| pubmed-article:19021755 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19021755 | lifeskim:mentions | umls-concept:C0009753 | lld:lifeskim |
| pubmed-article:19021755 | lifeskim:mentions | umls-concept:C1519021 | lld:lifeskim |
| pubmed-article:19021755 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:19021755 | lifeskim:mentions | umls-concept:C0004348 | lld:lifeskim |
| pubmed-article:19021755 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:19021755 | pubmed:dateCreated | 2008-11-21 | lld:pubmed |
| pubmed-article:19021755 | pubmed:abstractText | In budding yeast, the protein phosphatase Cdc14 is a key regulator of late mitotic events. Research over the last decade has revealed many of its functions and today we know that this protein phosphatase orchestrates several aspects of chromosome segregation and is the key trigger of exit from mitosis. Elucidation of the mechanisms controlling Cdc14 activity through nucleolar sequestration now serves as a paradigm for how regulation of the subcellular localization of proteins regulates protein function. Here I review these findings focusing on how discoveries in my laboratory helped elucidate the function and regulation of Cdc14. | lld:pubmed |
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| pubmed-article:19021755 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19021755 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19021755 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19021755 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19021755 | pubmed:month | Dec | lld:pubmed |
