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http://purl.uniprot.org/citations/36952351http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36952351http://www.w3.org/2000/01/rdf-schema#comment"The orchestrated activity of the mitochondrial respiratory or electron transport chain (ETC) and ATP synthase convert reduction power (NADH, FADH2) into ATP, the cell's energy currency in a process named oxidative phosphorylation (OXPHOS). Three out of the four ETC complexes are found in supramolecular assemblies: complex I, III, and IV form the respiratory supercomplexes (SC). The plasticity model suggests that SC formation is a form of adaptation to changing conditions such as energy supply, redox state, and stress. Complex I, the NADH-dehydrogenase, is part of the largest supercomplex (CI + CIII2 + CIVn). Here, we demonstrate the role of NDUFB10, a subunit of the membrane arm of complex I, in complex I and supercomplex assembly on the one hand and bioenergetics function on the other. NDUFB10 knockout was correlated with a decrease of SCAF1, a supercomplex assembly factor, and a reduction of respiration and mitochondrial membrane potential. This likely is due to loss of proton pumping since the CI P P -module is downregulated and the P D -module is completely abolished in NDUFB10 knock outs."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.org/dc/terms/identifier"doi:10.1515/hsz-2022-0309"xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Hippler M."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Scholz M."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Enriquez J.A."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Psathaki O.E."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Busch K.B."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Marx N."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Arroum T."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Borowski M.T."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/author"Schmelter F."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/name"Biol Chem"xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/pages"399-415"xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/title"Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation."xsd:string
http://purl.uniprot.org/citations/36952351http://purl.uniprot.org/core/volume"404"xsd:string
http://purl.uniprot.org/citations/36952351http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/36952351
http://purl.uniprot.org/citations/36952351http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/36952351
http://purl.uniprot.org/uniprot/#_A8K761-mappedCitation-36952351http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36952351
http://purl.uniprot.org/uniprot/#_O96000-mappedCitation-36952351http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36952351
http://purl.uniprot.org/uniprot/#_Q96RX5-mappedCitation-36952351http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36952351
http://purl.uniprot.org/uniprot/A8K761http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36952351
http://purl.uniprot.org/uniprot/O96000http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36952351
http://purl.uniprot.org/uniprot/Q96RX5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36952351