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Volumn 31, Issue 3, 2011, Pages 165-173

Thrombin activatable fibrinolysis inhibitor

Author keywords

Fibrinolysis; ProCPU; Tafi; Thrombin activatable fibrinolysis inhibitor

Indexed keywords

CARBOXYPEPTIDASE; ENZYME INHIBITOR; ENZYME PRECURSOR; FIBRIN; LYSINE; PLASMIN; PLASMINOGEN; POTATO TUBER CARBOXYPEPTIDASE INHIBITOR; THROMBIN; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; UNCLASSIFIED DRUG;

EID: 80052437004     PISSN: 07209355     EISSN: None     Source Type: Journal    
DOI: 10.5482/ha-1155     Document Type: Review
Times cited : (28)

References (99)
  • 1
    • 84945736607 scopus 로고
    • Characterization of a carboxypeptidase in humanserum destinct from carboxypeptidase-N
    • Hendriks D, Scharpe S, Vansande M et al. Characterization of a carboxypeptidase in humanserum destinct from carboxypeptidase-N. J Clin Chem Clin Biochem 1989; 27: 277-285.
    • (1989) J Clin Chem Clin Biochem , vol.27 , pp. 277-285
    • Hendriks, D.1    Scharpe, S.2    Vansande, M.3
  • 2
    • 0024412863 scopus 로고
    • An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits
    • Campbell W, Okada H. An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits. Biochem Biophys Res Commun 1989; 162: 933-939.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 933-939
    • Campbell, W.1    Okada, H.2
  • 3
    • 0025748556 scopus 로고
    • Isolation, molecular-cloning, and partial characterization of a novel carboxypeptidase-B from human plasma
    • Eaton DL, Malloy BE, Tsai SP et al. Isolation, molecular-cloning, and partial characterization of a novel carboxypeptidase-B from human plasma. J Biol Chem 1991; 266: 21833-21838.
    • (1991) J Biol Chem , vol.266 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3
  • 4
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activatable fibrinolysis inhibitor
    • Bajzar L, Manuel R, Nesheim ME. 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.E.3
  • 5
    • 0028243478 scopus 로고
    • Characterization of a stable form of human meizothrombin derived from recombinant prothrombin (R155A, R271A and R284A)
    • Cote HCF, Stevens WK, Bajzar L et al. Characterization of a stable form of human meizothrombin derived from recombinant prothrombin (R155A, R271A and R284A). J Biol Chem 1994; 269: 11374-11380.
    • (1994) J Biol Chem , vol.269 , pp. 11374-11380
    • Cote, H.C.F.1    Stevens, W.K.2    Bajzar, L.3
  • 6
    • 0030589619 scopus 로고    scopus 로고
    • The gene for human carboxypeptidase U (CPU) - A proposed novel regulator of plasminogen activation - Maps to 13q14.11
    • Vanhoof G, Wauters J, Schatteman K et al. The gene for human carboxypeptidase U (CPU) - A proposed novel regulator of plasminogen activation - Maps to 13q14.11. Genomics 1996; 38: 454-455.
    • (1996) Genomics , vol.38 , pp. 454-455
    • Vanhoof, G.1    Wauters, J.2    Schatteman, K.3
  • 7
    • 0037177891 scopus 로고    scopus 로고
    • Identification and characterization of three members of the human metallocarboxypeptidase gene family
    • Wei SW, Segura S, Vendrell J et al. Identification and characterization of three members of the human metallocarboxypeptidase gene family. J Biol Chem 2002; 277: 14954-14964.
    • (2002) J Biol Chem , vol.277 , pp. 14954-14964
    • Wei, S.W.1    Segura, S.2    Vendrell, J.3
  • 8
    • 0036384505 scopus 로고    scopus 로고
    • Human procarboxypeptidase B: Three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)
    • Pereira PJB, Segura-Martin S, Oliva B et al. Human procarboxypeptidase B: Three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI). J Mol Biol 2002; 321: 537-547.
    • (2002) J Mol Biol , vol.321 , pp. 537-547
    • Pereira, P.J.B.1    Segura-Martin, S.2    Oliva, B.3
  • 9
    • 29744453508 scopus 로고    scopus 로고
    • Measurement of procarboxypeptidase U (TAFI) in human plasma: A laboratory challenge
    • Willemse JL, Hendriks DF. Measurement of procarboxypeptidase U (TAFI) in human plasma: A laboratory challenge. Clin Chem 2006; 52: 30-36.
    • (2006) Clin Chem , vol.52 , pp. 30-36
    • Willemse, J.L.1    Hendriks, D.F.2
  • 10
    • 0025718644 scopus 로고
    • Characterization of the binding of plasminogen to fibrin surfaces; the role of carboxy-terminal lysines
    • Fleury V, Anglescano E. Characterization of the binding of plasminogen to fibrin surfaces; the role of carboxy-terminal lysines. Biochemistry 1991; 30: 7630-7638.
    • (1991) Biochemistry , vol.30 , pp. 7630-7638
    • Fleury, V.1    Anglescano, E.2
  • 11
    • 0020472522 scopus 로고
    • Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin
    • Hoylaerts M, Rijken DC, Lijnen HR et al. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J Biol Chem 1982; 257: 2912-2919.
    • (1982) J Biol Chem , vol.257 , pp. 2912-2919
    • Hoylaerts, M.1    Rijken, D.C.2    Lijnen, H.R.3
  • 12
    • 0031915389 scopus 로고    scopus 로고
    • Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties
    • Boffa MB, Wang W, Bajzar L et al. Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties. J Biol Chem 1998; 273: 2127-2135.
