{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T20:46:38Z","timestamp":1783629998929,"version":"3.55.0"},"reference-count":31,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[1998,9,1]],"date-time":"1998-09-01T00:00:00Z","timestamp":904608000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[1998,9,1]],"date-time":"1998-09-01T00:00:00Z","timestamp":904608000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biometals"],"published-print":{"date-parts":[[1998,9]]},"DOI":"10.1023\/a:1009274131473","type":"journal-article","created":{"date-parts":[[2003,3,18]],"date-time":"2003-03-18T20:12:43Z","timestamp":1048018363000},"page":"207-212","source":"Crossref","is-referenced-by-count":48,"title":["Decrease of cytochrome c oxidase protein in heart mitochondria of copper-deficient rats"],"prefix":"10.1007","volume":"11","author":[{"given":"Luisa","family":"Rossi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giovanna","family":"Lippe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eliana","family":"Marchese","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angelo","family":"De Martino","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Mavelli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giuseppe","family":"Rotilio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria R","family":"Ciriolo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","reference":[{"key":"182011_CR1","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1007\/s004390050367","volume":"99","author":"R Amaravadi","year":"1997","unstructured":"Amaravadi R, Glerum DM, Tzagoloff A. 1997 Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment. Hum Genet\n99, 329-333.","journal-title":"Hum Genet"},{"key":"182011_CR2","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/0092-8674(94)90346-8","volume":"76","author":"C Askwith","year":"1994","unstructured":"Askwith C, Eide DE, Van Ho A, et al. 1994 The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell\n76, 403-410.","journal-title":"Cell"},{"key":"182011_CR3","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/0003-9861(90)90326-T","volume":"280","author":"A Azzi","year":"1990","unstructured":"Azzi A, Muller M. 1990 Cytochrome c oxidase polypeptide composition, role of subunits, and location of active metal centers. Arch Biochem Biophys\n280, 242-251.","journal-title":"Arch Biochem Biophys"},{"key":"182011_CR4","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1097\/00005792-199205000-00004","volume":"71","author":"GJ Brewer","year":"1992","unstructured":"Brewer GJ, Yuzbasiyan-Gurkan V. 1992 Wilson disease. Medicine\n71, 139-164.","journal-title":"Medicine"},{"key":"182011_CR5","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/0014-5793(91)80131-L","volume":"2278","author":"MT Carr\u00ec","year":"1991","unstructured":"Carr\u00ec MT, Galiazzo F, Ciriolo MR, Rotilio G. 1991 Evidence for co-regulation of Cu, Zn superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE 1 factor. FEBS Lett\n2278, 263-266.","journal-title":"FEBS Lett"},{"key":"182011_CR6","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/S0021-9258(18)44883-1","volume":"189","author":"SJ Cooperstein","year":"1951","unstructured":"Cooperstein SJ, Lazarow A. 1951 A microspectrophotometric method for the determination of cytochrome oxidase. J Biol Chem\n189, 665-670.","journal-title":"J Biol Chem"},{"key":"182011_CR7","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0925-4439(96)00064-6","volume":"1360","author":"M DiDonato","year":"1997","unstructured":"DiDonato M, Sarkar B. 1997 Copper transport and its alterations in Menkes and Wilson diseases. Biochim Biophys Acta\n1360, 3-16.","journal-title":"Biochim Biophys Acta"},{"key":"182011_CR8","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1152\/physrev.1973.53.3.535","volume":"53","author":"OW. Evans","year":"1973","unstructured":"Evans OW. 1973 Copper homeostasis in the mammalian system. Physiol Rev\n53, 535-570.","journal-title":"Physiol Rev"},{"key":"182011_CR9","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1111\/j.1432-1033.1991.tb15848.x","volume":"196","author":"F Galiazzo","year":"1991","unstructured":"Galiazzo F, Ciriolo MR, Carr\u00ec MT et al. 1991 Activation and induction by copper of Cu, Zn superoxide dismutase in Saccharomyces cerevisiae. Eur J Biochem\n196, 545-549.","journal-title":"Eur J Biochem"},{"key":"182011_CR10","doi-asserted-by":"crossref","first-page":"14504","DOI":"10.1074\/jbc.271.24.14504","volume":"271","author":"DM