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Volumn 149, Issue 1 SUPPL., 2005, Pages

The challenge of regulating anticoagulant drugs: Focus on warfarin

Author keywords

[No Author keywords available]

Indexed keywords

ANTICOAGULANT AGENT; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 7; BLOOD CLOTTING FACTOR 9; FATTY ACID BINDING PROTEIN; PROTEIN C; PROTEIN S; PROTHROMBIN; THROMBIN; VITAMIN K GROUP; WARFARIN; XIMELAGATRAN;

EID: 10944261270     PISSN: 00028703     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ahj.2004.10.021     Document Type: Article
Times cited : (18)

References (37)
  • 1
    • 0006698429 scopus 로고
    • Hemmorrhages in chicks reared on artificial diets. A new deficiency disease
    • H. Dam Hemmorrhages in chicks reared on artificial diets. A new deficiency disease Nature (London) 133 1934 909 910
    • (1934) Nature (London) , vol.133 , pp. 909-910
    • Dam, H.1
  • 2
    • 0000638825 scopus 로고
    • Antihaemorrhagic vitamin of chick
    • H. Dam Antihaemorrhagic vitamin of chick Biochem. J. 29 1935 1273 1285
    • (1935) Biochem. J. , vol.29 , pp. 1273-1285
    • Dam, H.1
  • 3
    • 0000593528 scopus 로고
    • Studies on the hemorrhagic sweet clover disease. IV. The isolation and crystallization of the hemorrhagic agent
    • H.A. Cambell, and K.P. Link Studies on the hemorrhagic sweet clover disease. IV. The isolation and crystallization of the hemorrhagic agent J. Biol. Chem. 138 1941 21 33
    • (1941) J. Biol. Chem. , vol.138 , pp. 21-33
    • Cambell, H.A.1    Link, K.P.2
  • 4
    • 0000175224 scopus 로고
    • A preparation from spoiled sweet clover [3,3′-methylene-bis-(4- hydroxycoumarin)] which prolongs coagulation and prothrombin time of the blood: Preliminary report of experimental and clinical studies
    • H.R. Butt, E.V. Allen, and J.L. Bollman A preparation from spoiled sweet clover [3,3′-methylene-bis-(4-hydroxycoumarin)] which prolongs coagulation and prothrombin time of the blood: preliminary report of experimental and clinical studies Proc. Staff Meet. Mayo Clin. 16 1941 388 395
    • (1941) Proc. Staff Meet. Mayo Clin. , vol.16 , pp. 388-395
    • Butt, H.R.1    Allen, E.V.2    Bollman, J.L.3
  • 5
    • 0002008477 scopus 로고
    • The prothrombin time in haemophilia and in obstructive jaundice
    • A.J. Quick The prothrombin time in haemophilia and in obstructive jaundice J. Biol. Chem. 109 1935 73 74
    • (1935) J. Biol. Chem. , vol.109 , pp. 73-74
    • Quick, A.J.1
  • 6
    • 0016264341 scopus 로고
    • Vitamin K and the biosynthesis of prothrombin. IV. Isolation of peptides containing prosthetic groups from normal prothrombin and the corresponding peptides from dicoumarol-induced prothrombin
    • J. Stenflo Vitamin K and the biosynthesis of prothrombin. IV. Isolation of peptides containing prosthetic groups from normal prothrombin and the corresponding peptides from dicoumarol-induced prothrombin J. Biol. Chem. 249 1974 5527 5535
    • (1974) J. Biol. Chem. , vol.249 , pp. 5527-5535
    • Stenflo, J.1
  • 7
    • 0141707881 scopus 로고    scopus 로고
    • Thrombin formation
    • K.G. Mann Thrombin formation Chest 124 2003 4S 10S
    • (2003) Chest , vol.124
    • Mann, K.G.1
  • 10
    • 0041819513 scopus 로고    scopus 로고
    • Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins
    • M. Huang, A.C. Rigby, and X. Morelli Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins Nat. Struct. Biol. 10 2003 751 756
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 751-756
    • Huang, M.1    Rigby, A.C.2    Morelli, X.3
  • 11
    • 0023924910 scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complexes
    • K.G. Mann, R.J. Jenny, and S. Krishnaswamy Cofactor proteins in the assembly and expression of blood clotting enzyme complexes Annu. Rev. Biochem. 57 1988 915 956
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 12
    • 0023851758 scopus 로고
    • Tissue factor and hemostasis
    • Y. Nemerson Tissue factor and hemostasis Blood 71 1988 1 8
    • (1988) Blood , vol.71 , pp. 1-8
    • Nemerson, Y.1
  • 13
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • K.G. Mann, M.E. Nesheim, and W.R. Church Surface-dependent reactions of the vitamin K-dependent enzyme complexes Blood 76 1990 1 16
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3
  • 14
