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
Cited by
Sorted by citations
Items 601–700 of 1,001
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Yamamoto, K., Yoshida, K., Miyagoe, Y., Ishikawa, A., Hanaoka, K., Nomoto, S., Kaneko, K., Ikeda, S., & Takeda, S. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(02)00165-5 · Cited by 52
Role of duodenal iron transporters and hepcidin in patients with alcoholic liver disease
Dostalikova‐Cimburova, M., Balušíková, K., Krátká, K., Chmelíková, J., Hejda, V., Hnaníček, J., Neubauerová, J., Vránová, J., Kovár̆, J., & Horák, J. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12310 · Cited by 52
Superinfection in malaria: Plasmodium shows its iron will
Portugal, S., Drakesmith, H., & Mota, M. M. (2011) · EMBO Reports · doi:10.1038/embor.2011.213 · Cited by 55
Tsuji, Y. (2020) · PLoS ONE · doi:10.1371/journal.pone.0235563 · Cited by 50
Animal models with enhanced erythropoiesis and iron absorption
Latunde-Dada, G. O., McKie, A. T., & Simpson, R. J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.12.007 · Cited by 50
Self-citationLudwiczek, S., Theurl, I., Bahram, S., Schümann, K., & Weiß, G. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20315 · Cited by 51
Latunde-Dada, G. O., Vulpe, C. D., Anderson, G. J., Simpson, R. J., & McKie, A. T. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.011 · Cited by 50
Self-citationLocalization of iron transport and regulatory proteins in human cells
Griffiths, W. J., Kelly, A., Smith, S. J., & Cox, T. M. (2000) · QJM · doi:10.1093/qjmed/93.9.575 · Cited by 50
Cadmium induces iron deficiency anemia through the suppression of iron transport in the duodenum
Fujiwara, Y., Lee, J.-Y., Banno, H., Imai, S., Tokumoto, M., Hasegawa, T., Seko, Y., Nagase, H., & Satoh, M. (2020) · Toxicology Letters · doi:10.1016/j.toxlet.2020.07.005 · Cited by 49
Esophageal Cancer Stem-like Cells Resist Ferroptosis-Induced Cell Death by Active Hsp27-GPX4 Pathway
Liu, C., Li, H.-H., Lin, J.-H., Chiang, M., Hsu, T.-W., Li, A. F., Yen, D. H.-T., Hsu, H., & Hung, S. (2021) · Biomolecules · doi:10.3390/biom12010048 · Cited by 49
Transgenic expression of DwMYB2 impairs iron transport from root to shoot in Arabidopsis thaliana
Chen, Y.-H., Wu, X., Ling, H., & Yang, W. (2006) · Cell Research · doi:10.1038/sj.cr.7310099 · Cited by 49
Wang, X., Miller, D. S., & Zheng, W. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.02.024 · Cited by 49
Essential but toxic: Controlling the flux of iron in the body
Anderson, G. J., & Wang, F. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05661.x · Cited by 51
Overdosing on iron: Elevated iron and degenerative brain disorders
D’Mello, S. R., & Kindy, M. S. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220953065 · Cited by 49
Mechanisms of cellular iron sensing, regulation of erythropoiesis and mitochondrial iron utilization
Maio, N., Zhang, D., Ghosh, M. C., Jain, A., SantaMaria, A. M., & Rouault, T. A. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.06.001 · Cited by 50
Raha, A. A., Biswas, A., Henderson, J. W., Chakraborty, S., Holland, A. J., Friedland, R. P., Mukaetova-Ladinska, E. B., Zaman, S. H., & Raha‐Chowdhury, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031060 · Cited by 52
Adaptive changes of duodenal iron transport proteins in celiac disease
Barisani, D., Parafioriti, A., Bardella, M. T., Zoller, H., Conte, D., Armiraglio, E., Trovato, C. M. C., Koch, R., & Weiß, G. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00211.2003 · 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
Aydemir, F., Jenkitkasemwong, S., Gulec, S., & Knutson, M. D. (2009) · The Journal of Nutrition · doi:10.3945/jn.108.094052 · Cited by 49
The Iron Metabolism with a Specific Focus on the Functioning of the Nervous System
Kulaszyńska, M., Kwiatkowski, S., & Skonieczna‐Żydecka, K. (2024) · Biomedicines · doi:10.3390/biomedicines12030595 · Cited by 54
Pleiotropic actions of iron balance in diabetes mellitus
Wang, X., Fang, X., & Wang, F. (2014) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-014-9303-y · Cited by 49
Factors influencing disease phenotype and penetrance in HFE haemochromatosis
Rochette, J., Gac, G. L., Lassoued, K., Férec, C., & Robson, K. (2010) · Human Genetics · doi:10.1007/s00439-010-0852-1 · Cited by 52
New perspectives on the regulation of iron absorption via cellular zinc concentrations in humans
Knez, M., Graham, R. D., Welch, R. M., & Stangoulis, J. (2015) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2015.1050483 · Cited by 50
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
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
Pathogenesis of hereditary hemochromatosis
Fleming, R. E., Britton, R. S., Waheed, A., Sly, W. S., & Bacon, B. R. (2004) · Clinics in Liver Disease · doi:10.1016/j.cld.2004.06.004 · Cited by 48
Molecular and clinical correlates in iron overload associated with mutations in ferroportin.
