| pubmed-article:6190674 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0042666 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0022564 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0002630 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0031603 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0026255 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0700114 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:6190674 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
| pubmed-article:6190674 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6190674 | pubmed:dateCreated | 1983-8-17 | lld:pubmed |
| pubmed-article:6190674 | pubmed:abstractText | Two-dimensional gel electrophoresis (IEF) analysis of short-term [32P]orthophosphate-labelled intermediate-sized filament proteins (keratins and vimentin) from transformed mitotic amnion cells (AMA), have shown that these proteins are modified coordinately and that the half life of the phosphate is about 13 min for the keratins and 11 min for vimentin. These results support the notion that the preferential modification of intermediate-sized filament proteins during mitosis may play a role in modulating filament associations with organelles and other cellular structures. | lld:pubmed |
| pubmed-article:6190674 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6190674 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6190674 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6190674 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6190674 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6190674 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6190674 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6190674 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6190674 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:6190674 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:6190674 | pubmed:author | pubmed-author:CelisJ EJE | lld:pubmed |
| pubmed-article:6190674 | pubmed:author | pubmed-author:FeyS JSJ | lld:pubmed |
| pubmed-article:6190674 | pubmed:author | pubmed-author:LarsenP MPM | lld:pubmed |
| pubmed-article:6190674 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6190674 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:6190674 | pubmed:volume | 157 | lld:pubmed |
| pubmed-article:6190674 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6190674 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6190674 | pubmed:pagination | 165-9 | lld:pubmed |
| pubmed-article:6190674 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:meshHeading | pubmed-meshheading:6190674-... | lld:pubmed |
| pubmed-article:6190674 | pubmed:year | 1983 | lld:pubmed |
| pubmed-article:6190674 | pubmed:articleTitle | Evidence for coordinated phosphorylation of keratins and vimentin during mitosis in transformed human amnion cells. Phosphate turnover of modified proteins. | lld:pubmed |
| pubmed-article:6190674 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6190674 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:6190674 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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