| Autor: |
Frick DN; Department of Biochemistry & Molecular Biology, New York Medical College, Valhalla, NY, USA., Ginzburg O, Lam AM |
| Jazyk: |
angličtina |
| Zdroj: |
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2010; Vol. 587, pp. 223-33. |
| DOI: |
10.1007/978-1-60327-355-8_16 |
| Abstrakt: |
The hepatitis C virus NS3 protein contains an N-terminal serine protease and a C-terminal helicase that unwinds RNA or DNA duplexes. The HCV NS3 protein is the target for several antiviral drugs in clinical trials, which inhibit the protease function. A method is reported to simultaneously monitor the helicase and protease function of the NS3 protein in a single reaction using fluorescence spectroscopy and a single chain recombinant protein where NS3 is fused to its protease activator NS4A. The method monitors both activities together in real time and is amenable to high-throughput screening. This new procedure could be used to identify compounds that inhibit both the helicase and protease activity of NS3. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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