The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Mobilization of liver iron by ferroxidase (ceruloplasmin).
Open accessAbstract
Abstract Iron was mobilized by human ferroxidase from dog liver into the perfusate under simulated physiological conditions. The rate of mobilization was estimated to be 1.8 µm per min per 4.9 µm ferroxidase. Human serum albumin with trace copper was found to be inactive in iron mobilization. The low Km and high k1 values of ferroxidase toward ferrous ion enabled us to deduce that the elimination of free iron in the perfusate by ferroxidase would generate a very steep concentration gradient between iron storage cells and the capillary system. This concentration gradient would promote a rapid iron out-flux from the cells by diffusion.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“Transport is facilitated by multicopper ferroxidases including the abundant serum protein ceruloplasmin and its membrane-bound intestinal homolog hephaestin.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [80]
Citations
Cites
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
Holmberg, C. G., Laurell, C. ‐., Åkeson, Å., Linnasalmi, A., & Laukkanen, P. (1947) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.01-0944 · Cited by 212
Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase (Ceruloplasmin)
Osaki, S. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99669-9 · Cited by 160
Lahey, M. E., Gubler, C. J., Chase, M., Cartwright, G. E., & Wintrobe, M. M. (1952) · Blood · doi:10.1182/blood.v7.11.1053.1053 · Cited by 136
A Micromethod for the Determination of Ferroxidase (Ceruloplasmin) in Human Serums
Johnson, D. A., Osaki, S., & Frieden, E. (1967) · Clinical Chemistry · doi:10.1093/clinchem/13.2.142 · Cited by 108
Copper deficiency and copper toxicity in the rat
Owen, C. A., & Hazelrig, J. (1968) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1968.215.2.334 · Cited by 76
Mobilization of iron from ferritin by chelating agents
Pape, L., Multani, J. S., Stitt, C., & Saltman, P. (1968) · Biochemistry · doi:10.1021/bi00842a015 · Cited by 64
Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase
Osaki, S., & Walaas, O. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99620-1 · Cited by 62
Cartwright, G. E., Gubler, C. J., BUSH, J. A., & Wintrobe, M. M. (1956) · Blood · doi:10.1182/blood.v11.2.143.143 · Cited by 55
THE NECESSITY OF COPPER AS A SUPPLEMENT TO IRON FOR HEMOGLOBIN FORMATION IN THE PIG
Elvehjem, C. A., & Hart, E. B. (1932) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)76382-5 · Cited by 39
Research works printed but not linked: 1
- Ragan, H. A., Nacht, S., Leb, G. R., Bishop, C. R., and Cartwright, G. E., Amer. J. Physiol., in press.
Cited by
Sorted by citations
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
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
Drakesmith, H., Nemeth, E., & Ganz, T. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.006 · Cited by 638
Forging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623
Iron homeostasis: insights from genetics and animal models
Andrews, N. C. (2000) · Nature Reviews Genetics · doi:10.1038/35042073 · Cited by 425
Ceruloplasmin. A scavenger of superoxide anion radicals.
