pubmed-article:16120310 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C0684063 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C0030664 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C0022095 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C0005495 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:16120310 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
pubmed-article:16120310 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:16120310 | pubmed:dateCreated | 2005-8-25 | lld:pubmed |
pubmed-article:16120310 | pubmed:abstractText | Iron-sulfur (Fe-S) clusters are ubiquitous co-factors of proteins that play an important role in metabolism, electron-transfer and regulation of gene expression. In eukaryotes mitochondria are the primary site of Fe-S cluster biogenesis. The organelles contain some ten proteins of the so-called iron-sulfur cluster (ISC) assembly machinery that is well-conserved in bacteria and eukaryotes. The ISC assembly machinery is responsible for biogenesis of Fe-S proteins within mitochondria. In addition, this machinery is involved in the maturation of extra-mitochondrial Fe-S proteins by cooperating with mitochondrial proteins with an exclusive function in this process. This review summarizes recent developments in our understanding of the biogenesis of cellular Fe-S proteins in eukaryotes. Particular emphasis is given to disorders in Fe-S protein biogenesis causing human disease. | lld:pubmed |
pubmed-article:16120310 | pubmed:language | eng | lld:pubmed |
pubmed-article:16120310 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16120310 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
pubmed-article:16120310 | pubmed:month | Nov | lld:pubmed |
pubmed-article:16120310 | pubmed:issn | 1567-7249 | lld:pubmed |
pubmed-article:16120310 | pubmed:author | pubmed-author:LillRolandR | lld:pubmed |
pubmed-article:16120310 | pubmed:author | pubmed-author:GerberJanaJ | lld:pubmed |
pubmed-article:16120310 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16120310 | pubmed:volume | 2 | lld:pubmed |
pubmed-article:16120310 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16120310 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16120310 | pubmed:pagination | 71-86 | lld:pubmed |
pubmed-article:16120310 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:16120310 | pubmed:articleTitle | Biogenesis of iron-sulfur proteins in eukaryotes: components, mechanism and pathology. | lld:pubmed |
pubmed-article:16120310 | pubmed:affiliation | Institut für Zytobiologie und Zytopathologie der Philipps-Universität Marburg, Robert-Koch-Strasse 5, 35033 Marburg, Germany. | lld:pubmed |
pubmed-article:16120310 | pubmed:publicationType | Journal Article | lld:pubmed |
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