| pubmed-article:15381069 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15381069 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:15381069 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
| pubmed-article:15381069 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:15381069 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:15381069 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15381069 | pubmed:dateCreated | 2004-9-21 | lld:pubmed |
| pubmed-article:15381069 | pubmed:abstractText | An important step in copper homeostasis is delivery of copper to a specific P-type ATPase in the Golgi apparatus (Ccc2 in yeast, ATP7A and ATP7B in humans) by a small copper chaperone protein (Atx1 in yeast, ATOX1 in humans). Atx1 and ATOX1 both contain an MXCXXC motif that is also present in Ccc2 (two motifs) and ATP7A/B (six motifs). Protein-protein interactions probably require coordination of one Cu(I) by cysteines from both MXCXXC motifs. We applied yeast two-hybrid analysis to screen systematically all possible interactions between MXCXXC-containing domains in these proteins. We demonstrate that ATOX1 and Atx1 preferentially interact with domains 2 and 4 of ATP7B and that Atx1 interacts with both Ccc2 domains. All combinations show a remarkable bell-shaped dependency on copper concentration that is maximal just below normal copper levels. Our results suggest that yeast two-hybrid analysis can be used to study the intracellular copper status of a cell. | lld:pubmed |
| pubmed-article:15381069 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15381069 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15381069 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15381069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15381069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15381069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15381069 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15381069 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15381069 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15381069 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:15381069 | pubmed:author | pubmed-author:MerkxMaartenM | lld:pubmed |
| pubmed-article:15381069 | pubmed:author | pubmed-author:KlompLeo W... | lld:pubmed |
| pubmed-article:15381069 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:15381069 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15381069 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:15381069 | pubmed:volume | 323 | lld:pubmed |
| pubmed-article:15381069 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15381069 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15381069 | pubmed:pagination | 789-95 | lld:pubmed |
| pubmed-article:15381069 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15381069 | pubmed:meshHeading | pubmed-meshheading:15381069... | lld:pubmed |
| pubmed-article:15381069 | pubmed:meshHeading | pubmed-meshheading:15381069... | lld:pubmed |
| pubmed-article:15381069 | pubmed:meshHeading | pubmed-meshheading:15381069... | lld:pubmed |
| pubmed-article:15381069 | pubmed:meshHeading | pubmed-meshheading:15381069... | lld:pubmed |
| pubmed-article:15381069 | pubmed:meshHeading | pubmed-meshheading:15381069... | lld:pubmed |
| pubmed-article:15381069 | pubmed:meshHeading | pubmed-meshheading:15381069... | lld:pubmed |
| pubmed-article:15381069 | pubmed:meshHeading | pubmed-meshheading:15381069... | lld:pubmed |
| pubmed-article:15381069 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15381069 | pubmed:articleTitle | Copper-dependent protein-protein interactions studied by yeast two-hybrid analysis. | lld:pubmed |
| pubmed-article:15381069 | pubmed:affiliation | Laboratory of Macromolecular and Organic Chemistry, Department of Biomedical Engineering, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven, The Netherlands. | lld:pubmed |
| pubmed-article:15381069 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15381069 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15381069 | pubmed:publicationType | Evaluation Studies | lld:pubmed |
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