COX4I2: Difference between revisions

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Latest revision as of 07:19, 10 January 2019

Cytochrome c oxidase subunit 4 isoform 2, mitochondrial is an enzyme that in humans is encoded by the COX4I2 gene.^[1]^[2] COX4I2 is a nuclear-encoded isoform of cytochrome c oxidase (COX) subunit 4. Cytochrome c oxidase (complex IV) is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane, acting as the terminal enzyme of the mitochondrial respiratory chain. Mutations in COX4I2 have been associated with exocrine pancreatic insufficiency, dyserythropoietic anemia, and calvarial hyperostosis (EPIDACH).^[3]^[4]

Structure

COX4I2 is located on the q arm of chromosome 20 in position 11.21 and has 6 exons.^[3] The COX4I2 gene produces a 20 kDa protein composed of 171 amino acids.^[5]^[6] The protein encoded by COX4I2 belongs to the cytochrome c oxidase IV family. COX4I2 has a transit peptide domain and a disulfide bond amino acid modification.^[7]^[8] A Glu138 residue, which corresponds to a Glu136 residue in COX4I1, is believed to be highly conserved and structurally important for the mitochondrial COX response to hypoxia.^[4]

Function

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. The COX4I2 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. It is located on the inner mitochondrial membrane on the matrix side. Expression of COX4I2 is highest in the placenta and the lungs.^[3]^[7]^[8] Additionally, the expression of COX4I2, along with COX4I1, may be regulated by oxygen levels, with reduced levels of oxygen leading to increased COX4I2 expression and COX4I1 degradation. This suggests a role for COX4I2 in the optimization of the electron transfer chain under different conditions.^[9]

Clinical Significance

Mutations in COX4I2 have been associated with exocrine pancreatic insufficiency, dyserythropoeitic anemia, and calvarial hyperostosis (EPIDACH). Characteristics of this disease include pancreatic insufficiency, intestinal malabsorption, failure to thrive, and anemia soon after birth. Additional symptoms have included steatorrhea, splenomegaly and hepatomegaly, pancreatic atrophy, generalized muscle hypotonia, hyperostosis, yellowish sclera associated with mild indirect hyperbilirubinemia, impaired coagulation functions, elevated LDH, alanine, and bilirubin, and reduced vitamin E levels. A homozygous mutation, E138K, has been found to result in reduced COX4I2 expression (25% in fibroblasts) and an impaired response to hypoxia. Functional COX4I2 expression below 40% of its normal level is predicted to be rate-limiting, with the E138K mutation occurring in what is believed to be a highly conserved residue of subunit IV.^[7]^[8]^[4]

Interactions

COX4I2 has been shown to interact with Cytochrome c (CYCS).^[10]^[11]^[12]^[13] Additionally, APP, COA3, and KRAS have been found to have protein-protein interactions with COX4I2.^[14]

References

↑ Hüttemann M, Kadenbach B, Grossman LI (April 2001). "Mammalian subunit IV isoforms of cytochrome c oxidase". Gene. 267 (1): 111–23. doi:10.1016/S0378-1119(01)00385-7. PMID 11311561.
↑ Hüttemann M, Lee I, Liu J, Grossman LI (November 2007). "Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element". The FEBS Journal. 274 (21): 5737–48. doi:10.1111/j.1742-4658.2007.06093.x. PMID 17937768.
↑ ^3.0 ^3.1 ^3.2 "Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)". This article incorporates text from this source, which is in the public domain.
↑ ^4.0 ^4.1 ^4.2 Shteyer E, Saada A, Shaag A, Al-Hijawi FA, Kidess R, Revel-Vilk S, Elpeleg O (March 2009). "Exocrine pancreatic insufficiency, dyserythropoeitic anemia, and calvarial hyperostosis are caused by a mutation in the COX4I2 gene". American Journal of Human Genetics. 84 (3): 412–7. doi:10.1016/j.ajhg.2009.02.006. PMC 2668012. PMID 19268275.
↑ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (October 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
↑ Yao, Daniel. "Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information". amino.heartproteome.org. Retrieved 2018-08-06.
↑ ^7.0 ^7.1 ^7.2 "COX4I2 - Cytochrome c oxidase subunit 4 isoform 2, mitochondrial precursor - Homo sapiens (Human) - COX4I2 gene & protein". www.uniprot.org. Retrieved 2018-08-06.File:CC-BY-icon-80x15.png This article incorporates text available under the CC BY 4.0 license.
↑ ^8.0 ^8.1 ^8.2 "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMC 5210571. PMID 27899622.
↑ Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL (April 2007). "HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells". Cell. 129 (1): 111–22. doi:10.1016/j.cell.2007.01.047. PMID 17418790.
↑ Michel B, Bosshard HR (August 1984). "Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase". The Journal of Biological Chemistry. 259 (16): 10085–91. PMID 6088481.
↑ Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS (March 2000). "Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples". Analytical Biochemistry. 279 (1): 55–60. doi:10.1006/abio.1999.4434. PMID 10683230.
↑ Sampson V, Alleyne T (December 2001). "Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover". European Journal of Biochemistry. 268 (24): 6534–44. doi:10.1046/j.0014-2956.2001.02608.x. PMID 11737208.
↑ Lynch SR, Sherman D, Copeland RA (January 1992). "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase". The Journal of Biological Chemistry. 267 (1): 298–302. PMID 1309738.
↑ Lab, Mike Tyers. "COX4I2 Result Summary | BioGRID". thebiogrid.org. Retrieved 2018-08-06.

