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Volumn 31, Issue 4, 2008, Pages 598-606

Structure of Activated Thrombin-Activatable Fibrinolysis Inhibitor, a Molecular Link between Coagulation and Fibrinolysis

Author keywords

PROTEIN

Indexed keywords

HYDROLASE; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR;

EID: 49449087930     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2008.05.031     Document Type: Article
Times cited : (35)

References (57)
  • 1
    • 0027965043 scopus 로고
    • Latexin: a molecular marker for regional specification in the neocortex
    • Arimatsu Y. Latexin: a molecular marker for regional specification in the neocortex. Neurosci. Res. 20 (1994) 131-135
    • (1994) Neurosci. Res. , vol.20 , pp. 131-135
    • Arimatsu, Y.1
  • 2
    • 13544272567 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization
    • Arolas J.L., Lorenzo J., Rovira A., Castella J., Aviles F.X., and Sommerhoff C.P. A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: isolation, cDNA cloning, recombinant expression, and characterization. J. Biol. Chem. 280 (2005) 3441-3448
    • (2005) J. Biol. Chem. , vol.280 , pp. 3441-3448
    • Arolas, J.L.1    Lorenzo, J.2    Rovira, A.3    Castella, J.4    Aviles, F.X.5    Sommerhoff, C.P.6
  • 3
    • 20444446808 scopus 로고    scopus 로고
    • The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode
    • Arolas J.L., Popowicz G.M., Lorenzo J., Sommerhoff C.P., Huber R., Avilés F.X., and Holak T.A. The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode. J. Mol. Biol. 350 (2005) 489-498
    • (2005) J. Mol. Biol. , vol.350 , pp. 489-498
    • Arolas, J.L.1    Popowicz, G.M.2    Lorenzo, J.3    Sommerhoff, C.P.4    Huber, R.5    Avilés, F.X.6    Holak, T.A.7
  • 5
    • 84944033965 scopus 로고    scopus 로고
    • 240. Carboxypeptidase A
    • Barrett A.J., Rawlings N.D., and Woessner Jr. J.F. (Eds), Elsevier Academic Press, London
    • Auld D.S. 240. Carboxypeptidase A. In: Barrett A.J., Rawlings N.D., and Woessner Jr. J.F. (Eds). Handbook of proteolytic enzymes (2004), Elsevier Academic Press, London 812-821
    • (2004) Handbook of proteolytic enzymes , pp. 812-821
    • Auld, D.S.1
  • 6
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • Bajzar L., Manuel R., and Nesheim M.E. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J. Biol. Chem. 270 (1995) 14477-14484
    • (1995) J. Biol. Chem. , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 7
    • 49449103612 scopus 로고    scopus 로고
    • Bedaiwy, M., and Casper, R. (2006). Diagnosis and treatment of endometriosis. In World Intellectual Property Organization (International Bureau, Mount Sinai Hospital, Toronto, CA), November 9, 2006. Patent no. WO 2006/116873A1.
    • Bedaiwy, M., and Casper, R. (2006). Diagnosis and treatment of endometriosis. In World Intellectual Property Organization (International Bureau, Mount Sinai Hospital, Toronto, CA), November 9, 2006. Patent no. WO 2006/116873A1.
