pubmed-article:9278474 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9278474 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:9278474 | lifeskim:mentions | umls-concept:C0035696 | lld:lifeskim |
pubmed-article:9278474 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:9278474 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
pubmed-article:9278474 | lifeskim:mentions | umls-concept:C0242494 | lld:lifeskim |
pubmed-article:9278474 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:9278474 | pubmed:dateCreated | 1997-10-17 | lld:pubmed |
pubmed-article:9278474 | pubmed:abstractText | The Elav-like proteins are specific mRNA binding proteins which are required for cellular differentiation. They contain three characteristic RNP2/RNP1-type RNA binding motifs. Previously we have shown that the first and second RNA binding domains bind to AU-rich elements in the 3'-UTR of mRNA. In this paper we show that the Elav-like proteins exhibit poly(A) binding activity. This activity is distinct from poly(A) binding activities that have been previously described. The Elav-like proteins specifically bind to long chain poly(A) tails. We have shown that the third RNA binding domain encompasses this poly(A) binding activity. Using poly(A)-Sepharose beads in a 'sandwich' assay we have shown that the Elav-like proteins can bind simultaneously to the AU-rich element and to the poly(A) tail. | lld:pubmed |
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pubmed-article:9278474 | pubmed:language | eng | lld:pubmed |
pubmed-article:9278474 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9278474 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9278474 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9278474 | pubmed:month | Sep | lld:pubmed |
pubmed-article:9278474 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:9278474 | pubmed:author | pubmed-author:ChungSS | lld:pubmed |
pubmed-article:9278474 | pubmed:author | pubmed-author:FurneauxHH | lld:pubmed |
pubmed-article:9278474 | pubmed:author | pubmed-author:MaW JWJ | lld:pubmed |
pubmed-article:9278474 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9278474 | pubmed:day | 15 | lld:pubmed |
pubmed-article:9278474 | pubmed:volume | 25 | lld:pubmed |
pubmed-article:9278474 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9278474 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9278474 | pubmed:pagination | 3564-9 | lld:pubmed |
pubmed-article:9278474 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
pubmed-article:9278474 | pubmed:meshHeading | pubmed-meshheading:9278474-... | lld:pubmed |
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pubmed-article:9278474 | pubmed:meshHeading | pubmed-meshheading:9278474-... | lld:pubmed |
pubmed-article:9278474 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9278474 | pubmed:articleTitle | The Elav-like proteins bind to AU-rich elements and to the poly(A) tail of mRNA. | lld:pubmed |
pubmed-article:9278474 | pubmed:affiliation | Program in Molecular Pharmacology and Therapeutics, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10021 USA. | lld:pubmed |
pubmed-article:9278474 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9278474 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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