    • (1998) J Biol Chem , vol.273 , pp. 2127-2135
    • Boffa, M.B.1    Wang, W.2    Bajzar, L.3
  • 13
    • 24944454291 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFla): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease
    • Leurs J, Hendriks D. Carboxypeptidase U (TAFla): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease. Thromb Haemost 2005; 94: 471-487.
    • (2005) Thromb Haemost , vol.94 , pp. 471-487
    • Leurs, J.1    Hendriks, D.2
  • 14
    • 3142579973 scopus 로고    scopus 로고
    • The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability
    • Walker JB, Bajzar L. The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability. J Biol Chem 2004; 279: 27896-27904.
    • (2004) J Biol Chem , vol.279 , pp. 27896-27904
    • Walker, J.B.1    Bajzar, L.2
  • 15
    • 3142584783 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism
    • Leurs J, Nerme V, Sim Y et al. Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism. J Thromb Haemost 2004; 2: 416-423.
    • (2004) J Thromb Haemost , vol.2 , pp. 416-423
    • Leurs, J.1    Nerme, V.2    Sim, Y.3
  • 16
    • 0028348825 scopus 로고
    • Procarboxypeptidase R cleaves bradykinin following activation
    • Shinohara T, Sakurada C, Suzuki T et al. Procarboxypeptidase R cleaves bradykinin following activation. Int Arch Allergy Immunol 1994; 103: 400-404.
    • (1994) Int Arch Allergy Immunol , vol.103 , pp. 400-404
    • Shinohara, T.1    Sakurada, C.2    Suzuki, T.3
  • 17
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell WD, Lazoura E, Okada N et al. Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiol Immunol 2002; 46: 131-134.
    • (2002) Microbiol Immunol , vol.46 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3
  • 18
    • 0345803939 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation
    • Myles T, Nishimura T, Yun TH et al. Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation. J Biol Chem 2003; 278: 51059-51067.
    • (2003) J Biol Chem , vol.278 , pp. 51059-51067
    • Myles, T.1    Nishimura, T.2    Yun, T.H.3
  • 19
    • 55949084990 scopus 로고    scopus 로고
    • Regulation of tissue inflammation by thrombi n-activatable carboxypeptidase B (or TAFI)
    • Leung LLK, Myles T, Nishimura T et al. Regulation of tissue inflammation by thrombi n-activatable carboxypeptidase B (or TAFI). Mol Immunol 2008; 45: 4080-4083.
    • (2008) Mol Immunol , vol.45 , pp. 4080-4083
    • Leung, L.L.K.1    Myles, T.2    Nishimura, T.3
  • 20
    • 33645451489 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor deficiency attenuates bleomycin-induced lung fibrosis
    • Fujimoto H, Gabazza EC, Taguchi O et al. Thrombin-activatable fibrinolysis inhibitor deficiency attenuates bleomycin-induced lung fibrosis. Am J Pathol 2006; 168: 1086-1096.
    • (2006) Am J Pathol , vol.168 , pp. 1086-1096
    • Fujimoto, H.1    Gabazza, E.C.2    Taguchi, O.3
  • 21
    • 77953779759 scopus 로고    scopus 로고
    • What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse?
    • Morser J, Gabazza EC, Myles T et al. What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse? J Thromb Haemost 2010; 8: 868-876.
    • (2010) J Thromb Haemost , vol.8 , pp. 868-876
    • Morser, J.1    Gabazza, E.C.2    Myles, T.3
  • 22
    • 0036843274 scopus 로고    scopus 로고
    • In vivo regulation of plasminogen function by plasma carboxypeptidase B
    • Swaisgood CM, Schmitt D, Eaton D et al. In vivo regulation of plasminogen function by plasma carboxypeptidase B. J Clin Invest 2002; 110: 1275-1282.
    • (2002) J Clin Invest , vol.110 , pp. 1275-1282
    • Swaisgood, C.M.1    Schmitt, D.2    Eaton, D.3
  • 23
    • 35148845916 scopus 로고    scopus 로고
    • TAFI and pancreatic carboxypeptidase B modulate in vitro capillary tube formation by human microvascular endothelial cells
    • Guimaraes AHC, Laurens N, Weijers EM et al. TAFI and pancreatic carboxypeptidase B modulate in vitro capillary tube formation by human microvascular endothelial cells. Arterioscler Thromb Vasc Biol 2007; 27: 2157-2162.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2157-2162
    • Guimaraes, A.H.C.1    Laurens, N.2    Weijers, E.M.3
  • 24
    • 0842311473 scopus 로고    scopus 로고
    • Impaired healing of cutaneous wounds and colonic anastomoses in mice lacking thrombin-activatable fibrinolysis inhibitor
    • te Velde EA, Wagenaar GTM, Reijerkerk A et al. Impaired healing of cutaneous wounds and colonic anastomoses in mice lacking thrombin-activatable fibrinolysis inhibitor. J Thromb Haemost 2003; 1: 2087-2096.
    • (2003) J Thromb Haemost , vol.1 , pp. 2087-2096
    • te Velde, E.A.1    Wagenaar, G.T.M.2    Reijerkerk, A.3
  • 25
    • 0026464017 scopus 로고
    • The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome13
    • Tsai SP, Drayna D. The gene encoding human plasma carboxypeptidase B (CPB2) resides on chromosome13. Genomics. 1992; 14: 549-550.
    • (1992) Genomics , vol.14 , pp. 549-550
    • Tsai, S.P.1    Drayna, D.2
  • 26
    • 38049153468 scopus 로고    scopus 로고
    • Effect of single nucleotide polymorphisms on expression of the gene encoding thrombin-activatable fibrinolysis inhibitor: a functional analysis
    • Boffa MB, Maret D, Hamill JD et al. Effect of single nucleotide polymorphisms on expression of the gene encoding thrombin-activatable fibrinolysis inhibitor: a functional analysis. Blood. 2008; 111: 183-189.
