(Q27748908)

2

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J P Griffith

3

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M D Dwyer

4

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J A Thomson

5

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M A Murcko

6

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C Lin

7

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P R Caron

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

8

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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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Genetic analysis of an NTP-binding motif in poliovirus polypeptide 2C

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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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Transmission of hepatitis C by intrahepatic inoculation with transcribed RNA

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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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The P-loop--a common motif in ATP- and GTP-binding proteins

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Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution

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Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp)

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Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

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Crystal structure of a yeast TBP/TATA-box complex

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Co-crystal structure of TBP recognizing the minor groove of a TATA element

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A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization.

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Mechanism of adenylate kinase. Demonstration of a functional relationship between aspartate 93 and Mg2+ by site-directed mutagenesis and proton, phosphorus-31, and magnesium-25 NMR.

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Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction

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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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The QRxGRxGRxxxG motif of the vaccinia virus DExH box RNA helicase NPH-II is required for ATP hydrolysis and RNA unwinding but not for RNA binding

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The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis

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Mutation of a highly conserved arginine in motif IV of Escherichia coli DNA helicase II results in an ATP-binding defect.

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Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase

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X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes

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Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7

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Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding

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

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Pestivirus NS3 (p80) protein possesses RNA helicase activity

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Resolution of phase ambiguity in macromolecular crystallography

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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