  • 8
    • 0020457447 scopus 로고
    • Mechanism of the anticoagulant action of heparin
    • Bjork I., and Lindahl U. Mechanism of the anticoagulant action of heparin. Mol. Cell. Biochem. 48 (1982) 161-182
    • (1982) Mol. Cell. Biochem. , vol.48 , pp. 161-182
    • Bjork, I.1    Lindahl, U.2
  • 9
    • 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 M.B., Wang W., Bajzar L., and Nesheim M.E. 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. 273 (1998) 2127-2135
    • (1998) J. Biol. Chem. , vol.273 , pp. 2127-2135
    • Boffa, M.B.1    Wang, W.2    Bajzar, L.3    Nesheim, M.E.4
  • 10
    • 0034725120 scopus 로고    scopus 로고
    • Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor
    • Boffa M.B., Bell R., Stevens W.K., and Nesheim M.E. Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. J. Biol. Chem. 275 (2000) 12868-12878
    • (2000) J. Biol. Chem. , vol.275 , pp. 12868-12878
    • Boffa, M.B.1    Bell, R.2    Stevens, W.K.3    Nesheim, M.E.4
  • 11
    • 0010090951 scopus 로고    scopus 로고
    • Thrombin activable fibrinolysis inhibitor (TAFI): molecular genetics of an emerging potential risk factor for thrombotic disorders
    • Boffa M.B., Nesheim M.E., and Koschinsky M.L. Thrombin activable fibrinolysis inhibitor (TAFI): molecular genetics of an emerging potential risk factor for thrombotic disorders. Curr. Drug Targets Cardiovasc. Haematol. Disord. 1 (2001) 59-74
    • (2001) Curr. Drug Targets Cardiovasc. Haematol. Disord. , vol.1 , pp. 59-74
    • Boffa, M.B.1    Nesheim, M.E.2    Koschinsky, M.L.3
  • 12
    • 33947585401 scopus 로고    scopus 로고
    • Curiouser and curiouser: recent advances in measurement of thrombin-activatable fibrinolysis inhibitor (TAFI) and in understanding its molecular genetics, gene regulation, and biological roles
    • Boffa M.B., and Koschinsky M.L. Curiouser and curiouser: recent advances in measurement of thrombin-activatable fibrinolysis inhibitor (TAFI) and in understanding its molecular genetics, gene regulation, and biological roles. Clin. Biochem. 40 (2007) 431-442
    • (2007) Clin. Biochem. , vol.40 , pp. 431-442
    • Boffa, M.B.1    Koschinsky, M.L.2
  • 13
    • 14044259258 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis
    • Bouma B.N., and Mosnier L.O. Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis. Pathophysiol. Haemost. Thromb. 33 (2003) 375-381
    • (2003) Pathophysiol. Haemost. Thromb. , vol.33 , pp. 375-381
    • Bouma, B.N.1    Mosnier, L.O.2
  • 14
    • 39449126006 scopus 로고    scopus 로고
    • Biochemical importance of glycosylation in thrombin activatable fibrinolysis inhibitor
    • Buelens K., Hillmayer K., Compernolle G., Declerck P.J., and Gils A. Biochemical importance of glycosylation in thrombin activatable fibrinolysis inhibitor. Circ. Res. 102 (2008) 295-301
    • (2008) Circ. Res. , vol.102 , pp. 295-301
    • Buelens, K.1    Hillmayer, K.2    Compernolle, G.3    Declerck, P.J.4    Gils, A.5
  • 15
    • 13244270050 scopus 로고    scopus 로고
    • Crystal structure of thrombin bound to heparin
    • Carter W.J., Cama E., and Huntington J.A. Crystal structure of thrombin bound to heparin. J. Biol. Chem. 280 (2005) 2745-2749
    • (2005) J. Biol. Chem. , vol.280 , pp. 2745-2749
    • Carter, W.J.1    Cama, E.2    Huntington, J.A.3
  • 16
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 17
  • 18
    • 34548840834 scopus 로고    scopus 로고
    • Comparative evaluation of stable TAFIa variants importance of alpha-helix 9 and beta-sheet 11 for TAFIa (in)stability
    • Ceresa E., De Maeyer M., Jonckheer A., Peeters M., Engelborghs Y., Declerck P.J., and Gils A. Comparative evaluation of stable TAFIa variants importance of alpha-helix 9 and beta-sheet 11 for TAFIa (in)stability. J. Thromb. Haemost. 5 (2007) 2105-2112
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 2105-2112
    • Ceresa, E.1    De Maeyer, M.2    Jonckheer, A.3    Peeters, M.4    Engelborghs, Y.5    Declerck, P.J.6    Gils, A.7
  • 19
    • 0025977159 scopus 로고
    • Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity
    • Coll M., Guasch A., Aviles F.X., and Huber R. Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity. EMBO J. 10 (1991) 1-9
    • (1991) EMBO J. , vol.10 , pp. 1-9
    • Coll, M.1    Guasch, A.2    Aviles, F.X.3    Huber, R.4
  • 21
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • Eaton D.L., Malloy B.E., Tsai S.P., Henzel W., and Drayna D. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem. 266 (1991) 21833-21838
    • (1991) J. Biol. Chem. , vol.266 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3    Henzel, W.4    Drayna, D.5
  • 22
    • 49449107950 scopus 로고    scopus 로고
    • Gabazza, E.C., Taguchi, O., Fujimoto, H., and Nagashima, M. (2006). TAFI inhibitors and their use to treat pulmonary fibrosis. In World Intellectual Property Organization (International Bureau, Schering AG, Berlin, Germany; Mie University Graduate School of Medicine, Mie, Japan; and Michael John Morser, San Francisco, CA, US), April 20, 2006. Patent no. WO 2006/041808 A2.
