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Volumn 22, Issue , 2016, Pages 3-8

Rethinking events in the haemostatic process: role of factor V and TFPI

Author keywords

bleeding disorders; coagulation; factor V; factor Va; haemophilia; TFPI

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 5A; PROTEIN TFPIALPHA; TISSUE FACTOR PATHWAY INHIBITOR; UNCLASSIFIED DRUG; HEMOSTATIC AGENT; LIPOPROTEIN; LIPOPROTEIN-ASSOCIATED COAGULATION INHIBITOR; THROMBIN; THROMBOPLASTIN;

EID: 84978870374     PISSN: 13518216     EISSN: 13652516     Source Type: Journal    
DOI: 10.1111/hae.13004     Document Type: Review
Times cited : (26)

References (61)
  • 1
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann KG, Nesheim ME, Church WR, Haley P, Krishnaswamy S. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 1990; 76: 1–16.
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 2
    • 65349111124 scopus 로고    scopus 로고
    • Overview of inherited hemorrhagic disorders
    • In, Colman RW, Marder VJ, Clowes AW, Gerorge JN, Goldhaber SZ, eds., Philadelphia, Lippincott Williams & Wilkins
    • Roberts HR, Ma AD. Overview of inherited hemorrhagic disorders. In: Colman RW, Marder VJ, Clowes AW, Gerorge JN, Goldhaber SZ eds. Hemostasis and Thrombosis: Basic Principles and Clinical Practice. Philadelphia: Lippincott Williams & Wilkins, 2006: 877–85.
    • (2006) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 877-885
    • Roberts, H.R.1    Ma, A.D.2
  • 3
    • 0002733934 scopus 로고
    • The tissue factor pathway of coagulation: factor VII, tissue factor, and tissue factor pathway inhibitor
    • In, Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD, eds., New York, Churchill Livingstone
    • Broze GJ Jr. The tissue factor pathway of coagulation: factor VII, tissue factor, and tissue factor pathway inhibitor. In: Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD eds. Haemostasis and Thrombosis. New York: Churchill Livingstone, 1994: 349–77.
    • (1994) Haemostasis and Thrombosis , pp. 349-377
    • Broze, G.J.1
  • 4
    • 84952636616 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor: multiple anticoagulant activities for a single protein
    • Mast AE. Tissue factor pathway inhibitor: multiple anticoagulant activities for a single protein. Arterioscler Thromb Vasc Biol 2016; 36: 9–14.
    • (2016) Arterioscler Thromb Vasc Biol , vol.36 , pp. 9-14
    • Mast, A.E.1
  • 5
    • 84883236723 scopus 로고    scopus 로고
    • Parahemophilia: new insights into factor v deficiency
    • Thalji N, Camire RM. Parahemophilia: new insights into factor v deficiency. Semin Thromb Hemost 2013; 39: 607–12.
    • (2013) Semin Thromb Hemost , vol.39 , pp. 607-612
    • Thalji, N.1    Camire, R.M.2
  • 7
    • 0024996842 scopus 로고
    • Expression of tissue factor procoagullant activity: regulation by cystosolic calcium
    • Bach R, Rifkin DB. Expression of tissue factor procoagullant activity: regulation by cystosolic calcium. Proc Natl Acad Sci USA 1990; 87: 6995–9.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6995-6999
    • Bach, R.1    Rifkin, D.B.2
  • 8
    • 34548698444 scopus 로고    scopus 로고
    • Coagulation factor V and thrombophilia: background and mechanisms
    • Segers K, Dahlback B, Nicolaes GA. Coagulation factor V and thrombophilia: background and mechanisms. Thromb Haemost 2007; 98: 530–42.