Goldstein, I. M., Kaplan, H. B., Edelson, H. S., & Weissmann, G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50692-x · Cited by 365
Iron Metabolism: A Comprehensive Review
Beard, J. L., Dawson, H. D., & Piñero, D. J. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1996.tb03794.x · Cited by 323
Ceruloplasmin and other copper binding components of blood plasma and their functions: an update
Linder, M. C. (2016) · Metallomics · doi:10.1039/c6mt00103c · Cited by 327
Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
Mukhopadhyay, C. K., Mazumder, B., & Fox, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000636200 · Cited by 274
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
Chillappagari, S., Seubert, A., Trip, H., Kuipers, O. P., Marahiel, M. A., & Miethke, M. (2010) · Journal of Bacteriology · doi:10.1128/jb.00058-10 · Cited by 249
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
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 244
Anderson, E. R., & Shah, Y. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120016 · Cited by 262
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
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
Caeruloplasmin: Physiological and Pathological Perspectives
Gutteridge, J. M. C., & Stocks, J. (1981) · CRC Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408368109105866 · Cited by 217
Singh, N., Haldar, S., Tripathi, A. K., Horback, K., Wong, J., Sharma, D., Beserra, A., Suda, S., Anbalagan, C., Dev, S., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4931 · Cited by 208
Metal ions in macrophage antimicrobial pathways: emerging roles for zinc and copper
Stafford, S. L., Bokil, N. J., Achard, M. E. S., Kapétanovic, R., Schembri, M. A., McEwan, A. G., & Sweet, M. J. (2013) · Bioscience Reports · doi:10.1042/bsr20130014 · Cited by 217
Role of Ceruloplasmin in Cellular Iron Uptake
Mukhopadhyay, C. K., Attieh, Z. K., & Fox, P. L. (1998) · Science · doi:10.1126/science.279.5351.714 · Cited by 199
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
Thompson, K., Menzies, S. L., Muckenthaler, M. U., Torti, F. M., Wood, T. L., Torti, S. V., Hentze, M. W., Beard, J., & Connor, J. R. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10463 · Cited by 171
Copper Availability Contributes to Iron Perturbations in Human Nonalcoholic Fatty Liver Disease
Aigner, E. S., Theurl, I., Haufe, H., Seifert, M., Hohla, F., Scharinger, L., Stickel, F., Mourlane, F., Weiß, G., & Datz, C. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.04.007 · Cited by 165
The copper-iron chronicles: The story of an intimate relationship
Fox, P. L. (2003) · BioMetals · doi:10.1023/a:1020799512190 · Cited by 168
Genetic Defects in Copper Metabolism
Shim, H., & Harris, Z. L. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1527s · Cited by 167
Klomp, L. W. J. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.12.1989 · Cited by 161
Unexpected role of ceruloplasmin in intestinal iron absorption
Cherukuri, S., Potla, R., Sarkar, J., Nurko, S., Harris, Z. L., & Fox, P. L. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.003 · Cited by 163
Copper storage diseases: Menkes, Wilson's, and Cancer
Kenyon, G. L. (2004) · Frontiers in bioscience · doi:10.2741/1424 · Cited by 146
Basic and Clinical Aspects of Copper
Harris, E. D. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360390250649 · Cited by 156
Carroll, J. A., Reuter, R. R., Chase, C. C., Coleman, S. W., Riley, D. G., Spiers, D. E., Arthington, J. D., & Galyean, M. L. (2009) · Innate Immunity · doi:10.1177/1753425908099170 · Cited by 133
The molecular basis of copper and iron interactions
Sharp, P. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004386 · Cited by 125
Hepcidin – central regulator of iron metabolism
Atanasiu, V., Manolescu, B. N., & Stoian, I. A.-M. (2006) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2006.00772.x · Cited by 123
Redox Cycling in Iron Uptake, Efflux, and Trafficking
