Factor IX oligomerization underlies reduced activity upon disruption of physiological conditions.

@article{Simhadri2014FactorIO,
  title={Factor IX oligomerization underlies reduced activity upon disruption of physiological conditions.},
  author={Vijaya Lakshmi Simhadri and Nobuko Hamasaki-Katagiri and Sandra Chang Tseng and Amber A. Bentley and Ran Zichel and Alon Y. Hershko and Anton A. Komar and Chava Kimchi-Sarfaty},
  journal={Haemophilia : the official journal of the World Federation of Hemophilia},
  year={2014},
  volume={20 2},
  pages={
          e157-63
        }
}
Coagulation factor IX (FIX) is a serine protease that plays a pivotal role in the blood coagulation cascade. FIX deficiency leads to a blood clotting disorder known as haemophilia B. FIX, synthesized as a prepro-peptide of 461 amino acids, is processed and secreted into plasma. The protein undergoes numerous modifications, including, but not limited to glycosylation, γ-carboxylation and disulphide bond formation. Upon processing and limited proteolysis, the protein is converted into an active… CONTINUE READING
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