Willebrand factor interaction von - Cytoskeletal regulation of the platelet glycoprotein Ib/V/IX

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• Publication year

  2013

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  Biology, Medicine, Chemistry

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  Open on Semantic Scholar

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  Semantic Scholar

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• vivo wound (see comments) whole blood stimulated by thrombin, adenosine diphosphate, or an in Downregulation of the platelet surface glycoprotein Ib-IX complex in

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• The von Willebrand Factor-Glycoprotein Ib/V/IX Interaction Induces Actin Polymerization and Cytoskeletal Reorganization in Rolling Platelets and Glycoprotein Ib/V/IX-transfected Cells*

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  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
• von Willebrand factor-cleaving protease in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome.

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  1998cited by this paper
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• The cytoplasmic domain of glycoprotein (GP) Ibalpha constrains the lateral diffusion of the GP Ib-IX complex and modulates von Willebrand factor binding.

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• Identification of a Binding Sequence for the 14-3-3 Protein within the Cytoplasmic Domain of the Adhesion Receptor, Platelet Glycoprotein Ib (*)

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• Transmembrane Calcium Influx Associated with von Willebrand Factor Binding to GP Ib in the Initiation of Shear-Induced Platelet Aggregation

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• Elevated platelet count as a cause of abnormal von Willebrand factor multimer distribution in plasma.

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• Biochemical characterization of murine FcγRI

  1993cited by this paper
• Identification of a region in the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX complex that binds to purified actin-binding protein.

  1992cited by this paper
• Interaction of purified actin-binding protein with the platelet membrane glycoprotein Ib-IX complex.

  1991cited by this paper
• Downregulation of the platelet surface glycoprotein Ib-IX complex in whole blood stimulated by thrombin, adenosine diphosphate, or an in vivo wound.

  1991cited by this paper
• The role of von Willebrand factor and fibrinogen in platelet aggregation under varying shear stress.

  1991cited by this paper
• Thrombin induces a rapid redistribution of glycoprotein Ib-IX complexes within the membrane systems of activated human platelets

  1990cited by this paper
• Latrunculins--novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D.

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• Fibrinogen-independent platelet adhesion and thrombus formation on subendothelium mediated by glycoprotein IIb-IIIa complex at high shear rate.

  1989cited by this paper
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  1989cited by this paper
• Localization of the domain of actin-binding protein that binds to membrane glycoprotein Ib and actin in human platelets.

  1988cited by this paper
• The platelet membrane glycoprotein IIb-IIIa complex.

  1988cited by this paper
• Inducible secretion of large, biologically potent von Willebrand factor multimers.

  1986cited by this paper
• Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation.

  1986cited by this paper
• Linkage of a membrane skeleton to integral membrane glycoproteins in human platelets. Identification of one of the glycoproteins as glycoprotein Ib.

  1985cited by this paper
• Interaction of asialo von Willebrand factor with glycoprotein Ib induces fibrinogen binding to the glycoprotein IIb/IIIa complex and mediates platelet aggregation.

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• Asialo von Willebrand factor interactions with platelets. Interdependence of glycoproteins Ib and IIb/IIIa for binding and aggregation.

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• On the association of glycoprotein Ib and actin-binding protein in human platelets

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• Platelet-type von Willebrand's disease: characterization of a new bleeding disorder

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• An improved method for determining the actin filament content of nonmuscle cells by the DNase I inhibition assay.

  1981cited by this paper
• von Willebrand's disease antigen II. A new plasma and platelet antigen deficient in severe von Willebrand's disease.

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• Incorporation of fibrinogen into soluble fibrin complexes.

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• Studies on apyrases.

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• No citing papers are available for this paper.