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Volumn 2, Issue 3, 2004, Pages 199-228

Biochemical strategies to anticoagulation: A comparative overview

Author keywords

Anticoagulant; FVII; FX; Hypercoagulability; Inflammation; Thrombin; Thrombosis; Tissue factor

Indexed keywords

2 [4 [(1 ACETIMIDOYL 3 PYRROLIDINYL)OXY]PHENYL] 3 (7 AMIDINO 2 NAPHTHYL)PROPIONIC ACID; 4H 3,1 BENZOXAZIN 4 ONE DERIVATIVE; [N [4 [(1 ACETIMIDOYL 4 PIPERIDYL)OXY]PHENYL] N [(7 AMIDINO 2 NAPHTHYL)METHYL]SULFAMOYL]ACETIC ACID; [N [4 [(1 ACETIMIDOYL 4 PIPERIDYL)OXY]PHENYL] N [(7 AMIDINO 2 NAPHTHYL)METHYL]SULFAMOYL]ACETIC ACID METHANESULFONATE; ACTIVATED PROTEIN C; ANTICOAGULANT AGENT; ANTITHROMBIN; APOLIPOPROTEIN B100; BEMIPARIN; BLOOD CLOTTING FACTOR 7; BLOOD CLOTTING FACTOR 7A INHIBITOR; BOTHROJARACIN; CEDARLANE; CONCANAVALIN A; DEXTRAN SULFATE; DX 9065 A; ENOXAPARIN; HEPARIN; HEPARIN COFACTOR II; LIPOPROTEIN; MARCKS PROTEIN; N [2 (5 AMIDINO 2 HYDROXYPHENOXY) 3,5 DIFLUORO 6 [3 (1 METHYL 1H 2 IMIDAZOLIN 2 YL)PHENOXY] 4 PYRIDINYL] N METHYLGLYCINE; PROTEIN S; REVIPARIN; SERINE PROTEINASE INHIBITOR; SPHINGOSINE; THROMBIN INHIBITOR; THROMBOMODULIN; THROMBOPLASTIN; TISSUE FACTOR PATHWAY INHIBITOR; UNINDEXED DRUG; WARFARIN;

EID: 3042696879     PISSN: 15701611     EISSN: None     Source Type: Journal    
DOI: 10.2174/1570161043385673     Document Type: Review
Times cited : (14)

References (506)
  • 1
    • 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; 46: 103-12.
    • (1995) Annu. Rev. Med. , vol.46 , pp. 103-112
    • Broze Jr., G.J.1
  • 2
    • 0030070996 scopus 로고    scopus 로고
    • Cell biology of tissue factor, the principal indicator of blood coagulation
    • Camerer E, Kolsto AB, Prydz H. Cell biology of tissue factor, the principal indicator of blood coagulation. Thromb Res 1996; 81: 1-41.
    • (1996) Thromb. Res. , vol.81 , pp. 1-41
    • Camerer, E.1    Kolsto, A.B.2    Prydz, H.3
  • 3
    • 0028235662 scopus 로고
    • Structural biology of tissue factor, the initiator of thrombogenesis in vivo
    • Ruf W, Edgington TS. Structural biology of tissue factor, the initiator of thrombogenesis in vivo. FASEB J 1994; 8: 385-90.
    • (1994) FASEB J. , vol.8 , pp. 385-390
    • Ruf, W.1    Edgington, T.S.2
  • 4
    • 0035992707 scopus 로고    scopus 로고
    • Improving the safety profile of Warfarin
    • Chai SJ, Macik BG. Improving the safety profile of Warfarin. Semin Hematol 2002; 39: 179-186.
    • (2002) Semin. Hematol. , vol.39 , pp. 179-186
    • Chai, S.J.1    Macik, B.G.2
  • 5
    • 0034919239 scopus 로고    scopus 로고
    • Heparins and venous thromboembolism: Current practice and future directions
    • Prandoni P. Heparins and venous thromboembolism: current practice and future directions. Thromb Haemost 2001; 86: 488-498.
    • (2001) Thromb. Haemost. , vol.86 , pp. 488-498
    • Prandoni, P.1
  • 6
    • 0030858230 scopus 로고    scopus 로고
    • Low-molecular-weight-heparins
    • Weitz JI. Low-molecular-weight-heparins. N Engl J Med 1997; 337: 688-98.
    • (1997) N. Engl. J. Med. , vol.337 , pp. 688-698
    • Weitz, J.I.1
  • 7
    • 0035169891 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor: An update of potential implications in the treatment of cardiovascular disorders
    • Kaiser B, Hoppensteadt DA, Fareed J. Tissue factor pathway inhibitor: an update of potential implications in the treatment of cardiovascular disorders. Expert Opin Investig Drug 2001; 10: 1925-1935.
    • (2001) Expert Opin. Investig. Drug , vol.10 , pp. 1925-1935
    • Kaiser, B.1    Hoppensteadt, D.A.2    Fareed, J.3
  • 8
    • 0034925134 scopus 로고    scopus 로고
    • Protein C anticoagulant pathway and its role in controlling microvascular thrombosis and inflammation
    • Esmon CT. Protein C anticoagulant pathway and its role in controlling microvascular thrombosis and inflammation. Crit Care Med 2001; 29: S48-S51.
    • (2001) Crit. Care Med. , vol.29
    • Esmon, C.T.1
  • 9
    • 0035992710 scopus 로고    scopus 로고
    • Activated protein C: Potential therapy for severe sepsis, thromosis and stroke
    • Griffin JH, Zlokovic B, Fernandez JA. Activated protein C: potential therapy for severe sepsis, thromosis and stroke. Semin Hematol 2002; 39: 197-205.
    • (2002) Semin. Hematol. , vol.39 , pp. 197-205
    • Griffin, J.H.1    Zlokovic, B.2    Fernandez, J.A.3
  • 11
  • 12
    • 0036588776 scopus 로고    scopus 로고
    • Synthetic direct and indirect factor Xa inhibitor
    • Samama MM. Synthetic direct and indirect factor Xa inhibitor. Thromb Res 2002; 106: V267-73.
    • (2002) Thromb. Res. , vol.106
    • Samama, M.M.1
  • 13
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie EW, Fujikawa K, Kisiel W. The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 1991; 30: 10363-70.
    • (1991) Biochemistry , vol.30 , pp. 10363-10370
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 15
    • 0025355427 scopus 로고
    • Synthesis, purification and characterization of an Arg 152-Glu site-directed mutant of recombinant human blood clotting factor VII
    • Wildgoose P, Berkner KL, Kisiel W. Synthesis, purification and characterization of an Arg 152-Glu site-directed mutant of recombinant human blood clotting factor VII. Biochemistry 1990; 29: 3413-20.
    • (1990) Biochemistry , vol.29 , pp. 3413-3420
    • Wildgoose, P.1    Berkner, K.L.2    Kisiel, W.3
  • 16
    • 0034468725 scopus 로고    scopus 로고
    • Activation of Factor IX by factor XIa
    • Gailani D. Activation of Factor IX by factor XIa. Trends Cardiovasc Med 2000; 10: 198-204.
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 198-204
    • Gailani, D.1
  • 18
    • 0033456269 scopus 로고    scopus 로고
    • Compound 48/80 suppresses monocytic tissue factor-initiated extrinsic blood coagulation induced by bacetrial endotoxin
    • Chu AJ, Raphael UO, Prasad JK, Beydoun S, Ramos N. II. Compound 48/80 suppresses monocytic tissue factor-initiated extrinsic blood coagulation induced by bacetrial endotoxin. J Surg Res 1999; 87: 252-7.
    • (1999) J. Surg. Res. , vol.87 , pp. 252-257
    • Chu, A.J.1    Raphael, U.O.2    Prasad, J.K.3    Beydoun, S.4    Ramos II, N.5
  • 19
    • 0030830360 scopus 로고    scopus 로고
    • Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, adhesive, and proinflammatory attributes
    • Colman RW, Schmaier AH. Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, adhesive, and proinflammatory attributes. Blood 1997; 90; 3819-43.
    • (1997) Blood , vol.90 , pp. 3819-3843
    • Colman, R.W.1    Schmaier, A.H.2
  • 21
    • 0020565895 scopus 로고
    • Thrombosis or myocardial infarction in congential clotting factor abnormalilties and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases
    • Goodnough LT, Saito H, Ratnoff OD. Thrombosis or myocardial infarction in congential clotting factor abnormalilties and chronic thrombocytopenias: a report of 21 patients and a review of 50 previously reported cases. Medicine 1983; 62: 248-55.
    • (1983) Medicine , vol.62 , pp. 248-255
    • Goodnough, L.T.1    Saito, H.2    Ratnoff, O.D.3
  • 22
    • 0021807758 scopus 로고
    • Multiple cerebral thrombosis in Fletcher factor (prekallikerin) deficiency: A case report
    • Harris MG, Exner T, Rickard KA, Kronenberg H. Multiple cerebral thrombosis in Fletcher factor (prekallikerin) deficiency: a case report. Am J Hematol 1985; 19: 387-93.
    • (1985) Am. J. Hematol. , vol.19 , pp. 387-393
    • Harris, M.G.1    Exner, T.2    Rickard, K.A.3    Kronenberg, H.4
  • 23
    • 0031973492 scopus 로고    scopus 로고
    • High molecular weight kininogen regulates prekallilrein assembly and activation on endothelial cells: A novel mechansism for contact activation
    • Motta G, Rojkjaer R, Hasan AA, Cines DB, Schmaier AH. High molecular weight kininogen regulates prekallilrein assembly and activation on endothelial cells: a novel mechansism for contact activation. Blood 1998; 91: 516-28.
    • (1998) Blood , vol.91 , pp. 516-528
    • Motta, G.1    Rojkjaer, R.2    Hasan, A.A.3    Cines, D.B.4    Schmaier, A.H.5
  • 25
    • 0034610405 scopus 로고    scopus 로고
    • Comparison of novel hemostatic factors and conventional risk factors for prediction of coronary heart disease
    • Cooper JA, Miller GJ, Bauer KA, Morrissey JH, Meade TW, Howarth DJ. Comparison of novel hemostatic factors and conventional risk factors for prediction of coronary heart disease. Circulation 2000; 102: 2816-22.
    • (2000) Circulation , vol.102 , pp. 2816-2822
    • Cooper, J.A.1    Miller, G.J.2    Bauer, K.A.3    Morrissey, J.H.4    Meade, T.W.5    Howarth, D.J.6
  • 28
    • 0028349373 scopus 로고
    • Hypercoagulable states as an evolving risk for spontaneous venous and arterial thrombosis
    • Levy PJ, Gonzales FM, Rush DS, Haynes JL. Hypercoagulable states as an evolving risk for spontaneous venous and arterial thrombosis. J Am Coll Surg 1994; 178: 266-70.
    • (1994) J. Am. Coll. Surg. , vol.178 , pp. 266-270
    • Levy, P.J.1    Gonzales, F.M.2    Rush, D.S.3    Haynes, J.L.4
  • 29
    • 0030893834 scopus 로고    scopus 로고
    • Hypercoagulability in venous and arterial thrombosis
    • Thomas DP, Roberts HR. Hypercoagulability in venous and arterial thrombosis. Ann Intern Med 1997; 126: 638-44.
    • (1997) Ann. Intern. Med. , vol.126 , pp. 638-644
    • Thomas, D.P.1    Roberts, H.R.2
  • 30
    • 0035225084 scopus 로고    scopus 로고
    • Risk factors of venous thromboembolism
    • Barczyk A, Pierzchala W. Risk factors of venous thromboembolism. Wiad Lek 2001; 54: 311-24.
    • (2001) Wiad Lek , vol.54 , pp. 311-324
    • Barczyk, A.1    Pierzchala, W.2
  • 32
    • 0035119009 scopus 로고    scopus 로고
    • Clinical evaluation of hypercoagulable states
    • Subar M. Clinical evaluation of hypercoagulable states. Clin Geriatr Med 2001; 17: 57-70.
    • (2001) Clin. Geriatr. Med. , vol.17 , pp. 57-70
    • Subar, M.1
  • 34
    • 0027352915 scopus 로고
    • Factor VII for a molecular marker in hypercoagulable state
    • Takamiya O, Okumura N, Factor VII for a molecular marker in hypercoagulable state. Rinsho Byori 1993; 41: 83-7.
    • (1993) Rinsho Byori , vol.41 , pp. 83-87
    • Takamiya, O.1    Okumura, N.2
  • 37
    • 0014322942 scopus 로고
    • Experimental hypercoagulable state induced by factor X: Comparison of the nonaciivated and activated forms
    • Wessler S, Yin ET. Experimental hypercoagulable state induced by factor X: comparison of the nonaciivated and activated forms. J Lab Clin Med 1968; 72: 256-60.
    • (1968) J. Lab. Clin. Med. , vol.72 , pp. 256-260
    • Wessler, S.1    Yin, E.T.2
  • 38
    • 0034969115 scopus 로고    scopus 로고
    • Fibrinogen and its degradtion products as thrombotic risk factors
    • Lowe GDO, Rumley A. Fibrinogen and its degradtion products as thrombotic risk factors. Ann N Y Acad Sci 2001; 936: 560-5.
    • (2001) Ann. N. Y. Acad. Sci. , vol.936 , pp. 560-565
    • Lowe, G.D.O.1    Rumley, A.2
  • 39
    • 0032719688 scopus 로고    scopus 로고
    • Mechanisms of hypercoagulability
    • Dahl OE. Mechanisms of hypercoagulability. Thromb Haemost 1999; 82: 902-6.
    • (1999) Thromb. Haemost. , vol.82 , pp. 902-906
    • Dahl, O.E.1
  • 41
    • 0034532266 scopus 로고    scopus 로고
    • Use of D-dmer assays in the diagnosis of venous thrombosis
    • Dempfle CE. Use of D-dmer assays in the diagnosis of venous thrombosis. Semin Thromb Hemost 2000; 26: 631-41.
    • (2000) Semin. Thromb. Hemost. , vol.26 , pp. 631-641
    • Dempfle, C.E.1
  • 42
    • 0024494725 scopus 로고
    • Plasma D-dimer levels and their relationship to serum fibrinogen/fibrin degradation products in hypercoagulable state
    • Wilde JT, Kitchen S, Kinsey S, Greaves M, Preston FE. Plasma D-dimer levels and their relationship to serum fibrinogen/fibrin degradation products in hypercoagulable state. Br J Haematol 1989; 71: 65-70.
    • (1989) Br. J. Haematol. , vol.71 , pp. 65-70
    • Wilde, J.T.1    Kitchen, S.2    Kinsey, S.3    Greaves, M.4    Preston, F.E.5
  • 43
    • 0026722973 scopus 로고
    • Prothrombin fragment F1+2 and thrombin-antithrombin III complex are useful markers of the hypercoagulable state in aterial fibrillation
    • Asakura H, Hifumi S, Jokaji H, Saito M, Kumabashiri I, Uotani C, et al. Prothrombin fragment F1+2 and thrombin-antithrombin III complex are useful markers of the hypercoagulable state in aterial fibrillation. Blood Coagul Fibrinolysis 1992; 3: 469-73.
    • (1992) Blood Coagul. Fibrinolysis , vol.3 , pp. 469-473
    • Asakura, H.1    Hifumi, S.2    Jokaji, H.3    Saito, M.4    Kumabashiri, I.5    Uotani, C.6
  • 44
    • 0026198861 scopus 로고
    • Thrombin-antithrombin III complex
    • Matsuo T, Kario K, Matsuo M. Thrombin-antithrombin III complex. Rinsho Byori 1991; 39: 701-6.
    • (1991) Rinsho Byori , vol.39 , pp. 701-706
    • Matsuo, T.1    Kario, K.2    Matsuo, M.3
  • 45
    • 0035116929 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor response does not correlate with tissue factor-induced disseminated intravascular coagulation and multiple organ dysfunction syndrome in trauma patients
    • Gando S, Nanzaki S, Morimoto Y, Ishitani T, Kemmotsu O. Tissue factor pathway inhibitor response does not correlate with tissue factor-induced disseminated intravascular coagulation and multiple organ dysfunction syndrome in trauma patients. Crit Care Med 2001; 29: 262-6.
    • (2001) Crit. Care Med. , vol.29 , pp. 262-266
    • Gando, S.1    Nanzaki, S.2    Morimoto, Y.3    Ishitani, T.4    Kemmotsu, O.5
  • 46
    • 18044385747 scopus 로고    scopus 로고
    • The tissue factor pathway in disseminated intravascular coagulation
    • Osterud B, Bjorklid E. The tissue factor pathway in disseminated intravascular coagulation. Semin Thromb Hemost 2001; 27: 605-17.
    • (2001) Semin. Thromb. Hemost. , vol.27 , pp. 605-617
    • Osterud, B.1    Bjorklid, E.2
  • 47
    • 0030818682 scopus 로고    scopus 로고
    • Effect of warfarin on markers of hypercoagulability in patients with heart failure
    • Jafri SM, Mammen EF, Masura J, Goldstein S. Effect of warfarin on markers of hypercoagulability in patients with heart failure. Am Heart J 1997; 134: 27-36.
    • (1997) Am. Heart J. , vol.134 , pp. 27-36
    • Jafri, S.M.1    Mammen, E.F.2    Masura, J.3    Goldstein, S.4
  • 48
    • 0031427325 scopus 로고    scopus 로고
    • Hypercoagulability in heart failure
    • Jafri SM. Hypercoagulability in heart failure. Semin Thromb Hemost 1997; 23: 543-5.
    • (1997) Semin. Thromb. Hemost. , vol.23 , pp. 543-545
    • Jafri, S.M.1
  • 49
    • 0031682255 scopus 로고    scopus 로고
    • Raised factor VIII is associated with coronary thrombotic events
    • Gorog DA, Rakhit R, Parums D, Laffan M, Davies GJ. Raised factor VIII is associated with coronary thrombotic events. Heart 1998; 80: 415-7.
    • (1998) Heart , vol.80 , pp. 415-417
    • Gorog, D.A.1    Rakhit, R.2    Parums, D.3    Laffan, M.4    Davies, G.J.5
  • 50
    • 0036438811 scopus 로고    scopus 로고
    • Hematological risk factors for coronary heart disease
    • El-Hazmi MA. Hematological risk factors for coronary heart disease. Med Princ Pract 2002; 11: 56-62.
    • (2002) Med. Princ. Pract. , vol.11 , pp. 56-62
    • El-Hazmi, M.A.1
  • 52
    • 0031846797 scopus 로고    scopus 로고
    • Does hypertension confer a hypercoagulable state?
    • Lip GY, Li-Saw-Hee FL. Does hypertension confer a hypercoagulable state? J Hypertens 1998; 16: 913-6.
    • (1998) J. Hypertens. , vol.16 , pp. 913-916
    • Lip, G.Y.1    Li-Saw-Hee, F.L.2
  • 53
    • 0033755029 scopus 로고    scopus 로고
    • Hypertension and the prothrombotic state
    • Lip GY. Hypertension and the prothrombotic state. J Hum Hypertens; 2000; 14: 687-90.
    • (2000) J. Hum. Hypertens. , vol.14 , pp. 687-690
    • Lip, G.Y.1
  • 54
    • 0033117108 scopus 로고    scopus 로고
    • Does heart failure confer a hypercoagulable state? Virchow's triad revisited
    • Lip GY, Gibbs CR. Does heart failure confer a hypercoagulable state? Virchow's triad revisited. J Am Coll Cardiol 1999; 33: 1424-6.
    • (1999) J. Am. Coll. Cardiol. , vol.33 , pp. 1424-1426
    • Lip, G.Y.1    Gibbs, C.R.2
  • 55
    • 0028140534 scopus 로고
    • Disseminated intravascular coagulation syndrome in myocardial infarct
    • Arkhangel'ski AV, Kovalev VI. Disseminated intravascular coagulation syndrome in myocardial infarct. Kardiologiia 1993; 33: 37-40.
    • (1993) Kardiologiia , vol.33 , pp. 37-40
    • Arkhangel'ski, A.V.1    Kovalev, V.I.2
  • 57
    • 0032943711 scopus 로고    scopus 로고
    • Coagulation factor II, V, VII, X, prothrombin gene 20210G/A transition, and factor V Leiden in coronary artery disease: High factor V clotting activity is an independent risk factor for myocardial infarction
    • Redondo M, Watzke HH, Stucki B, Sulzer I, Biasiutti FD, Binder BR, et al. Coagulation factor II, V, VII, X, prothrombin gene 20210G/A transition, and factor V Leiden in coronary artery disease: high factor V clotting activity is an independent risk factor for myocardial infarction. Arterioscler Thromb Vasc Biol 1999; 19: 1020-5.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 1020-1025
    • Redondo, M.1    Watzke, H.H.2    Stucki, B.3    Sulzer, I.4    Biasiutti, F.D.5    Binder, B.R.6
  • 58
    • 0028790207 scopus 로고
    • Activation of blood coagulation after cardiac arrest is not balanced adequately by activation of endogenous fibrinolysis
    • Bottiger BW, Motsch J, Bohrer H, Boker T, Aulmann M, Nawroth PP, Martin E. Activation of blood coagulation after cardiac arrest is not balanced adequately by activation of endogenous fibrinolysis. Circulation 1995; 92: 2572-8.
    • (1995) Circulation , vol.92 , pp. 2572-2578
    • Bottiger, B.W.1    Motsch, J.2    Bohrer, H.3    Boker, T.4    Aulmann, M.5    Nawroth, P.P.6    Martin, E.7
  • 60
    • 0025495669 scopus 로고
    • Atherosclerotic plaque growth: Presence of stmulatory fibrin degradation products
    • Thompson WD, Smith EB, Stirk CM, Kochhar A. Atherosclerotic plaque growth: presence of stmulatory fibrin degradation products. Blood Coagul Fibrinolysis 1990; 1: 489-93.
    • (1990) Blood Coagul. Fibrinolysis , vol.1 , pp. 489-493
    • Thompson, W.D.1    Smith, E.B.2    Stirk, C.M.3    Kochhar, A.4
  • 61
    • 0028789033 scopus 로고
    • Hemostasis and atherosclerosis
    • Warkentin TE. Hemostasis and atherosclerosis. Can J Cardiol 1995;11:29C-34C.
    • (1995) Can. J. Cardiol. , vol.11
    • Warkentin, T.E.1
  • 64
    • 0033559725 scopus 로고    scopus 로고
    • Prothrombin fragments F1+2, thrombin-antithrombin III complexs, fibrin monomers and fibrinogen in patients with coronary atherosclerosis
    • Giannitsis E, Siemens HJ, Mitusch R, Tettenborn I, Wiegand U, Schmucker G, et al. Prothrombin fragments F1+2, thrombin-antithrombin III complexs, fibrin monomers and fibrinogen in patients with coronary atherosclerosis. Int J Cardiol 1999; 68; 269-74.
    • (1999) Int. J. Cardiol. , vol.68 , pp. 269-274
    • Giannitsis, E.1    Siemens, H.J.2    Mitusch, R.3    Tettenborn, I.4    Wiegand, U.5    Schmucker, G.6
  • 65
    • 0033678470 scopus 로고    scopus 로고
    • In situ analysis of tissue factor-dependent thrombin generation in human atherosclerotic vessels
    • Westmuckett AD, Lupu C, Goulding DA, Das S, Kakkar VV, Lupu F. In situ analysis of tissue factor-dependent thrombin generation in human atherosclerotic vessels. Thromb Haemost 2000; 84: 904-11.
    • (2000) Thromb. Haemost. , vol.84 , pp. 904-911
    • Westmuckett, A.D.1    Lupu, C.2    Goulding, D.A.3    Das, S.4    Kakkar, V.V.5    Lupu, F.6
  • 66
    • 0036846990 scopus 로고    scopus 로고
    • In vivo imaging of thrombin activity in experimental thrombi using a thrombin-sensitive near-infrared molecular probe
    • Jaffer AF, Tung C-H, Gerszten RE, Weissleder R. In vivo imaging of thrombin activity in experimental thrombi using a thrombin-sensitive near-infrared molecular probe. Arterioscler Thrmob Vasc Biol 2002; 22: 1929-35.
    • (2002) Arterioscler. Thrmob. Vasc. Biol. , vol.22 , pp. 1929-1935
    • Jaffer, A.F.1    Tung, C.-H.2    Gerszten, R.E.3    Weissleder, R.4
  • 67
    • 0033952726 scopus 로고    scopus 로고
    • Plasma fibrinogen, haemostatic factors and predication of peripheral arterial disease in the Edinburgh Artery Study
    • Smith FB, Lee AJ, Hau CM, Rumley A, Lowe GD, Fowkes FG. Plasma fibrinogen, haemostatic factors and predication of peripheral arterial disease in the Edinburgh Artery Study. Blood Coagul Fibrinolysis 2000; 11: 43-50.
    • (2000) Blood Coagul. Fibrinolysis , vol.11 , pp. 43-50
    • Smith, F.B.1    Lee, A.J.2    Hau, C.M.3    Rumley, A.4    Lowe, G.D.5    Fowkes, F.G.6
  • 68
    • 0033028586 scopus 로고    scopus 로고
    • Hyperhomocysteinemia, atherosclerosis and thrombosis
    • Cattaneo M. Hyperhomocysteinemia, atherosclerosis and thrombosis. Thromb Haemost 1999: 81: 165-176.
    • (1999) Thromb. Haemost. , vol.81 , pp. 165-176
    • Cattaneo, M.1
  • 70
    • 0034655148 scopus 로고    scopus 로고
    • Smoth muscle cells outgrowth stimulated by fibrin degradation products. The potential role of fibrin fragment E in restenosis and atherogenesis
    • Naito M, Stirk CM, Smith EB, Thompson WD. Smoth muscle cells outgrowth stimulated by fibrin degradation products. The potential role of fibrin fragment E in restenosis and atherogenesis. Thromb Res 2000; 98: 165-74.
