| pubmed-article:15824109 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C1519692 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15824109 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15824109 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:15824109 | pubmed:dateCreated | 2005-6-6 | lld:pubmed |
| pubmed-article:15824109 | pubmed:abstractText | The tumor suppressor function of the von Hippel-Lindau protein (pVHL) has previously been linked to its role in regulating hypoxia-inducible factor levels. However, VHL gene mutations suggest a hypoxia-inducible factor-independent function for the N-terminal acidic domain in tumor suppression. Here, we report that phosphorylation of the N-terminal acidic domain of pVHL by casein kinase-2 is essential for its tumor suppressor function. This post-translational modification did not affect the levels of hypoxia-inducible factor; however, it did change the binding of pVHL to another known binding partner, fibronectin. Cells expressing phospho-defective mutants caused improper fibronectin matrix deposition and demonstrated retarded tumor formation in mice. We propose that phosphorylation of the acidic domain plays a role in the regulation of proper fibronectin matrix deposition and that this may be relevant for the development of VHL-associated malignancies. | lld:pubmed |
| pubmed-article:15824109 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15824109 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15824109 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15824109 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15824109 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15824109 | pubmed:author | pubmed-author:HillRichard... | lld:pubmed |
| pubmed-article:15824109 | pubmed:author | pubmed-author:OhhMichaelM | lld:pubmed |
| pubmed-article:15824109 | pubmed:author | pubmed-author:VoestEmile... | lld:pubmed |
| pubmed-article:15824109 | pubmed:author | pubmed-author:GilesRachel... | lld:pubmed |
| pubmed-article:15824109 | pubmed:author | pubmed-author:GervaisMichel... | lld:pubmed |
| pubmed-article:15824109 | pubmed:author | pubmed-author:LolkemaMartij... | lld:pubmed |
| pubmed-article:15824109 | pubmed:author | pubmed-author:SnijckersCris... | lld:pubmed |
| pubmed-article:15824109 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15824109 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:15824109 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15824109 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15824109 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15824109 | pubmed:pagination | 22205-11 | lld:pubmed |
| pubmed-article:15824109 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15824109 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15824109 | pubmed:articleTitle | Tumor suppression by the von Hippel-Lindau protein requires phosphorylation of the acidic domain. | lld:pubmed |
| pubmed-article:15824109 | pubmed:affiliation | Department of Medical Oncology, University Medical Center Utrecht, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:15824109 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15824109 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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