Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification.
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Mass-spectrometry analysis of immunopurified human Complex I resolved the human homologues of the beef-heart complex I polypeptides, including the ESSS subunit (NDUFB11 / Np17.3), establishing NDUFB11 as an integral subunit.
"we can resolve and identify the human homologues of 42 polypeptides detected so far in the more extensively studied beef heart complex I."
A proteome-scale map of the human interactome network.
Accessory subunits are integral for assembly and function of human mitochondrial complex I.
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Gene-editing knockouts and quantitative proteomics demonstrated that accessory subunits, including NDUFB11, are integral for the assembly and function of human Complex I; loss of a subunit destabilizes others in the same structural module.
"Accessory subunits are integral for assembly and function of human mitochondrial complex I."
Architecture of Human Mitochondrial Respiratory Megacomplex I(2)III(2)IV(2).
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Cryo-EM of the human respiratory megacomplex resolved the precise assignment of individual Complex I subunits, placing NDUFB11 within the membrane arm of the inner-membrane-embedded complex.
"The structure not only reveals the precise assignment of individual subunits of human CI and CIII"
Assembly of mammalian oxidative phosphorylation complexes I-V and supercomplexes.
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Review of OXPHOS assembly noting that human respiratory complexes comprise catalytic core proteins plus numerous supernumerary subunits that play essential roles in assembly, regulation and stability.
"a large number of 'supernumerary' subunits that play essential roles in assembly, regulation and stability."
BAP31 regulates mitochondrial function via interaction with Tom40 within ER-mitochondria contact sites.
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BAP31 (BCAP31) forms an ER-mitochondria bridging complex that stimulates Complex I biogenesis; disrupting the BAP31-Tom40 complex reduces Complex I activity. NDUFB11 interacts with BCAP31 and is localized to mitochondria/inner membrane in this study.
"Disruption of the BAP31-Tom40 complex inhibits mitochondrial complex I activity"
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Complex I oxidises NADH to NAD+, reduces CoQ to CoQH2
Intermediate 1 binds HP subcomplex to form Intermediate 2
Peripheral arm subunits bind the 815kDa complex to form a 980kDa complex
Intermediate 2 binds MT-ND1:NDUFAF5:NDUFAF6 to form a 315kDa subcomplex
The MCIA complex, NDUFAF2-7 all dissociate from the 980kDa complex, resulting in Complex I
ND4, ND5 bind the 550kDa complex to form the 815kDa complex
The 315kDa subcomplex binds the 370kDa subcomplex to form the 550kDa complex