The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation
Open accessAbstract
Iron absorption by the duodenal mucosa is initiated by uptake of ferrous Fe(II) iron across the brush border membrane and culminates in transfer of the metal across the basolateral membrane to the portal vein circulation by an unknown mechanism. We describe here the isolation and characterization of a novel cDNA (Ireg1) encoding a duodenal protein that is localized to the basolateral membrane of polarized epithelial cells. Ireg1 mRNA and protein expression are increased under conditions of increased iron absorption, and the 5' UTR of the Ireg1 mRNA contains a functional iron-responsive element (IRE). IREG1 stimulates iron efflux following expression in Xenopus oocytes. We conclude that IREG1 represents the long-sought duodenal iron export protein and is upregulated in the iron overload disease, hereditary hemochromatosis.
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In the citing paper
“After export by FPN1, iron is reoxidized to its ferric form by membrane-anchored hephaestin or by circulating ceruloplasmin (McKie et al., 2000;Vulpe et al., 1999).”
From Iron in infection and immunity (2020) · cites this paper as McKie et al., 2000
In the citing paper
“The key iron exporter is ferroportin (FPN, also called SLC40A1) which exports Fe2+ iron (McKie et al., 2000).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as McKie et al., 2000
In the citing paper
“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 [24]
In the citing paper
“CYBRD1 was one of 2 iron transport-related molecules discovered by McKie through a very productive RNA subtraction approach.53,54”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [54]
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 [54]
In the citing paper
“Overexpression of ferritoid resulted in a shift in ferritin H distribution from cytoplasm to nucleus (201).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [201]
In the citing paper
“Ferritoid is a 30-kDa protein consisting of 270 amino acids specifically expressed in corneal epithelial cells (201).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [201]
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
Self-citationHentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292
Self-citationMicrocytic 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
Fleming, M. D., Romano, M. A., Su, M. A., Garrick, L. M., Garrick, M. D., & Andrews, N. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.1148 · Cited by 936
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
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
The biochemical basis of the NADPH oxidase of phagocytes
Segal, A. W., & Abo, A. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90051-n · Cited by 622
Zhong, H., & Simons, J. W. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0815 · Cited by 473
Flemming (1998) · Medical Entomology and Zoology · Cited by 412
Research works printed but not linked: 1
- Umbreit, 1998, Iron absorption and cellular transport, Semin. Hematol., 35, 13
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Items 101–200 of 1,001
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Roemhild, K., von Maltzahn, F., Weiskirchen, R., Knüchel, R., von Stillfried, S. F., & Lammers, T. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.05.001 · Cited by 329
The discovery of the new haemochromatosis gene
Brissot, P. (2003) · Journal of Hepatology · doi:10.1016/s0168-8278(03)00142-9 · Cited by 313
Gardenghi, S., Marongiu, M. F., Ramos, P., Guy, E. C., Breda, L., Chadburn, A., Liu, Y.-F., Amariglio, N., Rechavi, G., Rachmilewitz, E. A., et al. (2007) · Blood · doi:10.1182/blood-2006-09-048868 · Cited by 314
Iron-dependent regulation of the divalent metal ion transporter
Gunshin, H., Allerson, C. R., Polycarpou-Schwarz, M., Rofts, A., Rogers, J. T., Kishi, F., Hentze, M. W., Rouault, T. A., Andrews, N. C., & Hediger, M. A. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03189-1 · Cited by 305
Self-citationZoller, H., Weiss, G., Theurl, I., Koch, R. O., Vogel, W., Obrist, P., Pietrangelo, A., Montosi, G., & Haile, D. J. (2001) · Gastroenterology · doi:10.1053/gast.2001.24033 · Cited by 304
The physiological functions of iron regulatory proteins in iron homeostasis - an update
Zhang, D., Ghosh, M. C., & Rouault, T. A. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00124 · Cited by 310
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
Iron regulatory proteins in pathobiology
Cairo, G., & Pietrangelo, A. (2000) · Biochemical Journal · doi:10.1042/bj3520241 · Cited by 299
Burdo, J. R., Menzies, S. L., Simpson, I. A., Garrick, L. M., Garrick, M. D., Dolan, K. G., Haile, D. J., Beard, J. L., & Connor, J. R. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1256 · Cited by 297
Muckenthaler, M. U., Roy, C. N., Custodio, Á. O., Miñana, B., DEGRAAF, J., Montross, L. K., Andrews, N. C., & Hentze, M. W. (2003) · Nature Genetics · doi:10.1038/ng1152 · Cited by 295
Self-citationNeural roles for heme oxygenase: Contrasts to nitric oxide synthase
Barañano, D. E., & Snyder, S. H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191351298 · Cited by 293
Evstatiev, R., & Gasché, C. (2011) · Gut · doi:10.1136/gut.2010.214312 · Cited by 302
Theil, E. C. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.24.012003.132212 · Cited by 291
Transport of toxic metals by molecular mimicry.