    • Gabazza, E.C., Taguchi, O., Fujimoto, H., and Nagashima, M. (2006). TAFI inhibitors and their use to treat pulmonary fibrosis. In World Intellectual Property Organization (International Bureau, Schering AG, Berlin, Germany; Mie University Graduate School of Medicine, Mie, Japan; and Michael John Morser, San Francisco, CA, US), April 20, 2006. Patent no. WO 2006/041808 A2.
  • 23
    • 84945736607 scopus 로고
    • Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N
    • Hendriks D., Scharpé S., van Sande M., and Lommaert M.P. Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N. J. Clin. Chem. Clin. Biochem. 27 (1989) 277-285
    • (1989) J. Clin. Chem. Clin. Biochem. , vol.27 , pp. 277-285
    • Hendriks, D.1    Scharpé, S.2    van Sande, M.3    Lommaert, M.P.4
  • 24
    • 33750079554 scopus 로고    scopus 로고
    • Characterization of rat thrombin-activatable fibrinolysis inhibitor (TAFI)-a comparative study assessing the biological equivalence of rat, murine and human TAFI
    • Hillmayer K., Macovei A., Pauwels D., Compernolle G., Declerck P.J., and Gils A. Characterization of rat thrombin-activatable fibrinolysis inhibitor (TAFI)-a comparative study assessing the biological equivalence of rat, murine and human TAFI. J. Thromb. Haemost. 4 (2006) 2470-2477
    • (2006) J. Thromb. Haemost. , vol.4 , pp. 2470-2477
    • Hillmayer, K.1    Macovei, A.2    Pauwels, D.3    Compernolle, G.4    Declerck, P.J.5    Gils, A.6
  • 25
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper N.M. Families of zinc metalloproteases. FEBS Lett. 354 (1994) 1-6
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 26
    • 49449101879 scopus 로고    scopus 로고
    • Hsu, M.-Y., Matsueda, G.R., and Tamura, J.K. (2007). Baboon TAFI polypeptides. March 13, 2007. U.S. patent 7189829 (United States, Bristol-Myers Squibb Company).
    • Hsu, M.-Y., Matsueda, G.R., and Tamura, J.K. (2007). Baboon TAFI polypeptides. March 13, 2007. U.S. patent 7189829 (United States, Bristol-Myers Squibb Company).
