Article
Differential effects of the loss of intrachain- versus interchain-disulfide bonds in the cystine-knot domain of von Willebrand factor on the clinical phenotype of von Willebrand disease.
Thrombosis and haemostasis - 1 Dec 2006
Tjernberg Pernilla, Vos Hans L, Spaargaren-van Riel Caroline C, Luken Brenda M, Voorberg Jan, Bertina Rogier M, Eikenboom Jeroen C J
Abstract excerpt
Von Willebrand factor (VWF) contains a large number of cysteine residues, which all form disulfide bonds. Mutations of cysteines located in the cystine-knot (CK) domain of VWF have been identified in both qualitative type 2A (IID) and quantitative type 3 von Willebrand disease (VWD). Our objective was to test the hypothesis that the difference in phenotype is related to whether the mutated cysteine residue is...
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