A macrocyclic HCV NS3/4A protease inhibitor interacts with protease and helicase residues in the complex with its full-length target.

@article{Schiering2011AMH,
  title={A macrocyclic HCV NS3/4A protease inhibitor interacts with protease and helicase residues in the complex with its full-length target.},
  author={Nikolaus Schiering and Allan D'arcy and Frederic Villard and Oliver Simic and Marion Kamke and Gaby Monnet and Ulrich Hassiepen and Dmitri I. Svergun and Ruth Pulfer and J{\"o}rg Eder and Prakash Raman and Ursula Bodendorf},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 52},
  pages={21052-6}
}
Hepatitis C virus (HCV) infection is a global health burden with over 170 million people infected worldwide. In a significant portion of patients chronic hepatitis C infection leads to serious liver diseases, including fibrosis, cirrhosis, and hepatocellular carcinoma. The HCV NS3 protein is essential for viral polyprotein processing and RNA replication and hence viral replication. It is composed of an N-terminal serine protease domain and a C-terminal helicase/NTPase domain. For full activity… CONTINUE READING
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