  • 27
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J., and Chothia C. The structure of protein-protein recognition sites. J. Biol. Chem. 265 (1990) 16027-16030
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 28
    • 0032877624 scopus 로고    scopus 로고
    • A novel approach to arterial thrombolysis
    • Klement P., Liao P., and Bajzar L. A novel approach to arterial thrombolysis. Blood 94 (1999) 2735-2743
    • (1999) Blood , vol.94 , pp. 2735-2743
    • Klement, P.1    Liao, P.2    Bajzar, L.3
  • 29
    • 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., Andersson M., Berntsson P., Furebring C., Harrysson A., Hager A.C., Wissing B.M., Hendriks D., and Cronet P. 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. 273 (2006) 778-792
    • (2006) FEBS J. , vol.273 , pp. 778-792
    • Knecht, W.1    Willemse, J.2    Stenhamre, H.3    Andersson, M.4    Berntsson, P.5    Furebring, C.6    Harrysson, A.7    Hager, A.C.8    Wissing, B.M.9    Hendriks, D.10    Cronet, P.11
  • 30
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 31
    • 0023924910 scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complexes
    • Mann K.G., Jenny R.J., and Krishnaswamy S. Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Annu. Rev. Biochem. 57 (1988) 915-956
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 32
    • 0033521034 scopus 로고    scopus 로고
    • Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans
    • Mao S.S., Cooper C.M., Wood T., Shafer J.A., and Gardell S.J. Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans. J. Biol. Chem. 274 (1999) 35046-35052
    • (1999) J. Biol. Chem. , vol.274 , pp. 35046-35052
    • Mao, S.S.1    Cooper, C.M.2    Wood, T.3    Shafer, J.A.4    Gardell, S.J.5
  • 33
    • 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 P.F., Hackeng T.M., Dawson P.E., Griffin J.H., Meijers J.C., and Bouma B.N. Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. J. Biol. Chem. 275 (2000) 12410-12415
    • (2000) J. Biol. Chem. , vol.275 , pp. 12410-12415
    • Marx, P.F.1    Hackeng, T.M.2    Dawson, P.E.3    Griffin, J.H.4    Meijers, J.C.5    Bouma, B.N.6
  • 34
    • 1342346593 scopus 로고    scopus 로고
    • Generation and characterization of a highly stable form of activated thrombin-activable fibrinolysis inhibitor
    • Marx P.F., Havik S.R., Marquart J.A., Bouma B.N., and Meijers J.C. Generation and characterization of a highly stable form of activated thrombin-activable fibrinolysis inhibitor. J. Biol. Chem. 279 (2004) 6620-6628
    • (2004) J. Biol. Chem. , vol.279 , pp. 6620-6628
    • Marx, P.F.1    Havik, S.R.2    Marquart, J.A.3    Bouma, B.N.4    Meijers, J.C.5
  • 35
    • 0033971420 scopus 로고    scopus 로고
    • A novel carboxypeptidase B that processes native β-amyloid precursor protein is present in human hippocampus
    • Matsumoto A., Itoh K., and Matsumoto R. A novel carboxypeptidase B that processes native β-amyloid precursor protein is present in human hippocampus. Eur. J. Neurosci. 12 (2000) 227-238
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 227-238
    • Matsumoto, A.1    Itoh, K.2    Matsumoto, R.3
  • 36
    • 0035000638 scopus 로고    scopus 로고
    • Human brain carboxypeptidase B, which cleaves β-amyloid peptides in vitro, is expressed in the endoplasmic reticulum of neurons
    • Matsumoto A., Itoh K., Seki T., Motozaki K., and Matsuyama S. Human brain carboxypeptidase B, which cleaves β-amyloid peptides in vitro, is expressed in the endoplasmic reticulum of neurons. Eur. J. Neurosci. 13 (2001) 1653-1657
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 1653-1657
    • Matsumoto, A.1    Itoh, K.2    Seki, T.3    Motozaki, K.4    Matsuyama, S.5
  • 37
    • 33750222459 scopus 로고    scopus 로고
    • Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis
    • Mosnier L.O., and Bouma B.N. Regulation of fibrinolysis by thrombin activatable fibrinolysis inhibitor, an unstable carboxypeptidase B that unites the pathways of coagulation and fibrinolysis. Arterioscler. Thromb. Vasc. Biol. 26 (2006) 2445-2453
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 2445-2453
    • Mosnier, L.O.1    Bouma, B.N.2
  • 38
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50 (1994) 157-163
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 39
    • 0029616569 scopus 로고
    • Purification, cDNA cloning, functional expression, and characterization of a 26-kDa endogenous mammalian carboxypeptidase inhibitor
    • Normant E., Martres M.P., Schwartz J.C., and Gros C. Purification, cDNA cloning, functional expression, and characterization of a 26-kDa endogenous mammalian carboxypeptidase inhibitor. Proc. Natl. Acad. Sci. USA 92 (1995) 12225-12229
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12225-12229
    • Normant, E.1    Martres, M.P.2    Schwartz, J.C.3    Gros, C.4
  • 42
    • 0020491126 scopus 로고
    • Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å resolution
    • Rees D.C., and Lipscomb W.N. Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å resolution. J. Mol. Biol. 160 (1982) 475-498
    • (1982) J. Mol. Biol. , vol.160 , pp. 475-498
    • Rees, D.C.1    Lipscomb, W.N.2
  • 45
    • 0037059828 scopus 로고    scopus 로고
    • Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme
    • Schneider M., Boffa M., Stewart R., Rahman M., Koschinsky M., and Nesheim M. Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme. J. Biol. Chem. 277 (2002) 1021-1030
    • (2002) J. Biol. Chem. , vol.277 , pp. 1021-1030
    • Schneider, M.1    Boffa, M.2    Stewart, R.3    Rahman, M.4    Koschinsky, M.5    Nesheim, M.6
  • 47
    • 49449118438 scopus 로고    scopus 로고
    • Taylor, F.B., and Bajzar, L. (2005). Treatment of sepsis with TAFI. January 4, 2005. U.S. patent US6,838,432B2 (USA, Oklahoma Medical Research Foundation, Oklahoma City, OK, US; and McMaster University, Hamilton, CA).
