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A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Open accessAbstract
We have isolated and characterized a novel iron-regulated gene that is homologous to the divalent metal transporter 1 family of metal transporters. This gene, termed metal transporter protein (mtp1), is expressed in tissues involved in body iron homeostasis including the developing and mature reticuloendothelial system, the duodenum, and the pregnant uterus. MTP1 is also expressed in muscle and central nervous system cells in the embryo. At the subcellular level, MTP1 is localized to the basolateral membrane of the duodenal epithelial cell and a cytoplasmic compartment of reticuloendothelial system cells. Overexpression of MTP1 in tissue culture cells results in intracellular iron depletion. In the adult mouse, MTP1 expression in the liver and duodenum are reciprocally regulated. Iron deficiency induces MTP1 expression in the duodenum but down-regulates expression in the liver. These data indicate that MTP1 is an iron-regulated membrane-spanning protein that is involved in intracellular iron metabolism.
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“Iron can then be transported across the phagolysosomal membrane by DMT1 and NRAMP1, whereas FPN1 mediates iron export to the circulation (Abboud and Haile, 2000;Soe-Lin et al., 2009), where iron is incorporated in TF for cargo to tissues and organs.”
From Iron in infection and immunity (2020) · cites this paper as Abboud and Haile, 2000
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“Cellular iron export – and, therefore, gastrointestinal absorption of iron – is uniquely mediated by the iron transporter ferroportin (FPN or SLC40A1). 21 , 22 , 23 , 24”
From The battle for iron in enteric infections (2020) · cites this paper as [21]
In the citing paper
“The basolateral iron transporter, discovered simultaneously by 3 labs, is ferroportin (also called IREG1, MTP1, SLC39A1, and now SLC40A1).54,77,78”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [77]
In the citing paper
“Simultaneous studies characterized Fpn, which is abundantly expressed on the basolateral membrane of polarized enterocytes in the duodenum, in the cytosol of reticuloendothelial cells, and on the basal surface of syncytiotrophoblasts of the placenta (1, 72, 198).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [1]
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Citations
Cites
Tuerk, C., & Gold, L. (1990) · Science · doi:10.1126/science.2200121 · Cited by 10,421
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
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
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
Canonne-Hergaux, F., Gruenheid, S., Ponka, P., & Gros, P. (1999) · Blood · doi:10.1182/blood.v93.12.4406 · Cited by 451
Haile, D. J., Rouault, T. A., Tang, C., Chin, J., Harford, J. B., & Klausner, R. D. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7536 · Cited by 270
Self-citationCrystal, R. G. (1997) · Nature Medicine · doi:10.1038/nm0497-383 · Cited by 204
Sibille, J., Kondo, H. G., & Aisen, P. (1988) · Hepatology · doi:10.1002/hep.1840080218 · Cited by 139
Pinner, E., Gruenheid, S., Raymond, M., & Gros, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.28933 · Cited by 115
Research works printed but not linked: 2
- Umbreit, 1998, Semin. Hematol., 35, 13
- Oates, 1997, Am. J. Physiol., 273, G636
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Kim, D., Kim, K., Choi, B., Youn, P., Ryu, D., Klaassen, C. D., & Park, J. (2006) · Archives of Toxicology · doi:10.1007/s00204-006-0160-7 · Cited by 106
Mechanisms and regulation of transferrin and iron transport in a model blood–brain barrier system
Burdo, J. R., Antonetti, D. A., Wolpert, E. B., & Connor, J. R. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00590-6 · Cited by 106
Emerging therapeutic targets for treatment of leishmaniasis
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The flatiron mutation in mouse ferroportin acts as a dominant negative to cause ferroportin disease.
