Population
Recombinant full-length NS3 polypeptide of 67 kDa of hepatitis C virus expressed in Escherichia coli
Comparison
In vitro enzymatic assays vs Isolated N-terminal and C-terminal domains of NS3
Design
Preclinical
Authors
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Does not support changes to HCV protease inhibitor strategies; extends in vitro NS3 characterization but leaves open cellular relevance.
The full-length HCV NS3 protein retains multiple enzymatic activities comparable to its isolated domains, with RNA directly inhibiting its protease domain.
Gallinari et al. (1998) studied this question.
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