NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations

Journal of Biological Chemistry

Volumn 284, Issue 8, 2009, Pages 4806-4814

  Jennings, Thomas A ^a   Mackintosh, Samuel G ^a   Harrison, Melody K ^a   Sikora, Deniz ^a   Sikora, Bartek ^a   Dave, Bhuvanesh ^a   Tackett, Alan J ^a   Cameron, Craig E ^b   Raney, Kevin D ^a  

^a UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACCEPTOR MOLECULES; CONCENTRATION OF; DATA SUPPORT; DISSOCIATION CONSTANT; DNA BINDING ACTIVITY; DNA CONCENTRATION; DNA UNWINDING; DOMINANT NEGATIVE; DOUBLE STRANDED DNA; ENZYME CONCENTRATIONS; EQUILIBRIUM DISSOCIATION CONSTANT; FLUORESCENCE ANISOTROPY; FLUORESCENCE ENERGY TRANSFER; HELICASE; HEPATITIS C VIRUS; MONOMERIC FORMS; OLIGOMERIC STRUCTURE; RELATIVE CONCENTRATION; SPECIFIC ACTIVITY; SUBSTRATE CONCENTRATIONS;

CONCENTRATION (PROCESS); DISSOCIATION; DNA; ENERGY TRANSFER; ENZYMES; FLUORESCENCE; GENES; OLIGOMERIZATION; OLIGOMERS; OLIGONUCLEOTIDES; RNA;

NUCLEIC ACIDS;

HELICASE; HELICASE NS3; MONOMER; OLIGOMER; OLIGONUCLEOTIDE; UNCLASSIFIED DRUG; VIRUS DNA; DNA; DOUBLE STRANDED RNA; NS3 PROTEIN, HEPATITIS C VIRUS; RNA HELICASE; VIRUS PROTEIN;

ANISOTROPY; ARTICLE; DISSOCIATION CONSTANT; DNA BINDING; DNA DENATURATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEPATITIS C VIRUS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; AMINO ACID SUBSTITUTION; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MISSENSE MUTATION; PHYSIOLOGY; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

HEPATITIS C VIRUS;

AMINO ACID SUBSTITUTION; DNA; HEPACIVIRUS; MUTATION, MISSENSE; OLIGONUCLEOTIDES; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RNA HELICASES; RNA, DOUBLE-STRANDED; SUBSTRATE SPECIFICITY; VIRAL NONSTRUCTURAL PROTEINS;

EID: 64149127878     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M805540200     Document Type: Article

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