    • (2007) Thromb Haemost , vol.98 , pp. 530-542
    • Segers, K.1    Dahlback, B.2    Nicolaes, G.A.3
  • 9
    • 84887103363 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor-alpha inhibits prothrombinase during the initiation of blood coagulation
    • Wood JP, Bunce MW, Maroney SA, Tracy PB, Camire RM, Mast AE. Tissue factor pathway inhibitor-alpha inhibits prothrombinase during the initiation of blood coagulation. Proc Natl Acad Sci USA 2013; 110: 17838–43.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 17838-17843
    • Wood, J.P.1    Bunce, M.W.2    Maroney, S.A.3    Tracy, P.B.4    Camire, R.M.5    Mast, A.E.6
  • 10
    • 77449128728 scopus 로고    scopus 로고
    • The molecular basis of factor V and VIII procofactor activation
    • Camire RM, Bos MHA. The molecular basis of factor V and VIII procofactor activation. J Thromb Haemost 2009; 7: 1951–61.
    • (2009) J Thromb Haemost , vol.7 , pp. 1951-1961
    • Camire, R.M.1    Bos, M.H.A.2
  • 12
    • 0018786088 scopus 로고
    • The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits and reconstitution of biological activity
    • Esmon CT. The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits and reconstitution of biological activity. J Biol Chem 1979; 254: 964–73.
    • (1979) J Biol Chem , vol.254 , pp. 964-973
    • Esmon, C.T.1
  • 13
    • 0018412614 scopus 로고
    • Thrombin-catalyzed activation of single chain bovine factor V
    • Nesheim ME, Mann KG. Thrombin-catalyzed activation of single chain bovine factor V. J Biol Chem 1979; 254: 1326–34.
    • (1979) J Biol Chem , vol.254 , pp. 1326-1334
    • Nesheim, M.E.1    Mann, K.G.2
  • 14
    • 0018909419 scopus 로고
    • Human coagulation factor V purification and thrombin-catalyzed activation
    • Dahlback B. Human coagulation factor V purification and thrombin-catalyzed activation. J Clin Invest 1980; 66: 583–91.
    • (1980) J Clin Invest , vol.66 , pp. 583-591
    • Dahlback, B.1
  • 15
    • 0019862464 scopus 로고
    • Purification and characterization of human coagulation factor V
    • Kane WH, Majerus PW. Purification and characterization of human coagulation factor V. J Biol Chem 1981; 256: 1002–7.
    • (1981) J Biol Chem , vol.256 , pp. 1002-1007
    • Kane, W.H.1    Majerus, P.W.2
  • 16
    • 0020320628 scopus 로고
    • Thrombin-catalyzed activation of human coagulation factor V
    • Suzuki K, Dahlback B, Stenflo J. Thrombin-catalyzed activation of human coagulation factor V. J Biol Chem 1982; 257: 6556–64.
    • (1982) J Biol Chem , vol.257 , pp. 6556-6564
    • Suzuki, K.1    Dahlback, B.2    Stenflo, J.3
  • 17
    • 0025139882 scopus 로고
    • Activation of human factor V by factor Xa and thrombin
    • Monkovic DD, Tracy PB. Activation of human factor V by factor Xa and thrombin. Biochemistry 1990; 29: 1118–28.
    • (1990) Biochemistry , vol.29 , pp. 1118-1128
    • Monkovic, D.D.1    Tracy, P.B.2
  • 18
    • 0021356149 scopus 로고
    • Characterization of factor V activation intermediates
    • Nesheim ME, Foster WB, Hewick R, Mann KG. Characterization of factor V activation intermediates. J Biol Chem 1984; 259: 3187–96.
    • (1984) J Biol Chem , vol.259 , pp. 3187-3196
    • Nesheim, M.E.1    Foster, W.B.2    Hewick, R.3    Mann, K.G.4
  • 19
    • 0023600774 scopus 로고
    • The regulation of human factor V by a neutrophil protease
    • Oates AM, Salem HH. The regulation of human factor V by a neutrophil protease. Blood 1987; 70: 846–51.
    • (1987) Blood , vol.70 , pp. 846-851
    • Oates, A.M.1    Salem, H.H.2
  • 20
    • 0023855464 scopus 로고
    • Factor V is activated and cleaved by platelet calpain: comparison with thrombin proteolysis
    • Bradford HN, Annamalai A, Doshi K, Colman RW. Factor V is activated and cleaved by platelet calpain: comparison with thrombin proteolysis. Blood 1988; 71: 388–94.