External links

Human COX4I2 genome location and COX4I2 gene details page in the UCSC Genome Browser.

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''Cytochrome c oxidase subunit 4 isoform 2, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''COX4I2'' [[gene]].<ref name="pmid11311561">{{cite journal | vauthors = Hüttemann M, Kadenbach B, Grossman LI | title = Mammalian subunit IV isoforms of cytochrome c oxidase | journal = Gene | volume = 267 | issue = 1 | pages = 111–23 | date = April 2001 | pmid = 11311561 | pmc =  | doi = 10.1016/S0378-1119(01)00385-7 }}</ref><ref name="pmid17937768">{{cite journal | vauthors = Hüttemann M, Lee I, Liu J, Grossman LI | title = Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element | journal = The FEBS Journal | volume = 274 | issue = 21 | pages = 5737–48 | date = November 2007 | pmid = 17937768 | pmc =  | doi = 10.1111/j.1742-4658.2007.06093.x }}</ref> COX4I2 is a [[Nuclear gene|nuclear]]-encoded [[Protein isoform|isoform]] of [[cytochrome c oxidase]] (COX) [[Protein subunit|subunit]] 4. Cytochrome c oxidase ([[Cytochrome c oxidase|complex IV]]) is a multi-subunit enzyme complex that couples the transfer of [[electron]]s from [[cytochrome c]] to molecular [[oxygen]] and contributes to a [[hydronium|proton]] [[electrochemical gradient]] across the [[inner mitochondrial membrane]], acting as the terminal enzyme of the [[Mitochondrion|mitochondrial]] [[electron transport chain|respiratory chain]]. Mutations in ''COX4I2'' have been associated with [[exocrine pancreatic insufficiency]], [[Congenital dyserythropoietic anemia|dyserythropoietic anemia]], and [[Craniomandibular osteopathy|calvarial hyperostosis]] (EPIDACH).<ref name="entrez">{{cite web|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84701|title=Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)|access-date=}}{{PD-notice}}</ref><ref name=":0">{{cite journal | vauthors = Shteyer E, Saada A, Shaag A, Al-Hijawi FA, Kidess R, Revel-Vilk S, Elpeleg O | title = Exocrine pancreatic insufficiency, dyserythropoeitic anemia, and calvarial hyperostosis are caused by a mutation in the COX4I2 gene | journal = American Journal of Human Genetics | volume = 84 | issue = 3 | pages = 412–7 | date = March 2009 | pmid = 19268275 | pmc = 2668012 | doi = 10.1016/j.ajhg.2009.02.006 }}</ref>
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Structure ==
-{{GNF_Protein_box
+''COX4I2'' is located on the [[Locus (genetics)|q arm]] of [[chromosome 20]] in position 11.21 and has 6 [[exon]]s.<ref name="entrez" /> The ''COX4I2'' gene produces a 20 kDa [[protein]] composed of 171 [[amino acid]]s.<ref>{{cite journal | vauthors = Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P | title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase | journal = Circulation Research | volume = 113 | issue = 9 | pages = 1043–53 | date = October 2013 | pmid = 23965338 | pmc = 4076475 | doi = 10.1161/CIRCRESAHA.113.301151 }}</ref><ref>{{Cite web|url=https://amino.heartproteome.org/web/protein/Q96KJ9|title=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information|last=Yao|first=Daniel|website=amino.heartproteome.org|access-date=2018-08-06}}</ref> The protein encoded by ''COX4I2'' belongs to the cytochrome c oxidase IV family. ''COX4I2'' has a [[Signal peptide|transit peptide]] domain and a [[disulfide bond]] amino acid modification.<ref name=":1">{{Cite web|url=https://www.uniprot.org/uniprot/Q96KJ9|title=COX4I2 - Cytochrome c oxidase subunit 4 isoform 2, mitochondrial precursor - Homo sapiens (Human) - COX4I2 gene & protein|website=www.uniprot.org|language=en|access-date=2018-08-06}}{{CC-notice|cc=by4}}</ref><ref name=":3">{{cite journal | vauthors =  | title = UniProt: the universal protein knowledgebase | journal = Nucleic Acids Research | volume = 45 | issue = D1 | pages = D158-D169 | date = January 2017 | pmid = 27899622 | pmc = 5210571 | doi = 10.1093/nar/gkw1099 | url = https://doi.org/10.1093/nar/gkw1099 }}</ref> A [[Glutamic acid|Glu]]138 residue, which corresponds to a Glu136 residue in [[COX4I1]], is believed to be [[Conserved sequence|highly conserved]] and structurally important for the mitochondrial COX response to [[Hypoxia (medical)|hypoxia]].<ref name=":0" />
