| pubmed-article:18216497 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18216497 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:18216497 | lifeskim:mentions | umls-concept:C1579259 | lld:lifeskim |
| pubmed-article:18216497 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:18216497 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:18216497 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18216497 | pubmed:dateCreated | 2008-3-10 | lld:pubmed |
| pubmed-article:18216497 | pubmed:abstractText | Mammalian polo-like kinase 1 (Plk1) has been studied intensively as a key element in regulating diverse mitotic events during M-phase progression. Plk1 is spatially regulated through the targeting activity of the conserved polo-box domain (PBD) present in the C-terminal non-catalytic region. Over the years, studies have demonstrated that the PBD forms a phospho-epitope binding module and the PBD-dependent interaction is critical for proper subcellular localization of Plk1. The current prevailing model is that the PBD binds to a phospho-epitope generated by Cdc2 or other Pro-directed kinases. Here we discuss a recent finding that Plk1 also self-promotes its localization by generating its own PBD-docking site. | lld:pubmed |
| pubmed-article:18216497 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18216497 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18216497 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18216497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18216497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18216497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18216497 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18216497 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18216497 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:18216497 | pubmed:issn | 1551-4005 | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:ParkJung-EunJ... | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:EriksonRaymon... | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:LeeKyung SKS | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:SeongYeon-Sun... | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:SoungNak-Kyun... | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:KwakSahng-Jun... | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:ZimmermanWend... | lld:pubmed |
| pubmed-article:18216497 | pubmed:author | pubmed-author:KangYoung HYH | lld:pubmed |
| pubmed-article:18216497 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18216497 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:18216497 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:18216497 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18216497 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18216497 | pubmed:pagination | 141-5 | lld:pubmed |
| pubmed-article:18216497 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:meshHeading | pubmed-meshheading:18216497... | lld:pubmed |
| pubmed-article:18216497 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18216497 | pubmed:articleTitle | Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: self- versus non-self-priming. | lld:pubmed |
| pubmed-article:18216497 | pubmed:affiliation | Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-4258, USA. kyunglee@mail.nih.gov | lld:pubmed |
| pubmed-article:18216497 | pubmed:publicationType | Journal Article | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18216497 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18216497 | lld:pubmed |
