| pubmed-article:11434916 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11434916 | lifeskim:mentions | umls-concept:C0812246 | lld:lifeskim |
| pubmed-article:11434916 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:11434916 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:11434916 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
| pubmed-article:11434916 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:11434916 | pubmed:dateCreated | 2001-7-3 | lld:pubmed |
| pubmed-article:11434916 | pubmed:abstractText | Human transmembrane tumor necrosis factor (pro-TNF) was examined for protein acylation. The cDNA encoding pro-TNF was expressed in both COS-1 cells and Sf9 cells and metabolic labeling with [(3)H]myristic or [(3)H]palmitic acid was attempted. The 17 kDa mature TNF secreted from the transfected cells was not labeled, whereas the 26 kDa pro-TNF was specifically labeled with [(3)H]palmitic acid. The [(3)H]palmitic acid labeling of pro-TNF was eliminated by treatment with hydroxylamine, indicating that the labeling was due to palmitoylation of a cysteine residue via a thioester bond. Site-directed mutagenesis of the two cysteine residues residing in the leader sequence of pro-TNF demonstrated that palmitoylation of pro-TNF occurs solely at Cys-47, located at the boundary between the transmembrane and cytoplasmic domains of pro-TNF. Thus, pro-TNF interacts with the plasma membrane via both its proteinaceous transmembrane domain and a lipid anchor. | lld:pubmed |
| pubmed-article:11434916 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11434916 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11434916 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11434916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11434916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11434916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11434916 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11434916 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11434916 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11434916 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:11434916 | pubmed:author | pubmed-author:TanakaKK | lld:pubmed |
| pubmed-article:11434916 | pubmed:author | pubmed-author:KirkCC | lld:pubmed |
| pubmed-article:11434916 | pubmed:author | pubmed-author:KlostergaardJ... | lld:pubmed |
| pubmed-article:11434916 | pubmed:author | pubmed-author:UtsumiTT | lld:pubmed |
| pubmed-article:11434916 | pubmed:author | pubmed-author:TakamiKK | lld:pubmed |
| pubmed-article:11434916 | pubmed:author | pubmed-author:TakeshigeTT | lld:pubmed |
| pubmed-article:11434916 | pubmed:author | pubmed-author:IshisakaRR | lld:pubmed |
| pubmed-article:11434916 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11434916 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:11434916 | pubmed:volume | 500 | lld:pubmed |
| pubmed-article:11434916 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11434916 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11434916 | pubmed:pagination | 1-6 | lld:pubmed |
| pubmed-article:11434916 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:meshHeading | pubmed-meshheading:11434916... | lld:pubmed |
| pubmed-article:11434916 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11434916 | pubmed:articleTitle | Transmembrane TNF (pro-TNF) is palmitoylated. | lld:pubmed |
| pubmed-article:11434916 | pubmed:affiliation | Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515, Japan. utsumi@agr.yamaguchi-u.ac.jp | lld:pubmed |
| pubmed-article:11434916 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11434916 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11434916 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11434916 | lld:pubmed |
