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February 15, 2001Blood

The arginine-552-cysteine (R1315C) mutation within the A1 loop of von Willebrand factor induces an abnormal folding with a loss of function resulting in type 2A–like phenotype of von Willebrand disease: study of 10 patients and mutated recombinant von Willebrand factor

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Authors

ARAnne‐Sophie RibbaCentre National de la Recherche ScientifiqueLHLysiane HilbertLFB (United States)JLJean‐Maurice LavergneInserm

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Cite This Study

Ribba et al. (2001) studied this question.

synapsesocial.com/papers/6a8b18dca42d46e0ffcaadd3https://doi.org/10.1182/blood.v97.4.952
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Ristocetin and Botrocetin Involve Two Distinct Domains of von Willebrand Factor for Binding to Platelet Membrane Glycoprotein lb1990 · 67 citations
  2. 2Epitope Mapping of Inhibitory Monoclonal Antibodies to Human von Willebrand Factor by Using Recombinant cDNA Libraries1994 · 39 citations
  3. 3Impaired intracellular transport produced by a subset of type IIA von Willebrand disease mutations.1992 · 233 citations
  4. 4Localization of von Willebrand Factor-binding Sites for Platelet Glycoprotein Ib and Botrocetin by Charged-to-Alanine Scanning Mutagenesis2000 · 73 citations
  5. 5Modeling and Functional Analysis of the Interaction between von Willebrand Factor A1 Domain and Glycoprotein Ibα2000 · 38 citations