A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans

The Metabolic Basis of Inherited Disease

(1990) · Annals of Internal Medicine · doi:10.7326/0003-4819-112-5-389_2 · Cited by 3,990 · see citing works

The Wilson disease gene is a putative copper transporting P–type ATPase similar to the Menkes gene

Bull, P. C., Thomas, G. R., Rommens, J. M., Forbes, J., & Cox, D. W. (1993) · Nature Genetics · doi:10.1038/ng1293-327 · Cited by 1,939 · see citing works

Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper–transporting ATPase

Vulpe, C. D., Levinson, B., Whitney, S., Packman, S., & Gitschier, J. M. (1993) · Nature Genetics · doi:10.1038/ng0193-7 · Cited by 1,412 · see citing works

The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene

Tanzi, R. E., Petrukhin, K. E., Чернов, И. П., Pellequer, J., Wasco, W., Ross, B., Romano, D., Parano, E., Pavone, P., Brzustowicz, L. M., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-344 · Cited by 1,367 · see citing works

Absorption, transport, and hepatic metabolism of copper and zinc: special reference to metallothionein and ceruloplasmin.

Cousins, R. J. (1985) · Physiological Reviews · doi:10.1152/physrev.1985.65.2.238 · Cited by 1,335 · see citing works

Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein

Chelly, J., Tümer, Z., Tønnesen, T., Petterson, A., Ishikawa-Brush, Y., Tommerup, N., Horn, N., & Monaco, A. P. (1993) · Nature Genetics · doi:10.1038/ng0193-14 · Cited by 718 · see citing works

Isolation of a partial candidate gene for Menkes disease by positional cloning

Mercer, J. F. B., Livingston, J., Hall, B., Paynter, J. A., Begy, C. R., Chandrasekharappa, S. C., Lockhart, P. J., Grimes, A., Bhave, M. R., Siemieniak, D. R., et al. (1993) · Nature Genetics · doi:10.1038/ng0193-20 · Cited by 693 · see citing works

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 · see citing works

The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.

Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670 · see citing works

Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport

Dancis, A., Yuan, D. S., Haile, D., Askwith, C., Eide, D., Moehle, C., Kaplan, J., & Klausner, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90345-x · Cited by 659 · see citing works

Isolation and Characterization of a Human Liver cDNA as a Candidate Gene for Wilson Disease

Yamaguchi, Y., Heiny, M. E., & Gitlin, J. D. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2471 · Cited by 508 · see citing works

Mapping, cloning and genetic characterization of the region containing the Wilson disease gene

Petrukhin, K. E., Fischer, S. G., Pirastu, M., Tanzi, R. E., Чернов, И. П., Devoto, M., Brzustowicz, L. M., Cayanis, E., Vitale, E., Russo, J. J., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-338 · Cited by 501 · see citing works

The role of ceruloplasmin in iron metabolism.

Roeser, H. P., Lee, G. R., Nacht, S., & Cartwright, G. E. (1970) · Journal of Clinical Investigation · doi:10.1172/jci106460 · Cited by 365 · see citing works

Nonsense Mutations in the Dihydrofolate Reductase Gene Affect RNA Processing

Urlaub, G., Mitchell, P. J., Ciudad, C. J., & Chasin, L. A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.7.2868 · Cited by 354 · see citing works

Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration

Miyajima, H., Nishimura, Y., Mimguchi, K., Sakamoto, M., Shimizu, T., & Honda, N. (1987) · Neurology · doi:10.1212/wnl.37.5.761 · Cited by 295 · see citing works

Iron metabolism in copper-deficient swine

Lee, G. R., Nacht, S., Lukens, J. N., & Cartwright, G. E. (1968) · Journal of Clinical Investigation · doi:10.1172/jci105891 · Cited by 259 · see citing works

Hereditary ceruloplasmin deficiency with hemosiderosis: A clinicopathological study of a japanese family

Morita, H., Ikeda, S., Yamamoto, K., Morita, S., Yoshida, K., Nomoto, S., Kato, M., & Yanagisawa, N. (1995) · Annals of Neurology · doi:10.1002/ana.410370515 · Cited by 245 · see citing works

The Mobilization of Iron from the Perfused Mammalian Liver by a Serum Copper Enzyme, Ferroxidase I

Osaki, S., Johnson, D. A., & Frieden, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62284-7 · Cited by 236 · see citing works

Premature Translation Termination Mediates Triosephosphate Isomerase mRNA Degradation

Daar, I. O., & Maquat, L. E. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.2.802 · Cited by 217 · see citing works

Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule.