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • C.T. Esmon The roles of protein C and thrombomodulin in the regulation of blood coagulation J. Biol. Chem. 264 1989 4743 4746
    • (1989) J. Biol. Chem. , vol.264 , pp. 4743-4746
    • Esmon, C.T.1
  • 15
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • E.W. Davie, and O.D. Ratnoff Waterfall sequence for intrinsic blood clotting Science 145 1964 1310 1312
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 16
    • 37049044629 scopus 로고
    • An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier
    • R.G. McFarlane An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier Nature 202 1964 498 499
    • (1964) Nature , vol.202 , pp. 498-499
    • McFarlane, R.G.1
  • 17
    • 0029082791 scopus 로고
    • Tissue factor pathway inhibitor
    • G.J. Broze Jr. Tissue factor pathway inhibitor Thromb. Haemost. 74 1995 90 93
    • (1995) Thromb. Haemost. , vol.74 , pp. 90-93
    • Broze Jr., G.J.1
  • 20
    • 0036660207 scopus 로고    scopus 로고
    • Thrombin functions during tissue factor-induced blood coagulation
    • K.E. Brummel, S.G. Paradis, and S. Butenas Thrombin functions during tissue factor-induced blood coagulation Blood 100 2002 148 152
    • (2002) Blood , vol.100 , pp. 148-152
    • Brummel, K.E.1    Paradis, S.G.2    Butenas, S.3
  • 22
    • 0027130012 scopus 로고
    • International standardization of laboratory control of oral anticoagulant therapy: A survey of thromboplastin reagents used for prothrombin time testing
    • A.M. van den Besselaar International standardization of laboratory control of oral anticoagulant therapy: a survey of thromboplastin reagents used for prothrombin time testing J. Heart Valve Dis. 2 1993 42 52
    • (1993) J. Heart Valve Dis. , vol.2 , pp. 42-52
    • Van Den Besselaar, A.M.1
  • 23
    • 0033761482 scopus 로고    scopus 로고
    • Enhanced standardization of the International Normalized Ratio through the use of plasma calibrants: A concise review
    • D.M. Adcock, and S. Duff Enhanced standardization of the International Normalized Ratio through the use of plasma calibrants: a concise review Blood Coagul. Fibrinolysis 11 2000 583 590
    • (2000) Blood Coagul. Fibrinolysis , vol.11 , pp. 583-590
    • Adcock, D.M.1    Duff, S.2
  • 24
    • 1842285734 scopus 로고
    • Isolation of cDNA clones coding for human tissue factor: Primary structure of the protein and cDNA
    • E.K. Spicer, R. Horton, and L. Bloem Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA Proc. Natl. Acad. Sci. USA 84 1987 5148 5152
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5148-5152
    • Spicer, E.K.1    Horton, R.2    Bloem, L.3
  • 25
    • 0025891262 scopus 로고
    • High level expression of recombinant human tissue factor in Chinese hamster ovary cells as a human thromboplastin
    • A. Rehemtulla, M. Pepe, and T.S. Edgington High level expression of recombinant human tissue factor in Chinese hamster ovary cells as a human thromboplastin Thromb. Haemost. 65 1991 521 527
    • (1991) Thromb. Haemost. , vol.65 , pp. 521-527
    • Rehemtulla, A.1    Pepe, M.2    Edgington, T.S.3
  • 26
    • 2642651894 scopus 로고    scopus 로고
    • Blood coagulation in hemophilia a and hemophilia C
    • K.M. Cawthern, C. van't Veer, and J.B. Lock Blood coagulation in hemophilia A and hemophilia C Blood 91 1998 4581 4592
    • (1998) Blood , vol.91 , pp. 4581-4592
    • Cawthern, K.M.1    Van'T Veer, C.2    Lock, J.B.3
  • 27
    • 0036800809 scopus 로고    scopus 로고
    • Hirudin as alternative anticoagulant: A historical review
    • F. Markwardt Hirudin as alternative anticoagulant: a historical review Semin. Thromb. Hemost. 28 2002 405 414
    • (2002) Semin. Thromb. Hemost. , vol.28 , pp. 405-414
    • Markwardt, F.1
  • 28
    • 2442509800 scopus 로고    scopus 로고
    • Predicting the pharmacology of thrombin inhibitors
    • T.E. Adams, S.J. Everse, and K.G. Mann Predicting the pharmacology of thrombin inhibitors J. Thromb. Haemost. 1 2003 1024 1027
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1024-1027
    • Adams, T.E.1    Everse, S.J.2    Mann, K.G.3
  • 29
    • 0025346345 scopus 로고
    • Design and characterization of hirulogs: A novel class of bivalent peptide inhibitors of thrombin
    • J.M. Maraganore, P. Bourdon, and J. Jablonski Design and characterization of hirulogs: a novel class of bivalent peptide inhibitors of thrombin Biochemistry 29 1990 7095 7101
