| pubmed-article:8308007 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C2700455 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0031603 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0040005 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0108555 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C1947974 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C1881217 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:8308007 | lifeskim:mentions | umls-concept:C1720655 | lld:lifeskim |
| pubmed-article:8308007 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8308007 | pubmed:dateCreated | 1994-3-17 | lld:pubmed |
| pubmed-article:8308007 | pubmed:abstractText | The in vitro phosphorylation of the microtubule-associated protein tau by casein kinase II was studied. Purified human brain tau was phosphorylated by casein kinase II to a stoichiometry of 0.7 mol of 32P/mol of tau. Individual recombinant human tau isoforms were phosphorylated to stoichiometries ranging from 0.2 to 0.8 mol of 32P/mol of tau. Casein kinase II catalyzed a 4-fold greater incorporation of phosphate into the tau isoform containing a 58-amino acid insert near its amino terminus (T4L) than the isoforms without the 58-amino acid insert (T3 and T4). Phosphopeptide mapping of casein kinase II phosphorylated human tau and recombinant tau isoforms suggested that the isoforms containing an amino-terminal insert constitute the major substrates for casein kinase II within the tau family. The sites of phosphorylation on T4L were identified by digesting phosphorylated T4L with the protease Asp-N, separating the peptides by reversed phase high performance liquid chromatography, and analyzing the isolated peptides by liquid-secondary ion mass spectrometry and solid-phase amino-terminal sequencing. Thr39 was identified as the predominant phosphorylation site, which is located 5 residues from the amino-terminal insert in T4L. Phosphopeptide mapping of tau isolated from LA-N-5 neuroblastoma cells indicates that Thr39 is phosphorylated in situ. To our knowledge, this is the first demonstration of a differential phosphorylation of the human tau isoforms, with the isoforms containing the acidic amino-terminal insert being the preferred substrates of casein kinase II. | lld:pubmed |
| pubmed-article:8308007 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8308007 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8308007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8308007 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8308007 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8308007 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8308007 | pubmed:author | pubmed-author:ScottC WCW | lld:pubmed |
| pubmed-article:8308007 | pubmed:author | pubmed-author:GreenwoodJ... | lld:pubmed |
| pubmed-article:8308007 | pubmed:author | pubmed-author:CaputoC BCB | lld:pubmed |
| pubmed-article:8308007 | pubmed:author | pubmed-author:JohnsonG VGV | lld:pubmed |
| pubmed-article:8308007 | pubmed:author | pubmed-author:SpreenR CRC | lld:pubmed |
| pubmed-article:8308007 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8308007 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:8308007 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8308007 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8308007 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8308007 | pubmed:pagination | 4373-80 | lld:pubmed |
| pubmed-article:8308007 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:meshHeading | pubmed-meshheading:8308007-... | lld:pubmed |
| pubmed-article:8308007 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8308007 | pubmed:articleTitle | Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor. | lld:pubmed |
| pubmed-article:8308007 | pubmed:affiliation | Department of Psychiatry and Behavioral Neurobiology, University of Alabama at Birmingham 35294. | lld:pubmed |
| pubmed-article:8308007 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8308007 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8308007 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8308007 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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