Titlebook: Current Aspects of Blood Coagulation, Fibrinolysis, and Platelets; Ming-Ching Shen (Professor and Chairman),Che-Ming Conference proceedin

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https://doi.org/10.1007/978-3-030-05123-5d 7 days old, namely melena neonatorum which is rather mild, and whose incidence is one hundred times more than that of the late hemorrhagic disease [1, 4]. This disease is still seen because the immediate administration of VK after birth to newborns has not yet widely accepted because of the risk o

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Ming-Ching Shen (Professor and Chairman),Che-Ming

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Current Aspects of Blood Coagulation, Fibrinolysis, and Platelets978-4-431-68323-0

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Calcium Binding Properties of Vitamin K-Dependent Clotting Factorsommonly referred to as a procoagulant cascade. The final zymogen activation is the conversion of prothrombin to thrombin, the latter subsequently cleaving four peptide bonds in soluble fibrinogen, which becomes transformed into insoluble fibrin (1–4). The procoagulant cascade is regulated by an anti

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Recognition Sites for Thrombomodulin, Procoagulant and Anticoagulant Proteins around the Active Centactor V and platelets. When thrombin binds to thrombomodulin (TM), a receptor on the vascular endothelial cells [1,2], thrombin acts on the plasma anticoagulant protein C [1,3], thereby completely diminishing its ability to activate the procoagulant proteins [4–6]. On the mechanism of this conversio

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Heparin-Binding Site(S) of Antithrombin III, Histidine-Rich Glycoprotein and Activated Protein C with heparin. These include antithrombin III (ATIII), heparin cofactor II, protein C inhibitor, plasminogen activator inhibitor 1, tissue factor pathway inhibitor, histidine-rich glycoprotein (HRG), vitronectin, thrombospondin and platelet factor 4. In addition, recently, we found that activated pr

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The Cleavage of a Serine Protease Inhibitor at the Reactive Center by Its Target Protease: Analysis n plasma the activity of such proteases are controlled by specific inhibitors belonging to the serine protease inhibitor (SERPIN) family that forms stoichiometric tight complexes with the target proteases. The inhibitors of the SERPIN family are thought to have a common tertiary structure[1] with a

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