    • (2008) Blood , vol.111 , pp. 183-189
    • Boffa, M.B.1    Maret, D.2    Hamill, J.D.3
  • 27
    • 0035885942 scopus 로고    scopus 로고
    • A novel, possibly functional, single nucleotide polymorphism in the coding region of the thrombin-activatable fibrinolysis inhibitor (TAFI) gene is also associated with TAFI levels
    • Brouwers GJ, Vos HL, Leebeek FWG et al. A novel, possibly functional, single nucleotide polymorphism in the coding region of the thrombin-activatable fibrinolysis inhibitor (TAFI) gene is also associated with TAFI levels. Blood. 2001; 98: 1992-1993.
    • (2001) Blood , vol.98 , pp. 1992-1993
    • Brouwers, G.J.1    Vos, H.L.2    Leebeek, F.W.G.3
  • 28
    • 0035279930 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U)
    • Bouma BN, Marx PF, Mosnier LO et al. Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U). Thromb Res 2001; 101: 329-354.
    • (2001) Thromb Res , vol.101 , pp. 329-354
    • Bouma, B.N.1    Marx, P.F.2    Mosnier, L.O.3
  • 29
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar L, Nesheim ME, Tracy PB. The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood 1996; 88: 2093-2100.
    • (1996) Blood , vol.88 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 30
    • 0031775510 scopus 로고    scopus 로고
    • Plasma TAFI levels influence the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation
    • Mosnier LO, von dem Borne PAK, Meijers JCM et al. Plasma TAFI levels influence the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation. Thromb Haemost 1998; 80: 829-835.
    • (1998) Thromb Haemost , vol.80 , pp. 829-835
    • Mosnier, L.O.1    von dem Borne, P.A.K.2    Meijers, J.C.M.3
  • 31
    • 12444326201 scopus 로고    scopus 로고
    • Development of a genotype 325-specific proCPU/TAFI ELISA
    • Gils A, Alessi MC, Brouwers E et al. Development of a genotype 325-specific proCPU/TAFI ELISA. Arterioscler Thromb Vasc Biol 2003; 23: 1122-1127.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 1122-1127
    • Gils, A.1    Alessi, M.C.2    Brouwers, E.3
  • 32
    • 33748132990 scopus 로고    scopus 로고
    • Fine mapping of quantitative trait nucleotides underlying thrombin-activatable fibrinolysis inhibitor antigen levels by a transethnic study
    • Frere C, Tregouet DA, Morange PE et al. Fine mapping of quantitative trait nucleotides underlying thrombin-activatable fibrinolysis inhibitor antigen levels by a transethnic study. Blood. 2006; 108: 1562-1568.
    • (2006) Blood , vol.108 , pp. 1562-1568
    • Frere, C.1    Tregouet, D.A.2    Morange, P.E.3
  • 33
    • 78650926093 scopus 로고    scopus 로고
    • The role of thrombin activatable fibrinolysis inhibitor and factor XI in platelet-mediated fibrinolysis resistance: a thromboelastographic study in whole blood
    • Carrieri C, Galasso R, Semeraro F et al. The role of thrombin activatable fibrinolysis inhibitor and factor XI in platelet-mediated fibrinolysis resistance: a thromboelastographic study in whole blood. J Thromb Haemost 2011; 9: 154-162.
    • (2011) J Thromb Haemost , vol.9 , pp. 154-162
    • Carrieri, C.1    Galasso, R.2    Semeraro, F.3
  • 34
    • 0038454527 scopus 로고    scopus 로고
    • Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets
    • Mosnier LO, Buijtenhuijs P, Marx PF et al. Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets. Blood 2003; 101: 4844-4846.
    • (2003) Blood , vol.101 , pp. 4844-4846
    • Mosnier, L.O.1    Buijtenhuijs, P.2    Marx, P.F.3
  • 35
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombinthrombomodulin complex
    • Bajzar L, Morser J, Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombinthrombomodulin complex. J Biol Chem 1996; 271: 16603-16608.
    • (1996) J Biol Chem , vol.271 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 36
    • 0033521034 scopus 로고    scopus 로고
    • Characterization of plasmin-mediated activation of plasma procarboxypeptidase B - Modulation by glycosaminoglycans
    • Mao SS, Cooper CM, Wood T et al. Characterization of plasmin-mediated activation of plasma procarboxypeptidase B - Modulation by glycosaminoglycans. J Biol Chem 1999; 274: 35046-35052.
    • (1999) J Biol Chem , vol.274 , pp. 35046-35052
    • Mao, S.S.1    Cooper, C.M.2    Wood, T.3
  • 37
    • 36148996511 scopus 로고    scopus 로고
    • Thrombinthrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon
    • Binette TM, Taylor FB, Peer G et al. Thrombinthrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon. Blood 2007; 110: 3168-3175.
    • (2007) Blood , vol.110 , pp. 3168-3175
    • Binette, T.M.1    Taylor, F.B.2    Peer, G.3
  • 38
    • 79955960414 scopus 로고    scopus 로고
    • Evaluation of the profibrinolytic properties of an anti-TAFI monoclonal antibody in a mouse thromboembolism model
    • Vercauteren E, Emmerechts J, Peeters M et al. Evaluation of the profibrinolytic properties of an anti-TAFI monoclonal antibody in a mouse thromboembolism model. Blood 2011; 117: 4615-4622.
    • (2011) Blood , vol.117 , pp. 4615-4622
    • Vercauteren, E.1    Emmerechts, J.2    Peeters, M.3
  • 39
    • 79960069147 scopus 로고    scopus 로고
    • Identification and characterisation of monoclonal antibodies that impair the activation of human thrombin activatable fibrinolysis inhibitor through different mechanisms
    • DOI: 10.1160/TH10-08-0546
    • Mishra N, Vercauteren E, Develter J et al. Identification and characterisation of monoclonal antibodies that impair the activation of human thrombin activatable fibrinolysis inhibitor through different mechanisms. Thromb Haemost. 2011; 106: DOI: 10.1160/TH10-08-0546.
