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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

COX15 homolog, cytochrome c oxidase assembly protein

COX15, Cox15p
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 essential for the biogenesis of COX formation and may function in the hydroxylation of heme O, according to the yeast mutant studies. This protein is predicted to contain 5 transmembrane domains localized in the mitochondrial inner membrane. Alternative splicing of this gene generates two transcript variants diverging in the 3' region. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on COX15
Analysis of the genes coding for subunit 10 and 15 of cytochrome c oxidase in Alzheimer's disease.
GeneRIF
Finazzi et al., Brescia, Italy. In J Neural Transm, 2009
COX 15 mRNA was significantly more abundant in the cerebral tissue of Alzheimer's disease (AD) patients and COX10 and COX15 SNP were significantly less represented in the patient group, suggesting a possible protective role toward the risk for AD
Expression of the alternative oxidase complements cytochrome c oxidase deficiency in human cells.
GeneRIF
Rustin et al., Paris, France. In Embo Mol Med, 2009
The expression of the AOX, well-tolerated by the cells, compensates for both the growth defect and the pronounced oxidant-sensitivity of COX-deficient human cells.
Regulation of the heme A biosynthetic pathway: differential regulation of heme A synthase and heme O synthase in Saccharomyces cerevisiae.
GeneRIF
Hegg et al., East Lansing, United States. In J Biol Chem, 2009
COX10, the physiological partner of COX15, does not share the same regulatory mechanism with COX15
Enhancement of cell proliferation in various mammalian cell lines by gene insertion of a cyclin-dependent kinase homolog.
GeneRIF
Shiloach et al., Bethesda, United States. In Bmc Biotechnol, 2006
cdkl3 transfected in anchorage-independent (suspension) HeLa cells overexpressed relative to attached cells and lead to elevated proliferation and viability relative to untransfected. Same in two HEK-293 and a CHO cell lines.
Functional and genetic studies demonstrate that mutation in the COX15 gene can cause Leigh syndrome.
GeneRIF
Brown et al., In J Med Genet, 2004
A patient with typical clinical and neuroradiological features of Leigh syndrome and cytochrome oxidase deficiency was found to have a mutation in the COX15 gene.
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