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Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor
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Some factor VIII (FVIII) inhibitors recognise a FVIII epitope(s) that is present only on FVIII-vWF complexes
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A novel cause of mild/moderate haemophilia A: Mutations scattered in the factor VIII C1 domain reduce factor VIII binding to von Willebrand factor
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9144271163
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Deletion of alanine 2201 in the FVIII C2 domain results in mild hemophilia A by impairing FVIII binding to VWF and phospholipids and destroys a major FVIII antigenic determinant involved in inhibitor development
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D'Oiron R, Lavergne JM, Lavend'homme R, Benhida A, Bordet JC, Negrier C, Peerlinck K, Vermylen J, Saint-Remy JM, Jacquemin M: Deletion of alanine 2201 in the FVIII C2 domain results in mild hemophilia A by impairing FVIII binding to VWF and phospholipids and destroys a major FVIII antigenic determinant involved in inhibitor development. Blood 2004; 103:155-157.
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Patients with severe von Willebrand disease are insensitive to the releasing effect of DDAVP: Evidence that the DDAVP-induced increase in plasma factor VIII is not secondary to the increase in plasma von Willebrand factor
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Cattaneo M, Simoni L, Gringeri A, Mannucci PM: Patients with severe von Willebrand disease are insensitive to the releasing effect of DDAVP: evidence that the DDAVP-induced increase in plasma factor VIII is not secondary to the increase in plasma von Willebrand factor. Br J Haematol 1994;86:333- 337.
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FVIII production by human lung microvascular endothelial cells
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Jacquemin M, Neyrinck A, Hermanns MI, Lavend'homme R, Rega F, Saint-Remy JM, Peerlinck K, Van Raemdonck D, Kirkpatrick CJ: FVIII production by human lung microvascular endothelial cells. Blood 2006;108: 515-517.
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Abnormal binding of factor V III is linked with the subst it ution of glutamine for arginine 91 in von Willebrand factor in a variant form of von Willebrand disease
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Kroner PA, Friedman KD, Fahs SA, Scott JP, Montgomery RR: Abnormal binding of factor V III is linked with the subst it ution of glutamine for arginine 91 in von Willebrand factor in a variant form of von Willebrand disease. J Biol Chem 1991;266:19146-19149.
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53→Trp causes von Willebrand disease Normandy by abolishing binding to factor VIII. Studies with recombinant von Willebrand factor
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The defective interaction between von Willebrand factor and factor VIII in a patient with type 1 von Willebrand disease is caused by substitution of Arg19 and His54 in mature von Willebrand factor
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A patient with type 2N von Willebrand disease is heterozygous for a new mutation: Gly22Glu. Demonstration of a defective expression of the second allele by the use of monoclonal antibodies
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Gu J, Jorieux S, Lavergne JM, Ruan C, Mazurier C, Meyer D: A patient with type 2N von Willebrand disease is heterozygous for a new mutation: Gly22Glu. Demonstration of a defective expression of the second allele by the use of monoclonal antibodies. Blood 1997; 89:3263-3269.
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0026557952
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A patient with von Willebrand's disease characterized by a compound heterozygosity for a substitution of Arg854 by Gln in the putative factor-VIII-binding domain of von Willebrand factor (vWF) on one allele and very low levels of mRNA from the second vWF allele
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Peerlinck K, Eikenboom JC, Ploos Van Amstel HK, Sangtawesin W, Arnout J, Reitsma PH, Vermylen J, Briët E: A patient with von Willebrand's disease characterized by a compound heterozygosity for a substitution of Arg854 by Gln in the putative factor-VIII-binding domain of von Willebrand factor (vWF) on one allele and very low levels of mRNA from the second vWF allele. Br J Haematol 1992; 80:358-363.
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Peerlinck K, Jacquemin MG, Arnout J, Hoylaerts MF, Gilles JG, Lavend'homme R, Johnson KM, Freson K, Scandella D, Saint-Remy JM, Vermylen J: Antifactor VIII antibody inhibiting allogeneic but not autologous factor VIII in patients with mild hemophilia A. Blood 1999;93:2267-2273.
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