Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding (Q27748908)

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J P Griffith

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M D Dwyer

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J A Thomson

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M A Murcko

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C Lin

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P R Caron

An amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4A

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publication date

15 January 1998

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published in

Structure

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volume

6

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issue

1

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page(s)

89-100

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cites work

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Hepatitis C virus-encoded nonstructural protein NS4A has versatile functions in viral protein processing

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Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide

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The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3)

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Expression, isolation, and characterization of the hepatitis C virus ATPase/RNA helicase

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A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain

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Polynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cells

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Characterization of RNA binding activity and RNA helicase activity of the hepatitis C virus NS3 protein

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Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase

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Hepatitis C virus shares amino acid sequence similarity with pestiviruses and flaviviruses as well as members of two plant virus supergroups

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The bovine papilloma virus E1 protein has ATPase activity essential to viral DNA replication and efficient transformation in cells

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Mechanisms of helicase-catalyzed DNA unwinding

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Structure of the hepatitis C virus RNA helicase domain

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Crystal structure of a DExx box DNA helicase

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Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP

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A point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 protein

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Hepatitis C virus NS3 serine proteinase: trans-cleavage requirements and processing kinetics

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