    • (2000) Thromb. Res. , vol.98 , pp. 165-174
    • Naito, M.1    Stirk, C.M.2    Smith, E.B.3    Thompson, W.D.4
  • 71
    • 0026486960 scopus 로고
    • Homocysteine and other sulfhydryl compounds enhance the binding of lipoprotein (a) to fibrin: A potential biochemical link between thrombosis, atherogeneis, and sulfhydryl compound metabolism
    • Harpel PC, Chang VT, Borth W. Homocysteine and other sulfhydryl compounds enhance the binding of lipoprotein (a) to fibrin: a potential biochemical link between thrombosis, atherogeneis, and sulfhydryl compound metabolism. Proc Natl Acad Sci USA 1992; 89: 10193-97.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10193-10197
    • Harpel, P.C.1    Chang, V.T.2    Borth, W.3
  • 72
    • 0035892139 scopus 로고    scopus 로고
    • Lpiprotein (a) binds and inactivates tissue factor pathway inhibitor: A novel link between lipoproteins and thrombosis
    • Caplice NM, Panetta C, Peterson TE, Kleppe LS, Mueske CS, Kostner GM, et al. Lpiprotein (a) binds and inactivates tissue factor pathway inhibitor: a novel link. between lipoproteins and thrombosis. Blood 2001; 98: 2980-87.
    • (2001) Blood , vol.98 , pp. 2980-2987
    • Caplice, N.M.1    Panetta, C.2    Peterson, T.E.3    Kleppe, L.S.4    Mueske, C.S.5    Kostner, G.M.6
  • 73
    • 0027955330 scopus 로고
    • Lipoprotein (a) regulates plasmin generation and inhibition
    • Edelberg J, Pizzo SV. Lipoprotein (a) regulates plasmin generation and inhibition. Chem Phys Lipids 1994; 67/68: 363-8.
    • (1994) Chem. Phys. Lipids , vol.67-68 , pp. 363-368
    • Edelberg, J.1    Pizzo, S.V.2
  • 74
    • 0032851935 scopus 로고    scopus 로고
    • Treatment of hyperhomocysteinemia with folic acid and vitamin B12 and B6 attenuates thrombin generation
    • Undas A, Domagala TB, Jankowski M, Szczeklik A. Treatment of hyperhomocysteinemia with folic acid and vitamin B12 and B6 attenuates thrombin generation. Thromb Res 1999; 95: 281-8.
    • (1999) Thromb. Res. , vol.95 , pp. 281-288
    • Undas, A.1    Domagala, T.B.2    Jankowski, M.3    Szczeklik, A.4
  • 75
    • 0036335481 scopus 로고    scopus 로고
    • Effect of homocysteine reduction by B-vitamin supplementation on markers of clotting activation
    • Klerk M, Verhoef P, Verbruggen B, Schouten EG, Blom HJ, Bos GM, et al. Effect of homocysteine reduction by B-vitamin supplementation on markers of clotting activation. Thromb Haemost 2002; 88: 230-5.
    • (2002) Thromb. Haemost. , vol.88 , pp. 230-235
    • Klerk, M.1    Verhoef, P.2    Verbruggen, B.3    Schouten, E.G.4    Blom, H.J.5    Bos, G.M.6
  • 76
    • 0014434483 scopus 로고
    • Activation of Hageman factor by L-homocysteine
    • Ratnoff OD. Activation of Hageman factor by L-homocysteine. Science 1968; 162: 1007-9.
    • (1968) Science , vol.162 , pp. 1007-1009
    • Ratnoff, O.D.1
  • 77
    • 0022472013 scopus 로고
    • Activation of endogenous factor V by homocysteine-induced vascular endothelial cell activator
    • Rodgers GM, Kane WH. Activation of endogenous factor V by homocysteine-induced vascular endothelial cell activator. J Clin Invest 1986; 77: 1909-16.
    • (1986) J. Clin. Invest. , vol.77 , pp. 1909-1916
    • Rodgers, G.M.1    Kane, W.H.2
  • 78
    • 0027250615 scopus 로고
    • Homocysteine, a risk for premature vascular disease and thrombosis, induces tissue factor activity in endothelial cells
    • Fryer RH, Wilson BD, Gubler DB, Fitzgerald LA, Rodgers GM Homocysteine, a risk for premature vascular disease and thrombosis, induces tissue factor activity in endothelial cells. Arteriosclerosis Thromb 1993; 13: 1327-33.
    • (1993) Arteriosclerosis Thromb. , vol.13 , pp. 1327-1333
    • Fryer, R.H.1    Wilson, B.D.2    Gubler, D.B.3    Fitzgerald, L.A.4    Rodgers, G.M.5
  • 79
    • 0025190042 scopus 로고
    • Homocysteine, an atherogenic stimulus, reduces protein C activation by arterial and venous endothelial cells
    • Rodgers GM, Conn MT. Homocysteine, an atherogenic stimulus, reduces protein C activation by arterial and venous endothelial cells. Blood 1990; 75: 895-901.
    • (1990) Blood , vol.75 , pp. 895-901
    • Rodgers, G.M.1    Conn, M.T.2
  • 80
    • 0026345948 scopus 로고
    • Inhibiton of thrombomodulin surface expression and protein C activation by the thromgenic agent homocysteine
    • Lentz SR, Sadler JE. Inhibiton of thrombomodulin surface expression and protein C activation by the thromgenic agent homocysteine. J Clin Invest 1991; 88: 1906-14.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1906-1914
    • Lentz, S.R.1    Sadler, J.E.2
  • 81
    • 0026773724 scopus 로고
    • An atherogenic stimulus homocysteine inhibits cofactor activity of thrombomodulin and enhances thrombomodulin expression in human umbilical vein endothelial cells
    • Hayashi T, Honda G, Suzuki K. An atherogenic stimulus homocysteine inhibits cofactor activity of thrombomodulin and enhances thrombomodulin expression in human umbilical vein endothelial cells. Blood 1992; 79: 2930-36.
    • (1992) Blood , vol.79 , pp. 2930-2936
    • Hayashi, T.1    Honda, G.2    Suzuki, K.3
  • 83
    • 0027319970 scopus 로고
    • Homocytsteine, a thrombogenic agent, suppresses anticoagulant heparan sulfate expression in cultured porcine aortic endothelial cells
    • Nishinaga M, Ozawa T, Shimada K. Homocytsteine, a thrombogenic agent, suppresses anticoagulant heparan sulfate expression in cultured porcine aortic endothelial cells. J Clin Invest 1993; 92: 1381-6.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1381-1386
    • Nishinaga, M.1    Ozawa, T.2    Shimada, K.3
  • 84
    • 0027288252 scopus 로고
    • Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor
    • Hajjar KA. Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor. J Clin Invest 1993; 91 2873-79.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2873-2879
    • Hajjar, K.A.1
  • 85
    • 0034720436 scopus 로고    scopus 로고
    • Enhancement by homocysteine of plasminogen activator inhibitor-1 gene expression and secretion from vascular endothelial and smooth muscle cells
    • Midorikawa S, Sanada H, Hashimoto S, Watanabe T. Enhancement by homocysteine of plasminogen activator inhibitor-1 gene expression and secretion from vascular endothelial and smooth muscle cells. Biochem Biophys Res Commun 2000; 272: 182-5.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 182-185
    • Midorikawa, S.1    Sanada, H.2    Hashimoto, S.3    Watanabe, T.4
  • 86
    • 0036847628 scopus 로고    scopus 로고
    • Association between increased homocysteine levels and impaired fibrinolytic potential: Potential mechanism for cardiovascular risk
    • Tofler GH, D'Agostino RB, Jacques PF, Bostom AG, Wilson PW, Lipinska I, et al. Association between increased homocysteine levels and impaired fibrinolytic potential: potential mechanism for cardiovascular risk. Haemost 2002; 88: 799-804.
    • (2002) Haemost. , vol.88 , pp. 799-804
    • Tofler, G.H.1    D'Agostino, R.B.2    Jacques, P.F.3    Bostom, A.G.4    Wilson, P.W.5    Lipinska, I.6
  • 87
    • 0008492767 scopus 로고
    • Inherited antithrombin deficiency causing thrombophilia
    • Egeberg O. Inherited antithrombin deficiency causing thrombophilia. Thromb Diath Haemorrh 1965; 116: 754-61.
    • (1965) Thromb. Diath. Haemorrh. , vol.116 , pp. 754-761
    • Egeberg, O.1
  • 88
    • 0030037196 scopus 로고    scopus 로고
    • Molecular genetics of antithrombin deficiency
    • Lane DA, Kunz G, Olds RJ, Thein SL. Molecular genetics of antithrombin deficiency. Blood Rev 1996; 10: 59-74.
    • (1996) Blood Rev. , vol.10 , pp. 59-74
    • Lane, D.A.1    Kunz, G.2    Olds, R.J.3    Thein, S.L.4
  • 89
    • 0022385451 scopus 로고
    • Hereditary protein C deficiency
    • Broekmans AW. Hereditary protein C deficiency. Hemostasis 1985; 15: 233-40
    • (1985) Hemostasis , vol.15 , pp. 233-240
    • Broekmans, A.W.1
  • 90
    • 0021741550 scopus 로고
    • Familial protein S deficiency is associated with recurrent thrombosis
    • Comp PC, Nixon R, Cooper M, Esmon C. Familial protein S deficiency is associated with recurrent thrombosis. J Clin Invest 1984; 74; 2082-8.
    • (1984) J. Clin. Invest. , vol.74 , pp. 2082-2088
    • Comp, P.C.1    Nixon, R.2    Cooper, M.3    Esmon, C.4
  • 92
    • 0025169536 scopus 로고
    • Hereditary protein S deficiency in young adults with arterial occlusive disease
    • Allaart CF, Aronson D, Ruys T. Hereditary protein S deficiency in young adults with arterial occlusive disease. Thromb Haemost 1990; 64: 206-10.
    • (1990) Thromb. Haemost. , vol.64 , pp. 206-210
    • Allaart, C.F.1    Aronson, D.2    Ruys, T.3
  • 94
    • 0030062348 scopus 로고    scopus 로고
    • Molecular and cellular basis for type I heparin cofactor II deficiency
    • Kondo S, Tokunaga F, Kario K, Matsuo T, Koide T. Molecular and cellular basis for type I heparin cofactor II deficiency. Blood 1996; 87: 1006-12.
    • (1996) Blood , vol.87 , pp. 1006-1012
    • Kondo, S.1    Tokunaga, F.2    Kario, K.3    Matsuo, T.4    Koide, T.5
  • 95
    • 0036880595 scopus 로고    scopus 로고
    • Heparin cofactor II deficiency
    • Tollefsen DM. Heparin cofactor II deficiency. Arch Pathol Lab Med 2002; 126: 1394-1400.
    • (2002) Arch. Pathol. Lab. Med. , vol.126 , pp. 1394-1400
    • Tollefsen, D.M.1
  • 96
    • 0036881556 scopus 로고    scopus 로고
    • Laboratory evaluation of hypercoagulability with venous or arterial thrombosis
    • Van Cott EM, Laposata M, Prins MH. Laboratory evaluation of hypercoagulability with venous or arterial thrombosis. Arch Pathol Lab Med 2002; 126: 1281-95.
    • (2002) Arch. Pathol. Lab. Med. , vol.126 , pp. 1281-1295
    • Van Cott, E.M.1    Laposata, M.2    Prins, M.H.3
  • 97
    • 0028098210 scopus 로고
    • Resistance to activated protein C as a basis for venous thrombosis
    • Svensson PJ, Dahlback B. Resistance to activated protein C as a basis for venous thrombosis. N Engl J Med 1994; 330; 517-22.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 517-522
    • Svensson, P.J.1    Dahlback, B.2
  • 98
    • 0030929275 scopus 로고    scopus 로고
    • Resistance to activated protein C caused by the R506Q mutantion in the gene for factor V is a common risk factor for venous thrombosis
    • Dahback B. Resistance to activated protein C caused by the R506Q mutantion in the gene for factor V is a common risk factor for venous thrombosis. J Intern Med 1997; 740(S): 1-8.
    • (1997) J. Intern. Med. , vol.740 , Issue.SUPPL. , pp. 1-8
    • Dahback, B.1
  • 99
    • 0029850530 scopus 로고    scopus 로고
    • A common genetic variation in the 3′-untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increase in venous thrombosis
    • Poort SR, Rosendaal FR, Reitsma PH, Bertina RM. A common genetic variation in the 3′-untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increase in venous thrombosis. Blood 1996; 88: 3698-703.
    • (1996) Blood , vol.88 , pp. 3698-3703
    • Poort, S.R.1    Rosendaal, F.R.2    Reitsma, P.H.3    Bertina, R.M.4
  • 100
    • 17344373283 scopus 로고    scopus 로고
    • Clinical studies and thrombin generation in patients homozygous or heterozygous for the G20210A mutation in the prothrombin gene
    • Kyrle PA, Mannhalter C, Beguin S, Stumpflen A, Hirschl M, Weltermann A, et al. Clinical studies and thrombin generation in patients homozygous or heterozygous for the G20210A mutation in the prothrombin gene. Arterioscler Thromb Vasc Biol 1998; 18: 1287-91.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 1287-1291
    • Kyrle, P.A.1    Mannhalter, C.2    Beguin, S.3    Stumpflen, A.4    Hirschl, M.5    Weltermann, A.6
  • 101
    • 0030793124 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor: Clinical deficiency states
    • Sandset PM, Bendz B. Tissue factor pathway inhibitor: clinical deficiency states. Thromb Haemost 1996; 78: 467-70.
    • (1996) Thromb. Haemost. , vol.78 , pp. 467-470
    • Sandset, P.M.1    Bendz, B.2
  • 102
    • 0035130684 scopus 로고    scopus 로고
    • Acquired antithrombin III deficiency in sepsis
    • White B, Perry D. Acquired antithrombin III deficiency in sepsis. Br J Haematol 2001; 112: 26-31.
    • (2001) Br. J. Haematol. , vol.112 , pp. 26-31
    • White, B.1    Perry, D.2
  • 103
    • 0036658149 scopus 로고    scopus 로고
    • Plasma levels of heparin cofactor II (HC II) and thrombin-HC II complex in patients with disseminated intravascular coagulation
    • Noda A, Wada H, Kusiya F, Sakakura M, Onishi K, Nakatani K, et al. Plasma levels of heparin cofactor II (HC II) and thrombin-HC II complex in patients with disseminated intravascular coagulation. Clin Appl Thromb Hemost 2002; 8: 265-71.
    • (2002) Clin. Appl. Thromb. Hemost. , vol.8 , pp. 265-271
    • Noda, A.1    Wada, H.2    Kusiya, F.3    Sakakura, M.4    Onishi, K.5    Nakatani, K.6
  • 104
    • 0035673016 scopus 로고    scopus 로고
    • The phenomenon known as acquired activated protein C resistance
    • Clark P, Walker ID. The phenomenon known as acquired activated protein C resistance. Br J Haematol 2001; 115: 767-71.
    • (2001) Br. J. Haematol. , vol.115 , pp. 767-771
    • Clark, P.1    Walker, I.D.2
  • 106
    • 0035093810 scopus 로고    scopus 로고
    • Diabetes mellitus: A hypercoagulable state
    • Carr ME. Diabetes mellitus: a hypercoagulable state. J Diab Complications 2001; 15: 44-54.
    • (2001) J. Diab. Complications , vol.15 , pp. 44-54
    • Carr, M.E.1
  • 108
  • 109
  • 111
  • 113
  • 114
    • 0025218674 scopus 로고
    • The role of hyperglycaemia-induced alterations of antithrombin III and factor X activation in the thrombin hyperactivity of diabetes mellitus
    • Ceriello A, Quatraro A, Marchi E, Barbanti M, Dello E, Russo P, et al. The role of hyperglycaemia-induced alterations of antithrombin III and factor X activation in the thrombin hyperactivity of diabetes mellitus. Diabet Med 1990; 7: 343-8.
    • (1990) Diabet. Med. , vol.7 , pp. 343-348
    • Ceriello, A.1    Quatraro, A.2    Marchi, E.3    Barbanti, M.4    Dello, E.5    Russo, P.6
  • 115
    • 0023461644 scopus 로고
    • Fibrinogen-fibrin degradation products in diabetes mellitus
    • Alakhverdian R, Koev D. Fibrinogen-fibrin degradation products in diabetes mellitus. Vutr Boles 1987; 26: 72-5.
    • (1987) Vutr. Boles , vol.26 , pp. 72-75
    • Alakhverdian, R.1    Koev, D.2
  • 116
    • 0027427638 scopus 로고
    • Enhanced prothrombin and intrinsci factor X activation on blood platelets from diabetic patients
    • Lupu C, Calb M, Ionescu M, Lupu F. Enhanced prothrombin and intrinsci factor X activation on blood platelets from diabetic patients. Thromb Haemost 1993; 70: 579-83.
    • (1993) Thromb. Haemost. , vol.70 , pp. 579-583
    • Lupu, C.1    Calb, M.2    Ionescu, M.3    Lupu, F.4
  • 117
    • 0032007011 scopus 로고    scopus 로고
    • Advanced glycosylation end products induced tissue factor expression in human monocyte-like U937 cells and increased tissue factor expression in monocytes from diabetic patients
    • Ichikawa K, Yoshinari M, Iwase M, Wakisaka M, Doi Y, Iino K, et al. Advanced glycosylation end products induced tissue factor expression in human monocyte-like U937 cells and increased tissue factor expression in monocytes from diabetic patients. Atherosclerosis 1998; 136; 281-7.
    • (1998) Atherosclerosis , vol.136 , pp. 281-287
    • Ichikawa, K.1    Yoshinari, M.2    Iwase, M.3    Wakisaka, M.4    Doi, Y.5    Iino, K.6
  • 118
    • 0030761061 scopus 로고    scopus 로고
    • Thrombomodulin and induced tissue factor expression on monocytes as markers of diabetic microangiopathy: A prospective study on hemostasis and lipoproteins in insulin-dependent diabetes mellitus
    • Reverter JL, Reverter JC, Tassies D, Rius F, Monteagudo J, Rubies-Prat J, et al. Thrombomodulin and induced tissue factor expression on monocytes as markers of diabetic microangiopathy: a prospective study on hemostasis and lipoproteins in insulin-dependent diabetes mellitus. Am J Hematol 1997; 56: 93-9.
    • (1997) Am. J. Hematol. , vol.56 , pp. 93-99
    • Reverter, J.L.1    Reverter, J.C.2    Tassies, D.3    Rius, F.4    Monteagudo, J.5    Rubies-Prat, J.6
  • 120
    • 0025986115 scopus 로고
    • 15 parameters of coagulation and fibrinolysis in children with type I diabetes mellitus (onset period)
    • Koert M, Nowak-Gotl U, Kreuz W, Gruttner HP, Kornhuber B, Breddin HK. 15 parameters of coagulation and fibrinolysis in children with type I diabetes mellitus (onset period). Klin Padistr 1991; 203: 429-32.
    • (1991) Klin. Padistr. , vol.203 , pp. 429-432
    • Koert, M.1    Nowak-Gotl, U.2    Kreuz, W.3    Gruttner, H.P.4    Kornhuber, B.5    Breddin, H.K.6
  • 122
    • 0030897021 scopus 로고    scopus 로고
    • Increased tissue factor pathway inhibitor (TFPI) and coagulation in patients with insulin-dependent diabetes mellitus
    • Leurs PB, van Oerle R, Wolffenbuttel BH, Hamulyak K. Increased tissue factor pathway inhibitor (TFPI) and coagulation in patients with insulin-dependent diabetes mellitus. Thromb Res 1997; 77: 472-6.
    • (1997) Thromb. Res. , vol.77 , pp. 472-476
    • Leurs, P.B.1    van Oerle, R.2    Wolffenbuttel, B.H.3    Hamulyak, K.4
  • 124
    • 0022470867 scopus 로고
    • Decreased proteins C levels in patients with insulin-dependent type I diabetes mellitus
    • Vukovich TC, Schernthaner G. Decreased proteins C levels in patients with insulin-dependent type I diabetes mellitus. Diabetes 1986; 35: 617-9.
    • (1986) Diabetes , vol.35 , pp. 617-619
    • Vukovich, T.C.1    Schernthaner, G.2
  • 125
    • 0030867218 scopus 로고    scopus 로고
    • No effect of unfractioned or low molecular weight heparin treatment on markers of vascular wall and hemostatic function in incipient diabetic nephropathy
    • Myrup B, Jensen T, Gram J, Kluft C, Jespersen J, Deckert T. No effect of unfractioned or low molecular weight heparin treatment on markers of vascular wall and hemostatic function in incipient diabetic nephropathy. Diabetes Care 1997; 20: 1615-19.
    • (1997) Diabetes Care , vol.20 , pp. 1615-1619
    • Myrup, B.1    Jensen, T.2    Gram, J.3    Kluft, C.4    Jespersen, J.5    Deckert, T.6
  • 126
    • 0033832185 scopus 로고    scopus 로고
    • Elevation of fibrinogen and thrombin-antithrombin III complex levels of type 2 diabetes mellitus patients with retinopathy and nephropathy
    • Asakawa H, Tokunaga K, Kawakami F. Elevation of fibrinogen and thrombin-antithrombin III complex levels of type 2 diabetes mellitus patients with retinopathy and nephropathy. J Diabetes Complications 2000; 14: 121-6.
    • (2000) J. Diabetes Complications , vol.14 , pp. 121-126
    • Asakawa, H.1    Tokunaga, K.2    Kawakami, F.3
  • 127
    • 8544226987 scopus 로고    scopus 로고
    • Increased soluble fibrin monomer and soluble thrombomodulin levels in non-insulin-dependent diabetes mellitus
    • Sumida Y, Wada H, Fujii M, Mori Y, Nakasaki T, Shimura M, et al. Increased soluble fibrin monomer and soluble thrombomodulin levels in non-insulin-dependent diabetes mellitus. Blood Coagul Fibrinolysis 1997; 8: 303-7.
    • (1997) Blood Coagul. Fibrinolysis , vol.8 , pp. 303-307
    • Sumida, Y.1    Wada, H.2    Fujii, M.3    Mori, Y.4    Nakasaki, T.5    Shimura, M.6
  • 129
    • 0030070114 scopus 로고    scopus 로고
    • Hypercoagulability and high lipoprotein (a) levels in patients with Type II diabetes mellitus
    • Morishita E, Asakura H, Jokaji H, Saito M, Uotani C, Kumabashiri I, et al. Hypercoagulability and high lipoprotein (a) levels in patients with Type II diabetes mellitus. Atherosclerosis 1996; 120: 7-14.
    • (1996) Atherosclerosis , vol.120 , pp. 7-14
    • Morishita, E.1    Asakura, H.2    Jokaji, H.3    Saito, M.4    Uotani, C.5    Kumabashiri, I.6
  • 130
    • 0032250114 scopus 로고    scopus 로고
    • Circulating thrombomodulin and hematological alterations in type 2 diabetic patients with retinopathy
    • Fujiwara Y, Tagami S, Kawakami Y. Circulating thrombomodulin and hematological alterations in type 2 diabetic patients with retinopathy. J Atheroscler Thromb 1998; 5: 21-8.
    • (1998) J. Atheroscler. Thromb. , vol.5 , pp. 21-28
    • Fujiwara, Y.1    Tagami, S.2    Kawakami, Y.3
  • 131
    • 0036117399 scopus 로고    scopus 로고
    • Impaired fibrinolytic compensation for hypercoagulability in obese patients with type 2 dabetes: Association with increased plasminogen activator inhibitor-1
    • Aso Y, Matsumoto S, Fujiwara Y, Tayama K, Inukai T, Takemura Y. Impaired fibrinolytic compensation for hypercoagulability in obese patients with type 2 dabetes: association with increased plasminogen activator inhibitor-1. Metabolism 2002; 51: 471-6.
    • (2002) Metabolism , vol.51 , pp. 471-476
    • Aso, Y.1    Matsumoto, S.2    Fujiwara, Y.3    Tayama, K.4    Inukai, T.5    Takemura, Y.6
  • 133
    • 0034847716 scopus 로고    scopus 로고
    • Physical training decreases plasma thrombomodulin in type I and type II diabetic patients
    • Rigla M, Fontcuberta J, Mateo J, Caixas A, Pou JM, de Leiva A, et al. Physical training decreases plasma thrombomodulin in type I and type II diabetic patients. Diabetologia 2001; 44: 693-9.
    • (2001) Diabetologia , vol.44 , pp. 693-699
    • Rigla, M.1    Fontcuberta, J.2    Mateo, J.3    Caixas, A.4    Pou, J.M.5    de Leiva, A.6
  • 134
    • 0035760887 scopus 로고    scopus 로고
    • Regulation of tissue factor gene expression in obesity
    • Samad F, Pandey M, Loskutoff DJ. Regulation of tissue factor gene expression in obesity. Blood 2001; 98: 3353-8.
    • (2001) Blood , vol.98 , pp. 3353-3358
    • Samad, F.1    Pandey, M.2    Loskutoff, D.J.3
  • 135
    • 0022881467 scopus 로고
    • Effect of insulin therapy on coagulation and platelet function in type II (non-insulin-dependent) diabetes mellitus
    • Small M, Douglas JT, Lowe GD, MacCuish AC, Forbes CD. Effect of insulin therapy on coagulation and platelet function in type II (non-insulin-dependent) diabetes mellitus. Haemostasis 1986; 16: 417-23.