Ballatori, N. (2002) · Environmental Health Perspectives · doi:10.1289/ehp.02110s5689 · Cited by 285
Delaby, C., Pilard, N., Gonçalves, A. S., Beaumont, C., & Canonne-Hergaux, F. (2005) · Blood · doi:10.1182/blood-2005-06-2398 · Cited by 283
Vert, G., Briat, J., & Curie, C. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.016089 · Cited by 283
Zhang, D.-L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., & Rouault, T. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.006 · Cited by 281
ACG Clinical Guideline: Hereditary Hemochromatosis
Kowdley, K. V., Brown, K. E., Ahn, J. C., & Sundaram, V. (2019) · The American Journal of Gastroenterology · doi:10.14309/ajg.0000000000000315 · Cited by 294
Rouault, T. A., & Cooperman, S. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.002 · Cited by 280
Nichol, H., Law, J. H., & Winzerling, J. J. (2002) · Annual Review of Entomology · doi:10.1146/annurev.ento.47.091201.145237 · Cited by 282
Manganese homeostasis in the nervous system
Chen, P., Chakraborty, S., Mukhopadhyay, S., Lee, E., Paoliello, M. M. B., Bowman, A. B., & Aschner, M. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13170 · Cited by 278
Pathogenesis and treatment of anaemia of chronic disease
Weiß, G. (2002) · Blood Reviews · doi:10.1054/blre.2002.0193 · Cited by 276
Autocrine formation of hepcidin induces iron retention in human monocytes
Theurl, I., Theurl, M., Seifert, M., Mair, S., Nairz, M., Rumpold, H., Zoller, H., Bellmann-Weiler, R., Niederegger, H., Talasz, H., et al. (2008) · Blood · doi:10.1182/blood-2007-05-090019 · Cited by 275
Iron Acquisition and Transcriptional Regulation
Kaplan, C. D., & Kaplan, J. (2009) · Chemical Reviews · doi:10.1021/cr9001676 · Cited by 281
Fleming, R. E., & Sly, W. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161296298 · Cited by 273
Divalent Metal Transporter 1 in Lead and Cadmium Transport
Bressler, J. P., Olivi, L., Cheong, J. H., Kim, Y., & BANNONA, D. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.011 · Cited by 278
P HYSIOLOGY AND M OLECULAR B IOLOGY OF D IETARY I RON A BSORPTION
Miret, S., Simpson, R. J., & McKie, A. T. (2003) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.23.011702.073139 · Cited by 274
Self-citationThe importance of non-transferrin bound iron in disorders of iron metabolism
Breuer, W., Hershko, C., & Cabantchik, Z. I. (2000) · Transfusion Science · doi:10.1016/s0955-3886(00)00087-4 · Cited by 268
Taylor, M., Qu, A., Anderson, E. R., Matsubara, T., Martin, A., Gonzalez, F. J., & Shah, Y. M. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.03.007 · Cited by 265
A Short Review of Iron Metabolism and Pathophysiology of Iron Disorders
Yiannikourides, A., & Latunde-Dada, G. O. (2019) · Medicines · doi:10.3390/medicines6030085 · Cited by 276
Resistance to hepcidin is conferred by hemochromatosis-associated mutations of ferroportin
Drakesmith, H., Schimanski, L. M., Ormerod, E., Merryweather-Clarke, A. T., Viprakasit, V., Edwards, J. P., Sweetland, E., Bastin, J. M., Cowley, D., Chinthammitr, Y., et al. (2005) · Blood · doi:10.1182/blood-2005-02-0561 · Cited by 264
Iron homeostasis and toxicity in retinal degeneration
He, X., Hahn, P., Iacovelli, J., Wong, R., King, C., Bhisitkul, R., Massaro-Giordano, M., & Dunaief, J. L. (2007) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2007.07.004 · Cited by 260
The role of transporters in cellular heme and porphyrin homeostasis
Krishnamurthy, P. C., Xie, T., & Schuetz, J. D. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.02.001 · Cited by 268
Formigari, A., Irato, P., & Santon, A. (2007) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2007.07.010 · Cited by 258
Mechanisms of heme iron absorption: Current questions and controversies
West, A. R., & Oates, P. S. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.4101 · Cited by 257
The Regulation of Iron Absorption and Homeostasis.