    • (1988) Blood , vol.71 , pp. 388-394
    • Bradford, H.N.1    Annamalai, A.2    Doshi, K.3    Colman, R.W.4
  • 21
    • 0024546279 scopus 로고
    • Activation/Inactivation of human factor V by plasmin
    • Lee CD, Mann KG. Activation/Inactivation of human factor V by plasmin. Blood 1989; 73: 185–90.
    • (1989) Blood , vol.73 , pp. 185-190
    • Lee, C.D.1    Mann, K.G.2
  • 23
    • 0026754715 scopus 로고
    • Activation of bovine factor V by an activator purified from the venom of Naja Naja Oxiana
    • Gerads I, Tans G, Yukelson LY, Zwaal RFA, Rosing J. Activation of bovine factor V by an activator purified from the venom of Naja Naja Oxiana. Toxicon 1992; 30: 1065–79.
    • (1992) Toxicon , vol.30 , pp. 1065-1079
    • Gerads, I.1    Tans, G.2    Yukelson, L.Y.3    Zwaal, R.F.A.4    Rosing, J.5
  • 26
    • 0028890305 scopus 로고
    • Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface
    • Allen DH, Tracy PB. Human coagulation factor V is activated to the functional cofactor by elastase and cathepsin G expressed at the monocyte surface. J Biol Chem 1995; 270: 1408–15.
    • (1995) J Biol Chem , vol.270 , pp. 1408-1415
    • Allen, D.H.1    Tracy, P.B.2
  • 27
    • 0030787645 scopus 로고    scopus 로고
    • Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V
    • Samis JA, Garrett M, Manuel RP, Nesheim ME, Giles AR. Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V. Blood 1997; 90: 1065–74.
    • (1997) Blood , vol.90 , pp. 1065-1074
    • Samis, J.A.1    Garrett, M.2    Manuel, R.P.3    Nesheim, M.E.4    Giles, A.R.5
  • 28
    • 0032566343 scopus 로고    scopus 로고
    • Proteolysis of factor V by cathepsin G and elastase indicates that cleavage at Arg 1545 optimizes cofactor function by facilitating factor Xa binding
    • Camire RM, Kalafatis M, Tracy PB. Proteolysis of factor V by cathepsin G and elastase indicates that cleavage at Arg 1545 optimizes cofactor function by facilitating factor Xa binding. Biochemistry 1998; 37: 11896–906.
    • (1998) Biochemistry , vol.37 , pp. 11896-11906
    • Camire, R.M.1    Kalafatis, M.2    Tracy, P.B.3
  • 30
    • 0042858164 scopus 로고    scopus 로고
    • Structural requirements for expression of factor Va activity
    • Kalafatis M, Beck DO, Mann KG. Structural requirements for expression of factor Va activity. J Biol Chem 2004; 278: 33550–61.
    • (2004) J Biol Chem , vol.278 , pp. 33550-33561
    • Kalafatis, M.1    Beck, D.O.2    Mann, K.G.3
  • 31
    • 0028043332 scopus 로고
    • Role of the B domain for factor VIII and factor V expression and function
    • Pittman DD, Marquette KA, Kaufman RJ. Role of the B domain for factor VIII and factor V expression and function. Blood 1994; 84: 4214–25.
    • (1994) Blood , vol.84 , pp. 4214-4225
    • Pittman, D.D.1    Marquette, K.A.2    Kaufman, R.J.3
  • 32
    • 0028784206 scopus 로고
    • The factor V B-domain provides two functions to facilitate thrombin cleavage and release of the light chain
    • Marquette KA, Pittman DD, Kaufman RJ. The factor V B-domain provides two functions to facilitate thrombin cleavage and release of the light chain. Blood 1995; 86: 3026–34.
