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We provide evidence that COX4-1 controls BMI1 (show BMI1 Proteins) expression via a redox mechanism
COXIV mRNA (1.6 fold; P<0.01) and COXIV protein expression (1.5 fold; P<0.05) were increased by training but COXIV protein expression was decreased (20%; P<0.01) by acute exercise pre- and post-training.
Identification of three transcription factors that bind a conserved responsive element of the COX4I2 gene, namely recombination signal sequence-binding protein Jkappa (RBPJ (show RBPJ Proteins)), coiled-coil-helix-coiled-coil-helix domain 2 (CHCHD2) and CXXC finger protein 5 (CXXC5 (show CXXC5 Proteins)).
COX (show COX8A Proteins) activity (electron transport complex IV) is reduced by 29% in maternal history of Alzheimer's disease compared to normal controls, and by 30% compared to paternal history of Alzheimer's disease.
Studies suggest a model that links cell signaling with the phosphorylation state of Cytochrome c (Cytc (show CYCS Proteins)) and cytochrome c (show CYCS Proteins) oxidase (COX (show COX8A Proteins)).
Studies suggest that the main function of nuclear encoded subunits of cytochrome c (show CYCS Proteins) oxidase appears to be "only" to control the activity of the mitochondrial subunits.
Studies indicate that the mechanism for proton pumping in cytochrome c (show CYCS Proteins) oxidase is based on an electrostatic analysis of a kinetic experiment for the O to E transition.
Studies indicate that nitric oxide (NO) inhibition of cytochrome c (show CYCS Proteins) oxidase (CcOX (show COX5A Proteins)) is rapid and reversible and may occur in competition with oxygen.
Novel insights into the assembly and function of human nuclear-encoded cytochrome c (show CYCS Proteins) oxidase subunits 4
Data found that subunits Cox6a (show COX6A1 Proteins), Cox6b (show COX6B1 Proteins) and Cox7a (show COX7A1 Proteins) assembled into pre-existing complex IV, while Cox4-1 and Cox6c (show COX6C Proteins) subunits assembled into subcomplexes that may represent rate-limiting intermediates.
Studies indicate that the patterns of charge translocation of cytochrome c (show CYCS Proteins) oxidase coupled to transfer of the 3rd and 4th electrons are very similar.
Studies indicate that mutational amino acid replacement in proton channels, at the negative (N) side of membrane-inserted prokaryotic aa(3 (show ACY3 Proteins)) oxidases, as well as Zn(2+) binding at this site in the bovine oxidase, uncouples proton pumping.
Studies indicate that nitric oxide (NO) binding to reduced ba(3) and bovine cytochrome aa3 (show ACY3 Proteins).
Studies indicate that X-ray structure of heart cytochrome c (show CYCS Proteins) oxidase (CcO (show RYR1 Proteins)) suggest that O(2) molecules are transiently trapped at the Cu(B) site before binding to Fe(a3)(2+) to provide O(2)(-).
Studies indicate that photoexcitation of Ru (II) to Ru(II*) leads to rapid electron transfer to the ferric heme group in cytochrome c (show CYCS Proteins) (Cc), followed by electron transfer to Cu(A) in cytochrome c (show CYCS Proteins) oxidase (CcO (show RYR1 Proteins)) with a rate constant of 60,000s(-1).
Studies suggest for the His291 model of proton pumping in cytochrome c (show CYCS Proteins) oxidase (CcO (show RYR1 Proteins)).
exercise training caused an increase in mRNA and protein levels of COXIV, whereas NAC intervention lowered the two so significantly that even exercise training could not reverse the effect of NAC intervention
Data suggest that that obesity affects both sperm and seminal plasma composition; Cox4i1 mRNA is up-regulated in spermatozoa of obese mice compared to control mice.
Our data suggest that MPP(+) acts on astrocytes in a sex- and brain region-specific manner involving cytochrome c (show CYCS Proteins) oxidase isoform expression in an impairment of energy production and elevated oxidative stress levels
Knockdown of small interfering RNA-mediated COX (show CPOX Proteins) subunit IV decreases progesterone synthesis in steroidogenic cells.
Under conditions of reduced oxygen availability, hypoxia-inducible factor 1 (show HIF1A Proteins) reciprocally regulates COX4 subunit expression by activating transcription of the genes encoding COX4-2 and LON (show LONP1 Proteins), a mitochondrial protease that is required for COX4-1 degradation.
Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It 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 be involved in the regulation and assembly of the complex. This nuclear gene encodes isoform 2 of subunit IV. Isoform 1 of subunit IV is encoded by a different gene, however, the two genes show a similar structural organization. Subunit IV is the largest nuclear encoded subunit which plays a pivotal role in COX regulation.
cytochrome c oxidase subunit 4 isoform 1, mitochondrial
, OXPHOS complex IV subunit IV
, cytochrome c oxidase polypeptide IV
, cytochrome c oxidase subunit IV
, COX IV-1
, cytochrome c oxydase subunit 4
, cytochrome c oxidase, subunit IVa
, cytochrome c oxidase, subunit 4a
, cytochrome c oxidase, subunit IV
, COX IV-2
, cytochrome c oxidase subunit 4 isoform 2, mitochondrial
, cytochrome c oxidase subunit IV-like 2