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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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 501–600 of 1,001
Xu, H., Lam, S. H., Shen, Y., & Gong, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068737 · Cited by 66
Gac, G. L., Ka, C., Joubrel, R., Gourlaouen, I., Lehn, P., Mornon, J., Férec, C., & Callebaut, I. (2013) · Human Mutation · doi:10.1002/humu.22369 · Cited by 67
Molecular basis of iron-loading disorders
Darshan, D., Frazer, D. M., & Anderson, G. J. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399410001687 · Cited by 63
Hepcidin and its therapeutic potential in neurodegenerative disorders
Qian, Z., & Ke, Y. (2019) · Medicinal Research Reviews · doi:10.1002/med.21631 · Cited by 65
Anderle, P., Sengstag, T., Mutch, D. M., Rumbo, M., Praz, V., Mansourian, R., Delorenzi, M., Williamson, G., & Roberts, M.-A. (2005) · BMC Genomics · doi:10.1186/1471-2164-6-69 · Cited by 65
Oral iron therapy: Current concepts and future prospects for improving efficacy and outcomes
Ebea, P. O., Vidyasagar, S., Connor, J. R., Frazer, D. M., Knutson, M. D., & Collins, J. F. (2024) · British Journal of Haematology · doi:10.1111/bjh.19268 · Cited by 68
Iron elevations in the aging Parkinsonian brain: a consequence of impaired iron homeostasis?
Lee, D. W., & Andersen, J. K. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06470.x · Cited by 63
Harrison, S. A., & Bacon, B. R. (2005) · Medical Clinics of North America · doi:10.1016/j.mcna.2004.08.005 · Cited by 62
Ward, D. G., Roberts, K., Stonelake, P. S., Goon, P. K. Y., Zampronio, C. G., Martin, A., Johnson, P. J., Iqbal, T. H., & Tselepis, C. (2008) · Proteome Science · doi:10.1186/1477-5956-6-28 · Cited by 62
Targeting Iron Homeostasis in Acute Kidney Injury
Walker, V. J., & Agarwal, A. (2016) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2016.01.003 · Cited by 62
Kawabata, H. (2017) · International Journal of Hematology · doi:10.1007/s12185-017-2365-3 · Cited by 64
Blanchette-Farra, N., Kita, D., Konstorum, A., Tesfay, L., Lemler, D. J., Hegde, P., Claffey, K. P., Torti, F. M., & Torti, S. V. (2018) · Oncogene · doi:10.1038/s41388-018-0243-y · Cited by 63
Therapeutic Advances in Regulating the Hepcidin/Ferroportin Axis
Hawula, Z. J., Wallace, D. F., Subramaniam, V. N., & Rishi, G. (2019) · Pharmaceuticals · doi:10.3390/ph12040170 · Cited by 62
Relationships and distinctions in iron-regulatory networks responding to interrelated signals
Muckenthaler, M. U., Richter, A., Gunkel, N., Riedel, D., Polycarpou‐Schwarz, M., Hentze, S., Falkenhahn, M., Stremmel, W., Ansorge, W. J., & Hentze, M. W. (2003) · Blood · doi:10.1182/blood-2002-07-2140 · Cited by 62
Self-citationHepcidin: an important new regulator of iron homeostasis
Hugman, A. (2006) · Clinical & Laboratory Haematology · doi:10.1111/j.1365-2257.2006.00768.x · Cited by 62
Role of Copper in the Proteosome-mediated Degradation of the Multicopper Oxidase Hephaestin
Nittis, T., & Gitlin, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401151200 · Cited by 63
Duodenal expression of iron transport molecules in untreated haemochromatosis subjects
Stuart, K. A., Anderson, G. J., Frazer, D. M., Powell, L. W., McCullen, M., Fletcher, L. M., & Crawford, D. H. G. (2003) · Gut · doi:10.1136/gut.52.7.953 · Cited by 61
Reeves, P. G., DeMars, L. C. S., Johnson, W. T., & Lukaski, H. C. (2005) · Journal of Nutrition · doi:10.1093/jn/135.1.92 · Cited by 61
Griffiths, W. J., Cox, T. M., & Sly, W. S. (2001) · Gastroenterology · doi:10.1053/gast.2001.24050 · Cited by 61
Recent advances in understanding haemochromatosis: a transition state
Robson, K., Merryweather-Clarke, A. T., Cadet, E., Viprakasit, V., Zaahl, M. G., Pointon, J. J., Weatherall, D. J., & Rochette, J. (2004) · Journal of Medical Genetics · doi:10.1136/jmg.2004.020644 · Cited by 62
Wolkow, N. (2011) · Archives of Ophthalmology · doi:10.1001/archophthalmol.2011.309 · Cited by 61
van Swelm, R. P. L., Wetzels, J. F. M., Verweij, V. G. M., Laarakkers, C. M., Pertijs, J. C. L. M., van der Wijst, J., Thévenod, F., Masereeuw, R., & Swinkels, D. W. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015040461 · Cited by 60
Yanatori, I., Richardson, D. R., Toyokuni, S., & Kishi, F. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129685 · Cited by 61
Johnson, D., Bayele, H. K., Johnston, K. L., Tennant, J. P., Srai, S. K., & Sharp, P. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.081 · Cited by 60
Roy, C. N., Weinstein, D. A., & Andrews, N. C. (2003) · Pediatric Research · doi:10.1203/01.pdr.0000049513.67410.2d · Cited by 60
