993) Methods in Enzymology Part A , pp. 525-559
    • Olson, S.T.1    Bjork, I.2    Shore, J.D.3
  • 34
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem. 1989;182(2):319-326. (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von, H.P.H.2
  • 35
    • 0032522957 scopus 로고    scopus 로고
    • Platelet-derived factor Va/VaLeiden cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C
    • Camire RM, Kalafatis M, Simioni P, Girolami A, Tracy PB. Platelet-derived factor Va/VaLeiden cofactor activities are sustained on the surface of activated platelets despite the presence of activated protein C. Blood. 1998;91(8):2818-2829.
    • (1998) Blood , vol.91 , Issue.8 , pp. 2818-2829
    • Camire, R.M.1    Kalafatis, M.2    Simioni, P.3    Girolami, A.4    Tracy, P.B.5
  • 36
    • 0242401773 scopus 로고    scopus 로고
    • Calibrated automated thrombin generation measurement in clotting plasma
    • Hemker HC, Giesen P, Al DR, et al. Calibrated automated thrombin generation measurement in clotting plasma. Pathophysiol Haemost Thromb. 2003;33(1):4-15.
    • (2003) Pathophysiol Haemost Thromb , vol.33 , Issue.1 , pp. 4-15
    • Hemker, H.C.1    Giesen, P.2    Al, D.R.3
  • 37
    • 0026719689 scopus 로고
    • Analysis of residuals: Criteria for determining goodness-of-fit
    • Straume M, Johnson ML. Analysis of residuals: criteria for determining goodness-of-fit. Methods Enzymol. 1992;210:87-105.
    • (1992) Methods Enzymol , vol.210 , pp. 87-105
    • Straume, M.1    Johnson, M.L.2
  • 39
    • 0032479424 scopus 로고    scopus 로고
    • Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa
    • Rezaie AR. Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa. J Biol Chem. 1998;273(27):16824- 16827.
    • (1998) J Biol Chem , vol.273 , Issue.27 , pp. 16824-16827
    • Rezaie, A.R.1
  • 40
    • 0032549024 scopus 로고    scopus 로고
    • Regulation of extrinsic pathway factor Xa formation by tissue factor pathway inhibitor
    • Baugh RJ, Broze GJ Jr, Krishnaswamy S. Regulation of extrinsic pathway factor Xa formation by tissue factor pathway inhibitor. J Biol Chem. 1998;273(8):4378-4386.
    • (1998) J Biol Chem , vol.273 , Issue.8 , pp. 4378-4386
    • Baugh, R.J.1    Broze Jr., G.J.2    Krishnaswamy, S.3
  • 41
    • 0021673530 scopus 로고
    • Inhibition of prothrombinase complex by plasma proteinase inhibitors
    • Ellis V, Scully MF, Kakkar VV. Inhibition of prothrombinase complex by plasma proteinase inhibitors. Biochemistry. 1984;23(24):5582-5587.
    • (1984) Biochemistry , vol.23 , Issue.24 , pp. 5582-5587
    • Ellis, V.1    Scully, M.F.2    Kakkar, V.V.3
  • 42
    • 0035871772 scopus 로고    scopus 로고
    • Prothrombin protects factor Xa in the prothrombinase complex from inhibition by the heparin-antithrombin complex
    • Rezaie AR. Prothrombin protects factor Xa in the prothrombinase complex from inhibition by the heparin-antithrombin complex. Blood. 2001;97(8):2308- 2313.
    • (2001) Blood , vol.97 , Issue.8 , pp. 2308-2313
    • Rezaie, A.R.1
  • 43
    • 2642651894 scopus 로고    scopus 로고
    • Blood coagulation in hemophilia A and hemophilia C
    • Cawthern KM, van't Veer C, Lock JB, et al. Blood coagulation in hemophilia A and hemophilia C. Blood. 1998;91(12):4581-4592.
    • (1998) Blood , vol.91 , Issue.12 , pp. 4581-4592
    • Cawthern, K.M.1    Van't Veer, C.2    Lock, J.B.3
  • 44
    • 29244450161 scopus 로고    scopus 로고
    • Thrombin-activable factor X re-establishes an intrinsic amplification in tenase-deficient plasmas
    • Louvain-Quintard VB, Bianchini EP, Calmel-Tareau C, Tagzirt M, Le Bonniec BF. Thrombin-activable factor X re-establishes an intrinsic amplification in tenase-deficient plasmas. J Biol Chem. 2005;280(50):41352-41359.
