Lateral self-association of VWF involves the Cys2431-Cys2453 disulfide/dithiol in the C2 domain.

@article{Ganderton2011LateralSO,
  title={Lateral self-association of VWF involves the Cys2431-Cys2453 disulfide/dithiol in the C2 domain.},
  author={Tim Ganderton and Jason W. H. Wong and Christina Schroeder and Philip J Hogg},
  journal={Blood},
  year={2011},
  volume={118 19},
  pages={5312-8}
}
VWF is a plasma protein that binds platelets to an injured vascular wall during thrombosis. When exposed to the shear forces found in flowing blood, VWF molecules undergo lateral self-association that results in a meshwork of VWF fibers. Fiber formation has been shown to involve thiol/disulfide exchange between VWF molecules. A C-terminal fragment of VWF was expressed in mammalian cells and examined for unpaired cysteine thiols using tandem mass spectrometry (MS). The VWF C2 domain Cys2431… CONTINUE READING
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