    • Thromb Haemost , vol.106 , pp. 106
    • Mishra, N.1    Vercauteren, E.2    Develter, J.3
  • 40
    • 0037059828 scopus 로고    scopus 로고
    • Two naturally occurring variants of TAFI (Thr-325 and Il-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme
    • Schneider M, Boffa M, Stewart R et al. Two naturally occurring variants of TAFI (Thr-325 and Il-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme. J Biol Chem 2002; 277: 1021-1030.
    • (2002) J Biol Chem , vol.277 , pp. 1021-1030
    • Schneider, M.1    Boffa, M.2    Stewart, R.3
  • 41
    • 33744920851 scopus 로고    scopus 로고
    • Generation of a stable activated thrombin activable fibrinolysis inhibitor variant
    • Ceresa E, Van de Borne K, Peeters M et al. Generation of a stable activated thrombin activable fibrinolysis inhibitor variant. J Biol Chem 2006; 281: 15878-15883.
    • (2006) J Biol Chem , vol.281 , pp. 15878-15883
    • Ceresa, E.1    Van de Borne, K.2    Peeters, M.3
  • 42
    • 33846444017 scopus 로고    scopus 로고
    • Announcing a TAFIa mutant with a 180-fold increased half-life and concomitantly a strongly increased antifibrinolytic potential
    • Ceresa E, Peeters M, Declerck PJ et al. Announcing a TAFIa mutant with a 180-fold increased half-life and concomitantly a strongly increased antifibrinolytic potential. J Thromb Haemost 2007; 5: 418-420.
    • (2007) J Thromb Haemost , vol.5 , pp. 418-420
    • Ceresa, E.1    Peeters, M.2    Declerck, P.J.3
  • 43
    • 33644952604 scopus 로고    scopus 로고
    • Limited mutagenesis increases the stability of human carboxypeptidase U (TAFIa) and demonstrates the importance of CPU stability over proCPU concentration in down-regulating fibrinolysis
    • Knecht W, Willemse J, Stenhamre H et al. Limited mutagenesis increases the stability of human carboxypeptidase U (TAFIa) and demonstrates the importance of CPU stability over proCPU concentration in down-regulating fibrinolysis. FEBS J 2006; 273: 778-792.
    • (2006) FEBS J , vol.273 , pp. 778-792
    • Knecht, W.1    Willemse, J.2    Stenhamre, H.3
  • 44
    • 0034725120 scopus 로고    scopus 로고
    • Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor
    • Boffa MB, Bell R, Stevens WK et al. Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 2000; 275: 12868-12878.
    • (2000) J Biol Chem , vol.275 , pp. 12868-12878
    • Boffa, M.B.1    Bell, R.2    Stevens, W.K.3
  • 45
    • 53449101060 scopus 로고    scopus 로고
    • Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation
    • Marx PF, Brondijk THC, Plug T et al. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation. Blood 2008; 112: 2803-2809.
    • (2008) Blood , vol.112 , pp. 2803-2809
    • Marx, P.F.1    Brondijk, T.H.C.2    Plug, T.3
  • 46
    • 0034725047 scopus 로고    scopus 로고
    • Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage
    • Marx PF, Hackeng TM, Dawson PE et al. Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. J Biol Chem 2000; 275: 12410-12415.
    • (2000) J Biol Chem , vol.275 , pp. 12410-12415
    • Marx, P.F.1    Hackeng, T.M.2    Dawson, P.E.3
  • 47
    • 1342346593 scopus 로고    scopus 로고
    • Generation and characterization of a highly stable form of activated thrombin-activable fibrinolysis inhibitor
    • Marx PF, Havik SR, Marquart JA et al. Generation and characterization of a highly stable form of activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 2004; 279: 6620-6628.
    • (2004) J Biol Chem , vol.279 , pp. 6620-6628
    • Marx, P.F.1    Havik, S.R.2    Marquart, J.A.3
  • 48
    • 77449151896 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy?
    • Willemse JL, Heylen E, Nesheim ME et al. Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy? J Thromb Haemost 2009; 7: 1962-1971.
    • (2009) J Thromb Haemost , vol.7 , pp. 1962-1971
    • Willemse, J.L.1    Heylen, E.2    Nesheim, M.E.3
  • 49
    • 0028222563 scopus 로고
    • Carboxypeptidase-U, a plasma carboxypeptidase with high-affinity for plasminogen
    • Wang W, Hendriks DF, Scharpe SS. Carboxypeptidase-U, a plasma carboxypeptidase with high-affinity for plasminogen. J Biol Chem 1994; 269: 15937-15944.
    • (1994) J Biol Chem , vol.269 , pp. 15937-15944
    • Wang, W.1    Hendriks, D.F.2    Scharpe, S.S.3
  • 50
    • 0036775320 scopus 로고    scopus 로고
    • Rational structure-based design of a novel carboxypeptidase R inhibitor
    • Lazoura E, Campbell W, Yamaguchi Y et al. Rational structure-based design of a novel carboxypeptidase R inhibitor. Chem Biol 2002; 9: 1129-1139.
    • (2002) Chem Biol , vol.9 , pp. 1129-1139
    • Lazoura, E.1    Campbell, W.2    Yamaguchi, Y.3
  • 51
    • 10744228937 scopus 로고    scopus 로고
    • Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics
    • Barrow JC, Nantermet PG, Stauffer SR et al. Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics. J Med Chem 2003; 46: 5294-5297.
