The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
Open accessAbstract
Aceruloplasminemia is an autosomal recessive disorder of iron metabolism. Affected individuals evidence iron accumulation in tissue parenchyma in association with absent serum ceruloplasmin. Genetic studies of such patients reveal inherited mutations in the ceruloplasmin gene. To elucidate the role of ceruloplasmin in iron homeostasis, we created an animal model of aceruloplasminemia by disrupting the murine ceruloplasmin ( Cp ) gene. Although normal at birth, Cp −/− mice demonstrate progressive accumulation of iron such that by one year of age all animals have a prominent elevation in serum ferritin and a 3- to 6-fold increase in the iron content of the liver and spleen. Histological analysis of affected tissues in these mice shows abundant iron stores within reticuloendothelial cells and hepatocytes. Ferrokinetic studies in Cp +/+ and Cp −/− mice reveal equivalent rates of iron absorption and plasma iron turnover, suggesting that iron accumulation results from altered compartmentalization within the iron cycle. Consistent with this concept, Cp −/− mice showed no abnormalities in cellular iron uptake but a striking impairment in the movement of iron out of reticuloendothelial cells and hepatocytes. Our findings reveal an essential physiologic role for ceruloplasmin in determining the rate of iron efflux from cells with mobilizable iron stores.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Coexposure to iron and H2O2 were shown to enhance α-synuclein aggregation in vitro (126).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [126]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166
Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
Tybulewicz, V. L. J., Crawford, C. E., Jackson, P. K., Bronson, R. T., & Mulligan, R. C. (1991) · Cell · doi:10.1016/0092-8674(91)90011-m · Cited by 1,281
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159
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
Heme oxygenase 1 is required for mammalian iron reutilization
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10919 · Cited by 1,016
Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921
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
Transferrin receptor is necessary for development of erythrocytes and the nervous system
Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574
Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.
Harris, Z. L., Takahashi, Y., Miyajima, H., Serizawa, M., MacGillivray, R. T., & Gitlin, J. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2539 · Cited by 558
Self-citationHFE gene knockout produces mouse model of hereditary hemochromatosis
Zhou, X. Y., Tomatsu, S., Fleming, R. E., Parkkila, S., Waheed, A., Jiang, J., Fei, Y., Brunt, E. M., Ruddy, D. A., Prass, C. E., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2492 · Cited by 519
Research works printed but not linked: 4
- P Ponka, C Beaumont, D R Richardson Semin Hematol 35, 35–54 (1998).
- B R Bacon, M L Schilsky Adv Intern Med 44, 91–116 (1999).
- J I Logan, K B Harveyson, G B Wisdom, A E Hughes, G P R Archbold Q J Med 87, 663–670 (1994).
- J D Torrance, T H Bothwell Methods in Hematology: Iron, ed J D Cook (Churchill Livingstone, New York), pp. 104–109 (1980).
