메뉴 건너뛰기




Volumn 11, Issue 1 P.1-446, 2006, Pages 256-271

Role of tissue factor in thrombosis. Coagulation-inflammation-thrombosis circuit

Author keywords

Cardiovascular system; Heart; Hypercoagulability; Inflammation; Protease Activated Receptor; Review; Thrombosis; Tissue Factor; Vessel

Indexed keywords

THROMBUS;

EID: 32844470037     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1796     Document Type: Review
Times cited : (36)

References (190)
  • 1
    • 0028932993 scopus 로고
    • Tissue pathway inhibitor and revised theory of coagulation
    • Broze G. J. Jr.: Tissue pathway inhibitor and revised theory of coagulation. Annu Rev Med 46, 103-112 (1995)
    • (1995) Annu Rev Med , vol.46 , pp. 103-112
    • Broze Jr., G.J.1
  • 2
    • 0030872898 scopus 로고    scopus 로고
    • The structural basis of function of the TF/VIIa complex in the cellular initiation of coagulation
    • Edgington T. S., Dickinson C.D. & W. Ruf: The structural basis of function of the TF/VIIa complex in the cellular initiation of coagulation. Thromb Haemost 78, 401-405 (1997)
    • (1997) Thromb Haemost , vol.78 , pp. 401-405
    • Edgington, T.S.1    Dickinson, C.D.2    Ruf, W.3
  • 3
    • 3042696879 scopus 로고    scopus 로고
    • Biochemical strategies to anticoagulation: A comparative overview
    • Chu A. J.: Biochemical strategies to anticoagulation: a comparative overview. Curr Vasc Pharmacol 2, 199-228 (2004)
    • (2004) Curr Vasc Pharmacol , vol.2 , pp. 199-228
    • Chu, A.J.1
  • 4
    • 23744503066 scopus 로고    scopus 로고
    • Tissue factor mediates inflammation
    • in press
    • Chu A. J.: Tissue factor mediates inflammation. Arch Biochem Biophys (2005) (in press)
    • (2005) Arch Biochem Biophys
    • Chu, A.J.1
  • 5
    • 0037673379 scopus 로고    scopus 로고
    • Tissue factor signal transduction in angiogenesis
    • Versteeg H. H., M. P. Peppelenbosch & C. A. Spek: Tissue factor signal transduction in angiogenesis. Carcinogenesis 24, 1009-1013 (2003)
    • (2003) Carcinogenesis , vol.24 , pp. 1009-1013
    • Versteeg, H.H.1    Peppelenbosch, M.P.2    Spek, C.A.3
  • 6
    • 0036341469 scopus 로고    scopus 로고
    • Tissue factor and angiogenesis in cancer
    • Fernandez P. M. & F. R. Rickles: Tissue factor and angiogenesis in cancer. Curr Opin Hematol 9, 401-406 (2002)
    • (2002) Curr Opin Hematol , vol.9 , pp. 401-406
    • Fernandez, P.M.1    Rickles, F.R.2
  • 8
    • 0032498848 scopus 로고    scopus 로고
    • A role for tissue factor in cell adhesion and migration mediated by interaction with actin-binding protein 280
    • Ott I., E. G. Fischer, Y. Miyagi, B. M. Mueller & W. Ruf: A role for tissue factor in cell adhesion and migration mediated by interaction with actin-binding protein 280. J Cell Biol 140, 1241-1253 (1998)
    • (1998) J Cell Biol , vol.140 , pp. 1241-1253
    • Ott, I.1    Fischer, E.G.2    Miyagi, Y.3    Mueller, B.M.4    Ruf, W.5
  • 10
    • 0032523148 scopus 로고    scopus 로고
    • Tissue factor-dependent vascular endothelial growth factor production by human fibroblasts in response to activated factor VII
    • Ollivier V., S. Bentolila, J. Chabbat, J. Hakim & D. de Prost: Tissue factor-dependent vascular endothelial growth factor production by human fibroblasts in response to activated factor VII. Blood 91, 2698-2703 (1998)
    • (1998) Blood , vol.91 , pp. 2698-2703
    • Ollivier, V.1    Bentolila, S.2    Chabbat, J.3    Hakim, J.4    De Prost, D.5
  • 11
    • 32844469661 scopus 로고    scopus 로고
    • Tissue factor upregulation drives a thrombosis-inflammation circuit in relation to cardiovascular complications
    • Epub ahead of print
    • Chu A. J.: Tissue factor upregulation drives a thrombosis-inflammation circuit in relation to cardiovascular complications. Cell Biochem Funct Dec 22; [Epub ahead of print] (2004)
    • (2004) Cell Biochem Funct Dec , vol.22
    • Chu, A.J.1
  • 13
    • 0038306868 scopus 로고    scopus 로고
    • Coagulation dysfunction in sepsis and multiple organ system failure
    • Nimah M. & R. J. Brilli: Coagulation dysfunction in sepsis and multiple organ system failure. Crit Care Clin 19, 441-458 (2003)
    • (2003) Crit Care Clin , vol.19 , pp. 441-458
    • Nimah, M.1    Brilli, R.J.2
  • 16
    • 0038141058 scopus 로고    scopus 로고
    • Apoptosis, a major determinant of atherothrombosis
    • Tedgui A. & Z. Mallat: Apoptosis, a major determinant of atherothrombosis. Arch Mal Coeur Vaiss 96, 671-675 (2003)
    • (2003) Arch Mal Coeur Vaiss , vol.96 , pp. 671-675
    • Tedgui, A.1    Mallat, Z.2
  • 17
    • 0031005422 scopus 로고    scopus 로고
    • Mechanism of tissue factor activation on HL-60 cells
    • Bach R. R. & C. F. Moldow: Mechanism of tissue factor activation on HL-60 cells. Blood 89, 3270-3276 (1997)
    • (1997) Blood , vol.89 , pp. 3270-3276
    • Bach, R.R.1    Moldow, C.F.2
  • 18
    • 0035851276 scopus 로고    scopus 로고
    • Hypercoagulability syndromes
    • Thomas R. H. Hypercoagulability syndromes. Arch Intern Med. 161, 2433-2439 (2001)
    • (2001) Arch Intern Med. , vol.161 , pp. 2433-2439
    • Thomas, R.H.1
  • 19
    • 0842320985 scopus 로고    scopus 로고
    • Vascular biology-the role of tissue factor
    • Hathcock J.: Vascular biology-the role of tissue factor. Semin Hematol 41(S1), 30-34 (2004)
    • (2004) Semin Hematol , vol.41 , Issue.S1 , pp. 30-34
    • Hathcock, J.1
  • 20
    • 0032722282 scopus 로고    scopus 로고
    • Changes in the levels of soluble adhesion molecules and coagulation factors in patients with deep vein thrombosis
    • Smith A., J. W. Quarmby, M. Collins, S. M. Lockhart & K. G. Burnand: Changes in the levels of soluble adhesion molecules and coagulation factors in patients with deep vein thrombosis. Thromb Haemost 82, 1593-1599 (1999)
    • (1999) Thromb Haemost , vol.82 , pp. 1593-1599
    • Smith, A.1    Quarmby, J.W.2    Collins, M.3    Lockhart, S.M.4    Burnand, K.G.5
  • 22
    • 0029052487 scopus 로고
    • Retinoic acid reduces induction of monocyte tissue factor and tissue factor/factor VIIa-dependent arterial thrombus formation
    • Barstad R. M., M. J. Hamers, R. W. Stephens & K. S. Sakariassen: Retinoic acid reduces induction of monocyte tissue factor and tissue factor/factor VIIa-dependent arterial thrombus formation. Blood 86, 212-218 (1995)
    • (1995) Blood , vol.86 , pp. 212-218
    • Barstad, R.M.1    Hamers, M.J.2    Stephens, R.W.3    Sakariassen, K.S.4
  • 23
    • 0028942291 scopus 로고
    • Procoagulant human monocytes mediate tissue factor/factor VIIa-dependent platelet-thrombus formation when exposed to flowing nonanticoagulated human blood
    • Barstad R. M., M. J. Hamers, P. Kierulf, A. B. Westvik & K. S. Sakariassen: Procoagulant human monocytes mediate tissue factor/factor VIIa-dependent platelet-thrombus formation when exposed to flowing nonanticoagulated human blood. Arterioscler Thromb Vasc Biol 15, 11-16 (1995)
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 11-16
    • Barstad, R.M.1    Hamers, M.J.2    Kierulf, P.3    Westvik, A.B.4    Sakariassen, K.S.5
  • 24
    • 0029984074 scopus 로고    scopus 로고
    • Procoagulant activity on injured arteries and associated thrombi is mediated primarily by the complex of tissue factor and factor VIIa
    • Speidel C. M., J. D. Thornton, Y. Y. Meng, P. R. Eisenberg, T. S. Edgington & D. R. Abendschein: Procoagulant activity on injured arteries and associated thrombi is mediated primarily by the complex of tissue factor and factor VIIa. Coron Artery Dis 7, 57-62 (1996)
    • (1996) Coron Artery Dis , vol.7 , pp. 57-62
    • Speidel, C.M.1    Thornton, J.D.2    Meng, Y.Y.3    Eisenberg, P.R.4    Edgington, T.S.5    Abendschein, D.R.6
  • 25
    • 0035871156 scopus 로고    scopus 로고
    • Inhibition of tissue factor-activated platelets by low-molecular-weight heparins and glycoprotein IIb/IIIa receptor antagonist
    • Ahmad S., W. P. Jeske, Q. Ma, J. M. Walenga & J. Fareed: Inhibition of tissue factor-activated platelets by low-molecular-weight heparins and glycoprotein IIb/IIIa receptor antagonist. Thromb Res 102, 143-151 (2001)
    • (2001) Thromb Res , vol.102 , pp. 143-151
    • Ahmad, S.1    Jeske, W.P.2    Ma, Q.3    Walenga, J.M.4    Fareed, J.5
  • 26
    • 0038630698 scopus 로고    scopus 로고
    • Effects of recombinant factor VIIa on platelet function and clot structure in blood with deficient prothrombin conversion
    • Carr M. E. Jr., E. J. Martin, J. G. Kuhn & S. V. Seremetis: Effects of recombinant factor VIIa on platelet function and clot structure in blood with deficient prothrombin conversion. Thromb Haemost 89, 803-811 (2003)
    • (2003) Thromb Haemost , vol.89 , pp. 803-811
    • Carr Jr., M.E.1    Martin, E.J.2    Kuhn, J.G.3    Seremetis, S.V.4
  • 27
