메뉴 건너뛰기




Volumn 29, Issue 1, 2015, Pages 17-24

Fibrinolysis and the control of blood coagulation

Author keywords

Coagulation; Fibrin(ogen); Fibrinolysis; Hemostasis; Thrombosis

Indexed keywords

ALPHA 2 ANTIPLASMIN; FIBRIN; FIBRIN DEGRADATION PRODUCT; FIBRINOGEN; LIPOCORTIN 2; PLASMIN; PLASMINOGEN ACTIVATOR INHIBITOR 1; PLASMINOGEN ACTIVATOR INHIBITOR 2; PROTEIN C; THROMBIN; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; THROMBOMODULIN; TISSUE PLASMINOGEN ACTIVATOR; UROKINASE; FIBRINOGEN VARIANT;

EID: 84922002483     PISSN: 0268960X     EISSN: 15321681     Source Type: Journal    
DOI: 10.1016/j.blre.2014.09.003     Document Type: Article
Times cited : (575)

References (161)
  • 4
  • 5
    • 0001737647 scopus 로고    scopus 로고
    • The molecular basis of fibrinolysis
    • Saunders/Elsevier, Philadelphia, S.A. Orkin, D.G. Nathan, D. Ginsburg, A.T. Look, D.E. Fisher, S.E. Lux (Eds.)
    • Hajjar K.A. The molecular basis of fibrinolysis. Nathan and Orkin's Hematology of Infancy and Childhood 2014, Saunders/Elsevier, Philadelphia. 8th ed. S.A. Orkin, D.G. Nathan, D. Ginsburg, A.T. Look, D.E. Fisher, S.E. Lux (Eds.).
    • (2014) Nathan and Orkin's Hematology of Infancy and Childhood
    • Hajjar, K.A.1
  • 6
    • 34047229067 scopus 로고    scopus 로고
    • Thrombin generation and fibrin clot structure
    • Wolberg A.S. Thrombin generation and fibrin clot structure. Blood Rev 2007, 21(3):131-142.
    • (2007) Blood Rev , vol.21 , Issue.3 , pp. 131-142
    • Wolberg, A.S.1
  • 7
    • 84898969214 scopus 로고    scopus 로고
    • Fibrinogen and red blood cells in venous thrombosis
    • Aleman M.M., Walton B.L., Byrnes J.R., Wolberg A.S. Fibrinogen and red blood cells in venous thrombosis. Thromb Res 2014, 133(Suppl. 1):S38-S40.
    • (2014) Thromb Res , vol.133 , pp. S38-S40
    • Aleman, M.M.1    Walton, B.L.2    Byrnes, J.R.3    Wolberg, A.S.4
  • 9
    • 78649726921 scopus 로고    scopus 로고
    • Flow profoundly influences fibrin network structure: implications for fibrin formation and clot stability in haemostasis
    • Campbell R.A., Aleman M., Gray L.D., Falvo M.R., Wolberg A.S. Flow profoundly influences fibrin network structure: implications for fibrin formation and clot stability in haemostasis. Thromb Haemost 2010, 104(6):1281-1284.
    • (2010) Thromb Haemost , vol.104 , Issue.6 , pp. 1281-1284
    • Campbell, R.A.1    Aleman, M.2    Gray, L.D.3    Falvo, M.R.4    Wolberg, A.S.5
  • 10
    • 77950635369 scopus 로고    scopus 로고
    • Thrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow
    • Neeves K.B., Illing D.A., Diamond S.L. Thrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow. Biophys J 2010, 98(7):1344-1352.
    • (2010) Biophys J , vol.98 , Issue.7 , pp. 1344-1352
    • Neeves, K.B.1    Illing, D.A.2    Diamond, S.L.3
  • 11
    • 0027965921 scopus 로고
    • Fibrin in human plasma: gel architectures governed by rate and nature of fibrinogen activation
    • Blombäck B., Carlsson K., Fatah K., Hessel B., Procyk R. Fibrin in human plasma: gel architectures governed by rate and nature of fibrinogen activation. Thromb Res 1994, 75(5):521-538.
    • (1994) Thromb Res , vol.75 , Issue.5 , pp. 521-538
    • Blombäck, B.1    Carlsson, K.2    Fatah, K.3    Hessel, B.4    Procyk, R.5
  • 12
    • 0036741158 scopus 로고    scopus 로고
    • Analyzing fibrin clot structure using a microplate reader
    • Wolberg A.S., Gabriel D.A., Hoffman M. Analyzing fibrin clot structure using a microplate reader. Blood Coagul Fibrinolysis 2002, 13(6):533-539.
    • (2002) Blood Coagul Fibrinolysis , vol.13 , Issue.6 , pp. 533-539
    • Wolberg, A.S.1    Gabriel, D.A.2    Hoffman, M.3
  • 13
    • 0037534900 scopus 로고    scopus 로고
    • Elevated prothrombin results in clots with an altered fiber structure: a possible mechanism of the increased thrombotic risk
    • Wolberg A.S., Monroe D.M., Roberts H.R., Hoffman M. Elevated prothrombin results in clots with an altered fiber structure: a possible mechanism of the increased thrombotic risk. Blood 2003, 101(8):3008-3013.
    • (2003) Blood , vol.101 , Issue.8 , pp. 3008-3013
    • Wolberg, A.S.1    Monroe, D.M.2    Roberts, H.R.3    Hoffman, M.4
  • 14
    • 81755161511 scopus 로고    scopus 로고
    • Fibrin clot structure and function: a role in the pathophysiology of arterial and venous thromboembolic diseases
    • Undas A., Ariëns R.A. Fibrin clot structure and function: a role in the pathophysiology of arterial and venous thromboembolic diseases. Arterioscler Thromb Vasc Biol 2011, 31(12):e88-e99.
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , Issue.12 , pp. e88-e99
    • Undas, A.1    Ariëns, R.A.2
  • 16
    • 84880620943 scopus 로고    scopus 로고
    • Fibrin(ogen) and thrombotic disease
    • Ariëns R.A. Fibrin(ogen) and thrombotic disease. J Thromb Haemost 2013, 11(Suppl. 1):294-305.
    • (2013) J Thromb Haemost , vol.11 , pp. 294-305
    • Ariëns, R.A.1
  • 17
    • 33644797001 scopus 로고    scopus 로고
    • High dose factor VIIa improves clot structure and stability in a model of haemophilia B
    • Wolberg A.S., Allen G.A., Monroe D.M., Hedner U., Roberts H.R., Hoffman M. High dose factor VIIa improves clot structure and stability in a model of haemophilia B. Br J Haematol 2005, 131(5):645-655.
    • (2005) Br J Haematol , vol.131 , Issue.5 , pp. 645-655
    • Wolberg, A.S.1    Allen, G.A.2    Monroe, D.M.3    Hedner, U.4    Roberts, H.R.5    Hoffman, M.6
  • 18
    • 82355161117 scopus 로고    scopus 로고
    • Recombinant factor VIIa analog NN1731 (V158D/E296V/M298Q-FVIIa) enhances fibrin formation, structure and stability in lipidated hemophilic plasma
    • Gray L.D., Hussey M.A., Larson B.M., Machlus K.R., Campbell R.A., Koch G., et al. Recombinant factor VIIa analog NN1731 (V158D/E296V/M298Q-FVIIa) enhances fibrin formation, structure and stability in lipidated hemophilic plasma. Thromb Res 2011, 128(6):570-576.
    • (2011) Thromb Res , vol.128 , Issue.6 , pp. 570-576
    • Gray, L.D.1    Hussey, M.A.2    Larson, B.M.3    Machlus, K.R.4    Campbell, R.A.5    Koch, G.6
  • 20
    • 0029100827 scopus 로고
    • Effect of fibrin structure on plasmin-mediated dissolution of plasma clots
    • Carr M.E., Alving B.M. Effect of fibrin structure on plasmin-mediated dissolution of plasma clots. Blood Coagul Fibrinolysis 1995, 6(6):567-573.
    • (1995) Blood Coagul Fibrinolysis , vol.6 , Issue.6 , pp. 567-573
    • Carr, M.E.1    Alving, B.M.2
  • 21
    • 0026491075 scopus 로고
    • The effect of fibrin structure on fibrinolysis
    • Gabriel D.A., Muga K., Boothroyd E.M. The effect of fibrin structure on fibrinolysis. J Biol Chem 1992, 267(34):24259-24263.
