| pubmed-article:19011756 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19011756 | lifeskim:mentions | umls-concept:C0682323 | lld:lifeskim |
| pubmed-article:19011756 | lifeskim:mentions | umls-concept:C0108555 | lld:lifeskim |
| pubmed-article:19011756 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
| pubmed-article:19011756 | lifeskim:mentions | umls-concept:C1416640 | lld:lifeskim |
| pubmed-article:19011756 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:19011756 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:19011756 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19011756 | pubmed:dateCreated | 2009-2-2 | lld:pubmed |
| pubmed-article:19011756 | pubmed:abstractText | Protein kinase CK2 is a highly conserved serine/threonine kinase that is ubiquitously expressed in eukaryotic cells. CK2 is a constitutively active tetrameric enzyme composed of two catalytic alpha and/or alpha'-subunits and two regulatory beta-subunits. There is increasing evidence that the individual subunits may have independent functions and that they are asymmetrically distributed inside the cell. To gain a better understanding of the functions of the individual subunits, we employed a yeast-two-hybrid screen with CK2alpha and CK2alpha'. We identified the motor neuron protein KIF5C as a new binding partner for CK2. The interaction found in the yeast-two-hybrid screen was confirmed by co-sedimentation analysis on a sucrose density gradient and by co-immunoprecipitation analysis. Pull-down experiments and surface plasmon resonance spectrometry revealed a direct binding of KIF5C to CK2alpha'. Co-localization studies with neuroblastoma cells, bone marrow and with primary neurons confirmed the biochemical analysis that KIF5C preferentially bound to CK2alpha'. | lld:pubmed |
| pubmed-article:19011756 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19011756 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19011756 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19011756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19011756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19011756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19011756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19011756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19011756 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19011756 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:19011756 | pubmed:issn | 1420-9071 | lld:pubmed |
| pubmed-article:19011756 | pubmed:author | pubmed-author:SchäferBB | lld:pubmed |
| pubmed-article:19011756 | pubmed:author | pubmed-author:MattaMM | lld:pubmed |
| pubmed-article:19011756 | pubmed:author | pubmed-author:DudekJJ | lld:pubmed |
| pubmed-article:19011756 | pubmed:author | pubmed-author:GötzCC | lld:pubmed |
| pubmed-article:19011756 | pubmed:author | pubmed-author:MontenarhMM | lld:pubmed |
| pubmed-article:19011756 | pubmed:author | pubmed-author:HessenauerAA | lld:pubmed |
| pubmed-article:19011756 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19011756 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:19011756 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19011756 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19011756 | pubmed:pagination | 339-49 | lld:pubmed |
| pubmed-article:19011756 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:19011756 | pubmed:meshHeading | pubmed-meshheading:19011756... | lld:pubmed |
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| pubmed-article:19011756 | pubmed:meshHeading | pubmed-meshheading:19011756... | lld:pubmed |
| pubmed-article:19011756 | pubmed:meshHeading | pubmed-meshheading:19011756... | lld:pubmed |
| pubmed-article:19011756 | pubmed:meshHeading | pubmed-meshheading:19011756... | lld:pubmed |
| pubmed-article:19011756 | pubmed:meshHeading | pubmed-meshheading:19011756... | lld:pubmed |
| pubmed-article:19011756 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19011756 | pubmed:articleTitle | KIF5C: a new binding partner for protein kinase CK2 with a preference for the CK2alpha' subunit. | lld:pubmed |
| pubmed-article:19011756 | pubmed:affiliation | Medizinische Biochemie und Molekularbiologie, Universität des Saarlandes, Gebäude 44, 66424, Homburg, Germany. | lld:pubmed |
| pubmed-article:19011756 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19011756 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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