| pubmed-article:19948260 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19948260 | lifeskim:mentions | umls-concept:C1516511 | lld:lifeskim |
| pubmed-article:19948260 | lifeskim:mentions | umls-concept:C0949596 | lld:lifeskim |
| pubmed-article:19948260 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:19948260 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19948260 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:19948260 | pubmed:dateCreated | 2010-2-3 | lld:pubmed |
| pubmed-article:19948260 | pubmed:abstractText | High mobility group nucleosome-binding (HMGN) proteins are architectural non-histone chromosomal proteins that bind to nucleosomes and modulate the structure and function of chromatin. The interaction of HMGN proteins with nucleosomes is dynamic and the proteins compete with the linker histone H1 chromatin-binding sites. HMGNs reduce the H1-mediated compaction of the chromatin fiber and facilitate the targeting of regulatory factors to chromatin. They modulate the cellular epigenetic profile, affect gene expression and impact the biological processes such as development and the cellular response to environmental and hormonal signals. Here we review the role of HMGN in chromatin structure, the link between HMGN proteins and histone modifications, and discuss the consequence of this link on nuclear processes and cellular phenotype. | lld:pubmed |
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| pubmed-article:19948260 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19948260 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19948260 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19948260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19948260 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19948260 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19948260 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:19948260 | pubmed:author | pubmed-author:BustinMichael... | lld:pubmed |
| pubmed-article:19948260 | pubmed:author | pubmed-author:PostnikovYuri... | lld:pubmed |
| pubmed-article:19948260 | pubmed:copyrightInfo | Published by Elsevier B.V. | lld:pubmed |
| pubmed-article:19948260 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19948260 | pubmed:volume | 1799 | lld:pubmed |
| pubmed-article:19948260 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19948260 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19948260 | pubmed:pagination | 62-8 | lld:pubmed |
| pubmed-article:19948260 | pubmed:dateRevised | 2011-9-29 | lld:pubmed |
| pubmed-article:19948260 | pubmed:meshHeading | pubmed-meshheading:19948260... | lld:pubmed |
| pubmed-article:19948260 | pubmed:meshHeading | pubmed-meshheading:19948260... | lld:pubmed |
| pubmed-article:19948260 | pubmed:meshHeading | pubmed-meshheading:19948260... | lld:pubmed |
