The Helicase from Hepatitis C Virus Is Active as an Oligomer
Open Access
- 1 November 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (45), 31839-31846
- https://doi.org/10.1074/jbc.274.45.31839
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Crystal Structures of Complexes of PcrA DNA Helicase with a DNA Substrate Indicate an Inchworm MechanismCell, 1999
- Staying on Track: Common Features of DNA Helicases and Microtubule MotorsCell, 1998
- Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super‐families of helicasesProtein Science, 1998
- Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwindingStructure, 1998
- The Protein Family of RNA HelicasesCritical Reviews in Biochemistry and Molecular Biology, 1998
- Asymmetric Interactions of Hexameric Bacteriophage T7 DNA Helicase with the 5′- and 3′-Tails of the Forked DNA SubstratePublished by Elsevier ,1997
- DNA Helicase Activity of the Hepatitis C Virus Nonstructural Protein 3European Journal of Biochemistry, 1997
- MECHANISMS OF HELICASE-CATALYZED DNA UNWINDINGAnnual Review of Biochemistry, 1996
- DNA helicases: Enzymes with essential roles in all aspects of DNA metabolismBioEssays, 1994
- Helicases: amino acid sequence comparisons and structure-function relationshipsCurrent Opinion in Structural Biology, 1993