NS5B

TL;DR: These results provide the first clinical validation of an inhibitor of HCV NS5A, a protein with no known enzymatic function, as an approach to the suppression of virus replication that offers potential as part of a therapeutic regimen based on combinations ofHCV inhibitors.

TL;DR: The convenient and efficient screening and development of an on-chip viral protein inhibitor using a QDs-RNA oligonucleotide assay is achievable with high sensitivity and simplicity and is expected to be applicable toward the inhibitor screening of other types of diseases.

TL;DR: The results suggest α‐actinin may be a component of the HCV replication complex and studies of theHCV subgenomic replicon system with small interference RNA indicate that α‐actsinin is essential for HCV RNA replication.

TL;DR: All of the compounds had the potential to inhibit both the enzymes, indicating that the fullerene derivatives may be dual inhibitors against NS5B and NS3/4A and could be novel lead compounds for the treatment of HCV infections.

TL;DR: Affinity chromatography experiments and UV-crosslinking assays revealed that CSFV NS5A and NS5B bound its cognate 3'UTR and that NS5 A had higher affinity than NS5 B protein in binding to 3'utR, and competitive electrophoretic mobility shift assays indicated that binding ofCSFVNS5A to3'UTRSL-1 is more efficiently than to 3’UT RSL-2.