Takahashi, N., Ortel, T. L., & Putnam, F. W. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.2.390 · Cited by 208 · see citing works

Mechanisms of copper incorporation during the biosynthesis of human ceruloplasmin.

Sato, M., & Gitlin, J. D. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67764-1 · Cited by 191 · see citing works

Translation to Near the Distal End of the Penultimate Exon Is Required for Normal Levels of Spliced Triosephosphate Isomerase mRNA

Cheng, J., Fogel‐Petrovic, M., & Maquat, L. E. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.10.5215 · Cited by 157 · see citing works

Effect of ceruloplasmin on plasma iron in copper-deficient swine

Ragan, H. A., Nacht, S., Lee, G., Bishop, C., & Cartwright, G. (1969) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1969.217.5.1320 · Cited by 146 · see citing works

Characterization, mapping, and expression of the human ceruloplasmin gene.

Yang, F., Naylor, S. L., LUM, J. B., Cutshaw, S., McCombs, J. L., Naberhaus, K. H., McGill, J. R., Adrian, G. S., Moore, C. M., & Barnett, D. R. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.10.3257 · Cited by 139 · see citing works

Severe deficiency of cystic fibrosis transmembrane conductance regulator messenger RNA carrying nonsense mutations R553X and W1316X in respiratory epithelial cells of patients with cystic fibrosis.

Hamosh, A., Trapnell, B. C., Zeitlin, P. L., Montrose‐Rafizadeh, C., Rosenstein, B. J., Crystal, R. G., & Cutting, G. R. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115510 · Cited by 136 · see citing works

Complete cDNA sequence of human preceruloplasmin.

Koschinsky, M. L., Funk, W. D., van Oost, B. A., & MacGillivray, R. T. A. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.14.5086 · Cited by 131 · see citing works

Hereditary caeruloplasmin deficiency, dementia and diabetes mellitus

LOGAN, J. I., HARVEYSON, K. B., WISDOM, G. B., HUGHES, A. E., & ARCHBOLD, G. P. R. (1994) · QJM · doi:10.1093/oxfordjournals.qjmed.a068881 · Cited by 130 · see citing works

Nonsense mutations and diminished mRNA levels

McIntosh, I., Hamosh, A., & Dietz, H. C. (1993) · Nature Genetics · doi:10.1038/ng0793-219 · Cited by 103 · see citing works

Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains.

Ortel, T. L., Takahashi, N., & Putnam, F. W. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.15.4761 · Cited by 100 · see citing works

Disorders of copper transport

Dm, D. (1989) · Medical Entomology and Zoology · Cited by 96 · see citing works

Chemical evidence that proteolytic cleavage causes the heterogeneity present in human ceruloplasmin preparations.

Kingston, I. B., Kingston, B. L., & Putnam, F. W. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5377 · Cited by 76 · see citing works

Effects of iron on copper metabolism and copper on iron metabolism in rats

Owen, C. A. (1973) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1973.224.3.514 · Cited by 75 · see citing works

Internal triplication in the structure of human ceruloplasmin.

Takahashi, N., Bauman, R. A., Ortel, T. L., Dwulet, F. E., Wang, C. C., & Putnam, F. W. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.1.115 · Cited by 58 · see citing works

A nonsense mutation in the apolipoprotein C-IIPadova gene in a patient with apolipoprotein C-II deficiency.

Fojo, S. S., Lohse, P., Parrott, C. L., Baggio, G., Gabelli, C., THOMAS, F. J., Hoffman, J., & Brewer, H. B. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114287 · Cited by 56 · see citing works

Internal duplication and evolution of human ceruloplasmin.

