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Ceruloplasmin Regulates Iron Levels in the CNS and Prevents Free Radical Injury
Open accessAbstract
Ceruloplasmin is a ferroxidase that oxidizes toxic ferrous iron to its nontoxic ferric form. We have previously reported that a glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed in the mammalian CNS. To better understand the role of ceruloplasmin in iron homeostasis in the CNS, we generated a ceruloplasmin gene-deficient (Cp(-/-)) mouse. Adult Cp(-/-) mice showed increased iron deposition in several regions of the CNS such as the cerebellum and brainstem. Increased lipid peroxidation was also seen in some CNS regions. Cerebellar cells from neonatal Cp(-/-) mice were also more susceptible to oxidative stress in vitro. Cp(-/-) mice showed deficits in motor coordination that were associated with a loss of brainstem dopaminergic neurons. These results indicate that ceruloplasmin plays an important role in maintaining iron homeostasis in the CNS and in protecting the CNS from iron-mediated free radical injury. Therefore, the antioxidant effects of ceruloplasmin could have important implications for various neurodegenerative diseases such as Parkinson's disease and Alzheimer's disease in which iron deposition is known to occur.
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In the citing paper
“Ceruloplasmin dysfunction might be associated with Parkinson’s disease.135,136”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [135]
In the citing paper
“Ferritin H is induced by NF-κB in response to TNF-α treatment, resulting in suppression of ROS and inhibition of apoptosis (243).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [243]
In the citing paper
“NF-κB is activated by TNF-α and has been shown to induce mouse and human ferritin H (171, 243).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [243]
In the citing paper
“Ferritin H was found as a TNF-α– or IL-1–inducible gene (171, 243, 294).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [243]
In the citing paper
“Apoptosis induced by TNF-α was inhibited by NF-κB”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [243]
In the citing paper
“Many studies set a precedent of ferritin in cytoprotection against free-iron–catalyzed production of ROS (227, 243, 301).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [243]
In the citing paper
“Ferritin was identified as the downstream mediator of the antioxidant and protective activities of NF-κB in response to TNF-α signaling in inflammation and apoptosis (243, 294).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [243]
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Cites
Hansen, M., Nielsen, S. E., & Berg, K. (1989) · Journal of Immunological Methods · doi:10.1016/0022-1759(89)90397-9 · Cited by 3,488
Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422
Toxicity of iron and hydrogen peroxide: the Fenton reaction
Winterbourn, C. C. (1995) · Toxicology Letters · doi:10.1016/0378-4274(95)03532-x · Cited by 1,415
Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,365
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084
A radical hypothesis for neurodegeneration
Olanow, C. W. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90070-3 · Cited by 722
Altered Brain Metabolism of Iron as a Cause of Neurodegenerative Diseases?
Gerlach, M., Ben‐Shachar, D., Riederer, P. F., & Youdim, M. B. H. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63030793.x · Cited by 704
Frey, D., Schneider, C., Xu, L., Borg, J., Spooren, W. P. J. M., & Caroni, P. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-07-02534.2000 · Cited by 683
The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.
Osaki, S., Johnson, D. A., & Frieden, E. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96527-0 · Cited by 679
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Ta, A. D., Batavani, R. A., Rezae, S. A., & Ahmadi, M. R. (2008) · Pakistan Journal of Biological Sciences · doi:10.3923/pjbs.2008.571.576 · Cited by 25