    • (2005) J Biol Chem , vol.280 , Issue.50 , pp. 41352-41359
    • Louvain-Quintard, V.B.1    Bianchini, E.P.2    Calmel-Tareau, C.3    Tagzirt, M.4    Le Bonniec, B.F.5
  • 46
    • 0242494903 scopus 로고    scopus 로고
    • Improved hemostasis with superactive analogs of factor VIIa in a mouse model of hemophilia A
    • Tranholm M, Kristensen K, Kristensen AT, et al. Improved hemostasis with superactive analogs of factor VIIa in a mouse model of hemophilia A. Blood. 2003;102(10):3615-3620.
    • (2003) Blood , vol.102 , Issue.10 , pp. 3615-3620
    • Tranholm, M.1    Kristensen, K.2    Kristensen, A.T.3
  • 47
    • 0034059153 scopus 로고    scopus 로고
    • In vivo bypass of hemophilia A coagulation defect by factor XIIa implant
    • Ton-That TT, Doron D, Pollard BS, Bacher J, Pollard HB. In vivo bypass of hemophilia A coagulation defect by factor XIIa implant. Nat Biotechnol. 2000;18(3):289-295.
    • (2000) Nat Biotechnol , vol.18 , Issue.3 , pp. 289-295
    • Ton-That, T.T.1    Doron, D.2    Pollard, B.S.3    Bacher, J.4    Pollard, H.B.5
  • 48
    • 0028811109 scopus 로고
    • Procoagulant activity of reversibly acylated human factor Xa
    • Wolf DL, Lin PH, Hollenbach S et al. Procoagulant activity of reversibly acylated human factor Xa. Blood. 1995;86(11):4153-4157.
    • (1995) Blood , vol.86 , Issue.11 , pp. 4153-4157
    • Wolf, D.L.1    Lin, P.H.2    Hollenbach, S.3
  • 49
    • 0034923318 scopus 로고    scopus 로고
    • Protein Z-dependent regulation of coagulation
    • Broze GJ Jr. Protein Z-dependent regulation of coagulation. Thromb Haemost. 2001;86(1):8-13.
    • (2001) Thromb Haemost , vol.86 , Issue.1 , pp. 8-13
    • Broze Jr., G.J.1
  • 50
    • 0030695063 scopus 로고    scopus 로고
    • Platelet activity of high-dose factor VIIa is independent of tissue factor
    • Monroe DM, Hoffman M, Oliver JA, Roberts HR. Platelet activity of high-dose factor VIIa is independent of tissue factor. Br J Haematol. 1997;99(3):542-547.
    • (1997) Br J Haematol , vol.99 , Issue.3 , pp. 542-547
    • Monroe, D.M.1    Hoffman, M.2    Oliver, J.A.3    Roberts, H.R.4
  • 51
    • 0034651933 scopus 로고    scopus 로고
    • Inhibition of thrombin generation by the zymogen factor VII: Implications for the treatment of hemophilia A by factor VIIa
    • van 't Veer C, Golden NJ, Mann KG. Inhibition of thrombin generation by the zymogen factor VII: implications for the treatment of hemophilia A by factor VIIa. Blood. 2000;95(4):1330-1335.
    • (2000) Blood , vol.95 , Issue.4 , pp. 1330-1335
    • Van't Veer, C.1    Golden, N.J.2    Mann, K.G.3
  • 52
    • 0036464599 scopus 로고    scopus 로고
    • Mechanism of factor VIIa-dependent coagulation in hemophilia blood
    • DOI 10.1182/blood.V99.3.923
    • Butenas S, Brummel KE, Branda RF, Paradis SG, Mann KG. Mechanism of factor VIIa-dependent coagulation in hemophilia blood. Blood. 2002;99(3):923-930. (Pubitemid 34525554)
    • (2002) Blood , vol.99 , Issue.3 , pp. 923-930
    • Butenas, S.1    Brummel, K.E.2    Branda, R.F.3    Paradis, S.G.4    Mann, K.G.5


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