Cited by
Sorted by citations
Items 101–200 of 567
Allen, M. D., del Campo, J. A., Kropat, J., & Merchant, S. (2007) · Eukaryotic Cell · doi:10.1128/ec.00205-07 · Cited by 137
Srinivasan, C., Liba, A., Imlay, J. A., Valentine, J. S., & Gralla, E. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004239200 · Cited by 134
Copper Transport and Metabolism Are Normal in Aceruloplasminemic Mice
Meyer, L. A., Durley, A. P., Prohaska, J. R., & Harris, Z. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105361200 · Cited by 136
Self-citationPhysiology of iron transport and the hemochromatosis gene
Pietrangelo, A. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00404.2001 · Cited by 135
Functional consequences of ferroportin 1 mutations
Liu, X.-B., Yang, F., & Haile, D. J. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.04.005 · Cited by 136
The Regulation of Hepcidin and Its Effects on Systemic and Cellular Iron Metabolism
Fleming, M. D. (2008) · Hematology · doi:10.1182/asheducation-2008.1.151 · Cited by 134
Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function
Stoj, C. S., & Kosman, D. J. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01218-3 · Cited by 132
Sampath, P., Mazumder, B., Seshadri, V., & Fox, P. L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1509-1519.2003 · Cited by 130
Impact of Copper Limitation on Expression and Function of Multicopper Oxidases (Ferroxidases)
Prohaska, J. R. (2011) · Advances in Nutrition · doi:10.3945/an.110.000208 · Cited by 130
The molecular basis of copper and iron interactions
Sharp, P. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004386 · Cited by 125
Schilsky, M. L., Roberts, E. A., Bronstein, J. M., Dhawan, A. K., Hamilton, J. P., Rivard, A. M., Washington, M. K., Weiss, K. H., & Zimbrean, P. C. (2022) · Hepatology · doi:10.1002/hep.32801 · Cited by 136
The role of insufficient copper in lipid synthesis and fatty‐liver disease
Morrell, A., Tallino, S., Yu, L., & Burkhead, J. L. (2017) · IUBMB Life · doi:10.1002/iub.1613 · Cited by 126
Molecular Mediators Governing Iron-Copper Interactions
Güleç, Ş., & Collins, J. F. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161215 · Cited by 122
Chen, H., Attieh, Z. K., Syed, B. A., Kuo, Y.-M., Stevens, V., Fuqua, B. K., Andersen, H. S., Naylor, C. E., Evans, R. W., Gambling, L., et al. (2010) · The Journal of Nutrition · doi:10.3945/jn.109.117531 · Cited by 122
Regulation of zinc-dependent enzymes by metal carrier proteins
Thompson, M. W. (2022) · BioMetals · doi:10.1007/s10534-022-00373-w · Cited by 130
Chen, H., Su, T., Attieh, Z. K., Fox, T. C., McKie, A. T., Anderson, G. J., & Vulpe, C. D. (2003) · Blood · doi:10.1182/blood-2003-02-0347 · Cited by 121
Mazumder, B., Sampath, P., & Fox, P. L. (2005) · Molecules and Cells · doi:10.1016/s1016-8478(23)13213-4 · Cited by 119
Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice
Viatte, L., Lesbordes, J.-C., Lou, D.-Q., Bennoun, M., Nicolas, G., Kahn, A., Canonne‐Hergaux, F., & Vaulont, S. (2005) · Blood · doi:10.1182/blood-2004-12-4608 · Cited by 119
Copper and Iron Transport Across the Placenta: Regulation and Interactions
McArdle, H. J., Andersen, H. S., Jones, H. N., & Gambling, L. (2008) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2008.01658.x · Cited by 120
Retinal iron homeostasis in health and disease
Song, D., & Dunaief, J. L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00024 · Cited by 122
Dunaief, J. L., Richa, C. G., Franks, E. P., Schultze, R. L., Alemán, T. S., Schenck, J. F., Zimmerman, E. A., & BROOKS, D. (2005) · Ophthalmology · doi:10.1016/j.ophtha.2004.12.029 · Cited by 118
Placental iron transport: The mechanism and regulatory circuits