Maltais, D. B., Desroches, D., Aouffen, M., Mateescu, M. A., Wang, R., & Paquin, J. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00325-7 · Cited by 25
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Shin, E., Jeong, J. H., Chung, C. K., Kim, D.-J., Wie, M., Park, E. S., Chung, Y. H., Nam, Y., Tran, T.-V., Lee, S. Y., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.031 · Cited by 24
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Tian, S., Jones, S. M., Jose, A., & Solomon, E. I. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b03661 · Cited by 22
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Yang, S., Hua, Y., Nakamura, T., Keep, R. F., & Xi, G. (2006) · Springer eBooks · doi:10.1007/3-211-30714-1_44 · Cited by 23
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Zanardi, A., & Alessio, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020663 · Cited by 25
Ruiz-Pablos, M., Paiva, B., & Zabaleta, A. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04515-7 · Cited by 23
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Yamauchi, T., Nishiyama, M., Moroishi, T., Kawamura, A., & Nakayama, K. I. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00470-16 · Cited by 22
A study of serum copper and ceruloplasmin in Alzheimer's disease in Kerman, Iran
Sedighi, B., & Shariati, M. (2006) · Cited by 21
Shahandeh, A., Bui, B. V., Finkelstein, D. I., & Nguyen, C. T. O. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.794809 · Cited by 21
Ruhs, S., Naß, N., Bartling, B., Brömme, H., Leuner, B., Somoza, V., Friess, U., Silber, R., & Simm, A. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.08.001 · Cited by 21
Jin, L., Wan, W., Wang, L., Wang, C., Xiao, J., Zhang, F., Zhao, J., Wang, J., Zhan, C., & Zhong, C. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.09.034 · Cited by 21
Iron Pathophysiology in Neurodegeneration with Brain Iron Accumulation
Levi, S., Cozzi, A., & Santambrogio, P. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_9 · Cited by 21
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Dutra, F., Ciriolo, M. R., Calabrese, L., & Bechara, E. J. H. (2005) · Chemical Research in Toxicology · doi:10.1021/tx049655u · Cited by 20
Schulpis, K. H., Papastamataki, M., Stamou, H., Papassotiriou, I., & Margeli, A. P. (2010) · Acta Paediatrica · doi:10.1111/j.1651-2227.2010.01890.x · Cited by 20
Wang, W., Wu, X., Yang, C. S., & Zhang, J. (2021) · Antioxidants · doi:10.3390/antiox10101564 · Cited by 23
Guerreiro, C. C., Silva, B. D. R., Crespo, Â. C., Marques, L., Costa, S., Timóteo, Â., Marcelino, E., Maruta, C., Vilares, A., Matos, M., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.07.017 · Cited by 19
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Chen, H., Attieh, Z. K., Gao, H., Huang, G., Su, T., Ke, W., & Vulpe, C. D. (2009) · BioMetals · doi:10.1007/s10534-009-9229-0 · Cited by 18
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Marques, J. P., Rolf Gruetter, A., & van der Zwaag, W. (2010) · The Cerebellum · doi:10.1007/s12311-010-0189-2 · Cited by 18
Viktorínová, A. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.07.022 · Cited by 18
Bulnes, M., Bonilla, J., Suazo, M., Michelotti, T. C., Paz, A., Lefler, J., Marotz, C. A., Embree, M. M., Begalli, G. G., Halfen, J., et al. (2024) · Journal of Dairy Science · doi:10.3168/jds.2024-25058 · Cited by 17
Nanto-Hara, F., Ohtsu, H., Yamazaki, M., Hirakawa, T., Sato, K., & Murakami, H. (2020) · The Journal of Poultry Science · doi:10.2141/jpsa.0200063 · Cited by 20
Induction of ferroxidase enzymatic activity by copper reduces MPP+-evoked neurotoxicity in rats
Rubio‐Osornio, M., Montes, S., Heras‐Romero, Y., Guevara, J., Rubio, C., Aguilera, P., Rivera-Mancía, S., Floriano-Sánchez, E., Monroy‐Noyola, A., & Rı́os, C. (2013) · Neuroscience Research · doi:10.1016/j.neures.2012.12.003 · Cited by 17
Role of a Tyrosine Radical in Human Ceruloplasmin Catalysis
Tian, S., Jones, S. M., & Solomon, E. I. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00953 · Cited by 17