    • (2003) J Med Chem , vol.46 , pp. 5294-5297
    • Barrow, J.C.1    Nantermet, P.G.2    Stauffer, S.R.3
  • 52
    • 10744221306 scopus 로고    scopus 로고
    • Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa)
    • Polla MO, Tottie L, Norden C et al. Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa). Bioorg Med Chem 2004; 12: 1151-1175.
    • (2004) Bioorg Med Chem , vol.12 , pp. 1151-1175
    • Polla, M.O.1    Tottie, L.2    Norden, C.3
  • 53
    • 20144381372 scopus 로고    scopus 로고
    • Inhibition of Thrombin Activatable Fibrinolysis Inhibitor by cysteine derivatives
    • Do YH, Gifford-Moore DS, Beight DW et al. Inhibition of Thrombin Activatable Fibrinolysis Inhibitor by cysteine derivatives. Thromb Res 2005; 116: 265-271.
    • (2005) Thromb Res , vol.116 , pp. 265-271
    • Do, Y.H.1    Gifford-Moore, D.S.2    Beight, D.W.3
  • 54
    • 37849034911 scopus 로고    scopus 로고
    • Discovery of potent & selective inhibitors of activated thrombinactivatable fibrinolysis inhibitor for the treatment of thrombosis
    • Bunnage ME, Blagg J, Steele J et al. Discovery of potent & selective inhibitors of activated thrombinactivatable fibrinolysis inhibitor for the treatment of thrombosis. J Med Chem 2007; 50: 6095-103.
    • (2007) J Med Chem , vol.50 , pp. 6095-6103
    • Bunnage, M.E.1    Blagg, J.2    Steele, J.3
  • 55
    • 33846907430 scopus 로고    scopus 로고
    • 3-Mercaptopropionic acids as efficacious inhibitors of activated thrombin activatable fibrinolysis inhibitor (TAFIa)
    • Islam I, Bryant J, Maya K et al. 3-Mercaptopropionic acids as efficacious inhibitors of activated thrombin activatable fibrinolysis inhibitor (TAFIa). Bioorg Med Chem Lett 2007; 17: 1349-1354.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 1349-1354
    • Islam, I.1    Bryant, J.2    Maya, K.3
  • 56
    • 33846975810 scopus 로고    scopus 로고
    • A novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor (TAFIa) - Part I: Pharmacological characterization
    • Wang YX, Zhao L, Nagashima M et al. A novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor (TAFIa) - Part I: Pharmacological characterization. Thromb Haemost 2007; 97: 45-53.
    • (2007) Thromb Haemost , vol.97 , pp. 45-53
    • Wang, Y.X.1    Zhao, L.2    Nagashima, M.3
  • 57
    • 67650470216 scopus 로고    scopus 로고
    • EF6265, a novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor, protects against sepsis-induced organ dysfunction in rats
    • Muto Y, Suzuki K, Iida H et al. EF6265, a novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor, protects against sepsis-induced organ dysfunction in rats. Crit Care Med 2009; 37: 1744-1749.
    • (2009) Crit Care Med , vol.37 , pp. 1744-1749
    • Muto, Y.1    Suzuki, K.2    Iida, H.3
  • 58
    • 0032484025 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis - Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization
    • Reverter D, Vendrell J, Canals F et al. A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis - Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization. J Biol Chem 1998; 273: 32927-32933.
    • (1998) J Biol Chem , vol.273 , pp. 32927-32933
    • Reverter, D.1    Vendrell, J.2    Canals, F.3
  • 59
    • 13544272567 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the tick Rhipicephalus bursa
    • Arolas JL, Lorenzo J, Rovira A et al. A carboxypeptidase inhibitor from the tick Rhipicephalus bursa. J Biol Chem 2005; 280: 3441-3448.
    • (2005) J Biol Chem , vol.280 , pp. 3441-3448
    • Arolas, J.L.1    Lorenzo, J.2    Rovira, A.3
  • 60
    • 0141484363 scopus 로고    scopus 로고
    • Reversible inhibitors of TAFIa can both promote and inhibit fibrinolysis
    • Schneider M, Nesheim M. Reversible inhibitors of TAFIa can both promote and inhibit fibrinolysis. J Thromb Haemost 2003; 1: 147-154.
    • (2003) J Thromb Haemost , vol.1 , pp. 147-154
    • Schneider, M.1    Nesheim, M.2
  • 61
    • 29244465865 scopus 로고    scopus 로고
    • Modulation of TAFI function through different pathways - implications for the development of TAFI inhibitors
    • Gils A, Ceresa E, Macovei AM et al. Modulation of TAFI function through different pathways - implications for the development of TAFI inhibitors. J Thromb Haemost 2005; 3: 2745-2753.
    • (2005) J Thromb Haemost , vol.3 , pp. 2745-2753
    • Gils, A.1    Ceresa, E.2    Macovei, A.M.3
  • 62
    • 54149105360 scopus 로고    scopus 로고
    • Discovery of novel mechanisms and molecular targets for the inhibition of activated thrombin activatable fibrinolysis inhibitor
    • Hillmayer K, Vancraenenbroeck R, De Maeyer M et al. Discovery of novel mechanisms and molecular targets for the inhibition of activated thrombin activatable fibrinolysis inhibitor. J Thromb Haemost 2008; 6: 1892-1899.
    • (2008) J Thromb Haemost , vol.6 , pp. 1892-1899
    • Hillmayer, K.1    Vancraenenbroeck, R.2    De Maeyer, M.3
  • 63
    • 77954477917 scopus 로고    scopus 로고
    • Generation and characterization of inhibitory nanobodies towards thrombin activatable fibrinolysis inhibitor
    • Buelens K, Hassanzadeh-Ghassabeh G, Muyldermans S et al. Generation and characterization of inhibitory nanobodies towards thrombin activatable fibrinolysis inhibitor. J Thromb Haemost 2010; 8: 1302-1312.