    • 0242580099 scopus 로고    scopus 로고
    • Interaction between platelets and the coagulation system
    • (Ed: Michelson A.) Academic Press, San Diego
    • Bouchard B. A., S. Butenas, K. G. Mann & P. B. Tracy: Interaction between platelets and the coagulation system. In Platelets (Ed: Michelson A.) Academic Press, San Diego, p 229-253 (2002)
    • (2002) Platelets , pp. 229-253
    • Bouchard, B.A.1    Butenas, S.2    Mann, K.G.3    Tracy, P.B.4
  • 28
    • 0033824021 scopus 로고    scopus 로고
    • rFVIIa-its thrombogenicity
    • Aledort L. M.: rFVIIa-its thrombogenicity. Thromb Haemost 84, 522-523 (2000)
    • (2000) Thromb Haemost , vol.84 , pp. 522-523
    • Aledort, L.M.1
  • 31
    • 0032418249 scopus 로고    scopus 로고
    • Local delivery of a tissue factor antibody reduces early leukocyte infiltration but fails to limit intimal hyperplasia in experimental vein grafts
    • Annex B. H., M. G. Davies, G. J. Fulton, T. T. Huynh, K. M. Channon, M. D. Ezekowitz & P. O. Hagen: Local delivery of a tissue factor antibody reduces early leukocyte infiltration but fails to limit intimal hyperplasia in experimental vein grafts. J Surg Res 80, 164-170 (1998)
    • (1998) J Surg Res , vol.80 , pp. 164-170
    • Annex, B.H.1    Davies, M.G.2    Fulton, G.J.3    Huynh, T.T.4    Channon, K.M.5    Ezekowitz, M.D.6    Hagen, P.O.7
  • 32
    • 4544368518 scopus 로고    scopus 로고
    • The effect of vascular smooth muscle cell-targeted expression of tissue factor pathway inhibitor in a murine model of arterial thrombosis
    • Pan S., L. S. Kleppe, T. A. Witt, C. S. Mueske & R. D. Simari: The effect of vascular smooth muscle cell-targeted expression of tissue factor pathway inhibitor in a murine model of arterial thrombosis. Thromb Haemost 92, 495-502 (2004)
    • (2004) Thromb Haemost , vol.92 , pp. 495-502
    • Pan, S.1    Kleppe, L.S.2    Witt, T.A.3    Mueske, C.S.4    Simari, R.D.5
  • 33
    • 0035954299 scopus 로고    scopus 로고
    • Deficiency of tissue factor pathway inhibitor promotes atherosclerosis and thrombosis in mice
    • Westrick R. J., P. F. Bodary, Z. Xu, Y. C. Shen, G. J. Broze & D. T. Eitzman: Deficiency of tissue factor pathway inhibitor promotes atherosclerosis and thrombosis in mice. Circulation 103, 3044-3046 (2001)
    • (2001) Circulation , vol.103 , pp. 3044-3046
    • Westrick, R.J.1    Bodary, P.F.2    Xu, Z.3    Shen, Y.C.4    Broze, G.J.5    Eitzman, D.T.6
  • 34
    • 3943103349 scopus 로고    scopus 로고
    • Anti-tissue factor pathway inhibitor activity in subjects with antiphospholipid syndrome is associated with increased thrombin generation
    • Adams M., L. Breckler, P. Stevens, J. Thorn, R. Baker & R. Oostryck: Anti-tissue factor pathway inhibitor activity in subjects with antiphospholipid syndrome is associated with increased thrombin generation. Haematologica 89, 985-990 (2004)
    • (2004) Haematologica , vol.89 , pp. 985-990
    • Adams, M.1    Breckler, L.2    Stevens, P.3    Thorn, J.4    Baker, R.5    Oostryck, R.6
  • 35
    • 0001795967 scopus 로고
    • Pathogenesis of thrombosis
    • (Eds: Williams WJ, Beutler E, Erslev AJ, Lictman MA.) McGraw-Hill, New York
    • Harker L. A.: Pathogenesis of thrombosis. In Hematology (Eds: Williams WJ, Beutler E, Erslev AJ, Lictman MA.) McGraw-Hill, New York, 1559-1568 (1990)
    • (1990) Hematology , pp. 1559-1568
    • Harker, L.A.1
  • 36
    • 0028919701 scopus 로고
    • Thrombin hypothesis of thrombus generation and vascular lesion formation
    • Harker L. A., S. R. Hanson & M. Runge: Thrombin hypothesis of thrombus generation and vascular lesion formation. Am J Cardio 75, 12B-17B (1995)
    • (1995) Am J Cardio , vol.75
    • Harker, L.A.1    Hanson, S.R.2    Runge, M.3
  • 37
    • 0842320987 scopus 로고    scopus 로고
    • New insights into factors affecting clot stability: A role for thrombin activatable fibrinolysis inhibitor (TAFI; plasma procarboxypeptidase B, plasma procarboxypeptidase U, procarboxypeptidase R)
    • Bouma B. N. & J. C. Meijers: New insights into factors affecting clot stability: A role for thrombin activatable fibrinolysis inhibitor (TAFI; plasma procarboxypeptidase B, plasma procarboxypeptidase U, procarboxypeptidase R) Semin Hematol 41 (S1), 13-19 (2004)
    • (2004) Semin Hematol , vol.41 , Issue.S1 , pp. 13-19
    • Bouma, B.N.1    Meijers, J.C.2
  • 38
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • van Tilburg N. H., F. R. Rosendaal & R. M. Bertina: Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis Blood 95, 2855-2859 (2000)
    • (2000) Blood , vol.95 , pp. 2855-2859
    • Van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 39
    • 0035479232 scopus 로고    scopus 로고
    • Activity and antigen levels of thrombin-activatable fibrinolysis inhibitor in plasma of patients with disseminated intravascular coagulation
    • Watanabe R., H. Wada, Y. Watanabe, M. Sakakura, T. Nakasaki, Y. Mori, M. Nishikawa, E. C. Gabazza, T. Nobori & H. Shiku: Activity and antigen levels of thrombin-activatable fibrinolysis inhibitor in plasma of patients with disseminated intravascular coagulation. Thromb Res 104, 1-6 (2001)
    • (2001) Thromb Res , vol.104 , pp. 1-6
    • Watanabe, R.1    Wada, H.2    Watanabe, Y.3    Sakakura, M.4    Nakasaki, T.5    Mori, Y.6    Nishikawa, M.7    Gabazza, E.C.8    Nobori, T.9    Shiku, H.10
  • 40
    • 0037383184 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor levels in the acute phase of ischemic stroke
    • Montaner J., M. Ribo, J. Monasterio, C. A. Molina & J. Alvarez-Sabin: Thrombin-activable fibrinolysis inhibitor levels in the acute phase of ischemic stroke. Stroke 34, 1038-1040 (2003)
    • (2003) Stroke , vol.34 , pp. 1038-1040
    • Montaner, J.1    Ribo, M.2    Monasterio, J.3    Molina, C.A.4    Alvarez-Sabin, J.5
  • 42
    • 1642380858 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor (TAFI) affects fibrinolysis in a plasminogen activator concentration-dependent manner. Study of seven plasminogen activators in an internal clot lysis model
    • Guimaraes A. H. & D. C. Rijken: Thrombin activatable fibrinolysis inhibitor (TAFI) affects fibrinolysis in a plasminogen activator concentration-dependent manner. Study of seven plasminogen activators in an internal clot lysis model. Thromb Haemost 91, 473-479 (2004)
    • (2004) Thromb Haemost , vol.91 , pp. 473-479
    • Guimaraes, A.H.1    Rijken, D.C.2
  • 43
    • 1642398603 scopus 로고    scopus 로고
    • Thrombus lysis by uPA, scuPA and tPA is regulated by plasma TAFI
    • Mutch N. J., N. R. Moore, E. Wang & N. A. Booth: Thrombus lysis by uPA, scuPA and tPA is regulated by plasma TAFI. J Thromb Haemost 1, 2000-2007 (2003)
    • (2003) J Thromb Haemost , vol.1 , pp. 2000-2007
    • Mutch, N.J.1    Moore, N.R.2    Wang, E.3    Booth, N.A.4
  • 44
    • 0032538557 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor
    • Wang W., M. B. Boffa, L. Bajzar, J. B. Walker & M. E. Nesheim: A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 273, 27176-2781 (1998)
    • (1998) J Biol Chem , vol.273 , pp. 27176-32781
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3    Walker, J.B.4    Nesheim, M.E.5
  • 45
    • 1842728323 scopus 로고    scopus 로고
    • Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin
    • Schneider M., N. Brufatto, E. Neill & M. Nesheim: Activated thrombin-activatable fibrinolysis inhibitor reduces the ability of high molecular weight fibrin degradation products to protect plasmin from antiplasmin. J Biol Chem 279, 13340-13345 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 13340-13345
    • Schneider, M.1    Brufatto, N.2    Neill, E.3    Nesheim, M.4
  • 46
    • 1842678168 scopus 로고    scopus 로고
    • A study of the protection of plasmin from antiplasmin inhibition within an intact fibrin clot during the course of clot lysis
    • Schneider M. & M. Nesheim: A study of the protection of plasmin from antiplasmin inhibition within an intact fibrin clot during the course of clot lysis. J Biol Chem 279, 13333-13339 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 13333-13339
    • Schneider, M.1    Nesheim, M.2
  • 47
    • 0033430107 scopus 로고    scopus 로고
    • Thrombin upregulates production of plasminogen activator inhibitor type 1 in human peritoneal mesothelial cells
    • Mandl-Weber S., B. Haslinger & T. Sitter: Thrombin upregulates production of plasminogen activator inhibitor type 1 in human peritoneal mesothelial cells. Peril Dial Int 19, 319-324 (1999)
    • (1999) Peril Dial Int , vol.19 , pp. 319-324
    • Mandl-Weber, S.1    Haslinger, B.2    Sitter, T.3
  • 49
  • 51
    • 0036681940 scopus 로고    scopus 로고
    • Characterization of thrombin-induced leukocyte rolling and adherence: A potential proinflammatory role for proteinase-activated receptor-4