    • (1995) Blood , vol.86 , pp. 3026-3034
    • Marquette, K.A.1    Pittman, D.D.2    Kaufman, R.J.3
  • 34
    • 0030805611 scopus 로고    scopus 로고
    • Cleavage requirements for activation of factor V by factor Xa
    • Thorelli E, Kaufman RJ, Dahlback B. Cleavage requirements for activation of factor V by factor Xa. Eur J Biochem 1997; 247: 12–20.
    • (1997) Eur J Biochem , vol.247 , pp. 12-20
    • Thorelli, E.1    Kaufman, R.J.2    Dahlback, B.3
  • 35
    • 0037064117 scopus 로고    scopus 로고
    • Thrombin-mediated proteolysis of factor V resulting in gradual B-domain release and exposure of the factor Xa-binding site
    • Steen M, Dahlback B. Thrombin-mediated proteolysis of factor V resulting in gradual B-domain release and exposure of the factor Xa-binding site. J Biol Chem 2002; 277: 38424–30.
    • (2002) J Biol Chem , vol.277 , pp. 38424-38430
    • Steen, M.1    Dahlback, B.2
  • 36
    • 0035742922 scopus 로고    scopus 로고
    • Proteases from Vipera lebetina venom affecting coagulation and fibrinolysis
    • Siigur J, Aaspollu A, Tonismagi K, Trummal K, Samel M, Vija H et al. Proteases from Vipera lebetina venom affecting coagulation and fibrinolysis. Haemostasis 2001; 31: 123–32.
    • (2001) Haemostasis , vol.31 , pp. 123-132
    • Siigur, J.1    Aaspollu, A.2    Tonismagi, K.3    Trummal, K.4    Samel, M.5    Vija, H.6
  • 37
    • 33748447516 scopus 로고    scopus 로고
    • Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina
    • Segers K, Rosing J, Nicolaes GA. Structural models of the snake venom factor V activators from Daboia russelli and Daboia lebetina. Proteins 2006; 64: 968–84.
    • (2006) Proteins , vol.64 , pp. 968-984
    • Segers, K.1    Rosing, J.2    Nicolaes, G.A.3
  • 38
    • 33646839132 scopus 로고    scopus 로고
    • Factor VIII structure and function
    • Fay PJ. Factor VIII structure and function. Int J Hematol 2006; 83: 103–8.
    • (2006) Int J Hematol , vol.83 , pp. 103-108
    • Fay, P.J.1
  • 39
    • 0025289454 scopus 로고
    • Expression and characterization of recombinant human factor V and a mutant lacking a major portion of the connecting region
    • Kane WH, Devore-Carter D, Ortel TL. Expression and characterization of recombinant human factor V and a mutant lacking a major portion of the connecting region. Biochemistry 1990; 29: 6762–8.
    • (1990) Biochemistry , vol.29 , pp. 6762-6768
    • Kane, W.H.1    Devore-Carter, D.2    Ortel, T.L.3
  • 40
    • 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: 21643–50.
    • (2004) J Biol Chem , vol.279 , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 41
    • 34447513246 scopus 로고    scopus 로고
    • Inhibitory sequences within the B-domain stabilize circulating factor V in an inactive state
    • Zhu H, Toso R, Camire RM. Inhibitory sequences within the B-domain stabilize circulating factor V in an inactive state. J Biol Chem 2007; 282: 15033–9.
    • (2007) J Biol Chem , vol.282 , pp. 15033-15039
    • Zhu, H.1    Toso, R.2    Camire, R.M.3
  • 42
    • 84864386285 scopus 로고    scopus 로고
    • A bipartite autoinhibitory region within the B-domain suppresses function in factor V
    • Bos MH, Camire RM. A bipartite autoinhibitory region within the B-domain suppresses function in factor V. J Biol Chem 2012; 287: 26342–51.
    • (2012) J Biol Chem , vol.287 , pp. 26342-26351
    • Bos, M.H.1    Camire, R.M.2
  • 43
    • 84886881353 scopus 로고    scopus 로고
    • Restoring the procofactor state of factor Va-like variants by complementation with B-domain peptides
    • Bunce MW, Bos MH, Krishnaswamy S, Camire RM. Restoring the procofactor state of factor Va-like variants by complementation with B-domain peptides. J Biol Chem 2013; 288: 30151–60.