Dwulet, F. E., & Putnam, F. W. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.5.2805 · Cited by 45 · see citing works

Model of the active site in the blue oxidases based on the ceruloplasmin-plastocyanin homology.

Rydén, L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.22.6767 · Cited by 41 · see citing works

Complete amino acid sequence of a histidine-rich proteolytic fragment of human ceruloplasmin.

Kingston, I. B., Kingston, B. L., & Putnam, F. W. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.4.1668 · Cited by 32 · see citing works

Isolation and characterization of a processed gene for human ceruloplasmin

Koschinsky, M. L., Chow, B., Schwartz, J., HAMERTON, J. L., & MacGillivray, R. T. A. (1987) · Biochemistry · doi:10.1021/bi00398a034 · Cited by 25 · see citing works

Circular dichroism study of undegraded human ceruloplasmin

Noyer, M., & Putnam, F. W. (1981) · Biochemistry · doi:10.1021/bi00515a036 · Cited by 22 · see citing works

Metal Ions in Biological Systems

Sigel, H., & Sigel, A. (2024) · CRC Press eBooks · doi:10.1201/9781003573913 · Cited by 21 · see citing works

Isolation of a human ceruloplasmin cDNA clone that includes the N‐terminal leader sequence

Mercer, J. F. B., & Grimes, A. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80739-6 · Cited by 17 · see citing works

[A case of ceruloplasmin deficiency which showed dementia, ataxia and iron deposition in the brain].

Morita, H., Inoue, A., & Yanagisawa, N. (1992) · PubMed · Cited by 14 · see citing works

Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. II. Amino acid sequence of the tryptic peptides.

Kingston, I. B., Kingston, B. L., & Putnam, F. W. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85823-4 · Cited by 12 · see citing works

Ceruloplasmin

Poulik, M. D., & Weiss, M. L. (1975) · Elsevier eBooks · doi:10.1016/b978-0-12-568402-6.50009-9 · Cited by 12 · see citing works

Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.

Kingston, I. B., Kingston, B. L., & Putnam, F. W. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85822-2 · Cited by 11 · see citing works

Lack of Copper Binding Sites in Ceruloplasmin of LEC Rats with Abnormal Copper Metabolism

Hiyamuta, S., & Takeichi, N. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2596 · Cited by 10 · see citing works

Monoclonal Antibody Against the Active Site of Caeruloplasmin and the ELISA System Detecting Active Caeruloplasmin

Hiyamuta, S., & ITO, K. (1994) · Hybridoma · doi:10.1089/hyb.1994.13.139 · Cited by 7 · see citing works

Disorders of Iron Metabolism

Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130 · see citing works

Iron, brain ageing and neurodegenerative disorders

Zecca, L., Youdim, M. B. H., Riederer, P., Connor, J. R., & Crichton, R. R. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1537 · Cited by 1,801 · see citing works

Copper biochemistry and molecular biology

Linder, M. C., & Hazegh-Azam, M. (1996) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/63.5.797 · Cited by 1,443 · see citing works

Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 ( <i>USF2</i> ) knockout mice

Nicolas, G., Bennoun, M., Devaux, I., Beaumont, C., Grandchamp, B., Kahn, A., & Vaulont, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151179498 · Cited by 1,233 · see citing works

Iron metabolism and toxicity

Papanikolaou, G., & Pantopoulos, K. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.06.021 · Cited by 1,070 · see citing works

Trace elements in human physiology and pathology. Copper

Tapiero, H., Townsend, D. M., & Tew, K. D. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(03)00012-x · Cited by 1,046 · see citing works

Hereditary Hemochromatosis — A New Look at an Old Disease

Pietrangelo, A. (2004) · New England Journal of Medicine · doi:10.1056/nejmra031573 · Cited by 992 · see citing works

C ERULOPLASMIN M ETABOLISM AND F UNCTION

Hellman, N. E., & Gitlin, J. D. (2002) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.22.012502.114457 · Cited by 954 · see citing works

The Role of Copper in Neurodegenerative Disease

Waggoner, D., Bartnikas, T. B., & Gitlin, J. D. (1999) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0250 · Cited by 864 · see citing works

The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells

Richardson, D. R., & Ponka, P. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(96)00014-7 · Cited by 714 · see citing works

A permease-oxidase complex involved in high-affinity iron uptake in yeast.