    • (2010) J Thromb Haemost , vol.8 , pp. 1302-1312
    • Buelens, K.1    Hassanzadeh-Ghassabeh, G.2    Muyldermans, S.3
  • 64
    • 33747165030 scopus 로고    scopus 로고
    • The intrinsic enzymatic activity of plasma procarboxypeptidase U (TAFI) can interfere with plasma carboxypeptidase N assays
    • Willemse JL, Polla M, Hendriks DF. The intrinsic enzymatic activity of plasma procarboxypeptidase U (TAFI) can interfere with plasma carboxypeptidase N assays. Anal Biochem 2006; 356: 157-159.
    • (2006) Anal Biochem , vol.356 , pp. 157-159
    • Willemse, J.L.1    Polla, M.2    Hendriks, D.F.3
  • 65
    • 34047264612 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase
    • Valnickova Z, Thogersen IB, Potempa J et al. Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase. J Biol Chem 2007; 282: 3066-3076.
    • (2007) J Biol Chem , vol.282 , pp. 3066-3076
    • Valnickova, Z.1    Thogersen, I.B.2    Potempa, J.3
  • 66
    • 34250176224 scopus 로고    scopus 로고
    • The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolysis rate: a rebuttal
    • Willemse JL, Heylen E, Hendriks DF. The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolysis rate: a rebuttal. J Thromb Haemost 2007; 5: 1334-1336.
    • (2007) J Thromb Haemost , vol.5 , pp. 1334-1336
    • Willemse, J.L.1    Heylen, E.2    Hendriks, D.F.3
  • 67
    • 44049087406 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis
    • Foley JH, Kim P, Nesheim ME. Thrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis. J Biol Chem 2008; 283: 8863-8867.
    • (2008) J Biol Chem , vol.283 , pp. 8863-8867
    • Foley, J.H.1    Kim, P.2    Nesheim, M.E.3
  • 68
    • 0037646413 scopus 로고    scopus 로고
    • Stabilization versus inhibition of TAFIa by competitive inhibitors in vitro
    • Walker JB, Hughes B, James I et al. Stabilization versus inhibition of TAFIa by competitive inhibitors in vitro. J Biol Chem 2003; 278: 8913-8921.
    • (2003) J Biol Chem , vol.278 , pp. 8913-8921
    • Walker, J.B.1    Hughes, B.2    James, I.3
  • 69
    • 57649223597 scopus 로고    scopus 로고
    • The crystal structure of thrombin-activable fibrinolysis inhibitor (TAFI) provides the structural basis for its intrinsic activity and the short half-life of TAFIa
    • Anand K, Pallares I, Valnickova Z et al. The crystal structure of thrombin-activable fibrinolysis inhibitor (TAFI) provides the structural basis for its intrinsic activity and the short half-life of TAFIa. J Biol Chem 2008; 283: 29416-29423.
    • (2008) J Biol Chem , vol.283 , pp. 29416-29423
    • Anand, K.1    Pallares, I.2    Valnickova, Z.3
  • 70
    • 0038691686 scopus 로고    scopus 로고
    • Electrochemiluminescence assay for basic carboxypeptidases: inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor
    • Mao SS, Colussi D, Bailey CM et al. Electrochemiluminescence assay for basic carboxypeptidases: inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor. Anal Biochem 2003; 319: 159-170.
    • (2003) Anal Biochem , vol.319 , pp. 159-170
    • Mao, S.S.1    Colussi, D.2    Bailey, C.M.3
  • 71
    • 49449087930 scopus 로고    scopus 로고
    • Structure of activated thrombin-activatable fibrinolysis inhibitor, a molecular link between coagulation and fibrinolysis
    • Sanglas L, Valnickova Z, Arolas JL et al. Structure of activated thrombin-activatable fibrinolysis inhibitor, a molecular link between coagulation and fibrinolysis. Mol Cell 2008; 31: 598-606.
    • (2008) Mol Cell , vol.31 , pp. 598-606
    • Sanglas, L.1    Valnickova, Z.2    Arolas, J.L.3
  • 72
    • 77953755642 scopus 로고    scopus 로고
    • Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor
    • Sanglas L, Arolas JL, Valnickova Z et al. Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor. J Thromb Haemost 2010; 8: 1056-1065.
    • (2010) J Thromb Haemost , vol.8 , pp. 1056-1065
    • Sanglas, L.1    Arolas, J.L.2    Valnickova, Z.3
  • 73
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • van Tilburg NH, Rosendaal FR, Bertina RM. Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood 2000; 95: 2855-2859.
    • (2000) Blood , vol.95 , pp. 2855-2859
    • van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 74
    • 0036797501 scopus 로고    scopus 로고
    • Co-segregation of thrombophilic disorders in factor V Leiden carriers; the contributions of factor VIII, factor XI, thrombin activatable fibrinolysis inhibitor and lipoprotein(a) to the absolute risk of venous thromboembolism
    • Libourel EJ, Bank I, Meinardi JR et al. Co-segregation of thrombophilic disorders in factor V Leiden carriers; the contributions of factor VIII, factor XI, thrombin activatable fibrinolysis inhibitor and lipoprotein(a) to the absolute risk of venous thromboembolism. Haematologica 2002; 87: 1068-1073.
    • (2002) Haematologica , vol.87 , pp. 1068-1073
    • Libourel, E.J.1    Bank, I.2    Meinardi, J.R.3
  • 75
    • 0033832483 scopus 로고    scopus 로고
    • Plasma Procarboxypeptidase U in Men with Symptomatic Coronary Artery Disease
    • Silveira A, Schatteman K, Goossens F et al. Plasma Procarboxypeptidase U in Men with Symptomatic Coronary Artery Disease. Thromb Haemost 2000; 84: 364-368.
