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A new mutation, S1285F, within the A1 loop of von Willebrand factor induces a conformational change in A1 loop with abnormal binding to platelet GPIb and botrocetin causing type 2M von Willebrand disease.
Stepanian A, Ribba AS, Lavergne JM, Fressinaud E, Juhan-Vague I, Mazurier C, Girma JP, Meyer D. Stepanian A, et al. Among authors: fressinaud e. Br J Haematol. 2003 Feb;120(4):643-51. doi: 10.1046/j.1365-2141.2003.04168.x. Br J Haematol. 2003. PMID: 12588351 Free article.
Two novel mutations, Q1053H and C1060R, located in the D3 domain of von Willebrand factor, are responsible for decreased FVIII-binding capacity.
Hilbert L, Jorieux S, Proulle V, Favier R, Goudemand J, Parquet A, Meyer D, Fressinaud E, Mazurier C; INSERM Network on Molecular Abnormalities in von Willebrand Disease. Hilbert L, et al. Among authors: fressinaud e. Br J Haematol. 2003 Feb;120(4):627-32. doi: 10.1046/j.1365-2141.2003.04163.x. Br J Haematol. 2003. PMID: 12588349 Free article.
von Willebrand factor: structure and function.
Meyer D, Piétu G, Fressinaud E, Girma JP. Meyer D, et al. Among authors: fressinaud e. Mayo Clin Proc. 1991 May;66(5):516-23. doi: 10.1016/s0025-6196(12)62394-5. Mayo Clin Proc. 1991. PMID: 1903172 Review.
103 results