    • (1986) Haemostasis , vol.16 , pp. 417-423
    • Small, M.1    Douglas, J.T.2    Lowe, G.D.3    MacCuish, A.C.4    Forbes, C.D.5
  • 136
    • 0027654230 scopus 로고
    • The fibrnogen degradation products (FgDP) levels in liver disease
    • Song KS, Kim HS, Park KE, Kwon OH. The fibrnogen degradation products (FgDP) levels in liver disease. Yonsei Med J 1993; 34: 234-8.
    • (1993) Yonsei Med. J. , vol.34 , pp. 234-238
    • Song, K.S.1    Kim, H.S.2    Park, K.E.3    Kwon, O.H.4
  • 137
    • 0026581553 scopus 로고
    • Protein C in patients with alcoholic cirrhosis and other liver diseases
    • Bell H, Odegaard OR, Andersson T, Raknerud N. Protein C in patients with alcoholic cirrhosis and other liver diseases. J Hepatol 1992; 14: 163-7.
    • (1992) J. Hepatol. , vol.14 , pp. 163-167
    • Bell, H.1    Odegaard, O.R.2    Andersson, T.3    Raknerud, N.4
  • 139
    • 0029438528 scopus 로고
    • Increased rate of thrombin generation in hepatitis C virus cirrhotic patients. Relationship to venous thrombosis
    • Violi F, Ferro D, Basili S, Artini M, Valesini G, Levrero M, Cordova C. Increased rate of thrombin generation in hepatitis C virus cirrhotic patients. Relationship to venous thrombosis. J Investig Med 1995; 43: 550-4.
    • (1995) J. Investig. Med. , vol.43 , pp. 550-554
    • Violi, F.1    Ferro, D.2    Basili, S.3    Artini, M.4    Valesini, G.5    Levrero, M.6    Cordova, C.7
  • 140
    • 0032428745 scopus 로고    scopus 로고
    • Thrombin-antithrombin III and D-dimer plasma levels in patients with benign or malignant ovarian tumours
    • den Ouden M, Ubachs JM, Stoot JE, van Wersch JW. Thrombin-antithrombin III and D-dimer plasma levels in patients with benign or malignant ovarian tumours. Scan J Clin Lab Invest 1998; 58: 555-9.
    • (1998) Scan. J. Clin. Lab. Invest. , vol.58 , pp. 555-559
    • den Ouden, M.1    Ubachs, J.M.2    Stoot, J.E.3    van Wersch, J.W.4
  • 144
    • 0031663262 scopus 로고    scopus 로고
    • Elevated TFPI in malignant disease: Relation to cancer type and hypercoagulation
    • Iversen N, Lindahl AK, Abildgaard U. Elevated TFPI in malignant disease: relation to cancer type and hypercoagulation. Br J Haematol 1998; 102: 889-95.
    • (1998) Br. J. Haematol. , vol.102 , pp. 889-895
    • Iversen, N.1    Lindahl, A.K.2    Abildgaard, U.3
  • 148
    • 0026743902 scopus 로고
    • Plasma factor VII and thrombin-antithrombin III levels indicate increased tissue factor activity in sickle cells patients
    • Kurantsin-Mills J, Ofosu FA, Safa TK, Siegel RS, Lessin LS. Plasma factor VII and thrombin-antithrombin III levels indicate increased tissue factor activity in sickle cells patients. Br J Haematol 1992; 81: 539-44.
    • (1992) Br. J. Haematol. , vol.81 , pp. 539-544
    • Kurantsin-Mills, J.1    Ofosu, F.A.2    Safa, T.K.3    Siegel, R.S.4    Lessin, L.S.5
  • 149
    • 0032101042 scopus 로고    scopus 로고
    • Whole blood tissue factor procoagulant activity is elevated in patients with sickle cell disease
    • Key NS, Slungaard A, Dandelet L, Nelson SC, Moertel C, Styles LA, et al. Whole blood tissue factor procoagulant activity is elevated in patients with sickle cell disease. Blood 1998; 91: 4216-23.
    • (1998) Blood , vol.91 , pp. 4216-4223
    • Key, N.S.1    Slungaard, A.2    Dandelet, L.3    Nelson, S.C.4    Moertel, C.5    Styles, L.A.6
  • 156
    • 0033068813 scopus 로고    scopus 로고
    • Increased levels of factor VII, fibrinogen and activity of plasminogen activator inhibitor during postprandial triglyceridemia in patients with ischemic heart disease confirmed by angiography
    • Jastrzebska M, Przybycien K, Chelstowski K, Torbus-Lisiecka B, Kornacewicz-Jach Z, Naruszewicz M. Increased levels of factor VII, fibrinogen and activity of plasminogen activator inhibitor during postprandial triglyceridemia in patients with ischemic heart disease confirmed by angiography. Nutr Metab Cardiovasc Dis 1999; 9: 33-40.
    • (1999) Nutr. Metab. Cardiovasc. Dis. , vol.9 , pp. 33-40
    • Jastrzebska, M.1    Przybycien, K.2    Chelstowski, K.3    Torbus-Lisiecka, B.4    Kornacewicz-Jach, Z.5    Naruszewicz, M.6
  • 157
    • 85086683683 scopus 로고    scopus 로고
    • Correction of circulating 17 beta-oestradiol with haemostatic factors in healthy postmenopausal women
    • Mukherjee M, Dawson G, Sembhi K, Kakkar VV. Correction of circulating 17 beta-oestradiol with haemostatic factors in healthy postmenopausal women. Thromb Haemost 1996: 76: 500-1.
    • (1996) Thromb. Haemost. , vol.76 , pp. 500-501
    • Mukherjee, M.1    Dawson, G.2    Sembhi, K.3    Kakkar, V.V.4
  • 158
    • 0036840659 scopus 로고    scopus 로고
    • Association of factor VII levels with inflammatory parameters in hypercholesterolemic patients
    • Porreca E, Di Febbo C, di Castelnuovo A, Bcante G, Amore C, Angelini A, et al. Association of factor VII levels with inflammatory parameters in hypercholesterolemic patients. Atherosclerosis 2002; 165: 159-63.
    • (2002) Atherosclerosis , vol.165 , pp. 159-163
    • Porreca, E.1    Di Febbo, C.2    di Castelnuovo, A.3    Bcante, G.4    Amore, C.5    Angelini, A.6
  • 159
    • 0033302805 scopus 로고    scopus 로고
    • Hypercoagulable state in hypercholesterolemic subjects assessed by platelet-dependent thrombin generation: In vitro effect of cerivasstatin
    • Puccetti L, Bruni F, Di Renzo M, Bova G, Cercignani M, Iadanza A, et al. Hypercoagulable state in hypercholesterolemic subjects assessed by platelet-dependent thrombin generation: in vitro effect of cerivasstatin. Eur Rev Med Pharmacol 1999; 3: 197-204.
    • (1999) Eur. Rev. Med. Pharmacol. , vol.3 , pp. 197-204
    • Puccetti, L.1    Bruni, F.2    Di Renzo, M.3    Bova, G.4    Cercignani, M.5    Iadanza, A.6
  • 160
    • 0033644736 scopus 로고    scopus 로고
    • Hypercoagulability in various autoimmune diseases: No association with factor V Leiden mutation
    • Regeczy N, Balogh I, Lakos G, Zeher M, Bodolay E, Szucs G, et al. Hypercoagulability in various autoimmune dieascs: no association with factor V Leiden mutation. Haematologia 2000; 30: 35-9.
    • (2000) Haematologia , vol.30 , pp. 35-39
    • Regeczy, N.1    Balogh, I.2    Lakos, G.3    Zeher, M.4    Bodolay, E.5    Szucs, G.6
  • 162
    • 0036092892 scopus 로고    scopus 로고
    • The hypercoagulable state in thalassemia
    • Eldor A, Rachmilewitz E. The hypercoagulable state in thalassemia. Blood 2002; 99: 36-43.
    • (2002) Blood , vol.99 , pp. 36-43
    • Eldor, A.1    Rachmilewitz, E.2
  • 164
    • 0030978428 scopus 로고    scopus 로고
    • Acquired isolated factor VII deficiency during sepsis
    • Biron C, Bengler C, Gris JC, Schved JF. Acquired isolated factor VII deficiency during sepsis. Haemostasis 1997; 27: 51-6.
    • (1997) Haemostasis , vol.27 , pp. 51-56
    • Biron, C.1    Bengler, C.2    Gris, J.C.3    Schved, J.F.4
  • 165
    • 0034924586 scopus 로고    scopus 로고
    • Rationale for restoration of physiological anticoagulant pathways in patients with sepsis and disseminated intravascular coagulation
    • Levi M, de Jonge E, van der Poll T. Rationale for restoration of physiological anticoagulant pathways in patients with sepsis and disseminated intravascular coagulation. Crit Care Ned 2001; 29: S0-90-4.
    • (2001) Crit. Care Ned. , vol.29
    • Levi, M.1    de Jonge, E.2    van der Poll, T.3
  • 166
  • 167
    • 0033901546 scopus 로고    scopus 로고
    • Thrombophilia in pregnancy
    • Walker ID. Thrombophilia in pregnancy. J Clin Pathol 2002; 53: 573-80.
    • (2002) J. Clin. Pathol. , vol.53 , pp. 573-580
    • Walker, I.D.1
  • 169
    • 0021363703 scopus 로고
    • The coagulation factor VII in pregnancy
    • Dalaker K, Prydz H. The coagulation factor VII in pregnancy. Br J Haematol 1984; 56: 233-41.
    • (1984) Br. J. Haematol. , vol.56 , pp. 233-241
    • Dalaker, K.1    Prydz, H.2
  • 170
    • 0030920155 scopus 로고    scopus 로고
    • Coagulation and fibrinolysis changes in normal pregnancy. Increased levels of procoagulants and reduced levels of inhibitors during pregnancy induce a hypercoagulable state, combined with a reactive fibrinolysis
    • Cerneca F, Ricci G, Simeone R, Malisano M, Alberico S, Guaschino S. Coagulation and fibrinolysis changes in normal pregnancy. Increased levels of procoagulants and reduced levels of inhibitors during pregnancy induce a hypercoagulable state, combined with a reactive fibrinolysis. Eur J Obstet Gynecol Reprod Biol 1997; 73: 31-6.
    • (1997) Eur. J. Obstet. Gynecol. Reprod. Biol. , vol.73 , pp. 31-36
    • Cerneca, F.1    Ricci, G.2    Simeone, R.3    Malisano, M.4    Alberico, S.5    Guaschino, S.6
  • 174
    • 0025511512 scopus 로고
    • A hypercoagulation syndrome in pregnancy due to an antithrombin III defect
    • Janku K, Penka MA hypercoagulation syndrome in pregnancy due to an antithrombin III defect. Cesk Gynecol 1990; 55: 657-60.
    • (1990) Cesk Gynecol. , vol.55 , pp. 657-660
    • Janku, K.1    Penka, M.2
  • 177
    • 0023571303 scopus 로고
    • Excessive deposition of fibrin, platelets and platelet thrombi on vascular subendothelium during contraceptive drug treatment
    • Inauen W, Baumgartner HR, Haeberli A, Straub PW. Excessive deposition of fibrin, platelets and platelet thrombi on vascular subendothelium during contraceptive drug treatment. Thromb Haemost 1987; 57: 306-9.
    • (1987) Thromb. Haemost. , vol.57 , pp. 306-309
    • Inauen, W.1    Baumgartner, H.R.2    Haeberli, A.3    Straub, P.W.4
  • 178
    • 0032705598 scopus 로고    scopus 로고
    • Low-oestrogen oral contraceptives as a major risk factor for cerebral venous and sinus thrombosis: Evidence from a clinical series
    • Buccino G, Scoditti U, Pini M, Tagliaferri AR, Manotti C, Mancia D. Low-oestrogen oral contraceptives as a major risk factor for cerebral venous and sinus thrombosis: evidence from a clinical series. Ital J Neurol Sci 1999; 20: 231-5.
    • (1999) Ital. J. Neurol. Sci. , vol.20 , pp. 231-235
    • Buccino, G.1    Scoditti, U.2    Pini, M.3    Tagliaferri, A.R.4    Manotti, C.5    Mancia, D.6
  • 179
    • 0032729747 scopus 로고    scopus 로고
    • Monocyte tissue factor expression is enhanced in women who smoke and use oral contraceptives
    • Holschermann H, Terhalle HM, Zakel U, Maus U, Parviz B, Tillmanns H, et al. Monocyte tissue factor expression is enhanced in women who smoke and use oral contraceptives. Thromb Haemost 1999; 82: 1614-20.
    • (1999) Thromb. Haemost. , vol.82 , pp. 1614-1620
    • Holschermann, H.1    Terhalle, H.M.2    Zakel, U.3    Maus, U.4    Parviz, B.5    Tillmanns, H.6
  • 180
    • 0025183051 scopus 로고
    • Clinical aspects of the relationship between oral contraceptives and abnormalities of the hemostasis system: Relation to the development of cardiovascular disease
    • Kelleher CC. Clinical aspects of the relationship between oral contraceptives and abnormalities of the hemostasis system: relation to the development of cardiovascular disease. Am J Obstet Gynecol 1990; 163: 392-5.
    • (1990) Am. J. Obstet. Gynecol. , vol.163 , pp. 392-395
    • Kelleher, C.C.1
  • 181
    • 0030860570 scopus 로고    scopus 로고
    • Epidemiology of coagulation factors, inhibitors and activation markers: The third Glasgow MONICA survey I. Illustrative reference ranges by age, sex and hormone use
    • Lowe GDO, Rumley A, Woodward M, Morrison CE, Philippou H, Lane DA, et al. Epidemiology of coagulation factors, inhibitors and activation markers: The third Glasgow MONICA survey I. Illustrative reference ranges by age, sex and hormone use. Br J Haematol 1997; 97: 775-84.
    • (1997) Br. J. Haematol. , vol.97 , pp. 775-784
    • Lowe, G.D.O.1    Rumley, A.2    Woodward, M.3    Morrison, C.E.4    Philippou, H.5    Lane, D.A.6
  • 182
    • 0032089069 scopus 로고    scopus 로고
    • Activated protein C resistance and deficiencies of antithrombin III, protein C or protein S and the risk of thromboembolic disease in users of oral contraceptives
    • Winkler UH. Activated protein C resistance and deficiencies of antithrombin III, protein C or protein S and the risk of thromboembolic disease in users of oral contraceptives. Eur J Contracept Reprod Health Care 1998; 3: 65-74.
    • (1998) Eur. J. Contracept. Reprod. Health Care , vol.3 , pp. 65-74
    • Winkler, U.H.1
  • 183
    • 0033401976 scopus 로고    scopus 로고
    • Biological coagulation findings in third-generation oral contraceptives
    • Conard J. Biological coagulation findings in third-generation oral contraceptives. Hum Reprod Update 1999; 5: 672-80.
    • (1999) Hum. Reprod. Update , vol.5 , pp. 672-680
    • Conard, J.1
  • 184
    • 0034084228 scopus 로고    scopus 로고
    • Effects on haemostasis variables by second and third generation combined oral contraceptives: A review of directly comparative studies
    • Kluft C. Effects on haemostasis variables by second and third generation combined oral contraceptives: a review of directly comparative studies. Curr Med Chem 2000; 7: 585-91.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 585-591
    • Kluft, C.1
  • 186
    • 0024312887 scopus 로고
    • Lipid metabolism and coagulation during the normal menstrual cycle
    • Lebech AM, Kjaer A. Lipid metabolism and coagulation during the normal menstrual cycle. Horm Metab Res 1989; 21: 445-8.
    • (1989) Horm. Metab. Res. , vol.21 , pp. 445-448
    • Lebech, A.M.1    Kjaer, A.2
  • 187
    • 0035002657 scopus 로고    scopus 로고
    • Hormone replacement therapy in healthy postmenpausal women: A randomized, placebo-controlled study of effects on coagulation and fibrinolytic factors
    • Gottsater A, Rendell M, Hulthen UL, Berntorp E, Mattiasson I. Hormone replacement therapy in healthy postmenpausal women: a randomized, placebo-controlled study of effects on coagulation and fibrinolytic factors. J Intern Med 2001; 249: 237-46.
    • (2001) J. Intern. Med. , vol.249 , pp. 237-246
    • Gottsater, A.1    Rendell, M.2    Hulthen, U.L.3    Berntorp, E.4    Mattiasson, I.5
  • 189
    • 0019510311 scopus 로고
    • Response of blood coagulation parameters to elevated endogenous 17 beta-estradiol levels induced by human menopausal gonadotropins
    • Kim HC, Kemmann E, Shelden RM, Saidi P. Response of blood coagulation parameters to elevated endogenous 17 beta-estradiol levels induced by human menopausal gonadotropins. Am J Obstet Gynecol 1981; 140: 807-10.
    • (1981) Am. J. Obstet. Gynecol. , vol.140 , pp. 807-810
    • Kim, H.C.1    Kemmann, E.2    Shelden, R.M.3    Saidi, P.4
  • 192
    • 0035218409 scopus 로고    scopus 로고
    • Disseminated intravascular coagulation in trauma patients
    • Gando S. Disseminated intravascular coagulation in trauma patients. Semin Thromb Hemost 2001; 27: 585-92.
    • (2001) Semin. Thromb. Hemost. , vol.27 , pp. 585-592
    • Gando, S.1
  • 194
    • 0036165560 scopus 로고    scopus 로고
    • Effect of tissue injury on D-Dimer levels: A prospective study in trauma patients
    • Johna S, Cemaj S, O'Callaghan T, Catalano R.Effect of tissue injury on D-Dimer levels: a prospective study in trauma patients. Med Sci Monit 2002; 8: CR5-CR8.
    • (2002) Med. Sci. Monit. , vol.8
    • Johna, S.1    Cemaj, S.2    O'Callaghan, T.3    Catalano, R.4
  • 196
    • 0036089510 scopus 로고    scopus 로고
    • Injury induces increased monocyte expression of tissue factor: Factors associated with head injury attenuate the injury-related monocyte expression of tissue factor
    • Utter GH, Owings JT, Jacoby RC, Gosselin RC, Paglieroni TG. Injury induces increased monocyte expression of tissue factor: factors associated with head injury attenuate the injury-related monocyte expression of tissue factor. J Trauma 2002; 52: 1071-7.
    • (2002) J. Trauma , vol.52 , pp. 1071-1077
    • Utter, G.H.1    Owings, J.T.2    Jacoby, R.C.3    Gosselin, R.C.4    Paglieroni, T.G.5
  • 198
    • 0024392043 scopus 로고
    • Postoperative changes in hemostasis analyzed by the serial determination of fibrinopeptides and D-dimer
    • Kang J, Kambayashi J, Sakon M, Tsujinaka T, Mori T. Postoperative changes in hemostasis analyzed by the serial determination of fibrinopeptides and D-dimer. Jpn J Surg 1989; 19: 262-8.
    • (1989) Jpn. J. Surg. , vol.19 , pp. 262-268
    • Kang, J.1    Kambayashi, J.2    Sakon, M.3    Tsujinaka, T.4    Mori, T.5
  • 202
    • 0030942790 scopus 로고    scopus 로고
    • Monocyte tissue factor expression, cell activation, and thrombin generation during cardiopulmonary bypass: A clinical study
    • Ernofsson M, Thelin S, Siegbahn A. Monocyte tissue factor expression, cell activation, and thrombin generation during cardiopulmonary bypass: a clinical study. J Thorac Cardiovasc Surg 1997; 113: 576-84.
    • (1997) J. Thorac. Cardiovasc. Surg. , vol.113 , pp. 576-584
    • Ernofsson, M.1    Thelin, S.2    Siegbahn, A.3
  • 203
    • 0033934056 scopus 로고    scopus 로고
    • Tissue factor is rapidly elevated in plasma collected from the pericardial cavity during cardiopulmonary bypass
    • Philippou H, Adami A, Davidson SJ, Pepper JR, Burman JF, Lane DA. Tissue factor is rapidly elevated in plasma collected from the pericardial cavity during cardiopulmonary bypass. Thromb Haemost 2000; 84: 124-8.
    • (2000) Thromb. Haemost. , vol.84 , pp. 124-128
    • Philippou, H.1    Adami, A.2    Davidson, S.J.3    Pepper, J.R.4    Burman, J.F.5    Lane, D.A.6
  • 205
    • 0037804799 scopus 로고    scopus 로고
    • Estimating the rate of thrombin and fibrin generation in vivo during cardiopulmonary bypass
    • Chandler WL, Velan T. Estimating the rate of thrombin and fibrin generation in vivo during cardiopulmonary bypass. Blood 2003; 101: 4355-62.
    • (2003) Blood , vol.101 , pp. 4355-4362
    • Chandler, W.L.1    Velan, T.2
  • 207
    • 0034638705 scopus 로고    scopus 로고
    • Association between acute hypobaric hypoxoa and activation of coagulation in human beings
    • Bendz B, Rostrup M, Sevre K, Andersen TO, Sandset PM. Association between acute hypobaric hypoxoa and activation of coagulation in human beings. Lancet 2000; 356: 1657-8.
    • (2000) Lancet , vol.356 , pp. 1657-1658
    • Bendz, B.1    Rostrup, M.2    Sevre, K.3    Andersen, T.O.4    Sandset, P.M.5
  • 208
    • 15144351713 scopus 로고    scopus 로고
    • Tissue factor is associated with the nonbacterial thrombotic endocarditis induced by a hypobaric hypoxic environment in rats
    • Nakanishi K, Tajima F, Nakata Y, Osada H, Ogata K, Kawai T, et al. Tissue factor is associated with the nonbacterial thrombotic endocarditis induced by a hypobaric hypoxic environment in rats. Virchows Arch 1998; 433: 375-9.
    • (1998) Virchows Arch. , vol.433 , pp. 375-379
    • Nakanishi, K.1    Tajima, F.2    Nakata, Y.3    Osada, H.4    Ogata, K.5    Kawai, T.6
  • 209
    • 0034897486 scopus 로고    scopus 로고
    • Low molecular weight heparin prevents activation of coagulation in a hypobaric environment
    • Bendz B, Sevre K, Andersen TO, Sandset PM. Low molecular weight heparin prevents activation of coagulation in a hypobaric environment. Blood Coagul Fibrinolysis 2001; 12: 371-4.
    • (2001) Blood Coagul. Fibrinolysis , vol.12 , pp. 371-374
    • Bendz, B.1    Sevre, K.2    Andersen, T.O.3    Sandset, P.M.4
  • 210
    • 0023154903 scopus 로고
    • Fibrinogen, cigarette smoking, and risk of cardiovascular disease: Insights from the Framington Study
    • Kannel WB, D'Agostino RB, Belanger AJ. Fibrinogen, cigarette smoking, and risk of cardiovascular disease: insights from the Framington Study. Am Heart J 1987; 113: 1006- 10.
    • (1987) Am. Heart J. , vol.113 , pp. 1006-1010
    • Kannel, W.B.1    D'Agostino, R.B.2    Belanger, A.J.3
  • 211
    • 0030761812 scopus 로고    scopus 로고
    • Epidemiology of coagulation factors, inhibitors and activation markers: The third Glasgow MONICA survey II. Relationships to cardiovascular risk factors and prevalent cardiovascular disease
    • Woodward M, Lowe GDO, Rumley A, Tunstall-Pedoe H, Philippou H, Lane DA, et al. Epidemiology of coagulation factors, inhibitors and activation markers: The third Glasgow MONICA survey II. Relationships to cardiovascular risk factors and prevalent cardiovascular disease. Br J Haematol 1997; 97: 785-97.
    • (1997) Br. J. Haematol. , vol.97 , pp. 785-797
    • Woodward, M.1    Lowe, G.D.O.2    Rumley, A.3    Tunstall-Pedoe, H.4    Philippou, H.5    Lane, D.A.6
  • 212
    • 0028237114 scopus 로고
    • Thrombin generation as an acute effect of cigarette smoking
    • Kimura S, Nishinaga M, Ozawa T, Shimada K. Thrombin generation as an acute effect of cigarette smoking. Am Heart J 1994; 128: 7-11.
    • (1994) Am. Heart J. , vol.128 , pp. 7-11
    • Kimura, S.1    Nishinaga, M.2    Ozawa, T.3    Shimada, K.4
  • 213
    • 0034121768 scopus 로고    scopus 로고
    • The effect of alcohol ingestion on the exercise-induced changes in fibrin and fibrinogen degradation products in man
    • El-Sayed MS, Nieuwenhuizen W. The effect of alcohol ingestion on the exercise-induced changes in fibrin and fibrinogen degradation products in man. Blood Coagul Fibrinolysis 2000; 11: 359-65.
    • (2000) Blood Coagul. Fibrinolysis , vol.11 , pp. 359-365
    • El-Sayed, M.S.1    Nieuwenhuizen, W.2
  • 215
  • 217
    • 0031571110 scopus 로고    scopus 로고
    • Daily supplementation with MaxEPA suppresses bacterial endotoxin-inducible procoagulation in dogs
    • Chu AJ, Moore J, Sampell RM. Daily supplementation with MaxEPA suppresses bacterial endotoxin-inducible procoagulation in dogs. J Surg Res 1997; 71: 93-9.
    • (1997) J. Surg. Res. , vol.71 , pp. 93-99
    • Chu, A.J.1    Moore, J.2    Sampell, R.M.3
  • 219
    • 0035137644 scopus 로고    scopus 로고
    • A stearic acid-rich diet improves thrombogenic and atherogenic risk factor profiles in healthy mates
    • Kelly FD, Sinclair AJ, Mann NJ, Turner AH, Abedin L, Li D. A stearic acid-rich diet improves thrombogenic and atherogenic risk factor profiles in healthy mates. Eur J Clin Nutr 2001; 55: 88-96.
