pubmed-article:20098424 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:20098424 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:20098424 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
pubmed-article:20098424 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:20098424 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
pubmed-article:20098424 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
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pubmed-article:20098424 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:20098424 | pubmed:dateCreated | 2010-2-4 | lld:pubmed |
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pubmed-article:20098424 | pubmed:abstractText | Addition of poly(ADP-ribose) (PAR) is an important post-translational modification in higher eukaryotes. Several DNA repair and checkpoint proteins possess specific PAR-binding zinc-finger (PBZ) modules critical for function. Here, we present solution structures of the two PBZ modules of aprataxin and PNK-like factor (APLF), revealing a novel type of zinc finger. By combining in vivo PAR-binding data with NMR interaction data using PAR fragments, we propose a structural basis for PBZ-PAR recognition. | lld:pubmed |
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pubmed-article:20098424 | pubmed:language | eng | lld:pubmed |
pubmed-article:20098424 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20098424 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20098424 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:20098424 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20098424 | pubmed:month | Feb | lld:pubmed |
pubmed-article:20098424 | pubmed:issn | 1545-9985 | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:NeuhausDavidD | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:WestStephen... | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:AhelIvanI | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:LoakesDavidD | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:BrockmannChri... | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:YangJi-ChunJC | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:EustermannSeb... | lld:pubmed |
pubmed-article:20098424 | pubmed:author | pubmed-author:MehrotraPawan... | lld:pubmed |
pubmed-article:20098424 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20098424 | pubmed:volume | 17 | lld:pubmed |
pubmed-article:20098424 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20098424 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20098424 | pubmed:pagination | 241-3 | lld:pubmed |
pubmed-article:20098424 | pubmed:dateRevised | 2010-9-28 | lld:pubmed |
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pubmed-article:20098424 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20098424 | pubmed:articleTitle | Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose). | lld:pubmed |
pubmed-article:20098424 | pubmed:affiliation | MRC Laboratory of Molecular Biology, Cambridge, UK. | lld:pubmed |
pubmed-article:20098424 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20098424 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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