Stearman, R., Yuan, D. S., Yamaguchi-Iwai, Y., Klausner, R. D., & Dancis, A. (1996) · Science · doi:10.1126/science.271.5255.1552 · Cited by 683 · see citing works

h CTR1 : A human gene for copper uptake identified by complementation in yeast

Zhou, B., & Gitschier, J. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7481 · Cited by 572 · see citing works

Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux

Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10812 · Cited by 568 · see citing works

Copper and iron disorders of the brain

Madsen, E., & Gitlin, J. D. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.30.051606.094232 · Cited by 557 · see citing works

Metabolism and functions of copper in brain

Scheiber, I. F., Mercer, J. F. B., & Dringen, R. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.01.002 · Cited by 524 · see citing works

Iron homeostasis: insights from genetics and animal models

Andrews, N. C. (2000) · Nature Reviews Genetics · doi:10.1038/35042073 · Cited by 425 · see citing works

The copper transporter CTR1 provides an essential function in mammalian embryonic development

Kuo, Y., Zhou, B., Cosco, D., & Gitschier, J. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111057298 · Cited by 402 · see citing works

Identification and Functional Expression of HAH1, a Novel Human Gene Involved in Copper Homeostasis

Klomp, L. W. J., Lin, S.-J., Yuan, D., Klausner, R. D., Culotta, V., & Gitlin, J. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9221 · Cited by 383 · see citing works

The ferroportin disease

Pietrangelo, A. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2003.08.003 · Cited by 382 · see citing works

Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury

Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J.-P., & David, S. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06578.2002 · Cited by 379 · see citing works

DMT1: A mammalian transporter for multiple metals

Garrick, M. D., Dolan, K. G., Horbinski, C., Ghio, A. J., Higgins, D. M., Porubcin, M., Moore, E., Hainsworth, L. N., Umbreit, J. N., Conrad, M. E., et al. (2003) · BioMetals · doi:10.1023/a:1020702213099 · Cited by 378 · see citing works

Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system

Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377 · see citing works

Iron Metabolism in the Reticuloendothelial System

Knutson, M. D., & Wessling‐Resnick, M. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609210 · Cited by 360 · see citing works

Hepcidin, A New Iron Regulatory Peptide

Nicolas, G., Viatte, L., Bennoun, M., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0573 · Cited by 354 · see citing works

Iron misregulation in the brain: a primary cause of neurodegenerative disorders

Ke, Y., & Qian, Z. (2003) · The Lancet Neurology · doi:10.1016/s1474-4422(03)00353-3 · Cited by 341 · see citing works

The Inherited Basis of Diabetes Mellitus: Implications for the Genetic Analysis of Complex Traits

Florez, J. C., Hirschhorn, J., & Altshuler, D. (2003) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.4.070802.110436 · Cited by 329 · see citing works

A Novel Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin Is Expressed by Mammalian Astrocytes

Patel, B. N., & David, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.20185 · Cited by 327 · see citing works

The Role of Iron Regulation in Immunometabolism and Immune-Related Disease

Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works

The molecular basis of copper-transport diseases

Mercer, J. F. B. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)01920-7 · Cited by 297 · see citing works

THE MOLECULAR BIOLOGY OF METAL ION TRANSPORT INSACCHAROMYCES CEREVISIAE

Eide, D. J. (1998) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.18.1.441 · Cited by 295 · see citing works

Iron mediated toxicity and programmed cell death: A review and a re-examination of existing paradigms

Eid, R., Arab, N. T. T., & Greenwood, M. T. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.12.002 · Cited by 295 · see citing works

Genetic and molecular basis for copper toxicity

Harris, Z. L., & Gitlin, J. (1996) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/63.5.836 · Cited by 286 · see citing works