Sangkhae, V., & Nemeth, E. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.001 · Cited by 119
Neurodegenerative disease and iron storage in the brain
Thomas, M., & Jankovic, J. J. (2004) · Current Opinion in Neurology · doi:10.1097/01.wco.0000137534.61244.d1 · Cited by 117
The Oral Iron Chelator Deferiprone Protects against Iron Overload–Induced Retinal Degeneration
Hadziahmetovic, M., Song, Y., Wolkow, N., Iacovelli, J., Grieco, S. F., Lee, J., Lyubarsky, A., Praticò, D., Connelly, J., Spino, M., et al. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-6207 · Cited by 119
Self-citationZebrafish in the sea of mineral (iron, zinc, and copper) metabolism
Zhao, L., Xia, Z., & Wang, F. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00033 · Cited by 119
The Ceruloplasmin Homolog Hephaestin and the Control of Intestinal Iron Absorption
Anderson, G. J., Frazer, D. M., McKie, A. T., & Vulpe, C. D. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0576 · Cited by 111
Ceruloplasmin gene variations and substantia nigra hyperechogenicity in Parkinson disease
Hochstrasser, H., Bauer, P., Walter, U., Behnke, S., Spiegel, J., Csoti, I., Zeiler, B., Bornemann, A., Pahnke, J., Becker, G., et al. (2004) · Neurology · doi:10.1212/01.wnl.0000144276.29988.c3 · Cited by 111
Roy, C. N. (2010) · Hematology · doi:10.1182/asheducation-2010.1.276 · Cited by 114
Iron homeostasis in breast cancer
Marques, O., da Silva, B. M., Porto, G., & Lopes, C. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.01.029 · Cited by 116
Chen, H., Huang, G., Su, T., Gao, H., Attieh, Z. K., McKie, A. T., Anderson, G. J., & Vulpe, C. D. (2006) · Journal of Nutrition · doi:10.1093/jn/136.5.1236 · Cited by 109
Brain iron accumulation in aging and neurodegenerative disorders
Hagemeier, J., Geurts, J. J. G., & Zivadinov, R. (2012) · Expert Review of Neurotherapeutics · doi:10.1586/ern.12.128 · Cited by 114
Ceruloplasmin-ferroportin system of iron traffic in vertebrates
Musci, G. (2014) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v5.i2.204 · Cited by 111
Metal transporters and disease
Andrews, N. C. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00307-1 · Cited by 110
A physiological model to study iron recycling in macrophages
Delaby, C., Pilard, N., Hetet, G., Driss, F., Grandchamp, B., Beaumont, C., & Canonne-Hergaux, F. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.07.002 · Cited by 103
Kono, S. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00007-7 · Cited by 107
Ironing out the details of ferroptosis
Zhang, D. D. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01361-7 · Cited by 108
Aceruloplasminemia: new clinical, pathophysiological and therapeutic insights
Loréal, O., Turlin, B., Pigeon, C., Moisan, A., Ropert, M., Morice, P., Gandon, Y., Jouanolle, A., Vérin, M., Hider, R. C., et al. (2002) · Journal of Hepatology · doi:10.1016/s0168-8278(02)00042-9 · Cited by 106
The placenta: the forgotten essential organ of iron transport
Cao, C. Q., & Fleming, M. D. (2016) · Nutrition Reviews · doi:10.1093/nutrit/nuw009 · Cited by 102
Molecular control of iron metabolism
Andrews, N. C. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.10.004 · Cited by 109
Kwok, E. Y., Severance, S., & Kosman, D. J. (2006) · Biochemistry · doi:10.1021/bi052173c · Cited by 103
Role of Ceruloplasmin in Macrophage Iron Efflux during Hypoxia
Sarkar, J., Seshadri, V., Tripoulas, N. A., Ketterer, M. E., & Fox, P. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304926200 · Cited by 101
The physiopathological significance of ceruloplasmin
Floris, G., Medda, R., Padiglia, A., & Musci, G. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00399-3 · Cited by 101
Does Ceruloplasmin Defend Against Neurodegenerative Diseases?
