The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measuredIn 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 [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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Cited by
Sorted by citations
Items 501–600 of 1,001
Nramp1 equips macrophages for efficient iron recycling
Soe-Lin, S., Sheftel, A. D., Wasyluk, B., & Ponka, P. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.02.013 · Cited by 56
Pietrangelo, A. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111226 · Cited by 57
Neogenin Interacts with Hemojuvelin through Its Two Membrane-Proximal Fibronectin Type III Domains
Yang, F., West, A. P., Allendorph, G. P., Choe, S., & Björkman, P. J. (2008) · Biochemistry · doi:10.1021/bi800036h · Cited by 57
Pathways for the regulation of body iron homeostasis in response to experimental iron overload
Theurl, I., Ludwiczek, S., Eller, K., Seifert, M., Artner, E., Brunner, P., & Weiß, G. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2005.03.030 · Cited by 57
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
Development and iron‐dependent expression of hephaestin in different brain regions of rats
Qian, Z., Chang, Y., Zhu, L., Yang, L., Du, J., Ho, K., Wang, Q. L., Li, L., Wang, C., Ge, X., et al. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21352 · Cited by 55
Absorption of Manganese and Iron in a Mouse Model of Hemochromatosis
Kim, J., Buckett, P. D., & Wessling‐Resnick, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064944 · Cited by 55
Disordered signaling governing ferroportin transcription favors breast cancer growth
Chen, Y., Zhang, S., Wang, X., Guo, W., Wang, L., Zhang, D., Yuan, L., Zhang, Z., Xu, Y., & Liu, S. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.11.002 · Cited by 54
Ferroportin mutation in autosomal dominant hemochromatosis: loss of function, gain in understanding
Fleming, R. E., & Sly, W. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13739 · Cited by 54
Yang, L., Wang, D., Wang, X., Lu, Y., & Zhu, L. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.10.185 · Cited by 54
Copper-induced ferroportin-1 expression in J774 macrophages is associated with increased iron efflux
Chung, J., Haile, D. J., & Wessling‐Resnick, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306622101 · Cited by 55
Self-citationKwok, J. C., & Richardson, D. R. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.4.888 · Cited by 54
Expression of ferroportin1, hephaestin and ceruloplasmin in rat heart
Qian, Z., Chang, Y. Z., Leung, G., Du, J. R., Zhu, L., Wang, Q. L., Niu, L., Xu, Y. J., Yang, L., Ho, K. P., et al. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.02.006 · Cited by 55
Crosstalk between Iron Metabolism and Erythropoiesis
Li, H., & Ginzburg, Y. Z. (2010) · Advances in Hematology · doi:10.1155/2010/605435 · Cited by 53
Iron as a target of chemoprevention for longevity in humans
Toyokuni, S. (2011) · Free Radical Research · doi:10.3109/10715762.2011.564170 · Cited by 53
Iron Overload in Diabetic Retinopathy: A Cause or a Consequence of Impaired Mechanisms?