Cellular iron metabolism

Ponka, P. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.055suppl.69002.x · Cited by 278 · see citing works

Copper transport

Linder, M. C., Wooten, L., Cerveza, P., Cotton, S., Shulze, R., & Lomeli, N. A. (1998) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/67.5.965s · Cited by 273 · see citing works

Iron Homeostasis in the Liver

Anderson, E. R., & Shah, Y. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120016 · Cited by 259 · see citing works

Aceruloplasminemia: an inherited neurodegenerative disease with impairment of iron homeostasis

Harris, Z. L., Klomp, L. W. J., & Gitlin, J. (1998) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/67.5.972s · Cited by 254 · see citing works

Old iron, young copper: from Mars to Venus

Crichton, R. R., & Pierre, J.-L. (2001) · Biometals · doi:10.1023/a:1016710810701 · Cited by 248 · see citing works

The long history of iron in the Universe and in health and disease

Sheftel, A. D., Mason, A. B., & Ponka, P. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.002 · Cited by 243 · see citing works

Brain iron metabolism: Neurobiology and neurochemistry

Ke, Y., & Qian, Z. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.07.009 · Cited by 239 · see citing works

Iron and neurodegenerative disorders

Thompson, K. J., Shoham, S., & Connor, J. R. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00510-x · Cited by 235 · see citing works

Expression of iron transport proteins and excessive iron accumulation in the brain in neurodegenerative disorders

Qian, Z., & Wang, Q. (1998) · Brain Research Reviews · doi:10.1016/s0165-0173(98)00012-5 · Cited by 230 · see citing works

The iron metabolism of neoplastic cells: Alterations that facilitate proliferation?

Kwok, J. C., & Richardson, D. R. (2002) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(01)00213-x · Cited by 215 · see citing works

Structure to function relationships in ceruloplasmin: a 'moonlighting' protein

Bielli, P., & Calabrese, L. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8519-2 · Cited by 212 · see citing works

A mutation, in the iron-responsive element of H ferritin mRNA, causing autosomal dominant iron overload.

Kato, J., Fujikawa, K., Kanda, M., Fukuda, N., Sasaki, K., Takayama, T., Kobune, M., Takada, K., Takimoto, R., Hamada, H., et al. (2001) · The American Journal of Human Genetics · doi:10.1086/321261 · Cited by 211 · see citing works

Iron Metabolism: Iron Deficiency and Iron Overload

Andrews, N. C. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.75 · Cited by 211 · see citing works

Copper and Copper Proteins in Parkinson’s Disease

Montes, S., Rivera-Mancia, S., Diaz-Ruiz, A., Tristan-Lopez, L., & Rios, C. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/147251 · Cited by 203 · see citing works

Alternative RNA Splicing Generates a Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin in Mammalian Brain

Patel, B. N., Dunn, R. J., & David, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4305 · Cited by 202 · see citing works

Design of base-discriminating fluorescent nucleosides

Okamoto, A., Saito, Y., & Saito, I. (2005) · Journal of Photochemistry and Photobiology C Photochemistry Reviews · doi:10.1016/j.jphotochemrev.2005.07.002 · Cited by 196 · see citing works

Ceruloplasmin gene expression in the murine central nervous system.

Klomp, L. W. J., Farhangrazi, Z. S., Dugan, L. L., & Gitlin, J. D. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118768 · Cited by 194 · see citing works

A Systems Biology Approach to Iron Metabolism

Chifman, J., Laubenbacher, R., & Torti, S. V. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-2095-2_10 · Cited by 188 · see citing works

Brain Iron Metabolism Dysfunction in Parkinson’s Disease

Jiang, H. F., Wang, J., Rogers, J. T., & Xie, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9879-1 · Cited by 184 · see citing works

Iron homeostasis: new tales from the crypt

Roy, C. N., & Enns, C. A. (2000) · Blood · doi:10.1182/blood.v96.13.4020 · Cited by 177 · see citing works

