Stability of mutant serpin/furin complexes: dependence on pH and regulation at the deacylation step.

@article{Dufour2005StabilityOM,
  title={Stability of mutant serpin/furin complexes: dependence on pH and regulation at the deacylation step.},
  author={Erick K. Dufour and Antoine D{\'e}silets and Jean-Michel Longpr{\'e} and Richard Leduc},
  journal={Protein science : a publication of the Protein Society},
  year={2005},
  volume={14 2},
  pages={
          303-15
        }
}
Furin proteolytically cleaves a wide variety of proprotein substrates mainly within the trans-Golgi network (TGN) but also at the cell membrane and in endosomal compartments where pH is more acidic. Incorporation of furin recognition sequences within the reactive site loop (RSL) of alpha(1)-antitrypsin (AT) leads to the production of furin inhibitors. In an attempt to design more stable, potent, and specific serpin-based inhibitors, we constructed a series of AT and alpha(1)-antichymotrypsin… CONTINUE READING
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