The DOI matches its Crossref record; 19 of the 20 references it cites were found in a registry or an index.
Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing.
Open accessAbstract
HFE and transferrin receptor 2 (TFR2) are membrane proteins integral to mammalian iron homeostasis and associated with human hereditary hemochromatosis. Here we demonstrate that HFE and TFR2 interact in cells, that this interaction is not abrogated by disease-associated mutations of HFE and TFR2, and that TFR2 competes with TFR1 for binding to HFE. We propose a new model for the mechanism of iron status sensing that results in the regulation of iron homeostasis.
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
“Taking this into account, we have proposed a model in which TFR2 escorts HFE away from TFR1 when the serum iron level (reflected in the transferrin saturation) is elevated.149,150”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [150]
In the citing paper
“Like TFR1, TFR2 interacts with HFE to form a stable protein complex.150”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [150]
Citations
Cites
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
Self-citationNicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214
Molecular Cloning of Transferrin Receptor 2
Kawabata, H., Yang, R., Hirama, T., Vuong, P. T., Kawano, S., Gombart, A. F., & Koeffler, H. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20826 · Cited by 661
Weinstein, D. A., Roy, C. N., Fleming, M. D., Loda, M. F., Wolfsdorf, J. I., & Andrews, N. C. (2002) · Blood · doi:10.1182/blood-2002-04-1260 · Cited by 632
Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
Bennett, M. J., Lebrón, J. A., & Björkman, P. J. (2000) · Nature · doi:10.1038/47417 · Cited by 343
Wu, J. C., Merlino, G. T., & Fausto, N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.674 · Cited by 317
The C282Y Mutation Causing Hereditary Hemochromatosis Does Not Produce a Null Allele
Levy, J. E., Montross, L. K., Cohen, D. E., Fleming, M. D., & Andrews, N. C. (1999) · Blood · doi:10.1182/blood.v94.1.9.413a43_9_11 · Cited by 259
West, A. P., Bennett, M. J., Sellers, V. M., Andrews, N. C., Enns, C. A., & Bjorkman, P. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000664200 · Cited by 257
Self-citationDiferric transferrin regulates transferrin receptor 2 protein stability
Johnson, M. B., & Enns, C. A. (2004) · Blood · doi:10.1182/blood-2004-06-2477 · Cited by 235
Research works printed but not linked: 1
- Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. & Struhl, K. (eds) Current Protocols in Molecular Biology, pp. 9.1.1–9.1.11 and 12.1.1–12.1.6, Wiley-Interscience, New York
Cited by
Sorted by citations
Items 201–300 of 351
Heat stress stimulates hepcidin mRNA expression and C/EBPα protein expression in aged rodent liver
Bloomer, S. A., Kregel, K. C., & Brown, K. E. (2013) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2013.07.012 · Cited by 19
“There was no difference in TFR2 expression between young and old animals (Fig.”
InfluentialProtective role of calreticulin in HFE hemochromatosis
Pinto, J. P., Ramos, P., de Almeida, S. F., Oliveira, S. J., Breda, L., Michalak, M., Porto, G., Rivella, S., & de Sousa, M. A. B. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.014 · Cited by 18
McLaren, C. E., Barton, J. C., Eckfeldt, J. H., McLaren, G. D., Acton, R. T., Adams, P. C., Henkin, L. F., Gordeuk, V. R., Vulpe, C. D., Harris, E. L., et al. (2009) · American Journal of Hematology · doi:10.1002/ajh.21585 · Cited by 17
Jaroszewicz, J. (2010) · World Journal of Gastroenterology · doi:10.3748/wjg.v16.i14.1747 · Cited by 16
How mutant HFE causes hereditary hemochromatosis
Muckenthaler, M. U. (2014) · Blood · doi:10.1182/blood-2014-07-581744 · Cited by 16
Iron absorption in hepcidin1 knockout mice
Masaratana, P., Laftah, A. H., Latunde-Dada, G. O., Vaulont, S., Simpson, R. J., & McKie, A. T. (2011) · British Journal Of Nutrition · doi:10.1017/s0007114510005507 · Cited by 17
“high-Fe or haemochromatosis protein, haemojuvelin (HFE2) and transferrin receptor 2((2,3)).”
BackgroundBuretić‐Tomljanović, A., Vlastelić, I., Badovinac, A. R., Čizmarević, N. S., Nadalin, S., & Ristič, S. (2008) · Fertility and Sterility · doi:10.1016/j.fertnstert.2008.02.129 · Cited by 16
“Hepcidin, a main regulator of whole-body iron homeostasis, is induced by HFE protein, which represents a part of the systemic iron sensor (20).”
Importance of Iron Absorption in Human Health: An Overview
Dixit, S. P., Logesh, R., Palaniswamy, D. S., & Mohankumar, S. K. (2020) · Current Nutrition & Food Science · doi:10.2174/1573401316999200801021752 · Cited by 18
Tackling the unknowns in understanding and management of hospital acquired anemia
Bressman, E., Jhang, J. S., McClaskey, J. H., & Ginzburg, Y. Z. (2021) · Blood Reviews · doi:10.1016/j.blre.2021.100830 · Cited by 18
Iron as a Therapeutic Target in HFE-Related Hemochromatosis: Usual and Novel Aspects
Loréal, O., Cavey, T., Robin, F., Kenawi, M., Guggenbuhl, P., & Brissot, P. (2018) · Pharmaceuticals · doi:10.3390/ph11040131 · Cited by 17
“The mechanism potentially involved in such regulation is a decrease of the physical interaction between TFR1 and HFE proteins when transferrin saturation increases [31].”