Ceruloplasmin and cardiovascular disease

Fox, P. L., Mazumder, B., Ehrenwald, E., & Mukhopadhyay, C. K. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00231-8 · Cited by 176 · see citing works

Mechanisms of Copper Incorporation into Human Ceruloplasmin

Hellman, N. E., Kono, S., Mancini, G. M. S., Hoogeboom, A. J. M., de Jong, G. J., & Gitlin, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206246200 · Cited by 175 · see citing works

Use of desferrioxamine in the treatment of aceruloplasminemia

Miyajima, H., Takahashi, Y., Kamata, T., Shimizu, H., Sakai, N., & Gitlin, J. D. (1997) · Annals of Neurology · doi:10.1002/ana.410410318 · Cited by 173 · see citing works

Classification and diagnosis of iron overload.

Piperno, A. (1998) · PubMed · Cited by 171 · see citing works

The Regulation of Cellular Iron Metabolism

Chua, A. C. G., Graham, R. M., Trinder, D., & Olynyk, J. K. (2007) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701428257 · Cited by 171 · see citing works

Genetic Defects in Copper Metabolism

Shim, H., & Harris, Z. L. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1527s · Cited by 167 · see citing works

Cerebral Iron Deposition in Neurodegeneration

Dušek, P., Hofer, T., Alexander, J., Roos, P. M., & Aaseth, J. (2022) · Biomolecules · doi:10.3390/biom12050714 · Cited by 166 · see citing works

Effect of copper deficiency on prenatal development and pregnancy outcome

Keen, C. L., Uriu‐Hare, J. Y., Hawk, S. N., Jankowski, M., Daston, G. P., Kwik-Uribe, C. L., & Rucker, R. B. (1998) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/67.5.1003s · Cited by 166 · see citing works

Restriction of Copper Export in Saccharomyces cerevisiae to a Late Golgi or Post-Golgi Compartment in the Secretory Pathway

Yuan, D., Dancis, A., & Klausner, R. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.41.25787 · Cited by 166 · see citing works

The Molecular Basis of Copper Homeostasis Copper-Related Disorders

Llanos, R. M., & Mercer, J. F. B. (2002) · DNA and Cell Biology · doi:10.1089/104454902753759681 · Cited by 165 · see citing works

Neurodegeneration with brain iron accumulation: update on pathogenic mechanisms

Levi, S., & Finazzi, D. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00099 · Cited by 164 · see citing works

Iron transport across the blood–brain barrier: development, neurovascular regulation and cerebral amyloid angiopathy

McCarthy, R. C., & Kosman, D. J. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1771-4 · Cited by 163 · see citing works

Nigral Iron Elevation Is an Invariable Feature of Parkinson’s Disease and Is a Sufficient Cause of Neurodegeneration

Ayton, S., & Lei, P. (2014) · BioMed Research International · doi:10.1155/2014/581256 · Cited by 163 · see citing works

Genetic and Clinical Description of Hemochromatosis Probands and Heterozygotes: Evidence That Multiple Genes Linked to the Major Histocompatibility Complex Are Responsible for Hemochromatosis

Barton, J. C., Shih, W. W. H., Sawada-Hirai, R., Acton, R. T., Harmon, L., Rivers, C. A., & Rothenberg, B. E. (1997) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.1997.0129 · Cited by 163 · see citing works

Expression of the ceruloplasmin gene in the human retina and brain: implications for a pathogenic model in aceruloplasminemia

Klomp, L. W. J. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.12.1989 · Cited by 161 · see citing works

Aceruloplasminemia: An Inherited Neurodegenerative Disease with Impairment of Iron Homeostasis

XU, X., PIN, S., GATHINJI, M., FUCHS, R., & HARRIS, Z. L. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.024 · Cited by 160 · see citing works

Basic and Clinical Aspects of Copper

Harris, E. D. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360390250649 · Cited by 156 · see citing works

Ceruloplasmin in neurodegenerative diseases

Vassiliev, V. B., Harris, Z. L., & Zatta, P. F. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.03.003 · Cited by 151 · see citing works