    • (2013) J Biol Chem , vol.288 , pp. 30151-30160
    • Bunce, M.W.1    Bos, M.H.2    Krishnaswamy, S.3    Camire, R.M.4
  • 44
    • 0037220079 scopus 로고    scopus 로고
    • Factor V: a combination of Dr. Jekyll and Mr. Hyde
    • Mann KG, Kalafatis M. Factor V: a combination of Dr. Jekyll and Mr. Hyde. Blood 2002; 101: 20–30.
    • (2002) Blood , vol.101 , pp. 20-30
    • Mann, K.G.1    Kalafatis, M.2
  • 45
    • 73349141742 scopus 로고    scopus 로고
    • Factor V Leiden and activated protein C resistance
    • Segers O, Castoldi E. Factor V Leiden and activated protein C resistance. Adv Clin Chem 2009; 49: 121–57.
    • (2009) Adv Clin Chem , vol.49 , pp. 121-157
    • Segers, O.1    Castoldi, E.2
  • 46
    • 0027446268 scopus 로고
    • Familial thrombophilia due to a previously unrecognized mechanism by poor anticoagulant response to activated protein C: prediction of a cofactor to activated protein C
    • Dahlback B, Carlsson M, Svensson PJ. Familial thrombophilia due to a previously unrecognized mechanism by poor anticoagulant response to activated protein C: prediction of a cofactor to activated protein C. Proc Natl Acad Sci USA 1993; 90: 1004–8.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1004-1008
    • Dahlback, B.1    Carlsson, M.2    Svensson, P.J.3
  • 48
    • 0017842254 scopus 로고
    • The inhibition of activated bovine coagulation factors X and VII by antithrombin III
    • Jesty J. The inhibition of activated bovine coagulation factors X and VII by antithrombin III. Arch Biochem Biophys 1978; 185: 165–73.
    • (1978) Arch Biochem Biophys , vol.185 , pp. 165-173
    • Jesty, J.1
  • 49
    • 84860303349 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor: structure-function
    • Broze GJ Jr, Girard TJ. Tissue factor pathway inhibitor: structure-function. Front Biosci 2012; 17: 262–80.
    • (2012) Front Biosci , vol.17 , pp. 262-280
    • Broze, G.J.1    Girard, T.J.2
  • 50
    • 84903210055 scopus 로고    scopus 로고
    • Biology of tissue factor pathway inhibitor
    • Wood JP, Ellery PE, Maroney SA, Mast AE. Biology of tissue factor pathway inhibitor. Blood 2014; 123: 2934–43.
    • (2014) Blood , vol.123 , pp. 2934-2943
    • Wood, J.P.1    Ellery, P.E.2    Maroney, S.A.3    Mast, A.E.4
  • 51
    • 0030039385 scopus 로고    scopus 로고
    • Physiological concentrations of tissue factor pathway inhibitor do not inhibit prothrombinase
    • Mast AE, Broze GJ Jr. Physiological concentrations of tissue factor pathway inhibitor do not inhibit prothrombinase. Blood 1996; 87: 1845–50.
    • (1996) Blood , vol.87 , pp. 1845-1850
    • Mast, A.E.1    Broze, G.J.2
  • 52
    • 80053100269 scopus 로고    scopus 로고
    • Alternatively spliced tissue factor pathway inhibitor: functional implications
    • Mast AE. Alternatively spliced tissue factor pathway inhibitor: functional implications. Front Biosci (Schol Ed) 2011; 3: 1457–62.
    • (2011) Front Biosci (Schol Ed) , vol.3 , pp. 1457-1462
    • Mast, A.E.1
  • 53
    • 77949321986 scopus 로고    scopus 로고
    • Residual platelet factor V ensures thrombin generation in patients with severe congenital factor V deficiency and mild bleeding symptoms
    • Duckers C, Simioni P, Spiezia L, Radu C, Dabrilli P, Gavasso S et al. Residual platelet factor V ensures thrombin generation in patients with severe congenital factor V deficiency and mild bleeding symptoms. Blood 2009; 115: 879–86.