    • Vergnolle N., C. K. Derian, M. R. D'Andrea, M. Steinhoff & P. Andrade-Gordon: Characterization of thrombin-induced leukocyte rolling and adherence: a potential proinflammatory role for proteinase-activated receptor-4. J Immunol 169, 1467-1473 (2002)
    • (2002) J Immunol , vol.169 , pp. 1467-1473
    • Vergnolle, N.1    Derian, C.K.2    D'Andrea, M.R.3    Steinhoff, M.4    Andrade-Gordon, P.5
  • 53
    • 0033571257 scopus 로고    scopus 로고
    • Tissue factor and factor VIIa receptor/ligand interactions induce proinflammatory effects in macrophages
    • Cunningham M. A., P. Romas, P. Hutchinson, S. R. Holdsworth & P. G. Tipping: Tissue factor and factor VIIa receptor/ligand interactions induce proinflammatory effects in macrophages. Blood 94, 3413-3420 (1999)
    • (1999) Blood , vol.94 , pp. 3413-3420
    • Cunningham, M.A.1    Romas, P.2    Hutchinson, P.3    Holdsworth, S.R.4    Tipping, P.G.5
  • 54
    • 0038633316 scopus 로고    scopus 로고
    • Activation of coagulation by administration of recombinant factor VIIa elicits interleukin 6 (IL-6) and IL-8 release in healthy human subjects
    • De Jonge E., P. W. Friederich, G. P. Vlasuk, W. E. Rote, M. B. Vroom, M. Levi & T. van der Poll: Activation of coagulation by administration of recombinant factor VIIa elicits interleukin 6 (IL-6) and IL-8 release in healthy human subjects. Clin Diagn Lab Immunol 10, 495-497 (2003)
    • (2003) Clin Diagn Lab Immunol , vol.10 , pp. 495-497
    • De Jonge, E.1    Friederich, P.W.2    Vlasuk, G.P.3    Rote, W.E.4    Vroom, M.B.5    Levi, M.6    Van Der Poll, T.7
  • 55
    • 0031057653 scopus 로고    scopus 로고
    • The effect of factor Xa/phospholipid infusion on the acute phase response in baboons
    • Kruithof E. K., D. Agay, J. C. Mestries, M. P. Gascon & A. Ythier: The effect of factor Xa/phospholipid infusion on the acute phase response in baboons. Thromb Haemost 77, 308-311 (1997)
    • (1997) Thromb Haemost , vol.77 , pp. 308-311
    • Kruithof, E.K.1    Agay, D.2    Mestries, J.C.3    Gascon, M.P.4    Ythier, A.5
  • 56
    • 0036464689 scopus 로고    scopus 로고
    • Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo
    • Szaba F. M. & S. T. Smiley: Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. Blood 99, 1053-1059 (2002)
    • (2002) Blood , vol.99 , pp. 1053-1059
    • Szaba, F.M.1    Smiley, S.T.2
  • 57
    • 0030978393 scopus 로고    scopus 로고
    • The coagulation and fibrinolytic responses of baboons after in vivo thrombin generation-effect of interleukin 6
    • Kruithof E. K., J. C. Mestries, M. P. Gascon & A. Ythier: The coagulation and fibrinolytic responses of baboons after in vivo thrombin generation-effect of interleukin 6. Thromb Haemost 77, 905-910 (1997)
    • (1997) Thromb Haemost , vol.77 , pp. 905-910
    • Kruithof, E.K.1    Mestries, J.C.2    Gascon, M.P.3    Ythier, A.4
  • 58
    • 12444303861 scopus 로고    scopus 로고
    • Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P-selectin glycoprotein ligand 1 and platelet P-selectin
    • Falati S., Q. Liu, P. Gross, G. Merrill-Skoloff, J. Chou, E. Vandendries, A. Celi, K. Croce, B. C. Furie & B. Furie: Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P-selectin glycoprotein ligand 1 and platelet P-selectin. J Exp Med 197, 1585-1598 (2003)
    • (2003) J Exp Med , vol.197 , pp. 1585-1598
    • Falati, S.1    Liu, Q.2    Gross, P.3    Merrill-Skoloff, G.4    Chou, J.5    Vandendries, E.6    Celi, A.7    Croce, K.8    Furie, B.C.9    Furie, B.10
  • 59
    • 0035317069 scopus 로고    scopus 로고
    • Pulmonary tissue factor mRNA expression during murine traumatic shock: Effect of P-selectin blockade
    • Armstead V. E., A. G. Minchenko, R. Scalla & A. M. Lefer: Pulmonary tissue factor mRNA expression during murine traumatic shock: effect of P-selectin blockade. Shock 15, 323-326 (2001)
    • (2001) Shock , vol.15 , pp. 323-326
    • Armstead, V.E.1    Minchenko, A.G.2    Scalla, R.3    Lefer, A.M.4
  • 62
    • 0343742520 scopus 로고    scopus 로고
    • Activation of monocyte/macrophage functions related to acute atheroma complication by ligation of CD40: Induction of collagenase, stromelysin, and tissue factor
    • Mach F., U. Schonbeck, J. Y. Bonnefoy, J. S. Pober & P. Libby: Activation of monocyte/macrophage functions related to acute atheroma complication by ligation of CD40: induction of collagenase, stromelysin, and tissue factor. Circulation 96, 396-399 (1997)
    • (1997) Circulation , vol.96 , pp. 396-399
    • Mach, F.1    Schonbeck, U.2    Bonnefoy, J.Y.3    Pober, J.S.4    Libby, P.5
  • 63
    • 0036592015 scopus 로고    scopus 로고
    • Protease-activated receptors: A means of converting extracellular proteolysis into intracellular signals
    • Mackie E. J., C. N. Pagel, R. Smith, M. R. de Niese, S. J. Song & R. N. Pike: Protease-activated receptors: a means of converting extracellular proteolysis into intracellular signals. IUBMB Life 53, 277-281 (2002)
    • (2002) IUBMB Life , vol.53 , pp. 277-281
    • Mackie, E.J.1    Pagel, C.N.2    Smith, R.3    De Niese, M.R.4    Song, S.J.5    Pike, R.N.6
  • 64
    • 0032523148 scopus 로고    scopus 로고
    • Tissue factor-dependent vascular endothelial growth factor production by human fibroblasts in response to activated factor VII
    • Ollivier V., S. Bentolila, J. Chabbat, J. Hakim & D. de Prost: Tissue factor-dependent vascular endothelial growth factor production by human fibroblasts in response to activated factor VII. Blood 91, 2698-2703 (1998)
    • (1998) Blood , vol.91 , pp. 2698-2703
    • Ollivier, V.1    Bentolila, S.2    Chabbat, J.3    Hakim, J.4    De Prost, D.5
  • 65
    • 1642538075 scopus 로고    scopus 로고
    • Factor Xa and thrombin, but not factor VIIa, elicit specific cellular responses in dermal fibroblasts
    • Bachli E. B., C. M. Pech, K. M. Johnson, D. J. Johnson, E. G. Tuddenham & J. H. McVey: Factor Xa and thrombin, but not factor VIIa, elicit specific cellular responses in dermal fibroblasts. J Thromb Haemost 9, 1935-1944 (2003)
    • (2003) J Thromb Haemost , vol.9 , pp. 1935-1944
    • Bachli, E.B.1    Pech, C.M.2    Johnson, K.M.3    Johnson, D.J.4    Tuddenham, E.G.5    McVey, J.H.6
  • 66
    • 23744481763 scopus 로고    scopus 로고
    • Role of PGE(2) in protease-activated receptor-1, -2 and -4 mediated relaxation in the mouse isolated trachea
    • Lan R. S., D. A. Knight, G. A. Stewart & P. J. Henry: Role of PGE(2) in protease-activated receptor-1, -2 and -4 mediated relaxation in the mouse isolated trachea. Br J Pharmacol 131, 689-694 2000)
    • (2000) Br J Pharmacol , vol.131 , pp. 689-694
    • Lan, R.S.1    Knight, D.A.2    Stewart, G.A.3    Henry, P.J.4
  • 67
    • 0037031487 scopus 로고    scopus 로고
    • Galpha(q) and Gbetagamma regulate PAR-1 signaling of thrombin-induced NF-kappaB activation and ICAM-1 transcription in endothelial cells
    • Rahman A., A. L. True, K. N. Anwar, R. D. Ye, T. A. Voyno-Yasenetskaya & A. B. Malik: Galpha(q) and Gbetagamma regulate PAR-1 signaling of thrombin-induced NF-kappaB activation and ICAM-1 transcription in endothelial cells. Circ Res 91, 398-405 (2002)
    • (2002) Circ Res , vol.91 , pp. 398-405
    • Rahman, A.1    True, A.L.2    Anwar, K.N.3    Ye, R.D.4    Voyno-Yasenetskaya, T.A.5    Malik, A.B.6
  • 68
    • 0034670162 scopus 로고    scopus 로고
    • Inhibition of cellular action of thrombin by N3-cyclopropyl-7-((4-(1- methylethyl)phenyl)methyl)-7H-pyrrolo(3,2-f)quinazoline-1,3-diamine (SCH 79797), a nonpeptide thrombin receptor antagonist
    • Ahn H. S., C. Foster, G. Boykow, A. Stamford, M. Manna & M. Graziano: Inhibition of cellular action of thrombin by N3-cyclopropyl-7-((4-(1- methylethyl)phenyl)methyl)-7H-pyrrolo(3,2-f)quinazoline-1,3-diamine (SCH 79797), a nonpeptide thrombin receptor antagonist. Biochem Pharmacol 60, 1425-1434 (2000)
    • (2000) Biochem Pharmacol , vol.60 , pp. 1425-1434
    • Ahn, H.S.1    Foster, C.2    Boykow, G.3    Stamford, A.4    Manna, M.5    Graziano, M.6
  • 69
    • 0041328272 scopus 로고    scopus 로고
    • The agonist of the protease-activated receptor-1 (PAR) but not PAR3 mimics thrombin-induced vascular endothelial growth factor release in human smooth muscle cells
    • Arisato T., K, P. Sarker, K. Kawahara, M. Nakata, T. Hashiguchi, M. Osame, I. Kitajima & I. Maruyama: The agonist of the protease-activated receptor-1 (PAR) but not PAR3 mimics thrombin-induced vascular endothelial growth factor release in human smooth muscle cells. Cell Mol Life Sci 60, 1716-1724 (2003)
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1716-1724
    • Arisato, T.1    Sarker, K.P.2    Kawahara, K.3    Nakata, M.4    Hashiguchi, T.5    Osame, M.6    Kitajima, I.7    Maruyama, I.8