Wallace, D. F. (2016) · PubMed · Cited by 268
Ferroportin1 deficiency in mouse macrophages impairs iron homeostasis and inflammatory responses
Zhang, Z., Zhang, F., An, P., Guo, X., Shen, Y., Tao, Y., Wu, Q., Zhang, Y., Yu, Y., Ning, B., et al. (2011) · Blood · doi:10.1182/blood-2011-01-330324 · Cited by 250
Anderson, E. R., & Shah, Y. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120016 · Cited by 262
Gehrke, S. G., Kulaksiz, H., Herrmann, T. R. W., Riedel, H.-D., Bents, K., Veltkamp, C., & Stremmel, W. (2003) · Blood · doi:10.1182/blood-2002-11-3610 · Cited by 246
Iron regulatory proteins and their role in controlling iron metabolism
Kühn, L. C. (2015) · Metallomics · doi:10.1039/c4mt00164h · Cited by 242
White, C., Yuan, X., Schmidt, P. J., Bresciani, E., Samuel, T. K., Campagna, D. R., Hall, C., Bishop, K. S., Calicchio, M. L., Lapierre, A., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.005 · Cited by 257
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
Schaaf, G., Honsbein, A., Meda, A. R., Kirchner, S., Wipf, D., & von Wirén, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601062200 · Cited by 236
Cardiac ferroportin regulates cellular iron homeostasis and is important for cardiac function
Lakhal-Littleton, S., Wolna, M., Carr, C. A., Miller, J. J. J., Christian, H. C., Ball, V., Santos, A., Diaz, R., Biggs, D., Stillion, R., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422373112 · Cited by 234
The Metabolism of Neuronal Iron and Its Pathogenic Role in Neurological Disease: Review
Moos, T., & Morgan, E. H. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.002 · Cited by 234
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
The Spectrum of Achalasia: Lessons From Studies of Pathophysiology and High-Resolution Manometry
Kahrilas, P. J., & Boeckxstaens, G. E. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.08.038 · Cited by 236
Cellular iron: Ferroportin is the only way out
Ganz, T. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.02.005 · Cited by 236
Brasse–Lagnel, C., Karim, Z., Letteron, P., Bekri, S., Bado, A., & Beaumont, C. (2011) · Gastroenterology · doi:10.1053/j.gastro.2010.12.037 · Cited by 230
The molecular basis of ferroportin-linked hemochromatosis
De Domenico, I., Ward, D. M., Nemeth, E., Vaughn, M. B., Musci, G., Ganz, T., & Kaplan, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503804102 · Cited by 230
Yoon, D., Pastore, Y. D., Divoký, V., Liu, E., Mlodnicka, A., Rainey, K., Poňka, P., Semenza, G. L., Schumacher, A., & Prchal, J. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602329200 · Cited by 231
Iron loading and erythrophagocytosis increase ferroportin 1 (FPN1) expression in J774 macrophages
Knutson, M. D., Vafa, M. R., Haile, D. J., & Wessling-Resnick, M. (2003) · Blood · doi:10.1182/blood-2003-04-1250 · Cited by 227
Kippler, M. J., Hoque, A. M. W., Raqib, R., Öhrvik, H., Ekström, E., & Vahter, M. (2009) · Toxicology Letters · doi:10.1016/j.toxlet.2009.10.018 · Cited by 227
Modulation of iron transport proteins in human colorectal carcinogenesis
Brookes, M. J., Hughes, S., Turner, F. E., Reynolds, G., Sharma, N., Ismail, T., Berx, G., McKie, A. T., Hotchin, N., Anderson, G. J., et al. (2006) · Gut · doi:10.1136/gut.2006.094060 · Cited by 226
Self-citationAberrant iron distribution via hepatocyte-stellate cell axis drives liver lipogenesis and fibrosis
Gao, H., Jin, Z., Bandyopadhyay, G., Wang, G., Zhang, D., Rocha, K. C. E., Liu, X., Zhao, H., Kisseleva, T., Brenner, D. A., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.07.006 · Cited by 224
Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 224
Self-citationIron deficiency: A concise review
Umbreit, J. N. (2005) · American Journal of Hematology · doi:10.1002/ajh.20249 · Cited by 220
Lawen, A., & Lane, D. J. R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4271 · Cited by 221