Biochemical Features of Ceruloplasmin Gene Mutations Linked to Aceruloplasminemia
Kono, S., Suzuki, H., Oda, T., Miyajima, H., Takahashi, Y., Shirakawa, K., Ishikawa, K., & Kitagawa, M. (2006) · NeuroMolecular Medicine · doi:10.1385/nmm:8:3:361 · Cited by 17
Prohaska, J. R. (2012) · doi:10.1002/9781119946045.ch35 · Cited by 17
González, D. A. S., Cheli, V. T., Rosenblum, S. L., Denaroso, G., & Paez, P. M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102118 · Cited by 16
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Minhas, G., Modgil, S., & Anand, A. (2014) · Metabolic Brain Disease · doi:10.1007/s11011-014-9522-7 · Cited by 16
Age-Related Features of Ceruloplasmin Biosynthesis and Distribution in Rats
Платонова, Н. А., Zhiguleva, E. A., Васильевна, Ц. Н., Bs, M., Vasin, A. V., Zhivulko, T., & Puchkova, L. V. (2004) · Russian Journal of Developmental Biology · doi:10.1023/b:rudo.0000029711.35897.6f · Cited by 16
Stoj, C. S., & Kosman, D. J. (2005) · Wiley eBooks · doi:10.1002/9781119951438.eibc0053 · Cited by 16
Agostini, F., Sgalletta, B., & Bisaglia, M. (2024) · Cells · doi:10.3390/cells13161376 · Cited by 17
Matysiak-Brynda, E., Botz, A. J. R., Clausmeyer, J., Wagner, B. J., Schuhmann, W. W., Stojek, Z. J., & Nowicka, A. M. (2015) · Langmuir · doi:10.1021/acs.langmuir.5b01155 · Cited by 14
Ceruloplasmin Deficiency Impaired Brain Iron Metabolism and Behavior in Mice
Niu, L., Zhou, Y., Lu, L., Su, A., & Guo, X. (2022) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-022-01061-9 · Cited by 16
A role for ceruloplasmin in the control of human glioblastoma cell responses to radiation
Roy, C., Avril, S., Legendre, C., Lelièvre, B., Vellenriter, H., Boni, S., Cayon, J., Guillet, C., Guilloux, Y., Chérel, M., et al. (2022) · BMC Cancer · doi:10.1186/s12885-022-09808-6 · Cited by 12
Raia, S., Conti, A., Zanardi, A., Ferrini, B., Scotti, G. M., Gilberti, E., Palma, G. D., David, S., & Alessio, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021150 · Cited by 14
Self-citationHarned, J., Fleisher, L. N., & McGahan, M. C. (2006) · Experimental Eye Research · doi:10.1016/j.exer.2006.01.018 · Cited by 14
Duce, J. A., Ayton, S., Miller, A. A., Tsatsanis, A., Lam, L. Q., Leone, L., Corbin, J. E., Butzkueven, H., Kilpatrick, T. J., Rogers, J. T., et al. (2012) · Molecular Psychiatry · doi:10.1038/mp.2011.168 · Cited by 14
Ceruloplasmin expression and its role in iron transport in C6 cells
Chang, Y. Z., Qian, Z., Du, J. R., Zhu, L., Xu, Y., Li, L., Wang, C., Wang, Q., Ge, X. H., Ho, K. P., et al. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.01.004 · Cited by 14
Wotton, J. M., Peterson, E., Flenniken, A. M., Bains, R. S., Veeraragavan, S., Bower, L. R., Bubier, J. A., Parisien, M., Bezginov, A., Haselimashhadi, H., et al. (2021) · Pain · doi:10.1097/j.pain.0000000000002481 · Cited by 13
Li, Z., Kang, S., Li, H., Yu, P., Xie, R., Li, C., Qi, J., Gong, Z., Li, L., Li, Z., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103611 · Cited by 13
Lelliott, P. M., McMorran, B. J., Foote, S. J., & Burgio, G. (2015) · Infection and Immunity · doi:10.1128/iai.00926-15 · Cited by 12
Sebastiani, G., & Pantopoulos, K. (2010) · CRC Press eBooks · doi:10.1201/9781420059984-c13 · Cited by 12
Warming, H., Deinhardt, K., Garland, P., More, J. E., Bulters, D. O., Galea, I., & Vargas‐Caballero, M. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15936 · Cited by 11
Role and Regulation of Copper and Zinc Transport Proteins in the Central Nervous System
Levenson, C. W., & Tassabehji, N. M. (2007) · Springer eBooks · doi:10.1007/978-0-387-30380-2_13 · Cited by 11
Schizophrenia-like psychosis and aceruloplasminemia
Walterfang, M., March, E. G., Varghese, D., Miller, K., Simpson, L. C., Tomlinson, B., & Velakoulis, D. (2006) · Neuropsychiatric Disease and Treatment · doi:10.2147/nedt.2006.2.4.577 · Cited by 11
Costa, N. D. A., Simão, L. C. V., dos Santos, R. A., Afonso, J. A. B., Fagliari, J. J., Cardoso, E. D. C., Soares, P. C., & de Mendonça, C. L. (2010) · Pesquisa Veterinária Brasileira · doi:10.1590/s0100-736x2010000500011 · Cited by 11