  • 70
    • 0031938090 scopus 로고    scopus 로고
    • The role of secondary growth factor production in thrombin-induced proliferation of vascular smooth muscle cells
    • Stouffer, G. A. & M. S. Runge: The role of secondary growth factor production in thrombin-induced proliferation of vascular smooth muscle cells. Semin Thromb Hemost 24, 145-150 (1998)
    • (1998) Semin Thromb Hemost , vol.24 , pp. 145-150
    • Stouffer, G.A.1    Runge, M.S.2
  • 71
    • 0035961680 scopus 로고    scopus 로고
    • Fibrin stimulates microfilament reorganization and IL-1 beta production in human monocytic THP-1 cells
    • Lee M. E., S. M. Kweon & S. U. Nham: Fibrin stimulates microfilament reorganization and IL-1 beta production in human monocytic THP-1 cells. Mol Cell 11, 13-20 (2001)
    • (2001) Mol Cell , vol.11 , pp. 13-20
    • Lee, M.E.1    Kweon, S.M.2    Nham, S.U.3
  • 72
    • 0033611621 scopus 로고    scopus 로고
    • Fragment e derived from both fibrin and fibrinogen stimulates interleukin-6 production in rat peritoneal macrophages
    • Lee M. E., K. J. Rhee & S. U. Nham: Fragment E derived from both fibrin and fibrinogen stimulates interleukin-6 production in rat peritoneal macrophages. Mol Cell 9, 7-13 (1999)
    • (1999) Mol Cell , vol.9 , pp. 7-13
    • Lee, M.E.1    Rhee, K.J.2    Nham, S.U.3
  • 73
    • 0034326635 scopus 로고    scopus 로고
    • Fibrin(ogen)-induced expression of ICAM-1 and chemokines in human synovial fibroblasts
    • Liu X. & T. H. Piela-Smith: Fibrin(ogen)-induced expression of ICAM-1 and chemokines in human synovial fibroblasts. J. Immunol 165, 5255-5261 (2000)
    • (2000) J Immunol , vol.165 , pp. 5255-5261
    • Liu, X.1    Piela-Smith, T.H.2
  • 74
    • 0031938090 scopus 로고    scopus 로고
    • The role of secondary growth factor production in thrombin-induced proliferation of vascular smooth muscle cells
    • Stouffer G. A. & M. S. Runge: The role of secondary growth factor production in thrombin-induced proliferation of vascular smooth muscle cells. Semin Thromb Hemost 24, 145-150 (1998)
    • (1998) Semin Thromb Hemost , vol.24 , pp. 145-150
    • Stouffer, G.A.1    Runge, M.S.2
  • 75
    • 1242317779 scopus 로고    scopus 로고
    • Vascular endothelium and immune responses: Implications for inflammation and angiogenesis
    • Szekanecz Z. & A. E. Koch: Vascular endothelium and immune responses: implications for inflammation and angiogenesis. Rheum Dis Clin North Am 30, 97-114 (2004)
    • (2004) Rheum Dis Clin North Am , vol.30 , pp. 97-114
    • Szekanecz, Z.1    Koch, A.E.2
  • 76
    • 0032510949 scopus 로고    scopus 로고
    • The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets
    • Schmidt V.A., W. C. Nierman, D. R. Maglott, L. D. Cupit, K. A. Moskowitz, J. A. Wainer & W. F. Bahou: The human proteinase-activated receptor-3 (PAR-3) gene. Identification within a Par gene cluster and characterization in vascular endothelial cells and platelets. J Biol Chem 273, 15061-15068 (1998)
    • (1998) J Biol Chem , vol.273 , pp. 15061-15068
    • Schmidt, V.A.1    Nierman, W.C.2    Maglott, D.R.3    Cupit, L.D.4    Moskowitz, K.A.5    Wainer, J.A.6    Bahou, W.F.7
  • 77
    • 0035799341 scopus 로고    scopus 로고
    • Inflammation and thrombosis: The clot thickens
    • Libby, P. & D. I. Simon: Inflammation and thrombosis: The clot thickens. Circulation 103, 1718-1720 (2001)
    • (2001) Circulation , vol.103 , pp. 1718-1720
    • Libby, P.1    Simon, D.I.2
  • 78
  • 79
    • 0034750626 scopus 로고    scopus 로고
    • Inhibition of factor Xa suppresses the expression of tissue factor in human monocytes and lipopolysaccharide-induced endotoxemia in rats
    • Akahane K., K. Okamoto, M. Kikuchi, H. Todoroki, A. Higure, T. Ohuchida, K. Kitahara, S. Takeda, H. Itoh & K. Ohsato: Inhibition of factor Xa suppresses the expression of tissue factor in human monocytes and lipopolysaccharide-induced endotoxemia in rats. Surgery 130, 809-818 (2001)
    • (2001) Surgery , vol.130 , pp. 809-818
    • Akahane, K.1    Okamoto, K.2    Kikuchi, M.3    Todoroki, H.4    Higure, A.5    Ohuchida, T.6    Kitahara, K.7    Takeda, S.8    Itoh, H.9    Ohsato, K.10
  • 80
    • 0034764322 scopus 로고    scopus 로고
    • Human thrombin and FXa mediate porcine endothelial cell activation; modulation by expression of TFPI-CD4 and hirudin-CD4 fusion proteins
    • Chen D., K. Riesbeck, J. H. McVey, G. Kemball-Cook, E. G. Tuddenham, R. I. Lechler & A. Dorling: Human thrombin and FXa mediate porcine endothelial cell activation; modulation by expression of TFPI-CD4 and hirudin-CD4 fusion proteins. Xenotransplantation 8, 258-265 (2001)
    • (2001) Xenotransplantation , vol.8 , pp. 258-265
    • Chen, D.1    Riesbeck, K.2    McVey, J.H.3    Kemball-Cook, G.4    Tuddenham, E.G.5    Lechler, R.I.6    Dorling, A.7
  • 81
    • 0032943041 scopus 로고    scopus 로고
    • Endothelial protease-activated receptor-2 induces tissue factor expression and von Willebrand factor release
    • Langer F., C. Morys-Wortmann, B. Kusters & J. Storck: Endothelial protease-activated receptor-2 induces tissue factor expression and von Willebrand factor release. Br J Haematol 105, 542-550 (1999)
    • (1999) Br J Haematol , vol.105 , pp. 542-550
    • Langer, F.1    Morys-Wortmann, C.2    Kusters, B.3    Storck, J.4
  • 82
    • 0035657829 scopus 로고    scopus 로고
    • Endothelial tissue factor stimulation by proteinase 3 and elastase
    • Haubitz M., M. Gerlach, H. J. Kruse & R. Brunkhorst: Endothelial tissue factor stimulation by proteinase 3 and elastase. Clin Exp Immunol 126, 584-588 (2001)
    • (2001) Clin Exp Immunol , vol.126 , pp. 584-588
    • Haubitz, M.1    Gerlach, M.2    Kruse, H.J.3    Brunkhorst, R.4
  • 83
    • 0024317058 scopus 로고
    • Regulation of endothelial cell coagulant properties. Modulation of tissue factor, plasminogen activator inhibitors, and thrombomodulin by phorbol 12-myristate 13-acetate and tumor necrosis factor
    • Scarpati E. M. & J. E. Sadler: Regulation of endothelial cell coagulant properties. Modulation of tissue factor, plasminogen activator inhibitors, and thrombomodulin by phorbol 12-myristate 13-acetate and tumor necrosis factor. J. Biol Chem 264, 20705-20713 (1989)
    • (1989) J Biol Chem , vol.264 , pp. 20705-20713
    • Scarpati, E.M.1    Sadler, J.E.2
  • 84
    • 0033790858 scopus 로고    scopus 로고
    • Cytokines and hemostasis
    • Grignani G. & A. Maiolo: Cytokines and hemostasis. Haematologica 85, 967-972 (2000)
    • (2000) Haematologica , vol.85 , pp. 967-972
    • Grignani, G.1    Maiolo, A.2
  • 88
    • 0035174972 scopus 로고    scopus 로고
    • Specificity, diversity, and convergence in VEGF and TNF-alpha signaling events leading to tissue factor up-regulation via EGR-1 in endothelial cells
    • Mechtcheriakova D., G. Schabbauer, M. Lucerna, M. Clauss, R. De Martin, B. R. Binder & E. Hofer: Specificity, diversity, and convergence in VEGF and TNF-alpha signaling events leading to tissue factor up-regulation via EGR-1 in endothelial cells. FASEB J 15, 230-242 (2001)
    • (2001) FASEB J , vol.15 , pp. 230-242
    • Mechtcheriakova, D.1    Schabbauer, G.2    Lucerna, M.3    Clauss, M.4    De Martin, R.5    Binder, B.R.6    Hofer, E.7
  • 89
    • 0030722998 scopus 로고    scopus 로고
    • Up-regulation of tissue factor expression by platelet-derived growth factor in human vascular smooth muscle cells in culture-role of mitogen-activated protein kinase and effects of intracellular cyclic AMP
    • Xuereb J. M., P. Sie, B. Boneu & J. Constans: Up-regulation of tissue factor expression by platelet-derived growth factor in human vascular smooth muscle cells in culture-role of mitogen-activated protein kinase and effects of intracellular cyclic AMP. Thromb Haemost 78, 1520-1526 (1997)
    • (1997) Thromb Haemost , vol.78 , pp. 1520-1526
    • Xuereb, J.M.1    Sie, P.2    Boneu, B.3    Constans, J.4
  • 90
    • 0032530146 scopus 로고    scopus 로고
    • Presence of tissue factor pathway inhibitor in human atherosclerotic plaques is associated with reduced tissue factor activity
    • Caplice N. M., C. S. Mueske, L. S. Kleppe & R. D. Simari: Presence of tissue factor pathway inhibitor in human atherosclerotic plaques is associated with reduced tissue factor activity. Circulation 98, 1051-1057 (1998)
    • (1998) Circulation , vol.98 , pp. 1051-1057
    • Caplice, N.M.1    Mueske, C.S.2    Kleppe, L.S.3    Simari, R.D.4
  • 91
    • 0036014821 scopus 로고    scopus 로고
    • Extrinsic coagulation blockade attenuates lung injury and proinflammatory cytokine release after intratracheal lipopolysaccharide
    • Miller D. L., K. Welty-Wolf, M. S. Carraway, M. Ezban, A. Ghio, H. Suliman & C. A. Piantadosi: Extrinsic coagulation blockade attenuates lung injury and proinflammatory cytokine release after intratracheal lipopolysaccharide. Am J Respir Cell Mol Biol 26, 650-658 (2002)
    • (2002) Am J Respir Cell Mol Biol , vol.26 , pp. 650-658
    • Miller, D.L.1    Welty-Wolf, K.2    Carraway, M.S.3    Ezban, M.4    Ghio, A.5    Suliman, H.6    Piantadosi, C.A.7
  • 92
    • 0035881168 scopus 로고    scopus 로고
    • FXa-induced responses in vascular wall cells are PAR-mediated and inhibited by ZK-807834
    • McLean K., S. Schirm, A. Johns, J. Morser & D. R. Light: FXa-induced responses in vascular wall cells are PAR-mediated and inhibited by ZK-807834. Thromb Res 103, 281-297 (2001)
    • (2001) Thromb Res , vol.103 , pp. 281-297
    • McLean, K.1    Schirm, S.2    Johns, A.3    Morser, J.4    Light, D.R.5
  • 93
    • 0036825390 scopus 로고    scopus 로고
    • Tissue factor regulation and cytokine expression in monocyte-endothelial cell cocultures. Effects of a statin, an ACE-inhibitor and a low-molecular-weight heparin
    • Lindmark E. & A. Siegbahn: Tissue factor regulation and cytokine expression in monocyte-endothelial cell cocultures. Effects of a statin, an ACE-inhibitor and a low-molecular-weight heparin. Thromb Res 108, 77-84 (2002)
    • (2002) Thromb Res , vol.108 , pp. 77-84
    • Lindmark, E.1    Siegbahn, A.2
  • 96
    • 0037630699 scopus 로고    scopus 로고
    • Hirulog-like peptide reduces restenosis and expression of tissue factor and transforming growth factor-beta in carotid artery of atherosclerotic rabbits
    • Chen X., S. Ren, M. G. Ma, S. Dharmalingam, L. Lu, M. Xue, J. Ducas & G. X. Shen: Hirulog-like peptide reduces restenosis and expression of tissue factor and transforming growth factor-beta in carotid artery of atherosclerotic rabbits. Atherosclerosis 169, 31-40 (2003)
    • (2003) Atherosclerosis , vol.169 , pp. 31-40
    • Chen, X.1    Ren, S.2    Ma, M.G.3    Dharmalingam, S.4    Lu, L.5    Xue, M.6    Ducas, J.7    Shen, G.X.8
  • 97
    • 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. (2001) Antithrombin inhibits lipopolysaccharide-induced tissue factor and interleukin-6 production by mononuclear cells, human umbilical vein endothelial cells, and whole blood. Crit Care Med 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
  • 98
    • 0031958730 scopus 로고    scopus 로고
    • The protease-activated receptors and their cellular expression and function in blood-related cells
    • Hou L., G. L. Howells, S. Kapas & M. G. Macey: The protease-activated receptors and their cellular expression and function in blood-related cells. Br J Haematol 101, 1-9 (1998)
    • (1998) Br J Haematol , vol.101 , pp. 1-9
    • Hou, L.1    Howells, G.L.2    Kapas, S.3    Macey, M.G.4
  • 101
    • 0026495238 scopus 로고
    • Leukocyte accumulation promoting fibrin deposition is mediated in vivo by P-selectin on adherent platelets
    • Palabrica T., R. Lobb, B. C. Furie, M. Aronovitz, C. Benjamin, Y. M. Hsu, S. A. Sajer & B. Furie: Leukocyte accumulation promoting fibrin deposition is mediated in vivo by P-selectin on adherent platelets. Nature 359 (6398), 848-851 (1992)
    • (1992) Nature , vol.359 , Issue.6398 , pp. 848-851
    • Palabrica, T.1    Lobb, R.2    Furie, B.C.3    Aronovitz, M.4    Benjamin, C.5    Hsu, Y.M.6    Sajer, S.A.7    Furie, B.8
  • 102
    • 0037330480 scopus 로고    scopus 로고
    • A peptide (P2) derived from the variable heavy chain of an anti-P-selectin monoclonal antibody (LYP20) inhibits leucocyte adhesion to thrombin-activated platelets and endothelial cells
    • Murphy J. F. & J.L. McGregor: A peptide (P2) derived from the variable heavy chain of an anti-P-selectin monoclonal antibody (LYP20) inhibits leucocyte adhesion to thrombin-activated platelets and endothelial cells. Br J Haematol 120, 605-610 (2003)
    • (2003) Br J Haematol , vol.120 , pp. 605-610
    • Murphy, J.F.1    McGregor, J.L.2
  • 103
    • 0029559140 scopus 로고
    • Pretreatment with a blocking monoclonal antibody to P-selectin accelerates pharmacological thrombolysis in a primate model of arterial thrombosis
    • Toombs C. F., G. L. DeGraaf, J. P. Martin, J. G. Geng, D. C. Anderson & R. J. Shebuski: Pretreatment with a blocking monoclonal antibody to P-selectin accelerates pharmacological thrombolysis in a primate model of arterial thrombosis. J Pharmacol Exp Ther 275, 941-949 (1995)
    • (1995) J Pharmacol Exp Ther , vol.275 , pp. 941-949
    • Toombs, C.F.1    DeGraaf, G.L.2    Martin, J.P.3    Geng, J.G.4    Anderson, D.C.5    Shebuski, R.J.6
  • 105
    • 0037070170 scopus 로고    scopus 로고
    • Identification of functional VEGF receptors on human platelets
    • Selheim F., H. Holmsen & F. S. Vassbotn: Identification of functional VEGF receptors on human platelets. FEBS Lett 512, 107-110 (2002)
    • (2002) FEBS Lett , vol.512 , pp. 107-110
    • Holmsen, S.F.H.1    Vassbotn, F.S.2
  • 106
    • 0033135772 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of inflammation and thrombosis
    • Tan P., F. W. Luscinskas & S. Homer-Vanniasinkam: Cellular and molecular mechanisms of inflammation and thrombosis. Eur J Vasc Surg 17, 373-389 (1999)
    • (1999) Eur J Vasc Surg , vol.17 , pp. 373-389
    • Tan, P.1    Luscinskas, F.W.2    Homer-Vanniasinkam, S.3
  • 107
    • 0036884012 scopus 로고    scopus 로고
    • Sepsis- and endotoxemia-generated cytokines do not trigger activation of human platelets
    • Leytin V., S. Shakoor, M. Mody, D. Allen, B. Garvey & J. Freedman: Sepsis- and endotoxemia-generated cytokines do not trigger activation of human platelets. Crit. Care Med. 30, 2771-2773 (2002)
    • (2002) Crit Care Med , vol.30 , pp. 2771-2773
    • Leytin, V.1    Shakoor, S.2    Mody, M.3    Allen, D.4    Garvey, B.5    Freedman, J.6
  • 108
    • 0037080065 scopus 로고    scopus 로고
    • Aspirin for the primary prevention of cardiovascular events: A summary of the evidence for the U.S. Preventive Services Task Force
    • Hayden M., M. Pignone, C. Phillips & C. Mulrow: Aspirin for the primary prevention of cardiovascular events: a summary of the evidence for the U.S. Preventive Services Task Force. Ann Intern Med 136, 161-172 (2002)
    • (2002) Ann Intern Med , vol.136 , pp. 161-172
    • Hayden, M.1    Pignone, M.2    Phillips, C.3    Mulrow, C.4
  • 110
    • 0037047092 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibition and cardiovascular events
    • Pitt B., C. Pepine & J. T. Willerson: Cyclooxygenase-2 inhibition and cardiovascular events. Circulation 106, 167-169 (2002)
    • (2002) Circulation , vol.106 , pp. 167-169
    • Pitt, B.1    Pepine, C.2    Willerson, J.T.3
  • 111
    • 0038399865 scopus 로고    scopus 로고
    • Prevention of thrombosis and vascular inflammation: Benefits and limitations of selective or combined COX-1, COX-2 and 5-LOX inhibitors
    • de Gaetano G., M. B. Donati & C. Cerletti: Prevention of thrombosis and vascular inflammation: benefits and limitations of selective or combined COX-1, COX-2 and 5-LOX inhibitors. Trends Pharmacol Sci 24, 245-252 (2003)
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 245-252
    • Gaetano, G.1    Donati, M.B.2    Cerletti, C.3
  • 113
    • 0037783288 scopus 로고    scopus 로고
    • Extracellular mediators in atherosclerosis and thrombosis: Lessons from thrombin receptor knockout mice
    • Major C. D., R. J. Santulli, C. K. Derian & P. Andrade-Gordon: Extracellular mediators in atherosclerosis and thrombosis: lessons from thrombin receptor knockout mice. Arterioscler Thromb Vasc Biol 23, 931-939 (2003)
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 931-939
    • Major, C.D.1    Santulli, R.J.2    Derian, C.K.3    Andrade-Gordon, P.4
  • 115
    • 0035122836 scopus 로고    scopus 로고
    • Anti-thrombotic and haemorrhagic effects of active site-inhibited factor VIIa in rats
    • Ghrib F., P. Leger, M. Ezban, A. Kristensen, J. Cambus & B. Boneu: Anti-thrombotic and haemorrhagic effects of active site-inhibited factor VIIa in rats. Br J Haematol 112, 506-512 (2001)
    • (2001) Br J Haematol , vol.112 , pp. 506-512
    • Ghrib, F.1    Leger, P.2    Ezban, M.3    Kristensen, A.4    Cambus, J.5    Boneu, B.6
  • 118
    • 0029093197 scopus 로고
    • Active site-blocked factors VIIa and IXa differentially inhibit fibrin formation in a human ex vivo thrombosis model
    • Kirchhofer D., T. B. Tschopp & H. R. Baumgartner: Active site-blocked factors VIIa and IXa differentially inhibit fibrin formation in a human ex vivo thrombosis model. Arterioscler Thromb Vasc Biol 15, 1098-1106 (1995)
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 1098-1106
    • Kirchhofer, D.1    Tschopp, T.B.2    Baumgartner, H.R.3
  • 119
    • 0035077129 scopus 로고    scopus 로고