Zohn, I. E., De Domenico, I., Pollock, A., Ward, D. M., Goodman, J. F., Liang, X., Sanchez, A. J., Niswander, L., & Kaplan, J. (2007) · Blood · doi:10.1182/blood-2007-01-066068 · Cited by 104
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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
Becker, E., Lovejoy, D. B., Greer, J. M., Watts, R., & Richardson, D. R. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705089 · Cited by 103
Regulation of iron pathways in response to hypoxia
Chepelev, N. L., & Willmore, W. G. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.023 · Cited by 106
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Roetto, A., Merryweather‐Clarke, A. T., Daraio, F., Livesey, K., Pointon, J. J., Barbabietola, G., Piga, A. G., Mackie, P. H., Robson, K., & Camaschella, C. (2002) · Blood · doi:10.1182/blood-2002-03-0693 · Cited by 103
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Rychtarcikova, Z., Lettlova, S., Tomkova, V., Korenkova, V., Langerova, L., Simonova, E., Zjablovskaja, P., Alberich-Jorda, M., Neuzil, J., & Truksa, J. (2017) · Oncotarget · doi:10.18632/oncotarget.14093 · Cited by 100
The ins and outs of iron: Escorting iron through the mammalian cytosol
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Molecular and cellular bases of iron metabolism in humans
Васильевич, М. И., Suhodolo, I. V., Prokopieva, V. D., & Klimenteva, T. K. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916060018 · Cited by 103
Mitochondrial involvement in genetically determined transition metal toxicity
Mehta, R., Templeton, D. M., & O'Brien, P. J. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.05.011 · Cited by 104
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Anderson, E. R., Taylor, M. J., Xue, X., Ramakrishnan, S. K., Martin, A. S., Xie, L., Bredell, B. X., Gardenghi, S., Rivella, S., & Shah, Y. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314197110 · Cited by 101
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
Dupic, F., Fruchon, S., Bensaid, M., Borot, N., Radosavljevic, M., Loreal, O., Brissot, P., Gilfillan, S., Bahram, S., Coppin, H., et al. (2002) · Gastroenterology · doi:10.1053/gast.2002.31877 · Cited by 99
Iron Deficiency in Obesity and after Bariatric Surgery
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Małyszko, J., & Myśliwiec, M. (2007) · Kidney & Blood Pressure Research · doi:10.1159/000098522 · Cited by 99
Pietrangelo, A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.013 · Cited by 105
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 regulatory proteins control a mucosal block to intestinal iron absorption
Galy, B., Ferring-Appel, D., Becker, C., Gretz, N., Gröne, H.-J., Schümann, K., & Hentze, M. W. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.026 · Cited by 98
Role of Intestinal HIF-2α in Health and Disease
Ramakrishnan, S. K., & Shah, Y. M. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105202 · Cited by 100
Reprogramming of pro-inflammatory human macrophages to an anti-inflammatory phenotype by bile acids
Wammers, M., Schupp, A.-K., Bode, J. G., Ehlting, C., Wolf, S. D., Deenen, R., Köhrer, K., Häussinger, D., & Graf, D. (2018) · Scientific Reports · doi:10.1038/s41598-017-18305-x · Cited by 104
Iron in neurodegenerative disorders
Berg, D., Becker, G., Riederer, P. F., & Rieß, O. (2002) · Neurotoxicity Research · doi:10.1080/1029842021000045444 · Cited by 98
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
McCarthy, R. C., & Kosman, D. J. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00031 · Cited by 100
Rice, A. E., Mendez, M. J., Hokanson, C. A., Rees, D. C., & Björkman, P. J. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.063 · Cited by 102
Iron-Sensing Proteins that Regulate Hepcidin and Enteric Iron Absorption
Knutson, M. D. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104801 · Cited by 96
Thomsen, M. S., Andersen, M. V., Christoffersen, P., Jensen, M. D., Lichota, J., & Moos, T. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.013 · Cited by 96
Burkhart, A., Skjørringe, T., Johnsen, K. B., Siupka, P., Thomsen, L. B., Nielsen, M. S., Thomsen, L. L., & Moos, T. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9582-7 · Cited by 98
Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers
Roy, C. N. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.20.2181 · Cited by 96
Regulation of growth differentiation factor 15 expression by intracellular iron
Lakhal, S., Talbot, N. P., Crosby, A., Stoepker, C., Townsend, A. R. M., Robbins, P. A., Pugh, C. W., Ratcliffe, P. J., & Mole, D. R. (2009) · Blood · doi:10.1182/blood-2008-07-170431 · Cited by 95
Ferroportin1 and hephaestin are involved in the nigral iron accumulation of 6‐OHDA‐lesioned rats
Wang, J., Jiang, H. F., & Xie, J. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05515.x · Cited by 95
Role of the Ferroportin Iron-Responsive Element in Iron and Nitric Oxide Dependent Gene Regulation
Liu, X., Hill, P., & Haile, D. J. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0572 · Cited by 95
Self-citationRegulation of iron absorption in Hfe mutant mice
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Brain Iron Metabolism and Neurodegenerative Disorders
Sipe, J. C., Lee, P. L., & Beutler, E. (2002) · Developmental Neuroscience · doi:10.1159/000065701 · Cited by 94
