| pubmed-article:8344961 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8344961 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8344961 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:8344961 | lifeskim:mentions | umls-concept:C1307677 | lld:lifeskim |
| pubmed-article:8344961 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:8344961 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:8344961 | pubmed:dateCreated | 1993-9-7 | lld:pubmed |
| pubmed-article:8344961 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8344961 | pubmed:abstractText | RNA helicase A is an abundant nuclear enzyme of HeLa cells that unwinds double-stranded RNA in a 3' to 5'direction (Lee, C. G., and Hurwitz, J. (1992) J. Biol. Chem. 267, 4398-4407). A complementary DNA (cDNA) clone expressing RNA helicase A was isolated by screening a human cDNA library with polyclonal antibodies produced against the purified protein. The deduced amino acid sequence from this clone showed that RNA helicase A is a member of the DEAH family of proteins thought to be helicases. Sequence comparison among all known proteins of the DEAH family revealed that the highest homology was between RNA helicase A and the maleless protein (MLE) of Drosophila. There was 49% identity and 85% similarity throughout the overall primary sequences of both proteins, suggesting that RNA helicase A is the human counterpart of Drosophila MLE. Polyclonal antibodies against Drosophila MLE recognized RNA helicase A in crude nuclear extracts of HeLa cells as well as the purified protein. A recombinant RNA helicase A containing 6 histidine residues at the NH2 terminus was expressed in Sf9 cells using a baculovirus vector. The protein isolated from insect cells and the enzyme purified from HeLa cells exhibited identical RNA helicase and RNA-dependent ATPase activities. | lld:pubmed |
| pubmed-article:8344961 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8344961 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8344961 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8344961 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8344961 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8344961 | pubmed:author | pubmed-author:HurwitzJJ | lld:pubmed |
| pubmed-article:8344961 | pubmed:author | pubmed-author:LeeC GCG | lld:pubmed |
| pubmed-article:8344961 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8344961 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8344961 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8344961 | pubmed:geneSymbol | mle | lld:pubmed |
| pubmed-article:8344961 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8344961 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8344961 | pubmed:pagination | 16822-30 | lld:pubmed |
| pubmed-article:8344961 | pubmed:dateRevised | 2008-10-15 | lld:pubmed |
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| pubmed-article:8344961 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8344961 | pubmed:articleTitle | Human RNA helicase A is homologous to the maleless protein of Drosophila. | lld:pubmed |
| pubmed-article:8344961 | pubmed:affiliation | Graduate Program in Molecular Biology, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Institute, New York, New York 10021. | lld:pubmed |
| pubmed-article:8344961 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8344961 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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