Kosman, D. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.113217 · Cited by 127
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
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
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
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
Rincker, M. J., Hill, G. M., Link, J. E., & Rowntree, J. E. (2004) · Journal of Animal Science · doi:10.2527/2004.82113189x · Cited by 94
Machonkin, T. E., Quintanar, L., Palmer, A. E., Hassett, R. F., Severance, S., Kosman, D. J., & Solomon, E. I. (2001) · Journal of the American Chemical Society · doi:10.1021/ja003975s · Cited by 88
Rincker, M. J., Hill, G. M., Link, J. E., Meyer, A. M., & Rowntree, J. E. (2005) · Journal of Animal Science · doi:10.2527/2005.83122762x · Cited by 88
Machonkin, T. E., Zhang, H. H., Hedman, B., Hodgson, K. O., & Solomon, E. I. (1998) · Biochemistry · doi:10.1021/bi980434v · Cited by 87
Mocchegiani, E., Costarelli, L., Giacconi, R., Malavolta, M., Basso, A., Piacenza, F., Ostan, R., Cevenini, E., Gonos, E. S., & Monti, D. (2014) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2013.12.007 · Cited by 86
Early weaning alters the acute-phase reaction to an endotoxin challenge in beef calves1
Carroll, J. A., Arthington, J. D., & Chase, C. C. (2009) · Journal of Animal Science · doi:10.2527/jas.2009-2016 · Cited by 85
Iron Transport Across Biologic Membranes
Andrews, N. C., Fleming, M. D., & Gunshin, H. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1999.tb06934.x · Cited by 84
Mocchegiani, E., Costarelli, L., Giacconi, R., Piacenza, F., Basso, A., & Malavolta, M. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.01.004 · Cited by 83
Zumbrennen‐Bullough, K. B., & Babitt, J. L. (2013) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gft443 · Cited by 82
Machonkin, T. E., & Solomon, E. I. (2000) · Journal of the American Chemical Society · doi:10.1021/ja002339r · Cited by 78
Genetic Disorders Affecting Proteins of Iron Metabolism: Clinical Implications
Sheth, S., & Brittenham, G. M. (2000) · Annual Review of Medicine · doi:10.1146/annurev.med.51.1.443 · 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
Molecular mechanisms of copper homeostasis
Lalioti, V. S. (2009) · Frontiers in bioscience · doi:10.2741/3575 · Cited by 68
Hepatic iron accumulation in copper-deficient rats
Williams, D. M., Kennedy, F. S., & Green, B. G. (1983) · British Journal Of Nutrition · doi:10.1079/bjn19830136 · Cited by 66
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
Neuroinflammation and Copper in Alzheimer’s Disease
Choo, X. Y., Alukaidey, L., White, A. R., & Grubman, A. (2013) · International Journal of Alzheimer s Disease · doi:10.1155/2013/145345 · Cited by 70
Fetal regulation of iron transport during pregnancy
Gambling, L., Lang, C., & McArdle, H. J. (2011) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.000885 · Cited by 65
Identification and Purification of a Non-Ceruloplasmin Ferroxidase of Human Serum
Topham, R. W., & Frieden, E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62590-6 · Cited by 64
The transfer of iron between ceruloplasmin and transferrins
White, K., Conesa, C., Sánchez, L., Amini, M., Farnaud, S., Lorvoralak, C., & Evans, R. W. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.10.006 · Cited by 60
Role of ceruloplasmin and ascorbate in cellular iron release
Richardson, D. R. (1999) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(99)90166-x · Cited by 61
Plasma ceruloplasmin Evidence for its presence in and uptake by heart and other organs of the rat
Linder, M. C., & Moor, J. R. (1977) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(77)90064-2 · Cited by 60
Iron uptake and transfer from ceruloplasmin to transferrin
Eid, C., Hémadi, M., Duong, N.-T. H., & Chahine, J. E. H. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.01.011 · Cited by 57
Iron and copper, and their interactions during development
Gambling, L., Andersen, H. S., & McArdle, H. J. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361258 · Cited by 56