Domenico, I. D., Ward, D. M., Nemeth, E., Ganz, T., Corradini, E., Ferrara, F., Musci, G., Pietrangelo, A., & Kaplan, J. (2006) · PubMed · Cited by 48
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
Apical location of ferroportin 1 in airway epithelia and its role in iron detoxification in the lung
Yang, F., Haile, D. J., Wang, X., Dailey, L. A., Stonehuerner, J. G., & Ghio, A. J. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00456.2004 · Cited by 47
Moonlighting cell surface GAPDH recruits Apo Transferrin to effect iron egress from mammalian cells
Sheokand, N., Malhotra, H., Kumar, S., Tillu, V. A., Chauhan, A. S., Raje, C. I., & Raje, M. (2014) · Journal of Cell Science · doi:10.1242/jcs.154005 · Cited by 49
The Intestinal Heme Transporter Revealed
Rouault, T. A. (2005) · Cell · doi:10.1016/j.cell.2005.08.027 · Cited by 47
Xie, L., & Collins, J. F. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00023.2011 · Cited by 48
Perspective: What Makes It So Difficult to Mitigate Worldwide Anemia Prevalence?
Schümann, K., & Solomons, N. W. (2017) · Advances in Nutrition · doi:10.3945/an.116.013847 · Cited by 48
Wang, X., Zheng, X., Zhang, J., Zhao, S., Wang, Z., Wang, F., Shang, W., Barasch, J. M., & Qiu, A. (2018) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00072.2018 · Cited by 50
Czaja, A. J. (2019) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.15173 · Cited by 47
Role of Iron in the Molecular Pathogenesis of Diseases and Therapeutic Opportunities
Abbasi, U., Abbina, S., Gill, A., Takuechi, L. E., & Kizhakkedathu, J. N. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00122 · Cited by 48
Davies, P. S., & Enns, C. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400537200 · Cited by 47
The molecular regulation of iron metabolism
Donovan, A., & Andrews, N. C. (2004) · The Hematology Journal · doi:10.1038/sj.thj.6200540 · Cited by 48
Ferroportin/IREG-1/MTP-1/SLC40A1 modulates the uptake of iron at the apical membrane of enterocytes
Thomas, C. (2003) · Gut · doi:10.1136/gut.53.1.44 · Cited by 48
Iyengar, V., Pullakhandam, R., & Nair, K. M. (2011) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.06.008 · Cited by 46
An Aluminum-Inducible IREG Gene is Required for Internal Detoxification of Aluminum in Buckwheat
Yokosho, K., Yamaji, N., Mitani‐Ueno, N., Shen, R. F., & Feng, J. X. (2016) · Plant and Cell Physiology · doi:10.1093/pcp/pcw065 · Cited by 46
The Role of Iron Metabolism in Lung Inflammation and Injury
Kim, J. (2012) · Journal of Allergy & Therapy · doi:10.4172/2155-6121.s4-004 · Cited by 48
Reuben, A., Chung, J. W., Lapointe, R., & Santos, M. M. (2017) · Immunity Inflammation and Disease · doi:10.1002/iid3.158 · Cited by 46
The role of hepcidin and ferroportin in iron absorption.
