| pubmed-article:2982364 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2982364 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2982364 | lifeskim:mentions | umls-concept:C0085249 | lld:lifeskim |
| pubmed-article:2982364 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:2982364 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:2982364 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:2982364 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2982364 | pubmed:dateCreated | 1985-3-20 | lld:pubmed |
| pubmed-article:2982364 | pubmed:abstractText | beta-Adrenoreceptor stimulation of rat parotid acinar cells increases the activity of several microsomal membrane associated, dolichylmonophosphate (Dol-P) linked glycosyltransferases. The activities of Man-P-Dol synthase and Glc-P-Dol synthase are increased by approximately 50%, and the activity of N-acetylglucosaminyl 1-phosphate transferase plus N-acetylglucosaminyl transferase increased by approximately 60%, after agonist treatment. Increases in enzyme activity are (i) independent of endogenous Dol-P levels and (ii) observed under conditions in which the specific activities of donor sugar nucleotides are kept constant. Activation of these enzymes is specific since comparable levels of NADPH-cytochrome c reductase are found in control and agonist-treated membranes. The data thus provide the initial demonstration of neurotransmitter modulation of enzymes in the dolichol-linked pathway of protein N-glycosylation. | lld:pubmed |
| pubmed-article:2982364 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2982364 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2982364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2982364 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2982364 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2982364 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:2982364 | pubmed:author | pubmed-author:BaumB JBJ | lld:pubmed |
| pubmed-article:2982364 | pubmed:author | pubmed-author:KousvelariE... | lld:pubmed |
| pubmed-article:2982364 | pubmed:author | pubmed-author:BanerjeeD KDK | lld:pubmed |
| pubmed-article:2982364 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2982364 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:2982364 | pubmed:volume | 126 | lld:pubmed |
| pubmed-article:2982364 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2982364 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2982364 | pubmed:pagination | 123-9 | lld:pubmed |
| pubmed-article:2982364 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:meshHeading | pubmed-meshheading:2982364-... | lld:pubmed |
| pubmed-article:2982364 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2982364 | pubmed:articleTitle | beta-Adrenergic activation of glycosyltransferases in the dolichylmonophosphate-linked pathway of protein N-glycosylation. | lld:pubmed |
| pubmed-article:2982364 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2982364 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2982364 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2982364 | lld:pubmed |