    • Inhibition of arterial thrombosis by a soluble tissue factor mutant and active site-blocked factors IXa and Xa in the guinea pig
    • Himber J., C. J. Refino, L. Burcklen, S. Roux & D. Kirchhofer: Inhibition of arterial thrombosis by a soluble tissue factor mutant and active site-blocked factors IXa and Xa in the guinea pig. Thromb Haemost 85, 475-481 (2001)
    • (2001) Thromb Haemost , vol.85 , pp. 475-481
    • Himber, J.1    Refino, C.J.2    Burcklen, L.3    Roux, S.4    Kirchhofer, D.5
  • 120
    • 0036146048 scopus 로고    scopus 로고
    • A cyclic pentapeptide derived from the second EGF-like domain of Factor VII is an inhibitor of tissue factor dependent coagulation and thrombus formation
    • Orning L., P. M. Fischer, C. K. Hu, E. Agner, M. Engebretsen, M. Husbyn, L. B. Petersen, U. Orvim, M. Llinas & K. S. Sakariassen: A cyclic pentapeptide derived from the second EGF-like domain of Factor VII is an inhibitor of tissue factor dependent coagulation and thrombus formation. Thromb Haemost 87, 13-21 (2002)
    • (2002) Thromb Haemost , vol.87 , pp. 13-21
    • Orning, L.1    Fischer, P.M.2    Hu, C.K.3    Agner, E.4    Engebretsen, M.5    Husbyn, M.6    Petersen, L.B.7    Orvim, U.8    Llinas, M.9    Sakariassen, K.S.10
  • 121
  • 122
    • 4143117812 scopus 로고    scopus 로고
    • Pentasaccharides in the prophylaxis and treatment of venous thromboembolism: A systematic review
    • Nijkeuter M. & M. V. Huisman: Pentasaccharides in the prophylaxis and treatment of venous thromboembolism: a systematic review. Curr Opin Pulm Med 10, 338-344 (2004)
    • (2004) Curr Opin Pulm Med , vol.10 , pp. 338-344
    • Nijkeuter, M.1    Huisman, M.V.2
  • 123
    • 0036246897 scopus 로고    scopus 로고
    • Enoxaparin: A pharmacoeconomic review of its use in the prevention and treatment of venous thromboembolism and in acute coronary syndromes
    • Bergqvist D.: Enoxaparin: a pharmacoeconomic review of its use in the prevention and treatment of venous thromboembolism and in acute coronary syndromes. Pharmacoeconomics 20, 225-243 (2002)
    • (2002) Pharmacoeconomics , vol.20 , pp. 225-243
    • Bergqvist, D.1
  • 124
    • 0142248246 scopus 로고    scopus 로고
    • Bemiparin: A review of its use in the prevention of venous thromboembolism and treatment of deep vein thrombosis
    • Chapman T. M. & K. L. Goa: Bemiparin: a review of its use in the prevention of venous thromboembolism and treatment of deep vein thrombosis. Drugs 63, 2357-2377 (2003)
    • (2003) Drugs , vol.63 , pp. 2357-2377
    • Chapman, T.M.1    Goa, K.L.2
  • 125
    • 0034916276 scopus 로고    scopus 로고
    • Reviparin: A review of its efficacy in the prevention and treatment of venous thromboembolism
    • Wellington K., K. McClellan & B. Jarvis: Reviparin: a review of its efficacy in the prevention and treatment of venous thromboembolism. Drugs 61, 1185-1209 (2001)
    • (2001) Drugs , vol.61 , pp. 1185-1209
    • McClellan, W.K.K.1    Jarvis, B.2
  • 126
    • 0028785464 scopus 로고
    • A comparative study of the anticoagulant and anti-thrombotic effects of unfractionated heparin and a low molecular weight heparin (Fraxiparine) in an experimental model of human venous thrombosis
    • Diquelou A., D. Dupouy, R. Cariou, K. S. Sakariassen, B. Boneu & Y. Cadroy: A comparative study of the anticoagulant and anti-thrombotic effects of unfractionated heparin and a low molecular weight heparin (Fraxiparine) in an experimental model of human venous thrombosis. Thromb Haemost 74, 1286-1292 (1995)
    • (1995) Thromb Haemost , vol.74 , pp. 1286-1292
    • Diquelou, A.1    Dupouy, D.2    Cariou, R.3    Sakariassen, K.S.4    Boneu, B.5    Cadroy, Y.6
  • 127
    • 3242790119 scopus 로고    scopus 로고
    • Tinzaparin sodium: A review of its pharmacology and clinical use in the prophylaxis and treatment of thromboembolic disease
    • Cheer S. M., C. J. Dunn & R. Foster Tinzaparin sodium: a review of its pharmacology and clinical use in the prophylaxis and treatment of thromboembolic disease. Drugs 64, 1479-1502 (2004)
    • (2004) Drugs , vol.64 , pp. 1479-1502
    • Cheer, S.M.1    Dunn, C.J.2    Foster, R.3
  • 131
    • 0029610423 scopus 로고
    • Effect of selective factor Xa inhibition on arterial thrombus formation triggered by tissue factor/factor VIIa or collagen in an ex vivo model of shear-dependent human thrombogenesis
    • Orvim U., R. M. Barstad, G. P. Vlasuk & K. S. Sakariassen: Effect of selective factor Xa inhibition on arterial thrombus formation triggered by tissue factor/factor VIIa or collagen in an ex vivo model of shear-dependent human thrombogenesis. Arterioscler Thromb Vasc Biol 15, 2188-2194 (1995)
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 2188-2194
    • Orvim, U.1    Barstad, R.M.2    Vlasuk, G.P.3    Sakariassen, K.S.4
  • 132
    • 0033373234 scopus 로고    scopus 로고
    • Inactivation of factor Xa by the synthetic inhibitor DX-9065a causes strong anticoagulant and antiplatelet actions in human blood
    • Kaiser B., W. Jeske, J. M. Walenga & J. Fareed: Inactivation of factor Xa by the synthetic inhibitor DX-9065a causes strong anticoagulant and antiplatelet actions in human blood. Blood Coagul Fibrinolysis 10, 495-501 (1999)
    • (1999) Blood Coagul Fibrinolysis , vol.10 , pp. 495-501
    • Kaiser, B.1    Jeske, W.2    Walenga, J.M.3    Fareed, J.4
  • 133
    • 0036481635 scopus 로고    scopus 로고
    • Factor Xa-inhibitor (DX-9065a) modulates the leukocyte-endothelial cell interaction in endotoxemic rat
    • Iba T., A. Kidokoro, M. Fukunaga, S. Fuse, M. Suda, S. Kunitada & T. Kara: Factor Xa-inhibitor (DX-9065a) modulates the leukocyte-endothelial cell interaction in endotoxemic rat. Shock 17, 159-162 (2002)
    • (2002) Shock , vol.17 , pp. 159-162
    • Iba, T.1    Kidokoro, A.2    Fukunaga, M.3    Fuse, S.4    Suda, M.5    Kunitada, S.6    Kara, T.7
  • 134
    • 0029112614 scopus 로고
    • Antithrombotic effects of orally active synthetic antagonist of activated factor X in nonhuman primates
    • Yokoyama T., A. B. Kelly, U. M. Marzec, S. R. Hanson, S. Kunitada & L. A. Harker: Antithrombotic effects of orally active synthetic antagonist of activated factor X in nonhuman primates. Circulation 92, 485-491 (1995)
    • (1995) Circulation , vol.92 , pp. 485-491
    • Yokoyama, T.1    Kelly, A.B.2    Marzec, U.M.3    Hanson, S.R.4    Kunitada, S.5    Harker, L.A.6
  • 135
    • 2442429699 scopus 로고    scopus 로고
    • Effect of vascular injury on inhibition of venous thrombosis with ZK-807834, a direct inhibitor of factor Xa
    • Abendschein D. R., P. K. Baum, D. R. Light & J. Morser: Effect of vascular injury on inhibition of venous thrombosis with ZK-807834, a direct inhibitor of factor Xa. J Thromb Haemost 1, 1955-1958 (2003)
    • (2003) J Thromb Haemost , vol.1 , pp. 1955-1958
    • Abendschein, D.R.1    Baum, P.K.2    Light, D.R.3    Morser, J.4
  • 137
    • 0033957888 scopus 로고    scopus 로고
    • Nonpeptide factor Xa inhibitors: I. Studies with SF303 and SK549, a new class of potent antithrombotics
    • Wong P. C., M. L. Quan, E. J. Crain, C. A. Watson, R. R. Wexler & R. M. Knabb: Nonpeptide factor Xa inhibitors: I. Studies with SF303 and SK549, a new class of potent antithrombotics. J Pharmacol Exp Ther 292, 351-357 (2000)
    • (2000) J Pharmacol Exp Ther , vol.292 , pp. 351-357
    • Wong, P.C.1    Quan, M.L.2    Crain, E.J.3    Watson, C.A.4    Wexler, R.R.5    Knabb, R.M.6
  • 138
    • 0031793092 scopus 로고    scopus 로고
    • Comparison of the anticoagulant and antithrombotic effects of YM-75466, a novel orally-active factor Xa inhibitor, and warfarin in mice
    • Sato K., Y. Taniuchi, T. Kawasaki, F. Hirayama, H. Koshio, Y. Matsumoto & Y. Iizumi: Comparison of the anticoagulant and antithrombotic effects of YM-75466, a novel orally-active factor Xa inhibitor, and warfarin in mice. Jpn J Pharmacol 78, 191-197 (1998)
    • (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    Iizumi, Y.7
  • 139
    • 0034887402 scopus 로고    scopus 로고
    • Antithrombotic efficacy of a novel factor Xa inhibitor, FXV673, in a canine model of coronary artery thrombolysis
    • Rebello S. S., R. G. Bentley, S. R. Morgan, C. J. Kasiewski, V. Chu, M. H. Perrone & R. J. Leadley: Antithrombotic efficacy of a novel factor Xa inhibitor, FXV673, in a canine model of coronary artery thrombolysis. Br J Pharmacol 133, 1190-1198 (2001)
    • (2001) Br J Pharmacol , vol.133 , pp. 1190-1198
    • Rebello, S.S.1    Bentley, R.G.2    Morgan, S.R.3    Kasiewski, C.J.4    Chu, V.5    Perrone, M.H.6    Leadley, R.J.7
  • 140
    • 0036897444 scopus 로고    scopus 로고
    • Nonpeptide factor Xa inhibitors III: Effects of DPC423, an orally-active pyrazole antithrombotic agent, on arterial thrombosis in rabbits
