| pubmed-article:1327757 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C0525038 | lld:lifeskim |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C0178499 | lld:lifeskim |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:1327757 | lifeskim:mentions | umls-concept:C1626935 | lld:lifeskim |
| pubmed-article:1327757 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:1327757 | pubmed:dateCreated | 1992-11-19 | lld:pubmed |
| pubmed-article:1327757 | pubmed:abstractText | While all basic region/helix-loop-helix (bHLH) proteins bind the consensus CANNTG motif, other factors must be involved in determining regulatory specificity. In this report we show that bases outside this core 6 bp are involved in determining the specificity of binding. Thus, binding of the yeast bHLH protein PHO4, but not CPF-1, is inhibited by the presence of a T residue immediately 5' to their common CACGTG recognition sequence. PHO4 binding specificity is altered by mutation at any of three different positions in the basic region, including a single Glu to Asp substitution. The significance of these data for DNA-binding and transcription regulation by the bHLH family of transcription factors is discussed. | lld:pubmed |
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| pubmed-article:1327757 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1327757 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1327757 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1327757 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1327757 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1327757 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1327757 | pubmed:author | pubmed-author:FisherFF | lld:pubmed |
| pubmed-article:1327757 | pubmed:author | pubmed-author:GodingC RCR | lld:pubmed |
| pubmed-article:1327757 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1327757 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1327757 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1327757 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1327757 | pubmed:pagination | 4103-9 | lld:pubmed |
| pubmed-article:1327757 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1327757 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1327757 | pubmed:articleTitle | Single amino acid substitutions alter helix-loop-helix protein specificity for bases flanking the core CANNTG motif. | lld:pubmed |
| pubmed-article:1327757 | pubmed:affiliation | Marie Curie Research Institute, Oxted, Surrey, UK. | lld:pubmed |
| pubmed-article:1327757 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1327757 | pubmed:publicationType | Comparative Study | lld:pubmed |
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