The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate

RKF Beran, V Serebrov, AM Pyle - Journal of Biological Chemistry, 2007 - ASBMB
Nonstructural (NS) protein 3 is a DEXH/D-box motor protein that is an essential component
of the hepatitis C viral (HCV) replicative complex. The full-length NS3 protein contains two
functional modules, both of which are essential in the life cycle of HCV: a serine protease
domain at the N terminus and an ATPase/helicase domain (NS3hel) at the C terminus.
Truncated NS3hel constructs have been studied extensively; the ATPase, nucleic acid
binding, and helicase activities have been examined and NS3hel has been used as a target …

The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate. VOLUME 282 (2007) PAGES 34913 …

RKF Beran, V Serebrov, AM Pyle - Journal of Biological Chemistry, 2008 - ASBMB
In this study, to block the degradation of the endocannabinoid 2-arachidonoylglycerol (2AG),
we used a compound (URB754) that had been previously claimed to be a selective inhibitor
of the 2AG-hydrolyzing enzyme monoacylglycerol lipase (MAGL)(Makara, JK, Mor, M.,
Fegley, D., Szabo, SI, Kathuria, S., Astarita, G., Duranti, A., Tontini, A., Tarzia, G., Rivara, S.,
Freund, TF, and Piomelli, D.(2005) Nat. Neurosci. 8, 1139–1141). However, recent reports
have raised concerns about the selectivity of URB754 (Vandevoorde, S., Jonsson, KO …
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