    • (1992) J Biol Chem , vol.267 , Issue.34 , pp. 24259-24263
    • Gabriel, D.A.1    Muga, K.2    Boothroyd, E.M.3
  • 22
    • 78751560568 scopus 로고    scopus 로고
    • The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies
    • Longstaff C., Thelwell C., Williams S.C., Silva M.M., Szabó L., Kolev K. The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies. Blood 2011, 117(2):661-668.
    • (2011) Blood , vol.117 , Issue.2 , pp. 661-668
    • Longstaff, C.1    Thelwell, C.2    Williams, S.C.3    Silva, M.M.4    Szabó, L.5    Kolev, K.6
  • 23
    • 0038353228 scopus 로고    scopus 로고
    • Dynamic changes of fibrin architecture during fibrin formation and intrinsic fibrinolysis of fibrin-rich clots
    • Collet J.P., Lesty C., Montalescot G., Weisel J.W. Dynamic changes of fibrin architecture during fibrin formation and intrinsic fibrinolysis of fibrin-rich clots. J Biol Chem 2003, 278(24):21331-21335.
    • (2003) J Biol Chem , vol.278 , Issue.24 , pp. 21331-21335
    • Collet, J.P.1    Lesty, C.2    Montalescot, G.3    Weisel, J.W.4
  • 24
    • 0038494830 scopus 로고    scopus 로고
    • Fibrinogen gamma-chain splice variant gamma' alters fibrin formation and structure
    • Cooper A.V., Standeven K.F., Ariëns R.A. Fibrinogen gamma-chain splice variant gamma' alters fibrin formation and structure. Blood 2003, 102(2):535-540.
    • (2003) Blood , vol.102 , Issue.2 , pp. 535-540
    • Cooper, A.V.1    Standeven, K.F.2    Ariëns, R.A.3
  • 25
    • 34147133409 scopus 로고    scopus 로고
    • Elevated plasma fibrinogen gamma' concentration is associated with myocardial infarction: effects of variation in fibrinogen genes and environmental factors
    • Mannila M.N., Lovely R.S., Kazmierczak S.C., Eriksson P., Samnegård A., Farrell D.H., et al. Elevated plasma fibrinogen gamma' concentration is associated with myocardial infarction: effects of variation in fibrinogen genes and environmental factors. J Thromb Haemost 2007, 5(4):766-773.
    • (2007) J Thromb Haemost , vol.5 , Issue.4 , pp. 766-773
    • Mannila, M.N.1    Lovely, R.S.2    Kazmierczak, S.C.3    Eriksson, P.4    Samnegård, A.5    Farrell, D.H.6
  • 27
    • 57749189817 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of the fibrinolytic system
    • Rijken D.C., Lijnen H.R. New insights into the molecular mechanisms of the fibrinolytic system. J Thromb Haemost 2009, 7(1):4-13.
    • (2009) J Thromb Haemost , vol.7 , Issue.1 , pp. 4-13
    • Rijken, D.C.1    Lijnen, H.R.2
  • 28
    • 0028359176 scopus 로고
    • Cellular receptors for the plasminogen activators
    • Bu G., Warshawsky I., Schwartz A.L. Cellular receptors for the plasminogen activators. Blood 1994, 83(12):3427-3436.
    • (1994) Blood , vol.83 , Issue.12 , pp. 3427-3436
    • Bu, G.1    Warshawsky, I.2    Schwartz, A.L.3
  • 29
    • 18444386848 scopus 로고    scopus 로고
    • Molecular mechanisms of fibrinolysis
    • Cesarman-Maus G., Hajjar K.A. Molecular mechanisms of fibrinolysis. Br J Haematol 2005, 129(3):307-321.
    • (2005) Br J Haematol , vol.129 , Issue.3 , pp. 307-321
    • Cesarman-Maus, G.1    Hajjar, K.A.2
  • 30
    • 0020472522 scopus 로고
    • Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin
    • Hoylaerts M., Rijken D.C., Lijnen H.R., Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J Biol Chem 1982, 257(6):2912-2919.
    • (1982) J Biol Chem , vol.257 , Issue.6 , pp. 2912-2919
    • Hoylaerts, M.1    Rijken, D.C.2    Lijnen, H.R.3    Collen, D.4
  • 31
    • 0023101988 scopus 로고
    • Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis
    • Tate K.M., Higgins D.L., Holmes W.E., Winkler M.E., Heyneker H.L., Vehar G.A. Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis. Biochemistry 1987, 26(2):338-343.
    • (1987) Biochemistry , vol.26 , Issue.2 , pp. 338-343
    • Tate, K.M.1    Higgins, D.L.2    Holmes, W.E.3    Winkler, M.E.4    Heyneker, H.L.5    Vehar, G.A.6
  • 32
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis J., Salvesen G.S. Human plasma proteinase inhibitors. Annu Rev Biochem 1983, 52:655-709.
    • (1983) Annu Rev Biochem , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 33
    • 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., Nesheim M. A study of the protection of plasmin from antiplasmin inhibition within an intact fibrin clot during the course of clot lysis. J Biol Chem 2004, 279(14):13333-13339.
    • (2004) J Biol Chem , vol.279 , Issue.14 , pp. 13333-13339
    • Schneider, M.1    Nesheim, M.2
  • 34
    • 0023130521 scopus 로고
    • Plasminogen activator inhibitors
    • Sprengers E.D., Kluft C. Plasminogen activator inhibitors. Blood 1987, 69(2):381-387.
    • (1987) Blood , vol.69 , Issue.2 , pp. 381-387
    • Sprengers, E.D.1    Kluft, C.2
  • 36
    • 84861582367 scopus 로고    scopus 로고
    • Angiogenic and fibrinolytic factors in blood during the first half of pregnancy and adverse pregnancy outcomes
    • Coolman M., Timmermans S., de Groot C.J., Russcher H., Lindemans J., Hofman A., et al. Angiogenic and fibrinolytic factors in blood during the first half of pregnancy and adverse pregnancy outcomes. Obstet Gynecol 2012, 119(6):1190-1200.
    • (2012) Obstet Gynecol , vol.119 , Issue.6 , pp. 1190-1200
    • Coolman, M.1    Timmermans, S.2    de Groot, C.J.3    Russcher, H.4    Lindemans, J.5    Hofman, A.6
  • 37
    • 10544253848 scopus 로고    scopus 로고
    • Coagulation-dependent inhibition of fibrinolysis: role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma
    • Broze G.J., Higuchi D.A. Coagulation-dependent inhibition of fibrinolysis: role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma. Blood 1996, 88(10):3815-3823.
    • (1996) Blood , vol.88 , Issue.10 , pp. 3815-3823
    • Broze, G.J.1    Higuchi, D.A.2
  • 38
    • 0034757342 scopus 로고    scopus 로고
    • The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration
    • Mosnier L.O., Lisman T., van den Berg H.M., Nieuwenhuis H.K., Meijers J.C., Bouma B.N. The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration. Thromb Haemost 2001, 86(4):1035-1039.
    • (2001) Thromb Haemost , vol.86 , Issue.4 , pp. 1035-1039
    • Mosnier, L.O.1    Lisman, T.2    van den Berg, H.M.3    Nieuwenhuis, H.K.4    Meijers, J.C.5    Bouma, B.N.6
  • 39
    • 0019840121 scopus 로고
    • The presence and release of alpha 2-antiplasmin from human platelets
    • Plow E.F., Collen D. The presence and release of alpha 2-antiplasmin from human platelets. Blood 1981, 58(6):1069-1074.
    • (1981) Blood , vol.58 , Issue.6 , pp. 1069-1074
    • Plow, E.F.1    Collen, D.2
  • 40
    • 0020575314 scopus 로고
    • Factor XIII-mediated cross-linking of NH2-terminal peptide of alpha 2-plasmin inhibitor to fibrin
    • Ichinose A., Tamaki T., Aoki N. Factor XIII-mediated cross-linking of NH2-terminal peptide of alpha 2-plasmin inhibitor to fibrin. FEBS Lett 1983, 153(2):369-371.
    • (1983) FEBS Lett , vol.153 , Issue.2 , pp. 369-371
    • Ichinose, A.1    Tamaki, T.2    Aoki, N.3
  • 41
    • 0022979474 scopus 로고
    • Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor
    • Kimura S., Aoki N. Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor. J Biol Chem 1986, 261(33):15591-15595.
    • (1986) J Biol Chem , vol.261 , Issue.33 , pp. 15591-15595
    • Kimura, S.1    Aoki, N.2
  • 42
    • 48249103964 scopus 로고    scopus 로고
    • Searching for differences between fibrinogen and fibrin that affect the initiation of fibrinolysis
    • Doolittle R.F. Searching for differences between fibrinogen and fibrin that affect the initiation of fibrinolysis. Cardiovasc Hematol Agents Med Chem 2008, 6(3):181-189.
