http://purl.uniprot.org/citations/19628817 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19628817 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19628817 | http://www.w3.org/2000/01/rdf-schema#comment | "Mammalian mitochondria contain about 1100 proteins, nearly 300 of which are uncharacterized. Given the well-established role of mitochondrial defects in human disease, functional characterization of these proteins may shed new light on disease mechanisms. Starting with yeast as a model system, we investigated an uncharacterized but highly conserved mitochondrial protein (named here Sdh5). Both yeast and human Sdh5 interact with the catalytic subunit of the succinate dehydrogenase (SDH) complex, a component of both the electron transport chain and the tricarboxylic acid cycle. Sdh5 is required for SDH-dependent respiration and for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor). Germline loss-of-function mutations in the human SDH5 gene, located on chromosome 11q13.1, segregate with disease in a family with hereditary paraganglioma, a neuroendocrine tumor previously linked to mutations in genes encoding SDH subunits. Thus, a mitochondrial proteomics analysis in yeast has led to the discovery of a human tumor susceptibility gene."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1175689"xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1175689"xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Dephoure N."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Dephoure N."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Devilee P."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Devilee P."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Gygi S.P."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Gygi S.P."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Kremer H."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Kremer H."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Winge D.R."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Winge D.R."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Cremers C.W.R.J."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Cremers C.W.R.J."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Rutter J."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Rutter J."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Khalimonchuk O."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Khalimonchuk O."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Schraders M."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Schraders M."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Bayley J.-P."xsd:string |
http://purl.uniprot.org/citations/19628817 | http://purl.uniprot.org/core/author | "Bayley J.-P."xsd:string |