The Protease Domain Increases the Translocation Stepping Efficiency of the Hepatitis C Virus NS3-4A Helicase

Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism

(2010) M. Gu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The NS4A Protein of Hepatitis C Virus Promotes RNA-Coupled ATP Hydrolysis by the NS3 Helicase

(2009) R. K. F. Beran et al.   JOURNAL OF VIROLOGY

Coupling of DNA unwinding to nucleotide hydrolysis in a ring-shaped helicase

(2008) Ilker Donmez et al.   EMBO JOURNAL

Hepatitis C Viral NS3-4A Protease Activity Is Enhanced by the NS3 Helicase

(2008) Rudolf K. F. Beran et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Establishing a Mechanistic Basis for the Large Kinetic Steps of the NS3 Helicase

(2008) Victor Serebrov et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Hepatitis C virus proteins interfere with the activation of chemokine gene promoters and downregulate chemokine gene expression

(2008) M. Sillanpaa et al.   JOURNAL OF GENERAL VIROLOGY

Non-hexameric DNA helicases and translocases: mechanisms and regulation

(2008) Timothy M. Lohman et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Two-state model for helicase translocation and unwinding of nucleic acids

(2008) Ashok Garai et al.   PHYSICAL REVIEW E