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Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. Zusätzlich bieten wir Ihnen COX17 Antikörper (45) und COX17 Proteine (8) und viele weitere Produktgruppen zu diesem Protein an.
These results collectively indicate that Cox17 might not participate in the action of these anticancer organoruthenium complexes, and further verify the distinct anticancer mechanism of the organoruthenium(II) complexes from cisplatin.
In addition to Atox1 (zeige ATOX1 ELISA Kits), the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (zeige SOD1 ELISA Kits) (i.e. CCS (zeige CCS ELISA Kits)) and cytochrome c (zeige CYCS ELISA Kits) oxidase in mitochondria (i.e. Cox17). [review]
Data show that the redox state of cytochrome c oxidase assembly protein 17 (Cox17), mitochondrial membrane transport protein Mia40 (zeige CHCHD4 ELISA Kits) and superoxide dismutase 1 (SOD1 (zeige SOD1 ELISA Kits)) in the cytoplasm were directly observed with in-cell NMR spectroscopy.
Data suggest that Cox17 enhances the reactivity of some platinum/organoplatinum antineoplastic drugs but suppresses the reactivity of at least one platinum antineoplastic drug; glutathione modulates binding of platinum/organoplatinum drugs to Cox17.
CTR1 (zeige SLC31A1 ELISA Kits) silencing increased the protein levels of copper chaperone ATOX1 (zeige ATOX1 ELISA Kits) and copper chaperone for superoxide dismutase (zeige CCS ELISA Kits) 1 (zeige SOD1 ELISA Kits) (CCS (zeige CCS ELISA Kits)-1), but decreased copper chaperone for cytochrome c (zeige CYCS ELISA Kits) oxidase (COX17).
Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective.
Data imply that up-regulation of COX17 function and increased cytochrome c (zeige CYCS ELISA Kits) oxidase activity are frequent features of lung carcinogenesis.
The binding of copper to Cox17 is needed to activate cytochrome c (zeige CYCS ELISA Kits) oxidase by Cox17.
Cox17-mediated copper metallation of Sco1, as well as the subsequent failure of Cu(A) site maturation, is the basis for the inefficient assembly of the cytochrome c oxidase complex in SCO1 patients
Cox17 was studied with regard to its expression, purification, and formation of mixed disulfide adducts with sulfhydryl reagents.
Sp1 (zeige SP1 ELISA Kits), NRF-1 (zeige NRF1 ELISA Kits) and NRF-2 (zeige NFE2L2 ELISA Kits) are involved in basal transcription, similar to the transcription mechanism of other CCO (zeige RYR1 ELISA Kits)-related genes
cox17 has a role in activating cytochrome c (zeige CYCS ELISA Kits) oxidase in mice
Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.
cytochrome c oxidase copper chaperone
, COX17 homolog, cytochrome c oxidase assembly protein
, COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)
, COX17 homolog, cytochrome c oxidase assembly protein (yeast)
, COX17 cytochrome c oxidase assembly homolog
, cytochrome c oxidase 17 copper chaperone
, cytochrome c oxidase assembly homolog 17
, human homolog of yeast mitochondrial copper recruitment
, cytochrome c oxidase, subunit XVII assembly protein homolog
, cytochrome c oxidase subunit XVII assembly protein homolog