Kuo, Y., Su, T., Chen, H., Attieh, Z., Syed, B. A., McKie, A. T., Anderson, G. J., Gitschier, J. M., & Vulpe, C. D. (2004) · Gut · doi:10.1136/gut.2003.019026 · Cited by 60
Self-citationDuodenal cytochrome B and hephaestin expression in patients with iron deficiency and hemochromatosis
Zoller, H., Theurl, I., Koch, R., McKie, A. T., Vogel, W., & Weiss, G. (2003) · Gastroenterology · doi:10.1016/s0016-5085(03)01063-1 · Cited by 60
Self-citationCell‐type‐specific insights into iron regulatory processes
Mleczko‐Sanecka, K., & Silvestri, L. (2020) · American Journal of Hematology · doi:10.1002/ajh.26001 · Cited by 64
Dong, X., Gao, W., Shao, T.-M., Hong-lin, X., Jiang-tao, B., Jing-yi, Z., & Xi-qing, C. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.11.009 · Cited by 59
Nutrient Transport in the Mammary Gland: Calcium, Trace Minerals and Water Soluble Vitamins
Montalbetti, N., Dalghi, M. G., Albrecht, C., & Hediger, M. A. (2014) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-014-9317-9 · Cited by 62
Self-citationZebrafish as a model organism for blood diseases
Berman, J. N., Hsu, K., & Look, A. T. (2003) · British Journal of Haematology · doi:10.1046/j.1365-2141.2003.04682.x · Cited by 61
Copper repletion enhances apical iron uptake and transepithelial iron transport by Caco-2 cells
Han, O., & Wessling‐Resnick, M. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00414.2001 · Cited by 60
Discovery of RNA structural elements using evolutionary computation
Fogel, G. B. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf653 · Cited by 59
The battle for iron in enteric infections
Sousa Gerós, A., Simmons, A., Drakesmith, H., Aulicino, A., & Frost, J. N. (2020) · Immunology · doi:10.1111/imm.13236 · Cited by 58
Frataxin and the molecular mechanism of mitochondrial iron-loading in Friedreich's ataxia
Chiang, S., Kovačević, Ž., Sahni, S., Lane, D. J. R., Merlot, A. M., Kalinowski, D. S., Huang, M. L. H., & Richardson, D. R. (2016) · Clinical Science · doi:10.1042/cs20160072 · Cited by 58
SLC40A1 in iron metabolism, ferroptosis, and disease: A review
Zhang, Y., Zou, L., Li, X., Guo, L., Hu, B., Ye, H., & Liu, Y. (2024) · WIREs Mechanisms of Disease · doi:10.1002/wsbm.1644 · Cited by 64
Iron, the retina and the lens: A focused review
García-Castiñeiras, S. (2010) · Experimental Eye Research · doi:10.1016/j.exer.2010.03.003 · Cited by 60
The role of iron in hepatic inflammation and hepatocellular carcinoma
Miyanishi, K., Tanaka, S., Sakamoto, H., & Kato, J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.006 · Cited by 58
Chapter 6 Iron Homeostasis and Erythropoiesis
Wrighting, D. M., & Andrews, N. C. (2008) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(07)00006-3 · Cited by 59
Iron Treatment Downregulates DMT1 and IREG1 mRNA Expression in Caco-2 Cells
Martini, L. A., Tchack, L., & Wood, R. J. (2002) · Journal of Nutrition · doi:10.1093/jn/132.4.693 · Cited by 58
Syed, B. A., Beaumont, N. J., Patel, A., Naylor, C. E., Bayele, H. K., Joannou, C. L., Rowe, P. S., Evans, R. W., & Srai, S. K. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.3.205 · Cited by 59
Ludwiczek, S., Theurl, I., Artner-Dworzak, E., Chorney, M., & Weiss, G. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0542-3 · Cited by 57
Vlasveld, L. T., Janssen, R., Bardou-Jacquet, E., Venselaar, H., Hamdi-Roze, H., Drakesmith, H., & Swinkels, D. W. (2019) · Pharmaceuticals · doi:10.3390/ph12030132 · Cited by 57
Intestinal Hypoxia-inducible Factor-2α (HIF-2α) Is Critical for Efficient Erythropoiesis
Anderson, E. R., Xue, X., & Shah, Y. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.238667 · Cited by 58
Disorders associated with systemic or local iron overload: from pathophysiology to clinical practice
Sebastiani, G., & Pantopoulos, K. (2011) · Metallomics · doi:10.1039/c1mt00082a · Cited by 58
The struggle for iron: gastrointestinal microbes modulate the host immune response during infection
Markel, T. A., Crisostomo, P. R., Wang, M., Herring, C. M., Meldrum, K. K., Lillemoe, K. D., & Meldrum, D. R. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0906579 · Cited by 57
Scheers, N. (2013) · Nutrients · doi:10.3390/nu5030957 · Cited by 59
Interactions Between Ferroportin and Hephaestin in Rat Enterocytes Are Reduced After Iron Ingestion
Yeh, K., YEH, M. K. Y., & Glass, J. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.03.059 · Cited by 57
Aslam, M., Frazer, D., Faria, N., Bruggraber, S., Wilkins, S. J., Mirciov, C. S. G., Powell, J., Anderson, G. J., & Pereira, D. I. A. (2014) · The FASEB Journal · doi:10.1096/fj.14-251520 · Cited by 57
DNA-array of gene variants in venous leg ulcers: Detection of prognostic indicators