Iron homeostasis and inherited iron overload disorders: an overview
Heeney, M. M., & Andrews, N. C. (2004) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2004.06.018 · Cited by 56
Tapryal, N., Mukhopadhyay, C., Das, D., Fox, P. L., & Mukhopadhyay, C. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804079200 · Cited by 54
Young, S. N., & Curzon, G. (1972) · Biochemical Journal · doi:10.1042/bj1290273 · Cited by 54
Banha, J., Marques, L., Oliveira, R., Martins, M. D. F., Paixão, E., Pereira, D., Malhó, R., Penque, D., & Costa, L. M. G. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.10.032 · Cited by 53
Fuqua, B. K., Lu, Y., Frazer, D. M., Darshan, D., Wilkins, S. J., Dunn, L. A., Loguinov, A. V., Kogan, S. C., Matak, P., Chen, H., et al. (2018) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2018.06.006 · Cited by 56
Looking for a partner: ceruloplasmin in protein–protein interactions
Vasilyev, V. B. (2019) · BioMetals · doi:10.1007/s10534-019-00189-1 · Cited by 54
Iron and copper homeostasis and intestinal absorption using the Caco2 cell model
Linder, M. C., Zerounian, N. R., Moriya, M., & Malpe, R. (2003) · BioMetals · doi:10.1023/a:1020729831696 · Cited by 49
Craig, P. M., Galus, M., Wood, C. M., & McClelland, G. B. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90581.2008 · Cited by 49
Placental ceruloplasmin homolog is regulated by iron and copper and is implicated in iron metabolism
Danzeisen, R., Fosset, C., Chariana, Z., Page, K., David, S., & McArdle, H. J. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00019.2001 · Cited by 48
Redox active iron accumulation in aceruloplasminemia
Gonzalez‐Cuyar, L. F., Perry, G. L., Miyajima, H., Atwood, C., Ángel, M. R., Lyons, P. F., Siedlak, S. L., Smith, M. A., & Castellani, R. J. (2008) · Neuropathology · doi:10.1111/j.1440-1789.2008.00901.x · Cited by 47
Effects of copper and ceruloplasmin on iron transport in the Caco 2 cell intestinal model
Zerounian, N. R., & Linder, M. C. (2002) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(01)00205-4 · Cited by 46
Iron in Alzheimer’s Disease: From Physiology to Disease Disabilities
Pal, A., Cerchiaro, G., Rani, I., Ventriglia, M., Rongioletti, M. C. A., Longobardi, A., & Squitti, R. (2022) · Biomolecules · doi:10.3390/biom12091248 · Cited by 49
Danzeisen, R., Ponnambalam, S., Lea, R. G., Page, K., Gambling, L., & McArdle, H. J. (2000) · Placenta · doi:10.1053/plac.2000.0582 · Cited by 47
The therapeutic potential of iron chelators
Richardson, D. R. (1999) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.8.12.2141 · Cited by 42
Siotto, M., Pasqualetti, P., Marano, M., & Squitti, R. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1196-0 · Cited by 42
Evidence for the participation of intestinal xanthine oxidase in the mucosal processing of iron
Topham, R. W., Walker, M. C., Calisch, M. P., & Williams, R. W. (1982) · Biochemistry · doi:10.1021/bi00262a002 · Cited by 40
Ficiarà, E., Munir, Z., Boschi, S., Caligiuri, M. E., & Guiot, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094479 · Cited by 40
Dw, C. (1995) · Europe PMC (PubMed Central) · Cited by 38
Copper deficiency with increased hematogones mimicking refractory anemia with excess blasts
Koca, E., Büyükaşık, Y., Çetiner, D., Yılmaz, R., Sayınalp, N., Yasavul, Ü., & Üner, A. (2007) · Leukemia Research · doi:10.1016/j.leukres.2007.06.023 · Cited by 37
Das, D., Tapryal, N., Goswami, S. K., Fox, P. L., & Mukhopadhyay, C. K. (2007) · Biochemical Journal · doi:10.1042/bj20060963 · Cited by 37
Copper and Iron: A landmark connection of two essential metals
Harris, E. D. (2001) · The Journal of Trace Elements in Experimental Medicine · doi:10.1002/jtra.1029 · Cited by 36
Dual Role of Insulin in Transcriptional Regulation of the Acute Phase Reactant Ceruloplasmin
Seshadri, V., Fox, P. L., & Mukhopadhyay, C. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203610200 · Cited by 34
