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Plasma and recombinant thrombin-activatable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties
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Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme
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Schneider M, Boffa M, Stewart RJ, Rahman NL, Koschinsky ML, 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 2002; 277: 1021-30.
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Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism
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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
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Electrochemiluminescence assay for basic carboxypeptidases: Inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor
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Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI; a novel mechanism for enzyme auto-regulation
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Marx PF, Brondijk TH, Plug T, Romijn RA, Hemrika W, Meijers JC, Huizinga EG. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI; a novel mechanism for enzyme auto-regulation. Blood 2008; 112: 2803-9.
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The crystal structure of TAFI provides the structural basis for its intrinsic activity and the short half-life of TAFIa
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Anand K, Pallares I, Valnickova Z, Christensen T, Vendrell J, Wendt KU, Schreuder HA, Enghild JJ, Aviles FX. The crystal structure of TAFI provides the structural basis for its intrinsic activity and the short half-life of TAFIa. J Biol Chem 2008; 283: 29416-33.
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Biochemical importance of glycosylation in thrombin activatable fibrinolysis inhibitor
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Inactivation of activated thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage
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Characterization of mouse thrombin-activatable fibrinolysis inhibitor
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Marx PF, Wagenaar GTM, Reijerkerk A, Tiekstra MJ, Van Rossum AG, Gebbink MF, Meijers JC. Characterization of mouse thrombin-activatable fibrinolysis inhibitor. Thromb Haemost 2000; 83: 297-303.
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Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate
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Purification, characterization, and hydrodynamic properties of arginine kinase from gulf shrimp (Penaeus aztecus)
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Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins A and B
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Pahlman LI, Marx PF, Morgelin M, Lukomski S, Meijers JC, Herwald H. Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins A and B. J Biol Chem 2007; 282: 24873-81.
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Migration of the activation peptide of thrombin-activatable fibrinolysis inhibitor (TAFI) during SDS-polyacrylamide gel electrophoresis
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Guimaraes AH, Barrett-Bergshoeff MM, Gils A, Declerck PJ, Rijken DC. Migration of the activation peptide of thrombin-activatable fibrinolysis inhibitor (TAFI) during SDS-polyacrylamide gel electrophoresis. J Thromb Haemost 2004; 2: 780-4.
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