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Structure of the catalytic domain of the hepatitis C virus NS2-3 protease

Author

Listed:
  • Ivo C. Lorenz

    (The Rockefeller University)

  • Joseph Marcotrigiano

    (The Rockefeller University)

  • Thomas G. Dentzer

    (The Rockefeller University)

  • Charles M. Rice

    (The Rockefeller University)

Abstract

Vaccine wanted Over 150 million people are infected with hepatitis C virus, there is no vaccine, and current therapies are not always effective. More efficient antivirals are much sought after, so the report of the crystal structure of the NS2 autoprotease of hepatitis C virus is a major advance. The structure, which reveals NS2 as a dimeric cysteine protease, will help in elucidating NS2's role in the viral life cycle, and it may aid the design of new drugs.

Suggested Citation

  • Ivo C. Lorenz & Joseph Marcotrigiano & Thomas G. Dentzer & Charles M. Rice, 2006. "Structure of the catalytic domain of the hepatitis C virus NS2-3 protease," Nature, Nature, vol. 442(7104), pages 831-835, August.
    • Handle: RePEc:nat:nature:v:442:y:2006:i:7104:d:10.1038_nature04975
    DOI: 10.1038/nature04975
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    Cited by:

    1. David A. Smith & Carlota Fernandez-Antunez & Andrea Magri & Rory Bowden & Nimisha Chaturvedi & Jacques Fellay & John McLauchlan & Graham R. Foster & William L. Irving & Peter Simmonds & Vincent Pederg, 2021. "Viral genome wide association study identifies novel hepatitis C virus polymorphisms associated with sofosbuvir treatment failure," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    2. Sonu Kumar & Boris I Ratnikov & Marat D Kazanov & Jeffrey W Smith & Piotr Cieplak, 2015. "CleavPredict: A Platform for Reasoning about Matrix Metalloproteinases Proteolytic Events," PLOS ONE, Public Library of Science, vol. 10(5), pages 1-19, May.

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