    • (2008) Cardiovasc Hematol Agents Med Chem , vol.6 , Issue.3 , pp. 181-189
    • Doolittle, R.F.1
  • 43
    • 0027078388 scopus 로고
    • The mechanism of plasminogen activation and the variability of the fibrin effector during tissue-type plasminogen activator-mediated fibrinolysis
    • Thorsen S. The mechanism of plasminogen activation and the variability of the fibrin effector during tissue-type plasminogen activator-mediated fibrinolysis. Ann N Y Acad Sci 1992, 667:52-63.
    • (1992) Ann N Y Acad Sci , vol.667 , pp. 52-63
    • Thorsen, S.1
  • 44
    • 80052975849 scopus 로고    scopus 로고
    • The novel plasminogen receptor, plasminogen receptor(KT) (Plg-R(KT)), regulates catecholamine release
    • Bai H., Baik N., Kiosses W.B., Krajewski S., Miles L.A., Parmer R.J. The novel plasminogen receptor, plasminogen receptor(KT) (Plg-R(KT)), regulates catecholamine release. J Biol Chem 2011, 286(38):33125-33133.
    • (2011) J Biol Chem , vol.286 , Issue.38 , pp. 33125-33133
    • Bai, H.1    Baik, N.2    Kiosses, W.B.3    Krajewski, S.4    Miles, L.A.5    Parmer, R.J.6
  • 45
    • 0028944244 scopus 로고
    • The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae
    • Stahl A., Mueller B.M. The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae. J Cell Biol 1995, 129(2):335-344.
    • (1995) J Cell Biol , vol.129 , Issue.2 , pp. 335-344
    • Stahl, A.1    Mueller, B.M.2
  • 46
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane
    • Okamoto T., Schlegel A., Scherer P.E., Lisanti M.P. Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane. J Biol Chem 1998, 273(10):5419-5422.
    • (1998) J Biol Chem , vol.273 , Issue.10 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 47
    • 36349028713 scopus 로고    scopus 로고
    • S100A10/p11: family, friends and functions
    • Rescher U., Gerke V. S100A10/p11: family, friends and functions. Pflugers Arch 2008, 455(4):575-582.
    • (2008) Pflugers Arch , vol.455 , Issue.4 , pp. 575-582
    • Rescher, U.1    Gerke, V.2
  • 48
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: linking Ca2+ signalling to membrane dynamics
    • Gerke V., Creutz C.E., Moss S.E. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 2005, 6(6):449-461.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 49
    • 77950191136 scopus 로고    scopus 로고
    • Annexins as disease modifiers
    • Fatimathas L., Moss S.E. Annexins as disease modifiers. Histol Histopathol 2010, 25(4):527-532.
    • (2010) Histol Histopathol , vol.25 , Issue.4 , pp. 527-532
    • Fatimathas, L.1    Moss, S.E.2
  • 50
    • 3242877433 scopus 로고    scopus 로고
    • Annexins-unique membrane binding proteins with diverse functions
    • Rescher U., Gerke V. Annexins-unique membrane binding proteins with diverse functions. J Cell Sci 2004, 117(Pt 13):2631-2639.
    • (2004) J Cell Sci , vol.117 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 51
    • 0025363927 scopus 로고
    • Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase
    • Hajjar K.A., Hamel N.M. Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase. J Biol Chem 1990, 265(5):2908-2916.
    • (1990) J Biol Chem , vol.265 , Issue.5 , pp. 2908-2916
    • Hajjar, K.A.1    Hamel, N.M.2
  • 52
    • 0028844290 scopus 로고
    • Annexin II, tetramer: structure and function
    • Waisman D.M. Annexin II, tetramer: structure and function. Mol Cell Biochem 1995, 149-150:301-322.
    • (1995) Mol Cell Biochem , pp. 301-322
    • Waisman, D.M.1
  • 53
    • 79957955929 scopus 로고    scopus 로고
    • The annexin A2 system and vascular homeostasis
    • Flood E.C., Hajjar K.A. The annexin A2 system and vascular homeostasis. Vascul Pharmacol 2011, 54(3-6):59-67.
    • (2011) Vascul Pharmacol , vol.54 , Issue.3-6 , pp. 59-67
    • Flood, E.C.1    Hajjar, K.A.2
  • 55
    • 33744481250 scopus 로고    scopus 로고
    • Autoantibodies against the fibrinolytic receptor, annexin 2, in antiphospholipid syndrome
    • Cesarman-Maus G., Ríos-Luna N.P., Deora A.B., Huang B., Villa R., Cravioto Mdel C., et al. Autoantibodies against the fibrinolytic receptor, annexin 2, in antiphospholipid syndrome. Blood 2006, 107(11):4375-4382.
    • (2006) Blood , vol.107 , Issue.11 , pp. 4375-4382
    • Cesarman-Maus, G.1    Ríos-Luna, N.P.2    Deora, A.B.3    Huang, B.4    Villa, R.5    Cravioto Mdel, C.6
  • 56
    • 16844366938 scopus 로고    scopus 로고
    • Genetic dissection and prognostic modeling of overt stroke in sickle cell anemia
    • Sebastiani P., Ramoni M.F., Nolan V., Baldwin C.T., Steinberg M.H. Genetic dissection and prognostic modeling of overt stroke in sickle cell anemia. Nat Genet 2005, 37(4):435-440.
    • (2005) Nat Genet , vol.37 , Issue.4 , pp. 435-440
    • Sebastiani, P.1    Ramoni, M.F.2    Nolan, V.3    Baldwin, C.T.4    Steinberg, M.H.5
  • 61
    • 0000704637 scopus 로고
    • Action of thrombin in the clotting of fibrinogen
    • Bailey K., Bettelheim F.R., Lorand L., Middlebrook W.R. Action of thrombin in the clotting of fibrinogen. Nature 1951, 167(4241):233-234.
    • (1951) Nature , vol.167 , Issue.4241 , pp. 233-234
    • Bailey, K.1    Bettelheim, F.R.2    Lorand, L.3    Middlebrook, W.R.4
  • 62
    • 0011879835 scopus 로고
    • The clotting of fibrinogen. I. The liberation of peptide material
    • Bailey K., Bettelheim F.R. The clotting of fibrinogen. I. The liberation of peptide material. Biochim Biophys Acta 1955, 18(4):495-503.
    • (1955) Biochim Biophys Acta , vol.18 , Issue.4 , pp. 495-503
    • Bailey, K.1    Bettelheim, F.R.2
  • 63
    • 0001683864 scopus 로고
    • Inhibition of fibrin polymerization by fibrinogen proteolysis products
    • Latallo Z.S., Fletcher A.P., Alkjaersig N., Sherry S. Inhibition of fibrin polymerization by fibrinogen proteolysis products. Am J Physiol 1962, 202:681-686.
    • (1962) Am J Physiol , vol.202 , pp. 681-686
    • Latallo, Z.S.1    Fletcher, A.P.2    Alkjaersig, N.3    Sherry, S.4
  • 64
    • 84890505971 scopus 로고    scopus 로고
    • Evaluation of the innovance d-dimer assay for the diagnosis of disseminated intravascular coagulopathy in different clinical settings
    • Khalafallah A., Jarvis C., Morse M., Albarzan A.M., Stewart P., Bates G., et al. Evaluation of the innovance d-dimer assay for the diagnosis of disseminated intravascular coagulopathy in different clinical settings. Clin Appl Thromb Hemost 2014, 20(1):91-97.
    • (2014) Clin Appl Thromb Hemost , vol.20 , Issue.1 , pp. 91-97
    • Khalafallah, A.1    Jarvis, C.2    Morse, M.3    Albarzan, A.M.4    Stewart, P.5    Bates, G.6
  • 66
    • 84887536885 scopus 로고    scopus 로고
    • Variable D-dimer thresholds for diagnosis of clinically suspected acute pulmonary embolism
    • van der Hulle T., den Exter P.L., Erkens P.G., van Es J., Mos I.C., ten Cate H., et al. Variable D-dimer thresholds for diagnosis of clinically suspected acute pulmonary embolism. J Thromb Haemost 2013, 11(11):1986-1992.