Wang, B., & Wang, X. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180508113025 · Cited by 104
Iron transport in the kidney: implications for physiology and cadmium nephrotoxicity
Thévenod, F., & Wolff, N. A. (2015) · Metallomics · doi:10.1039/c5mt00215j · Cited by 101
Hereditary Causes of Disturbed Iron Homeostasis in the Central Nervous System
Ponka, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.022 · Cited by 99
Huston, W. M., Jennings, M. P., & McEwan, A. G. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03132.x · Cited by 99
Iron in neurodegenerative disorders
Berg, D., Becker, G., Riederer, P. F., & Rieß, O. (2002) · Neurotoxicity Research · doi:10.1080/1029842021000045444 · Cited by 98
Iron Efflux from Oligodendrocytes Is Differentially Regulated in Gray and White Matter
Schulz, K., Vulpe, C. D., Harris, Z. L., & David, S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2838-11.2011 · Cited by 98
Self-citationPietrangelo, A., Caleffi, A., & Corradini, E. (2011) · Seminars in Liver Disease · doi:10.1055/s-0031-1286061 · Cited by 99
The Ins and Outs of Iron Homeostasis
Donovan, A., Roy, C. N., & Andrews, N. C. (2006) · Physiology · doi:10.1152/physiol.00052.2005 · Cited by 101
Inherited Disorders of Iron Overload
Pantopoulos, K. (2018) · Frontiers in Nutrition · doi:10.3389/fnut.2018.00103 · Cited by 101
Hephaestin—a ferroxidase of cellular iron export
Petrák, J., & Vyoral, D. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.12.007 · Cited by 96
Iron metabolism: current facts and future decisions
Tandara, L., & Salamunić, I. (2012) · Biochemia Medica · doi:10.11613/bm.2012.034 · Cited by 102
Iron Homeostasis in the Lungs—A Balance between Health and Disease
Neves, J., Haider, T., Gassmann, M., & Muckenthaler, M. U. (2019) · Pharmaceuticals · doi:10.3390/ph12010005 · Cited by 94
Ferroptosis: Biological Rust of Lipid Membranes
Hassannia, B., Coillie, S. V., & Berghe, T. V. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8175 · Cited by 93
Ravia, J. J., Stephen, R. M., Ghishan, F. K., & Collins, J. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506727200 · Cited by 96
Molecular pathogenesis of iron overload
Trinder, D., Fox, C., Vautier, G., & Olynyk, J. K. (2002) · Gut · doi:10.1136/gut.51.2.290 · Cited by 93
Kim, H.-J., Son, H., Bailey, S. M., & Lee, J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90632.2008 · Cited by 92
Levi, S., & Tiranti, V. (2019) · Pharmaceuticals · doi:10.3390/ph12010027 · Cited by 90
Iron Homeostasis and Metabolism: Two Sides of a Coin
Venkataramani, V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_3 · Cited by 96
H ferritin knockout mice: a model of hyperferritinemia in the absence of iron overload
Ferreira, C., Santambrogio, P., Martin, M.-E., Andrieu, V., Feldmann, G., Hénin, D., & Beaumont, C. (2001) · Blood · doi:10.1182/blood.v98.3.525 · Cited by 89
Functional relevance of ceruloplasmin mutations in Parkinson's Disease
Hochstrasser, H., Tomiuk, J., Walter, U., Behnke, S., Spiegel, J., Krüger, R., Becker, G., Riess, O., & Berg, D. (2005) · The FASEB Journal · doi:10.1096/fj.04-3486fje · Cited by 87
Iron Metabolism and Ferroptosis in Physiological and Pathological Pregnancy
Zhang, Y., Lu, Y., & Jin, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169395 · Cited by 94
Finkenstedt, A., Wolf, E., Höfner, E., Gasser, B. I., Boesch, S., Bakry, R. S., Creus, M., Kremser, C., Schocke, M., Theurl, M., et al. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.04.039 · Cited by 90
Iron Homeostasis During Pregnancy: Maternal, Placental, and Fetal Regulatory Mechanisms
Sangkhae, V., Fisher, A. L., Ganz, T., & Nemeth, E. (2023) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-061021-030404 · Cited by 112
The impact of metal availability on immune function during infection
