rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1998-4-13
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pubmed:abstractText |
The hepatitis G virus (HGV) is a new member of the Flaviviridae family and has a genomic organization similar to that of hepatitis C virus (HCV). Protein sequence motifs are present suggesting that HGV encodes a serine proteinase, an RNA-dependent RNA polymerase and a helicase. We have cloned and expressed the putative helicase of HGV and have shown that it contains a poly (U)-stimulated NTPase activity and is able to function as a DNA helicase. Preliminary characterization of the HGV helicase activity reveals similarities with other members of the Flaviviridae, but especially with HCV, raising the possibility that HGV could be used as a surrogate virus for the development of therapies against HCV.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1352-0504
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21-6
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:9493513-Adenosine Triphosphatases,
pubmed-meshheading:9493513-Adenosine Triphosphate,
pubmed-meshheading:9493513-Amino Acid Sequence,
pubmed-meshheading:9493513-Carrier Proteins,
pubmed-meshheading:9493513-Chromatography, Thin Layer,
pubmed-meshheading:9493513-Cloning, Molecular,
pubmed-meshheading:9493513-DNA,
pubmed-meshheading:9493513-DNA, Complementary,
pubmed-meshheading:9493513-DNA, Single-Stranded,
pubmed-meshheading:9493513-DNA Helicases,
pubmed-meshheading:9493513-Flaviviridae,
pubmed-meshheading:9493513-Gene Expression,
pubmed-meshheading:9493513-Hepacivirus,
pubmed-meshheading:9493513-Hepatitis, Viral, Human,
pubmed-meshheading:9493513-Humans,
pubmed-meshheading:9493513-Maltose-Binding Proteins,
pubmed-meshheading:9493513-Molecular Sequence Data,
pubmed-meshheading:9493513-Polymerase Chain Reaction,
pubmed-meshheading:9493513-RNA, Viral,
pubmed-meshheading:9493513-Recombinant Fusion Proteins,
pubmed-meshheading:9493513-Sequence Alignment,
pubmed-meshheading:9493513-Sequence Analysis, DNA
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pubmed:year |
1998
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pubmed:articleTitle |
Expression and characterization of the hepatitis G virus helicase.
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pubmed:affiliation |
Department of Virology, Roche Discovery Welwyn, Welwyn Garden City, Hertfordshire, UK.
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pubmed:publicationType |
Journal Article
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