| pubmed-article:9662451 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9662451 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:9662451 | lifeskim:mentions | umls-concept:C0076552 | lld:lifeskim |
| pubmed-article:9662451 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9662451 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9662451 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9662451 | pubmed:dateCreated | 1998-7-29 | lld:pubmed |
| pubmed-article:9662451 | pubmed:abstractText | We have recently reported that G alpha12 is acylated with palmitic acid [Veit et al., FEBS Lett. 339 (1994) 160-164]. Here we identify cysteine 11 as the sole palmitoylation site and assess the function of G alpha12 palmitoylation after expression of wild type and acylation-deficient mutant in insect cells. Our experimental approach yielded the following results. (1) Palmitoylation of G alpha12 has no influence on the subunit interactions. (2) Palmitoylation promotes membrane binding of G alpha12 when this protein is expressed alone. Membrane attachment of the heterotrimer occurs independent of the presence of fatty acids in G alpha12. (3) Assays for agonist-stimulated binding of [35S]GTPgammaS after expression of the human thrombin receptor (PAR1) along with G alpha12 and the betagamma subunits revealed a 70% inhibition with the palmitoyl-deficient mutant. | lld:pubmed |
| pubmed-article:9662451 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9662451 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9662451 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9662451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9662451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9662451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9662451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9662451 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9662451 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9662451 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:9662451 | pubmed:author | pubmed-author:SchultzGG | lld:pubmed |
| pubmed-article:9662451 | pubmed:author | pubmed-author:SchmidtM FMF | lld:pubmed |
| pubmed-article:9662451 | pubmed:author | pubmed-author:HarteneckCC | lld:pubmed |
| pubmed-article:9662451 | pubmed:author | pubmed-author:PonimaskinEE | lld:pubmed |
| pubmed-article:9662451 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9662451 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:9662451 | pubmed:volume | 429 | lld:pubmed |
| pubmed-article:9662451 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9662451 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9662451 | pubmed:pagination | 370-4 | lld:pubmed |
| pubmed-article:9662451 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:meshHeading | pubmed-meshheading:9662451-... | lld:pubmed |
| pubmed-article:9662451 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9662451 | pubmed:articleTitle | A cysteine-11 to serine mutant of G alpha12 impairs activation through the thrombin receptor. | lld:pubmed |
| pubmed-article:9662451 | pubmed:affiliation | Institut für Immunologie und Molekularbiologie, Freie Universität Berlin, City Campus Veterinary Faculty, Germany. | lld:pubmed |
| pubmed-article:9662451 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9662451 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9662451 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9662451 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9662451 | lld:pubmed |