Gray, L. W., Kidane, T. Z., Nguyen, A., Akagi, S., Petrasek, K., Chu, Y.-L., Cabrera, A., Kantardjieff, K. A., Mason, A. Z., & Linder, M. C. (2008) · Biochemical Journal · doi:10.1042/bj20081983 · Cited by 33
Wong, B. X. W., Ayton, S., Lam, L. Q., Lei, P., Adlard, P. A., Bush, A. I., & Duce, J. A. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.08.006 · Cited by 32
The Amyloid Precursor Protein (APP) Does Not Have a Ferroxidase Site in Its E2 Domain
Ebrahimi, K. H., Dienemann, C., Hoefgen, S., Than, M. E., Hagedoorn, P., & Hagen, W. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072177 · Cited by 30
Caeruloplasmin: The enigmatic copper protein
Laurie, S. H. (1980) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80457-9 · Cited by 30
Biochemistry and Molecular Biology of Copper in Mammals
Linder, M. C. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-288-3_1 · Cited by 29
Pourvali, K., Matak, P., Latunde-Dada, G. O., Solomou, S., Mastrogiannaki, M., Peyssonnaux, C., & Sharp, P. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.05.058 · Cited by 29
Metzler-Zebeli, B. U., Caine, W. R., McFall, M. E., Miller, B., Ward, T. L., Kirkwood, R. N., & Mosenthin, R. (2009) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/j.1439-0396.2008.00904.x · Cited by 28
Iron metabolism in mammalian cells
Walker, B., Tiong, J., & Jefferies, W. A. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)11020-x · Cited by 27
Ceruloplasmin Induces Polymorphonuclear Leukocyte Priming in Localized Aggressive Periodontitis
Iwata, T., Kantarcı, A., Yagi, M., Jackson, T. S., Hastürk, H., Kurihara, H., & Dyke, T. E. V. (2009) · Journal of Periodontology · doi:10.1902/jop.2009.090092 · Cited by 26
Hematogone Hyperplasia in Copper Deficiency
Sutton, L. M., Vusirikala, M., & Chen, W. (2009) · American Journal of Clinical Pathology · doi:10.1309/ajcps3enuq5lkbsb · Cited by 26
Effect of Excess Dietary Zinc on Tissue Storage of Iron in Rats
O'Neil-Cutting, M. A., Bomford, A. B., & Munro, H. N. (1981) · Journal of Nutrition · doi:10.1093/jn/111.11.1969 · Cited by 26
Coppen, D. E., & Davies, N. T. (1988) · British Journal Of Nutrition · doi:10.1079/bjn19880106 · Cited by 24
The effect of iron substrate on mitochondria1 haem synthesis in copper deficiency
Williams, D. M., Kennedy, F. S., & Green, B. G. (1985) · British Journal Of Nutrition · doi:10.1079/bjn19850017 · Cited by 24
Discovery of the Ceruloplasmin Homologue Hephaestin: New Insight into the Copper/Iron Connection
Eisenstein, R. S. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.2000.tb01821.x · Cited by 23
Purification and characterization of the intestinal promoter of iron(3+)-transferrin formation
Topham, R. W., Woodruff, J. H., & Walker, M. C. (1981) · Biochemistry · doi:10.1021/bi00505a014 · Cited by 23
Caine, W. R., Metzler-Zebeli, B. U., McFall, M. E., Miller, B., Ward, T. L., Kirkwood, R. N., & Mosenthin, R. (2008) · Research in Veterinary Science · doi:10.1016/j.rvsc.2008.10.005 · Cited by 22
Zur Eisenverwertung bei unterschiedlicher Kupferversorgung
Grassmann, E., & Kirchgeßner, M. (1973) · Archiv für Tierernaehrung · doi:10.1080/17450397309424262 · Cited by 22
Metadata
- Authors
- Osaki, S., & Johnson, D. A.
- Affiliations
- Florida State University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1969-10
- Volume
- 244
- Issue
- 20
- Pages
- 5757-5758
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1565446694
- Cited by
- 159
- References
- 11
- Citations by year
- 2026: 1 · 2024: 4 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 2 · 2016: 2 · 2015: 5 · 2014: 7 · 2013: 7 · 2012: 3
- FWCI
- 2.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- ferroxidase, ceruloplasmin, liver iron, iron mobilization, ferrous iron oxidation, human serum albumin, copper, iron diffusion, canine liver
- MeSH terms
- Animals, Biological Transport, Ceruloplasmin, Dogs, Humans, Iron, Kinetics, Liver, Oxidoreductases, Perfusion, Serum Albumin, Spectrophotometry, Stimulation, Chemical, Time Factors, Transferrin, In Vitro Techniques
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