| pubmed-article:16859706 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C1185625 | lld:lifeskim |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C0018042 | lld:lifeskim |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C1420880 | lld:lifeskim |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C1519623 | lld:lifeskim |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C1444748 | lld:lifeskim |
| pubmed-article:16859706 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:16859706 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16859706 | pubmed:dateCreated | 2006-8-1 | lld:pubmed |
| pubmed-article:16859706 | pubmed:abstractText | TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion. To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1. Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques. PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262. By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1. In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment. This domain exhibits a pronounced secondary structure in a lipid environment. Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment. | lld:pubmed |
| pubmed-article:16859706 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16859706 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16859706 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16859706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16859706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16859706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16859706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16859706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16859706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16859706 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16859706 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16859706 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:GoettschSandr... | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:BayerPeterP | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:WotzlawChrist... | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:MuellerJonath... | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:Hartmann-Fatu... | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:RabillerMatth... | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:BadeaRodica... | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:SchoelermannB... | lld:pubmed |
| pubmed-article:16859706 | pubmed:author | pubmed-author:SchulzLarsL | lld:pubmed |
| pubmed-article:16859706 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16859706 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:16859706 | pubmed:volume | 361 | lld:pubmed |
| pubmed-article:16859706 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16859706 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16859706 | pubmed:pagination | 436-49 | lld:pubmed |
| pubmed-article:16859706 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
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| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
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| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:meshHeading | pubmed-meshheading:16859706... | lld:pubmed |
| pubmed-article:16859706 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16859706 | pubmed:articleTitle | Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment. | lld:pubmed |
| pubmed-article:16859706 | pubmed:affiliation | Department of Structural and Medicinal Biochemistry, University of Duisburg-Essen and Centre for Medicinal Biotechnology, Universitätsstr. 2-5, 45117 Essen, Germany. | lld:pubmed |
| pubmed-article:16859706 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16859706 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:8460 | entrezgene:pubmed | pubmed-article:16859706 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:16859706 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16859706 | lld:pubmed |