Ciudin, A., Hernández, C., & Simó, R. (2010) · Experimental Diabetes Research · doi:10.1155/2010/714108 · Cited by 56
de la Torre, V. S. G., Loulergue, C., González, D. A., Soubigou‐Taconnat, L., Rigaill, G. J., Pillon, Y., Barreau, L., Thomine, S., Fogliani, B., Sarramégna, V., et al. (2020) · New Phytologist · doi:10.1111/nph.16775 · Cited by 55
Beaumont, C., & Canonne‐Hergaux, F. (2005) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2005.04.017 · Cited by 57
Genetic haemochromatosis: genes and mutations associated with iron loading
Camaschella, C. (2002) · Best Practice & Research Clinical Haematology · doi:10.1016/s1521-6926(02)90207-0 · Cited by 52
Yi, Q., Yin, C., Chen, Y., Zhang, S., Jiang, L., Wang, F., Zhao, M., & Liu, S. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.01.017 · Cited by 53
Veuthey, T., D’Anna, M. C., & Roque, M. E. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90216.2008 · Cited by 52
Modulation of hepatitis C virus replication by iron and hepcidin in Huh7 hepatocytes
Bartolomei, G., Çevik, R. E., & Marcello, A. (2011) · Journal of General Virology · doi:10.1099/vir.0.032706-0 · Cited by 53
CDX2-regulated expression of iron transport protein hephaestin in intestinal and colonic epithelium
Hinoi, T., Gesina, G., Akyol, A., Kuick, R. D., Hanash, S., Giordano, T. J., Gruber, S. B., & Fearon, E. R. (2005) · Gastroenterology · doi:10.1053/j.gastro.2005.01.003 · Cited by 52
Wild-type and mutant ferroportins do not form oligomers in transfected cells
Gonçalves, A. S., Muzeau, F., Blaybel, R., Hetet, G., Driss, F., Delaby, C., Canonne‐Hergaux, F., & Beaumont, C. (2006) · Biochemical Journal · doi:10.1042/bj20051682 · Cited by 55
Gemmati, D., Zeri, G., Orioli, E., Gaetano, F. E. D., Salvi, F., Bartolomei, I., D’Alfonso, S., Dall’Osso, C., Leone, M. A., Singh, A. V., et al. (2012) · BMC Medical Genetics · doi:10.1186/1471-2350-13-70 · Cited by 53
Expression of alternative transcripts of ferroportin-1 during human erythroid differentiation.
Cianetti, L., Segnalini, P., Calzolari, A., Morsilli, O., Felicetti, F., Ramoni, C., Gabbianelli, M., Testa, U., & Sposi, N. M. (2005) · PubMed · Cited by 52
Preserving the National Blood Supply
Brittenham, G. M., Klein, H. G., Kushner, J. P., & Ajioka, R. S. (2001) · Hematology · doi:10.1182/asheducation-2001.1.422 · Cited by 52
The adaptor protein shc is involved in the negative regulation of NK cell-mediated cytotoxicity
Galandrini, R., Tassi, I., Morrone, S., Lanfrancone, L., Pelicci, P. G., Piccoli, M., Frati, L., & Santoni, A. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200107)31:7 · Cited by 32
Seifert, M., Nairz, M., Schroll, A., Schrettl, M., Haas, H., & Weiss, G. (2008) · Immunobiology · doi:10.1016/j.imbio.2008.07.010 · Cited by 51
Hennigar, S. R., McClung, J. P., Hatch‐McChesney, A., Allen, J. T., Wilson, M. A., Carrigan, C. T., Murphy, N. E., Teien, H. K., Martini, S., Gwin, J. A., et al. (2020) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqaa289 · Cited by 51
Regulation of the Profile of Iron-Management Proteins in Brain Microvasculature
Burdo, J. R., Simpson, I. A., Menzies, S. L., Beard, J., & Connor, J. R. (2003) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000095800.98378.03 · Cited by 51
Iron dysregulation in beta-thalassemia
Leecharoenkiat, K., Lithanatudom, P., Sornjai, W., & Smith, D. R. (2016) · Asian Pacific Journal of Tropical Medicine · doi:10.1016/j.apjtm.2016.07.035 · Cited by 52
Regulatory mechanisms for iron transport across the blood-brain barrier
Duck, K. A., Simpson, I. A., & Connor, J. R. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.10.083 · Cited by 51
Rare causes of hereditary iron overload
Ponka, P. (2002) · Seminars in Hematology · doi:10.1053/shem.2002.35638 · Cited by 52
Ge, X., Wang, Q. L., Qian, Z., Zhu, L., Du, F., Yung, W., Yang, L., & Ke, Y. (2008) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2008.07.014 · Cited by 54
Ghio, A. J., Turi, J. L., Yang, F., Garrick, L. M., & Garrick, M. D. (2006) · Biological Research · doi:10.4067/s0716-97602006000100008 · Cited by 52
Quantitative evaluation of expression of iron-metabolism genes in ceruloplasmin-deficient mice
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
Ludwiczek, 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
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