    • (2013) J Thromb Haemost , vol.11 , Issue.11 , pp. 1986-1992
    • van der Hulle, T.1    den Exter, P.L.2    Erkens, P.G.3    van Es, J.4    Mos, I.C.5    ten Cate, H.6
  • 67
    • 84897954632 scopus 로고    scopus 로고
    • Risk assessment for thrombosis in cancer
    • Gomes M., Khorana A.A. Risk assessment for thrombosis in cancer. Semin Thromb Hemost 2014, 40(3):319-324.
    • (2014) Semin Thromb Hemost , vol.40 , Issue.3 , pp. 319-324
    • Gomes, M.1    Khorana, A.A.2
  • 69
    • 0022534483 scopus 로고
    • Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B
    • Senior R.M., Skogen W.F., Griffin G.L., Wilner G.D. Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B. J Clin Investig. 1986, 77(3):1014-1019.
    • (1986) J Clin Investig. , vol.77 , Issue.3 , pp. 1014-1019
    • Senior, R.M.1    Skogen, W.F.2    Griffin, G.L.3    Wilner, G.D.4
  • 70
    • 0017237180 scopus 로고
    • Chemotaxis for human monocytes by fibrinogen-derived peptides
    • Richardson D.L., Pepper D.S., Kay A.B. Chemotaxis for human monocytes by fibrinogen-derived peptides. Br J Haematol 1976, 32(4):507-513.
    • (1976) Br J Haematol , vol.32 , Issue.4 , pp. 507-513
    • Richardson, D.L.1    Pepper, D.S.2    Kay, A.B.3
  • 71
    • 0037392651 scopus 로고    scopus 로고
    • Identification of a region of the fibrin molecule involved in upregulation of interleukin-8 expression from human oral squamous cell carcinoma cells
    • Lalla R.V., Tanzer M.L., Kreutzer D.L. Identification of a region of the fibrin molecule involved in upregulation of interleukin-8 expression from human oral squamous cell carcinoma cells. Arch Oral Biol 2003, 48(4):263-271.
    • (2003) Arch Oral Biol , vol.48 , Issue.4 , pp. 263-271
    • Lalla, R.V.1    Tanzer, M.L.2    Kreutzer, D.L.3
  • 72
    • 60249087722 scopus 로고    scopus 로고
    • Bbeta15-42 (FX06) reduces pulmonary, myocardial, liver, and small intestine damage in a pig model of hemorrhagic shock and reperfusion
    • Roesner J.P., Petzelbauer P., Koch A., Tran N., Iber T., Vagts D.A., et al. Bbeta15-42 (FX06) reduces pulmonary, myocardial, liver, and small intestine damage in a pig model of hemorrhagic shock and reperfusion. Crit Care Med 2009, 37(2):598-605.
    • (2009) Crit Care Med , vol.37 , Issue.2 , pp. 598-605
    • Roesner, J.P.1    Petzelbauer, P.2    Koch, A.3    Tran, N.4    Iber, T.5    Vagts, D.A.6
  • 74
    • 70350722262 scopus 로고    scopus 로고
    • Two families of synthetic peptides that enhance fibrin turbidity and delay fibrinolysis by different mechanisms
    • Pandi L., Kollman J.M., Lopez-Lira F., Burrows J.M., Riley M., Doolittle R.F. Two families of synthetic peptides that enhance fibrin turbidity and delay fibrinolysis by different mechanisms. Biochemistry 2009, 48(30):7201-7208.
    • (2009) Biochemistry , vol.48 , Issue.30 , pp. 7201-7208
    • Pandi, L.1    Kollman, J.M.2    Lopez-Lira, F.3    Burrows, J.M.4    Riley, M.5    Doolittle, R.F.6
  • 75
    • 2042481386 scopus 로고    scopus 로고
    • Detection of anticoagulant activities of isolated canine fibrinogen degradation products X, Y, D and E using resonance thrombography
    • Mischke R., Wolling H., Nolte I. Detection of anticoagulant activities of isolated canine fibrinogen degradation products X, Y, D and E using resonance thrombography. Blood Coagul Fibrinolysis 2004, 15(1):81-88.
    • (2004) Blood Coagul Fibrinolysis , vol.15 , Issue.1 , pp. 81-88
    • Mischke, R.1    Wolling, H.2    Nolte, I.3
  • 76
    • 0033803758 scopus 로고    scopus 로고
    • Influence of fibrinogen degradation products on thrombin time, activated partial thromboplastin time and prothrombin time of canine plasma
    • Mischke R., Wolling H. Influence of fibrinogen degradation products on thrombin time, activated partial thromboplastin time and prothrombin time of canine plasma. Haemostasis 2000, 30(3):123-130.
    • (2000) Haemostasis , vol.30 , Issue.3 , pp. 123-130
    • Mischke, R.1    Wolling, H.2
  • 77
    • 0018603151 scopus 로고
    • Effect of fibrin degradation products and thrombin on fibrinogen synthesis
    • Ittyerah T.R., Weidner N., Wochner R.D., Sherman L.A. Effect of fibrin degradation products and thrombin on fibrinogen synthesis. Br J Haematol 1979, 43(4):661-668.
    • (1979) Br J Haematol , vol.43 , Issue.4 , pp. 661-668
    • Ittyerah, T.R.1    Weidner, N.2    Wochner, R.D.3    Sherman, L.A.4
  • 78
    • 0023217132 scopus 로고
    • Inactivation of factor Va by plasmin
    • Omar M.N., Mann K.G. Inactivation of factor Va by plasmin. J Biol Chem 1987, 262:9750-9755.
    • (1987) J Biol Chem , vol.262 , pp. 9750-9755
    • Omar, M.N.1    Mann, K.G.2
  • 80
    • 0023096623 scopus 로고
    • The regulation of natural anticoagulant pathways
    • Esmon C.T. The regulation of natural anticoagulant pathways. Science 1987, 235:1348-1352.
    • (1987) Science , vol.235 , pp. 1348-1352
    • Esmon, C.T.1
  • 81
    • 0022483249 scopus 로고
    • Activation of plasminogen by tissue plasminogen activator on normal and thrombasthenic platelets: effects on surface proteins and platelet aggregation
    • Stricker R.B., Wong D., Shiu D.T., Reyes P.T., Shuman M.A. Activation of plasminogen by tissue plasminogen activator on normal and thrombasthenic platelets: effects on surface proteins and platelet aggregation. Blood 1986, 68:275-280.
    • (1986) Blood , vol.68 , pp. 275-280
    • Stricker, R.B.1    Wong, D.2    Shiu, D.T.3    Reyes, P.T.4    Shuman, M.A.5
  • 82
    • 0022862225 scopus 로고
    • Proteolysis of platelet glycoprotein by plasmin is facilitated by plasmin lysine-binding regions
    • Adelman B., Michelson A.D., Greenberg J., Handin R.I. Proteolysis of platelet glycoprotein by plasmin is facilitated by plasmin lysine-binding regions. Blood 1986, 68:1280-1284.
    • (1986) Blood , vol.68 , pp. 1280-1284
    • Adelman, B.1    Michelson, A.D.2    Greenberg, J.3    Handin, R.I.4
  • 83
    • 0024456136 scopus 로고
    • Correlation between template bleeding times and spontaneous bleeding during treatment of acute myocardial infarction with recombinant issue type plasminogen activator
    • Gimple L.W., Gold H.K., Leinbach R.C., Coller B.S, Werner W., Yasuda T., et al. Correlation between template bleeding times and spontaneous bleeding during treatment of acute myocardial infarction with recombinant issue type plasminogen activator. Circulation 1989, 80:581-588.
    • (1989) Circulation , vol.80 , pp. 581-588
    • Gimple, L.W.1    Gold, H.K.2    Leinbach, R.C.3    Coller, B.S.4    Werner, W.5    Yasuda, T.6
  • 84
    • 0025097994 scopus 로고
    • Platelets and thrombolytic therapy
    • Coller B.S. Platelets and thrombolytic therapy. N Engl J Med 1990, 322:33-42.
    • (1990) N Engl J Med , vol.322 , pp. 33-42
    • Coller, B.S.1
  • 85
    • 0024558370 scopus 로고
    • The roles of protein C and thrombomodulin in the regulation of blood coagulation
    • Esmon C.T. The roles of protein C and thrombomodulin in the regulation of blood coagulation. J Biol Chem 1989, 264:4743-4746.
    • (1989) J Biol Chem , vol.264 , pp. 4743-4746
    • Esmon, C.T.1
  • 86
    • 0029939761 scopus 로고    scopus 로고
    • Surface thrombomodulin modulates thrombin receptor responses on vascular smooth muscle cells
    • Grinnell B.W., Berg D.T. Surface thrombomodulin modulates thrombin receptor responses on vascular smooth muscle cells. Am J Physiol 1996, 270:H603-H609.