    • (1990) Biochemistry , vol.29 , pp. 7095-7101
    • Maraganore, J.M.1    Bourdon, P.2    Jablonski, J.3
  • 30
    • 0037453968 scopus 로고    scopus 로고
    • Bivalirudin and provisional glycoprotein IIb/IIIa blockade compared with heparin and planned glycoprotein IIb/IIIa blockade during percutaneous coronary intervention: REPLACE-2 randomized trial
    • A.M. Lincoff, J.A. Bittl, and R.A. Harrington Bivalirudin and provisional glycoprotein IIb/IIIa blockade compared with heparin and planned glycoprotein IIb/IIIa blockade during percutaneous coronary intervention: REPLACE-2 randomized trial JAMA 289 2003 853 863
    • (2003) JAMA , vol.289 , pp. 853-863
    • Lincoff, A.M.1    Bittl, J.A.2    Harrington, R.A.3
  • 31
    • 0037454036 scopus 로고    scopus 로고
    • Effects of ximelagatran, an oral direct thrombin inhibitor, r-hirudin and enoxaparin on thrombin generation and platelet activation in healthy male subjects
    • T.C. Sarich, M. Wolzt, and U.G. Eriksson Effects of ximelagatran, an oral direct thrombin inhibitor, r-hirudin and enoxaparin on thrombin generation and platelet activation in healthy male subjects J. Am. Coll. Cardiol. 41 2003 557 564
    • (2003) J. Am. Coll. Cardiol. , vol.41 , pp. 557-564
    • Sarich, T.C.1    Wolzt, M.2    Eriksson, U.G.3
  • 32
    • 0037108825 scopus 로고    scopus 로고
    • Ximelagatran versus warfarin for the prevention of venous thromboembolism after total knee arthroplasty. A randomized, double-blind trial
    • C.W. Francis, B.L. Davidson, and S.D. Berkowitz Ximelagatran versus warfarin for the prevention of venous thromboembolism after total knee arthroplasty. A randomized, double-blind trial Ann. Intern. Med. 137 2002 648 655
    • (2002) Ann. Intern. Med. , vol.137 , pp. 648-655
    • Francis, C.W.1    Davidson, B.L.2    Berkowitz, S.D.3
  • 33
    • 0141862287 scopus 로고    scopus 로고
    • Recombinant nematode anticoagulant protein c2 and other inhibitors targeting blood coagulation factor VIIa/tissue factor
    • A.Y. Lee, and G.P. Vlasuk Recombinant nematode anticoagulant protein c2 and other inhibitors targeting blood coagulation factor VIIa/tissue factor J. Intern. Med. 254 2003 313 321
    • (2003) J. Intern. Med. , vol.254 , pp. 313-321
    • Lee, A.Y.1    Vlasuk, G.P.2
  • 34
    • 0032701594 scopus 로고    scopus 로고
    • An inhibitory anti-factor IX antibody effectively reduces thrombus formation in a rat model of venous thrombosis
    • G.Z. Feuerstein, J.R. Toomey, and R. Valocik An inhibitory anti-factor IX antibody effectively reduces thrombus formation in a rat model of venous thrombosis Thromb. Haemost. 82 1999 1443 1445
    • (1999) Thromb. Haemost. , vol.82 , pp. 1443-1445
    • Feuerstein, G.Z.1    Toomey, J.R.2    Valocik, R.3
  • 35
    • 3543106257 scopus 로고    scopus 로고
    • Fibrin-targeted direct factor Xa inhibition: Construction and characterization of a recombinant factor Xa inhibitor composed of an anti-fibrin single-chain antibody and tick anticoagulant peptide
    • C.E. Hagemeyer, I. Tomic, and P. Jaminet Fibrin-targeted direct factor Xa inhibition: construction and characterization of a recombinant factor Xa inhibitor composed of an anti-fibrin single-chain antibody and tick anticoagulant peptide Thromb. Haemost. 92 2004 47 53
    • (2004) Thromb. Haemost. , vol.92 , pp. 47-53
    • Hagemeyer, C.E.1    Tomic, I.2    Jaminet, P.3
  • 36
    • 2942733232 scopus 로고    scopus 로고
    • Fondaparinux: A new synthetic and selective inhibitor of Factor Xa
    • K.A. Bauer Fondaparinux: a new synthetic and selective inhibitor of Factor Xa Best Pract. Res. Clin. Haematol. 17 2004 89 104
    • (2004) Best Pract. Res. Clin. Haematol. , vol.17 , pp. 89-104
    • Bauer, K.A.1
  • 37
    • 0031030267 scopus 로고    scopus 로고
    • Selective inhibition of the prothrombinase complex: Factor Va alters macromolecular recognition of a tick anticoagulant peptide mutant by factor Xa
    • A. Betz, G.P. Vlasuk, and P.W. Bergum Selective inhibition of the prothrombinase complex: factor Va alters macromolecular recognition of a tick anticoagulant peptide mutant by factor Xa Biochemistry 36 1997 181 191
    • (1997) Biochemistry , vol.36 , pp. 181-191
    • Betz, A.1    Vlasuk, G.P.2    Bergum, P.W.3


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