Glerum","year":"1996","unstructured":"Glerum DM, Shtanko A, Tzagoloff A. 1996a Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J Biol Chem\n271, 14504-14509.","journal-title":"J Biol Chem"},{"key":"182011_CR11","doi-asserted-by":"crossref","first-page":"20531","DOI":"10.1074\/jbc.271.34.20531","volume":"271","author":"DM Glerum","year":"1996","unstructured":"Glerum DM, Shtanko A, Tzagoloff A. 1996b SCO1 and SCO2 act as a high copy suppressor of mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J Biol Chem\n271, 20531-20535.","journal-title":"J Biol Chem"},{"key":"182011_CR12","doi-asserted-by":"crossref","first-page":"8558","DOI":"10.1073\/pnas.88.19.8558","volume":"88","author":"EB Gralla","year":"1991","unstructured":"Gralla EB, Thiele DJ, Silor P, Valentine JS. 1991 ACEl, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proc Natl Acad Sci\n88, 8558-8562.","journal-title":"Proc Natl Acad Sci"},{"key":"182011_CR13","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1038\/ng0193-3","volume":"3","author":"DH. Hamer","year":"1993","unstructured":"Hamer DH. 1993 Kinky hair disease sheds light on copper metabolism. Nature Genetics\n3, 3-4.","journal-title":"Nature Genetics"},{"key":"182011_CR14","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/0003-9861(75)90503-2","volume":"167","author":"E Keyhani","year":"1975","unstructured":"Keyhani E, Keyhani J. 1975 Cytochrome c oxidase biosynthesis and assembly in Candida utilis yeast cells. Arch Biochem Biophys\n167, 596-602.","journal-title":"Arch Biochem Biophys"},{"key":"182011_CR15","doi-asserted-by":"crossref","first-page":"797S","DOI":"10.1093\/ajcn\/63.5.797","volume":"63","author":"MC Linder","year":"1996","unstructured":"Linder MC, Hazegh-Azam M. 1996 Copper biochemistry and molecular biology. Am J Clin Nutr\n63, 797S-811S.","journal-title":"Am J Clin Nutr"},{"key":"182011_CR16","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","volume":"193","author":"OH Lowry","year":"1951","unstructured":"Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. 1951 Protein measurement with the Folin-phenol reagent. J Biol Chem\n193, 265-275.","journal-title":"J Biol Chem"},{"key":"182011_CR17","doi-asserted-by":"crossref","first-page":"262","DOI":"10.3181\/00379727-203-43599","volume":"203","author":"DM Medeiros","year":"1993","unstructured":"Medeiros DM, Davidson J, Jenkins J. E. 1993 A unified perspective on copper deficiency and cardiomiopathy. Proc Soc Exp Biol Med\n203, 262-273.","journal-title":"Proc Soc Exp Biol Med"},{"key":"182011_CR18","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0300-9629(96)00365-9","volume":"117","author":"DM Medeiros","year":"1997","unstructured":"Medeiros DM, Shiry L, Samelman T. 1997 Cardiac nuclear encoded cytochrome c oxidase subunits are decreased with copper restriction but not iron restriction: gene expression, protein synthesis and heat shock protein aspects. Comp Biochem Physiol A\n117, 77-87.","journal-title":"Comp Biochem Physiol A"},{"key":"182011_CR19","doi-asserted-by":"crossref","first-page":"1570","DOI":"10.1093\/jn\/109.9.1570","volume":"109","author":"JR Paynter","year":"1979","unstructured":"Paynter JR, Moir RJ, Underwood EJ. 1979 Changes in the activity of the Cu, Zn superoxide dismutase enzyme in tissues of the rat with changes in dietary copper. J Nutr\n109, 1570-1576.","journal-title":"J Nutr"},{"key":"182011_CR20","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1093\/jn\/121.3.355","volume":"121","author":"JR Prohaska","year":"1991","unstructured":"Prohaska JR 1991 Changes in Cu, Zn superoxide dismutase, cytochrome c oxidase, glutathione peroxidase and glutathione transferase activities in copper-deficient mice and rats. J Nutr\n121, 355-363.","journal-title":"J Nutr"},{"key":"182011_CR21","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0005-2736(95)00142-P","volume":"1239","author":"T Reinheckel","year":"1995","unstructured":"Reinheckel T, Wiswedel I, Noack H, Augustin W. 1995 Electrophoretic evidence for the impairment of the respiratory chain during iron\/ascorbate induced peroxidation in isolated rat liver mitochondria. Biochim Biophys Acta\n1239, 45-50.","journal-title":"Biochim Biophys Acta"},{"key":"182011_CR22","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1006\/bbrc.1994.2285","volume":"203","author":"L Rossi","year":"1994","unstructured":"Rossi L, Ciriolo, MR, Marchese, E. et