Gemmati, D., Federici, F., Catozzi, L., Gianesini, S., Tacconi, G., Scapoli, G. L., & Zamboni, P. (2009) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2009.07.103 · Cited by 57
Brittenham, G., Weiss, G., Brissot, P., Lainé, F., Guillygomarc’h, A., Guyader, D., Moirand, R., & Deugnier, Y. (2000) · Hematology · doi:10.1182/asheducation-2000.1.39 · Cited by 58
Molecular aspects of iron absorption: Insights into the role of HFE in hemochromatosis
Philpott, C. C. (2002) · Hepatology · doi:10.1053/jhep.2002.33466 · Cited by 57
Briat, J. (2007) · Advances in botanical research · doi:10.1016/s0065-2296(07)46004-9 · Cited by 56
Divalent metal‐dependent regulation of hepcidin expression by MTF‐1
Balesaria, S., Ramesh, B., McArdle, H. J., Bayele, H. K., & Srai, S. K. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.12.023 · Cited by 56
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
Gaitán, D., Flores, S. E., Saavedra, P., Miranda, C., Olivares, M., Arredondo, M., de Romaña, D. L., Lönnerdal, B. L., & Pizarro, F. (2011) · Journal of Nutrition · doi:10.3945/jn.111.138651 · Cited by 56
Hephaestin and ceruloplasmin facilitate iron metabolism in the mouse kidney
Jiang, B., Liu, G., Zheng, J., Chen, M., Maimaitiming, Z., Chen, M., Liu, S., Jiang, R., Fuqua, B. K., Dunaief, J. L., et al. (2016) · Scientific Reports · doi:10.1038/srep39470 · Cited by 59
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
Ferroportin deficiency impairs manganese metabolism in flatiron mice
Seo, Y. A., & Wessling‐Resnick, M. (2015) · The FASEB Journal · doi:10.1096/fj.14-262592 · Cited by 55
New insights into iron homeostasis through the study of non-HFE hereditary haemochromatosis
Roetto, A., & Camaschella, C. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.09.004 · Cited by 55
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
The bacterial siderophore enterobactin confers survival advantage to Salmonella in macrophages
Saha, P., Xiao, X., Yeoh, B. S., Chen, Q., Katkere, B., Kirimanjeswara, G. S., & Vijay–Kumar, M. (2018) · Gut Microbes · doi:10.1080/19490976.2018.1546519 · Cited by 56
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
Molecular and clinical aspects of iron homeostasis: from anemia to hemochromatosis
Nairz, M., & Weiß, G. (2006) · Wiener klinische Wochenschrift · doi:10.1007/s00508-006-0653-7 · 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
Comparative capacities of the pig colon and duodenum for luminal iron absorption
Blachier, F., Vaugelade, P., Robert, V., Ani-Kibangou, B., Canonne‐Hergaux, F., Delpal, S., Bureau, F., Blottière, H. M., & Bouglé, D. L. (2007) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y07-007 · Cited by 55
de Oliveira, J., Denadai, M. B., & Costa, D. L. (2022) · Antioxidants · doi:10.3390/antiox11050861 · 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
Xu, H., Jiang, H. F., Wang, J., & Xie, J. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22885 · Cited by 53
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
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
Wang, T.-P., Quintanar, L., Severance, S., Solomon, E. I., & Kosman, D. J. (2003) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-003-0456-5 · Cited by 55
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
Ferritin and iron studies in anaemia and chronic disease
Peng, Y. Y., & Uprichard, J. (2016) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1177/0004563216675185 · Cited by 57
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
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
Regulation of mammalian iron homeostasis
Schneider, B. D., & Leibold, E. A. (2000) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200007000-00005 · 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
Malik, I. A., Naz, N., Sheikh, N., Khan, S., Moriconi, F., Blaschke, M., & Ramadori, G. P. (2011) · Cell and Tissue Research · doi:10.1007/s00441-011-1152-3 · Cited by 52
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
Weinreb, O., Mandel, S. A., Bar‐Am, O., & Amit, T. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0597-6 · Cited by 51
Yun, S., & Vincelette, N. D. (2015) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2015.02.006 · Cited by 52
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
Bandyopadhyay, S., Huang, X., Cho, H. K., Greig, N. H., Youdim, M. B. H., & Rogers, J. T. (2006) · Springer eBooks · doi:10.1007/978-3-211-33328-0_25 · Cited by 51
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
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
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