Erlitzki, R., Long, J. C., & Theil, E. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207918200 · Cited by 96
Millard, K. N., Frazer, D. M., Wilkins, S. J., & Anderson, G. J. (2004) · Gut · doi:10.1136/gut.2003.031153 · Cited by 93
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
Cellular Iron Metabolism in Prognosis and Therapy of Breast Cancer
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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
Special delivery: distributing iron in the cytosol of mammalian cells
Philpott, C. C., & Ryu, M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00173 · Cited by 96
Molecular Diagnostic and Pathogenesis of Hereditary Hemochromatosis
Santos, P. C. J. L., Krieger, J. E., & Pereira, A. C. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13021497 · Cited by 94
Ferroportin1 is required for normal iron cycling in zebrafish
Fraenkel, P. G., Traver, D. J., Donovan, A., Zahrieh, D., & Zon, L. I. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23780 · Cited by 94
Advances in iron chelation: an update
Heli, H., Mirtorabi, S., & Karimian, K. (2011) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.569493 · Cited by 92
A general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 97
Iron metabolism and the role of the iron-regulating hormone hepcidin in health and disease
Daher, R., Manceau, H., & Karim, Z. (2017) · La Presse Médicale · doi:10.1016/j.lpm.2017.10.006 · Cited by 92
Expression of the DMT1 (NRAMP2/DCT1) iron transporter in mice with genetic iron overload disorders
Canonne‐Hergaux, F., Levy, J. E., Fleming, M. D., Montross, L. K., Andrews, N. C., & Gros, P. (2001) · Blood · doi:10.1182/blood.v97.4.1138 · Cited by 91
Hirayama, T., Niwa, M., Hirosawa, S., & Nagasawa, H. (2020) · ACS Sensors · doi:10.1021/acssensors.0c01445 · Cited by 90
Zhang, W., Yan, Z., Gao, J., Sun, L., Huang, X., Liu, Z., Yu, S., Cao, C.-J., Zuo, L.-J., Chen, Z., et al. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8586-4 · Cited by 91
Abouhamed, M., Gburek, J., Liu, W., Torchalski, B., Wilhelm, A., Wolff, N. A., Christensen, E. I., Thévenod, F., & Smith, C. P. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00359.2005 · Cited by 90
Guo, Q., Qian, C., Wang, X., & Qian, Z. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01436-x · Cited by 91
McCarthy, R. C., & Kosman, D. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.455428 · Cited by 93
Heat shock protein 27 downregulates the transferrin receptor 1-mediated iron uptake
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Sato, T., Chang, H., Bayeva, M., Shapiro, J. S., Ramos-Alonso, L., Kouzu, H., Jiang, X., Liu, T., Yar, S., Sawicki, K. T., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804701115 · Cited by 87
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Nanami, M., Ookawara, T., Otaki, Y., Ito, K., Moriguchi, R., Miyagawa, K., Hasuike, Y., Izumi, M., Eguchi, H., Suzuki, K., et al. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000190610.63878.20 · Cited by 87
Disorders of Iron Metabolism and Anemia in Chronic Kidney Disease
Panwar, B., & Gutiérrez, O. M. (2016) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2016.05.002 · Cited by 87
Role of Dietary Flavonoids in Iron Homeostasis
Lesjak, M. M., & Srai, S. K. (2019) · Pharmaceuticals · doi:10.3390/ph12030119 · Cited by 87
Nemeth, E. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05585.x · Cited by 91
Robach, P., Recalcati, S., Girelli, D., Gelfi, C., Aachmann‐Andersen, N. J., Thomsen, J. J., Norgaard, A. M., Alberghini, A., Campostrini, N., Castagna, A., et al. (2009) · Blood · doi:10.1182/blood-2008-09-178095 · Cited by 89
Regulation of systemic iron homeostasis: how the body responds to changes in iron demand
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The SLC40 basolateral iron transporter family (IREG1/ferroportin/MTP1)
McKie, A. T., & Barlow, D. J. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1102-3 · Cited by 89
Kong, Y., Hu, L., Lu, K., Wang, Y., Xie, Y., Gao, L., Yang, G., Xie, B., He, W., Chen, G., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1854-0 · Cited by 85
Molecular Mechanisms and Regulation of Iron Transport
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The molecular genetics of haemochromatosis
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A novel mutation in ferroportin1 is associated with haemochromatosis in a Solomon Islands patient
Arden, K. E., Wallace, D. F., Dixon, J. L., Summerville, L., Searle, J. W., Anderson, G. J., Ramm, G. A., Powell, L. W., & Subramaniam, V. N. (2003) · Gut · doi:10.1136/gut.52.8.1215 · Cited by 84
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Is ferroportin–hepcidin signaling altered in restless legs syndrome?
Clardy, S. L., Wang, X., Boyer, P. J., Earley, C. J., Allen, R. P., & Connor, J. R. (2006) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2006.04.008 · Cited by 84
Yeh, K., YEH, M. K. Y., Mims, L., & Glass, J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90298.2008 · Cited by 85
An important role of the hepcidin–ferroportin signaling in affecting tumor growth and metastasis
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Zebrafish a genetic model for vertebrate organogenesis and human disorders
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Iron overload due to mutations in ferroportin.