Monteith, A. J., & Skaar, E. P. (2021) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2021.08.004 · Cited by 83
Molecular Mechanisms and Regulation of Iron Transport
Chung, J., & Wessling‐Resnick, M. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609332 · Cited by 86
Mechanisms of Haem and Non-Haem Iron Absorption: Lessons from Inherited Disorders of Iron Metabolism
Anderson, G. J., Frazer, D. M., McKie, A. T., Vulpe, C. D., & Smith, A. (2005) · BioMetals · doi:10.1007/s10534-005-3708-8 · Cited by 90
Iron and Copper Interactions in Development and the Effect on Pregnancy Outcome
Gambling, L., Danzeisen, R., Fosset, C., Andersen, H. S., Dunford, S., Srai, S. K., & McArdle, H. J. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1554s · Cited by 85
Biochemical Analysis of a Missense Mutation in Aceruloplasminemia
Hellman, N. E., Kono, S., Miyajima, H., & Gitlin, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109123200 · Cited by 84
Self-citationDonker, A. E., Raymakers, R. A. P., Vlasveld, L. T., van Barneveld, T., Terink, R., Dors, N., Brons, P., Knoers, N. V. A. M., & Swinkels, D. W. (2014) · Blood · doi:10.1182/blood-2014-01-548776 · Cited by 88
Systemic iron metabolism: a review and implications for brain iron metabolism
Rouault, T. A. (2001) · Pediatric Neurology · doi:10.1016/s0887-8994(01)00260-0 · Cited by 81
Wessling‐Resnick, M. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.129 · Cited by 83
Engström, G., Lind, P., Hedblad, B., Stavenow, L., Janzon, L., & Lindgärde, F. (2002) · Stroke · doi:10.1161/01.str.0000034787.02925.1f · Cited by 80
Human transferrin: An inorganic biochemistry perspective
Silva, A. M. N., Moniz, T., de Castro, B., & Rangel, M. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214186 · Cited by 79
Han, O., & Kim, E. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21392 · Cited by 77
Recycling Iron in Normal and Pathological States
Beaumont, C., & Delaby, C. (2009) · Seminars in Hematology · doi:10.1053/j.seminhematol.2009.06.004 · Cited by 84
The biology of mammalian multi-copper ferroxidases
Helman, S. L., Zhou, J., Fuqua, B. K., Lu, Y., Collins, J. F., Chen, H., Vulpe, C. D., Anderson, G. J., & Frazer, D. M. (2022) · BioMetals · doi:10.1007/s10534-022-00370-z · Cited by 83
Rethinking the role of ceruloplasmin in brain iron metabolism
Qian, Z. M., & Ke, Y. (2001) · Brain Research Reviews · doi:10.1016/s0165-0173(01)00056-x · Cited by 76
Classification and molecular pathogenesis of NBIA syndromes
Meo, I. D., & Tiranti, V. (2018) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2018.01.008 · Cited by 75
The copper-iron connection: Hereditary aceruloplasminemia
Nittis, T., & Gitlin, J. D. (2002) · Seminars in Hematology · doi:10.1053/shem.2002.35633 · Cited by 74
Self-citationLipiński, P., Styś, A., & Starzyński, R. R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1018-1 · Cited by 76
Hepatic iron overload in aceruloplasminaemia
Hellman, N. E., Schaefer, M., Gehrke, S., Stegen, P., Hoffman, W. J., Gitlin, J. D., & Stremmel, W. (2000) · Gut · doi:10.1136/gut.47.6.858 · Cited by 73
Self-citationSiah, C. W., Trinder, D., & Olynyk, J. K. (2005) · Clinica Chimica Acta · doi:10.1016/j.cccn.2005.02.022 · Cited by 75
Ranganathan, P. N., Lu, Y., Jiang, L., Kim, C., & Collins, J. F. (2011) · Blood · doi:10.1182/blood-2011-05-352112 · Cited by 74
Marques, L., Auriac, A., Willemetz, A., Banha, J., Silva, B. D. R., Canonne‐Hergaux, F., & Costa, L. M. G. (2011) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2011.11.005 · Cited by 73
Iron and Neurodegeneration: From Cellular Homeostasis to Disease
Batista-Nascimento, L. S., Pimentel, C., Menezes, R., & Rodrigues‐Pousada, C. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/128647 · Cited by 74
Iron transport: emerging roles in health and disease
Goswami, T., Rolfs, A., & Hediger, M. A. (2002) · Biochemistry and Cell Biology · doi:10.1139/o02-159 · Cited by 70
