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rdf:type |
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lifeskim:mentions |
umls-concept:C0028953,
umls-concept:C0084378,
umls-concept:C0233820,
umls-concept:C0444626,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1513371,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1999230,
umls-concept:C2349209,
umls-concept:C2737044,
umls-concept:C2825311
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pubmed:issue |
1
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pubmed:dateCreated |
1998-4-16
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pubmed:abstractText |
Hepatitis C virus (HCV) represents a major health concern as it is responsible for a significant number of hepatitis cases worldwide. Much research has focused on the replicative enzymes of HCV as possible targets for more effective therapeutic agents. HCV NS3 helicase may provide one such suitable target. Helicases are enzymes which can unwind double-stranded regions of DNA or RNA in an ATP-dependent reaction. The structures of several helicases have been published but the structural details as to how ATP binding and hydrolysis are coupled to RNA unwinding are unknown.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
89-100
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pubmed:dateRevised |
2005-12-29
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pubmed:meshHeading |
pubmed-meshheading:9493270-Amino Acid Sequence,
pubmed-meshheading:9493270-Conserved Sequence,
pubmed-meshheading:9493270-Crystallography, X-Ray,
pubmed-meshheading:9493270-DNA, Single-Stranded,
pubmed-meshheading:9493270-Hepacivirus,
pubmed-meshheading:9493270-Models, Molecular,
pubmed-meshheading:9493270-Molecular Sequence Data,
pubmed-meshheading:9493270-Nucleic Acid Conformation,
pubmed-meshheading:9493270-Protein Conformation,
pubmed-meshheading:9493270-Protein Folding,
pubmed-meshheading:9493270-Protein Structure, Secondary,
pubmed-meshheading:9493270-RNA-Binding Proteins,
pubmed-meshheading:9493270-Sequence Alignment,
pubmed-meshheading:9493270-Viral Nonstructural Proteins,
pubmed-meshheading:9493270-Viral Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.
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pubmed:affiliation |
Vertex Pharmaceuticals Incorporated, Cambridge, Massachusetts 02139-4242, USA. jkim@vpharm.com caron@vpharm.com
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pubmed:publicationType |
Journal Article
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