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Volumn 41, Issue 32, 2002, Pages 10332-10342
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Hepatitis C virus NS3 ATPase/helicase: An ATP switch regulates the cooperativity among the different substrate binding sites
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Author keywords
[No Author keywords available]
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Indexed keywords
BINDING SITES;
ADENOSINETRIPHOSPHATE;
CHEMOTHERAPY;
CRYSTALLOGRAPHY;
ENZYMES;
NUCLEIC ACIDS;
VIRUSES;
ADENOSINE TRIPHOSPHATE;
DIMER;
HELICASE;
NS3 HELICASE;
NS3 PROTEASE;
NUCLEIC ACID;
PROTEINASE;
UNCLASSIFIED DRUG;
ARTICLE;
BINDING AFFINITY;
BINDING SITE;
ENZYME ACTIVITY;
ENZYME ANALYSIS;
ENZYME BINDING;
ENZYME CONFORMATION;
ENZYME KINETICS;
ENZYME SUBSTRATE COMPLEX;
HEPATITIS C VIRUS;
MODEL;
NONHUMAN;
PRIORITY JOURNAL;
REACTION ANALYSIS;
ADENOSINE TRIPHOSPHATASES;
ADENOSINE TRIPHOSPHATE;
BINDING SITES;
CROSS-LINKING REAGENTS;
DIMERIZATION;
DNA, SINGLE-STRANDED;
HEPACIVIRUS;
HYDROLYSIS;
KINETICS;
OLIGONUCLEOTIDES;
PROTEIN STRUCTURE, TERTIARY;
RNA HELICASES;
SERINE ENDOPEPTIDASES;
SPECTROPHOTOMETRY;
SUBSTRATE SPECIFICITY;
VIRAL NONSTRUCTURAL PROTEINS;
HEPATITIS C VIRUS;
RNA VIRUSES;
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EID: 0037072271
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi026082g Document Type: Article |
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Times cited : (33)
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References (19)
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