Insights into thrombin activatable fibrinolysis inhibitor function and regulation

Author:

Foley J. H.1,Kim P. Y.2,Mutch N. J.3,Gils A.4

Affiliation:

1. Centre for Blood Research; University of British Columbia; Vancouver BC Canada

2. Thrombosis and Atherosclerosis Research Institute; McMaster University; Hamilton ON Canada

3. Institute of Medical Sciences; University of Aberdeen; Aberdeen UK

4. Laboratory for Therapeutic and Diagnostic Antibodies; KU Leuven; Leuven Belgium

Funder

Canadian Institutes of Health Research

British Heart Foundation Fellowship

Publisher

Wiley

Subject

Hematology

Reference114 articles.

1. Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N;Hendriks;J Clin Chem Clin Biochem,1989

2. An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits;Campbell;Biochem Biophys Res Commun,1989

3. Isolation, molecular-cloning, and partial characterization of a novel carboxypeptidase-B from human plasma;Eaton;J Biol Chem,1991

4. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor;Bajzar;J Biol Chem,1995

5. Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen;Wang;J Biol Chem,1994

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