Licia Tomei

TL;DR: This superposition reveals the majority of the amino acid residues of the hepatitis C virus enzyme that are likely to be implicated in binding to the replicating RNA molecule and to the incoming NTP and suggests a rearrangement of the thumb domain as well as a possible concerted movement of thumb and fingertips during translocation of the RNA template-primer in successive polymerization rounds.

TL;DR: It is shown that the amino-terminal region of the HCV polyprotein is processed in vitro by cellular proteases releasing three structural proteins: p21 (core), gp37 (E1), and gp61 (E2), and implicate NS3 as a serine protease and demonstrate that a catalytically active NS3 is necessary for cleavage of the nonstructural region of HCV.

TL;DR: The data suggest that HCV NS4A may be the functional analog of flavivirus NS2B and pestivirus p10 proteins and thatNS4A can activate the NS3 protease when supplied in trans.

TL;DR: A systematic high-resolution X-ray crystallographic analysis of complexes of the hepatitis C virus (HCV) RNA polymerase with ribonucleoside triphosphates (rNTPs) and divalent metal ions strengthens the proposal that the two enzymes initiate replication de novo by similar mechanisms.

TL;DR: 2′-C-methyl-substituted ribonucleosides are efficient chain-terminating inhibitors of HCV genome replication and the combination of these agents with interferon-α results in synergistic inhibition of HCv genome replication in cell culture.