| pubmed-article:8422685 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8422685 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8422685 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:8422685 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:8422685 | lifeskim:mentions | umls-concept:C1446409 | lld:lifeskim |
| pubmed-article:8422685 | lifeskim:mentions | umls-concept:C1156200 | lld:lifeskim |
| pubmed-article:8422685 | lifeskim:mentions | umls-concept:C0444454 | lld:lifeskim |
| pubmed-article:8422685 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8422685 | pubmed:dateCreated | 1993-2-24 | lld:pubmed |
| pubmed-article:8422685 | pubmed:abstractText | Acetylation of the N-terminal tails of the core histones directly facilitates the recognition by TFIIIA of the 5S RNA gene within model chromatin templates. This effect is independent of a reduction in the extent of histone-DNA interactions or a change in DNA helical repeat; it is also independent of whether a histone tetramer or octamer inhibits TFIIIA binding. Removal of the N-terminal tails from the core histones also facilitates the association of TFIIIA with nucleosomal templates. We suggest that the histone tails have a major role in restricting transcription factor access to DNA and that their acetylation releases this restriction by directing dissociation of the tails from DNA and/or inducing a change in DNA configuration on the histone core to allow transcription factor binding. Acetylation of core histones might be expected to exert a major influence on the accessibility of chromatin to regulatory molecules. | lld:pubmed |
| pubmed-article:8422685 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8422685 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8422685 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8422685 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8422685 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8422685 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:8422685 | pubmed:author | pubmed-author:HayesJ JJJ | lld:pubmed |
| pubmed-article:8422685 | pubmed:author | pubmed-author:LeeD YDY | lld:pubmed |
| pubmed-article:8422685 | pubmed:author | pubmed-author:WolffeA PAP | lld:pubmed |
| pubmed-article:8422685 | pubmed:author | pubmed-author:PrussDD | lld:pubmed |
| pubmed-article:8422685 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8422685 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8422685 | pubmed:volume | 72 | lld:pubmed |
| pubmed-article:8422685 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8422685 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8422685 | pubmed:pagination | 73-84 | lld:pubmed |
| pubmed-article:8422685 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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| pubmed-article:8422685 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8422685 | pubmed:articleTitle | A positive role for histone acetylation in transcription factor access to nucleosomal DNA. | lld:pubmed |
| pubmed-article:8422685 | pubmed:affiliation | Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:8422685 | pubmed:publicationType | Journal Article | lld:pubmed |
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