| pubmed-article:1622930 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1622930 | lifeskim:mentions | umls-concept:C0043342 | lld:lifeskim |
| pubmed-article:1622930 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1622930 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:1622930 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
| pubmed-article:1622930 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:1622930 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:1622930 | lifeskim:mentions | umls-concept:C0179400 | lld:lifeskim |
| pubmed-article:1622930 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1622930 | pubmed:dateCreated | 1992-8-7 | lld:pubmed |
| pubmed-article:1622930 | pubmed:abstractText | The Y box factors bind to a specific DNA sequence (the Y box, containing a reverse CCAAT element) and have been implicated in the regulation of transcription. We have used deletion mutagenesis to define the protein domains of two Xenopus Y box factors, FRG Y1 and FRG Y2, that are essential for DNA binding, multimerization, and transcription. A domain of the Y box factors homologous to an Escherichia coli cold shock protein is required for DNA binding. Both the E. coli protein and the Y box factors recognize DNA sequences with similar selectivity. The conserved region between these proteins does not contain any previously defined DNA-binding motifs. The hydrophilic C-terminal tail of the proteins contributes to the assembly of nucleoprotein complexes. This region contains an unusual pattern of basic and acidic amino acids and represents a new type of domain mediating protein-protein interactions in transcription factors. Both the DNA-binding and the multimerization domains are important for stimulating transcription from the Xenopus hsp70 promoter in vitro. | lld:pubmed |
| pubmed-article:1622930 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1622930 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1622930 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1622930 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1622930 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1622930 | pubmed:issn | 1043-4674 | lld:pubmed |
| pubmed-article:1622930 | pubmed:author | pubmed-author:WolffeA PAP | lld:pubmed |
| pubmed-article:1622930 | pubmed:author | pubmed-author:TafuriS RSR | lld:pubmed |
| pubmed-article:1622930 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1622930 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:1622930 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1622930 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1622930 | pubmed:pagination | 349-59 | lld:pubmed |
| pubmed-article:1622930 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:1622930 | pubmed:meshHeading | pubmed-meshheading:1622930-... | lld:pubmed |
| pubmed-article:1622930 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1622930 | pubmed:articleTitle | DNA binding, multimerization, and transcription stimulation by the Xenopus Y box proteins in vitro. | lld:pubmed |
| pubmed-article:1622930 | pubmed:affiliation | Laboratory of Molecular Embryology, NICHD, NIH, Bethesda, MD 20892. | lld:pubmed |
| pubmed-article:1622930 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1622930 | pubmed:publicationType | In Vitro | lld:pubmed |
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