Binding of von Willebrand factor to glycoproteins Ib and IIb/IIIa complex: affinity is related to multimeric size
Author:
Publisher
Wiley
Subject
Hematology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2141.1989.tb00226.x/fullpdf
Reference25 articles.
1. A murine monoclonal antibody that completely blocks the binding of fibrinogen to platelets produces a thrombasthenic-like state in normal platelets and binds to glycoproteins IIb and/or IIIa.
2. von Willebrand factor interaction with the glycoprotein IIb/IIa complex. Its role in platelet function as demonstrated in patients with congenital afibrinogenemia.
3. Carbohydrate moiety of von Willebrand factor is not necessary for maintaining multimeric structure and ristocetin cofactor activity but protects from proteolytic degradation.
4. Adhesive properties of the carbohydrate-modified von Willebrand factor (CHO-vWF)
5. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycoluril
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