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| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C1705660 | lld:lifeskim |
| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C0230398 | lld:lifeskim |
| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C0008546 | lld:lifeskim |
| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C0019646 | lld:lifeskim |
| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C1415406 | lld:lifeskim |
| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:19500350 | lifeskim:mentions | umls-concept:C1538866 | lld:lifeskim |
| pubmed-article:19500350 | pubmed:dateCreated | 2009-6-23 | lld:pubmed |
| pubmed-article:19500350 | pubmed:abstractText | Modulation of chromatin structure has emerged as a critical molecular device to control gene expression. Histones undergo different post-translational modifications that increase chromatin accessibility to a number of regulatory factors. Among them, histone ubiquitination appears relevant in nuclear processes that govern gene silencing, either by inhibiting or activating transcription, and maintain genome stability, acting as scaffold to properly organize the DNA damage response. Thus, it is of paramount importance the identification and the characterization of new ubiquitin ligases that address histones. | lld:pubmed |
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| pubmed-article:19500350 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19500350 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19500350 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19500350 | pubmed:issn | 1471-2199 | lld:pubmed |
| pubmed-article:19500350 | pubmed:author | pubmed-author:CitterioElisa... | lld:pubmed |
| pubmed-article:19500350 | pubmed:author | pubmed-author:GaudinoGiovan... | lld:pubmed |
| pubmed-article:19500350 | pubmed:author | pubmed-author:PenengoLorenz... | lld:pubmed |
| pubmed-article:19500350 | pubmed:author | pubmed-author:PinatoSabrina... | lld:pubmed |
| pubmed-article:19500350 | pubmed:author | pubmed-author:ScandiuzziCri... | lld:pubmed |
| pubmed-article:19500350 | pubmed:author | pubmed-author:ArnaudoNadiaN | lld:pubmed |
| pubmed-article:19500350 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19500350 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:19500350 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19500350 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19500350 | pubmed:pagination | 55 | lld:pubmed |
| pubmed-article:19500350 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:19500350 | pubmed:meshHeading | pubmed-meshheading:19500350... | lld:pubmed |
| pubmed-article:19500350 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19500350 | pubmed:articleTitle | RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX. | lld:pubmed |
| pubmed-article:19500350 | pubmed:affiliation | Department of DISCAFF and DFB Center, University of Piemonte Orientale A, Avogadro, Novara, Italy. sabrina.pinato@pharm.unipmn.it | lld:pubmed |
| pubmed-article:19500350 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19500350 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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