    • (2001) Eur. J. Clin. Nutr. , vol.55 , pp. 88-96
    • Kelly, F.D.1    Sinclair, A.J.2    Mann, N.J.3    Turner, A.H.4    Abedin, L.5    Li, D.6
  • 220
    • 0032935334 scopus 로고    scopus 로고
    • The thrombophilic state induced by therapeutic agents in the cancer patient
    • Lee AY, Levine MN. The thrombophilic state induced by therapeutic agents in the cancer patient. Semin Thromb Haemost 1999; 25: 137-45.
    • (1999) Semin. Thromb. Haemost. , vol.25 , pp. 137-145
    • Lee, A.Y.1    Levine, M.N.2
  • 221
    • 0025650987 scopus 로고
    • The induction of a hypercoagulable state by medroxyprogesterone acetate in breast cancer patients
    • Fukutomi T, Naasawa T, Yamamoto H, Adachi I, Watanabe T. The induction of a hypercoagulable state by medroxyprogesterone acetate in breast cancer patients. Jpn J Surg 1990; 20: 665-70.
    • (1990) Jpn. J. Surg. , vol.20 , pp. 665-670
    • Fukutomi, T.1    Naasawa, T.2    Yamamoto, H.3    Adachi, I.4    Watanabe, T.5
  • 222
    • 0027732767 scopus 로고
    • The influence of tamoxifen in vivo on the main natural anticoagulants and fibrinolysis
    • Pemberton KD, Melissari E, Kakkar VV. The influence of tamoxifen in vivo on the main natural anticoagulants and fibrinolysis. Blood Coagul Fibrinolysis 1993; 4: 935-42.
    • (1993) Blood Coagul. Fibrinolysis , vol.4 , pp. 935-942
    • Pemberton, K.D.1    Melissari, E.2    Kakkar, V.V.3
  • 224
    • 0020678228 scopus 로고
    • L-asparaginase induces antithrombin III deficiency: Evidence against the production of a hypercoagulable state
    • Bauer KA, Teitel JM, Rosenberg RD. L-asparaginase induces antithrombin III deficiency: evidence against the production of a hypercoagulable state. Thromb Res 1983; 29: 437-42.
    • (1983) Thromb. Res. , vol.29 , pp. 437-442
    • Bauer, K.A.1    Teitel, J.M.2    Rosenberg, R.D.3
  • 229
    • 0026331883 scopus 로고
    • High frequency of antithrombin III and protein C deficiency following autologous bone marrow transplantation for lymphoma
    • Gordon B, Haire W, Kessinger A, Duggan M, Armitage J. High frequency of antithrombin III and protein C deficiency following autologous bone marrow transplantation for lymphomaBone Marrow Transplant 1991; 8: 497-502.
    • (1991) Bone Marrow Transplant. , vol.8 , pp. 497-502
    • Gordon, B.1    Haire, W.2    Kessinger, A.3    Duggan, M.4    Armitage, J.5
  • 230
    • 0030761592 scopus 로고    scopus 로고
    • Prethrombotic state due to hypercoagulability in patients with permanent transvenous pacemarkers
    • Ito T, Tanouchi J, Kato J, Nishino M, Iwai K, Tanahashi H, et al. Prethrombotic state due to hypercoagulability in patients with permanent transvenous pacemarkers. Angiology 1997; 48: 901-6.
    • (1997) Angiology , vol.48 , pp. 901-906
    • Ito, T.1    Tanouchi, J.2    Kato, J.3    Nishino, M.4    Iwai, K.5    Tanahashi, H.6
  • 232
    • 0025322455 scopus 로고
    • Blood coagulation after long distance running: Antithrombin III prevents fibrin formation
    • Bartsch P, Haeberli A, Straub PW. Blood coagulation after long distance running: antithrombin III prevents fibrin formation. Thromb Haemost 1990; 63: 430-4.
    • (1990) Thromb. Haemost. , vol.63 , pp. 430-434
    • Bartsch, P.1    Haeberli, A.2    Straub, P.W.3
  • 233
  • 236
    • 0036784722 scopus 로고    scopus 로고
    • Hemodilution with albumin, but not hextend ®, results in hypercoagulability as assessed by thrombelastography in rabbit: Role of heparin-dependent seroins and factor VIII complex
    • McCammon AT, Wright JP, Figueroa M, Nielsen VG. Hemodilution with albumin, but not hextend ®, results in hypercoagulability as assessed by thrombelastography in rabbit: Role of heparin-dependent seroins and factor VIII complex. Anesth Analg 2002; 95: 844-50.
    • (2002) Anesth. Analg. , vol.95 , pp. 844-850
    • McCammon, A.T.1    Wright, J.P.2    Figueroa, M.3    Nielsen, V.G.4
  • 237
    • 0032447678 scopus 로고    scopus 로고
    • Natural anticoagulants, aging, and thromboembolism
    • Sagripanti A, Carpi A. Natural anticoagulants, aging, and thromboembolism. Exp Gerontol 1998; 33: 891-6.
    • (1998) Exp. Gerontol. , vol.33 , pp. 891-896
    • Sagripanti, A.1    Carpi, A.2
  • 239
    • 0028904792 scopus 로고
    • Fibrin degradation product concentration (D-dimers) in the course of ageing
    • Hager K, Platt D. Fibrin degradation product concentration (D-dimers) in the course of ageing. Gerontology 1995; 41: 159-65.
    • (1995) Gerontology , vol.41 , pp. 159-165
    • Hager, K.1    Platt, D.2
  • 242
    • 0027422176 scopus 로고
    • Lipid-related hemostatic abnormalities in the elderly: Imbalance between coagulation and fibrinolysis
    • Kario K, Matsuo T. Lipid-related hemostatic abnormalities in the elderly: imbalance between coagulation and fibrinolysis. Atherosclerosis 1993; 103: 131-8.
    • (1993) Atherosclerosis , vol.103 , pp. 131-138
    • Kario, K.1    Matsuo, T.2
  • 243
    • 0025963647 scopus 로고
    • Factor VII hyperactivity in the elderly
    • Kario K, Matsuo T, Nakao K. Factor VII hyperactivity in the elderly. Thromb Haemost 199 1; 65: 25-7.
    • (1991) Thromb. Haemost. , vol.65 , pp. 25-27
    • Kario, K.1    Matsuo, T.2    Nakao, K.3
  • 244
    • 0028490523 scopus 로고
    • High factor VII activity in the elderly is related to vascular disease through activation of the coagulation system
    • Karin K, Matsuo T. High factor VII activity in the elderly is related to vascular disease through activation of the coagulation system. J Cardiovasc Risk 1994; 1: 165-71.
    • (1994) J. Cardiovasc. Risk , vol.1 , pp. 165-171
    • Karin, K.1    Matsuo, T.2
  • 245
    • 0026625147 scopus 로고
    • Heparin cofactor deficiency in the elderly: Comparison with antithrombin III
    • Kario K, Matsuo T, Kobayashi H. Heparin cofactor deficiency in the elderly: comparison with antithrombin III. Thromb Res 1992; 66: 489-98.
    • (1992) Thromb. Res. , vol.66 , pp. 489-498
    • Kario, K.1    Matsuo, T.2    Kobayashi, H.3
  • 247
    • 0028867012 scopus 로고
    • Effects of aging on the synthesis of antithrombin-binding sites on heparin chains and heparan sulphate chains in the rat
    • Horner AA. Effects of aging on the synthesis of antithrombin-binding sites on heparin chains and heparan sulphate chains in the rat. Biochem J 1995; 312: 245-9.
    • (1995) Biochem. J. , vol.312 , pp. 245-249
    • Horner, A.A.1
  • 248
    • 0035216020 scopus 로고    scopus 로고
    • Anticoagulant factor concentrates in disseminated intravascular coagulation: Rationale for use and clinical experience
    • de Jonge E, van der Poll T, Kesecioglu J, Levi M. Anticoagulant factor concentrates in disseminated intravascular coagulation: rationale for use and clinical experience. Semin. Thromb Hemost 2001; 27: 667-74.
    • (2001) Semin. Thromb. Hemost. , vol.27 , pp. 667-674
    • de Jonge, E.1    van der Poll, T.2    Kesecioglu, J.3    Levi, M.4
  • 249
    • 0027475222 scopus 로고
    • Complex-dependent inhibition of factor FVIIa by antithrombin III and heparin
    • Lawson JH, Butenas S, Ribarik N, Mann KG. Complex-dependent inhibition of factor FVIIa by antithrombin III and heparin. J Biol Chem 1993; 268: 767-70.
    • (1993) J. Biol. Chem. , vol.268 , pp. 767-770
    • Lawson, J.H.1    Butenas, S.2    Ribarik, N.3    Mann, K.G.4
  • 250
    • 0031081697 scopus 로고    scopus 로고
    • Mechanism of thrombin inhibition by antithrombin and heparin cofactor II in the presence of heparin
    • Maaroufi RM, Jozefowicz M, Tapon-Bretaudiere J, Fischer AM. Mechanism of thrombin inhibition by antithrombin and heparin cofactor II in the presence of heparin. Biomaterials 1997; 18: 203-11.
    • (1997) Biomaterials , vol.18 , pp. 203-211
    • Maaroufi, R.M.1    Jozefowicz, M.2    Tapon-Bretaudiere, J.3    Fischer, A.M.4
  • 252
    • 0025146426 scopus 로고
    • Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors
    • Weitz JI, Hudoba M, Massel D, Maraganore J, Hirsh J. Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors. J Clin Invest 1991; 86: 385-91.
    • (1991) J. Clin. Invest. , vol.86 , pp. 385-391
    • Weitz, J.I.1    Hudoba, M.2    Massel, D.3    Maraganore, J.4    Hirsh, J.5
  • 253
    • 0032509526 scopus 로고    scopus 로고
    • Covalent heparin cofactor II-heparin and heparin cofactor-dermatan sulfate complexes. Characterization of novel anticoagulants
    • Monagle P, Berry L, O'Brodovich H, Andrew M, Chan A. Covalent heparin cofactor II-heparin and heparin cofactor-dermatan sulfate complexes. Characterization of novel anticoagulants. J Biol Chem 1998; 273: 33566-71.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33566-33571
    • Monagle, P.1    Berry, L.2    O'Brodovich, H.3    Andrew, M.4    Chan, A.5
  • 254
    • 0028200016 scopus 로고
    • Prevention of thrombus formation and growth by antithrombin III and heparin cofactor II-dependent thrombin inhibitors: Importance of heparin cofactor II
    • Buchanan MR, Liao P, Smith LJ, Ofosu FA. Prevention of thrombus formation and growth by antithrombin III and heparin cofactor II-dependent thrombin inhibitors: importance of heparin cofactor II. Thromb Res 1994; 74: 463-75.
    • (1994) Thromb. Res. , vol.74 , pp. 463-475
    • Buchanan, M.R.1    Liao, P.2    Smith, L.J.3    Ofosu, F.A.4
  • 257
  • 258
    • 0028556587 scopus 로고
    • Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans
    • Sheehan JP, Tollefsen DM, Sadler JE. Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans. J Biol Chem 1994; 269: 32747-51.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32747-32751
    • Sheehan, J.P.1    Tollefsen, D.M.2    Sadler, J.E.3
  • 259
    • 0037143655 scopus 로고    scopus 로고
    • Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism
    • Baglin TP, Carrell RW, Church FC, Esmon CT, Huntington JA. Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. Proc Natl Acad Sci USA 2002; 99: 11079-84.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11079-11084
    • Baglin, T.P.1    Carrell, R.W.2    Church, F.C.3    Esmon, C.T.4    Huntington, J.A.5
  • 260
    • 0035869411 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor play an important role in protein C activation
    • Taylor FB, Peer GT, Lockhart MS, Ferrell G, Esmon CT. Endothelial cell protein C receptor play an important role in protein C activation. Blood 2001; 97: 1685-8.
    • (2001) Blood , vol.97 , pp. 1685-1688
    • Taylor, F.B.1    Peer, G.T.2    Lockhart, M.S.3    Ferrell, G.4    Esmon, C.T.5
  • 261
    • 0028110027 scopus 로고
    • The mechanism of inactivation of human factor V and human factor Va by activated protein C
    • Kalafatis M, Rand MD, Mann KG. The mechanism of inactivation of human factor V and human factor Va by activated protein C. J Biol Chem 1994; 269: 31869-80.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31869-31880
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 262
    • 0025888388 scopus 로고
    • Activated protein C-catalyzed inactivation of human factor VIII and factor VIIIa
    • Fay PJ, Smudzin TM, Walker FJ. Activated protein C-catalyzed inactivation of human factor VIII and factor VIIIa. J Biol Chem 1991; 266: 20139-45.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20139-20145
    • Fay, P.J.1    Smudzin, T.M.2    Walker, F.J.3
  • 263
    • 0028290275 scopus 로고
    • Factor V and protein S as synergistic cofactors to activated protein C in degradation of factor VIIIa
    • Shen L, Dahlback B. Factor V and protein S as synergistic cofactors to activated protein C in degradation of factor VIIIa. J Biol Chem 1994; 269: 18735-38.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18735-18738
    • Shen, L.1    Dahlback, B.2
  • 264
    • 0036086486 scopus 로고    scopus 로고
    • Role of tissue factor pathway inhibitor in the regulation of tissue factor-dependent blood coagulation
    • Golino P, Ragni M, Cimmino G, Forte L. Role of tissue factor pathway inhibitor in the regulation of tissue factor-dependent blood coagulation. Cardiovasc Drug Rev 2002; 20: 67-80.
    • (2002) Cardiovasc. Drug. Rev. , vol.20 , pp. 67-80
    • Golino, P.1    Ragni, M.2    Cimmino, G.3    Forte, L.4
  • 265
    • 0027724106 scopus 로고
    • Kinetics of factor Xa inhibition by tissue factor pathway inhibitor
    • Huang ZF, Wun TC, Broze GJ Jr. Kinetics of factor Xa inhibition by tissue factor pathway inhibitor. J Biol Chem 1993; 268: 26950-5.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26950-26955
    • Huang, Z.F.1    Wun, T.C.2    Broze Jr., G.J.3
  • 266
    • 0034459007 scopus 로고    scopus 로고
    • Physiological function of tissue factor pathway inhibitor and interaction with heparins
    • Sandset PM, Bendz B, Hansen JB. Physiological function of tissue factor pathway inhibitor and interaction with heparins. Haemostasis 2000; 30: 48-56.
    • (2000) Haemostasis , vol.30 , pp. 48-56
    • Sandset, P.M.1    Bendz, B.2    Hansen, J.B.3
  • 267
    • 0029074965 scopus 로고
    • Tissue factor pathway inhibitor: Proposed heparin recognition region
    • Harenberg J, Malsch R, Heene DL. Tissue factor pathway inhibitor: proposed heparin recognition region. Blood Coagul Fibrinolysis 1995; 6(S): S50-60.
    • (1995) Blood Coagul. Fibrinolysis , vol.6 , Issue.SUPPL.
    • Harenberg, J.1    Malsch, R.2    Heene, D.L.3
  • 268
    • 0029040795 scopus 로고
    • The role of tissue factor pathway inhibitor in the mediateion of the antithrombotic actions of heparin and low-molecular-weight heparin
    • Hoppensteadt DA, Jeske W, Fareed J, Bermes EW Jr. The role of tissue factor pathway inhibitor in the mediateion of the antithrombotic actions of heparin and low-molecular-weight heparin. Blood Coagul Fibrinolysis 1995; 6(S): S57-64.
    • (1995) Blood Coagul. Fibrinolysis , vol.6 , Issue.SUPPL.
    • Hoppensteadt, D.A.1    Jeske, W.2    Fareed, J.3    Bermes Jr., E.W.4
  • 269
    • 0025222311 scopus 로고
    • Cultured normal human hepatocytes do not synthesize lipoprotein-associated coagulation inhibitor: Evidence that endothelium is the principal site of its synthesis
    • Bajaj MS, Kuppuswamy MN, Saito H, Spitzer SG, Bajaj SP. Cultured normal human hepatocytes do not synthesize lipoprotein-associated coagulation inhibitor: Evidence that endothelium is the principal site of its synthesis. Proc Natl Acad Sci USA 1990; 87: 8869-73.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8869-8873
    • Bajaj, M.S.1    Kuppuswamy, M.N.2    Saito, H.3    Spitzer, S.G.4    Bajaj, S.P.5
  • 270
    • 0028342419 scopus 로고
    • Simultaneous expression of tissue factor and tissue factor pathway inhibitor by human monocytes. A potential mechanism for localized control of blood coagulation
    • McGee MP, Foster S, Wang X. Simultaneous expression of tissue factor and tissue factor pathway inhibitor by human monocytes. A potential mechanism for localized control of blood coagulation. J Exp Med 1994; 179: 1847-54.
    • (1994) J. Exp. Med. , vol.179 , pp. 1847-1854
    • McGee, M.P.1    Foster, S.2    Wang, X.3
  • 271
    • 0023219464 scopus 로고
    • Binding of thrombin to thrombomodulin accelerates inhibition of the enzyme by antithrombin III. Evidence for heparin-independent mechanism
    • Preissner KT, Delvos U, Muller-Berghaus G. Binding of thrombin to thrombomodulin accelerates inhibition of the enzyme by antithrombin III. Evidence for heparin-independent mechanism. Biochemistry 1987; 26: 2521-28.
    • (1987) Biochemistry , vol.26 , pp. 2521-2528
    • Preissner, K.T.1    Delvos, U.2    Muller-Berghaus, G.3
  • 272
    • 0029022461 scopus 로고
    • The effect of lipid peroxidation and lipolysis on the ability of lipoproteins to influence thromboplastin activity
    • Ettelaie C, Howell RM, Bruckdorfer KR. The effect of lipid peroxidation and lipolysis on the ability of lipoproteins to influence thromboplastin activity. Biochim Biophys Acta 1995; 1257: 25-30.
    • (1995) Biochim Biophys. Acta , vol.1257 , pp. 25-30
    • Ettelaie, C.1    Howell, R.M.2    Bruckdorfer, K.R.3
  • 274
    • 0032527681 scopus 로고    scopus 로고
    • Identification of a domain in apolipoprotein B-100 that inhibits the procoagulant activity of tissue factor
    • Ettelaie C, James NJ, Adams JM, Nicola KP, Wilbourn B, Bruckdorfer KR. Identification of a domain in apolipoprotein B-100 that inhibits the procoagulant activity of tissue factor. Biochem J 1998; 333: 433-8.
    • (1998) Biochem. J. , vol.333 , pp. 433-438
    • Ettelaie, C.1    James, N.J.2    Adams, J.M.3    Nicola, K.P.4    Wilbourn, B.5    Bruckdorfer, K.R.6
  • 275
    • 0026470849 scopus 로고
    • The inhibition of thromboplastin by apolipoprotein B and the effect of various lipids
    • Ettelaie C, Howell RM. The inhibition of thromboplastin by apolipoprotein B and the effect of various lipids. Thromb Res 1992; 68: 175-84.
    • (1992) Thromb. Res. , vol.68 , pp. 175-184
    • Ettelaie, C.1    Howell, R.M.2
  • 277
    • 0019855312 scopus 로고
    • Plasma high density lipoproteins inhibit the activation of coagulation factor X by factor VIIa and tissue factor
    • Carson SD. Plasma high density lipoproteins inhibit the activation of coagulation factor X by factor VIIa and tissue factor. FEBS Letts 1981; 132: 37-40.
    • (1981) FEBS Letts , vol.132 , pp. 37-40
    • Carson, S.D.1
  • 278
    • 0023153160 scopus 로고
    • Tissue factor (coagulation factor III) inhibition by apolipoprotein A-II
    • Carson SD. Tissue factor (coagulation factor III) inhibition by apolipoprotein A-II. J Biol Chem 1987; 262: 718-21.
    • (1987) J. Biol. Chem. , vol.262 , pp. 718-721
    • Carson, S.D.1
  • 279
    • 3042802599 scopus 로고
    • New inhibitors of the first stage of blood clotting process
    • Hecht E. New inhibitors of the first stage of blood clotting process. Nature 1951; 167: 279-80.
    • (1951) Nature , vol.167 , pp. 279-280
    • Hecht, E.1
  • 280
    • 0343610888 scopus 로고
    • Sphingosine as an inhibitor of blood clotting
    • Hecht E, Shapiro D.Sphingosine as an inhibitor of blood clotting. Science 1957; 125: 1041-41.
    • (1957) Science , vol.125 , pp. 1041-1141
    • Hecht, E.1    Shapiro, D.2
  • 282
    • 0024459042 scopus 로고
    • Sphingosine inhibits monocyte tissue factor-initiated coagulation by altering factor VII binding
    • Conkling PR, Patton KL, Hannun YA, Greenberg CS, Weinberg JB. Sphingosine inhibits monocyte tissue factor-initiated coagulation by altering factor VII binding. J Biol Chem 1989; 264: 18440-44.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18440-18444
    • Conkling, P.R.1    Patton, K.L.2    Hannun, Y.A.3    Greenberg, C.S.4    Weinberg, J.B.5
  • 283
    • 0036040222 scopus 로고    scopus 로고
    • Possible role of Marcks in the cellular modulation of monocytic tissue factor-initiated hypercoagulation
    • Chu AJ, Lin S-H, Piasentin E. Possible role of Marcks in the cellular modulation of monocytic tissue factor-initiated hypercoagulation. Br J Haematol 2002; 118: 569-76.
    • (2002) Br. J. Haematol. , vol.118 , pp. 569-576
    • Chu, A.J.1    Lin, S.-H.2    Piasentin, E.3
  • 284
    • 0033382739 scopus 로고    scopus 로고
    • Contributions of GIA and EGF-like domains to the functions of vitamin K-dependent coagulation factors
    • Stenflo J. Contributions of GIA and EGF-like domains to the functions of vitamin K-dependent coagulation factors. Crit Rev Eukaryotic Gene Expr 1999; 9: 59-88.
    • (1999) Crit. Rev. Eukaryotic Gene Expr. , vol.9 , pp. 59-88
    • Stenflo, J.1
  • 285
    • 0027954408 scopus 로고
    • A monoclonal antibody against rabbit tissue factor inhibits thrombus formation in sterotic injured rabbit carotid arteries
    • Pawashe AB, Golino P, Ambrosio F, Ragni M, Pascucci I, Chiariello M, et al. A monoclonal antibody against rabbit tissue factor inhibits thrombus formation in sterotic injured rabbit carotid arteries. Cir Res 1994; 74: 56-63.
    • (1994) Cir. Res. , vol.74 , pp. 56-63
    • Pawashe, A.B.1    Golino, P.2    Ambrosio, F.3    Ragni, M.4    Pascucci, I.5    Chiariello, M.6
  • 286
    • 0028006127 scopus 로고
    • Inhibition of endotoxin-indced activation of coagulation and fibrinolysis by pentoxifylline or by a monoclonal anti-tissue factor antibody in chimpanzees
    • Levi M, ten Cate H, Bauer KA, van der Poll T, Edgington TS, Buller HR, et al. Inhibition of endotoxin-indced activation of coagulation and fibrinolysis by pentoxifylline or by a monoclonal anti-tissue factor antibody in chimpanzees. J Clin Invest 1994; 93: 114-20.
    • (1994) J. Clin. Invest. , vol.93 , pp. 114-120
    • Levi, M.1    ten Cate, H.2    Bauer, K.A.3    van der Poll, T.4    Edgington, T.S.5    Buller, H.R.6
  • 287
    • 0033753712 scopus 로고    scopus 로고
    • IV. Anticoagulant activity of compound 48/80: Inhibition of factor VII activation in Leukemia THP-1 monocytes
    • Chu AJ, Wang ZG, Raphael UO. IV. Anticoagulant activity of compound 48/80: Inhibition of factor VII activation in Leukemia THP-1 monocytes. J Cardiovasc Pharmacol 2000; 36: 649-55.
    • (2000) J. Cardiovasc. Pharmacol. , vol.36 , pp. 649-655
    • Chu, A.J.1    Wang, Z.G.2    Raphael, U.O.3
  • 288
    • 0034535492 scopus 로고    scopus 로고
    • Epitope location on tissue factor determines the anticoagulant potency of monoclonal anti-tissue factor antibodies
    • Kirchhofer D, Moran P, Chiang N, Kim J, Riederer MA, Eigenbrot C, Kelley RF. Epitope location on tissue factor determines the anticoagulant potency of monoclonal anti-tissue factor antibodies. Thromb Haemost 2000; 84: 1072-81.
    • (2000) Thromb. Haemost. , vol.84 , pp. 1072-1081
    • Kirchhofer, D.1    Moran, P.2    Chiang, N.3    Kim, J.4    Riederer, M.A.5    Eigenbrot, C.6    Kelley, R.F.7
  • 289
    • 0035083274 scopus 로고    scopus 로고
    • Generation of a humanized, high affinity anti-tissue factor antibody for use as a novel antithrombotic therapeutics
    • Presta L, Sims P, Meng YG, Moran P, Bullens S, Bunting S, et al. Generation of a humanized, high affinity anti-tissue factor antibody for use as a novel antithrombotic therapeutics. Thromb Haemost 2001; 85: 379-89.
    • (2001) Thromb. Haemost. , vol.85 , pp. 379-389
    • Presta, L.1    Sims, P.2    Meng, Y.G.3    Moran, P.4    Bullens, S.5    Bunting, S.6
  • 290
    • 0016428569 scopus 로고
    • Concanavalin A inhibits tissue factor coagulation activity
    • Pitlick FA. Concanavalin A inhibits tissue factor coagulation activity. J Clin Invest 1975; 55: 175-9.
