| pubmed-article:2171991 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0031678 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0069389 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C1304606 | lld:lifeskim |
| pubmed-article:2171991 | lifeskim:mentions | umls-concept:C0081429 | lld:lifeskim |
| pubmed-article:2171991 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:2171991 | pubmed:dateCreated | 1990-12-10 | lld:pubmed |
| pubmed-article:2171991 | pubmed:abstractText | Acanthifolicin (9,10-epithio-okadaic acid from Pandoras acanthifolium) inhibited protein phosphatase-1 (PP1) similarly to okadaic acid (IC50 = 20 nM and 19 nM, respectively) but was slightly less active against protein phosphatase-2A (PP2A) (IC50 = 1 nM and 0.2 nM, respectively). Methyl esterification of acanthifolicin sharply reduced its activity. PP2A was inhibited with an IC50 = 5.0 microM, whilst PP1 was inhibited less than 10% at 250 microM toxin. Okadaic acid methyl ester was similarly inactive whereas dinophysistoxin-1 (35-methyl okadaic acid) inhibited PP1/2A almost as potently as okadaic acid. Pure acanthifolicin/okadaic acid methyl ester may be useful as specific inhibitors of PP2A at 1-10 microM concentrations in vitro and perhaps in vivo. The data also indicate that a region on these toxins important for PP1/2A inhibition comprises the single carboxyl group. | lld:pubmed |
| pubmed-article:2171991 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2171991 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2171991 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2171991 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2171991 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2171991 | pubmed:author | pubmed-author:SchmitzF JFJ | lld:pubmed |
| pubmed-article:2171991 | pubmed:author | pubmed-author:HolmesC FCF | lld:pubmed |
| pubmed-article:2171991 | pubmed:author | pubmed-author:CarrierFF | lld:pubmed |
| pubmed-article:2171991 | pubmed:author | pubmed-author:LuuH AHA | lld:pubmed |
| pubmed-article:2171991 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2171991 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:2171991 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:2171991 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2171991 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2171991 | pubmed:pagination | 216-8 | lld:pubmed |
| pubmed-article:2171991 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:meshHeading | pubmed-meshheading:2171991-... | lld:pubmed |
| pubmed-article:2171991 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2171991 | pubmed:articleTitle | Inhibition of protein phosphatases-1 and -2A with acanthifolicin. Comparison with diarrhetic shellfish toxins and identification of a region on okadaic acid important for phosphatase inhibition. | lld:pubmed |
| pubmed-article:2171991 | pubmed:affiliation | National Research Council, Biotechnology Research Institute, Montreal, Québec, Canada. | lld:pubmed |
| pubmed-article:2171991 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2171991 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2171991 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2171991 | lld:pubmed |