Oates, P. S. (2007) · PubMed · doi:10.14670/hh-22.791 · Cited by 46
A genetic view of iron homeostasis
Andrews, N. C. (2002) · Seminars in Hematology · doi:10.1053/shem.2002.35632 · Cited by 46
Ferroptosis and Its Emerging Role in Pre-Eclampsia
Chen, Z., Gan, J., Zhang, M., Du, Y., & Zhao, H. (2022) · Antioxidants · doi:10.3390/antiox11071282 · Cited by 46
Impact of ferroptosis on preeclampsia: A review
Shan, Y., Guan, C., Wang, J., Qi, W., Chen, A., & Liu, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115466 · Cited by 47
Non-HFE hemochromatosis: Pathophysiological and diagnostic aspects
Bardou‐Jacquet, E., Ali, Z. B., Beaumont-Epinette, M.-P., Loréal, O., Jouanolle, A., & Brissot, P. (2013) · Clinics and Research in Hepatology and Gastroenterology · doi:10.1016/j.clinre.2013.11.003 · Cited by 47
Enculescu, M., Metzendorf, C., Sparla, R., Hahnel, M. J., Bode, J. G., Muckenthaler, M. U., & Legewie, S. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005322 · Cited by 46
Iron Deficiency in Pulmonary Arterial Hypertension: A Deep Dive into the Mechanisms
Quatredeniers, M., Mendes‐Ferreira, P., Santos‐Ribeiro, D., Nakhleh, M. K., Ghigna, M., Cohen‐Kaminsky, S., & Perros, F. (2021) · Cells · doi:10.3390/cells10020477 · Cited by 45
Enns, C. A. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.020303.x · Cited by 45
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
Gastrointestinal function, divalent metal transporter-1 expressionand intestinal iron absorption
Oates, P. S., Trinder, D., & Morgan, E. H. (2000) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s004240000319 · Cited by 45
Núñez, M. T., Tapia, V., Rojas, A., Aguirre, P., Gómez, F., & Nualart, F. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00168.2009 · Cited by 44
Ishizaka, N., Saito, K., FURUTA, K., Matsuzaki, G., Koike, K., Noiri, E., & Nagai, R. (2007) · Hypertension Research · doi:10.1291/hypres.30.195 · Cited by 44
Distribution of Ferroportin1 Protein in Different Regions of Developing Rat Brain
Jiang, D. H., Ke, Y., Cheng, Y. Z., Ho, K. P., & Qian, Z. (2002) · Developmental Neuroscience · doi:10.1159/000065687 · Cited by 44
Health Implications of Iron Overload: the Role of Diet and Genotype
Heath, A. M., & Fairweather‐Tait, S. J. (2003) · Nutrition Reviews · doi:10.1301/nr.2003.febr.45-62 · Cited by 44
Expression of iron regulatory genes in a rat model of hepatocellular carcinoma
Holmström, P., Gåfvels, M. E., Eriksson, L. C., Dzikaite, V., Hultcrantz, R. W., Eggertsen, G., & Stal, P. I. (2006) · Liver International · doi:10.1111/j.1478-3231.2006.01316.x · Cited by 44
Auriac, A., Willemetz, A., & Canonne‐Hergaux, F. (2010) · Haematologica · doi:10.3324/haematol.2009.019992 · Cited by 47
Ramakrishnan, U., & Semba, R. D. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-464-3_16 · Cited by 44
Agoro, R., & Mura, C. (2016) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2016.07.006 · Cited by 44
ATP-driven copper transport across the intestinal brush border membrane
Knöpfel, M., Smith, C. P., & Solioz, M. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.023 · Cited by 44
Redox control of iron regulatory proteins
Fillebeen, C., & Pantopoulos, K. (2002) · Redox Report · doi:10.1179/135100002125000136 · Cited by 44
A role for tumour necrosis factor α in human small bowel iron transport
Sharma, N., Laftah, A. H., Brookes, M., Cooper, B. T., Iqbal, T. H., & Tselepis, C. (2005) · Biochemical Journal · doi:10.1042/bj20050256 · Cited by 44
Hypoxia-Inducible Factor Prolyl Hydroxylase Inhibitors and Iron Metabolism
Ogawa, C., Tsuchiya, K., & Maeda, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24033037 · Cited by 45
Heterogenous distribution of ferroportin-containing neurons in mouse brain
Boserup, M. W., Lichota, J., Haile, D. J., & Moos, T. (2011) · BioMetals · doi:10.1007/s10534-010-9405-2 · Cited by 44
Hepcidin and the iron enigma in HCV infection
Georgopoulou, U., Dimitriadis, A., Foka, P., Karamichali, E., & Mamalaki, A. (2014) · Virulence · doi:10.4161/viru.28508 · Cited by 43
Ferroportin Diseases: Functional Studies, a Link Between Genetic and Clinical Phenotype