Intestinal Absorption of Cadmium Is Associated with Divalent Metal Transporter 1 in Rats
Park, J. D. (2002) · Toxicological Sciences · doi:10.1093/toxsci/68.2.288 · Cited by 214
Intersection of Iron and Copper Metabolism in the Mammalian Intestine and Liver
Doğuer, Ç., Ha, J., & Collins, J. F. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170045 · Cited by 225
In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations
Schimanski, L. M., Drakesmith, H., Merryweather-Clarke, A. T., Viprakasit, V., Edwards, J. P., Sweetland, E., Bastin, J. M., Cowley, D., Chinthammitr, Y., Robson, K. J. H., et al. (2005) · Blood · doi:10.1182/blood-2004-11-4502 · Cited by 212
Multi-Copper Oxidases and Human Iron Metabolism
Vashchenko, G., & MacGillivray, R. T. A. (2013) · Nutrients · doi:10.3390/nu5072289 · Cited by 223
The orchestration of body iron intake: how and where do enterocytes receive their cues?
Frazer, D. M., & Anderson, G. J. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00039-1 · Cited by 211
mRNA Stability and the Control of Gene Expression: Implications for Human Disease
Hollams, E. M., Giles, K. M., Thomson, A. M., & Leedman, P. J. (2002) · Neurochemical Research · doi:10.1023/a:1020992418511 · Cited by 212
Trafficking of Heme and Porphyrins in Metazoa
Severance, S., & Hamza, I. (2009) · Chemical Reviews · doi:10.1021/cr9001116 · Cited by 215
Molecular mechanisms involved in intestinal iron absorption
Sharp, P. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4716 · Cited by 205
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
Schmidt, P. J., Toudjarska, I., Sendamarai, A. K., Racie, T., Milstein, S., Bettencourt, B. R., Hettinger, J., Bumcrot, D., & Fleming, M. D. (2013) · Blood · doi:10.1182/blood-2012-09-453977 · Cited by 204
Potential involvement of iron in the pathogenesis of peritoneal endometriosis
Defrere, S., Lousse, J. C., Gonzalez-Ramos, R., Colette, S., Donnez, J., & Van Langendonckt, A. (2008) · Molecular Human Reproduction · doi:10.1093/molehr/gan033 · Cited by 204
Nairz, M., Schleicher, U., Schroll, A., Sonnweber, T., Theurl, I., Ludwiczek, S., Talasz, H., Brandacher, G., Moser, P. L., Muckenthaler, M. U., et al. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20121946 · Cited by 204
Iron and carcinogenesis: from Fenton reaction to target genes
Toyokuni, S. (2002) · Redox Report · doi:10.1179/135100002125000596 · Cited by 207
Iron Regulation: Macrophages in Control
Sukhbaatar, N., & Weichhart, T. (2018) · Pharmaceuticals · doi:10.3390/ph11040137 · Cited by 213
Regulation of reticuloendothelial iron transporter MTP1 (Slc11a3) by inflammation
Yang, F., Liu, X.-B., Quinones, M., Melby, P. C., Ghio, A., & Haile, D. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201485200 · Cited by 197
Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195
Self-citationFontaine, S. L., Quinn, J. M., Nakamoto, S. S., Page, M. D., Göhre, V., Moseley, J. L., Kropat, J., & Merchant, S. (2002) · Eukaryotic Cell · doi:10.1128/ec.1.5.736-757.2002 · Cited by 194
Understanding iron homeostasis through genetic analysis of hemochromatosis and related disorders
Camaschella, C. (2005) · Blood · doi:10.1182/blood-2005-05-1857 · Cited by 198
Hepcidin targets ferroportin for degradation in hepatocytes
Ramey, G., Deschemin, J., Durel, B., Canonne‐Hergaux, F., Nicolas, G., & Vaulont, S. (2009) · Haematologica · doi:10.3324/haematol.2009.014399 · Cited by 201
Modern iron replacement therapy: clinical and pathophysiological insights
Girelli, D., Ugolini, S., Busti, F., Marchi, G., & Castagna, A. (2017) · International Journal of Hematology · doi:10.1007/s12185-017-2373-3 · Cited by 196
Pathways underlying iron accumulation in human nonalcoholic fatty liver disease
Aigner, E., Theurl, I., Theurl, M., Lederer, D., Haufe, H., Dietze, O., Strasser, M., Datz, C., & Weiss, G. (2008) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/87.5.1374 · Cited by 190
