M
Michael E. Nesheim
Researcher at Queen's University
Publications - 153
Citations - 11775
Michael E. Nesheim is an academic researcher from Queen's University. The author has contributed to research in topics: Thrombin & Prothrombinase. The author has an hindex of 57, co-authored 153 publications receiving 11494 citations. Previous affiliations of Michael E. Nesheim include Mayo Clinic & University of Vermont.
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Surface-dependent reactions of the vitamin K-dependent enzyme complexes
TL;DR: It is concluded that factor VII is most likely a zymogen, just as are the other proenzymes of the blood clotting process, and the kinetic constants obtained for the various coagulation reactions determined in vitro provide some insights into how these pathways may function in vivo.
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Purification and Characterization of TAFI, a Thrombin-activable Fibrinolysis Inhibitor
TL;DR: 2-Guanidinoethylmercaptosuccinic acid, a competitive inhibitor of CPB, completely inhibits prolongation of lysis by activated TAFI in a purified system and the prolongation induced by II activation in barium-adsorbed plasma, suggesting that TAFi accounts for the antifibrinolytic effect that accompanies prothrombin activation.
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TAFI, or Plasma Procarboxypeptidase B, Couples the Coagulation and Fibrinolytic Cascades through the Thrombin-Thrombomodulin Complex
TL;DR: TAFI in vitro and possibly in vivo defines an explicit molecular connection between the coagulation and fibrinolytic cascades, such that expression of activity in the former down-regulates the activity of the latter.
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The contribution of bovine Factor V and Factor Va to the activity of prothrombinase.
TL;DR: The present data indicate that the model prothrombinase described in this paper consists of a phospholipid-bound, stoichiometric complex of Factor Va and Factor Xa, with bound Factor Va serving as the "binding site" for Factor V, in concert with its proposed role in platelets.
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A Study of the Mechanism of Inhibition of Fibrinolysis by Activated Thrombin-activable Fibrinolysis Inhibitor
TL;DR: It is concluded that TAFIa suppresses fibrinolysis by removing COOH-terminal lysine and arginine residues from fibrin, thereby reducing its cofactor functions in both plasminogen activation and the positive feedback conversion of Glu-plAsminogen to Lys-plasmineogen.