    • Wong P. C., E. J. Crain, C. A. Watson, A. M. Zaspel, M. R. Wright, P. Y. Lam, D. J. Pinto, R. R. Wexler & R. M. Knabb: Nonpeptide factor Xa inhibitors III: effects of DPC423, an orally-active pyrazole antithrombotic agent, on arterial thrombosis in rabbits. J Pharmacol Exp Ther 303, 993-1000 (2002)
    • (2002) J Pharmacol Exp Ther , vol.303 , pp. 993-1000
    • Wong, P.C.1    Crain, E.J.2    Watson, C.A.3    Zaspel, A.M.4    Wright, M.R.5    Lam, P.Y.6    Pinto, D.J.7    Wexler, R.R.8    Knabb, R.M.9
  • 143
    • 3543093189 scopus 로고    scopus 로고
    • Treatment of venous thromboembolism: Challenging the unfractionated heparin standard
    • Nutescu E., M. Singh-Khalsa; Heparin Consensus Group: Treatment of venous thromboembolism: challenging the unfractionated heparin standard. Pharmacotherapy 24(8 Pt 2), 127S-131S (2004)
    • (2004) Pharmacotherapy , vol.24 , Issue.8 PART 2
    • Nutescu, E.1    Singh-Khalsa, M.2
  • 144
    • 3843090636 scopus 로고    scopus 로고
    • The role of recombinant hirudins in the management of thrombotic disorders
    • Fischer K. G.: The role of recombinant hirudins in the management of thrombotic disorders. BioDrugs 18, 235-268 (2004)
    • (2004) BioDrugs , vol.18 , pp. 235-268
    • Fischer, K.G.1
  • 146
    • 2942665487 scopus 로고    scopus 로고
    • Small-molecule direct antithrombins: Argatroban
    • Fareed J. & W. P. Jeske: Small-molecule direct antithrombins: argatroban. Best Pract Res Clin Haematol 17, 127-138 (2004)
    • (2004) Best Pract Res Clin Haematol , vol.17 , pp. 127-138
    • Fareed, J.1    Jeske, W.P.2
  • 147
    • 2442561673 scopus 로고    scopus 로고
    • Antithrombotic properties of a direct thrombin inhibitor with a prolonged half-life and AT-mediated factor Xa inhibitory activity
    • Vogel G. M., D. G. Meuleman, T. G. Van Dinther, R. Buijsman, A. W. Princen & M. J. Smit: Antithrombotic properties of a direct thrombin inhibitor with a prolonged half-life and AT-mediated factor Xa inhibitory activity. J Thromb Haemost 1, 1945-1954 (2003)
    • (2003) J Thromb Haemost , vol.1 , pp. 1945-1954
    • Vogel, G.M.1    Meuleman, D.G.2    Van Dinther, T.G.3    Buijsman, R.4    Princen, A.W.5    Smit, M.J.6
  • 149
    • 0028082448 scopus 로고
    • Antithrombotic effect of recombinant truncated tissue factor pathway inhibitor (TFPI1-161) in experimental venous thrombosis - A comparison with low molecular weight heparin
    • Holst J., B. Lindblad, D. Bergqvist, O. Nordfang, P. B. Ostergaard, J. G. Petersen, G. Nielsen & U. Hedner: Antithrombotic effect of recombinant truncated tissue factor pathway inhibitor (TFPI1-161) in experimental venous thrombosis-a comparison with low molecular weight heparin. Thromb Haemost 71, 214-219 (1994)
    • (1994) Thromb Haemost , vol.71 , pp. 214-219
    • Holst, J.1    Lindblad, B.2    Bergqvist, D.3    Nordfang, O.4    Ostergaard, P.B.5    Petersen, J.G.6    Nielsen, G.7    Hedner, U.8
  • 150
    • 0034153611 scopus 로고    scopus 로고
    • Activated protein C resistance: The most common risk factor for venous thromboembolism
    • Sheppard D. R.: Activated protein C resistance: the most common risk factor for venous thromboembolism. J Am Board Fam Pract 13, 111-115 (2000)
    • (2000) J Am Board Fam Pract , vol.13 , pp. 111-115
    • Sheppard, D.R.1
  • 151
    • 2342428641 scopus 로고    scopus 로고
    • Venous thrombosis: Prevalence of prothrombotic defects in north Indian population
    • Bhattacharyya M., M. Kannan, V. P. Chaudhry & R. Saxena: Venous thrombosis: prevalence of prothrombotic defects in north Indian population. Indian J Pathol Microbiol 46, 621-624 (2003)
    • (2003) Indian J Pathol Microbiol , vol.46 , pp. 621-624
    • Bhattacharyya, M.1    Kannan, M.2    Chaudhry, V.P.3    Saxena, R.4
  • 153
    • 1542544890 scopus 로고    scopus 로고
    • Activated protein C attenuates coagulation-associated over-expression of fibrinolytic activity by suppressing the thrombin-dependent inactivation of PAI-1
    • Urano T., F. J. Castellino, H. Ihara, Y. Suzuki, M. Ohta, K. Suzuki & H. Mogami: Activated protein C attenuates coagulation-associated over-expression of fibrinolytic activity by suppressing the thrombin-dependent
    • (2003) J Thromb Haemost , vol.1 , pp. 2615-2620
    • Urano, T.1    Castellino, F.J.2    Ihara, H.3    Suzuki, Y.4    Ohta, M.5    Suzuki, K.6    Mogami, H.7
  • 154
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar L., M.E. Nesheim & P. B. Tracy: The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood 88, 2093-2100 (1996)
    • (1996) Blood , vol.88 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 155
    • 0033712641 scopus 로고    scopus 로고
    • Pharmacological profile of recombinant, human activated protein C (LY203638) in a canine model of coronary artery thrombosis
    • Jackson C. V., B. D. Bailey & T. J. Shetler: Pharmacological profile of recombinant, human activated protein C (LY203638) in a canine model of coronary artery thrombosis. J Pharmacol Exp Ther 295, 967-971 (2000)
    • (2000) J Pharmacol Exp Ther , vol.295 , pp. 967-971
    • Jackson, C.V.1    Bailey, B.D.2    Shetler, T.J.3
  • 156
    • 0033834720 scopus 로고    scopus 로고
    • Effect of activated human protein C on experimental venous thrombosis induced by stasis with operative invasion in mice
    • Aoki Y., Y. Fukumoto, K. Inoue, Y. Katsuura, K. Komoriya & S. Miyamoto: Effect of activated human protein C on experimental venous thrombosis induced by stasis with operative invasion in mice. Arzneimittelforschung 50, 695-699 (2000)
    • (2000) Arzneimittelforschung , vol.50 , pp. 695-699
    • Aoki, Y.1    Fukumoto, Y.2    Inoue, K.3    Katsuura, Y.4    Komoriya, K.5    Miyamoto, S.6
  • 157
    • 0031028066 scopus 로고    scopus 로고
    • Antithrombotic efficacy in the guinea pig of a derivative of human protein C with enhanced activation by thrombin
    • Kurz K. D., T. Smith, A. Wilson, B. Gerlitz, M. A. Richardson & B. W. Grinnell: Antithrombotic efficacy in the guinea pig of a derivative of human protein C with enhanced activation by thrombin. Blood 89, 534-540 (1997)
    • (1997) Blood , vol.89 , pp. 534-540
    • Kurz, K.D.1    Smith, T.2    Wilson, A.3    Gerlitz, B.4    Richardson, M.A.5    Grinnell, B.W.6
  • 158
    • 0025731750 scopus 로고
    • Inhibitory effects of activated protein C and heparin on thrombotic arterial occlusion in rat mesenteric arteries
    • Araki H., K. Nishi, N. Ishihara & K. Okajima: Inhibitory effects of activated protein C and heparin on thrombotic arterial occlusion in rat mesenteric arteries. Thromb Res 62, 209-216 (1991)
    • (1991) Thromb Res , vol.62 , pp. 209-216
    • Araki, H.1    Nishi, K.2    Ishihara, N.3    Okajima, K.4
  • 159
    • 0025030398 scopus 로고
    • Inhibition of thrombus formation by activated recombinant protein C in a primate model of arterial thrombosis
    • Gruber A., S. R. Hanson, A. B. Kelly, B. S. Yan, N. Bang, J. H. Griffin & L. A. Harker: Inhibition of thrombus formation by activated recombinant protein C in a primate model of arterial thrombosis. Circulation 82, 578-585 (1990)
    • (1990) Circulation , vol.82 , pp. 578-585
    • Gruber, A.1    Hanson, S.R.2    Kelly, A.B.3    Yan, B.S.4    Bang, N.5    Griffin, J.H.6    Harker, L.A.7
  • 160
    • 0042563262 scopus 로고    scopus 로고
    • Prevention of thrombosis following deep arterial injury in rats by bovine activated protein C requiring co-administration of bovine protein S
    • Malm K., B. Dahlback & B. Arnljots: Prevention of thrombosis following deep arterial injury in rats by bovine activated protein C requiring co-administration of bovine protein S. Thromb Haemost 90, 227-234 (2003)
    • (2003) Thromb Haemost , vol.90 , pp. 227-234
    • Malm, K.1    Dahlback, B.2    Arnljots, B.3
  • 161
    • 0027997469 scopus 로고
    • Inhibition of microarterial thrombosis by activated protein C in a rabbit model
    • Arnljots B., D. Bergqvist & B. Dahlback: Inhibition of microarterial thrombosis by activated protein C in a rabbit model. Thromb Haemost 72, 415-420 (1994)
    • (1994) Thromb Haemost , vol.72 , pp. 415-420
    • Arnljots, B.1    Bergqvist, D.2    Dahlback, B.3
  • 163
    • 0030851689 scopus 로고    scopus 로고
    • Antithrombin III prevents and rapidly reverses leukocyte recruitment in ischemia/reperfusion
    • Ostrovsky L., R. C. Woodman, D. Payne, D. Teoh & P. Kubes: Antithrombin III prevents and rapidly reverses leukocyte recruitment in ischemia/reperfusion. Circulation 96, 2302-2310 (1997)
    • (1997) Circulation , vol.96 , pp. 2302-2310
    • Ostrovsky, L.1    Woodman, R.C.2    Payne, D.3    Teoh, D.4    Kubes, P.5
  • 164
    • 5644271563 scopus 로고    scopus 로고
    • Low intensity warfarin: Is it clinically useful in venous thromboembolism management?