    • (1975) J. Clin. Invest. , vol.55 , pp. 175-179
    • Pitlick, F.A.1
  • 291
    • 0000095572 scopus 로고    scopus 로고
    • I. Suppression by compound 48/80 of bacterial endotoxin-inducible monocytic tissue factor activation: Direct blockade of Factor VII binding to THP-1 monocytes
    • Chu AJ, Walton MA, Seto A, Fox MJ, Prasad JK, Wang ZG. I. Suppression by compound 48/80 of bacterial endotoxin-inducible monocytic tissue factor activation: direct blockade of Factor VII binding to THP-1 monocytes. Biochim Biophys Acta 1999; 1472: 386-95.
    • (1999) Biochim. Biophys. Acta , vol.1472 , pp. 386-395
    • Chu, A.J.1    Walton, M.A.2    Seto, A.3    Fox, M.J.4    Prasad, J.K.5    Wang, Z.G.6
  • 292
    • 0034658664 scopus 로고    scopus 로고
    • III. Instantaneous inhibition by compound 48/80 of tissue factor-initiated coagulation is mediated by the downregulation of factor VII activation
    • Chu AJ, Wang ZG, Fox MJ. III. Instantaneous inhibition by compound 48/80 of tissue factor-initiated coagulation is mediated by the downregulation of factor VII activation. Arch Biochem Biophys 2000; 377: 357-65.
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 357-365
    • Chu, A.J.1    Wang, Z.G.2    Fox, M.J.3
  • 293
    • 0036489910 scopus 로고    scopus 로고
    • Novel anticoagulant activity of polybrene: Inhibition of monocytic tissue factor hypercoagulation following bacterial endotoxin induction
    • Chu AJ, Rauci M, Nwobi OI, Mathews ST, Beydoun S. Novel anticoagulant activity of polybrene: Inhibition of monocytic tissue factor hypercoagulation following bacterial endotoxin induction. Blood Coagul Fibrinolysis 2002; 13: 123-8.
    • (2002) Blood Coagul. Fibrinolysis , vol.13 , pp. 123-128
    • Chu, A.J.1    Rauci, M.2    Nwobi, O.I.3    Mathews, S.T.4    Beydoun, S.5
  • 294
    • 0035424526 scopus 로고    scopus 로고
    • Antimicrobial peptide Buforin I inhibits tissue factor-initiated coagulation
    • Chu AJ, Chen BM, Lin H, Beydoun S. Antimicrobial peptide Buforin I inhibits tissue factor-initiated coagulation. Arch Biochem Biophys 2001; 392: 3-7.
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 3-7
    • Chu, A.J.1    Chen, B.M.2    Lin, H.3    Beydoun, S.4
  • 295
  • 296
    • 0034939348 scopus 로고    scopus 로고
    • Blockade by ruthenium red of tissue factor-initiated coagulation
    • Chu AJ, Wang ZG, Nwobi OI, Beydoun S. Blockade by ruthenium red of tissue factor-initiated coagulation. Br J Pharmacol 2001; 133: 659-64.
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 659-664
    • Chu, A.J.1    Wang, Z.G.2    Nwobi, O.I.3    Beydoun, S.4
  • 297
    • 0027263354 scopus 로고
    • Binding of fcator VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa
    • Rao LA, Rapaport SI, Hoang AD. Binding of fcator VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa. Blood 1993; 81: 2600-7.
    • (1993) Blood , vol.81 , pp. 2600-2607
    • Rao, L.A.1    Rapaport, S.I.2    Hoang, A.D.3
  • 298
    • 0034209755 scopus 로고    scopus 로고
    • Protease nexin-2/amyloid beta protein precursor regulates factor FVIIa and the factor VIIa-tissue factor complex
    • Mahdi F, Rehemtulla A, Van Nostrand WE, Bajaj SP, Schmaier AH. Protease nexin-2/amyloid beta protein precursor regulates factor FVIIa and the factor VIIa-tissue factor complex. Thromb Res 2000; 99: 267-76.
    • (2000) Thromb. Res. , vol.99 , pp. 267-276
    • Mahdi, F.1    Rehemtulla, A.2    Van Nostrand, W.E.3    Bajaj, S.P.4    Schmaier, A.H.5
  • 299
    • 0029861673 scopus 로고    scopus 로고
    • Molecular mechansim of tissue factor-mediated acceleration of factor VIIa activity
    • Higashi S, Matsumoto N, Iwanaga S. Molecular mechansim of tissue factor-mediated acceleration of factor VIIa activity. J Biol Chem 1996; 271: 26569-74.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26569-26574
    • Higashi, S.1    Matsumoto, N.2    Iwanaga, S.3
  • 300
    • 0034720739 scopus 로고    scopus 로고
    • The tissue factor region that interacts with substrates factor IX and factor X
    • Kirchhofer D, Lipari MT, Moran P. The tissue factor region that interacts with substrates factor IX and factor X. Biochemistry 2000; 39: 7380-7.
    • (2000) Biochemistry , vol.39 , pp. 7380-7387
    • Kirchhofer, D.1    Lipari, M.T.2    Moran, P.3
  • 301
    • 0028896007 scopus 로고
    • Mechansim of antithrombin III inhibition of factor FVIIa/tissue factor activity on cell surface. Comparison with tissue factor pathway inhibitor/factor Xa-induced inhibition of factor VIIa/tissue factor activity
    • Rao LV, Nordfang O, Hoang AD, Pendurthi UR. Mechansim of antithrombin III inhibition of factor FVIIa/tissue factor activity on cell surface. Comparison with tissue factor pathway inhibitor/factor Xa-induced inhibition of factor VIIa/tissue factor activity. Blood 1995; 85: 121-9.
    • (1995) Blood , vol.85 , pp. 121-129
    • Rao, L.V.1    Nordfang, O.2    Hoang, A.D.3    Pendurthi, U.R.4
  • 302
    • 0037093065 scopus 로고    scopus 로고
    • Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary of the tick, Ixodes scapularis: Identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex
    • Francischetti IM, Valenzuela JG, Andersen JF, Mather TN, Ribeiro JM. Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex. Blood 2002; 99: 3602-12.
    • (2002) Blood , vol.99 , pp. 3602-3612
    • Francischetti, I.M.1    Valenzuela, J.G.2    Andersen, J.F.3    Mather, T.N.4    Ribeiro, J.M.5
  • 304
    • 0036796103 scopus 로고    scopus 로고
    • Recombinant Nematode anticoagulant protein c2, a novel inhibitor of tissue factor-factor VIIa activity, agrogates endotoxin-induced coagulation in chimpanzees
    • Moons AH, Peters RJ, Cate Ht H, Bauer KA, Vlasuk GP, Buller HR, et al. Recombinant Nematode anticoagulant protein c2, a novel inhibitor of tissue factor-factor VIIa activity, agrogates endotoxin-induced coagulation in chimpanzees. Thromb Haemost 2002; 88: 627-31.
    • (2002) Thromb. Haemost. , vol.88 , pp. 627-631
    • Moons, A.H.1    Peters, R.J.2    Cate, Ht.H.3    Bauer, K.A.4    Vlasuk, G.P.5    Buller, H.R.6
  • 305
    • 0030588161 scopus 로고    scopus 로고
    • Synthetic peptide analogs of tissue factor and factor VII which inhibit factor Xa formation by the tissue factor/factor VIIa complex
    • Ronning HF, Risoen UC, Orning L, Sletten K, Sakariassen KS. Synthetic peptide analogs of tissue factor and factor VII which inhibit factor Xa formation by the tissue factor/factor VIIa complex. Thromb Res 1996; 84: 73-81.
    • (1996) Thromb. Res. , vol.84 , pp. 73-81
    • Ronning, H.F.1    Risoen, U.C.2    Orning, L.3    Sletten, K.4    Sakariassen, K.S.5
  • 306
    • 0031727981 scopus 로고    scopus 로고
    • Interaction of activated factr VII and active site-inhbited activated factor VII with tissue factor
    • Sorensen BB, Rao LV. Interaction of activated factr VII and active site-inhbited activated factor VII with tissue factor. Blood Coagul Fibrinolysis 1998; S(1): S67-71.
    • (1998) Blood Coagul Fibrinolysis , vol.S , Issue.1
    • Sorensen, B.B.1    Rao, L.V.2
  • 307
    • 0031729308 scopus 로고    scopus 로고
    • The effects of activated factor VII in a cell-based model for tissue factor-initiated coagulation
    • Kjalke M, Monroe DM, Hoffman M, Oliver JA, Ezban M, Hedner U, et al. The effects of activated factor VII in a cell-based model for tissue factor-initiated coagulation. Blood Coagul Fibrinolysis 1998; 9(S1): S21-5.
    • (1998) Blood Coagul Fibrinolysis , vol.9 , Issue.SUPPL. 1
    • Kjalke, M.1    Monroe, D.M.2    Hoffman, M.3    Oliver, J.A.4    Ezban, M.5    Hedner, U.6
  • 310
    • 0030917536 scopus 로고    scopus 로고
    • A soluble tissue factor mutant is a selctive anticoagulant and antithrombotic agent
    • Kelley RF, Refino CJ, O'Connell MP, Modi N, Sehi P, Lowe D, et al. A soluble tissue factor mutant is a selctive anticoagulant and antithrombotic agent. Blood 1997; 90: 3219-27.
    • (1997) Blood , vol.90 , pp. 3219-3227
    • Kelley, R.F.1    Refino, C.J.2    O'Connell, M.P.3    Modi, N.4    Sehi, P.5    Lowe, D.6
  • 311
    • 0032512830 scopus 로고    scopus 로고
    • A novel soluble tissue factor variant with an altered factor VIIa binding interface
    • Lee GF, Kelley RF. A novel soluble tissue factor variant with an altered factor VIIa binding interface. J Biol Chem 1998; 273: 4149-54.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4149-4154
    • Lee, G.F.1    Kelley, R.F.2
  • 312
    • 0036123295 scopus 로고    scopus 로고
    • Enhnacing the anticoagulant potency of soluble tissue factor mutants by increasing their affinity to factor VIIa
    • Yang J, Lee GF, Rienderer MA, Kelley RF. Enhnacing the anticoagulant potency of soluble tissue factor mutants by increasing their affinity to factor VIIa. Thromb Res 2002; 87: 450-8.
    • (2002) Thromb. Res. , vol.87 , pp. 450-458
    • Yang, J.1    Lee, G.F.2    Rienderer, M.A.3    Kelley, R.F.4
  • 313
    • 0031007950 scopus 로고    scopus 로고
    • Potent bifunctional anticoagulants: Kunitz domain-tissue factor fusion proteins
    • Lee GY, Lazarus RA, Kelley RF. Potent bifunctional anticoagulants: Kunitz domain-tissue factor fusion proteins. Biochemistry 1997; 36: 5607-11.
    • (1997) Biochemistry , vol.36 , pp. 5607-5611
    • Lee, G.Y.1    Lazarus, R.A.2    Kelley, R.F.3
  • 314
    • 0033763192 scopus 로고    scopus 로고
    • Inhibition of the tissue factor/factor VIIa-induced coagulation: Synthesis and in vitro evaluation of novel 2-aryl substituted pyrid
    • Jakobsen P, Horneman AM, Persson E. Inhibition of the tissue factor/factor VIIa-induced coagulation: synthesis and in vitro evaluation of novel 2-aryl substituted pyrid. Bioorg Med Chem 2000; 8: 2803-12.
    • (2000) Bioorg Med. Chem. , vol.8 , pp. 2803-2812
    • Jakobsen, P.1    Horneman, A.M.2    Persson, E.3
  • 315
    • 0033866734 scopus 로고    scopus 로고
    • Inhibitors of the tissue factor/factor VIIa-induced coagulation: Synthesis and in vitro evaluation of novel specific 2-aryl sbstituted 4H-3,1-benzoxazin-4-ones
    • Jakobsen P, Pedersen BR, Persson E. Inhibitors of the tissue factor/factor VIIa-induced coagulation: synthesis and in vitro evaluation of novel specific 2-aryl sbstituted 4H-3,1-benzoxazin-4-ones. Bioorg Med Chem 2000; 8: 2095-103.
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 2095-2103
    • Jakobsen, P.1    Pedersen, B.R.2    Persson, E.3
  • 316
    • 0028072085 scopus 로고
    • Inhibition by heparin of human blood coagulation intrinsic pathway factor X activator
    • Barrow RT, Parker ET, Krishnaswamy S. Inhibition by heparin of human blood coagulation intrinsic pathway factor X activator. J Biol Chem 1994; 269: 26796-800.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26796-26800
    • Barrow, R.T.1    Parker, E.T.2    Krishnaswamy, S.3
  • 317
    • 0032170976 scopus 로고    scopus 로고
    • Phosphorothioate oligonucleotides inhibit the intrinsic tenase complex
    • Sheelan JP, Lan HC. Phosphorothioate oligonucleotides inhibit the intrinsic tenase complex. Blood 1998; 92: 1616-25.
    • (1998) Blood , vol.92 , pp. 1616-1625
    • Sheelan, J.P.1    Lan, H.C.2
  • 318
    • 0035942332 scopus 로고    scopus 로고
    • Phosphorothioate oligonucleotides inhibit the intrinsic tenase complex by an allosteric mechanism
    • Sheelan JP, Phan TM. Phosphorothioate oligonucleotides inhibit the intrinsic tenase complex by an allosteric mechanism. Biochemistry 2001; 40: 4980-9.
    • (2001) Biochemistry , vol.40 , pp. 4980-4989
    • Sheelan, J.P.1    Phan, T.M.2
  • 319
    • 0036811777 scopus 로고    scopus 로고
    • Antithrombin-independent anticoagulation by hypersulfated low-molecular-weight heparin
    • Fredenburgh JC, Anderson JAM, Weitz JI. Antithrombin-independent anticoagulation by hypersulfated low-molecular-weight heparin. Trends Cardiovasc Med 2002; 12: 281-7.
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 281-287
    • Fredenburgh, J.C.1    Anderson, J.A.M.2    Weitz, J.I.3
  • 320
    • 0024208025 scopus 로고
    • An inhibitory monoclonal antibody to factor X that blocks prothrombin activation but not prothrombinase enzyme assembly
    • Church WR, Messier TL, Tucker MM, Mann KG. An inhibitory monoclonal antibody to factor X that blocks prothrombin activation but not prothrombinase enzyme assembly. Blood 1988; 72: 1911-21.
    • (1988) Blood , vol.72 , pp. 1911-1921
    • Church, W.R.1    Messier, T.L.2    Tucker, M.M.3    Mann, K.G.4
  • 321
    • 0030790774 scopus 로고    scopus 로고
    • Enozaparin, a low-moleculae-weight heparin suppresses prothrombin activation more effectively than unfractionated heparin in patients treated for venous thromboembolism
    • Grosset AB, Spiro TE, Beynon J, Rodgers GM. Enozaparin, a low-moleculae-weight heparin suppresses prothrombin activation more effectively than unfractionated heparin in patients treated for venous thromboembolism. Thromb Res 1997; 86: 349-54.
    • (1997) Thromb. Res. , vol.86 , pp. 349-354
    • Grosset, A.B.1    Spiro, T.E.2    Beynon, J.3    Rodgers, G.M.4
  • 322
    • 0036507948 scopus 로고    scopus 로고
    • Effect of low-molecular weight dextran sulfate on coagulation and platelet function tests
    • Zeerleder S, Manton T, Lammle B, Wuillemin WA. Effect of low-molecular weight dextran sulfate on coagulation and platelet function tests. Thromb Res 2002; 105: 441-6.
    • (2002) Thromb. Res. , vol.105 , pp. 441-446
    • Zeerleder, S.1    Manton, T.2    Lammle, B.3    Wuillemin, W.A.4
  • 323
    • 0031977005 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor and anti-FXa kinetic profiles of a new low-molecular-mass heparin, Bemiparin, at therapeutic subcutaneous doses
    • Falkon L, Gari M, Barbanoj M, Amiral J, Fontcuberta J. Tissue factor pathway inhibitor and anti-FXa kinetic profiles of a new low-molecular-mass heparin, Bemiparin, at therapeutic subcutaneous doses. Blood Coagul Fibrinolysis 1998; 9: 137-141.
    • (1998) Blood Coagul. Fibrinolysis , vol.9 , pp. 137-141
    • Falkon, L.1    Gari, M.2    Barbanoj, M.3    Amiral, J.4    Fontcuberta, J.5
  • 324
    • 0034916276 scopus 로고    scopus 로고
    • Reviparin: A review of its efficacy in the prevention and treatment of venous thromboembolism
    • Wellington K, McClellan K, Jarvis B. Reviparin: A review of its efficacy in the prevention and treatment of venous thromboembolism. Drugs 2001; 61: 1185-209.
    • (2001) Drugs , vol.61 , pp. 1185-1209
    • Wellington, K.1    McClellan, K.2    Jarvis, B.3
  • 325
  • 326
    • 0034771722 scopus 로고    scopus 로고
    • Effects of sulfation on antithrombin-thrombin/factor Xa interactions in semisynthetic low molecular weight heparins
    • Sissi C, Naggi A, Torri G, Palumbo M. Effects of sulfation on antithrombin-thrombin/factor Xa interactions in semisynthetic low molecular weight heparins. Semin Thromb Hemost 2001; 27: 483-7.
    • (2001) Semin. Thromb. Hemost. , vol.27 , pp. 483-487
    • Sissi, C.1    Naggi, A.2    Torri, G.3    Palumbo, M.4
  • 327
    • 0036021104 scopus 로고    scopus 로고
    • Identification of critical molecular interactions mediating heparin activation of antithrombin. Implications for the design of improved heparin anticoagulants
    • Olson ST, Bjork I, Bock S. Identification of critical molecular interactions mediating heparin activation of antithrombin. Implications for the design of improved heparin anticoagulants. Trends Cardiovasc Med 2002; 12: 189-205.
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 189-205
    • Olson, S.T.1    Bjork, I.2    Bock, S.3
  • 328
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L, Smith DE, Arcui KE, Vlasuk GP. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 1990; 248: 593-96.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcui, K.E.3    Vlasuk, G.P.4
  • 329
    • 0026751368 scopus 로고
    • Reaction pathway for inhibition of blood coagulation factor Xa by tick anticoagulant peptide
    • Jordan SP, Mao SS, Lewis SD, Shafer JA. Reaction pathway for inhibition of blood coagulation factor Xa by tick anticoagulant peptide. Biochemistry 1992; 31: 5347-80.
    • (1992) Biochemistry , vol.31 , pp. 5347-5380
    • Jordan, S.P.1    Mao, S.S.2    Lewis, S.D.3    Shafer, J.A.4
  • 330
    • 0025683260 scopus 로고
    • Tick anticoagulant peptide: Kinetic analysis of the recombinant inhibitor with blood coagulation factor Xa
    • Jordan SP, Waxman L, Smith DE, Vlasuk GP. Tick anticoagulant peptide: kinetic analysis of the recombinant inhibitor with blood coagulation factor Xa. Biochemistry 1990; 29: 11095-100.
    • (1990) Biochemistry , vol.29 , pp. 11095-11100
    • Jordan, S.P.1    Waxman, L.2    Smith, D.E.3    Vlasuk, G.P.4
  • 331
    • 0028930192 scopus 로고
    • Identification and characterization of variants of tick anticoagulant peptide with increased inhibitory potency toward human factor Xa
    • Mao SS, Huang J, Welebob C, Neeper MP, Garsky VM, Shafer JA. Identification and characterization of variants of tick anticoagulant peptide with increased inhibitory potency toward human factor Xa. Biochemistry 1995; 34: 5098-103.
    • (1995) Biochemistry , vol.34 , pp. 5098-5103
    • Mao, S.S.1    Huang, J.2    Welebob, C.3    Neeper, M.P.4    Garsky, V.M.5    Shafer, J.A.6
  • 332
    • 0030267778 scopus 로고    scopus 로고
    • Isolation and characterization of an anticoagulant from the salivary glands of the tick, Ornithodoros savignyi
    • Gaspar AR, Joubert AM, Crause JC, Neitz AW. Isolation and characterization of an anticoagulant from the salivary glands of the tick, Ornithodoros savignyi. Exp Appl Acarol 1996; 20: 583-98.
    • (1996) Exp. Appl. Acarol. , vol.20 , pp. 583-598
    • Gaspar, A.R.1    Joubert, A.M.2    Crause, J.C.3    Neitz, A.W.4
  • 335
    • 0032759381 scopus 로고    scopus 로고
    • Draculin, the anticoagulant factor in vampire bat saliva, is a tight-binding, noncompetitive inhibitor of activated factor X
    • Fernandez AZ, Tablante A, Beguin S, Hemker HC, Apitz-Castro R. Draculin, the anticoagulant factor in vampire bat saliva, is a tight-binding, noncompetitive inhibitor of activated factor X. Biochim Biophys Acta 1999; 1434: 135-142.
    • (1999) Biochim. Biophys. Acta. , vol.1434 , pp. 135-142
    • Fernandez, A.Z.1    Tablante, A.2    Beguin, S.3    Hemker, H.C.4    Apitz-Castro, R.5
  • 336
    • 0029587304 scopus 로고
    • A factor Xa-directed anticoagulant from the salivary glands of the yellow fever mosquito Aedes adgypti
    • Stark KR, James AA. A factor Xa-directed anticoagulant from the salivary glands of the yellow fever mosquito Aedes adgypti. Exp Parasitol 1995; 81: 321-31.
    • (1995) Exp. Parasitol. , vol.81 , pp. 321-331
    • Stark, K.R.1    James, A.A.2
  • 337
    • 0030187447 scopus 로고    scopus 로고
    • Salivary gland anticoagulants in culicine and anopheline mosquitos (Diptera: Culicidae)
    • Stark KR, James AA. Salivary gland anticoagulants in culicine and anopheline mosquitos (Diptera: Culicidae). J Med Entomol 1996; 33: 645-50.
    • (1996) J. Med. Entomol. , vol.33 , pp. 645-650
    • Stark, K.R.1    James, A.A.2
  • 338
    • 0029014045 scopus 로고
    • Ancylostoma caninum anticoagulant peptide: A hookworm-derived inhibitor of human coagulation factor Xa
    • Cappello M, Valsuk GP, Bergun PW, Huang S, Hotez PJ. Ancylostoma caninum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation factor Xa. Proc Natl Acad Sci USA 1995; 92: 6152-6.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6152-6156
    • Cappello, M.1    Valsuk, G.P.2    Bergun, P.W.3    Huang, S.4    Hotez, P.J.5
  • 339
    • 0030856003 scopus 로고    scopus 로고
    • Antithrombotic efficacy of a recombinant nematode anticoagulant peptide (rNAP5) in canine models of thrombosis after single subcutaneous administration
    • Rebello SS, Blank HS, Vlasuk GP, Rote WE, Lucchesi BR. Antithrombotic efficacy of a recombinant nematode anticoagulant peptide (rNAP5) in canine models of thrombosis after single subcutaneous administration. J Pharmacol Exp Ther 1997; 283: 91-9.
    • (1997) J. Pharmacol. Exp. Ther. , vol.283 , pp. 91-99
    • Rebello, S.S.1    Blank, H.S.2    Vlasuk, G.P.3    Rote, W.E.4    Lucchesi, B.R.5
  • 341
    • 0028787671 scopus 로고
    • Protease nexin-2/amyloid beta protein precursor inhibits factor Xa in the prothrombinase complex
    • Mahdi F, Van Nostrand WE, Schmaier AH. Protease nexin-2/amyloid beta protein precursor inhibits factor Xa in the prothrombinase complex. J Biol Chem 1995; 270: 23468-74.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23468-23474
    • Mahdi, F.1    Van Nostrand, W.E.2    Schmaier, A.H.3
  • 342
    • 0007685566 scopus 로고
    • Dx-9065a, a synthetic and selective factor Xa inhibitor, species difference in its anticoagulant activity
    • Hara T, Kunitada S, Iwamoto M. Dx-9065a, a synthetic and selective factor Xa inhibitor, species difference in its anticoagulant activity. Thromb Haemost 1993; 69: 890-9.
    • (1993) Thromb. Haemost. , vol.69 , pp. 890-899
    • Hara, T.1    Kunitada, S.2    Iwamoto, M.3
  • 343
    • 0030727965 scopus 로고    scopus 로고
    • Antithrombotic and hemorrhagic effects of DX-9065a, a direct and selective factor Xa inhibitior: Comparison with a direct thrombin inhibitor and antithrombin III-dependent anticoagulants
    • Morishima y, Tanabe K, Terada Y, Hara T, Kunitada S. Antithrombotic and hemorrhagic effects of DX-9065a, a direct and selective factor Xa inhibitior: comparison with a direct thrombin inhibitor and antithrombin III-dependent anticoagulants. Thromb Haemost 1997; 78: 1366-71.
    • (1997) Thromb. Haemost. , vol.78 , pp. 1366-1371
    • Morishima, Y.1    Tanabe, K.2    Terada, Y.3    Hara, T.4    Kunitada, S.5
  • 345
    • 0032960904 scopus 로고    scopus 로고
    • DX-9065a, an orally active factor Xa inhibitor, does not facilitate haemorrhage induced by tail transection or gastric ulcer at the effective doses in rat thrombosis model
    • Tanabe K, Morishima Y, Shibutani T, Terada Y, Hara T, Shinohara Y, et al. DX-9065a, an orally active factor Xa inhibitor, does not facilitate haemorrhage induced by tail transection or gastric ulcer at the effective doses in rat thrombosis model. Thromb Haemost 1999; 81: 828-34.
