| pubmed-article:16267171 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16267171 | lifeskim:mentions | umls-concept:C0015450 | lld:lifeskim |
| pubmed-article:16267171 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
| pubmed-article:16267171 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16267171 | lifeskim:mentions | umls-concept:C0009968 | lld:lifeskim |
| pubmed-article:16267171 | lifeskim:mentions | umls-concept:C1427858 | lld:lifeskim |
| pubmed-article:16267171 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:16267171 | pubmed:dateCreated | 2005-11-21 | lld:pubmed |
| pubmed-article:16267171 | pubmed:abstractText | Copper is an essential transition metal but is toxic in excess; therefore, its metabolism needs to be tightly regulated. Defects in the regulation of copper can lead to various disorders characterized by copper deficiency or copper excess. Recently, we characterized the COMMD1 (previously MURR1) gene as the defective gene in canine copper toxicosis. The molecular functions of COMMD1 remain unknown, but significant progress has been made in identifying the cellular processes in which COMMD1 participates, through the identification of proteins interacting with COMMD1. This review discusses how COMMD1 functions as a regulator of not only copper homeostasis but also sodium transport and the NF-kappaB signaling pathway. We outline the possible mechanisms through which COMMD1 exerts these newly identified functions. | lld:pubmed |
| pubmed-article:16267171 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16267171 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16267171 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16267171 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16267171 | pubmed:issn | 0022-1503 | lld:pubmed |
| pubmed-article:16267171 | pubmed:author | pubmed-author:WijmengaCC | lld:pubmed |
| pubmed-article:16267171 | pubmed:author | pubmed-author:KlompLL | lld:pubmed |
| pubmed-article:16267171 | pubmed:author | pubmed-author:van de... | lld:pubmed |
| pubmed-article:16267171 | pubmed:author | pubmed-author:de BiePP | lld:pubmed |
| pubmed-article:16267171 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16267171 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:16267171 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16267171 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16267171 | pubmed:pagination | 803-11 | lld:pubmed |
| pubmed-article:16267171 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16267171 | pubmed:meshHeading | pubmed-meshheading:16267171... | lld:pubmed |
| pubmed-article:16267171 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16267171 | pubmed:articleTitle | The many faces of the copper metabolism protein MURR1/COMMD1. | lld:pubmed |
| pubmed-article:16267171 | pubmed:affiliation | Complex Genetics Section, DBG-Department of Medical Genetics, University Medical Center, 3508 TA Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:16267171 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16267171 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:16267171 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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