| pubmed-article:16415788 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C1335267 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C1719036 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C0542560 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C0456564 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16415788 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16415788 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16415788 | pubmed:dateCreated | 2006-4-4 | lld:pubmed |
| pubmed-article:16415788 | pubmed:abstractText | The post-translational modification of histones regulates many cellular processes, including transcription, replication and DNA repair. A large number of combinations of post-translational modifications are possible. This cipher is referred to as the histone code. Many of the enzymes that lay down this code have been identified. However, so far, few code-reading proteins have been identified. Here, we describe a protein-array approach for identifying methyl-specific interacting proteins. We found that not only chromo domains but also tudor and MBT domains bind to methylated peptides from the amino-terminal tails of histones H3 and H4. Binding specificity observed on the protein-domain microarray was corroborated using peptide pull-downs, surface plasma resonance and far western blotting. Thus, our studies expose tudor and MBT domains as new classes of methyl-lysine-binding protein modules, and also demonstrates that protein-domain microarrays are powerful tools for the identification of new domain types that recognize histone modifications. | lld:pubmed |
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| pubmed-article:16415788 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16415788 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16415788 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16415788 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16415788 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16415788 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16415788 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:16415788 | pubmed:issn | 1469-221X | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:FuZ HZH | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:BedfordMark... | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:ZhangYiY | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:DanielJeremyJ | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:EspejoAlexsan... | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:KimJeesunJ | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:KrishnaMurliM | lld:pubmed |
| pubmed-article:16415788 | pubmed:author | pubmed-author:LakeAimeeA | lld:pubmed |
| pubmed-article:16415788 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16415788 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:16415788 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16415788 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16415788 | pubmed:pagination | 397-403 | lld:pubmed |
| pubmed-article:16415788 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16415788 | pubmed:meshHeading | pubmed-meshheading:16415788... | lld:pubmed |
| pubmed-article:16415788 | pubmed:meshHeading | pubmed-meshheading:16415788... | lld:pubmed |
| pubmed-article:16415788 | pubmed:meshHeading | pubmed-meshheading:16415788... | lld:pubmed |
| pubmed-article:16415788 | pubmed:meshHeading | pubmed-meshheading:16415788... | lld:pubmed |
| pubmed-article:16415788 | pubmed:meshHeading | pubmed-meshheading:16415788... | lld:pubmed |
| pubmed-article:16415788 | pubmed:meshHeading | pubmed-meshheading:16415788... | lld:pubmed |
| pubmed-article:16415788 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16415788 | pubmed:articleTitle | Tudor, MBT and chromo domains gauge the degree of lysine methylation. | lld:pubmed |
| pubmed-article:16415788 | pubmed:affiliation | The University of Texas MD Anderson Cancer Center, Science Park-Research Division, Smithville, 78957, USA. | lld:pubmed |
| pubmed-article:16415788 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16415788 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:9682 | entrezgene:pubmed | pubmed-article:16415788 | lld:entrezgene |
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