pubmed-article:1647766 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1647766 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:1647766 | lifeskim:mentions | umls-concept:C0042666 | lld:lifeskim |
pubmed-article:1647766 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
pubmed-article:1647766 | lifeskim:mentions | umls-concept:C0069389 | lld:lifeskim |
pubmed-article:1647766 | lifeskim:mentions | umls-concept:C0332293 | lld:lifeskim |
pubmed-article:1647766 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
pubmed-article:1647766 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:1647766 | pubmed:dateCreated | 1991-7-31 | lld:pubmed |
pubmed-article:1647766 | pubmed:abstractText | Okadaic acid and dinophysistoxin-1 (35-methylokadaic acid) induced hyperphosphorylation of a 58 kDa protein in primary human fibroblasts, due to inhibition of protein phosphatase 1 and 2A activities. The protein was present in the nuclear and cytosolic fractions. Its pI was 5.3. The hyperphosphorylated protein reacted with monoclonal and polyclonal anti-vimentin antibodies, but not with anti-nucleolin antibody. Phosphorylation of vimentin was stimulated in vitro by dinophysistoxin-1 dose-dependently in the presence of protein phosphatase 2A and protein kinases. | lld:pubmed |
pubmed-article:1647766 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1647766 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1647766 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1647766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1647766 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1647766 | pubmed:month | Jun | lld:pubmed |
pubmed-article:1647766 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:1647766 | pubmed:author | pubmed-author:GoldmanR DRD | lld:pubmed |
pubmed-article:1647766 | pubmed:author | pubmed-author:OlsonM OMO | lld:pubmed |
pubmed-article:1647766 | pubmed:author | pubmed-author:YoshizawaSS | lld:pubmed |
pubmed-article:1647766 | pubmed:author | pubmed-author:FujikiHH | lld:pubmed |
pubmed-article:1647766 | pubmed:author | pubmed-author:SuganumaMM | lld:pubmed |
pubmed-article:1647766 | pubmed:author | pubmed-author:ErikssonJ EJE | lld:pubmed |
pubmed-article:1647766 | pubmed:author | pubmed-author:YatsunamiJJ | lld:pubmed |
pubmed-article:1647766 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1647766 | pubmed:day | 28 | lld:pubmed |
pubmed-article:1647766 | pubmed:volume | 177 | lld:pubmed |
pubmed-article:1647766 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1647766 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1647766 | pubmed:pagination | 1165-70 | lld:pubmed |
pubmed-article:1647766 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:1647766 | pubmed:meshHeading | pubmed-meshheading:1647766-... | lld:pubmed |
pubmed-article:1647766 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1647766 | pubmed:articleTitle | Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid. | lld:pubmed |
pubmed-article:1647766 | pubmed:affiliation | Cancer Prevention Division, National Cancer Center Research Institute, Tokyo, Japan. | lld:pubmed |
pubmed-article:1647766 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1647766 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1647766 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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