| pubmed-article:1850997 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1850997 | lifeskim:mentions | umls-concept:C0042666 | lld:lifeskim |
| pubmed-article:1850997 | lifeskim:mentions | umls-concept:C0248868 | lld:lifeskim |
| pubmed-article:1850997 | lifeskim:mentions | umls-concept:C1413043 | lld:lifeskim |
| pubmed-article:1850997 | lifeskim:mentions | umls-concept:C1519063 | lld:lifeskim |
| pubmed-article:1850997 | lifeskim:mentions | umls-concept:C1710548 | lld:lifeskim |
| pubmed-article:1850997 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:1850997 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1850997 | pubmed:dateCreated | 1991-6-5 | lld:pubmed |
| pubmed-article:1850997 | pubmed:abstractText | We identified the sites on vimentin that are phosphorylated by Ca2(+)-calmodulin-dependent protein kinase II (CaM-kinase II). Sequential analysis of the purified phosphopeptides demonstrated that the sites are -Thr-Arg-Thr-Tyr-Ser(PO4)38-Leu-Gly-Ser-Ala- and -Val-Arg-Leu-Leu-Gln-Asp-Ser(PO4)82-Val-Asp-, which are located within the amino-terminal head domain of vimentin. For Ser-82 but not Ser-38, the proposed CaM-kinase II recognition amino acid sequence (Arg-X-X-Ser/Thr) was not found. Studies with a series of synthetic peptide analogs corresponding to Ser-82 and its surrounding amino acid sequence indicate that Asp-84 acts as an essential substrate specificity determinant for the Ser-82 phosphorylation by CaM-kinase II. The CaM-kinase II recognition site may be more extensive than heretofore determined. | lld:pubmed |
| pubmed-article:1850997 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1850997 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1850997 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1850997 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1850997 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1850997 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1850997 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1850997 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1850997 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1850997 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:1850997 | pubmed:author | pubmed-author:TokuiTT | lld:pubmed |
| pubmed-article:1850997 | pubmed:author | pubmed-author:YamauchiTT | lld:pubmed |
| pubmed-article:1850997 | pubmed:author | pubmed-author:TanabeKK | lld:pubmed |
| pubmed-article:1850997 | pubmed:author | pubmed-author:SugiuraHH | lld:pubmed |
| pubmed-article:1850997 | pubmed:author | pubmed-author:AndoSS | lld:pubmed |
| pubmed-article:1850997 | pubmed:author | pubmed-author:InagakiMM | lld:pubmed |
| pubmed-article:1850997 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1850997 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:1850997 | pubmed:volume | 175 | lld:pubmed |
| pubmed-article:1850997 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1850997 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1850997 | pubmed:pagination | 955-62 | lld:pubmed |
| pubmed-article:1850997 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:1850997 | pubmed:meshHeading | pubmed-meshheading:1850997-... | lld:pubmed |
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| pubmed-article:1850997 | pubmed:meshHeading | pubmed-meshheading:1850997-... | lld:pubmed |
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| pubmed-article:1850997 | pubmed:meshHeading | pubmed-meshheading:1850997-... | lld:pubmed |
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| pubmed-article:1850997 | pubmed:meshHeading | pubmed-meshheading:1850997-... | lld:pubmed |
| pubmed-article:1850997 | pubmed:meshHeading | pubmed-meshheading:1850997-... | lld:pubmed |
| pubmed-article:1850997 | pubmed:meshHeading | pubmed-meshheading:1850997-... | lld:pubmed |
| pubmed-article:1850997 | pubmed:meshHeading | pubmed-meshheading:1850997-... | lld:pubmed |
| pubmed-article:1850997 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1850997 | pubmed:articleTitle | Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II. | lld:pubmed |
| pubmed-article:1850997 | pubmed:affiliation | Biophysics Unit, Aichi Cancer Center Research Institute, Japan. | lld:pubmed |
| pubmed-article:1850997 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1850997 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:22352 | entrezgene:pubmed | pubmed-article:1850997 | lld:entrezgene |
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