Détivaud, L., Island, M., Jouanolle, A., Ropert, M., Bardou‐Jacquet, E., Lan, C. L., Mosser, A., Leroyer, P., Deugnier, Y., David, V., et al. (2013) · Human Mutation · doi:10.1002/humu.22396 · Cited by 47
Beard, J., & Han, O. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.005 · Cited by 45
Ferroptosis in Neurological Disease
David, S., Ryan, F., Jhelum, P., & Kroner, A. (2022) · The Neuroscientist · doi:10.1177/10738584221100183 · Cited by 43
Porras, C. A.-M., & Rouault, T. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094490 · Cited by 44
Kim, E., Ham, S., Bradke, D., Ma, Q., & Han, O. (2011) · Journal of Nutrition · doi:10.3945/jn.110.134031 · Cited by 42
Rouault, T. A. (2003) · Alcohol · doi:10.1016/s0741-8329(03)00102-2 · Cited by 42
An IRP-like protein from Plasmodium falciparum binds to a mammalian iron-responsive element
Loyevsky, M., LaVaute, T. M., Allerson, C. R., Stearman, R. S., Kassim, O. O., Cooperman, S. S., Gordeuk, V. R., & Rouault, T. A. (2001) · Blood · doi:10.1182/blood.v98.8.2555 · Cited by 42
Molecular analysis of iron overload in β2-microglobulin-deficient mice
Muckenthaler, M. U., Rodrigues, P., Macedo, M. G., Miñana, B., Brennan, K., Cardoso, E. M., Hentze, M. W., & de Sousa, M. A. B. (2004) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2004.05.003 · Cited by 43
Self-citationMa, Y., Specian, R. D., Yeh, K., YEH, M. K. Y., Rodriguez‐Paris, J., & Glass, J. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00005.2002 · Cited by 42
Dysregulation of ferroportin 1 interferes with spleen organogenesis in polycythaemia mice
Mok, H., Mendoza, M., Prchal, J. T., Balogh, P., & Schumacher, A. (2004) · Development · doi:10.1242/dev.01342 · Cited by 43
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Correnti, M., Gammella, E., Cairo, G., & Recalcati, S. (2024) · Metabolites · doi:10.3390/metabo14040228 · Cited by 48
Iron delocalisation in the pathogenesis of malarial anaemia
Nweneka, C. V., Doherty, C. P., Cox, S. E., & Prentice, A. M. (2009) · Transactions of the Royal Society of Tropical Medicine and Hygiene · doi:10.1016/j.trstmh.2009.08.007 · Cited by 43
Layoun, A., Huang, H., Calvé, A., & Santos, M. M. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.01.046 · Cited by 43
Hamp1 but not Hamp2 regulates ferroportin in fish with two functionally distinct hepcidin types
Neves, J. V., Ramos, M. F., Moreira, A. C., Silva, T., Gomes, M. S., & Rodrigues, P. (2017) · Scientific Reports · doi:10.1038/s41598-017-14933-5 · Cited by 41
Regulating ferroportin‐1 and transferrin receptor‐1 expression: A novel function of hydrogen sulfide
Zhang, M., Yang, G., Zhou, Y., Qian, C., Mu, M., Ke, Y., & Qian, Z. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27431 · Cited by 41
Medicago truncatula Ferroportin2 mediates iron import into nodule symbiosomes
Escudero, V., Abreu, I., Tejada‐Jiménez, M., Rosa‐Núñez, E., Quintana, J., Prieto, R. I., Larue, C., Wen, J., Villanova, J., Mysore, K. S., et al. (2020) · New Phytologist · doi:10.1111/nph.16642 · Cited by 41
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Yang, J., Tang, Q., & Zeng, Y. H. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101717 · Cited by 41
FET3P, ceruloplasmin, and the role of copper in iron metabolism
Kosman, D. J. (2002) · Advances in protein chemistry · doi:10.1016/s0065-3233(02)60055-5 · Cited by 41
Koyama, C., Wakusawa, S., Hayashi, H., Ueno, T., SUZUKI, R., Yano, M., Saito, H., & OKAZAKI, T. (2005) · Internal Medicine · doi:10.2169/internalmedicine.44.990 · Cited by 41
Non‐haem iron transport in the rat proximal colon
Johnston, K. L., Johnson, D., Marks, J., Srai, S. K., Debnam, E. S., & Sharp, P. (2005) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2006.01585.x · Cited by 41
Kartikasari, A. E. R., Wagener, F. A. D. T. G., Yachie, A., Wiegerinck, E. T. G., Kemna, E., & Winkels, D. W. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00494.x · Cited by 41
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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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