Age-Related Changes in Iron Homeostasis and Cell Death in the Cerebellum of Ceruloplasmin-Deficient Mice

Jeong, S. Y., & David, S. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2922-06.2006 · Cited by 149 · see citing works

Parkinson's disease: Alterations in iron and redox biology as a key to unlock therapeutic strategies

Ma, L., Azad, M. G., Dharmasivam, M., Richardson, V., Quinn, R. J., Feng, Y., Pountney, D. L., Tonissen, K. F., Mellick, G. D., Yanatori, I., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101896 · Cited by 148 · see citing works

Does oxidative stress change ceruloplasmin from a protective to a vasculopathic factor?

Shukla, N., Maher, J., Masters, J. M., Angelini, G. D., & Jeremy, J. Y. (2006) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.11.035 · Cited by 146 · see citing works

Copper in medicine

Brewer, G. J. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(03)00018-8 · Cited by 144 · see citing works

Ceruloplasmin Ferroxidase Activity Stimulates Cellular Iron Uptake by a Trivalent Cation-specific Transport Mechanism

Attieh, Z. K., Mukhopadhyay, C. K., Seshadri, V., Tripoulas, N. A., & Fox, P. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.1116 · Cited by 144 · see citing works

Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites

Bento, I., Peixoto, C., Zaitsev, V., & Lindley, P. F. (2007) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744490604947x · Cited by 144 · see citing works

Neurodegeneration with brain iron accumulation–clinical syndromes and neuroimaging

Schipper, H. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.06.016 · Cited by 141 · see citing works

Aceruloplasminemia

Gitlin, J. D. (1998) · Pediatric Research · doi:10.1203/00006450-199809000-00001 · Cited by 140 · see citing works

Review: Insights into molecular mechanisms of disease in neurodegeneration with brain iron accumulation: unifying theories

Arber, C., Li, A., Houlden, H., & Wray, S. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12242 · Cited by 139 · see citing works

Copper dyshomoeostasis in Parkinson's disease: implications for pathogenesis and indications for novel therapeutics

Davies, K. M., Mercer, J. F. B., Chen, N., & Double, K. L. (2016) · Clinical Science · doi:10.1042/cs20150153 · Cited by 139 · see citing works

The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains

deMaré, F., Kurtz, D. M. J., & Nordlund, P. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0696-539 · Cited by 138 · see citing works

Copper Transporting P-Type ATPases and Human Disease

Cox, D. W., & Moore, S. D. P. (2002) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1021293818125 · Cited by 137 · see citing works

The Classification of Autosomal Recessive Cerebellar Ataxias: a Consensus Statement from the Society for Research on the Cerebellum and Ataxias Task Force

Beaudin, M., Matilla‐Dueñas, A., Soong, B., Pedroso, J. L., Barsottini, O. G. P., Mitoma, H., Tsuji, S., Schmahmann, J. D., Manto, M. U., Rouleau, G. A., et al. (2019) · The Cerebellum · doi:10.1007/s12311-019-01052-2 · Cited by 136 · see citing works

Aceruloplasminemia, an inherited disorder of iron metabolism

Miyajima, H., Takahashi, Y., & Kono, S. (2003) · BioMetals · doi:10.1023/a:1020775101654 · Cited by 136 · see citing works

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 · see citing works

Aceruloplasminemia, an iron metabolic disorder

Miyajima, H. (2003) · Neuropathology · doi:10.1046/j.1440-1789.2003.00521.x · Cited by 135 · see citing works

Relative Roles of Albumin and Ceruloplasmin in the Formation of Homocystine, Homocysteine-Cysteine-mixed Disulfide, and Cystine in Circulation

Sengupta, S., Wehbe, C., Majors, A. K., Ketterer, M. E., DiBello, P. M., & Jacobsen, D. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108451200 · Cited by 134 · see citing works

Current approach to hemochromatosis

Brissot, P., Troadec, M., Bardou‐Jacquet, E., Lan, C. L., Jouanolle, A., Deugnier, Y., & Loréal, O. (2008) · Blood Reviews · doi:10.1016/j.blre.2008.03.001 · Cited by 132 · see citing works