    • (1996) Am J Physiol , vol.270 , pp. H603-H609
    • Grinnell, B.W.1    Berg, D.T.2
  • 87
    • 0031965910 scopus 로고    scopus 로고
    • Thrombomodulin modulates the mitogenic response to thrombin of human umbilical vein endothelial cells
    • Lafay M., Laguna R., Le Bonniec B.F., Lasne D., Aiach M., Rendu F. Thrombomodulin modulates the mitogenic response to thrombin of human umbilical vein endothelial cells. Thromb Haemost 1998, 79:848-852.
    • (1998) Thromb Haemost , vol.79 , pp. 848-852
    • Lafay, M.1    Laguna, R.2    Le Bonniec, B.F.3    Lasne, D.4    Aiach, M.5    Rendu, F.6
  • 88
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin activatable fibrinolysis inhibitor
    • Bajzar L., Manuel R., Nesheim M. Purification and characterization of TAFI, a thrombin activatable fibrinolysis inhibitor. J Biol Chem 1995, 270:14477-14484.
    • (1995) J Biol Chem , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.3
  • 89
    • 0025889743 scopus 로고
    • Acceleration of the thrombin inactivation of single chain urokinase-type plasminogen activator (pro-urokinase) by thrombomodulin
    • de Munk G.A.W., Groeneveld E., Rijken D.C. Acceleration of the thrombin inactivation of single chain urokinase-type plasminogen activator (pro-urokinase) by thrombomodulin. J Clin Invest 1991, 88:1680-1684.
    • (1991) J Clin Invest , vol.88 , pp. 1680-1684
    • de Munk, G.A.W.1    Groeneveld, E.2    Rijken, D.C.3
  • 90
    • 0026594613 scopus 로고
    • Thrombomodulin is a cofactor for thrombin degradation of recombinant single-chain urokinase plasminogen activator in vitro and in a perfused rabbit heart model
    • Molinari A., Giorgetti C., Lansen J., Vaghi F., Orsini G., Faioni E.M., et al. Thrombomodulin is a cofactor for thrombin degradation of recombinant single-chain urokinase plasminogen activator in vitro and in a perfused rabbit heart model. Thromb Haemost 1992, 67:226-232.
    • (1992) Thromb Haemost , vol.67 , pp. 226-232
    • Molinari, A.1    Giorgetti, C.2    Lansen, J.3    Vaghi, F.4    Orsini, G.5    Faioni, E.M.6
  • 91
    • 0030877824 scopus 로고    scopus 로고
    • Molecular crosstalk between adhesion receptors and proteolytic cascades in vascular remodeling
    • Preissner K.T., May A.E., Wohn K.D., Germer M., Kanse S.M. Molecular crosstalk between adhesion receptors and proteolytic cascades in vascular remodeling. Thromb Haemost 1997, 78:88-95.
    • (1997) Thromb Haemost , vol.78 , pp. 88-95
    • Preissner, K.T.1    May, A.E.2    Wohn, K.D.3    Germer, M.4    Kanse, S.M.5
  • 93
  • 94
  • 95
    • 0032189655 scopus 로고    scopus 로고
    • Gamma-Chain dysfibrinogenemias: molecular structure-function relationships of naturally occurring mutations in the gamma chain of human fibrinogen
    • Côté H.C., Lord S.T., Pratt K.P. gamma-Chain dysfibrinogenemias: molecular structure-function relationships of naturally occurring mutations in the gamma chain of human fibrinogen. Blood 1998, 92(7):2195-2212.
    • (1998) Blood , vol.92 , Issue.7 , pp. 2195-2212
    • Côté, H.C.1    Lord, S.T.2    Pratt, K.P.3
  • 96
    • 0021341834 scopus 로고
    • Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation
    • Lijnen H.R., Soria J., Soria C., Collen D., Caen J.P. Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation. Thromb Haemost 1984, 51(1):108-109.
    • (1984) Thromb Haemost , vol.51 , Issue.1 , pp. 108-109
    • Lijnen, H.R.1    Soria, J.2    Soria, C.3    Collen, D.4    Caen, J.P.5
  • 97
    • 0343603909 scopus 로고    scopus 로고
    • Bleeding and thrombosis in 55 patients with inherited afibrinogenaemia
    • Lak M., Keihani M., Elahi F., Peyvandi F., Mannucci P.M. Bleeding and thrombosis in 55 patients with inherited afibrinogenaemia. Br J Haematol 1999, 107(1):204-206.
    • (1999) Br J Haematol , vol.107 , Issue.1 , pp. 204-206
    • Lak, M.1    Keihani, M.2    Elahi, F.3    Peyvandi, F.4    Mannucci, P.M.5
  • 98
    • 3042677724 scopus 로고    scopus 로고
    • Thrombin induces angiogenesis and vascular endothelial growth factor expression in human endothelial cells: possible relevance to HIF-1alpha
    • Dupuy E., Habib A., Lebret M., Yang R., Levy-Toledano S., Tobelem G. Thrombin induces angiogenesis and vascular endothelial growth factor expression in human endothelial cells: possible relevance to HIF-1alpha. J Thromb Haemost 2003, 1(5):1096-1102.
    • (2003) J Thromb Haemost , vol.1 , Issue.5 , pp. 1096-1102
    • Dupuy, E.1    Habib, A.2    Lebret, M.3    Yang, R.4    Levy-Toledano, S.5    Tobelem, G.6
  • 101
    • 84886641933 scopus 로고    scopus 로고
    • Pulmonary embolism in a patient with congenital afibrinogenemia
    • Chapin J., DeSancho M. Pulmonary embolism in a patient with congenital afibrinogenemia. Haemophilia 2013, 19(6):e380-e382.
    • (2013) Haemophilia , vol.19 , Issue.6 , pp. e380-e382
    • Chapin, J.1    DeSancho, M.2
  • 102
    • 84902080384 scopus 로고    scopus 로고
    • Bleeding and coagulopathies in critical care
    • Hunt B.J. Bleeding and coagulopathies in critical care. N Engl J Med 2014, 370(22):2153.
    • (2014) N Engl J Med , vol.370 , Issue.22 , pp. 2153
    • Hunt, B.J.1
  • 103
    • 79960241376 scopus 로고    scopus 로고
    • The coagulopathy of chronic liver disease
    • Tripodi A., Mannucci P.M. The coagulopathy of chronic liver disease. N Engl J Med 2011, 365(2):147-156.
    • (2011) N Engl J Med , vol.365 , Issue.2 , pp. 147-156
    • Tripodi, A.1    Mannucci, P.M.2
  • 104
    • 0036775077 scopus 로고    scopus 로고
    • Markers of endothelial cell injury and thrombin activatable fibrinolysis inhibitor in nephrotic syndrome
    • Malyszko J., Malyszko J.S., Mysliwiec M. Markers of endothelial cell injury and thrombin activatable fibrinolysis inhibitor in nephrotic syndrome. Blood Coagul Fibrinolysis 2002, 13(7):615-621.
    • (2002) Blood Coagul Fibrinolysis , vol.13 , Issue.7 , pp. 615-621
    • Malyszko, J.1    Malyszko, J.S.2    Mysliwiec, M.3
  • 105
    • 0025991654 scopus 로고
    • Alpha 2-antiplasmin, plasminogen activator inhibitor (PAI) and dilute blood clot lysis time in selected disease states
    • Cucuianu M., Knauer O., Roman S. Alpha 2-antiplasmin, plasminogen activator inhibitor (PAI) and dilute blood clot lysis time in selected disease states. Thromb Haemost 1991, 66(5):586-591.
    • (1991) Thromb Haemost , vol.66 , Issue.5 , pp. 586-591
    • Cucuianu, M.1    Knauer, O.2    Roman, S.3
  • 106
    • 0034063382 scopus 로고    scopus 로고
    • Reversion of primary hyperfibrinogenolysis in patients with hormone-refractory prostate cancer using docetaxel
    • Sallah S., Gagnon G.A. Reversion of primary hyperfibrinogenolysis in patients with hormone-refractory prostate cancer using docetaxel. Cancer Investig 2000, 18(3):191-196.
    • (2000) Cancer Investig , vol.18 , Issue.3 , pp. 191-196
    • Sallah, S.1    Gagnon, G.A.2
  • 107
    • 0014211632 scopus 로고
    • Fibrinolysis and hemorrhage in a fatal case of heat stroke
    • Meikle A.W., Graybill J.R. Fibrinolysis and hemorrhage in a fatal case of heat stroke. N Engl J Med 1967, 276(16):911-913.
