Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein.

@article{Kenny1998NaturallyOM,
  title={Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein.},
  author={Dermot Kenny and {\'O}lafur G{\'i}sli J{\'o}nsson and Patricia A. Morateck and Robert R. Montgomery},
  journal={Blood},
  year={1998},
  volume={92 1},
  pages={175-83}
}
The platelet GPIb-V-IX complex is the receptor for the initial binding of von Willebrand factor (vWF) mediating platelet adhesion. The complex is composed of four membrane-spanning glycoproteins (GP): GPIbalpha, GPIbbeta, GPIX, and GPV. Bernard-Soulier syndrome results from a qualitative or quantitative defect in one or more components of the platelet membrane GPIb-V-IX complex. We describe the molecular basis of a novel Bernard-Soulier syndrome variant in two siblings in whom GPIbalpha was not… CONTINUE READING
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A point mutation in glycoprotein IX coding sequence (Cys 735TGT6 to Tyr5TAT6) causes impaired surface expression of GPIb/IX/V complex in two families with Bernard-Soulier syndrome

  • M Noda, K Fujimura, +9 authors M Sano
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