- | image =
- | image_source =
- | PDB =
- | Name = Cytochrome c oxidase subunit IV isoform 2 (lung)
- | HGNCid = 16232
- | Symbol = COX4I2
- | AltSymbols =; COX4; COX4-2; COX4B; COX4L2; COXIV-2; dJ857M17.2
- | OMIM = 607976
- | ECnumber =
- | Homologene = 13082
- | MGIid = 2135755
- | GeneAtlas_image1 = PBB_GE_COX4I2_gnf1h00848_at_tn.png
- | Function = {{GNF_GO|id=GO:0004129 |text = cytochrome-c oxidase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
- | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005751 |text = mitochondrial respiratory chain complex IV}} {{GNF_GO|id=GO:0016020 |text = membrane}}
- | Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0045333 |text = cellular respiration}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 84701
-    | Hs_Ensembl = ENSG00000131055
-    | Hs_RefseqProtein = NP_115998
-    | Hs_RefseqmRNA = NM_032609
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 20
-    | Hs_GenLoc_start = 29689352
-    | Hs_GenLoc_end = 29696470
-    | Hs_Uniprot = Q96KJ9
-    | Mm_EntrezGene = 84682
-    | Mm_Ensembl = ENSMUSG00000009876
-    | Mm_RefseqmRNA = NM_053091
-    | Mm_RefseqProtein = NP_444321
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 2
-    | Mm_GenLoc_start = 152446596
-    | Mm_GenLoc_end = 152456322
-    | Mm_Uniprot = Q91W29
-  }}
-}}
-'''Cytochrome c oxidase subunit IV isoform 2 (lung)''', also known as '''COX4I2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84701| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Function ==
-{{PBB_Summary
-| section_title =
-| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84701| accessdate = }}</ref>
-}}
-==References==
+[[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 [[Heteromer|heteromeric]] complex consisting of 3 [[Catalysis|catalytic]] subunits encoded by [[Mitochondrial DNA|mitochondrial genes]] and multiple structural subunits encoded by [[Nuclear gene|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. The ''COX4I2'' nuclear gene encodes isoform 2 of subunit IV. [[COX4I1|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. It is located on the [[inner mitochondrial membrane]] on the [[Mitochondrial matrix|matrix]] side. Expression of ''COX4I2'' is highest in the [[placenta]] and the [[Lung|lungs]].<ref name="entrez" /><ref name=":1" /><ref name=":3" /> Additionally, the expression of ''COX4I2'', along with ''[[COX4I1]]'', may be regulated by oxygen levels, with reduced levels of oxygen leading to increased ''COX4I2'' expression and COX4I1 degradation. This suggests a role for COX4I2 in the optimization of the [[Electron transport chain|electron transfer chain]] under different conditions.<ref>{{cite journal | vauthors = Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL | title = HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells | journal = Cell | volume = 129 | issue = 1 | pages = 111–22 | date = April 2007 | pmid = 17418790 | doi = 10.1016/j.cell.2007.01.047 }}</ref>
-{{reflist|2}}
-==Further reading==
+== Clinical Significance ==