    • (1999) Thromb. Haemost. , vol.81 , pp. 828-834
    • Tanabe, K.1    Morishima, Y.2    Shibutani, T.3    Terada, Y.4    Hara, T.5    Shinohara, Y.6
  • 346
    • 18344374666 scopus 로고    scopus 로고
    • The discovery of YM-60828: A potent, selective and orally-bioavailable factor Xa inhibitor
    • Hirayama F, Koshio H, Katayama N, Kurihara H, Taniuchi Y, Sato K, et al. The discovery of YM-60828: A potent, selective and orally-bioavailable factor Xa inhibitor. Bioorg Med Chem 2002; 10: 1509-23.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 1509-1523
    • Hirayama, F.1    Koshio, H.2    Katayama, N.3    Kurihara, H.4    Taniuchi, Y.5    Sato, K.6
  • 347
    • 0031793092 scopus 로고    scopus 로고
    • Comparison of the anticoagulant and antithrombotic effects of YM-75466, a novel orally active factror Xa inhibitor and warfarin in mice
    • Sato K, Taniuchi Y, Kawasaki T, Hirayama F, Koshio H, Matsumoto Y, et al. Comparison of the anticoagulant and antithrombotic effects of YM-75466, a novel orally active factror Xa inhibitor and warfarin in mice. Jpn J Pharmacol 1998; 78: 191-7.
    • (1998) Jpn. J. Pharmacol. , vol.78 , pp. 191-197
    • Sato, K.1    Taniuchi, Y.2    Kawasaki, T.3    Hirayama, F.4    Koshio, H.5    Matsumoto, Y.6
  • 348
    • 0033810831 scopus 로고    scopus 로고
    • Nonpeptide factor Xa inhibitors II. Antithrombotic evaluation in a rabbit model of electrically induced carotid artery thrombosis
    • Wong PC, Crain EJ, Knabb RM, Meade RP, Quan ML, Watson CA, et al. Nonpeptide factor Xa inhibitors II. Antithrombotic evaluation in a rabbit model of electrically induced carotid artery thrombosis. J Pharmacol Exp Ther 2000; 295: 212-8.
    • (2000) J. Pharmacol. Exp. Ther. , vol.295 , pp. 212-218
    • Wong, P.C.1    Crain, E.J.2    Knabb, R.M.3    Meade, R.P.4    Quan, M.L.5    Watson, C.A.6
  • 349
    • 18244397236 scopus 로고    scopus 로고
    • Assessment of ex vivo pharmacodynamic markers during inhibition of thrombosis by CI-1031 (ZK-807834), a novel direct factor Xa inhibitor
    • Chi L, Pen YW, Potoczak R, Gibson-G, Hicks G, Mertz TE, et al. Assessment of ex vivo pharmacodynamic markers during inhibition of thrombosis by CI-1031 (ZK-807834), a novel direct factor Xa inhibitor. Pharmacology 2002; 64: 76-83.
    • (2002) Pharmacology , vol.64 , pp. 76-83
    • Chi, L.1    Pen, Y.W.2    Potoczak, R.3    Gibson, G.4    Hicks, G.5    Mertz, T.E.6
  • 350
    • 0035880858 scopus 로고    scopus 로고
    • Pharmacological characterization of novel factor Xa inhibitor, FXV673
    • Chu V, Brown K, Colussi D, Gao J, Bostwick J, Kasiewski C, et al. Pharmacological characterization of novel factor Xa inhibitor, FXV673. Thromb Res 2001; 103: 309-24.
    • (2001) Thromb. Res. , vol.103 , pp. 309-324
    • Chu, V.1    Brown, K.2    Colussi, D.3    Gao, J.4    Bostwick, J.5    Kasiewski, C.6
  • 351
  • 352
    • 0036544676 scopus 로고    scopus 로고
    • A peptide derived from human prothrombin fagment 2 inhibits prothrombinase and angiogenesis
    • Kim B, Koo S, Kim S. A peptide derived from human prothrombin fagment 2 inhibits prothrombinase and angiogenesis. Thromb Res 2002; 106: 81-6.
    • (2002) Thromb. Res. , vol.106 , pp. 81-86
    • Kim, B.1    Koo, S.2    Kim, S.3
  • 353
    • 0032508599 scopus 로고    scopus 로고
    • Inhibition of prothrominase by human secretory phospholipase A2 involves binding to factor Xa
    • Mounier CM, Hackeng TM, Schaeffer F, Faure G, Bon C, Griffin JH. Inhibition of prothrominase by human secretory phospholipase A2 involves binding to factor Xa. J Biol Chem 1998; 273: 23764-72.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23764-23772
    • Mounier, C.M.1    Hackeng, T.M.2    Schaeffer, F.3    Faure, G.4    Bon, C.5    Griffin, J.H.6
  • 354
    • 0034993220 scopus 로고    scopus 로고
    • Complexes of anti-prothrombin antibodies and prothrombin cause lupus anticoagulant activity by competing with the binding of cloning factors for catalytic phospholipid surfaces
    • Simmelink MJ, Horbach DA, Derksen RH, Meijers JC, Bevers EM, Willems GM, et al. Complexes of anti-prothrombin antibodies and prothrombin cause lupus anticoagulant activity by competing with the binding of cloning factors for catalytic phospholipid surfaces. Br J Haematol 2001; 113: 621-9.
    • (2001) Br. J. Haematol. , vol.113 , pp. 621-629
    • Simmelink, M.J.1    Horbach, D.A.2    Derksen, R.H.3    Meijers, J.C.4    Bevers, E.M.5    Willems, G.M.6
  • 355
    • 0034307023 scopus 로고    scopus 로고
    • Inhibition of prothrombin activation by Bothrojaracin, a C-type lectin from Bothrops jararaca venom
    • Monteiro RQ, Zingali RB. Inhibition of prothrombin activation by Bothrojaracin, a C-type lectin from Bothrops jararaca venom. Arch Biochem Biophs 2000; 382: 123-8.
    • (2000) Arch. Biochem. Biophs. , vol.382 , pp. 123-128
    • Monteiro, R.Q.1    Zingali, R.B.2
  • 357
    • 0022624465 scopus 로고
    • Penson polysulphate: Activation of heparin cofactor II or antithrombin III according to molecular weight fractionation
    • Scully MF, Ellis V, Kakkar VV. Penson polysulphate: activation of heparin cofactor II or antithrombin III according to molecular weight fractionation. Thromb Res 1986; 41: 489-99.
    • (1986) Thromb. Res. , vol.41 , pp. 489-499
    • Scully, M.F.1    Ellis, V.2    Kakkar, V.V.3
  • 358
    • 0025230643 scopus 로고
    • The effect of sulfation of the anticoagulant and antithrombin III-binding properties of a heparin fraction with low affinity for antithrombin III
    • Schoen P, Wielders S, Petitou M, Lindhout T. The effect of sulfation of the anticoagulant and antithrombin III-binding properties of a heparin fraction with low affinity for antithrombin III. Thromb Res 1990; 57: 415-23.
    • (1990) Thromb. Res. , vol.57 , pp. 415-423
    • Schoen, P.1    Wielders, S.2    Petitou, M.3    Lindhout, T.4
  • 359
    • 0031081212 scopus 로고    scopus 로고
    • Mechansim of thrombin inhibition by heparin cofactor II in the presence of dermatran sulfates, native or oversulfate, and a heparin-like dextran derivative
    • Maaroufi RM, Jozefowicz M, Tapon-Bretaudiere J, Jozefonvicz J, Fischer AM. Mechansim of thrombin inhibition by heparin cofactor II in the presence of dermatran sulfates, native or oversulfate, and a heparin-like dextran derivative. Biomaterials 1997; 18: 359-66.
    • (1997) Biomaterials , vol.18 , pp. 359-366
    • Maaroufi, R.M.1    Jozefowicz, M.2    Tapon-Bretaudiere, J.3    Jozefonvicz, J.4    Fischer, A.M.5
  • 360
    • 0025856283 scopus 로고
    • Heparin cofactor II: Experimental approach to a new assay and clinical results
    • Vinazzer H, Stocker K. Heparin cofactor II: experimental approach to a new assay and clinical results. Thromb Res 1991; 61: 235-41.
    • (1991) Thromb. Res. , vol.61 , pp. 235-241
    • Vinazzer, H.1    Stocker, K.2
  • 361
    • 0024544241 scopus 로고
    • Antithrombin activity of fucoidan. The interaction of fucoidan with heparin cofactor II, antithrombin III, and thrombin
    • Church FC, Meade JB, Treanor RE, Whinna HC. Antithrombin activity of fucoidan. The interaction of fucoidan with heparin cofactor II, antithrombin III, and thrombin. J Biol Chem 1989; 264: 3618-23.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3618-3623
    • Church, F.C.1    Meade, J.B.2    Treanor, R.E.3    Whinna, H.C.4
  • 362
    • 0026867012 scopus 로고
    • Anticoagulant and antithrombin activities of oversulfated fucans
    • Nishino T, Nagumo T. Anticoagulant and antithrombin activities of oversulfated fucans. Carbohydr Res 1992; 229: 355-62.
    • (1992) Carbohydr. Res. , vol.229 , pp. 355-362
    • Nishino, T.1    Nagumo, T.2
  • 364
    • 0037087219 scopus 로고    scopus 로고
    • Anticoagulant effect and action mechanism of sulfated flavonoids from Flaveria bidentis
    • Guglielmone HA, Agnese AM, Montoya SCN, Cabrera JL. Anticoagulant effect and action mechanism of sulfated flavonoids from Flaveria bidentis. Thromb Res 2002; 105: 183-8.
    • (2002) Thromb. Res. , vol.105 , pp. 183-188
    • Guglielmone, H.A.1    Agnese, A.M.2    Montoya, S.C.N.3    Cabrera, J.L.4
  • 366
    • 0025233866 scopus 로고
    • Mechansism of potentiation of antithrombin III and heparin cofactor II inhibition by sulfated xylans
    • Carson L, Doctor VM. Mechansism of potentiation of antithrombin III and heparin cofactor II inhibition by sulfated xylans. Thromb Res 1990; 58: 367-81.
    • (1990) Thromb. Res. , vol.58 , pp. 367-381
    • Carson, L.1    Doctor, V.M.2
  • 369
    • 0035081904 scopus 로고    scopus 로고
    • Anticoagulant and antiprotease profile of a novel natural heparinomimetic mannopentaose phosphate sulfate (PI-88)
    • Demir M, Iqbal O, Hoppensteadt DA, Piccolo P, Ahmad S, Schultz CL, et al. Anticoagulant and antiprotease profile of a novel natural heparinomimetic mannopentaose phosphate sulfate (PI-88). Clin Appl Thromb Hemost 2001; 7: 131-40.
    • (2001) Clin. Appl. Thromb. Hemost. , vol.7 , pp. 131-140
    • Demir, M.1    Iqbal, O.2    Hoppensteadt, D.A.3    Piccolo, P.4    Ahmad, S.5    Schultz, C.L.6
  • 371
  • 372
    • 0032833475 scopus 로고    scopus 로고
    • Incorporation of noncoded amino acids into the N-terminal domain 1-47 of hirudin yields a highhly potent and selective thrombin inhibitor
    • De Filippis V, Russo I, Vindigni A, Di Cera E, Salmaso S, Fontana A. Incorporation of noncoded amino acids into the N-terminal domain 1-47 of hirudin yields a highhly potent and selective thrombin inhibitor. Protein Sci 1999; 8: 2213-7.
    • (1999) Protein Sci. , vol.8 , pp. 2213-2217
    • De Filippis, V.1    Russo, I.2    Vindigni, A.3    Di Cera, E.4    Salmaso, S.5    Fontana, A.6
  • 373
  • 374
    • 0026511955 scopus 로고
    • Primary structure and function of novel O-hlycosylated hirudins from the leech Hirudinaria manillensis
    • Steiner V, Knecht R, Bornsen KO, Gassmann E, Stone SR, Raschdorf F. Primary structure and function of novel O-hlycosylated hirudins from the leech Hirudinaria manillensis. Biochemistry 1992; 31: 2294-8.
    • (1992) Biochemistry , vol.31 , pp. 2294-2298
    • Steiner, V.1    Knecht, R.2    Bornsen, K.O.3    Gassmann, E.4    Stone, S.R.5    Raschdorf, F.6
  • 375
    • 0029147003 scopus 로고
    • Core domain of hirudin from the leech Hirudinaria manillensis: Chemical synthesis, purification, and characterization of Trp3 analog of fragment 1-47
    • De Filippis V, Vindigni A, Altichieri L, Fontana A. Core domain of hirudin from the leech Hirudinaria manillensis: chemical synthesis, purification, and characterization of Trp3 analog of fragment 1-47. Biochemistry 1995; 34: 9552-64.
    • (1995) Biochemistry , vol.34 , pp. 9552-9564
    • De Filippis, V.1    Vindigni, A.2    Altichieri, L.3    Fontana, A.4
  • 376
    • 0027516408 scopus 로고
    • Isolation, sequence analysis, and cloning of haemadin. An anticoagulant peptide from the Indian leech
    • Strube KH, Kroger B, Bialojan S, Otte M, Dodt J. Isolation, sequence analysis, and cloning of haemadin. An anticoagulant peptide from the Indian leech. J Biol Chem 1993; 268: 8590-5.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8590-8595
    • Strube, K.H.1    Kroger, B.2    Bialojan, S.3    Otte, M.4    Dodt, J.5
  • 379
    • 0028784163 scopus 로고
    • Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • van de Locht A, Lamba D, Bauer M, Huber R, Friedrich T, Kroger B, et al. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 1995; 14: 5149-57.
    • (1995) EMBO J. , vol.14 , pp. 5149-5157
    • van de Locht, A.1    Lamba, D.2    Bauer, M.3    Huber, R.4    Friedrich, T.5    Kroger, B.6
  • 383
    • 0027959329 scopus 로고
    • Effects of synthetic thrombin inhibitor argatroban on fibrin or clot-incorporated thrombin: Comparison with heparin and recombinant hirudin
    • Berry C, Girardot C, Lecoffre C. Effects of synthetic thrombin inhibitor argatroban on fibrin or clot-incorporated thrombin: comparison with heparin and recombinant hirudin. Thromb Haemost 1994; 72: 381-6.
    • (1994) Thromb. Haemost. , vol.72 , pp. 381-386
    • Berry, C.1    Girardot, C.2    Lecoffre, C.3
  • 384
    • 0035836541 scopus 로고    scopus 로고
    • Argatroban anticoagulant therapy in patients with heparin-induced thrombocytopenia
    • Lewis B, Wallis D, Berkowitz S. Argatroban anticoagulant therapy in patients with heparin-induced thrombocytopenia. Circulation 2001; 103: 1838-43.
    • (2001) Circulation , vol.103 , pp. 1838-1843
    • Lewis, B.1    Wallis, D.2    Berkowitz, S.3
  • 385
    • 0033017497 scopus 로고    scopus 로고
    • Small, noncovalent serine protease inhibitos
    • Sanderson PE. Small, noncovalent serine protease inhibitos. Med Res Rev 1999; 19: 179-197.
    • (1999) Med. Res. Rev. , vol.19 , pp. 179-197
    • Sanderson, P.E.1
  • 386
    • 0035042243 scopus 로고    scopus 로고
    • Effect of LY287045, a thrombin/trypsin inhibitor, on thrombin and trypsin-induced aortic contraction and relaxation
    • Bhattacharya A, Smith GF, Cohen ML. Effect of LY287045, a thrombin/trypsin inhibitor, on thrombin and trypsin-induced aortic contraction and relaxation. J Pharmacol Exp Ther 2001; 297: 573-81.
    • (2001) J. Pharmacol. Exp. Ther. , vol.297 , pp. 573-581
    • Bhattacharya, A.1    Smith, G.F.2    Cohen, M.L.3
  • 387
    • 0021995951 scopus 로고
    • A monoclonal antibody, specific for human fibrinogen, fibrinopeptideA-containing fragmentsand not reacting with free fibrinopeptide A
    • Koppert PW, Huijsmans CM, Nieuwenhuizen W. A monoclonal antibody, specific for human fibrinogen, fibrinopeptideA-containing fragmentsand not reacting with free fibrinopeptide A. Blood 1985; 66: 503-7.
    • (1985) Blood , vol.66 , pp. 503-507
    • Koppert, P.W.1    Huijsmans, C.M.2    Nieuwenhuizen, W.3
  • 388
    • 0027385637 scopus 로고
    • Molecular approach to structure-function relationship of human coagulation factor XIIII
    • Ichinose A, Kaetsu H. Molecular approach to structure-function relationship of human coagulation factor XIIII. Method Enzymol 1993; 222: 36-51.
    • (1993) Method Enzymol. , vol.222 , pp. 36-51
    • Ichinose, A.1    Kaetsu, H.2
  • 391
    • 0035080857 scopus 로고    scopus 로고
    • Depletion of plasma factor XIII prevents disseminated intravascular coagulation-induced organ damage
    • Lee SY, Chang SK, Lee IH, Kim YM, Chung SI. Depletion of plasma factor XIII prevents disseminated intravascular coagulation-induced organ damage. Thromb Haemost 2001; 85: 464-9.
    • (2001) Thromb. Haemost. , vol.85 , pp. 464-469
    • Lee, S.Y.1    Chang, S.K.2    Lee, I.H.3    Kim, Y.M.4    Chung, S.I.5
  • 392
    • 0030843675 scopus 로고    scopus 로고
    • Thrombin interaction with fibrin polymerization sites
    • Hsieh K. Thrombin interaction with fibrin polymerization sites. Thromb Res 1997; 86: 301-16.
    • (1997) Thromb. Res. , vol.86 , pp. 301-316
    • Hsieh, K.1
  • 393
    • 0036091884 scopus 로고    scopus 로고
    • The effect of dimethylbiguanide on thrombin activity, FXIII activation, fibrin polymerization, and fibrin clot formation
    • Standeven KF, Ariens RA, Whitaker P, Ashcroft AE, Weisel JW, Grant PJ. The effect of dimethylbiguanide on thrombin activity, FXIII activation, fibrin polymerization, and fibrin clot formation. Diabetes 2002; 51; 189-97.
    • (2002) Diabetes , vol.51 , pp. 189-197
    • Standeven, K.F.1    Ariens, R.A.2    Whitaker, P.3    Ashcroft, A.E.4    Weisel, J.W.5    Grant, P.J.6
  • 394
    • 0036243671 scopus 로고    scopus 로고
    • Tissue factor- a therapeutic target for thrombotic disorders
    • Houston DS. Tissue factor- a therapeutic target for thrombotic disorders. Expert Opin Ther Targets 2002; 6: 159-74.
    • (2002) Expert Opin. Ther. Targets , vol.6 , pp. 159-174
    • Houston, D.S.1
  • 395
    • 0025951949 scopus 로고
    • Single amino acid substitutions dissociate fibrinogen clotting and thrombomodulin-binding activities of human thrombin
    • Wu Q, Sheehan JP, Tsiang M, Lentz SR, Birktoft JJ, Sadler JE. Single amino acid substitutions dissociate fibrinogen clotting and thrombomodulin-binding activities of human thrombin. Proc Natl Acad Sci USA 1991; 98: 6775-9.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6775-6779
    • Wu, Q.1    Sheehan, J.P.2    Tsiang, M.3    Lentz, S.R.4    Birktoft, J.J.5    Sadler, J.E.6
  • 396
    • 0028811156 scopus 로고
    • Conversion of thrombin into an anticoagulant by protein engineering
    • Gibbs GS, Coutre SE, Tsiang M, Li WX, Jain AK, Dunn KE, et al. Conversion of thrombin into an anticoagulant by protein engineering. Nature 1995; 378: 413-6.
    • (1995) Nature , vol.378 , pp. 413-416
    • Gibbs, G.S.1    Coutre, S.E.2    Tsiang, M.3    Li, W.X.4    Jain, A.K.5    Dunn, K.E.6
  • 397
    • 0030877442 scopus 로고    scopus 로고
    • Selective loss of fibrinogen clotting in loop-less thrombin
    • Dang QD, Sabetta M, Di Cera E. Selective loss of fibrinogen clotting in loop-less thrombin. J Biol Chem 1997; 272: 19649-51.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19649-19651
    • Dang, Q.D.1    Sabetta, M.2    Di Cera, E.3
  • 398
    • 0026785554 scopus 로고
    • Prothrombin Salakta: Substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity
    • Miyata T, Aruga R, Umeyama H, Bezeaud A, Guillin MC, Iwanaga S. Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity. Biochemistry 1992; 31: 7457-62.
    • (1992) Biochemistry , vol.31 , pp. 7457-7462
    • Miyata, T.1    Aruga, R.2    Umeyama, H.3    Bezeaud, A.4    Guillin, M.C.5    Iwanaga, S.6
  • 399
    • 0031052393 scopus 로고    scopus 로고
    • Rational engineering of activity and specificity in a serine protease
    • Dang QD, Guinto ER, Di Cera E. Rational engineering of activity and specificity in a serine protease. Nat Biotechnol 1997; 15: 146-9.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 146-149
    • Dang, Q.D.1    Guinto, E.R.2    Di Cera, E.3
  • 400
    • 0036363423 scopus 로고    scopus 로고
    • Gene targeting of tissue factor, factor X, and factor VII in mice: Their involvement, in embryonic development
    • Aasrum M, Prydz H. Gene targeting of tissue factor, factor X, and factor VII in mice: their involvement, in embryonic development. Biochemistry (Mosc) 2002; 67: 25-32.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 25-32
    • Aasrum, M.1    Prydz, H.2
  • 401
    • 0035259550 scopus 로고    scopus 로고
    • Gene targeting in hemostasis. Factor VII
    • Chan JC. Gene targeting in hemostasis. Factor VII. Front Biosci 2001; 6: D98-104.
    • (2001) Front. Biosci. , vol.6
    • Chan, J.C.1
  • 402
    • 0023227857 scopus 로고
    • Heparin promotes the inactivation of antithrombin by neutrophil elastase
    • Jordan RE, Kilpatrick J, Nelson RM. Heparin promotes the inactivation of antithrombin by neutrophil elastase. Science 1987; 237: 777-9.
    • (1987) Science , vol.237 , pp. 777-779
    • Jordan, R.E.1    Kilpatrick, J.2    Nelson, R.M.3
  • 403
    • 0024340631 scopus 로고
    • Inactivation of human antithrombin by neutrophil elastase. Kinetics of the heparin-dependent reaction
    • Jordan RE, Nelson RM, Kilpatrick J, Newgren JO, Esmon C, Fournel MA. Inactivation of human antithrombin by neutrophil elastase. Kinetics of the heparin-dependent reaction. J Biol Chem 1989; 264: 10493-500.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10493-10500
    • Jordan, R.E.1    Nelson, R.M.2    Kilpatrick, J.3    Newgren, J.O.4    Esmon, C.5    Fournel, M.A.6
  • 405
    • 0023621620 scopus 로고
    • Inactivation of heparin cofactor II by polymorphonuclear leukocytes
    • Sie P, Dupouy D, Dol F, Boneu B. Inactivation of heparin cofactor II by polymorphonuclear leukocytes. Thromb Res 1987; 47: 657-64.
    • (1987) Thromb. Res. , vol.47 , pp. 657-664
    • Sie, P.1    Dupouy, D.2    Dol, F.3    Boneu, B.4
  • 406
    • 0034282877 scopus 로고    scopus 로고
    • Matrix metalloproteinases cleave tissue factor pathway inhibitor. Effects on coagulation
    • Belaaouaj AA, Li A, Wun TC, Welgus HG, Sharpiro SD. Matrix metalloproteinases cleave tissue factor pathway inhibitor. Effects on coagulation. J Biol Chem 2000; 275: 27123-28.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27123-27128
    • Belaaouaj, A.A.1    Li, A.2    Wun, T.C.3    Welgus, H.G.4    Sharpiro, S.D.5
  • 407
    • 0037108733 scopus 로고    scopus 로고
    • Structural and functional characterization of tissue factor pathway inhibitor following degradation by matrix metalloproteinase-8
    • Cunningham AC, Hasty KA, Enghild JJ, Mast AE. Structural and functional characterization of tissue factor pathway inhibitor following degradation by matrix metalloproteinase-8. Biochem. J 2002; 367: 451-8.
    • (2002) Biochem. J. , vol.367 , pp. 451-458
    • Cunningham, A.C.1    Hasty, K.A.2    Enghild, J.J.3    Mast, A.E.4
  • 408
    • 0026341831 scopus 로고
    • The C-terminus of tissue factor pathway inhibitor is essentail to its anticaogulant activity
    • Nordfang O, Bjorn SE, Valentin S, Nielsen LS, Wildgoose P, Beck TC, et al. The C-terminus of tissue factor pathway inhibitor is essentail to its anticaogulant activity. Biochemistry 1991; 30: 10371-6.
    • (1991) Biochemistry , vol.30 , pp. 10371-10376
    • Nordfang, O.1    Bjorn, S.E.2    Valentin, S.3    Nielsen, L.S.4    Wildgoose, P.5    Beck, T.C.6
  • 409
    • 0032960667 scopus 로고    scopus 로고
    • Increased truncated form of plasma tissue factor pathway inhibitor levels in patients with disseminated intravascular coagulation
    • Shimura M, Wada H, Nakasaki T, Hiyoyama K, Mori Y, Nishikawa M, et al. Increased truncated form of plasma tissue factor pathway inhibitor levels in patients with disseminated intravascular coagulation. Am J Hematol 1999; 60: 94-8.