    • (2009) Blood , vol.115 , pp. 879-886
    • Duckers, C.1    Simioni, P.2    Spiezia, L.3    Radu, C.4    Dabrilli, P.5    Gavasso, S.6
  • 54
    • 84865776161 scopus 로고    scopus 로고
    • The C-terminus of tissue factor pathway inhibitor alpha is required for its interaction with factors V and Va
    • Ndonwi M, Girard TJ, Broze GJ Jr. The C-terminus of tissue factor pathway inhibitor alpha is required for its interaction with factors V and Va. J Thromb Haemost 2012; 10: 1944–6.
    • (2012) J Thromb Haemost , vol.10 , pp. 1944-1946
    • Ndonwi, M.1    Girard, T.J.2    Broze, G.J.3
  • 55
    • 84880329348 scopus 로고    scopus 로고
    • Factor Xa activation of factor V is of paramount importance in initiating the coagulation system: lessons from a tick salivary protein
    • Schuijt TJ, Bakhtiari K, Daffre S, Deponte K, Wielders SJ, Marquart JA et al. Factor Xa activation of factor V is of paramount importance in initiating the coagulation system: lessons from a tick salivary protein. Circulation 2013; 128: 254–66.
    • (2013) Circulation , vol.128 , pp. 254-266
    • Schuijt, T.J.1    Bakhtiari, K.2    Daffre, S.3    Deponte, K.4    Wielders, S.J.5    Marquart, J.A.6
  • 56
    • 84931385857 scopus 로고    scopus 로고
    • New insights into the biology of tissue factor pathway inhibitor
    • Maroney SA, Mast AE. New insights into the biology of tissue factor pathway inhibitor. J Thromb Haemost 2015; 13(Suppl 1): S200–7.
    • (2015) J Thromb Haemost , vol.13 , pp. S200-S207
    • Maroney, S.A.1    Mast, A.E.2
  • 58
    • 84931858449 scopus 로고    scopus 로고
    • A novel mutation in the F5 gene (factor V Amsterdam) associated with bleeding independent of factor V procoagulant function
    • Cunha ML, Bakhtiari K, Peter J, Marquart JA, Meijers JC, Middeldorp S. A novel mutation in the F5 gene (factor V Amsterdam) associated with bleeding independent of factor V procoagulant function. Blood 2015; 125: 1822–5.
    • (2015) Blood , vol.125 , pp. 1822-1825
    • Cunha, M.L.1    Bakhtiari, K.2    Peter, J.3    Marquart, J.A.4    Meijers, J.C.5    Middeldorp, S.6
  • 59
    • 85006216296 scopus 로고    scopus 로고
    • Emerging and future therapies for hemophilia
    • Carr ME, Tortella BJ. Emerging and future therapies for hemophilia. J Blood Med 2015; 6: 245–55.
    • (2015) J Blood Med , vol.6 , pp. 245-255
    • Carr, M.E.1    Tortella, B.J.2
  • 60
    • 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, Cooley B, Qin J, Racie T et al. An RNAi therapeutic targeting antithrombin to rebalance the coagulation system and promote hemostasis in hemophilia. Nat Med 2015; 21: 492–7.
    • (2015) Nat Med , vol.21 , pp. 492-497
    • Sehgal, A.1    Barros, S.2    Ivanciu, L.3    Cooley, B.4    Qin, J.5    Racie, T.6
  • 61
    • 84899567922 scopus 로고    scopus 로고
    • Novel products for haemostasis - current status
    • Oldenburg J, Albert T. Novel products for haemostasis - current status. Haemophilia 2014; 20(Suppl 4): 23–8.
    • (2014) Haemophilia , vol.20 , pp. 23-28
    • Oldenburg, J.1    Albert, T.2


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