Michael B. Cable

TL;DR: The HCV NS5B apoenzyme structure reported here can accommodate a template:primer duplex without global conformational changes, supporting the hypothesis that this structure is essentially preserved during the reaction pathway.

TL;DR: In this paper, a resolution structure of the HCV helicase from the positive-stranded RNA hepatitis C virus reveals a molecule with distinct NTPase and RNA binding domains, and the structure supports a mechanism of helicase activity involving initial recognition of the requisite 3' singlestranded region on the nucleic acid substrate by a conserved arginine-rich sequence on the RNA binding domain.

TL;DR: Four mechanisms for the allosteric regulation of the calcium and magnesium ion activated adenosinetriphosphatase (Ca,Mg-ATPase) of sarcoplasmic reticulum were examined and negative cooperativity in substrate binding was not supported by 3H-labeled 5'-adenylyl methylenediphosphate (AMPPCP) binding.

TL;DR: Aminothiazole-based inhibitors designed for HCV polymerase display low micromolar potencies in biochemical assays and the composition of these compounds suggests that they may be interacting at a recently discovered allosteric site on the polymerase.