    • (1999) Am. J. Hematol. , vol.60 , pp. 94-98
    • Shimura, M.1    Wada, H.2    Nakasaki, T.3    Hiyoyama, K.4    Mori, Y.5    Nishikawa, M.6
  • 410
    • 0034049830 scopus 로고    scopus 로고
    • Heparin induces synthesis and secretion of tissue factor pathway inhibitor from endothelial cells in vitro
    • Hansen JB, Svensson B, Olsen R, Ezban M, Osterud B, Paulssen RH. Heparin induces synthesis and secretion of tissue factor pathway inhibitor from endothelial cells in vitro. Thromb Haemost 2000; 83: 937-43.
    • (2000) Thromb. Haemost. , vol.83 , pp. 937-943
    • Hansen, J.B.1    Svensson, B.2    Olsen, R.3    Ezban, M.4    Osterud, B.5    Paulssen, R.H.6
  • 411
    • 0032952131 scopus 로고    scopus 로고
    • Tissue factor reduction and tissue factor pathway inhibitor release after heparin administration
    • Gori AM, Pepe G, Attanasio M, Falciani M, Abbate R, Prisco D, et al. Tissue factor reduction and tissue factor pathway inhibitor release after heparin administration. Thromb Haemost 1999; 81: 589-3.
    • (1999) Thromb. Haemost. , vol.81 , pp. 589-593
    • Gori, A.M.1    Pepe, G.2    Attanasio, M.3    Falciani, M.4    Abbate, R.5    Prisco, D.6
  • 413
    • 0034976081 scopus 로고    scopus 로고
    • Factor X levels, polymorphisms in the promoter region of factor X and the risk of venous thrombosis
    • deVisser MCH, Poort SR, Vos HC, Rosendaal FR, Bertina RM. Factor X levels, polymorphisms in the promoter region of factor X and the risk of venous thrombosis. Thromb Haemost 2001; 85: 1011-1017.
    • (2001) Thromb. Haemost. , vol.85 , pp. 1011-1017
    • deVisser, M.C.H.1    Poort, S.R.2    Vos, H.C.3    Rosendaal, F.R.4    Bertina, R.M.5
  • 414
    • 0032943711 scopus 로고    scopus 로고
    • Coagulation factor II, V, VII, and X, prothrombin gene 20210G-A transition and factor V Leiden in coronary artery disease: High factor V clotting activity is an independent risk factor for myocardial infarction
    • Redondo M, Watzke HH, Stucki B. Coagulation factor II, V, VII, and X, prothrombin gene 20210G-A transition and factor V Leiden in coronary artery disease: high factor V clotting activity is an independent risk factor for myocardial infarction. Arterioscler Thromb Vasc Biol 1999; 19: 1020-1025.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 1020-1025
    • Redondo, M.1    Watzke, H.H.2    Stucki, B.3
  • 415
    • 0035799341 scopus 로고    scopus 로고
    • Inflammation and thrombosis: The clot thickens
    • Libby P, Simon DI. Inflammation and thrombosis: the clot thickens. Circulation 2001; 103: 1718-20.
    • (2001) Circulation , vol.103 , pp. 1718-1720
    • Libby, P.1    Simon, D.I.2
  • 416
    • 0027725139 scopus 로고
    • Expression of tissue factor, thrombomodulin and E-selectin in baboons with lethal E. Coli sepsis
    • Drake TA, Cheng J, Chang ACK, Taylor FB. Expression of tissue factor, thrombomodulin and E-selectin in baboons with lethal E. Coli sepsis. Am J Pathol 1983; 142: 1458-63.
    • (1983) Am. J. Pathol. , vol.142 , pp. 1458-1463
    • Drake, T.A.1    Cheng, J.2    Chang, A.C.K.3    Taylor, F.B.4
  • 417
    • 0024319914 scopus 로고
    • Tumor necrosis factor infusions have a procoagulant effect on the hemostatic mechanism of humans
    • Bauer KA, ten Cate H, Barzegar S, Spriggs DR, Sherman ML, Rosenberg RD. Tumor necrosis factor infusions have a procoagulant effect on the hemostatic mechanism of humans. Blood 1989; 74: 165-72.
    • (1989) Blood , vol.74 , pp. 165-172
    • Bauer, K.A.1    ten Cate, H.2    Barzegar, S.3    Spriggs, D.R.4    Sherman, M.L.5    Rosenberg, R.D.6
  • 418
    • 2442724586 scopus 로고
    • Interleukin 1 induces endothelial cell procoagulant while suppressing cell-surface anticoagulant activity
    • Nawroth PP, Handley DA, Esmon CT, Stern DM. Interleukin 1 induces endothelial cell procoagulant while suppressing cell-surface anticoagulant activity. Proc Natl Acad Sci USA 1986; 83: 3460-4.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3460-3464
    • Nawroth, P.P.1    Handley, D.A.2    Esmon, C.T.3    Stern, D.M.4
  • 419
    • 0030978393 scopus 로고    scopus 로고
    • The coagulation and fibrinolytic responses of baboons after in vivo thrombin-generation-effect of interleukine 6
    • Kruithof EKO, Mestries JC, Gascon MP, Ythier A. The coagulation and fibrinolytic responses of baboons after in vivo thrombin-generation-effect of interleukine 6. Thromb Haemost 1997; 77: 905-10.
    • (1997) Thromb. Haemost. , vol.77 , pp. 905-910
    • Kruithof, E.K.O.1    Mestries, J.C.2    Gascon, M.P.3    Ythier, A.4
  • 420
    • 0020638083 scopus 로고
    • Inflammatory particles stimulate thromboplastin production by human monocytes
    • Dean RT, Prydz H. Inflammatory particles stimulate thromboplastin production by human monocytes. Thromb Res 1983; 30: 357-67.
    • (1983) Thromb. Res. , vol.30 , pp. 357-367
    • Dean, R.T.1    Prydz, H.2
  • 421
    • 0033504250 scopus 로고    scopus 로고
    • Possible involvement of cytokines in diffuse intravascular coagulation and thrombosis
    • Esmon CT. Possible involvement of cytokines in diffuse intravascular coagulation and thrombosis. Bailliere Clin Haematol 1999; 12: 343-359.
    • (1999) Bailliere Clin. Haematol. , vol.12 , pp. 343-359
    • Esmon, C.T.1
  • 422
    • 0035654918 scopus 로고    scopus 로고
    • The pleiotropic effects of tissue factor: A possible role for factor VIIa-induced intracellular signaling?
    • Versteeg HH, Peppelenbosch MP, Spek CA. The pleiotropic effects of tissue factor: a possible role for factor VIIa-induced intracellular signaling? Thromb Haemost 2001; 86: 1353-9.
    • (2001) Thromb. Haemost. , vol.86 , pp. 1353-1359
    • Versteeg, H.H.1    Peppelenbosch, M.P.2    Spek, C.A.3
  • 423
    • 0029847188 scopus 로고    scopus 로고
    • Coagulation factor VII and X induce Ca+2 oscillations in Madin-Darby canine kidney cells only when proteolytically active
    • Camerer E, Rottingen JA, Iversen JG, Prydz H. Coagulation factor VII and X induce Ca+2 oscillations in Madin-Darby canine kidney cells only when proteolytically active. J Biol Chem 1996; 271: 29034-42.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29034-29042
    • Camerer, E.1    Rottingen, J.A.2    Iversen, J.G.3    Prydz, H.4
  • 424
    • 0037189580 scopus 로고    scopus 로고
    • Factor VIIa induces tissue factor-dependent up-regulation of interleukin-8 in human keratinocyte line
    • Wang X, Gjernes E, Prydz H. Factor VIIa induces tissue factor-dependent up-regulation of interleukin-8 in human keratinocyte line. J Biol Chem 2002; 277: 23620-6.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23620-23626
    • Wang, X.1    Gjernes, E.2    Prydz, H.3
  • 425
    • 0034670040 scopus 로고    scopus 로고
    • Binding of factor VIIa to tissue factor on human fibroblasts leads to activation of phopholpase C and enhanced PDGF-BB-stimulated chemotaxis
    • Siegbahn A, Johnell M, Rorsman C, Ezban M, Heldin CH, Romistrand L. Binding of factor VIIa to tissue factor on human fibroblasts leads to activation of phopholpase C and enhanced PDGF-BB-stimulated chemotaxis. Blood 2000; 96: 3452-8.
    • (2000) Blood , vol.96 , pp. 3452-3458
    • Siegbahn, A.1    Johnell, M.2    Rorsman, C.3    Ezban, M.4    Heldin, C.H.5    Romistrand, L.6
  • 426
    • 0025133268 scopus 로고
    • Thrombin and factor Xa enhance the production of interleukine- 1
    • Jones A, Geczy CL. Thrombin and factor Xa enhance the production of interleukine- 1. Immunology 1990; 71: 236-41.
    • (1990) Immunology , vol.71 , pp. 236-241
    • Jones, A.1    Geczy, C.L.2
  • 427
    • 0032531987 scopus 로고    scopus 로고
    • Factor Xa induces cytokine production and expression of adhesion molecules by human umbilical vein endothelial cells
    • Senden NH, Jeunhomme TM, Heemskerk JW, Wagenvoord R, van't Veer C, Hemker HC, et al. Factor Xa induces cytokine production and expression of adhesion molecules by human umbilical vein endothelial cells. J Immunol 1998; 161: 4318-24.
    • (1998) J. Immunol. , vol.161 , pp. 4318-4324
    • Senden, N.H.1    Jeunhomme, T.M.2    Heemskerk, J.W.3    Wagenvoord, R.4    van't Veer, C.5    Hemker, H.C.6
  • 428
    • 0035874536 scopus 로고    scopus 로고
    • Gene induction by coagulation factor Xa is mediated by activation of protease-activated receptor 1
    • Riewald M, Kravchenko VV, Petrovan RJ, O'Brien PJ, Brass LF, Ulevitch RJ, et al. Gene induction by coagulation factor Xa is mediated by activation of protease-activated receptor 1. Blood 2001; 97: 3109-16.
    • (2001) Blood , vol.97 , pp. 3109-3116
    • Riewald, M.1    Kravchenko, V.V.2    Petrovan, R.J.3    O'Brien, P.J.4    Brass, L.F.5    Ulevitch, R.J.6
  • 431
    • 0034101945 scopus 로고    scopus 로고
    • Vascular endothelial growth factor production by fibroblasts in response to factor VIIa binding to tissue factor involves thrombin and factor Xa
    • Ollivier V, Chabbat J, Herbert JM, Hakim J, de Prost D. Vascular endothelial growth factor production by fibroblasts in response to factor VIIa binding to tissue factor involves thrombin and factor Xa. Arterioscler Thromb Vasc Biol 2000; 20: 1374-81.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1374-1381
    • Ollivier, V.1    Chabbat, J.2    Herbert, J.M.3    Hakim, J.4    de Prost, D.5
  • 432
    • 0037205286 scopus 로고    scopus 로고
    • Factor Xa releases matrix metalloproteinase-2 (MMP-2) from human vascular smooth muscle cells and stimulates the conversion of pro-MMP-2 to MMP-2: Role of MMP-2 in factor Xa-induced DNA synthesis and matrix invasion
    • Rauch BH, Bretschneider E, Braun M, Schror K. Factor Xa releases matrix metalloproteinase-2 (MMP-2) from human vascular smooth muscle cells and stimulates the conversion of pro-MMP-2 to MMP-2: role of MMP-2 in factor Xa-induced DNA synthesis and matrix invasion. Circ Res 2000; 31: 1122-7.
    • (2000) Circ. Res. , vol.31 , pp. 1122-1127
    • Rauch, B.H.1    Bretschneider, E.2    Braun, M.3    Schror, K.4
  • 433
    • 0033613183 scopus 로고    scopus 로고
    • How the protease thrombin talks to cells
    • Coughlin SR. How the protease thrombin talks to cells. Proc Natl Acad Sci USA 1999; 96: 11023-27.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11023-11027
    • Coughlin, S.R.1
  • 434
    • 0014191175 scopus 로고
    • Actions of thrombin and other coagulant and proteolytic enzymes on blood platelets
    • Davey M, Luscher E. Actions of thrombin and other coagulant and proteolytic enzymes on blood platelets. Nature (London) 1967; 216: 857-8.
    • (1967) Nature (London) , vol.216 , pp. 857-858
    • Davey, M.1    Luscher, E.2
  • 435
    • 0031681419 scopus 로고    scopus 로고
    • Thrombin receptor expression and responsiveness of human monocytic cells to thrombin is link to interferon-induced cellular differentiation
    • Naldini A, Sower L, Bocci V, Meyers B, Carney DH. Thrombin receptor expression and responsiveness of human monocytic cells to thrombin is link to interferon-induced cellular differentiation. J Cell Physiol 1998; 177: 76-84.
    • (1998) J. Cell Physiol. , vol.177 , pp. 76-84
    • Naldini, A.1    Sower, L.2    Bocci, V.3    Meyers, B.4    Carney, D.H.5
  • 436
    • 0028785163 scopus 로고
    • Thrombin enhances monocyte secretion of tumor necrosis factor and interleukin-1 beta by two distinct mechanisms
    • Hoffmann M, Cooper ST. Thrombin enhances monocyte secretion of tumor necrosis factor and interleukin-1 beta by two distinct mechanisms. Blood Cells Mol Dis 1995; 21: 156-67.
    • (1995) Blood Cells Mol. Dis. , vol.21 , pp. 156-167
    • Hoffmann, M.1    Cooper, S.T.2
  • 437
    • 0026462843 scopus 로고
    • Thrombin enhancement of interleukin-1 and tumor necrosis factor-alpha induced polymorphonuclear leukocyte migration
    • Drake WT, Lopes NN, Fenton JW Jr, Issekutz AC. Thrombin enhancement of interleukin-1 and tumor necrosis factor-alpha induced polymorphonuclear leukocyte migration. Lab Invest 1992; 67: 617-27.
    • (1992) Lab. Invest. , vol.67 , pp. 617-627
    • Drake, W.T.1    Lopes, N.N.2    Fenton Jr., J.W.3    Issekutz, A.C.4
  • 438
    • 0037035562 scopus 로고    scopus 로고
    • Thrombin induces IL-10 production in microglia as a negative feedback regulator of TNF-alpha release
    • Kim KY, Kim MY, Choi HS, Jin BK, Kim SU, Lee YB. Thrombin induces IL-10 production in microglia as a negative feedback regulator of TNF-alpha release. Neuroreport 2002; 13: 849-52.
    • (2002) Neuroreport , vol.13 , pp. 849-852
    • Kim, K.Y.1    Kim, M.Y.2    Choi, H.S.3    Jin, B.K.4    Kim, S.U.5    Lee, Y.B.6
  • 439
    • 0033822556 scopus 로고    scopus 로고
    • Thrombin-induced activation of cultured rodent microglia
    • Moller T, Hanisch UK, Ransom BR. Thrombin-induced activation of cultured rodent microglia. J Neurochem 2000; 75: 1539-47.
    • (2000) J. Neurochem. , vol.75 , pp. 1539-1547
    • Moller, T.1    Hanisch, U.K.2    Ransom, B.R.3
  • 440
    • 0034581513 scopus 로고    scopus 로고
    • Thrombin regulates the expression of proangiogenic cytokines via proteolytic activation of protease-activated receptor-1
    • Naldini A, Carney DH, Pucci A, Pasquali A, Carraro F. Thrombin regulates the expression of proangiogenic cytokines via proteolytic activation of protease-activated receptor-1. Gen Physiol 2000; 35: 255-9.
    • (2000) Gen. Physiol. , vol.35 , pp. 255-259
    • Naldini, A.1    Carney, D.H.2    Pucci, A.3    Pasquali, A.4    Carraro, F.5
  • 441
    • 0035884847 scopus 로고    scopus 로고
    • The IL-6 soluble IL-6R alpha autocrine loop of endothelial activation as an intermediate between acute and chroinc inflammation: An experimental model involving thrombin
    • Marin V, Montero-Julian FA, Gres S, Boulay V, Bongrand P, Farnarier C, Kapalnski G. The IL-6 soluble IL-6R alpha autocrine loop of endothelial activation as an intermediate between acute and chroinc inflammation: an experimental model involving thrombin. J Immunol 2001; 167: 3435-42.
    • (2001) J. Immunol. , vol.167 , pp. 3435-3442
    • Marin, V.1    Montero-Julian, F.A.2    Gres, S.3    Boulay, V.4    Bongrand, P.5    Farnarier, C.6    Kapalnski, G.7
  • 442
    • 0036464689 scopus 로고    scopus 로고
    • Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo
    • Szaba FM, Smiley ST. Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. Blood 2002; 99: 1053-9.
    • (2002) Blood , vol.99 , pp. 1053-1059
    • Szaba, F.M.1    Smiley, S.T.2
  • 443
    • 0032061273 scopus 로고    scopus 로고
    • Protease-activated receptors and their role n IL-6 and NF-IL-6 expression in human gingival fibroblasts
    • Hou L, Ravenall S, Macey MG, Harriott P, Kapas S, Howells GL. Protease-activated receptors and their role n IL-6 and NF-IL-6 expression in human gingival fibroblasts. J Periodontal Res 1998; 33: 205-11.
    • (1998) J. Periodontal. Res. , vol.33 , pp. 205-211
    • Hou, L.1    Ravenall, S.2    Macey, M.G.3    Harriott, P.4    Kapas, S.5    Howells, G.L.6
  • 444
    • 0033028896 scopus 로고    scopus 로고
    • Thrombin receptor mediated signals induce expressions of interleukin 6 and granulocyte colony stimulating factor via NF-kappa B activation in synovial fibroblasts
    • Shin H, Kitajima I, Nakajima T, Shao Q, Tokioka T, Takaski I, et al. Thrombin receptor mediated signals induce expressions of interleukin 6 and granulocyte colony stimulating factor via NF-kappa B activation in synovial fibroblasts. Ann Rheum Dis 1999; 58: 55-60.
    • (1999) Ann. Rheum. Dis. , vol.58 , pp. 55-60
    • Shin, H.1    Kitajima, I.2    Nakajima, T.3    Shao, Q.4    Tokioka, T.5    Takaski, I.6
  • 445
    • 0034319114 scopus 로고    scopus 로고
    • Thrombin induces IL-6 but not TNFalpha secretion by mouse mast cells: Threshold-level thrombin receptor and very low level Fcepsilon RI signaling synergistically enhance IL-6 secretion
    • Gordon JR, Zhang X, Stevenson K, Cosford K. Thrombin induces IL-6 but not TNFalpha secretion by mouse mast cells: threshold-level thrombin receptor and very low level Fcepsilon RI signaling synergistically enhance IL-6 secretion. Cell Immunol 2000; 205: 128-35.
    • (2000) Cell Immunol. , vol.205 , pp. 128-135
    • Gordon, J.R.1    Zhang, X.2    Stevenson, K.3    Cosford, K.4
  • 446
    • 0030893530 scopus 로고    scopus 로고
    • Thrombin and trypsin induce granulocyte-macrophage colony-stimulating factor and interleukin-6 gene expression in cultured normal human keratinocytes
    • Wakita H, Furukawa F, Takigawa M. Thrombin and trypsin induce granulocyte-macrophage colony-stimulating factor and interleukin-6 gene expression in cultured normal human keratinocytes. Proc Assoc Am Physicians 1997; 109: 190-207.
    • (1997) Proc. Assoc. Am. Physicians , vol.109 , pp. 190-207
    • Wakita, H.1    Furukawa, F.2    Takigawa, M.3
  • 448
    • 0034853329 scopus 로고    scopus 로고
    • Thrombin regulates chemokine induction during human retinal pigment epithelial cell/monocyte interaction
    • Yosida A, Elner SG, Bian ZM, Kunkel SL, Lukacs NW, Elner VM. Thrombin regulates chemokine induction during human retinal pigment epithelial cell/monocyte interaction. Am J Pathol 2001; 159: 1171-80.
    • (2001) Am. J. Pathol. , vol.159 , pp. 1171-1180
    • Yosida, A.1    Elner, S.G.2    Bian, Z.M.3    Kunkel, S.L.4    Lukacs, N.W.5    Elner, V.M.6
  • 449
    • 0033561364 scopus 로고    scopus 로고
    • Thrombin-induced interleukin 8 production and its regulation by interferon-gamma and prostaglandin E2 in human monocytic U937 cells
    • Suk K, Cha S. Thrombin-induced interleukin 8 production and its regulation by interferon-gamma and prostaglandin E2 in human monocytic U937 cells. Immunol Lett 1999; 67: 223-7.
    • (1999) Immunol. Lett. , vol.67 , pp. 223-227
    • Suk, K.1    Cha, S.2
  • 450
    • 0035437126 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase pathway plays a critical role in thrombin-induced endothelial chemokine production and leukocytye recruitment
    • Marin V, Farnarier C, Gres S, Kapalnski S, So MS, Dinarello CA, et al. The p38 mitogen-activated protein kinase pathway plays a critical role in thrombin-induced endothelial chemokine production and leukocytye recruitment. Blood 2001; 98: 667-73.
    • (2001) Blood , vol.98 , pp. 667-673
    • Marin, V.1    Farnarier, C.2    Gres, S.3    Kapalnski, S.4    So, M.S.5    Dinarello, C.A.6
  • 451
    • 0034748052 scopus 로고    scopus 로고
    • Pravastatin suppresses the interleukin-8 production induced by thrombin in human arotic endothelial cells cultured with high gucose by inhibiting the p44/42 mitogen activated protein kinase
    • Takata M, Urakaze M, Temaru R, Tamazaki K, Nakamura N, Nobata Y, et al. Pravastatin suppresses the interleukin-8 production induced by thrombin in human arotic endothelial cells cultured with high gucose by inhibiting the p44/42 mitogen activated protein kinase. Br J Pharmacol 2001; 134: 753-62.
    • (2001) Br. J. Pharmacol. , vol.134 , pp. 753-762
    • Takata, M.1    Urakaze, M.2    Temaru, R.3    Tamazaki, K.4    Nakamura, N.5    Nobata, Y.6
  • 452
    • 0031157455 scopus 로고    scopus 로고
    • Thrombin induces endothelial type II activation in vitro: IL-1 and TNF-alpha-independent IL-8 secretion and E-selectin expression
    • Kaplanski G, Fabrigoule M, Boulay V, Dinarello CA, Bongrand P, Kaplanski S, et al. Thrombin induces endothelial type II activation in vitro: IL-1 and TNF-alpha-independent IL-8 secretion and E-selectin expression. J Immunol 1997; 158: 5435-41.
    • (1997) J. Immunol. , vol.158 , pp. 5435-5441
    • Kaplanski, G.1    Fabrigoule, M.2    Boulay, V.3    Dinarello, C.A.4    Bongrand, P.5    Kaplanski, S.6
  • 455
    • 0034975449 scopus 로고    scopus 로고
    • Thrombin-induced MCP-1 expression involves activation of the p22phox-containing NADPH oxidase in human vascular smooth muscle cells
    • Brandes RP, Viedt C, Nguyen K, Beer S, Kreuzer J, Busse R, Gorlach A. Thrombin-induced MCP-1 expression involves activation of the p22phox-containing NADPH oxidase in human vascular smooth muscle cells. Thromb Haemost 2001; 85: 1104-10.
    • (2001) Thromb. Haemost. , vol.85 , pp. 1104-1110
    • Brandes, R.P.1    Viedt, C.2    Nguyen, K.3    Beer, S.4    Kreuzer, J.5    Busse, R.6    Gorlach, A.7
  • 456
    • 0034763273 scopus 로고    scopus 로고
    • Thrombin induces increased expression and secreation of VEGF from human FS4 fibroblasts, DU145 prostate cells and CHRF megakaryocytes
    • Huang YQ, Li JJ, Hu L, Lee M, Karpatkin S. Thrombin induces increased expression and secreation of VEGF from human FS4 fibroblasts, DU145 prostate cells and CHRF megakaryocytes. Thromb Haemost 2001; 86: 1094-8.
    • (2001) Thromb. Haemost. , vol.86 , pp. 1094-1098
    • Huang, Y.Q.1    Li, J.J.2    Hu, L.3    Lee, M.4    Karpatkin, S.5
  • 457
    • 0032529677 scopus 로고    scopus 로고
    • Thrombin-activated human endothelial cells support monocyte adhesion in vitro following expression of intercellular adhesion molecule-1 (ICAM-1; CD54) and vascular cell adhesion molecule-1 (VCAM-1; CD106)
    • Kaplanski G, Marin V, Fabrigoule M, Boulay V, Benoliel AM, Bongrand P, et al. Thrombin-activated human endothelial cells support monocyte adhesion in vitro following expression of intercellular adhesion molecule-1 (ICAM-1; CD54) and vascular cell adhesion molecule-1 (VCAM-1; CD106). Blood 1998; 92: 1259-67.
    • (1998) Blood , vol.92 , pp. 1259-1267
    • Kaplanski, G.1    Marin, V.2    Fabrigoule, M.3    Boulay, V.4    Benoliel, A.M.5    Bongrand, P.6
  • 458
    • 0035861596 scopus 로고    scopus 로고
    • Thrombin stimulation of the vascular cell adhesion molecule-1 promoter in endothelial cells is mediated by tandem nuclear factor-kappa B and GATA motifs
    • Minami T, Aird WC. Thrombin stimulation of the vascular cell adhesion molecule-1 promoter in endothelial cells is mediated by tandem nuclear factor-kappa B and GATA motifs. J Biol Chem 2001; 276: 47632-41.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47632-47641
    • Minami, T.1    Aird, W.C.2
  • 459
    • 0025195393 scopus 로고
    • Thrombin induces c-fos expression in cultured human endothelial cells by a Ca+2-dependent mechansim
    • Lampugnani MG, Colotta F, Polentarutti N, Pedenovi M, Mantovani A, Dejana E. Thrombin induces c-fos expression in cultured human endothelial cells by a Ca+2-dependent mechansim. Blood 1990; 76: 1173-80.
