The Role of the Second Growth-Factor Domain of Human Factor IXa in Binding to Platelets and in Factor-X Activation

Biochemical Journal- United Kingdom

doi 10.1042/bj3100427

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September 1, 1995

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Portland Press Ltd.

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The Role of the Second Growth-Factor Domain of Human Factor IXa in Binding to Platelets and in Factor-X Activation

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Platelet Receptor-Mediated Factor X Activation by Factor IXa. High-Affinity Factor IXa Receptors Induced by Factor VIII Are Deficient on Platelets in Scott Syndrome.

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The Role of the Second Growth-Factor Domain of Human Factor IXa in Binding to Platelets and in Factor-X Activation

Biochemical Journal- United Kingdom

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

The Role of the Second Growth-Factor Domain of Human Factor IXa in Binding to Platelets and in Factor-X Activation

Platelet Receptor-Mediated Factor X Activation by Factor IXa. High-Affinity Factor IXa Receptors Induced by Factor VIII Are Deficient on Platelets in Scott Syndrome.

Protease and EGF1 Domains of Factor IXa Play Distinct Roles in Binding to Factor VIIIa

Ca2+Binding to the First Epidermal Growth Factor-Like Domain of Human Blood Coagulation Factor IX Promotes Enzyme Activity and Factor VIII Light Chain Binding

Characterization of the Clotting Activities of Structurally Different Forms of Activated Factor IX. Enzymatic Properties of Normal Human Factor IXa Alpha, Factor IXa Beta, and Activated Factor IX Chapel Hill.

Lipid Specificity of the Membrane Binding Domain of Coagulation Factor X

Suppression of the Biological Activities of the Epidermal Growth Factor (EGF)-like Domain by the Heparin-Binding Domain of Heparin-Binding EGF-like Growth Factor

Lysophosphatidylcholine Increases Expression of Heparin-Binding Epidermal Growth Factor Like Growth Factor in Human T Lymphocytes

Nerve Growth Factor- And Epidermal Growth Factor-Stimulated Translocation of the ADP-ribosylation Factor-Exchange Factor GRP1 to the Plasma Membrane of PC12 Cells Requires Activation of Phosphatidylinositol 3-Kinase and the GRP1 Pleckstrin Homology Domain