Domenico, I. D., Ward, D. M., Musci, G., & Kaplan, J. (2006) · PubMed · Cited by 84
Watts, R., Ponka, P., & Richardson, D. R. (2003) · Biochemical Journal · doi:10.1042/bj20021302 · Cited by 84
Wallace, D. F., Clark, R. M., Harley, H. A. J., & Subramaniam, V. N. (2004) · Journal of Hepatology · doi:10.1016/j.jhep.2003.12.008 · Cited by 83
Heme and non-heme iron transporters in non-polarized and polarized cells
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Biasiotto, G., Belloli, S., Ruggeri, G., Zanella, I., Gerardi, G., Corrado, M., Gobbi, E., Albertini, A., & Arosio, P. (2003) · Clinical Chemistry · doi:10.1373/clinchem.2003.023440 · Cited by 83
Intestinal expression of genes involved in iron absorption in humans
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Structural basis of ion transport and inhibition in ferroportin
Pan, Y., Ren, Z., Gao, S., Shen, J., Wang, L., Xu, Z., Yu, Y., Bachina, P., Zhang, H., Fan, X., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19458-6 · Cited by 81
Haptoglobin reduces lung injury associated with exposure to blood
Yang, F., Haile, D. J., Berger, F. G., Herbert, D. C., Beveren, E. V., & Ghio, A. J. (2003) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00115.2002 · Cited by 81
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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
Garrick, M. D., Kuo, H.-C., Vargas, F. P., Singleton, S. T., Zhao, L., Smith, J. J., Paradkar, P. N., Roth, J. A., & Garrick, L. M. (2006) · Biochemical Journal · doi:10.1042/bj20051987 · Cited by 83
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Wallace, D. F., Harris, J. M., & Subramaniam, V. N. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00621.2008 · Cited by 84
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Crespo, Â. C., Silva, B. D. R., Marques, L., Marcelino, E., Maruta, C., Costa, S., Timóteo, Â., Vilares, A., do Couto, F. S., Faustino, P., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.10.078 · Cited by 82
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Deicher, R., & Hörl, W. H. (2006) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2006.01633.x · Cited by 80
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Meyron‐Holtz, E. G., Moshe-Belizowski, S., & Cohen, L. A. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0582-0 · Cited by 78
Chung, B., Chaston, T. B., Marks, J., Srai, S. K., & Sharp, P. (2009) · Journal of Nutrition · doi:10.3945/jn.108.102905 · Cited by 78
Leong, W.-I., Bowlus, C. L., Tallkvist, J., & Lönnerdal, B. L. (2003) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/78.6.1203 · Cited by 78
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Yang, F., Wang, X., Haile, D. J., Piantadosi, C. A., & Ghio, A. J. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00114.2002 · Cited by 78
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Parkkila, S., Niemelä, O. J., Britton, R. S., Fleming, R. E., Waheed, A., Bacon, B. R., & Sly, W. S. (2001) · Gastroenterology · doi:10.1053/gast.2001.29617 · Cited by 79
Han, O., & Kim, E. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21392 · Cited by 77
Metadata
- Authors
- Abboud, S., & Haile, D. J.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- Corresponding author
- Haile, David J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-06
- Volume
- 275
- Issue
- 26
- Pages
- 19906-19912
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2063617352
- Cited by
- 1,267
- References
- 14
- Citations by year
- 2026: 9 · 2025: 20 · 2024: 26 · 2023: 25 · 2022: 34 · 2021: 47 · 2020: 52 · 2019: 25 · 2018: 48 · 2017: 36 · 2016: 51 · 2015: 39 · 2014: 65 · 2013: 51 · 2012: 49
- FWCI
- 34.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk053079-02)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK-53079, R03DK96009)
- 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
- DMT1, iron homeostasis, duodenal epithelium, reticuloendothelial system, liver, iron deficiency, basolateral membrane, gene expression regulation
- MeSH terms
- Iron Deficiencies, Ferroportin, Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cloning, Molecular, Duodenum, Embryo, Mammalian, Ferritins, Humans, Iron, Liver, Mice, Inbred C57BL, Molecular Sequence Data, Plasmids, Sequence Homology, Nucleic Acid, Tissue Distribution, Transfection, Blotting, Western, Down-Regulation, Sequence Homology, Amino Acid, DNA, Complementary, Fluorescent Antibody Technique, Indirect, COS Cells, Cation Transport Proteins, Mice
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