    • (2000) Thromb Haemost , vol.84 , pp. 364-368
    • Silveira, A.1    Schatteman, K.2    Goossens, F.3
  • 76
    • 0347533966 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI): a novel predictor of angiographic coronary restenosis
    • Lau HK, Segev A, Hegele RA et al. Thrombin-activatable fibrinolysis inhibitor (TAFI): a novel predictor of angiographic coronary restenosis. Thromb Haemost 2003; 90: 1187-1191.
    • (2003) Thromb Haemost , vol.90 , pp. 1187-1191
    • Lau, H.K.1    Segev, A.2    Hegele, R.A.3
  • 77
    • 0037341621 scopus 로고    scopus 로고
    • Association between TAFI antigen and Ala 147Thr polymorphism of the TAFI gene and the angina pectoris incidence - The PRIME Study
    • Morange PE, Juhan-Vague I, Scarabin PY et al. Association between TAFI antigen and Ala 147Thr polymorphism of the TAFI gene and the angina pectoris incidence - The PRIME Study. Thromb Haemost 2003; 89: 554-560.
    • (2003) Thromb Haemost , vol.89 , pp. 554-560
    • Morange, P.E.1    Juhan-Vague, I.2    Scarabin, P.Y.3
  • 78
    • 1542297149 scopus 로고    scopus 로고
    • Very high TAFI antigen levels are associated with a lower risk of hard coronary events: the PRIME Study
    • Juhan-Vague I, Morange PE. Very high TAFI antigen levels are associated with a lower risk of hard coronary events: the PRIME Study. J Thromb Haemost 2003; 1: 2243-2244.
    • (2003) J Thromb Haemost , vol.1 , pp. 2243-2244
    • Juhan-Vague, I.1    Morange, P.E.2
  • 79
    • 0032992086 scopus 로고    scopus 로고
    • Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma
    • Schatteman KA, Goossens FJ, Scharpe SS et al. Assay of procarboxypeptidase U, a novel determinant of the fibrinolytic cascade, in human plasma. Clin Chem 1999; 45: 807-813.
    • (1999) Clin Chem , vol.45 , pp. 807-813
    • Schatteman, K.A.1    Goossens, F.J.2    Scharpe, S.S.3
  • 80
    • 0033813044 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor antigen levels and cardiovascular risk factors
    • Juhan-Vague I, Renucci JF, Grimaux M et al. Thrombin-activatable fibrinolysis inhibitor antigen levels and cardiovascular risk factors. Arterioscler Thromb Vasc Biol 2000; 20: 2156-2161.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 2156-2161
    • Juhan-Vague, I.1    Renucci, J.F.2    Grimaux, M.3
  • 81
    • 0035166273 scopus 로고    scopus 로고
    • Immunological assay for the determination of procarboxypeptidase U antigen levels in human plasma
    • Strömqvist M, Schatteman K, Leurs J et al. Immunological assay for the determination of procarboxypeptidase U antigen levels in human plasma. Thromb Haemost 2001; 85: 12-17.
    • (2001) Thromb Haemost , vol.85 , pp. 12-17
    • Strömqvist, M.1    Schatteman, K.2    Leurs, J.3
  • 82
    • 0037436061 scopus 로고    scopus 로고
    • Carboxypeptidase B inhibitors reduce tissue factor-induced renal microthrombi in rats
    • Muto Y, Suzuki K, Sato E et al. Carboxypeptidase B inhibitors reduce tissue factor-induced renal microthrombi in rats. Eur J Pharmacol 2003; 461: 181-189.
    • (2003) Eur J Pharmacol , vol.461 , pp. 181-189
    • Muto, Y.1    Suzuki, K.2    Sato, E.3
  • 83
    • 33644873097 scopus 로고    scopus 로고
    • Development of ELISAs measuring the extent of TAFI activation
    • Ceresa E, Brouwers E, Peeters M et al. Development of ELISAs measuring the extent of TAFI activation. Arterioscler Thromb Vasc Biol 2006; 26: 423-428.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 423-428
    • Ceresa, E.1    Brouwers, E.2    Peeters, M.3
  • 84
    • 57749176449 scopus 로고    scopus 로고
    • Activated thrombin activatable fibrinolysis inhibitor levels are associated with the risk of cardiovascular death in patients with coronary artery disease: the Athero-Gene study
    • Tregouet DA, Schnabel R, Alessi MC et al. Activated thrombin activatable fibrinolysis inhibitor levels are associated with the risk of cardiovascular death in patients with coronary artery disease: the Athero-Gene study. J Thromb Haemost 2009; 7: 49-57.
    • (2009) J Thromb Haemost , vol.7 , pp. 49-57
    • Tregouet, D.A.1    Schnabel, R.2    Alessi, M.C.3
  • 85
    • 34247275973 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor activation peptide shows association with all major subtypes of ischemic stroke and with TAFI gene variation
    • Ladenvall C, Gils A, Jood K et al. Thrombin activatable fibrinolysis inhibitor activation peptide shows association with all major subtypes of ischemic stroke and with TAFI gene variation. Arterioscler Thromb Vasc Biol 2007; 27: 955-962.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 955-962
    • Ladenvall, C.1    Gils, A.2    Jood, K.3
  • 86
    • 38549157626 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor is associated with severity and outcome of severe meningococcal infection in children
    • Emonts M, De Bruijne ELE, Guimaraes AHC et al. Thrombin activatable fibrinolysis inhibitor is associated with severity and outcome of severe meningococcal infection in children. J Thromb Haemost 2008; 6: 268-276.
    • (2008) J Thromb Haemost , vol.6 , pp. 268-276
    • Emonts, M.1    De Bruijne, E.L.E.2    Guimaraes, A.H.C.3
  • 87
    • 1642385045 scopus 로고    scopus 로고
    • TAFI: a promising drug target?