    • (1990) Blood , vol.76 , pp. 1173-1180
    • Lampugnani, M.G.1    Colotta, F.2    Polentarutti, N.3    Pedenovi, M.4    Mantovani, A.5    Dejana, E.6
  • 460
    • 0022205330 scopus 로고
    • Thrombin-mast cell interactions. Binding and cell activation
    • Razin E, Baranes D, Marx G. Thrombin-mast cell interactions. Binding and cell activation. Exp Cell Res 1985; 160: 380-6.
    • (1985) Exp. Cell Res. , vol.160 , pp. 380-386
    • Razin, E.1    Baranes, D.2    Marx, G.3
  • 461
    • 0028363702 scopus 로고
    • Fibrin degradation product D-dimer induces the synthesis and release of biologically active IL-1 beta, IL-6 and plasminogen activator inhibitors from monocytes in vitro
    • Robson SC, Shephard EG, Kirsch RE. Fibrin degradation product D-dimer induces the synthesis and release of biologically active IL-1 beta, IL-6 and plasminogen activator inhibitors from monocytes in vitro. Br J Haematol 1994; 86: 322-6.
    • (1994) Br. J. Haematol. , vol.86 , pp. 322-326
    • Robson, S.C.1    Shephard, E.G.2    Kirsch, R.E.3
  • 462
    • 0026074491 scopus 로고
    • FDP D-dimer induces the secretion of interleukin-1, urokinase-type-plasminogen activator, and plasminiogen activator inhibitor-2 in a human promonocytic leukiemia cell line
    • Hamaguchi M, Morishita Y, Takahashi I, Ogura M, Takamatsu J, Saito H. FDP D-dimer induces the secretion of interleukin-1, urokinase-type-plasminogen activator, and plasminiogen activator inhibitor-2 in a human promonocytic leukiemia cell line. Blood 1991; 77: 94-100.
    • (1991) Blood , vol.77 , pp. 94-100
    • Hamaguchi, M.1    Morishita, Y.2    Takahashi, I.3    Ogura, M.4    Takamatsu, J.5    Saito, H.6
  • 463
    • 0031697951 scopus 로고    scopus 로고
    • Prostaglandin-independent stimulation of interleukin-6 production by fibrinogen degradation product D in perfused murine liver
    • Csala M, Lerant I, Banhegyi G, Kardon T, Puskas F, Mucha I, et al. Prostaglandin-independent stimulation of interleukin-6 production by fibrinogen degradation product D in perfused murine liver. Scand J Immunol 1998; 48: 269-71.
    • (1998) Scand. J. Immunol. , vol.48 , pp. 269-271
    • Csala, M.1    Lerant, I.2    Banhegyi, G.3    Kardon, T.4    Puskas, F.5    Mucha, I.6
  • 464
    • 0033611621 scopus 로고    scopus 로고
    • Fragment E derived from both fibrin and fibrinogen stimulates interleukin-6 production in rat peritoneal macrophages
    • Lee ME, Rhee KJ, Nham SU. Fragment E derived from both fibrin and fibrinogen stimulates interleukin-6 production in rat peritoneal macrophages. Mol Cell 1999; 9: 7-13.
    • (1999) Mol. Cell , vol.9 , pp. 7-13
    • Lee, M.E.1    Rhee, K.J.2    Nham, S.U.3
  • 465
    • 0035745119 scopus 로고    scopus 로고
    • Fibrin fragment E stimulates the proliferation, migration and differentiation of human microvascular endothelial cells in vitro
    • Bootle-Wilbraham CA, Tazzyman S, Thompson WD, Stirk CM, Lewis CE. Fibrin fragment E stimulates the proliferation, migration and differentiation of human microvascular endothelial cells in vitro. Angiogenesis 2001; 4: 269-75.
    • (2001) Angiogenesis , vol.4 , pp. 269-275
    • Bootle-Wilbraham, C.A.1    Tazzyman, S.2    Thompson, W.D.3    Stirk, C.M.4    Lewis, C.E.5
  • 466
    • 0035961680 scopus 로고    scopus 로고
    • Fibrin stimulates microfilament reorganization and IL-1 beta production in human monocytic THP-1 cells
    • Lee ME, Kweon SM, Nham SU. Fibrin stimulates microfilament reorganization and IL-1 beta production in human monocytic THP-1 cells. Mol Cell 2001; 11: 13-20.
    • (2001) Mol. Cell , vol.11 , pp. 13-20
    • Lee, M.E.1    Kweon, S.M.2    Nham, S.U.3
  • 467
    • 0034326635 scopus 로고    scopus 로고
    • Fibrin(ogen)-induced expression of ICAM-1 and chemokines in human synovial fibroblasts
    • Liu X, Piela-Smith TH. Fibrin(ogen)-induced expression of ICAM-1 and chemokines in human synovial fibroblasts. J Immunol 2000; 165: 5255-61.
    • (2000) J. Immunol. , vol.165 , pp. 5255-5261
    • Liu, X.1    Piela-Smith, T.H.2
  • 468
    • 0002645732 scopus 로고    scopus 로고
    • Antithrombin deficiency
    • Scriver CR, Beaudet AL, Sly WS, Valle D, eds. 8th ed. New York, NY: McGraw-Hill
    • Tollefsen DM. Antithrombin deficiency. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The metabolic and molecular bases of inherited disease. 8th ed. New York, NY: McGraw-Hill; 2001: 4455-71.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 4455-4471
    • Tollefsen, D.M.1
  • 469
    • 17944378441 scopus 로고    scopus 로고
    • Decreased plasma activity of antithrombin or protein C is not due to consumption coagulopathy in septic patients with disseminated intravascular coagulation
    • Asakura H, Ontachi Y, Mizutani T, Kato M, Ito T, Saito M, et al. Decreased plasma activity of antithrombin or protein C is not due to consumption coagulopathy in septic patients with disseminated intravascular coagulation. Eur J Haematol 2001; 67: 170-5.
    • (2001) Eur. J. Haematol. , vol.67 , pp. 170-175
    • Asakura, H.1    Ontachi, Y.2    Mizutani, T.3    Kato, M.4    Ito, T.5    Saito, M.6
  • 470
    • 0036341343 scopus 로고    scopus 로고
    • Coagulation inhibition for sepsis
    • Key NS, Ely EW. Coagulation inhibition for sepsis. Curr Opin Hematol 2002; 9: 416-21.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 416-421
    • Key, N.S.1    Ely, E.W.2
  • 471
    • 0034797626 scopus 로고    scopus 로고
    • Antithrombin III inhibts lymphocyte proliferation, immunoglobulin production and mRNA expression of lymphocyte growth factors (IL-2, gamma-IFN and IL-4) in vitro
    • Zuo XJ, Nicolaidou E, Okada Y, Toyoda M, Jordan SC. Antithrombin III inhibts lymphocyte proliferation, immunoglobulin production and mRNA expression of lymphocyte growth factors (IL-2, gamma-IFN and IL-4) in vitro. Transpl Immunol 2001; 9: 1-6.
    • (2001) Transpl. Immunol. , vol.9 , pp. 1-6
    • Zuo, X.J.1    Nicolaidou, E.2    Okada, Y.3    Toyoda, M.4    Jordan, S.C.5
  • 472
    • 0035941066 scopus 로고    scopus 로고
    • The seine protease inhibitor antithrombin III inhibits LPS-mediated NF-kappaB activation by TLR-4
    • Mansell A, Reinicke A, Worrall DM, O'Neill LA. The seine protease inhibitor antithrombin III inhibits LPS-mediated NF-kappaB activation by TLR-4. FEBS Lett 2001; 508: 313-7.
    • (2001) FEBS Lett. , vol.508 , pp. 313-317
    • Mansell, A.1    Reinicke, A.2    Worrall, D.M.3    O'Neill, L.A.4
  • 473
    • 0031057343 scopus 로고    scopus 로고
    • The cytokine-mediated imblanced between coagulation and anticoagulation mechanism in sepsis and endotoxemia
    • Levi M, van der Poll T, ten Cate H, van Deventer SJH. The cytokine-mediated imblanced between coagulation and anticoagulation mechanism in sepsis and endotoxemia. Eur J Clin Invest 1997; 27: 3-9.
    • (1997) Eur. J. Clin. Invest. , vol.27 , pp. 3-9
    • Levi, M.1    van der Poll, T.2    ten Cate, H.3    van Deventer, S.J.H.4
  • 474
    • 0036493335 scopus 로고    scopus 로고
    • Antithrombin prevents endotoxin-induced hyptension by inhibiting the induction of nitric oxide synthesis in rats
    • Isobe H, Okajima K, Uchiba M, Harada N, Okabe H. Antithrombin prevents endotoxin-induced hyptension by inhibiting the induction of nitric oxide synthesis in rats. Blood 2002; 99: 1638-45.
    • (2002) Blood , vol.99 , pp. 1638-1645
    • Isobe, H.1    Okajima, K.2    Uchiba, M.3    Harada, N.4    Okabe, H.5
  • 475
  • 476
    • 0035007071 scopus 로고    scopus 로고
    • Inhibitory effects of antithrombin III against leukocyte rolling and infiltration during endotoxin-induced uveitis in rats
    • Yamashiro K, Kiryu J, Tsujikawa A, Honjo M, Nonaka A, Miyamoto K, et al. Inhibitory effects of antithrombin III against leukocyte rolling and infiltration during endotoxin-induced uveitis in rats. Invest Ophthalmol Vis Sci 2001; 42: 1553-60.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 1553-1560
    • Yamashiro, K.1    Kiryu, J.2    Tsujikawa, A.3    Honjo, M.4    Nonaka, A.5    Miyamoto, K.6
  • 477
    • 0035704379 scopus 로고    scopus 로고
    • Effects of antithrombin III on tumor necrosis factor-alpha and interleukin-1 beta synthesis in vascular smooth cells
    • Totzke G, Schobersberger W, Schloesser M, Czechowski M, Hoffmann GJ. Effects of antithrombin III on tumor necrosis factor-alpha and interleukin-1 beta synthesis in vascular smooth cells. J Interferon Cytokine Res 2001; 21: 1063-9.
    • (2001) J. Interferon. Cytokine Res. , vol.21 , pp. 1063-1069
    • Totzke, G.1    Schobersberger, W.2    Schloesser, M.3    Czechowski, M.4    Hoffmann, G.J.5
  • 478
    • 0036390175 scopus 로고    scopus 로고
    • Inhibition of human neutrophil chemotaxis toward interleukine 8 with six cinical antithrombin concentrates in vitro
    • Kaneider NC, Rabensteiner A, Reinisch CM, Dunzendorfer S, Wiedermann CJ. Inhibition of human neutrophil chemotaxis toward interleukine 8 with six cinical antithrombin concentrates in vitro. Intensive Care Med 2002; 28: 1447-52.
    • (2002) Intensive Care Med. , vol.28 , pp. 1447-1452
    • Kaneider, N.C.1    Rabensteiner, A.2    Reinisch, C.M.3    Dunzendorfer, S.4    Wiedermann, C.J.5
  • 479
    • 0036037343 scopus 로고    scopus 로고
    • The anti-inflammatory actions of antithrombin III
    • Wiedermann ChJ, Romisch J. The anti-inflammatory actions of antithrombin III. Acta Med Austriaca 2002; 29: 89-92.
    • (2002) Acta. Med. Austriaca. , vol.29 , pp. 89-92
    • Wiedermann, Ch.J.1    Romisch, J.2
  • 480
    • 0033810791 scopus 로고    scopus 로고
    • Therapeutic rationale for antithrombin III
    • Opal SM. Therapeutic rationale for antithrombin III. Crit Care Med 2000; 28: S34-7.
    • (2000) Crit. Care Med. , vol.28
    • Opal, S.M.1
  • 481
    • 0035904368 scopus 로고    scopus 로고
    • Caring for the critically ill patients. High-dose antithrombin III in severe sepsis: A randomized controlled trail
    • Warren BL, Eid A, Singer P, Pillay SS, Carl P, Novak I, et al. Caring for the critically ill patients. High-dose antithrombin III in severe sepsis: a randomized controlled trail. JAMA 2001; 286: 1869-78.
    • (2001) JAMA , vol.286 , pp. 1869-1878
    • Warren, B.L.1    Eid, A.2    Singer, P.3    Pillay, S.S.4    Carl, P.5    Novak, I.6
  • 482
    • 0000260461 scopus 로고    scopus 로고
    • Report of the international meeting on Intensive Care Medicine. Rome, Italy
    • Smith D. Report of the international meeting on Intensive Care Medicine. Rome, Italy. Critical Care 2000; 4: 255-62.
    • (2000) Critical Care , vol.4 , pp. 255-262
    • Smith, D.1
  • 483
    • 0034651773 scopus 로고    scopus 로고
    • Recombinant human antithrombin III improves survival and attenuates inflammatory responses in baboons lethally challenged with E. Coli
    • Minnema MC, Chang ACK, Jansen PM, Lubbers YTP, Pratt BM, Whittaker BG, et al. Recombinant human antithrombin III improves survival and attenuates inflammatory responses in baboons lethally challenged with E. Coli. Blood 2000; 95: 1117-23.
    • (2000) Blood , vol.95 , pp. 1117-1123
    • Minnema, M.C.1    Chang, A.C.K.2    Jansen, P.M.3    Lubbers, Y.T.P.4    Pratt, B.M.5    Whittaker, B.G.6
  • 484
    • 0036625064 scopus 로고    scopus 로고
    • Antithrombin III inhibits nuclear factor kappa B activation in human monocytes and vascular endothelial cells
    • Oelschlager C, Romisch J, Staubitz A, Stauss H, Leithauser B, Tillmanns H, et al. Antithrombin III inhibits nuclear factor kappa B activation in human monocytes and vascular endothelial cells. Blood 2002; 99: 4015-20.
    • (2002) Blood , vol.99 , pp. 4015-4020
    • Oelschlager, C.1    Romisch, J.2    Staubitz, A.3    Stauss, H.4    Leithauser, B.5    Tillmanns, H.6
  • 485
    • 0030615201 scopus 로고    scopus 로고
    • Nuclear factor-kappa B: A pivotal transcription factor in chronic inflammatory diseases
    • Barnes PI, Karin M. Nuclear factor-kappa B: a pivotal transcription factor in chronic inflammatory diseases. N Engl J Med 1997; 336: 1066-71.
    • (1997) N. Engl. J. Med. , vol.336 , pp. 1066-1071
    • Barnes, P.I.1    Karin, M.2
  • 486
    • 0035144440 scopus 로고    scopus 로고
    • Antithrombin inhibits lipopolysaccharide-induced tissue factor and interleukin-6 production by mononuclear cells, human umbilical vein endothelial cells, and whole blood
    • Souter PJ, Thomas S, Hubbard AR, Poole S, Romisch J, Gray E. Antithrombin inhibits lipopolysaccharide-induced tissue factor and interleukin-6 production by mononuclear cells, human umbilical vein endothelial cells, and whole blood. Crit Care Med 2001; 29: 134-9.
    • (2001) Crit. Care Med. , vol.29 , pp. 134-139
    • Souter, P.J.1    Thomas, S.2    Hubbard, A.R.3    Poole, S.4    Romisch, J.5    Gray, E.6
  • 487
    • 0035164538 scopus 로고    scopus 로고
    • Safety and dose relationship of recombinant human activated protein C for coagulopathy in severe sepsis
    • Barnard GR, Ely EW, Wright TJ, Fraiz J, Stasek JE, Russell JA, et al. Safety and dose relationship of recombinant human activated protein C for coagulopathy in severe sepsis. Crit Care Med 2001; 29: 2051-9.
    • (2001) Crit. Care Med. , vol.29 , pp. 2051-2059
    • Barnard, G.R.1    Ely, E.W.2    Wright, T.J.3    Fraiz, J.4    Stasek, J.E.5    Russell, J.A.6
  • 489
    • 0036250817 scopus 로고    scopus 로고
    • Recombinant human activated protein C attunates the inflammatory response in endothelium and monocytes by modulating nuclear factor-kappa B
    • Joyce DE, Grinnell BW. Recombinant human activated protein C attunates the inflammatory response in endothelium and monocytes by modulating nuclear factor-kappa B. Crit Care Med 2002; 30: S288-93.
    • (2002) Crit. Care Med. , vol.30
    • Joyce, D.E.1    Grinnell, B.W.2
  • 490
    • 0000001782 scopus 로고    scopus 로고
    • Activated protein C inhibits LPS-induced production of TNF-α by monocytes through inhibtion of activation of NFκB and MAPK pathways
    • Yuksel M, Uchiba M, Okjima K, Okabe H. Activated protein C inhibits LPS-induced production of TNF-α by monocytes through inhibtion of activation of NFκB and MAPK pathways. Thromb Haemost 2001; 85: S508-S516.
    • (2001) Thromb. Haemost. , vol.85
    • Yuksel, M.1    Uchiba, M.2    Okjima, K.3    Okabe, H.4
  • 491
    • 0034456899 scopus 로고    scopus 로고
    • Activated protein C inhibits tumor necrosis factor and macrophage migration inhibitory factor production in monocytes
    • Schmidt-Supprian M, Murphy C, White B, Lawler M, Kapurniotu A, Voelter W, et al. Activated protein C inhibits tumor necrosis factor and macrophage migration inhibitory factor production in monocytes. J Eur Cytokine Netw 2000; 11: 407-13.
    • (2000) J. Eur. Cytokine Netw. , vol.11 , pp. 407-413
    • Schmidt-Supprian, M.1    Murphy, C.2    White, B.3    Lawler, M.4    Kapurniotu, A.5    Voelter, W.6
  • 492
    • 0030909690 scopus 로고    scopus 로고
    • Activated protein C prevents LPS-induced pulmonary vascular injury by inhibiting cytokine production
    • Murakami K, Okajima K, Uchiba M, Johno M, Nakagaki T, Okabe H, et al. Activated protein C prevents LPS-induced pulmonary vascular injury by inhibiting cytokine production. Am J Physiol 1997; 272: L197-202.
    • (1997) Am. J. Physiol. , vol.272
    • Murakami, K.1    Okajima, K.2    Uchiba, M.3    Johno, M.4    Nakagaki, T.5    Okabe, H.6
  • 493
    • 0033880884 scopus 로고    scopus 로고
    • Activated protein C inhibits lipopolysaccharide-induced nuclear translocation of nuclear factor κB (NF-κB) and tumor necrosis factor α (TNF-α) production in the THP-1 moncytic cell line
    • White B, Schmidt M, Murrph C, Livingstone W, O'Toole DO, Lawler M, et al. Activated protein C inhibits lipopolysaccharide-induced nuclear translocation of nuclear factor κB (NF-κB) and tumor necrosis factor α (TNF-α) production in the THP-1 moncytic cell line. Br J Haematol 2000; 110: 130-34.
    • (2000) Br. J. Haematol. , vol.110 , pp. 130-134
    • White, B.1    Schmidt, M.2    Murrph, C.3    Livingstone, W.4    O'Toole, D.O.5    Lawler, M.6
  • 494
    • 0029626658 scopus 로고
    • Binding of activated protein C to a specific receptor on human monocuclear phagocytes inhibits intracellular calium signaling and monocyte dependent proliferative responses
    • Hancock WW, Grey ST, Hau L, Akalin E, Orthner C, Saygh MH, et al. Binding of activated protein C to a specific receptor on human monocuclear phagocytes inhibits intracellular calium signaling and monocyte dependent proliferative responses. Transplanation 1995; 60: 1525-32.
    • (1995) Transplanation , vol.60 , pp. 1525-1532
    • Hancock, W.W.1    Grey, S.T.2    Hau, L.3    Akalin, E.4    Orthner, C.5    Saygh, M.H.6
  • 495
    • 0035815747 scopus 로고    scopus 로고
    • Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis
    • Joyce DE, Gelbert L, Ciaccia A, DeHoff B, Grinnell BW. Gene expression profile of antithrombotic protein C defines new mechanisms modulating inflammation and apoptosis. J Biol Chem 2001; 276: 11199-203.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11199-11203
    • Joyce, D.E.1    Gelbert, L.2    Ciaccia, A.3    DeHoff, B.4    Grinnell, B.W.5
  • 496
    • 0032169362 scopus 로고    scopus 로고
    • The up-regulation of IL-6 and IL-8 in human endothelial cells by activated protein C
    • Hooper WC, Phillips DJ, Renshaw MA, Evatt BL, Benson JM. The up-regulation of IL-6 and IL-8 in human endothelial cells by activated protein C. J Immunol 1998; 16: 2567-73.
    • (1998) J. Immunol. , vol.16 , pp. 2567-2573
    • Hooper, W.C.1    Phillips, D.J.2    Renshaw, M.A.3    Evatt, B.L.4    Benson, J.M.5
  • 497
    • 0035424850 scopus 로고    scopus 로고
    • Activated protein C induction of MCP-1 in human endothelial cells: A possible role for edothelial cell nitric oxide synthase
    • Hooper WC, Phillips DJ, Renshaw MA. Activated protein C induction of MCP-1 in human endothelial cells: a possible role for edothelial cell nitric oxide synthase. Thromb Res 2001; 103: 209-19.
    • (2001) Thromb. Res. , vol.103 , pp. 209-219
    • Hooper, W.C.1    Phillips, D.J.2    Renshaw, M.A.3
  • 498
    • 0028853552 scopus 로고
    • Recombinant human soluble thrombomodolin reduces endotoxin-induced pulmonary vascular injury via protein C activation in rats
    • Uchiba M, Okajima K, Murakami K, Nawa H, Okabe H, Takatsuki, K. Recombinant human soluble thrombomodolin reduces endotoxin-induced pulmonary vascular injury via protein C activation in rats. Thromb Haemost 1995; 74: 1265-70.
    • (1995) Thromb Haemost , vol.74 , pp. 1265-1270
    • Uchiba, M.1    Okajima, K.2    Murakami, K.3    Nawa, H.4    Okabe, H.5    Takatsuki, K.6
  • 499
    • 0029819270 scopus 로고    scopus 로고
    • Recombinant thrombomodulin prevents endotoxin-induced lung injury by inhbiting activation of leukocyts in rats
    • Uchiba M, Okajima K, Murakami K, Johno M, Okabe H, Takatsuki, K. Recombinant thrombomodulin prevents endotoxin-induced lung injury by inhbiting activation of leukocyts in rats. Am J Physiol 1996; 271: L470-5.
    • (1996) Am. J. Physiol. , vol.271
    • Uchiba, M.1    Okajima, K.2    Murakami, K.3    Johno, M.4    Okabe, H.5    Takatsuki, K.6
  • 501
    • 0031056525 scopus 로고    scopus 로고
    • Effect of urinary thrombomodulin on endotoxin-induced intravascular coagulation and pulmonary vascular injury in rats
    • Uchiba M, Okajima K, Murakami K, Johno M, Okabe H, Takatsuki K. Effect of urinary thrombomodulin on endotoxin-induced intravascular coagulation and pulmonary vascular injury in rats. Am J Hematol 1997; 54: 118-23.
    • (1997) Am. J. Hematol. , vol.54 , pp. 118-123
    • Uchiba, M.1    Okajima, K.2    Murakami, K.3    Johno, M.4    Okabe, H.5    Takatsuki, K.6
  • 503
    • 0030926515 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor blocks cellular effects of endotoxin by binding to endotoxin and interfering with transfer to CD14
    • Park CT, Creasey AA, Wright SD. Tissue factor pathway inhibitor blocks cellular effects of endotoxin by binding to endotoxin and interfering with transfer to CD14. Blood 1997; 89: 4268-74.
    • (1997) Blood , vol.89 , pp. 4268-4274
    • Park, C.T.1    Creasey, A.A.2    Wright, S.D.3
  • 504
    • 18844480902 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor dose-dependently inhibits coagulation activation without influencing the fibrinolytic and cytokine response during human endotoxemia
    • de Jonge E, Dekkers PE, Creasey AA, Hack CE, Paulson SK, Karim A, et al. Tissue factor pathway inhibitor dose-dependently inhibits coagulation activation without influencing the fibrinolytic and cytokine response during human endotoxemia. Blood 1999; 95: 1124-29.
    • (1999) Blood , vol.95 , pp. 1124-1229
    • de Jonge, E.1    Dekkers, P.E.2    Creasey, A.A.3    Hack, C.E.4    Paulson, S.K.5    Karim, A.6
  • 505
    • 0035876892 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor does not influence inflammatory pathways during human endotoxemia
    • de Jonge E, Dekkers PE, Creasey AA, Hack CE, Paulson SK, Karim A, et al. Tissue factor pathway inhibitor does not influence inflammatory pathways during human endotoxemia. J Infect Dis 2001; 183: 1815-8.
    • (2001) J. Infect. Dis. , vol.183 , pp. 1815-1818
    • de Jonge, E.1    Dekkers, P.E.2    Creasey, A.A.3    Hack, C.E.4    Paulson, S.K.5    Karim, A.6
  • 506
    • 0034933683 scopus 로고    scopus 로고
    • Mechanistic coupling of protease signaling and initiation of coagulation by tissue factor
    • Riewald M, Ruf W. Mechanistic coupling of protease signaling and initiation of coagulation by tissue factor. Proc Natl Acad Sci USA 2001; 98: 7742-7.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7742-7747
    • Riewald, M.1    Ruf, W.2


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