| pubmed-article:16982196 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16982196 | lifeskim:mentions | umls-concept:C1325742 | lld:lifeskim |
| pubmed-article:16982196 | lifeskim:mentions | umls-concept:C0009968 | lld:lifeskim |
| pubmed-article:16982196 | lifeskim:mentions | umls-concept:C1420182 | lld:lifeskim |
| pubmed-article:16982196 | lifeskim:mentions | umls-concept:C0003737 | lld:lifeskim |
| pubmed-article:16982196 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16982196 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:16982196 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:16982196 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:16982196 | pubmed:dateCreated | 2006-10-30 | lld:pubmed |
| pubmed-article:16982196 | pubmed:abstractText | Copper is essential for biological processes such as free radical detoxification, mitochondrial respiration and iron metabolism. A central player in copper homeostasis is the high-affinity integral plasma membrane copper transporter Ctr1. However, the precise mechanisms by which Ctr1 functions are not known. Here, we highlight an important breakthrough in our understanding of how Ctr1 facilitates Cu(I) movement across membranes: the publication of structural details for human Ctr1 obtained from 2D crystallography and electron microscopy. | lld:pubmed |
| pubmed-article:16982196 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16982196 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16982196 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16982196 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16982196 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16982196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16982196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16982196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16982196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16982196 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16982196 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16982196 | pubmed:issn | 0968-0004 | lld:pubmed |
| pubmed-article:16982196 | pubmed:author | pubmed-author:NoseYasuhiroY | lld:pubmed |
| pubmed-article:16982196 | pubmed:author | pubmed-author:ThieleDennis... | lld:pubmed |
| pubmed-article:16982196 | pubmed:author | pubmed-author:ReesErin MEM | lld:pubmed |
| pubmed-article:16982196 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16982196 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:16982196 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16982196 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16982196 | pubmed:pagination | 604-7 | lld:pubmed |
| pubmed-article:16982196 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
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| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:meshHeading | pubmed-meshheading:16982196... | lld:pubmed |
| pubmed-article:16982196 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16982196 | pubmed:articleTitle | Structure of the Ctr1 copper trans'PORE'ter reveals novel architecture. | lld:pubmed |
| pubmed-article:16982196 | pubmed:affiliation | Department of Pharmacology and Cancer Biology, Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Research Drive-LSRC C351, Durham, NC 27710-3813, USA. | lld:pubmed |
| pubmed-article:16982196 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16982196 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16982196 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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