pubmed-article:19887368 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C0252409 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C0069141 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C0872318 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:19887368 | lifeskim:mentions | umls-concept:C0075804 | lld:lifeskim |
pubmed-article:19887368 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:19887368 | pubmed:dateCreated | 2009-12-28 | lld:pubmed |
pubmed-article:19887368 | pubmed:abstractText | Previous studies have shown that the kinase activation loop (KAL) of the oncogenic fusion protein NPM-ALK regulates its overall tyrosine phosphorylation status and tumorigenicity. Using tandem affinity purification-mass spectrometry, we assessed how the KAL of NPM-ALK regulates the phosphorylation status of its individual tyrosines. Using the lysates of GP293 cells transfected with NPM-ALK, our highly reproducible results showed evidence of phosphorylation in all 3 tyrosines in KAL and 8 tyrosines outside KAL. We created 7 KAL mutants, each of which carried a Tyr-to-Phe mutation of >or=1 of the 3 tyrosines in KAL. A complete loss of the 8 phosphotyrosines outside KAL was found in 3 KAL mutants, and their oncogenicity (assessed by cell viability, colony formation, and the ability to phosphorylate effector proteins) was abrogated. A partial loss of the 8 phosphotyrosines was found in 4 KAL mutants, but their oncogenicity did not show simple correlation with the number of residual phosphotyrosines. Tyr-to-Phe mutations of each of the 8 phosphotyrosines outside KAL did not result in a significant decrease in the oncogenicity. In conclusion, we have provided details of how the KAL in NPM-ALK regulates its tyrosine phosphorylation pattern. Our results challenge some of the current concepts regarding the relationship between the tyrosine phosphorylation and oncogenicity of NPM-ALK. | lld:pubmed |
pubmed-article:19887368 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:language | eng | lld:pubmed |
pubmed-article:19887368 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19887368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19887368 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19887368 | pubmed:month | Jan | lld:pubmed |
pubmed-article:19887368 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:19887368 | pubmed:author | pubmed-author:WangPengP | lld:pubmed |
pubmed-article:19887368 | pubmed:author | pubmed-author:LaiRaymondR | lld:pubmed |
pubmed-article:19887368 | pubmed:author | pubmed-author:LiLiangL | lld:pubmed |
pubmed-article:19887368 | pubmed:author | pubmed-author:WuFangF | lld:pubmed |
pubmed-article:19887368 | pubmed:author | pubmed-author:YoungLeah CLC | lld:pubmed |
pubmed-article:19887368 | pubmed:author | pubmed-author:MaYupoY | lld:pubmed |
pubmed-article:19887368 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19887368 | pubmed:day | 1 | lld:pubmed |
pubmed-article:19887368 | pubmed:volume | 285 | lld:pubmed |
pubmed-article:19887368 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19887368 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19887368 | pubmed:pagination | 95-103 | lld:pubmed |
pubmed-article:19887368 | pubmed:dateRevised | 2011-7-19 | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:meshHeading | pubmed-meshheading:19887368... | lld:pubmed |
pubmed-article:19887368 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:19887368 | pubmed:articleTitle | Functional characterization of the kinase activation loop in nucleophosmin (NPM)-anaplastic lymphoma kinase (ALK) using tandem affinity purification and liquid chromatography-mass spectrometry. | lld:pubmed |
pubmed-article:19887368 | pubmed:affiliation | Department of Laboratory Medicine and Pathology, University of Alberta and Cross Cancer Institute, Edmonton, Alberta T6G 2Z2, Canada. | lld:pubmed |
pubmed-article:19887368 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19887368 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:4869 | entrezgene:pubmed | pubmed-article:19887368 | lld:entrezgene |
entrez-gene:238 | entrezgene:pubmed | pubmed-article:19887368 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19887368 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19887368 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19887368 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19887368 | lld:pubmed |