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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1993-8-20
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pubmed:abstractText |
Most point substitutions in the highly-conserved 885-GDTDS motif of the HSV-1 DNA polymerase inactivate polymerase elongation activity. However, in an assay system based on expression by in vitro transcription-translation, the mutant GDTDA (S889A) possessed wild-type elongation activity which was highly resistant to phosphonoacetic acid and acyclovir triphosphate, but retained sensitivity to aphidicolin.
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pubmed:grant |
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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 |
Aug
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
195
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
831-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8337848-Amino Acid Sequence,
pubmed-meshheading:8337848-Antiviral Agents,
pubmed-meshheading:8337848-Base Sequence,
pubmed-meshheading:8337848-Cloning, Molecular,
pubmed-meshheading:8337848-Conserved Sequence,
pubmed-meshheading:8337848-DNA, Viral,
pubmed-meshheading:8337848-DNA-Directed DNA Polymerase,
pubmed-meshheading:8337848-Drug Resistance, Microbial,
pubmed-meshheading:8337848-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8337848-Exodeoxyribonucleases,
pubmed-meshheading:8337848-Molecular Sequence Data,
pubmed-meshheading:8337848-Mutagenesis, Site-Directed,
pubmed-meshheading:8337848-Point Mutation,
pubmed-meshheading:8337848-Viral Proteins
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pubmed:year |
1993
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pubmed:articleTitle |
Resistance to antiviral inhibitors caused by the mutation S889A in the highly-conserved 885-GDTDS motif of the herpes simplex virus type 1 DNA polymerase.
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pubmed:affiliation |
Division of Infectious Diseases, University of Connecticut Health Center, Farmington 06030.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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