| pubmed-article:16888362 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16888362 | lifeskim:mentions | umls-concept:C1511681 | lld:lifeskim |
| pubmed-article:16888362 | lifeskim:mentions | umls-concept:C1511658 | lld:lifeskim |
| pubmed-article:16888362 | pubmed:dateCreated | 2006-8-4 | lld:pubmed |
| pubmed-article:16888362 | pubmed:abstractText | Effective methods of probing chromatin structure without disrupting DNA-protein interactions and associations are necessary for creating an accurate picture of chromatin and its processes in vivo. Expression of cytidine-5 DNA methyltransferases (C5 DMTases) in Saccharomyces cerevisiae provides a powerful noninvasive method of assaying relative DNA accessibility in chromatin. DNA MTases are occluded from protein-associated DNA based on the strength and span of the DNA-protein interaction. Ectopic regulation of C5 DMTase expression systems allows for minimal disruption of yeast physiology. Methylated sites are detected by bisulfite genomic sequencing, which leads to a positive signal corresponding to modified cytidine residues. High-resolution C5 DMTases with dinucleotide recognition specificity are shown to provide sufficient coverage to map interactions spanning a relatively short distance. | lld:pubmed |
| pubmed-article:16888362 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16888362 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16888362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16888362 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16888362 | pubmed:issn | 1064-3745 | lld:pubmed |
| pubmed-article:16888362 | pubmed:author | pubmed-author:KladdeMichael... | lld:pubmed |
| pubmed-article:16888362 | pubmed:author | pubmed-author:HooseScott... | lld:pubmed |
| pubmed-article:16888362 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16888362 | pubmed:volume | 338 | lld:pubmed |
| pubmed-article:16888362 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16888362 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16888362 | pubmed:pagination | 225-44 | lld:pubmed |
| pubmed-article:16888362 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
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| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
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| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:meshHeading | pubmed-meshheading:16888362... | lld:pubmed |
| pubmed-article:16888362 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16888362 | pubmed:articleTitle | DNA methyltransferase probing of DNA-protein interactions. | lld:pubmed |
| pubmed-article:16888362 | pubmed:affiliation | Department of Biochemistry and Biophysics, Texas A & M University, College Station, TX, USA. | lld:pubmed |
| pubmed-article:16888362 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16888362 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16888362 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16888362 | lld:pubmed |
