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| http://purl.uniprot.org/citations/19944477 | http://www.w3.org/2000/01/rdf-schema#comment | "The translocase of the outer mitochondrial membrane (TOM complex) is a multi-subunit complex that serves as the general entry site for newly synthesized proteins into the organelle. The assembly of this complex is a multi-step process that requires the coordinated action of several proteins. A central, but rather undefined role in this process is played by Mim1, a mitochondrial outer membrane protein. The deletion of MIM1 leads to severe defects in the biogenesis of TOM complex subunits and to altered mitochondrial morphology. The protein is built from an N-terminal cytosolic domain, a central transmembrane segment, and a C-terminal domain facing the intermembrane space. In this review we summarize our current knowledge on the structure-function relationship of Mim1 and discuss some possibilities for its molecular function."xsd:string |
| http://purl.uniprot.org/citations/19944477 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.ejcb.2009.11.002"xsd:string |
| http://purl.uniprot.org/citations/19944477 | http://purl.uniprot.org/core/author | "Rapaport D."xsd:string |
| http://purl.uniprot.org/citations/19944477 | http://purl.uniprot.org/core/author | "Stefan Dimmer K."xsd:string |
| http://purl.uniprot.org/citations/19944477 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/19944477 | http://purl.uniprot.org/core/name | "Eur J Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/19944477 | http://purl.uniprot.org/core/pages | "212-215"xsd:string |
| http://purl.uniprot.org/citations/19944477 | http://purl.uniprot.org/core/title | "The enigmatic role of Mim1 in mitochondrial biogenesis."xsd:string |
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