al. 1994 Differential decrease of copper content and of copper binding to superoxide dismutase in liver, heart and brain of copper-deficient rats. Biochem Biophys Res Commun\n203, 1028-1034.","journal-title":"Biochem Biophys Res Commun"},{"key":"182011_CR23","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1023\/A:1018364130807","volume":"10","author":"L Rossi","year":"1997","unstructured":"Rossi L, Marchese E, De Martino A, Rotilio G, Ciriolo MR. 1997 Purification of a fully metal-depleted Cu, Zn superoxide dismutase from copper-deficient rat liver. BioMetals\n10, 257-262.","journal-title":"BioMetals"},{"key":"182011_CR24","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0003-2697(91)90094-A","volume":"199","author":"H Schagger","year":"1991","unstructured":"Schagger H, von Jagow G. 1991 Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem\n199, 223-231.","journal-title":"Anal Biochem"},{"key":"182011_CR25","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1007\/BF00687247","volume":"77","author":"K Seki","year":"1989","unstructured":"Seki K, Sato T, Ishigaki Y, et al. 1989 Decreased activity of cytochrome c oxidase in the macular mottled mouse. An immuno-electron microscopic study. Acta Neuropathol\n77, 465-471.","journal-title":"Acta Neuropathol"},{"key":"182011_CR26","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1111\/j.1750-3639.1993.tb00762.x","volume":"3","author":"M Sparaco","year":"1993","unstructured":"Sparaco M, Hirano A, Hirano M, Di Mauro S, Bonilla E. 1993 Cytochrome c oxidase deficiency and neuronal involvement in Menkes' kinky hair disease: immuno-histochemical study. Brain Pathol\n3, 349-354.","journal-title":"Brain Pathol"},{"key":"182011_CR27","doi-asserted-by":"crossref","first-page":"24580","DOI":"10.1016\/S0021-9258(18)54268-X","volume":"266","author":"C Steinkuhler","year":"1991","unstructured":"Steinkuhler C, Sapora O, Carr\u00ec MT, et al. 1991 Increase of Cu, Zn superoxide dismutase activity during differentiation of human K562 cells involves activation by copper of a constantly expressed copper-deficient protein. J Biol Chem\n266, 24580-24587.","journal-title":"J Biol Chem"},{"key":"182011_CR28","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1093\/nar\/20.6.1183","volume":"20","author":"DJ. Thiele","year":"1992","unstructured":"Thiele DJ. 1992 Metal-regulated transcription in eukaryotes. Nucleic Ac Res\n20, 1183-1191.","journal-title":"Nucleic Ac Res"},{"key":"182011_CR29","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/S0926-6593(66)80142-X","volume":"118","author":"BF. Van Gelder","year":"1966","unstructured":"Van Gelder BF. 1966 On cytochrome c oxidase. I. The extinction coefficients of cytochrome a and cytochrome a3. Biochim Biophys Acta\n118, 36-46.","journal-title":"Biochim Biophys Acta"},{"key":"182011_CR30","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1073\/pnas.92.7.2632","volume":"92","author":"DS Yuan","year":"1995","unstructured":"Yuan DS, Stearman R, Dancis A, et al. 1995 The Menkes\/ Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc Natl Acad Sci\n92, 2632-2636.","journal-title":"Proc Natl Acad Sci"},{"key":"182011_CR31","doi-asserted-by":"crossref","first-page":"2059","DOI":"10.1002\/elps.1150181131","volume":"18","author":"E Zerbetto","year":"1997","unstructured":"Zerbetto E Vergani L, Dabbeni-Sala F. 1997 Identification and quantification of mitochondrial oxidative phosphorylation chain complexes by applying histochemical staining to blue native polyacrilamide gel electrophoresis. Electrophoresis\n18, 2059-2064.","journal-title":"Electrophoresis"}],"container-title":["Biometals"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1023\/A:1009274131473.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1023\/A:1009274131473\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1023\/A:1009274131473.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,6,10]],"date-time":"2025-06-10T17:22:05Z","timestamp":1749576125000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1023\/A:1009274131473"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,9]]},"references-count":31,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1998,9]]}},"alternative-id":["182011"],"URL":"https:\/\/doi.org\/10.1023\/a:1009274131473","relation":{},"ISSN":["0966-0844","1572-8773"],"issn-type":[{"value":"0966-0844","type":"print"},{"value":"1572-8773","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,9]]}}}