    • Zirlik A. TAFI: a promising drug target? Thromb Haemost 2004; 91: 420-422.
    • (2004) Thromb Haemost , vol.91 , pp. 420-422
    • Zirlik, A.1
  • 88
    • 79959539564 scopus 로고    scopus 로고
    • An update on the role of carboxypeptidase U (TAFIa) in fibrinolysis
    • Heylen E, Willemse J, Hendriks D. An update on the role of carboxypeptidase U (TAFIa) in fibrinolysis. Front Biosci 2011: 17: 2427-2450.
    • (2011) Front Biosci , vol.17 , pp. 2427-2450
    • Heylen, E.1    Willemse, J.2    Hendriks, D.3
  • 89
    • 0142209155 scopus 로고    scopus 로고
    • Thrombolysis: Newer thrombolytic agents and their role in clinical medicine
    • Nordt TK, Bode C. Thrombolysis: Newer thrombolytic agents and their role in clinical medicine. Heart 2003; 89: 1358-1362.
    • (2003) Heart , vol.89 , pp. 1358-1362
    • Nordt, T.K.1    Bode, C.2
  • 90
    • 0032877624 scopus 로고    scopus 로고
    • A novel approach to arterial thrombolysis
    • Klement P, Liao P, Bajzar L. A novel approach to arterial thrombolysis. Blood 1999; 94: 2735-2743.
    • (1999) Blood , vol.94 , pp. 2735-2743
    • Klement, P.1    Liao, P.2    Bajzar, L.3
  • 91
    • 0034657826 scopus 로고    scopus 로고
    • An inhibitor of activated thrombin-activatable fibrinolysis inhibitor potentiates tissue-type plasminogen activator-induced thrombolysis in a rabbit jugular vein thrombolysis model
    • Nagashima M, Werner M, Wang M et al. An inhibitor of activated thrombin-activatable fibrinolysis inhibitor potentiates tissue-type plasminogen activator-induced thrombolysis in a rabbit jugular vein thrombolysis model. Thromb Res 2000; 98: 333-342.
    • (2000) Thromb Res , vol.98 , pp. 333-342
    • Nagashima, M.1    Werner, M.2    Wang, M.3
  • 92
    • 11144356646 scopus 로고    scopus 로고
    • Enhancement of fibrinolysis by EF6265[(S)-7-amino-2-[[[(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl] methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B
    • Suzuki K, Muto Y, Fushihara K et al. Enhancement of fibrinolysis by EF6265[(S)-7-amino-2-[[[(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl] methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B. J Pharmacol Exp Ther 2004; 309: 607-615.
    • (2004) J Pharmacol Exp Ther , vol.309 , pp. 607-615
    • Suzuki, K.1    Muto, Y.2    Fushihara, K.3
  • 93
    • 0036143120 scopus 로고    scopus 로고
    • Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life
    • Nagashima M, Yin ZF, Zhao L 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 , pp. 101-110
    • Nagashima, M.1    Yin, Z.F.2    Zhao, L.3
  • 94
    • 33846951195 scopus 로고    scopus 로고
    • Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis
    • Wang XK, Smith PL, Hsu MY. 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.K.1    Smith, P.L.2    Hsu, M.Y.3
  • 95
    • 24044500304 scopus 로고    scopus 로고
    • Demonstration of enhanced endogenous fibrinolysis in thrombin activatable fibrinolysis inhibitor-deficient mice
    • Mao SS, Holahan MA, Bailey C et al. Demonstration of enhanced endogenous fibrinolysis in thrombin activatable fibrinolysis inhibitor-deficient mice. Blood Coagul Fibrinolysis 2005; 16: 407-415.
    • (2005) Blood Coagul Fibrinolysis , vol.16 , pp. 407-415
    • Mao, S.S.1    Holahan, M.A.2    Bailey, C.3
  • 96
    • 0031974703 scopus 로고    scopus 로고
    • Enhancement of rabbit jugular vein thrombolysis by neutralization of factor XI - In vivo evidence for a role of factor XI as an anti-fibrinolytic factor
    • Minnema MC, Friederich PW, Levi M et al. Enhancement of rabbit jugular vein thrombolysis by neutralization of factor XI - In vivo evidence for a role of factor XI as an anti-fibrinolytic factor. J Clin Invest 1998; 101: 10-14.
    • (1998) J Clin Invest , vol.101 , pp. 10-14
    • Minnema, M.C.1    Friederich, P.W.2    Levi, M.3
  • 97
    • 10544253848 scopus 로고    scopus 로고
    • Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma
    • Broze GJ, Higuchi DA. Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma. Blood 1996; 88: 3815-23.
    • (1996) Blood , vol.88 , pp. 3815-3823
    • Broze, G.J.1    Higuchi, D.A.2
  • 98
    • 0034757342 scopus 로고    scopus 로고
    • The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration
    • Mosnier LO, Lisman T, van den Berg HM et al. The defective down regulation of fibrinolysis in haemophilia A can be restored by increasing the TAFI plasma concentration. Thromb Haemost 2001; 86: 1035-1039.
    • (2001) Thromb Haemost , vol.86 , pp. 1035-1039
    • Mosnier, L.O.1    Lisman, T.2    van den Berg, H.M.3
  • 99
    • 0036090268 scopus 로고    scopus 로고
    • Inhibition of fibrinolysis by recombinant factor VIIA in plasma from patients with severe hemophilia A
    • Lisman T, Mosnier LO, Lambert T et al. Inhibition of fibrinolysis by recombinant factor VIIA in plasma from patients with severe hemophilia A. Blood 2002; 99: 175-179.
    • (2002) Blood , vol.99 , pp. 175-179
    • Lisman, T.1    Mosnier, L.O.2    Lambert, T.3


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