    • Bauer K. A.: Low intensity warfarin: is it clinically useful in venous thromboembolism management? Br J Haematol 127, 155-158 (2004)
    • (2004) Br J Haematol , vol.127 , pp. 155-158
    • Bauer, K.A.1
  • 165
    • 0027325620 scopus 로고
    • Enhancement of thrombin receptor activation by thrombin receptor-derived heptapeptide with parafluorophenylalanine in place of phenylalalnine
    • Nose T., Y. Shimohigashi, M. Ohno, T. Costa, N. Shimizu & Y. Ogino: Enhancement of thrombin receptor activation by thrombin receptor-derived heptapeptide with parafluorophenylalanine in place of phenylalalnine. Biochem Biophys Res Commun 193, 694-699 (1993)
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 694-699
    • Nose, T.1    Shimohigashi, Y.2    Ohno, M.3    Costa, T.4    Shimizu, N.5    Ogino, Y.6
  • 166
    • 0033579967 scopus 로고    scopus 로고
    • Photoactivatable peptides based on BMS-197525: A potent antagonist of the human thrombin receptor (PAR-1)
    • Elliott J. T., W. J. Hoekstra, B. E. Maryanoff & G. D. Prestwich: Photoactivatable peptides based on BMS-197525: A potent antagonist of the human thrombin receptor (PAR-1) Bioorg Med Chem Lett 9, 279-284 (1999)
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 279-284
    • Elliott, J.T.1    Hoekstra, W.J.2    Maryanoff, B.E.3    Prestwich, G.D.4
  • 168
    • 0037310962 scopus 로고    scopus 로고
    • Blockade of the thrombin receptor protease-activated receptor-1 with a small-molecule antagonist prevents thrombus formation and vascular occlusion in nonhuman primates
    • Derian C. K., B. P. Damiano, M. F. Addo, A. L. Darrow, M. R. D'Andrea, M. Nedelman, H. C. Zhang, B. E. Maryanoff & P. Andrade-Gordon: Blockade of the thrombin receptor protease-activated receptor-1 with a small-molecule antagonist prevents thrombus formation and vascular occlusion in nonhuman primates. J Pharmacol Exp Ther 304, 855-861 (2003)
    • (2003) J Pharmacol Exp Ther , vol.304 , pp. 855-861
    • Derian, C.K.1    Damiano, B.P.2    Addo, M.F.3    Darrow, A.L.4    D'Andrea, M.R.5    Nedelman, M.6    Zhang, H.C.7    Maryanoff, B.E.8    Andrade-Gordon, P.9
  • 171
    • 0036285450 scopus 로고    scopus 로고
    • Selective inhibition of protease-activated receptor 4-dependent platelet activation by YD-3
    • Wu C. C., T. L. Hwang, C. H. Liao, S. C. Kuo, F. Y. Lee, C. Y. Lee & C. M. Teng: Selective inhibition of protease-activated receptor 4-dependent platelet activation by YD-3. Thromb Haemost 87, 1026-1033 (2000)
    • (2000) Thromb Haemost , vol.87 , pp. 1026-1033
    • Wu, C.C.1    Hwang, T.L.2    Liao, C.H.3    Kuo, S.C.4    Lee, F.Y.5    Lee, C.Y.6    Teng, C.M.7
  • 172
    • 0032543264 scopus 로고    scopus 로고
    • Antibody to thrombin receptor inhibits neointimal smooth muscle cell accumulation without causing inhibition of platelet aggregation or altering hemostatic parameters after angioplasty in rat
    • Takada M., H. Tanaka, T. Yamada, O. Ito, M. Kogushi, M. Yanagimachi, T. Kawamura, T. Musha, F. Yoshida, M. Ito, H. Kobayashi, S. Yoshitake & I. Saito: Antibody to thrombin receptor inhibits neointimal smooth muscle cell accumulation without causing inhibition of platelet aggregation or altering hemostatic parameters after angioplasty in rat. Cir Res 82, 980-987 (1998)
    • (1998) Cir Res , vol.82 , pp. 980-987
    • Takada, M.1    Tanaka, H.2    Yamada, T.3    Ito, O.4    Kogushi, M.5    Yanagimachi, M.6    Kawamura, T.7    Musha, T.8    Yoshida, F.9    Ito, M.10    Kobayashi, H.11    Yoshitake, S.12    Saito, I.13
  • 174
    • 2642535951 scopus 로고    scopus 로고
    • Inflammation as a cardiovascular risk factor
    • Willerson J.T. & P. M. Ridker: Inflammation as a cardiovascular risk factor. Circulation 109(S II), II2-10 (2004)
    • (2004) Circulation , vol.109
    • Willerson, J.T.1    Ridker, P.M.2
  • 175
    • 0030730606 scopus 로고    scopus 로고
    • Thrombosis and atherosclerosis
    • Holvoet P. & D. Collen: Thrombosis and atherosclerosis. Curr Opin Lipidol 8, 320-328 (1997)
    • (1997) Curr Opin Lipidol , vol.8 , pp. 320-328
    • Holvoet, P.1    Collen, D.2
  • 176
    • 0038725465 scopus 로고    scopus 로고
    • Management of thrombotic and cardiovascular disorders in the new millenium
    • Fareed J., D. A. Hoppensteadt & R. L. Bick: Management of thrombotic and cardiovascular disorders in the new millenium. Clin Appl Thromb Hemost 9, 101-108 (2003)
    • (2003) Clin Appl Thromb Hemost , vol.9 , pp. 101-108
    • Fareed, J.1    Hoppensteadt, D.A.2    Bick, R.L.3
  • 179
    • 0348050064 scopus 로고    scopus 로고
    • The management of unstable angina and non-ST-segment elevation myocardial infartion
    • Chen A. A. & M. S. Sabatine: The management of unstable angina and non-ST-segment elevation myocardial infartion. Minerva Cardioangiol 51, 433-445 (2003)
    • (2003) Minerva Cardioangiol , vol.51 , pp. 433-445
    • Chen, A.A.1    Sabatine, M.S.2
  • 180
    • 3142753510 scopus 로고    scopus 로고
    • Low-molecular-weight heparins in ischemic heart disease
    • Yan A. T. & S. G. Goodman: Low-molecular-weight heparins in ischemic heart disease. Curr Opin Cardiol 19, 309-316 (2004)
    • (2004) Curr Opin Cardiol , vol.19 , pp. 309-316
    • Yan, A.T.1    Goodman, S.G.2
  • 183
    • 2542581490 scopus 로고    scopus 로고
    • Bivalirudin: An anticoagulant option for percutaneous
    • Bates E. R.: Bivalirudin: an anticoagulant option for percutaneous. Expert Rev Cardiovasc Ther 2, 153-162 (2004)
    • (2004) Expert Rev Cardiovasc Ther , vol.2 , pp. 153-162
    • Bates, E.R.1
  • 184
    • 0036247598 scopus 로고    scopus 로고
    • Bivalirudin: A review of its potential place in the management of acute coronary syndromes
    • Carswell C. I. & G. L. Plosker: Bivalirudin: A Review of its Potential Place in the Management of Acute Coronary Syndromes. Drugs 62, 841-870 (2002)
    • (2002) Drugs , vol.62 , pp. 841-870
    • Carswell, C.I.1    Plosker, G.L.2
  • 185
    • 2542486654 scopus 로고    scopus 로고
    • Clinical application of enoxaparin
    • Hofmann T.: Clinical application of enoxaparin. Expert Rev Cardiovasc Ther 2, 321-337 (2004)
    • (2004) Expert Rev Cardiovasc Ther , vol.2 , pp. 321-337
    • Hofmann, T.1
  • 186
    • 11144240085 scopus 로고    scopus 로고
    • Ximelagatran: Oral direct thrombin inhibition as anticoagulant therapy in atrial fibrillation
    • Halperin J.L.: Ximelagatran: oral direct thrombin inhibition as anticoagulant therapy in atrial fibrillation. J Am Coll Cardiol 45, 1-9 (2005)
    • (2005) J Am Coll Cardiol , vol.45 , pp. 1-9
    • Halperin, J.L.1
  • 187
    • 0346970912 scopus 로고    scopus 로고
    • Bivalirudin for endovascular intervention in acute ischemic stroke: Case report
    • Harrigan M. R., E. I. Levy, B. R. Bendok & L. N. Hopkins: Bivalirudin for endovascular intervention in acute ischemic stroke: case report. Neurosurgery 54, 218-222 (2004)
    • (2004) Neurosurgery , vol.54 , pp. 218-222
    • Harrigan, M.R.1    Levy, E.I.2    Bendok, B.R.3    Hopkins, L.N.4
  • 188
    • 3442889161 scopus 로고    scopus 로고
    • Will oral antithrombin agents replace warfarin? The new oral direct thrombin inhibitor ximelagatran is at least equivalent to warfarin for stroke prevention in patients with non-valvar atrial fibrillation, and seems to be a promising adjunct to aspirin after acute coronary syndrome
    • Sinnaeve P. R. & F. J. Van de Werf: Will oral antithrombin agents replace warfarin? The new oral direct thrombin inhibitor ximelagatran is at least equivalent to warfarin for stroke prevention in patients with non-valvar atrial fibrillation, and seems to be a promising adjunct to aspirin after acute coronary syndrome. Heart 90, 827-828 (2004)
    • (2004) Heart , vol.90 , pp. 827-828
    • Sinnaeve, P.R.1    Van De Werf, F.J.2
  • 189
    • 0037945025 scopus 로고    scopus 로고
    • G-protein coupled receptor antagonists-1: Protease activated receptor-1 (PAR-1) antagonists as novel cardiovascular therapeutic agents
    • Chackalamannil S.: G-protein coupled receptor antagonists-1: protease activated receptor-1 (PAR-1) antagonists as novel cardiovascular therapeutic agents. Curr Top Med Chem 3, 1115-2113 (2003)
    • (2003) Curr Top Med Chem , vol.3 , pp. 1115-2113
    • Chackalamannil, S.1
  • 190
    • 4344638935 scopus 로고    scopus 로고
    • Proteinase-activated Receptor 2 (PAR2): A challenging new target for treatment of vascular diseases
    • McGuire J. J.: Proteinase-activated Receptor 2 (PAR2): a challenging new target for treatment of vascular diseases. Curr Pharm Des 10, 2769-2778 (2004)
    • (2004) Curr Pharm des , vol.10 , pp. 2769-2778
    • McGuire, J.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.