Naquin, E. R., Garg, R., Chen, W. J., Karmakar, E., Prasad, A., Mandadi, S., Depala, K. S., Gopianand, J. S., & Gnana‐Prakasam, J. P. (2025) · Nutrients · doi:10.3390/nu17182964 · Cited by 10
Thought-provoking Molecules for Drug Discovery: antioxidants
Celikyurt, I. K. (2011) · Pharmaceutica Analytica Acta · doi:10.4172/2153-2435.s3-001 · Cited by 10
Sakajiri, T., Nakatsuji, M., Teraoka, Y., Furuta, K., Ikuta, K., Shibusa, K., Sugano, E., Tomita, H., Inui, T., & Yamamura, T. (2021) · Metallomics · doi:10.1093/mtomcs/mfab065 · Cited by 11
Olfactory impairment and pathology in neurodegenerative disorders with brain iron accumulation
Dziewulska, D., Doi, H., Fasano, A. A., Erro, R., Fatehi, F., Fekete, R., Gatto, E. M., Pablos, E. G., Lehn, A., Miyajima, H., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1136-3 · Cited by 10
Stoj, C. S., & Kosman, D. J. (2005) · Wiley eBooks · doi:10.1002/0470862106.ia055 · Cited by 11
Wu, R., Chen, C., & Zhang, X. (2022) · Foods · doi:10.3390/foods11071035 · Cited by 9
Age-dependent expression of hephaestin in the brain of ceruloplasmin-deficient mice
Cui, R., Duan, X., Anderson, G. J., Qiao, Y.-T., Yu, P., Qian, Z., Yoshida, K., Takeda, S., Guo, P., Yang, Z.-L., et al. (2009) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2009.05.004 · Cited by 9
Molecular analysis of Ceruloplasmin in a South African cohort presenting with oesophageal cancer
Strickland, N. J., Matsha, T. E., Erasmus, R., & Zaahl, M. G. (2011) · International Journal of Cancer · doi:10.1002/ijc.26418 · Cited by 10
Reference Values of Ceruloplasmin across the Adult Age Range in a Large Italian Healthy Population
Pelucchi, S., Risca, G., Lanzafame, C., Scollo, C. M., Garofalo, A. M., Martinez, D., Mariani, R., Botti, M., Capitoli, G., Rossi, F., et al. (2024) · The Journal of Applied Laboratory Medicine · doi:10.1093/jalm/jfae098 · Cited by 8
Iron metabolism dysfunction in neuropsychiatric disorders: Implications for therapeutic intervention
Duarte-Silva, E. P., Maes, M. H. J., & Peixoto, C. A. (2024) · Behavioural Brain Research · doi:10.1016/j.bbr.2024.115343 · Cited by 10
Arnhold, J. (2025) · Biomolecules · doi:10.3390/biom15040547 · Cited by 8
Heinsberg, L. W., Alexander, S. A., Crago, E. A., Minster, R. L., Poloyac, S. M., Weeks, D. E., & Conley, Y. P. (2020) · Neurocritical Care · doi:10.1007/s12028-020-00961-z · Cited by 8
Yahyazadeh, A., & Altunkaynak, B. Z. (2020) · Brain Research · doi:10.1016/j.brainres.2020.146919 · Cited by 8
Villadsen, B., Thygesen, C., Grebing, M., Kempf, S. J., Sandberg, M. B., Jensen, P., Kolstrup, S. H., Nielsen, H. H., Larsen, M. R., & Finsen, B. R. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15754 · Cited by 8
Zhao, N., Xiao, J., Zheng, Z.-Y., Fei, G., Zhang, F., Jin, L., & Zhong, C. (2015) · Neuroscience Bulletin · doi:10.1007/s12264-014-1512-6 · Cited by 8
Genetics of Parkinson's Disease
Huang, Y. M., Chan, P., & Halliday, G. M. (2007) · Elsevier eBooks · doi:10.1016/b978-044452809-4/50169-1 · Cited by 10
Brain and retinal ferroportin 1 dysregulation in polycythaemia mice
Iacovelli, J., Mlodnicka, A., Veldman, P. B., Ying, G., Dunaief, J. L., & Schumacher, A. (2009) · Brain Research · doi:10.1016/j.brainres.2009.06.098 · Cited by 8
Role of Selenium, Iron, Copper, and Zinc in Parkinsonism
Qureshi, G. A., Syed, S. A., & Parvez, S. H. (2007) · Elsevier eBooks · doi:10.1016/b978-044452809-4/50171-x · Cited by 8
Astrocytes and Memory: Implications for the Treatment of Memory-related Disorders
Wang, J., Cheng, P., Qu, Y., & Zhu, G. (2024) · Current Neuropharmacology · doi:10.2174/1570159x22666240128102039 · Cited by 7
Bartnikas, T. B., Fleming, M. D., & Schmidt, P. J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.011 · Cited by 7
Inherited Disorders of Brain Iron Homeostasis
Schipper, H. M., & Ponka, P. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-462-9_15 · Cited by 8
Kono, S., & Miyajima, H. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-410529-4.00045-0 · Cited by 7
Lymphocyte ceruloplasmin and Behçet's disease.
