pubmed-article:7499328 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0043342 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0035668 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0036974 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0009264 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:7499328 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:7499328 | pubmed:issue | 47 | lld:pubmed |
pubmed-article:7499328 | pubmed:dateCreated | 1996-1-17 | lld:pubmed |
pubmed-article:7499328 | pubmed:abstractText | The Xenopus Y-box protein FRGY2 has a role in the translational silencing of masked maternal mRNA. Here, we determine that FRGY2 will recognize specific RNA sequences. The evolutionarily conserved nucleic acid-binding cold shock domain is required for sequence-specific interactions with RNA. However, RNA binding by FRGY2 is facilitated by N- and C-terminal regions flanking the cold shock domain. The hydrophilic C-terminal tail domain of FRGY2 interacts with RNA independent of the cold shock domain but does not determine sequence specificity. Thus, both sequence-specific and nonspecific RNA recognition domains are contained within the FRGY2 protein. | lld:pubmed |
pubmed-article:7499328 | pubmed:language | eng | lld:pubmed |
pubmed-article:7499328 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7499328 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7499328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7499328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7499328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7499328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7499328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7499328 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7499328 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7499328 | pubmed:month | Nov | lld:pubmed |
pubmed-article:7499328 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7499328 | pubmed:author | pubmed-author:MatsumotoKK | lld:pubmed |
pubmed-article:7499328 | pubmed:author | pubmed-author:BouvetPP | lld:pubmed |
pubmed-article:7499328 | pubmed:author | pubmed-author:WolffeA PAP | lld:pubmed |
pubmed-article:7499328 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7499328 | pubmed:day | 24 | lld:pubmed |
pubmed-article:7499328 | pubmed:volume | 270 | lld:pubmed |
pubmed-article:7499328 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7499328 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7499328 | pubmed:pagination | 28297-303 | lld:pubmed |
pubmed-article:7499328 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:7499328 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7499328 | pubmed:articleTitle | Sequence-specific RNA recognition by the Xenopus Y-box proteins. An essential role for the cold shock domain. | lld:pubmed |
pubmed-article:7499328 | pubmed:affiliation | Laboratory of Molecular Embryology, NICHID, National Institutes of Health, Bethesda, Maryland 20892-2710, USA. | lld:pubmed |
pubmed-article:7499328 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7499328 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:7499328 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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