Substructure of human von Willebrand factor.

@article{Fowler1985SubstructureOH,
  title={Substructure of human von Willebrand factor.},
  author={Walter E. Fowler and Larry Fretto and Kimberly Hamilton and Harold P Erickson and Patrick A. McKee},
  journal={The Journal of clinical investigation},
  year={1985},
  volume={76 4},
  pages={1491-500}
}
Using electron microscopy, we have visualized the substructure of human von Willebrand factor (vWf) purified by two different approaches. vWf multimers, which appear as flexible strands varying in length up to 2 micron, consist of dimeric units (protomers) polymerized linearly in an end-to-end fashion through disulfide bonds. Examination of small multimers (e.g., one-mers, two-mers, and three-mers) suggests that each protomer consists of two large globular end domains (22 X 6.5 nm) connected to… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 56 extracted citations

Force sensing by the vascular protein von Willebrand factor is tuned by a strong intermonomer interaction.

Proceedings of the National Academy of Sciences of the United States of America • 2016

Similar Papers

Loading similar papers…