pubmed-article:10513894 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10513894 | lifeskim:mentions | umls-concept:C0031689 | lld:lifeskim |
pubmed-article:10513894 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:10513894 | lifeskim:mentions | umls-concept:C2260997 | lld:lifeskim |
pubmed-article:10513894 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:10513894 | pubmed:dateCreated | 1999-11-4 | lld:pubmed |
pubmed-article:10513894 | pubmed:abstractText | Failure of actinomycin D to block the activation of Dol-P-Man synthase in isoproterenol-treated capillary endothelial cells, supported that isoproterenol effect was not mediated by active transcription of the Dol-P-Man synthase gene during a short-term beta-adrenoreceptor stimulation. Instead, it was a net effect of protein phosphorylation by cAMP-dependent protein kinase. Using antibody as a probe we have now demonstrated that Dol-P-Man synthase activity is associated with a 32 kDa ER phosphoprotein. | lld:pubmed |
pubmed-article:10513894 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:language | eng | lld:pubmed |
pubmed-article:10513894 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10513894 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10513894 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10513894 | pubmed:month | Jun | lld:pubmed |
pubmed-article:10513894 | pubmed:issn | 0144-8463 | lld:pubmed |
pubmed-article:10513894 | pubmed:author | pubmed-author:BanerjeeD KDK | lld:pubmed |
pubmed-article:10513894 | pubmed:author | pubmed-author:DaSilvaJ JJJ | lld:pubmed |
pubmed-article:10513894 | pubmed:author | pubmed-author:BigioBB | lld:pubmed |
pubmed-article:10513894 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10513894 | pubmed:volume | 19 | lld:pubmed |
pubmed-article:10513894 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10513894 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10513894 | pubmed:pagination | 169-77 | lld:pubmed |
pubmed-article:10513894 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:10513894 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10513894 | pubmed:articleTitle | Mannosylphosphodolichol synthase activity is associated with a 32 kDa phosphoprotein. | lld:pubmed |
pubmed-article:10513894 | pubmed:affiliation | Department of Biochemistry, School of Medicine, University of Puerto Rico, San Juan 00936-5067, USA. d.banerjee@remaca.upr.ciu.edu | lld:pubmed |
pubmed-article:10513894 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10513894 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |