| pubmed-article:12880202 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12880202 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:12880202 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:12880202 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:12880202 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12880202 | lifeskim:mentions | umls-concept:C0441587 | lld:lifeskim |
| pubmed-article:12880202 | pubmed:issue | 4-5 | lld:pubmed |
| pubmed-article:12880202 | pubmed:dateCreated | 2003-7-25 | lld:pubmed |
| pubmed-article:12880202 | pubmed:abstractText | The inner membrane of mitochondria harbours a large number of polypeptides, many of which have evolved from proteins of the prokaryotic progenitors of mitochondria. The sorting routes on which these proteins are integrated into the mitochondrial inner membrane reflect their phylogenetic origin: Proteins of eukaryotic descent typically reach their destination following arrest of import at the level of the inner membrane. In contrast, many proteins inherited from the prokaryotic progenitor cell are inserted into the inner membrane in an export step following translocation into the matrix. Recently, three different insertion pathways from the matrix into the inner membrane were identified which show considerable parallels to the protein insertion processes in bacteria and chloroplasts. Two of these pathways depend on the related inner membrane proteins Oxa1 and Cox18. A third route is less well defined and depends on the membrane-associated matrix protein Mba1. | lld:pubmed |
| pubmed-article:12880202 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12880202 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12880202 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12880202 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12880202 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12880202 | pubmed:issn | 1521-6543 | lld:pubmed |
| pubmed-article:12880202 | pubmed:author | pubmed-author:NeupertWalter... | lld:pubmed |
| pubmed-article:12880202 | pubmed:author | pubmed-author:HerrmannJohan... | lld:pubmed |
| pubmed-article:12880202 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12880202 | pubmed:volume | 55 | lld:pubmed |
| pubmed-article:12880202 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12880202 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12880202 | pubmed:pagination | 219-25 | lld:pubmed |
| pubmed-article:12880202 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12880202 | pubmed:meshHeading | pubmed-meshheading:12880202... | lld:pubmed |
| pubmed-article:12880202 | pubmed:meshHeading | pubmed-meshheading:12880202... | lld:pubmed |
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| pubmed-article:12880202 | pubmed:meshHeading | pubmed-meshheading:12880202... | lld:pubmed |
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| pubmed-article:12880202 | pubmed:meshHeading | pubmed-meshheading:12880202... | lld:pubmed |
| pubmed-article:12880202 | pubmed:articleTitle | Protein insertion into the inner membrane of mitochondria. | lld:pubmed |
| pubmed-article:12880202 | pubmed:affiliation | Institut für Physiologische Chemie, Butenandt. 5, 81377 München, Germany. | lld:pubmed |
| pubmed-article:12880202 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12880202 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:12880202 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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