+Mutations in ''COX4I2'' have been associated with [[exocrine pancreatic insufficiency]], [[Congenital dyserythropoietic anemia|dyserythropoeitic anemia]], and [[Craniomandibular osteopathy|calvarial hyperostosis]] (EPIDACH). Characteristics of this disease include pancreatic insufficiency, intestinal [[malabsorption]], [[failure to thrive]], and [[anemia]] soon after birth. Additional symptoms have included [[steatorrhea]], [[splenomegaly]] and [[hepatomegaly]], pancreatic [[atrophy]], generalized muscle [[hypotonia]], [[hyperostosis]], yellowish [[sclera]] associated with mild indirect hyperbilirubinemia, impaired [[coagulation]] functions, elevated LDH, [[alanine]], and  [[bilirubin]], and reduced [[vitamin E]] levels. A [[Zygosity|homozygous]] [[mutation]], E138K, has been found to result in reduced ''COX4I2'' expression (25% in [[Fibroblast|fibroblasts]]) and an impaired response to [[Hypoxia (medical)|hypoxia]]. Functional ''COX4I2'' expression below 40% of its normal level is predicted to be [[Rate-determining step|rate-limiting]], with the E138K mutation occurring in what is believed to be a [[Conserved sequence|highly conserved]] residue of subunit IV.<ref name=":1" /><ref name=":3" /><ref name=":0" />
+== Interactions ==
+COX4I2 has been shown to [[Protein-protein interaction|interact]] with [[Cytochrome c]] ([[CYCS (gene)|CYCS]]).<ref name=pmid6088481>{{cite journal | vauthors = Michel B, Bosshard HR | title = Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase | journal = The Journal of Biological Chemistry | volume = 259 | issue = 16 | pages = 10085–91 | date = August 1984 | pmid = 6088481 }}</ref><ref name=pmid10683230>{{cite journal | vauthors = Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS | title = Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples | journal = Analytical Biochemistry | volume = 279 | issue = 1 | pages = 55–60 | date = March 2000 | pmid = 10683230 | doi = 10.1006/abio.1999.4434 }}</ref><ref name=pmid11737208>{{cite journal | vauthors = Sampson V, Alleyne T | title = Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover | journal = European Journal of Biochemistry | volume = 268 | issue = 24 | pages = 6534–44 | date = December 2001 | pmid = 11737208 | doi = 10.1046/j.0014-2956.2001.02608.x }}</ref><ref name=pmid1309738>{{cite journal | vauthors = Lynch SR, Sherman D, Copeland RA | title = Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase | journal = The Journal of Biological Chemistry | volume = 267 | issue = 1 | pages = 298–302 | date = January 1992 | pmid = 1309738 }}</ref> Additionally, APP, COA3, and [[KRAS]] have been found to have protein-protein interactions with COX4I2.<ref>{{Cite web|url=https://thebiogrid.org/124215|title=COX4I2 Result Summary {{!}} BioGRID|last=Lab|first=Mike Tyers|website=thebiogrid.org |access-date=2018-08-06}}</ref>
+== References ==
+{{reflist}}
+== External links ==
+* {{UCSC gene info|COX4I2}}
+== Further reading ==
 {{refbegin | 2}}
-{{PBB_Further_reading
+* {{cite journal | vauthors = Garber EA, Margoliash E | title = Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition | journal = Biochimica et Biophysica Acta | volume = 1015 | issue = 2 | pages = 279–87 | date = February 1990 | pmid = 2153405 | doi = 10.1016/0005-2728(90)90032-Y }}
-| citations =
+* {{cite journal | vauthors = Bolli R, Nałecz KA, Azzi A | title = The interconversion between monomeric and dimeric bovine heart cytochrome c oxidase | journal = Biochimie | volume = 67 | issue = 1 | pages = 119–28 | date = January 1985 | pmid = 2986725 | doi = 10.1016/S0300-9084(85)80237-6 }}
-*{{cite journal  | author=Lynch SR, Sherman D, Copeland RA |title=Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 298-302 |year= 1992 |pmid= 1309738 |doi=  }}
+* {{cite journal | vauthors = Michel B, Bosshard HR | title = Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase | journal = The Journal of Biological Chemistry | volume = 259 | issue = 16 | pages = 10085–91 | date = August 1984 | pmid = 6088481 | doi =  }}
