pubmed-article:16824008 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C0684063 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C0022095 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C0005495 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:16824008 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:16824008 | pubmed:dateCreated | 2006-10-10 | lld:pubmed |
pubmed-article:16824008 | pubmed:abstractText | Iron-sulfur (Fe/S) clusters require a complex set of proteins to become assembled and incorporated into apoproteins in a living cell. Researchers have described three distinct assembly systems in eukaryotes that are involved in the maturation of cellular Fe/S proteins. Mitochondria are central for biogenesis. They contain the ISC-the iron-sulfur cluster assembly machinery that was inherited from a similar system of eubacteria in evolution and is involved in biogenesis of all cellular Fe/S proteins. The basic principle of mitochondrial (and bacterial) Fe/S protein maturation is the synthesis of the Fe/S cluster on a scaffold protein before the cluster is transferred to apoproteins. Biogenesis of cytosolic and nuclear Fe/S proteins is facilitated by the cytosolic iron-sulfur protein assembly (CIA) apparatus. This process requires the participation of mitochondria that export a still unknown component via the ISC export machinery, including an ABC transporter. | lld:pubmed |
pubmed-article:16824008 | pubmed:language | eng | lld:pubmed |
pubmed-article:16824008 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16824008 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:16824008 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16824008 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16824008 | pubmed:issn | 1081-0706 | lld:pubmed |
pubmed-article:16824008 | pubmed:author | pubmed-author:LillRolandR | lld:pubmed |
pubmed-article:16824008 | pubmed:author | pubmed-author:MühlenhoffUlr... | lld:pubmed |
pubmed-article:16824008 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16824008 | pubmed:volume | 22 | lld:pubmed |
pubmed-article:16824008 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16824008 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16824008 | pubmed:pagination | 457-86 | lld:pubmed |
pubmed-article:16824008 | pubmed:meshHeading | pubmed-meshheading:16824008... | lld:pubmed |
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pubmed-article:16824008 | pubmed:meshHeading | pubmed-meshheading:16824008... | lld:pubmed |
pubmed-article:16824008 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16824008 | pubmed:articleTitle | Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. | lld:pubmed |
pubmed-article:16824008 | pubmed:affiliation | Institut für Zytobiologie, Philipps Universität Marburg, 35037 Marburg, Germany. lill@staff.uni-marburg.de | lld:pubmed |
pubmed-article:16824008 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16824008 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:16824008 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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