Xie, T., Yao, L., & Li, X. (2024) · Antioxidants · doi:10.3390/antiox13060659 · Cited by 53
Iron overload in nonalcoholic steatohepatitis
Fujita, N., & Takei, Y. (2011) · Advances in clinical chemistry · doi:10.1016/b978-0-12-387042-1.00006-x · 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
Kumfu, S., Chattipakorn, S. C., Fucharoen, S., & Chattipakorn, N. (2016) · Experimental Physiology · doi:10.1113/ep085517 · 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
Altered dietary iron intake is a strong modulator of renal DMT1 expression
Wareing, M., Ferguson, C. J., Delannoy, M., Cox, A. G., McMahon, R. F., Green, R., Riccardi, D., & Smith, C. P. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00064.2003 · 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
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
Haemopexin affects iron distribution and ferritin expression in mouse brain
Morello, N., Tonoli, E., Logrand, F., Fiorito, V., Fagoonee, S., Turco, E., Silengo, L., Vercelli, A., Altruda, F., & Tolosano, E. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00611.x · 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
Hudson, D. M., Curtis, S. B., Smith, V. C., Griffiths, T. A. M., Wong, A. Y. K., Scudamore, C. H., Buchan, A. M. J., & MacGillivray, R. T. A. (2009) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00453.2009 · Cited by 48
Effects of iron loading on muscle: genome-wide mRNA expression profiling in the mouse
Rodríguez, A., Hilvo, M., Kytömäki, L., Fleming, R. E., Britton, R. S., Bacon, B. R., & Parkkila, S. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-379 · 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
Self-citationMoonlighting 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
Ji, C., Steimle, B. L., Bailey, D. K., & Kosman, D. J. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0568-z · Cited by 50
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
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
Excess iron intake induced liver injury: The role of gut-liver axis and therapeutic potential
Liu, Y., Li, G., Lu, F., Guo, Z., Cai, S., & Huo, T. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115728 · Cited by 53
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
Intravenous Iron Does Not Augment the Hemoglobin Mass Response to Simulated Hypoxia
Garvican‐Lewis, L. A., Vuong, V. L., Govus, A. D., Peeling, P., JUNG, G., Nemeth, E., Hughes, D. C., Lovell, G., Eichner, D., & Gore, C. J. (2018) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000001608 · Cited by 46
Dev, S., Kumari, S., Singh, N., Bal, S. K., Seth, P., & Mukhopadhyay, C. K. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.025 · Cited by 46
Erythropoiesis in Multiply Injured Patients
Robinson, Y., Hostmann, A., Matenov, A., Ertel, W., & Oberholzer, A. (2006) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/01.ta.0000240969.13891.9b · 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
Nrf2 knockout dysregulates iron metabolism and increases the hemolysis through ROS in aging mice
Liu, Z., Han, K., Huo, X., Yan, B., Gao, M., Lv, X., Yu, P., Gao, G., & Chang, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117838 · Cited by 45
Enns, C. A. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.020303.x · Cited by 45
Yang, C., Liu, S., Sun, B., Wang, X., Wang, N., & Chen, S. (2012) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2012.11.049 · Cited by 44
Santos, P. C. J. L., Dinardo, C. L., Cançado, R. D., Schettert, I. T., Krieger, J. E., & Pereira, A. C. (2012) · Revista Brasileira de Hematologia e Hemoterapia · doi:10.5581/1516-8484.20120079 · Cited by 45
Alpha-synuclein: relating metals to structure, function and inhibition
McDowall, J., & Brown, D. R. (2016) · Metallomics · doi:10.1039/c6mt00026f · 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
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
Agoro, R., & Mura, C. (2016) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2016.07.006 · 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
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
Self-citationHepcidin 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
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
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