COX17

COX17

COX17 cytochrome c oxidase assembly homolog (S. cerevisiae), also known as COX17, is a human gene.cite web | title = Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10063| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10063| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Amaravadi R, Glerum DM, Tzagoloff A |title=Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment. |journal=Hum. Genet. |volume=99 |issue= 3 |pages= 329–33 |year= 1997 |pmid= 9050918 |doi=
*cite journal | author=Punter FA, Adams DL, Glerum DM |title=Characterization and localization of human COX17, a gene involved in mitochondrial copper transport. |journal=Hum. Genet. |volume=107 |issue= 1 |pages= 69–74 |year= 2000 |pmid= 10982038 |doi=
*cite journal | author=Horvath R, Lochmüller H, Stucka R, "et al." |title=Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 2 |pages= 530–3 |year= 2000 |pmid= 11027508 |doi= 10.1006/bbrc.2000.3495
*cite journal | author=Kako K, Tsumori K, Ohmasa Y, "et al." |title=The expression of Cox17p in rodent tissues and cells. |journal=Eur. J. Biochem. |volume=267 |issue= 22 |pages= 6699–707 |year= 2000 |pmid= 11054125 |doi=
*cite journal | author=Heaton DN, George GN, Garrison G, Winge DR |title=The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. |journal=Biochemistry |volume=40 |issue= 3 |pages= 743–51 |year= 2001 |pmid= 11170391 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Suzuki C, Daigo Y, Kikuchi T, "et al." |title=Identification of COX17 as a therapeutic target for non-small cell lung cancer. |journal=Cancer Res. |volume=63 |issue= 21 |pages= 7038–41 |year= 2004 |pmid= 14612491 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Kako K, Takehara A, Arai H, "et al." |title=A selective requirement for copper-dependent activation of cytochrome c oxidase by Cox17p. |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 4 |pages= 1379–85 |year= 2005 |pmid= 15504366 |doi= 10.1016/j.bbrc.2004.09.211
*cite journal | author=Arnesano F, Balatri E, Banci L, "et al." |title=Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. |journal=Structure |volume=13 |issue= 5 |pages= 713–22 |year= 2005 |pmid= 15893662 |doi= 10.1016/j.str.2005.02.015
*cite journal | author=Stelzl U, Worm U, Lalowski M, "et al." |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Cobine PA, Pierrel F, Leary SC, "et al." |title=The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding. |journal=J. Biol. Chem. |volume=281 |issue= 18 |pages= 12270–6 |year= 2006 |pmid= 16520371 |doi= 10.1074/jbc.M600496200
*cite journal | author=Ma J, Dempsey AA, Stamatiou D, "et al." |title=Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects. |journal=Atherosclerosis |volume=191 |issue= 1 |pages= 63–72 |year= 2007 |pmid= 16806233 |doi= 10.1016/j.atherosclerosis.2006.05.032
*cite journal | author=Voronova A, Kazantseva J, Tuuling M, "et al." |title=Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulphide adducts with thiol reagents. |journal=Protein Expr. Purif. |volume=53 |issue= 1 |pages= 138–44 |year= 2007 |pmid= 17208454 |doi= 10.1016/j.pep.2006.11.014
*cite journal | author=Voronova A, Meyer-Klaucke W, Meyer T, "et al." |title=Oxidative switches in functioning of mammalian copper chaperone Cox17. |journal=Biochem. J. |volume=408 |issue= 1 |pages= 139–48 |year= 2007 |pmid= 17672825 |doi= 10.1042/BJ20070804

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