pubmed-article:11160883 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C2717841 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C1337104 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C2363291 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C0079686 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:11160883 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:11160883 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:11160883 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
pubmed-article:11160883 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:abstractText | We cloned cDNA encoding chicken cytoplasmic histone acetyltransferase-1, chHAT-1, comprising 408 amino acids including a putative initiation Met. It exhibits 80.4% identity to the human homolog and possesses a typical leucine zipper motif. The glutathione S:-transferase (GST) pull-down assay, involving truncated and missense mutants of the chicken chromatin assembly factor-1 (chCAF-1)p48, revealed not only that a region (comprising amino acids 376-405 of chCAF-1p48 and containing the seventh WD dipeptide motif) binds to chHAT-1 in vitro, but also that mutation of the motif has no influence on the in vitro interaction. The GST pull-down assay, involving truncated and missense chHAT-1 mutants, established that a region, comprising amino acids 380-408 of chHAT-1 and containing the leucine zipper motif, is required for its in vitro interaction with chCAF-1p48. In addition, mutation of each of four Leu residues in the leucine zipper motif prevents the in vitro interaction. The yeast two-hybrid assay revealed that all four Leu residues within the leucine zipper motif of chHAT-1 are necessary for its in vivo interaction with chCAF-1p48. These results indicate not only that the proper leucine zipper motif of chHAT-1 is essential for its interaction with chCAF-1p48, but also that the propeller structure of chCAF-1p48 expected to act as a platform for protein-protein interactions may not be necessary for this interaction of chHAT-1. | lld:pubmed |
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pubmed-article:11160883 | pubmed:language | eng | lld:pubmed |
pubmed-article:11160883 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11160883 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11160883 | pubmed:month | Feb | lld:pubmed |
pubmed-article:11160883 | pubmed:issn | 1362-4962 | lld:pubmed |
pubmed-article:11160883 | pubmed:author | pubmed-author:AhmadAA | lld:pubmed |
pubmed-article:11160883 | pubmed:author | pubmed-author:NakayamaTT | lld:pubmed |
pubmed-article:11160883 | pubmed:author | pubmed-author:TakamiYY | lld:pubmed |
pubmed-article:11160883 | pubmed:author | pubmed-author:NagamatsuNN | lld:pubmed |
pubmed-article:11160883 | pubmed:author | pubmed-author:KourikiHH | lld:pubmed |
pubmed-article:11160883 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:11160883 | pubmed:day | 1 | lld:pubmed |
pubmed-article:11160883 | pubmed:volume | 29 | lld:pubmed |
pubmed-article:11160883 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11160883 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11160883 | pubmed:pagination | 629-37 | lld:pubmed |
pubmed-article:11160883 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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