| pubmed-article:20836566 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20836566 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:20836566 | lifeskim:mentions | umls-concept:C0019652 | lld:lifeskim |
| pubmed-article:20836566 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:20836566 | lifeskim:mentions | umls-concept:C0220922 | lld:lifeskim |
| pubmed-article:20836566 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:20836566 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:20836566 | pubmed:dateCreated | 2010-11-5 | lld:pubmed |
| pubmed-article:20836566 | pubmed:abstractText | An important issue in epigenetic research is to understand how the numerous methylation marks associated with histone and certain nonhistone proteins are recognized and interpreted by the hundreds of chromatin-binding modules (CBMs) in a cell to control chromatin state, gene expression, and other cellular functions. We have assembled a peptide chip that represents known and putative lysine methylation marks on histones and p53 and probed the chip for binding to a group of CBMs to obtain a comprehensive interaction network mediated by lysine methylation. Interactions revealed by the peptide array screening were validated by in-solution binding assays. This study not only recapitulated known interactions but also uncovered new ones. A novel heterochromatin protein 1 beta (HP1?) chromodomain-binding site on histone H3, H3K23me, was discovered from the peptide array screen and subsequently verified by mass spectrometry. Data from peptide pull-down and colocalization in cells suggest that, besides the H3K9me mark, H3K23me may play a role in facilitating the recruitment of HP1? to the heterochromatin. Extending the peptide array and mass spectrometric approach presented here to more histone marks and CBMs would eventually afford a comprehensive specificity and interaction map to aid epigenetic studies. | lld:pubmed |
| pubmed-article:20836566 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20836566 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20836566 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20836566 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20836566 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20836566 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20836566 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20836566 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:20836566 | pubmed:issn | 1535-3907 | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:BedfordMark... | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:LiLeiL | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:LajoieGillesG | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:HuangZhipingZ | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:WangZezhouZ | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:LiuHuadongH | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:GalkaMarekM | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:LiShawn S CSS | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:IbergAimeeA | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:VossCourtneyC | lld:pubmed |
| pubmed-article:20836566 | pubmed:author | pubmed-author:JiangXinfengX | lld:pubmed |
| pubmed-article:20836566 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20836566 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:20836566 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:20836566 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20836566 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20836566 | pubmed:pagination | 5827-36 | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:meshHeading | pubmed-meshheading:20836566... | lld:pubmed |
| pubmed-article:20836566 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20836566 | pubmed:articleTitle | Systematic identification of methyllysine-driven interactions for histone and nonhistone targets. | lld:pubmed |
| pubmed-article:20836566 | pubmed:affiliation | Department of Biochemistry, The University of Western Ontario, London, Ontario, N6A 5C1, Canada. | lld:pubmed |
| pubmed-article:20836566 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20836566 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20836566 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20836566 | lld:pubmed |
