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May 1, 1993Journal of Clinical InvestigationOpen Access

von Willebrand factor mutation enhancing interaction with platelets in patients with normal multimeric structure.

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Authors

LHLars HolmbergLinköping UniversityJDJudith DentMedical University of South CarolinaRSReinhard SchneppenheimBeiersdorf (Germany)

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Holmberg et al. (1993) studied this question.

synapsesocial.com/papers/6a70d828febe604dd7099e1fhttps://doi.org/10.1172/jci116443
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Also Consider

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

  1. 1Dimeric ristocetin flocculates proteins, binds to platelets, and mediates von Willebrand factor-dependent agglutination of platelets1991 · 133 citations
  2. 2An HphI‐polymorphism in exon 28 of the von Willebrand factor gene, and its frequency among patients with various forms of von Willebrand's disease1991 · 16 citations
  3. 3Type IIB von Willebrand factor with normal sialic acid content induces platelet aggregation in the absence of ristocetin. Role of platelet activation, fibrinogen, and two distinct membrane receptors.1987 · 47 citations
  4. 4Structure and Function of von Willebrand Factor1999 · 333 citations
  5. 5Molecular basis of human von Willebrand disease: analysis of platelet von Willebrand factor mRNA.1989 · 137 citations