Identification of functionally important residues in TFPI Kunitz domain 3 required for the enhancement of its activity by protein S.

@article{Ahnstrm2012IdentificationOF,
  title={Identification of functionally important residues in TFPI Kunitz domain 3 required for the enhancement of its activity by protein S.},
  author={Josefin Ahnstr{\"o}m and Helena M. Andersson and Verity Hockey and Yiran Meng and Thomas J. Mckinnon and T. Hamuro and James T B Crawley and David A. Lane},
  journal={Blood},
  year={2012},
  volume={120 25},
  pages={
          5059-62
        }
}
Protein S is a cofactor for tissue factor pathway inhibitor (TFPI) that critically reduces the inhibition constant for FXa to below the plasma concentration of TFPI. TFPI Kunitz domain 3 is required for this enhancement to occur. To delineate the molecular mechanism underlying enhancement of TFPI function, in the present study, we produced a panel of Kunitz domain 3 variants of TFPI encompassing all 12 surface-exposed charged residues. Thrombin-generation assays in TFPI-depleted plasma… CONTINUE READING

Figures from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 16 CITATIONS

Factor V has an anticoagulant cofactor activity that targets the early phase of coagulation

  • The Journal of biological chemistry
  • 2017
VIEW 9 EXCERPTS
CITES BACKGROUND, METHODS & RESULTS
HIGHLY INFLUENCED

Amino acid residues in the laminin G domains of protein S involved in tissue factor pathway inhibitor interaction.

  • Thrombosis and haemostasis
  • 2015
VIEW 8 EXCERPTS
CITES RESULTS, METHODS & BACKGROUND
HIGHLY INFLUENCED

Discoveries of Serine Protease Inhibitors from Scorpions

Abdul Hakim, S Yang
  • 2016
VIEW 1 EXCERPT
CITES BACKGROUND

References

Publications referenced by this paper.
SHOWING 1-10 OF 15 REFERENCES

Similar Papers

Loading similar papers…