| pubmed-article:2176611 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2176611 | lifeskim:mentions | umls-concept:C0004611 | lld:lifeskim |
| pubmed-article:2176611 | lifeskim:mentions | umls-concept:C0038420 | lld:lifeskim |
| pubmed-article:2176611 | lifeskim:mentions | umls-concept:C1956003 | lld:lifeskim |
| pubmed-article:2176611 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:2176611 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:2176611 | lifeskim:mentions | umls-concept:C0075859 | lld:lifeskim |
| pubmed-article:2176611 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:2176611 | pubmed:dateCreated | 1991-2-20 | lld:pubmed |
| pubmed-article:2176611 | pubmed:abstractText | Tautomycin inhibited the catalytic subunits of protein phosphatase-1 (Kiapp = 0.16 nM) more potently than protein phosphatase 2A (Kiapp = 0.4 nM), and the native forms of these enzymes in mammalian, protozoan and plant extracts were inhibited in a similar manner. Protein phosphatase 2B was inhibited 10,000-fold less potently, while two other phosphatases and six protein kinases were unaffected at 10 microM. Okadaic acid prevented the binding of tautomycin to protein phosphatase 2A, indicating a common binding site for both inhibitors. The different relative potencies of tautomycin and okadaic acid for protein phosphatases 1 and 2A suggest that parallel use of both inhibitors may help to identify physiological substrates for each enzyme. | lld:pubmed |
| pubmed-article:2176611 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2176611 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2176611 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2176611 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2176611 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2176611 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:2176611 | pubmed:author | pubmed-author:KlumppSS | lld:pubmed |
| pubmed-article:2176611 | pubmed:author | pubmed-author:MacKintoshCC | lld:pubmed |
| pubmed-article:2176611 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2176611 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:2176611 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:2176611 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2176611 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2176611 | pubmed:pagination | 137-40 | lld:pubmed |
| pubmed-article:2176611 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:2176611 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2176611 | pubmed:articleTitle | Tautomycin from the bacterium Streptomyces verticillatus. Another potent and specific inhibitor of protein phosphatases 1 and 2A. | lld:pubmed |
| pubmed-article:2176611 | pubmed:affiliation | Department of Biochemistry, University of Dundee, Scotland, UK. | lld:pubmed |
| pubmed-article:2176611 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2176611 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2176611 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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