Cerebellar ataxia associated with heteroallelic ceruloplasmin gene mutation
Miyajima, H., Kono, S., Takahashi, Y., Sugimoto, M., Sakamoto, M., & Sakai, N. (2001) · Neurology · doi:10.1212/wnl.57.12.2205 · Cited by 68
Oxidative Stress, a Crossroad Between Rare Diseases and Neurodegeneration
Espinós, C., Galindo, M. I., García-Gimeno, M. A., Ibáñez-Cabellos, J. S., Martínez‐Rubio, D., Millán, J. M., Rodrigo, R., Sanz, P., Seco-Cervera, M., Sevilla, T., et al. (2020) · Antioxidants · doi:10.3390/antiox9040313 · Cited by 69
The Role of Hepcidin in Iron Homeostasis and Anemia in Hemodialysis Patients
Eleftheriadis, T., Liakopoulos, V., Antoniadi, G., Kartsios, C., & Stefanidis, I. (2009) · Seminars in Dialysis · doi:10.1111/j.1525-139x.2008.00532.x · Cited by 66
Iron homeostasis: new players, newer insights
Edison, E. S., Bajel, A. R., & Chandy, M. (2008) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2008.01143.x · Cited by 71
Afshari, A., Sourinejad, I., Gharaei, A., Johari, S. A., & Ghasemi, Z. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.736638 · Cited by 66
The (Bio)Chemistry of Non-Transferrin-Bound Iron
Silva, A. M. N., & Rangel, M. (2022) · Molecules · doi:10.3390/molecules27061784 · Cited by 67
Cabrera, A., Alonzo, E., Sauble, E., Chu, Y.-L., Nguyen, D., Linder, M. C., Sato, D. S., & Mason, A. Z. (2008) · BioMetals · doi:10.1007/s10534-008-9139-6 · Cited by 73
Iron transport & homeostasis mechanisms: their role in health & disease.
Nadadur, S. S., Srirama, K., & Mudipalli, A. (2008) · PubMed · Cited by 64
Reeves, P. G., DeMars, L. C. S., Johnson, W. T., & Lukaski, H. C. (2005) · Journal of Nutrition · doi:10.1093/jn/135.1.92 · Cited by 61
The molecular basis of iron overload disorders and iron-linked anemias
Kaplan, J., Ward, D. M., & Domenico, I. D. (2011) · International Journal of Hematology · doi:10.1007/s12185-010-0760-0 · Cited by 62
Iron chelation therapy in aceruloplasminaemia: study of a patient with a novel missense mutation
Mariani, R., Arosio, C., Pelucchi, S., Grisoli, M., Piga, A., Trombini, P., & Piperno, A. (2004) · Gut · doi:10.1136/gut.2003.030429 · Cited by 63
Effects of development and iron status on ceruloplasmin expression in rat brain
Chang, Y. Z., Qian, Z., Wang, K., Zhu, L., Yang, X. D., Du, J. R., Jiang, L. H., Ho, K. P., Wang, Q., & Ke, Y. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20321 · Cited by 64
Metadata
- Authors
- Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D.
- Affiliations
- Washington University in St. Louis (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1999-09-14
- Volume
- 96
- Issue
- 19
- Pages
- 10812-10817
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC17965
- OpenAlex
- W2104657893
- Cited by
- 568
- References
- 40
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 10 · 2023: 13 · 2022: 16 · 2021: 17 · 2020: 20 · 2019: 17 · 2018: 20 · 2017: 14 · 2016: 17 · 2015: 14 · 2014: 18 · 2013: 13 · 2012: 24
- FWCI
- 15.54
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (1p30hd033688-01, 5r01hl041536-13, 5k08dk002464-04, DK02464, HL41536)
- National Heart, Lung, and Blood Institute (HL41536)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK02464)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD 33688)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- ceruloplasmin, aceruloplasminemia, iron efflux, cellular iron homeostasis, iron accumulation, iron metabolism, ferrokinetics, reticuloendothelial cells, hepatocytes, serum ferritin, iron storage
- MeSH terms
- Animals, Apoproteins, Ceruloplasmin, Disease Models, Animal, Homeostasis, Iron, Liver, Metal Metabolism, Inborn Errors, Models, Genetic, Phenotype, Spleen, Time Factors, Mutagenesis, Insertional, Neurodegenerative Diseases, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