    • (1967) N Engl J Med , vol.276 , Issue.16 , pp. 911-913
    • Meikle, A.W.1    Graybill, J.R.2
  • 110
    • 76549101265 scopus 로고    scopus 로고
    • Managing fibrinolysis without aprotinin
    • Edmunds L.H. Managing fibrinolysis without aprotinin. Ann Thorac Surg 2010, 89(1):324-331.
    • (2010) Ann Thorac Surg , vol.89 , Issue.1 , pp. 324-331
    • Edmunds, L.H.1
  • 111
    • 77249085573 scopus 로고    scopus 로고
    • Impaired fibrinolysis in the antiphospholipid syndrome
    • Krone K.A., Allen K.L., McCrae K.R. Impaired fibrinolysis in the antiphospholipid syndrome. Curr Rheumatol Rep 2010, 12(1):53-57.
    • (2010) Curr Rheumatol Rep , vol.12 , Issue.1 , pp. 53-57
    • Krone, K.A.1    Allen, K.L.2    McCrae, K.R.3
  • 112
    • 40749143196 scopus 로고    scopus 로고
    • New role of plasminogen activator inhibitor-1 in alcohol-induced liver injury
    • Arteel G.E. New role of plasminogen activator inhibitor-1 in alcohol-induced liver injury. J Gastroenterol Hepatol 2008, 23(Suppl. 1):S54-S59.
    • (2008) J Gastroenterol Hepatol , vol.23 , pp. S54-S59
    • Arteel, G.E.1
  • 113
    • 84905106638 scopus 로고    scopus 로고
    • Prothrombotic alterations in plasma fibrin clot properties in thyroid disorders and their post-treatment modifications
    • Mazur P., Sokołowski G., Hubalewska-Dydejczyk A., Płaczkiewicz-Jankowska E., Undas A. Prothrombotic alterations in plasma fibrin clot properties in thyroid disorders and their post-treatment modifications. Thromb Res 2014, 134(2):510-517.
    • (2014) Thromb Res , vol.134 , Issue.2 , pp. 510-517
    • Mazur, P.1    Sokołowski, G.2    Hubalewska-Dydejczyk, A.3    Płaczkiewicz-Jankowska, E.4    Undas, A.5
  • 114
    • 29244431932 scopus 로고    scopus 로고
    • Hypofibrinolysis during induction treatment of multiple myeloma may increase the risk of venous thrombosis
    • van Marion A.M., Auwerda J.J., Minnema M.C., van Oosterom R., Adelmeijer J., de Groot P.G., et al. Hypofibrinolysis during induction treatment of multiple myeloma may increase the risk of venous thrombosis. Thromb Haemost 2005, 94(6):1341-1343.
    • (2005) Thromb Haemost , vol.94 , Issue.6 , pp. 1341-1343
    • van Marion, A.M.1    Auwerda, J.J.2    Minnema, M.C.3    van Oosterom, R.4    Adelmeijer, J.5    de Groot, P.G.6
  • 115
    • 33751224754 scopus 로고    scopus 로고
    • Livedoid vasculopathy associated with plasminogen activator inhibitor-1 promoter homozygosity (4G/4G) treated successfully with tissue plasminogen activator
    • Deng A., Gocke C.D., Hess J., Heyman M., Paltiel M., Gaspari A. Livedoid vasculopathy associated with plasminogen activator inhibitor-1 promoter homozygosity (4G/4G) treated successfully with tissue plasminogen activator. Arch Dermatol 2006, 142(11):1466-1469.
    • (2006) Arch Dermatol , vol.142 , Issue.11 , pp. 1466-1469
    • Deng, A.1    Gocke, C.D.2    Hess, J.3    Heyman, M.4    Paltiel, M.5    Gaspari, A.6
  • 116
    • 0022468096 scopus 로고
    • Atrophie blanche. A disorder associated with defective release of tissue plasminogen activator
    • Pizzo S.V., Murray J.C., Gonias S.L. Atrophie blanche. A disorder associated with defective release of tissue plasminogen activator. Arch Pathol Lab Med 1986, 110(6):517-519.
    • (1986) Arch Pathol Lab Med , vol.110 , Issue.6 , pp. 517-519
    • Pizzo, S.V.1    Murray, J.C.2    Gonias, S.L.3
  • 117
    • 33751181659 scopus 로고    scopus 로고
    • Molecular and clinical spectrum of type I plasminogen deficiency: a series of 50 patients
    • Tefs K., Gueorguieva M., Klammt J., Allen C.M., Aktas D., Anlar F.Y., et al. Molecular and clinical spectrum of type I plasminogen deficiency: a series of 50 patients. Blood 2006, 108(9):3021-3026.
    • (2006) Blood , vol.108 , Issue.9 , pp. 3021-3026
    • Tefs, K.1    Gueorguieva, M.2    Klammt, J.3    Allen, C.M.4    Aktas, D.5    Anlar, F.Y.6
  • 119
    • 55949119304 scopus 로고    scopus 로고
    • Plasminogen deficiency
    • Mehta R., Shapiro A.D. Plasminogen deficiency. Haemophilia 2008, 14(6):1261-1268.
    • (2008) Haemophilia , vol.14 , Issue.6 , pp. 1261-1268
    • Mehta, R.1    Shapiro, A.D.2
  • 120
    • 0029791836 scopus 로고    scopus 로고
    • Operative treatment of intramedullary hematoma associated with congenital deficiency of alpha 2-plasmin inhibitor: a report of three cases
    • Miyauchi Y., Mii Y., Aoki M., Tamai S., Takahashi Y., Yoshioka A. Operative treatment of intramedullary hematoma associated with congenital deficiency of alpha 2-plasmin inhibitor: a report of three cases. J Bone Joint Surg Am 1996, 78(9):1409-1414.
    • (1996) J Bone Joint Surg Am , vol.78 , Issue.9 , pp. 1409-1414
    • Miyauchi, Y.1    Mii, Y.2    Aoki, M.3    Tamai, S.4    Takahashi, Y.5    Yoshioka, A.6
  • 121
    • 55949110318 scopus 로고    scopus 로고
    • Alpha2-antiplasmin and its deficiency: fibrinolysis out of balance
    • Carpenter S.L., Mathew P. Alpha2-antiplasmin and its deficiency: fibrinolysis out of balance. Haemophilia 2008, 14(6):1250-1254.
    • (2008) Haemophilia , vol.14 , Issue.6 , pp. 1250-1254
    • Carpenter, S.L.1    Mathew, P.2
  • 122
    • 84859501126 scopus 로고    scopus 로고
    • PAI-1, progress in understanding the clinical problem and its aetiology
    • Iwaki T., Urano T., Umemura K. PAI-1, progress in understanding the clinical problem and its aetiology. Br J Haematol 2012, 157(3):291-298.
    • (2012) Br J Haematol , vol.157 , Issue.3 , pp. 291-298
    • Iwaki, T.1    Urano, T.2    Umemura, K.3
  • 123
    • 84858335416 scopus 로고    scopus 로고
    • The first report of uncontrollable subchorionic and retroplacental haemorrhage inducing preterm labour in complete PAI-1 deficiency in a human
    • Iwaki T., Nagahashi K., Kobayashi T., Umemura K., Terao T., Kanayama N. The first report of uncontrollable subchorionic and retroplacental haemorrhage inducing preterm labour in complete PAI-1 deficiency in a human. Thromb Res 2012, 129(4):e161-e163.
    • (2012) Thromb Res , vol.129 , Issue.4 , pp. e161-e163
    • Iwaki, T.1    Nagahashi, K.2    Kobayashi, T.3    Umemura, K.4    Terao, T.5    Kanayama, N.6
  • 124
    • 55949086898 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor type 1 deficiency
    • Mehta R., Shapiro A.D. Plasminogen activator inhibitor type 1 deficiency. Haemophilia 2008, 14(6):1255-1260.
    • (2008) Haemophilia , vol.14 , Issue.6 , pp. 1255-1260
    • Mehta, R.1    Shapiro, A.D.2
  • 125
    • 0028295979 scopus 로고
    • Physiological consequences of loss of plasminogen activator gene function in mice
    • Carmeliet P., Schoonjans L., Kieckens L., Ream B., Degen J., Bronson R., et al. Physiological consequences of loss of plasminogen activator gene function in mice. Nature 1994, 368(6470):419-424.