Iron in the Brain: An Important Contributor in Normal and Diseased States

Piñero, D. J., & Connor, J. R. (2000) · The Neuroscientist · doi:10.1177/107385840000600607 · Cited by 132 · see citing works

Transcript-Selective Translational Silencing by Gamma Interferon Is Directed by a Novel Structural Element in the Ceruloplasmin mRNA 3′ Untranslated Region

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 · see citing works

Non- HFE hemochromatosis

Pietrangelo, A. (2004) · Hepatology · doi:10.1002/hep.20007 · Cited by 127 · see citing works

Purification and Characterization of Fet3 Protein, a Yeast Homologue of Ceruloplasmin

de Silva, D., Davis-Kaplan, S. R., Fergestad, J., & Kaplan, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14208 · Cited by 124 · see citing works

Iron Metabolism in Eukaryotes—Mars and Venus at It Again

Kaplan, J., & O’Halloran, T. V. (1996) · Science · doi:10.1126/science.271.5255.1510 · Cited by 124 · see citing works

Identification of zyklopen, a new member of the vertebrate multicopper ferroxidase family, and characterization in rodents and human cells

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 · see citing works

Molecular biology of iron acquisition in Saccharomyces cerevisiae

Askwith, C. C., de Silva, D., & Kaplan, J. (1996) · Molecular Microbiology · doi:10.1111/j.1365-2958.1996.tb02485.x · Cited by 122 · see citing works

Brain iron transport

Qian, Z., & Ke, Y. (2019) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12521 · Cited by 118 · see citing works

Characterization of a Nonsense Mutation in the Ceruloplasmin Gene Resulting in Diabetes and Neurodegenerative Disease

Takahashi, Y., Miyajima, H., Shirabe, S., Nagataki, S., Suenaga, A., & Gitlin, J. D. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.1.81 · Cited by 118 · see citing works

Hereditary Hemochromatosis: Genetic Complexity and New Diagnostic Approaches

Swinkels, D. W., Janssen, M. C. H., Bergmans, J., & Marx, J. J. M. (2006) · Clinical Chemistry · doi:10.1373/clinchem.2006.068684 · Cited by 116 · see citing works

Genetic epidemiology of type 1 diabetes

Hirschhorn, J. N. (2003) · Pediatric Diabetes · doi:10.1034/j.1399-5448.2001.00013.x · Cited by 112 · see citing works

Hereditary ceruloplasmin deficiency with hemosiderosis

Okamoto, N., Wada, S., Oga, T., Kawabata, Y., Baba, Y., Habu, D., Takeda, Z., & Wada, Y. (1996) · Human Genetics · doi:10.1007/bf02346185 · Cited by 112 · see citing works

A novel splicing mutation in the ceruloplasmin gene responsible for hereditary ceruloplasmin deficiency with hemosiderosis

Yazaki, M., Yoshida, K., Nakamura, A., Furihata, K., Yonekawa, M., Okabe, T., Yamashita, N., Ohta, M., & Ikeda, S. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00015-x · Cited by 49 · see citing works

Hereditary ceruloplasmin deficiency with hemosiderosis

Okamoto, N., Wada, S., Oga, T., Kawabata, Y., Baba, Y., Habu, D., Takeda, Z., & Wada, Y. (1996) · Human Genetics · doi:10.1007/bf02346185 · Cited by 112 · see citing works

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 · see citing works

[A case of aceruloplasminemia presenting as cerebellar ataxia with homozygous mutation nt2602 delG].

Nagata, M., Takiyama, Y., Shimazaki, H., Nakano, I., & Miyajima, H. (2004) · PubMed · Cited by 2 · see citing works

Characterization of a Nonsense Mutation in the Ceruloplasmin Gene Resulting in Diabetes and Neurodegenerative Disease

Takahashi, Y., Miyajima, H., Shirabe, S., Nagataki, S., Suenaga, A., & Gitlin, J. D. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.1.81 · Cited by 118 · see citing works