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rdf:type |
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lifeskim:mentions |
|
|
pubmed:issue |
2
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pubmed:dateCreated |
1994-4-21
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pubmed:databankReference |
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pubmed:abstractText |
Putative cDNA clones for a nuclear antigen that cross-reacts with anti-human aldolase A monoclonal antibody MAb1A2 were isolated from the HeLa lambda gt11 cDNA library and a candidate clone (clone 3) was analyzed. The cDNA has an open reading frame (ORF) of 1,317 bp encoding a novel RNA helicase belonging to the DEAD RNA helicase family. The ORF also contains a nuclear targeting signal and the epitope for MAb1A2. The putative RNA helicase has sequence similarity to Escherichia coli RNA helicase DEAD, mouse translation factor eIF-4A, and human p68 and p54.
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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 |
Mar
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pubmed:issn |
0006-291X
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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 |
199
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
748-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8135819-Amino Acid Sequence,
pubmed-meshheading:8135819-Animals,
pubmed-meshheading:8135819-Base Sequence,
pubmed-meshheading:8135819-Cell Nucleus,
pubmed-meshheading:8135819-Cloning, Molecular,
pubmed-meshheading:8135819-DNA, Complementary,
pubmed-meshheading:8135819-Escherichia coli,
pubmed-meshheading:8135819-Eukaryotic Initiation Factor-4A,
pubmed-meshheading:8135819-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:8135819-Gene Library,
pubmed-meshheading:8135819-HeLa Cells,
pubmed-meshheading:8135819-Humans,
pubmed-meshheading:8135819-Mice,
pubmed-meshheading:8135819-Molecular Sequence Data,
pubmed-meshheading:8135819-Open Reading Frames,
pubmed-meshheading:8135819-Peptide Initiation Factors,
pubmed-meshheading:8135819-RNA Helicases,
pubmed-meshheading:8135819-RNA Nucleotidyltransferases,
pubmed-meshheading:8135819-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
A novel human homologue of a dead-box RNA helicase family.
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pubmed:affiliation |
Department of Biochemistry, Saga Medical School, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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