    • (1994) Nature , vol.368 , Issue.6470 , pp. 419-424
    • Carmeliet, P.1    Schoonjans, L.2    Kieckens, L.3    Ream, B.4    Degen, J.5    Bronson, R.6
  • 126
    • 84902456407 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator deficiency promotes neoplasmatogenesis in the colon of mice
    • [174-187.e175]
    • Karamanavi E., Angelopoulou K., Lavrentiadou S., Tsingotjidou A., Abas Z., Taitzoglou I., et al. Urokinase-type plasminogen activator deficiency promotes neoplasmatogenesis in the colon of mice. Transl Oncol 2014, 7(2). [174-187.e175].
    • (2014) Transl Oncol , vol.7 , Issue.2
    • Karamanavi, E.1    Angelopoulou, K.2    Lavrentiadou, S.3    Tsingotjidou, A.4    Abas, Z.5    Taitzoglou, I.6
  • 127
    • 84877029394 scopus 로고    scopus 로고
    • TAFI deficiency promotes liver damage in murine models of liver failure through defective down-regulation of hepatic inflammation
    • Hugenholtz G.C., Meijers J.C., Adelmeijer J., Porte R.J., Lisman T. TAFI deficiency promotes liver damage in murine models of liver failure through defective down-regulation of hepatic inflammation. Thromb Haemost 2013, 109(5):948-955.
    • (2013) Thromb Haemost , vol.109 , Issue.5 , pp. 948-955
    • Hugenholtz, G.C.1    Meijers, J.C.2    Adelmeijer, J.3    Porte, R.J.4    Lisman, T.5
  • 128
    • 0026597739 scopus 로고
    • Baseline fibrinolytic state and the risk of future venous thrombosis. A prospective study of endogenous tissue-type plasminogen activator and plasminogen activator inhibitor
    • Ridker P.M., Vaughan D.E., Stampfer M.J., Manson J.E., Shen C., Newcomer L.M., et al. Baseline fibrinolytic state and the risk of future venous thrombosis. A prospective study of endogenous tissue-type plasminogen activator and plasminogen activator inhibitor. Circulation 1992, 85(5):1822-1827.
    • (1992) Circulation , vol.85 , Issue.5 , pp. 1822-1827
    • Ridker, P.M.1    Vaughan, D.E.2    Stampfer, M.J.3    Manson, J.E.4    Shen, C.5    Newcomer, L.M.6
  • 129
    • 0035082403 scopus 로고    scopus 로고
    • Fibrinolytic variables in patients with recurrent venous thrombosis: a prospective cohort study
    • Crowther M.A., Roberts J., Roberts R., Johnston M., Stevens P., Skingley P., et al. Fibrinolytic variables in patients with recurrent venous thrombosis: a prospective cohort study. Thromb Haemost 2001, 85(3):390-394.
    • (2001) Thromb Haemost , vol.85 , Issue.3 , pp. 390-394
    • Crowther, M.A.1    Roberts, J.2    Roberts, R.3    Johnston, M.4    Stevens, P.5    Skingley, P.6
  • 131
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • van Tilburg N.H., Rosendaal F.R., Bertina R.M. Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood 2000, 95(9):2855-2859.
    • (2000) Blood , vol.95 , Issue.9 , pp. 2855-2859
    • van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 132
    • 12844278573 scopus 로고    scopus 로고
    • Reduced plasma fibrinolytic potential is a risk factor for venous thrombosis
    • Lisman T., de Groot P.G., Meijers J.C., Rosendaal F.R. Reduced plasma fibrinolytic potential is a risk factor for venous thrombosis. Blood 2005, 105(3):1102-1105.
    • (2005) Blood , vol.105 , Issue.3 , pp. 1102-1105
    • Lisman, T.1    de Groot, P.G.2    Meijers, J.C.3    Rosendaal, F.R.4
  • 133
    • 44449160869 scopus 로고    scopus 로고
    • Synergistic effects of hypofibrinolysis and genetic and acquired risk factors on the risk of a first venous thrombosis
    • Meltzer M.E., Lisman T., Doggen C.J., de Groot P.G., Rosendaal F.R. Synergistic effects of hypofibrinolysis and genetic and acquired risk factors on the risk of a first venous thrombosis. PLoS Med 2008, 5(5):e97.
    • (2008) PLoS Med , vol.5 , Issue.5
    • Meltzer, M.E.1    Lisman, T.2    Doggen, C.J.3    de Groot, P.G.4    Rosendaal, F.R.5
  • 135
    • 61849096750 scopus 로고    scopus 로고
    • Reduced plasma fibrinolytic capacity as a potential risk factor for a first myocardial infarction in young men
    • Meltzer M.E., Doggen C.J., de Groot P.G., Rosendaal F.R., Lisman T. Reduced plasma fibrinolytic capacity as a potential risk factor for a first myocardial infarction in young men. Br J Haematol 2009, 145(1):121-127.
    • (2009) Br J Haematol , vol.145 , Issue.1 , pp. 121-127
    • Meltzer, M.E.1    Doggen, C.J.2    de Groot, P.G.3    Rosendaal, F.R.4    Lisman, T.5
  • 136
    • 77955874727 scopus 로고    scopus 로고
    • Venous thrombosis risk associated with plasma hypofibrinolysis is explained by elevated plasma levels of TAFI and PAI-1
    • Meltzer M.E., Lisman T., de Groot P.G., Meijers J.C., le Cessie S., Doggen C.J., et al. Venous thrombosis risk associated with plasma hypofibrinolysis is explained by elevated plasma levels of TAFI and PAI-1. Blood 2010, 116(1):113-121.
    • (2010) Blood , vol.116 , Issue.1 , pp. 113-121
    • Meltzer, M.E.1    Lisman, T.2    de Groot, P.G.3    Meijers, J.C.4    le Cessie, S.5    Doggen, C.J.6
  • 137
    • 66749125298 scopus 로고    scopus 로고
    • Low thrombin activatable fibrinolysis inhibitor activity levels are associated with an increased risk of a first myocardial infarction in men
    • Meltzer M.E., Doggen C.J., de Groot P.G., Meijers J.C., Rosendaal F.R., Lisman T. Low thrombin activatable fibrinolysis inhibitor activity levels are associated with an increased risk of a first myocardial infarction in men. Haematologica 2009, 94(6):811-818.
    • (2009) Haematologica , vol.94 , Issue.6 , pp. 811-818
    • Meltzer, M.E.1    Doggen, C.J.2    de Groot, P.G.3    Meijers, J.C.4    Rosendaal, F.R.5    Lisman, T.6
  • 139
    • 84866847276 scopus 로고    scopus 로고
    • Evidence for an enhanced fibrinolytic capacity in cirrhosis as measured with two different global fibrinolysis tests
    • Rijken D.C., Kock E.L., Guimarães A.H., Talens S., Darwish Murad S., Janssen H.L., et al. Evidence for an enhanced fibrinolytic capacity in cirrhosis as measured with two different global fibrinolysis tests. J Thromb Haemost 2012, 10(10):2116-2122.
    • (2012) J Thromb Haemost , vol.10 , Issue.10 , pp. 2116-2122
    • Rijken, D.C.1    Kock, E.L.2    Guimarães, A.H.3    Talens, S.4    Darwish Murad, S.5    Janssen, H.L.6
  • 140
    • 69549126899 scopus 로고    scopus 로고
    • Thromboelastometry in patients with severe sepsis and disseminated intravascular coagulation
    • Sivula M., Pettilä V., Niemi T.T., Varpula M., Kuitunen A.H. Thromboelastometry in patients with severe sepsis and disseminated intravascular coagulation. Blood Coagul Fibrinolysis 2009, 20(6):419-426.
    • (2009) Blood Coagul Fibrinolysis , vol.20 , Issue.6 , pp. 419-426
    • Sivula, M.1    Pettilä, V.2    Niemi, T.T.3    Varpula, M.4    Kuitunen, A.H.5
  • 141
    • 84855342985 scopus 로고    scopus 로고
    • A comparative evaluation of rotation thromboelastometry and standard coagulation tests in hemodilution-induced coagulation changes after cardiac surgery
    • Ogawa S., Szlam F., Chen E.P., Nishimura T., Kim H., Roback J.D., et al. A comparative evaluation of rotation thromboelastometry and standard coagulation tests in hemodilution-induced coagulation changes after cardiac surgery. Transfusion 2012, 52(1):14-22.
    • (2012) Transfusion , vol.52 , Issue.1 , pp. 14-22
    • Ogawa, S.1    Szlam, F.2    Chen, E.P.3    Nishimura, T.4    Kim, H.5    Roback, J.D.6
  • 142
    • 84876435813 scopus 로고    scopus 로고
    • Thromboelastography-guided transfusion. Therapy in the trauma patient
    • Brazzel C. Thromboelastography-guided transfusion. Therapy in the trauma patient. AANA J 2013, 81(2):127-132.