Oliveira, R., Banha, J., Martins, F., Paixão, E., Pereira, D., Barcelos, F., Teixeira, A. M., Patto, J. V., & Costa, L. M. G. (2006) · PubMed · Cited by 6
The effect of 900MHz Electromagnetic Field on the Cerebellum: A Histopathological Investigation
Mercantepe, T. (2018) · SiSli Etfal Hastanesi Tip Bulteni / The Medical Bulletin of Sisli Hospital · doi:10.14744/semb.2018.42275 · Cited by 6
Sulong, A. H., ZULKIFLI, I., Ramiah, S. K., Chung, E. L. T., Awad, E. A., & Sazili, A. Q. (2021) · Italian Journal of Animal Science · doi:10.1080/1828051x.2021.1978879 · Cited by 6
iTRAQ-Based Proteomic Analysis of APP Transgenic Mouse Urine Exosomes
Zhou, X., Sheikh, A. M., Matsumoto, K., Mitaki, S., Shibly, A. Z., Zhang, Y., Garu, A., Yano, S., & Nagai, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010672 · Cited by 6
Regulation of Ceruloplasmin Gene in Mammals
Gyulikhandanova, N. E., Васильевна, Ц. Н., Платонова, Н. А., Babich, V., & Puchkova, L. V. (2004) · Bulletin of Experimental Biology and Medicine · doi:10.1023/b:bebm.0000038160.60211.6f · Cited by 6
Ducharme, P., Maltais, D., Desroches, D., Mateescu, M., & Paquin, J. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.02.039 · Cited by 6
Meling, S., Skovgaard, K., Bårdsen, K., Heegaard, P. M. H., & Ulvund, M. J. (2018) · BMC Veterinary Research · doi:10.1186/s12917-018-1607-9 · Cited by 8
Mitochondrial ceruloplasmin of mammals
Vasin, A. V., Платонова, Н. А., Povalikhin, R., Klotchenko, S. A., Samsonov, S. A., Васильевна, Ц. Н., & Puchkova, L. V. (2005) · Molecular Biology · doi:10.1007/s11008-005-0006-z · Cited by 6
Conti, A., & Alessio, M. (2015) · International review of neurobiology · doi:10.1016/bs.irn.2015.05.004 · Cited by 7
Perinatal Copper Deficiency Alters Rat Cerebellar Purkinje Cell Size and Distribution
Lyons, J., & Prohaska, J. R. (2009) · The Cerebellum · doi:10.1007/s12311-009-0136-2 · Cited by 5
Relationships between CTR1 activity and copper status in different rat organs
Samsonov, S. A., Платонова, Н. А., Skvortsov, A. N., Васильевна, Ц. Н., Vasin, A. V., & Puchkova, L. V. (2006) · Molecular Biology · doi:10.1134/s0026893306020051 · Cited by 5
Advances in hybrid MR–PET at 3 T and 9.4 T in humans
Shah, N. J., Mauler, J., Neuner, I., Oros‐Peusquens, A., Romanzetti, S., Vahedipour, K., Felder, J., Celik, A., Iida, H., Langen, K., et al. (2012) · Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment · doi:10.1016/j.nima.2012.08.053 · Cited by 5
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Metadata
- Authors
- Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J.-P., & David, S.
- Affiliations
- Montreal General Hospital (CA)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2002-08-01
- Volume
- 22
- Issue
- 15
- Pages
- 6578-6586
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6758125
- OpenAlex
- W1595395957
- Cited by
- 379
- References
- 51
- Citations by year
- 2026: 5 · 2025: 12 · 2024: 10 · 2023: 12 · 2022: 16 · 2021: 14 · 2020: 12 · 2019: 11 · 2018: 22 · 2017: 17 · 2016: 11 · 2015: 24 · 2014: 24 · 2013: 15 · 2012: 22
- FWCI
- 10.71
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Parkinson's Disease Foundation
- Canadian Institutes of Health Research
- Topics
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- ceruloplasmin, iron homeostasis, central nervous system, ferroxidase, oxidative damage, oxidative stress, lipid peroxidation, cerebellum, brainstem, dopaminergic neurons, motor coordination deficits, neurodegenerative diseases, Parkinson's disease, Alzheimer's disease, iron accumulation
- MeSH terms
- Animals, Astrocytes, Brain Stem, Cell Survival, Cells, Cultured, Central Nervous System, Ceruloplasmin, Disease Models, Animal, Free Radicals, Iron, Liver, Neurons, Transferrin, Lipid Peroxidation, Mice, Knockout, Oxidative Stress, Gene Targeting, Motor Skills Disorders, Mice
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