    • Taylor, F.B., and Bajzar, L. (2005). Treatment of sepsis with TAFI. January 4, 2005. U.S. patent US6,838,432B2 (USA, Oklahoma Medical Research Foundation, Oklahoma City, OK, US; and McMaster University, Hamilton, CA).
  • 48
    • 32244438306 scopus 로고    scopus 로고
    • Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation
    • Valnickova Z., Christensen T., Skottrup P., Thogersen I.B., Hojrup P., and Enghild J.J. Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation. Biochemistry 45 (2006) 1525-1535
    • (2006) Biochemistry , vol.45 , pp. 1525-1535
    • Valnickova, Z.1    Christensen, T.2    Skottrup, P.3    Thogersen, I.B.4    Hojrup, P.5    Enghild, J.J.6
  • 49
    • 34047264612 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase
    • Valnickova Z., Thogersen I.B., Potempa J., and Enghild J.J. Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase. J. Biol. Chem. 282 (2007) 3066-3076
    • (2007) J. Biol. Chem. , vol.282 , pp. 3066-3076
    • Valnickova, Z.1    Thogersen, I.B.2    Potempa, J.3    Enghild, J.J.4
  • 50
    • 0035073313 scopus 로고    scopus 로고
    • Low levels of thrombin activatable fibrinolysis inhibitor (TAFI) in patients with chronic liver disease
    • Van Thiel D.H., George M., and Fareed J. Low levels of thrombin activatable fibrinolysis inhibitor (TAFI) in patients with chronic liver disease. Thromb. Haemost. 85 (2001) 667-670
    • (2001) Thromb. Haemost. , vol.85 , pp. 667-670
    • Van Thiel, D.H.1    George, M.2    Fareed, J.3
  • 51
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • van Tilburg N.H., Rosendaal F.R., and Bertina R.M. Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood 95 (2000) 2855-2859
    • (2000) Blood , vol.95 , pp. 2855-2859
    • van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 52
    • 0034615567 scopus 로고    scopus 로고
    • Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties
    • Vendrell J., Querol E., and Avilés F.X. Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochim. Biophys. Acta 1477 (2000) 284-298
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 284-298
    • Vendrell, J.1    Querol, E.2    Avilés, F.X.3
  • 54
    • 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., and Schumacher W.A. Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis. J. Thromb. Thrombolysis 23 (2007) 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
  • 55
    • 34147159934 scopus 로고    scopus 로고
    • A role for procarboxypepidase U (TAFI) in thrombosis
    • Willemse J.L., and Hendriks D.F. A role for procarboxypepidase U (TAFI) in thrombosis. Front. Biosci. 12 (2007) 1973-1987
    • (2007) Front. Biosci. , vol.12 , pp. 1973-1987
    • Willemse, J.L.1    Hendriks, D.F.2
  • 56
    • 0019159024 scopus 로고
    • 2-antiplasmin
    • 2-antiplasmin. Biochem. J. 191 (1980) 229-232
    • (1980) Biochem. J. , vol.191 , pp. 229-232
    • Wiman, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.