    • (2013) AANA J , vol.81 , Issue.2 , pp. 127-132
    • Brazzel, C.1
  • 145
    • 70350459505 scopus 로고    scopus 로고
    • Hyperfibrinolysis after major trauma: differential diagnosis of lysis patterns and prognostic value of thrombelastometry
    • Schöchl H., Frietsch T., Pavelka M., Jámbor C. Hyperfibrinolysis after major trauma: differential diagnosis of lysis patterns and prognostic value of thrombelastometry. J Trauma 2009, 67(1):125-131.
    • (2009) J Trauma , vol.67 , Issue.1 , pp. 125-131
    • Schöchl, H.1    Frietsch, T.2    Pavelka, M.3    Jámbor, C.4
  • 146
    • 84898797572 scopus 로고    scopus 로고
    • Urokinase plasminogen activator gene deficiency inhibits fracture cartilage remodeling
    • Popa N.L., Wergedal J.E., Lau K.H., Mohan S., Rundle C.H. Urokinase plasminogen activator gene deficiency inhibits fracture cartilage remodeling. J Bone Miner Metab 2014, 32(2):124-135.
    • (2014) J Bone Miner Metab , vol.32 , Issue.2 , pp. 124-135
    • Popa, N.L.1    Wergedal, J.E.2    Lau, K.H.3    Mohan, S.4    Rundle, C.H.5
  • 149
    • 84903695006 scopus 로고    scopus 로고
    • The association between plasminogen activator inhibitor type 1 (PAI-1) levels, PAI-1 4G/5G polymorphism, and myocardial infarction: a Mendelian randomization meta-analysis
    • Nikolopoulos G.K., Bagos P.G., Tsangaris I., Tsiara C.G., Kopterides P., Vaiopoulos A., et al. The association between plasminogen activator inhibitor type 1 (PAI-1) levels, PAI-1 4G/5G polymorphism, and myocardial infarction: a Mendelian randomization meta-analysis. Clin Chem Lab Med 2014, 52(7):937-950.
    • (2014) Clin Chem Lab Med , vol.52 , Issue.7 , pp. 937-950
    • Nikolopoulos, G.K.1    Bagos, P.G.2    Tsangaris, I.3    Tsiara, C.G.4    Kopterides, P.5    Vaiopoulos, A.6
  • 151
    • 52249094419 scopus 로고    scopus 로고
    • The effect of the plasminogen activator inhibitor-1 4G/5G polymorphism on the thrombotic risk
    • Tsantes A.E., Nikolopoulos G.K., Bagos P.G., Bonovas S., Kopterides P., Vaiopoulos G. The effect of the plasminogen activator inhibitor-1 4G/5G polymorphism on the thrombotic risk. Thromb Res 2008, 122(6):736-742.
    • (2008) Thromb Res , vol.122 , Issue.6 , pp. 736-742
    • Tsantes, A.E.1    Nikolopoulos, G.K.2    Bagos, P.G.3    Bonovas, S.4    Kopterides, P.5    Vaiopoulos, G.6
  • 152
    • 2142653057 scopus 로고    scopus 로고
    • Tissue plasminogen activator -7351C/T enhancer polymorphism is a risk factor for lacunar stroke
    • Jannes J., Hamilton-Bruce M.A., Pilotto L., Smith B.J., Mullighan C.G., Bardy P.G., et al. Tissue plasminogen activator -7351C/T enhancer polymorphism is a risk factor for lacunar stroke. Stroke 2004, 35(5):1090-1094.
    • (2004) Stroke , vol.35 , Issue.5 , pp. 1090-1094
    • Jannes, J.1    Hamilton-Bruce, M.A.2    Pilotto, L.3    Smith, B.J.4    Mullighan, C.G.5    Bardy, P.G.6
  • 153
    • 85027955597 scopus 로고    scopus 로고
    • Genetic variations in the thrombin-activatable fibrinolysis inhibitor gene and risk of cardiovascular disease: a systematic review and meta-analysis
    • Shi J., Zhi P., Chen J., Wu P., Tan S. Genetic variations in the thrombin-activatable fibrinolysis inhibitor gene and risk of cardiovascular disease: a systematic review and meta-analysis. Thromb Res 2014, 134:610-616.
    • (2014) Thromb Res , vol.134 , pp. 610-616
    • Shi, J.1    Zhi, P.2    Chen, J.3    Wu, P.4    Tan, S.5
  • 154
    • 51849166149 scopus 로고    scopus 로고
    • Association between the Thr325Ile and Ala147Thr polymorphisms of the TAFI gene and the risk of venous thromboembolic disease
    • Verdú J., Marco P., Benlloch S., Lucas J. Association between the Thr325Ile and Ala147Thr polymorphisms of the TAFI gene and the risk of venous thromboembolic disease. Clin Appl Thromb Hemost 2008, 14(4):494-495.
    • (2008) Clin Appl Thromb Hemost , vol.14 , Issue.4 , pp. 494-495
    • Verdú, J.1    Marco, P.2    Benlloch, S.3    Lucas, J.4
  • 155
    • 70349856157 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor genetic polymorphisms as markers of the type of acute coronary syndrome
    • Tàssies D., Roqué M., Monteagudo J., Martorell T., Sionis A., Arzamendi D., et al. Thrombin-activatable fibrinolysis inhibitor genetic polymorphisms as markers of the type of acute coronary syndrome. Thromb Res 2009, 124(5):614-618.
    • (2009) Thromb Res , vol.124 , Issue.5 , pp. 614-618
    • Tàssies, D.1    Roqué, M.2    Monteagudo, J.3    Martorell, T.4    Sionis, A.5    Arzamendi, D.6
  • 156
    • 0028920904 scopus 로고
    • Plasminogen deficiency causes severe thrombosis but is compatible with development and reproduction
    • Bugge T.H., Flick M.J., Daugherty C.C., Degen J.L. Plasminogen deficiency causes severe thrombosis but is compatible with development and reproduction. Genes Dev 1995, 9:794-807.
    • (1995) Genes Dev , vol.9 , pp. 794-807
    • Bugge, T.H.1    Flick, M.J.2    Daugherty, C.C.3    Degen, J.L.4
  • 158
    • 0033106507 scopus 로고    scopus 로고
    • Alpha2-Antiplasmin gene deficiency in mice is associated with enhanced fibrinolytic potential without overt bleeding
    • Lijnen H.R., Okada K., Matsuo O., Collen D., Dewerchin M. Alpha2-Antiplasmin gene deficiency in mice is associated with enhanced fibrinolytic potential without overt bleeding. Blood 1999, 93:2274-2281.
    • (1999) Blood , vol.93 , pp. 2274-2281
    • Lijnen, H.R.1    Okada, K.2    Matsuo, O.3    Collen, D.4    Dewerchin, M.5
  • 159
    • 0027144754 scopus 로고
    • Plasminogen activator inhibitor-1 gene-deficient mice: I. Generation by homologous recombination and characterization
    • Carmeliet P., Kieckens L., Schoonjans L., Ream B., van Nuffelen A., Prendergast G., et al. Plasminogen activator inhibitor-1 gene-deficient mice: I. Generation by homologous recombination and characterization. J Clin Invest 1993, 92:2746-2755.
    • (1993) J Clin Invest , vol.92 , pp. 2746-2755
    • Carmeliet, P.1    Kieckens, L.2    Schoonjans, L.3    Ream, B.4    van Nuffelen, A.5    Prendergast, G.6
  • 160
    • 0036143120 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life
    • Nagashima M., Yin Z.F., Zhao L., White K., Zhu Y., Lasky N., et al. Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life. J Clin Invest 2002, 109(101):110.
    • (2002) J Clin Invest , vol.109 , Issue.101 , pp. 110
    • Nagashima, M.1    Yin, Z.F.2    Zhao, L.3    White, K.4    Zhu, Y.5    Lasky, N.6
  • 161
    • 33846951195 scopus 로고    scopus 로고
    • Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis
    • Wang X., Smith P.L., Hsu M.Y., Tamasi J.A., Bird E., Schumacher W.A. Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis. J Thromb Thrombolysis 2007, 23:41-49.
    • (2007) J Thromb Thrombolysis , vol.23 , pp. 41-49
    • Wang, X.1    Smith, P.L.2    Hsu, M.Y.3    Tamasi, J.A.4    Bird, E.5    Schumacher, W.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.