-*{{cite journal  | author=Garber EA, Margoliash E |title=Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition. |journal=Biochim. Biophys. Acta |volume=1015 |issue= 2 |pages= 279-87 |year= 1990 |pmid= 2153405 |doi=  }}
+* {{cite journal | vauthors = Hare JF, Ching E, Attardi G | title = Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase | journal = Biochemistry | volume = 19 | issue = 10 | pages = 2023–30 | date = May 1980 | pmid = 6246917 | doi = 10.1021/bi00551a003 }}
-*{{cite journal  | author=Bolli R, Nałecz KA, Azzi A |title=The interconversion between monomeric and dimeric bovine heart cytochrome c oxidase. |journal=Biochimie |volume=67 |issue= 1 |pages= 119-28 |year= 1985 |pmid= 2986725 |doi=  }}
+* {{cite journal | vauthors = Papadopoulou LC, Tsiftsoglou AS | title = Effects of hemin on apoptosis, suppression of cytochrome c oxidase gene expression, and bone-marrow toxicity induced by doxorubicin (adriamycin) | journal = Biochemical Pharmacology | volume = 52 | issue = 5 | pages = 713–22 | date = September 1996 | pmid = 8765469 | doi = 10.1016/0006-2952(96)00349-8 }}
-*{{cite journal  | author=Michel B, Bosshard HR |title=Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase. |journal=J. Biol. Chem. |volume=259 |issue= 16 |pages= 10085-91 |year= 1984 |pmid= 6088481 |doi=  }}
+* {{cite journal | vauthors = Vizirianakis IS, Pappas IS, Tsiftsoglou AS | title = Differentiation-dependent repression of c-myc, B22, COX II and COX IV genes in murine erythroleukemia (MEL) cells | journal = Biochemical Pharmacology | volume = 63 | issue = 5 | pages = 1009–17 | date = March 2002 | pmid = 11911854 | doi = 10.1016/S0006-2952(01)00937-6 }}
-*{{cite journal  | author=Hare JF, Ching E, Attardi G |title=Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase. |journal=Biochemistry |volume=19 |issue= 10 |pages= 2023-30 |year= 1980 |pmid= 6246917 |doi=  }}
-*{{cite journal  | author=Papadopoulou LC, Tsiftsoglou AS |title=Effects of hemin on apoptosis, suppression of cytochrome c oxidase gene expression, and bone-marrow toxicity induced by doxorubicin (adriamycin). |journal=Biochem. Pharmacol. |volume=52 |issue= 5 |pages= 713-22 |year= 1996 |pmid= 8765469 |doi=  }}
-*{{cite journal  | author=Wiedemann FR, Vielhaber S, Schröder R, ''et al.'' |title=Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples. |journal=Anal. Biochem. |volume=279 |issue= 1 |pages= 55-60 |year= 2000 |pmid= 10683230 |doi= 10.1006/abio.1999.4434 }}
-*{{cite journal  | author=Hüttemann M, Kadenbach B, Grossman LI |title=Mammalian subunit IV isoforms of cytochrome c oxidase. |journal=Gene |volume=267 |issue= 1 |pages= 111-23 |year= 2001 |pmid= 11311561 |doi=  }}
-*{{cite journal  | author=Sampson V, Alleyne T |title=Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover. |journal=Eur. J. Biochem. |volume=268 |issue= 24 |pages= 6534-44 |year= 2002 |pmid= 11737208 |doi=  }}
-*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
-*{{cite journal  | author=Vizirianakis IS, Pappas IS, Tsiftsoglou AS |title=Differentiation-dependent repression of c-myc, B22, COX II and COX IV genes in murine erythroleukemia (MEL) cells. |journal=Biochem. Pharmacol. |volume=63 |issue= 5 |pages= 1009-17 |year= 2002 |pmid= 11911854 |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=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=Fukuda R, Zhang H, Kim JW, ''et al.'' |title=HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. |journal=Cell |volume=129 |issue= 1 |pages= 111-22 |year= 2007 |pmid= 17418790 |doi= 10.1016/j.cell.2007.01.047 }}
-}}
 {{refend}}
-{{protein-stub}}
+{{NLM content}}
-{{WikiDoc Sources}}
+{{Portal bar|Mitochondria|Gene Wiki|border=no}}