Frazer, D. M. (2003) · Gut · doi:10.1136/gut.52.3.340 · Cited by 189
Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice
Gunshin, H., Starr, C. N., DiRenzo, C., Fleming, M. D., Jin, J., Greer, E. L., Sellers, V. M., Galica, S. M., & Andrews, N. C. (2005) · Blood · doi:10.1182/blood-2005-02-0716 · Cited by 188
Devalia, V., Carter, K., Walker, A. P., Perkins, S. J., Worwood, M., May, A. M., & Dooley, J. S. (2002) · Blood · doi:10.1182/blood-2001-11-0132 · Cited by 190
Hypoxia-inducible factors link iron homeostasis and erythropoiesis
Shah, Y. M., & Xie, L. (2014) · Gastroenterology · doi:10.1053/j.gastro.2013.12.031 · Cited by 187
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Merlot, A. M., Kalinowski, D. S., & Richardson, D. R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4540 · Cited by 195
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Lakhal-Littleton, S., Wolna, M., Chung, Y. J., Christian, H. C., Heather, L. C., Brescia, M., Ball, V., Diaz, R., Santos, A., Biggs, D., et al. (2016) · eLife · doi:10.7554/elife.19804 · Cited by 184
Catch me if you can! Novel aspects of cadmium transport in mammalian cells
Thévenod, F. (2010) · BioMetals · doi:10.1007/s10534-010-9309-1 · Cited by 184
Consequences of Disturbing Manganese Homeostasis
Baj, J., Flieger, W., Barbachowska, A., Kowalska, B., Flieger, M., Forma, A., Teresiński, G., Portincasa, P., Buszewicz, G., Radzikowska-Büchner, E., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914959 · Cited by 190
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 188
Nairz, M., Theurl, I., Ludwiczek, S., Theurl, M., Mair, S. M., Fritsche, G., & Weiss, G. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00942.x · Cited by 182
Iron homeostasis in the metabolic syndrome
Datz, C., Felder, T. K., Niederseer, D., & Aigner, E. (2013) · European Journal of Clinical Investigation · doi:10.1111/eci.12032 · Cited by 181
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Self-citationGambling, L., Danzeisen, R., Susan, G. A. I. R., Lea, R. G., CHARANIA, Z., Solanky, N., JOORY, K. D., Srai, S. K., & McArdle, H. J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560883 · Cited by 179
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Metadata
- Authors
- McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., Hediger, M. A., Hentze, M. W., & Simpson, R. J.
- Affiliations
- King's College London (GB)
- Brigham and Women's Hospital (US)
- European Molecular Biology Laboratory (DE)
- Universitat de Barcelona (ES)
- Corresponding author
- McKie, Andrew T
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 5
- Issue
- 2
- Pages
- 299-309
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2143900678
- Cited by
- 1,422
- References
- 41
- Citations by year
- 2026: 13 · 2025: 16 · 2024: 30 · 2023: 32 · 2022: 34 · 2021: 50 · 2020: 41 · 2019: 42 · 2018: 43 · 2017: 43 · 2016: 42 · 2015: 48 · 2014: 66 · 2013: 58 · 2012: 47
- FWCI
- 41.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- CYTED Ciencia y Tecnología para el Desarrollo
- 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
- iron absorption, iron-responsive element, iron overload, hereditary hemochromatosis, iron efflux, duodenal epithelial cells, cDNA cloning, iron homeostasis
- MeSH terms
- Ferroportin, Amino Acid Sequence, Animals, Base Sequence, Biological Transport, Carrier Proteins, Cell Compartmentation, Cloning, Molecular, Duodenum, Ferric Compounds, Gene Expression Regulation, Intestinal Absorption, Intestinal Mucosa, Iron, Membrane Proteins, Models, Biological, Molecular Sequence Data, Portal Vein, RNA, Messenger, Sequence Homology, Nucleic Acid, Transferrin, Cell Polarity, Sequence Homology, Amino Acid, Response Elements, Cation Transport Proteins, Mice
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