Can I read Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain on EtoBox?

Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain by Anja Johansson; Ina Hubatsch; Eva Åkerblom; Gunnar Lindeberg; Susanne Winiwarter; U.Helena Danielson; Anders Hallberg is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain about?

AbstractÐStructure±activity relationships (SARs) of product-based inhibitors of hepatitis C virus NS3 protease were evaluated using an in vitro assay system comprising the native bifunctional full-length NS3 (protease-helicase/NTPase). The results were compared to previously reported data derived from the corresponding NS3 protease domain assay. Shortening the length of the protease inhibitors from hexapeptides to tripeptides revealed that the decrease in potency was much less when determined in the assay system with the full-length NS3 protein. Disagreements in SARs at dierent positions (P5±P2) were also discovered. Taken together, the results suggest that the impact of the helicase domain upon protease inhibitor binding is substantial.

Who reads Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain?

Author

Anja Johansson; Ina Hubatsch; Eva Åkerblom; Gunnar Lindeberg; Susanne Winiwarter; U.Helena Danielson; Anders Hallberg

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0960-894X)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)