BackgroundBorch‐Iohnsen, B., Hagve, T., Hauge, A., & Thorstensen, K. (2009) · Tidsskrift for Den norske legeforening · doi:10.4045/tidsskr.08.0083 · Cited by 13
Ulvik, R. J. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.08.005 · Cited by 12
Sebastiani, G., & Pantopoulos, K. (2010) · CRC Press eBooks · doi:10.1201/9781420059984-c13 · Cited by 12
Shanmugam, N. K. N., & Cherayil, B. J. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.10.065 · Cited by 11
Swinkels, D. W., Venselaar, H., Wiegerinck, E. T. G., Bakker, E., Joosten, I., Jaspers, C. A. J. J., Vasmel, W. L. E., & Breuning, M. H. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.10.003 · Cited by 11
“Recently, however, it has been proposed that HFE plays its most important role in iron sensing in the liver by conveying the whole-body iron status, reflected by diferric transferrin from the HFE–TfR1 complex to TfR2, resulting in potential signalling of downstream events [5].”
BackgroundHereditary Hemochromatosis (HFE) genotypes in heart failure: Relation to etiology and prognosis
EchoCardiography and Heart Outcome Study (ECHOS) investigators, Møller, D. V., Pecini, R., Gustafsson, F., Hassager, C., Hedley, P. L., Jespersgaard, C., Torp-Pedersen, C. T., Christiansen, M., & Køber, L. (2010) · BMC Medical Genetics · doi:10.1186/1471-2350-11-117 · Cited by 12
“New insights into the function of the HFE protein suggests an iron sensing function, as well as a hepcidin regulating function[20] and subsequently a pivotal role in iron homeostasis.”
BackgroundPinto, J. P., Ramos, P., & de Sousa, M. A. B. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.01.005 · Cited by 11
Potential of natural source polysaccharides for the treatment of anemia: A review
Hou, H., Wu, Q., Yang, L., Sun, Y., Bai, N., & Chen, H. (2026) · Industrial Crops and Products · doi:10.1016/j.indcrop.2026.123211 · Cited by 10
Effect of HFE Variants on Sphingolipid Expression by SH-SY5Y Human Neuroblastoma Cells
Ali-Rahmani, F. G., Hengst, J. A., Connor, J. R., & Schengrund, C. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0403-8 · Cited by 10
“The presence/absence of WT-, H63D-, and C282Y-HFE in lipid rafts was ascertained because HFE was shown to associate with TfR2, a lipid raft component.”
InfluentialSrai, S. K., & Sharp, P. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_1 · Cited by 11
Bhatt, L., Murphy, C., O’Driscoll, L. S., Carmo‐Fonseca, M., McCaffrey, M., & Fleming, J. V. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07727.x · Cited by 10
Transferrin receptor 1: keeper of HFE
Parrow, N. L., & Fleming, R. E. (2023) · Blood · doi:10.1182/blood.2022018740 · Cited by 10
Lack of Hfe and TfR2 in Macrophages Impairs Iron Metabolism in the Spleen and the Bone Marrow
Comità, S., Falco, P., Mezzanotte, M., Spasić, M. V., & Roetto, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179142 · Cited by 9
“According to the most recent functional model, Hfe alternatively binds transferrin receptors 1 and 2 (TfR1 and TfR2, respectively) in its extracellular α 1-α 2 domain and is required for the physiological regulation of hepatic synthesis of Hepc [14].”
BackgroundAn Update on Iron Homeostasis: Make New Friends, but Keep the Old
Roy, C. N. (2013) · The American Journal of the Medical Sciences · doi:10.1097/maj.0000000000000190 · Cited by 9
Hamad, M. A., & Awadallah, S. M. (2013) · Medical Hypotheses · doi:10.1016/j.mehy.2013.10.019 · Cited by 9
Characterization of hepcidin response to holotransferrin in novel recombinant TfR1 HepG2 cells
Mehta, K. J., Busbridge, M., Renshaw, D. W., Evans, R. W., Farnaud, S., & Patel, V. B. (2016) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2016.06.008 · Cited by 9
Polycythemia in Patients With Hereditary Hemochromatosis: Real or Myth?
Asif, S., Begemann, M. E., & Raza, S. (2019) · Journal of Clinical Medicine Research · doi:10.14740/jocmr3816 · Cited by 9
[Progress on epigenetic regulation of iron homeostasis].
Duan, L., Yin, X., Meng, H., Fang, X., Min, J., & Wang, F. (2020) · PubMed · doi:10.3785/j.issn.1008-9292.2020.02.25 · Cited by 9
Niederau, C. (2009) · Medizinische Klinik - Intensivmedizin und Notfallmedizin · doi:10.1007/s00063-009-1192-6 · Cited by 9
“keltischer Abstammung liegt bei etwa 90% der Patienten mit Hämochromatose eine homozygote Punktmutation (C282Y) im HFE-Gen vor [2, 8, 17].”
Dostalikova‐Cimburova, M., Krátká, K., Balušíková, K., Chmelíková, J., Hejda, V., Hnaníček, J., Neubauerová, J., Vránová, J., Kovár̆, J., & Horák, J. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01458.x · Cited by 9
“The HFE/TFR2 complex is thought to serve as a body iron sensor, which regulates hepcidin expression [9].”
BackgroundInfluentialHershko, C. (2009) · Blood · doi:10.1182/blood-2009-04-216101 · Cited by 9
Buretić‐Tomljanović, A., Vraneković, J., Rubeša, G., Jonovska, S., Tomljanović, D., Jengić, V. Š., Kapović, M., & Ristič, S. (2011) · Molecular Biology Reports · doi:10.1007/s11033-011-0974-0 · Cited by 9
“Mutations in the HFE generally affect the ability of the protein to prevent TF from binding its receptors, thereby increasing cellular iron uptake [3].”
Porto, G., Cruz, E., Teles, M. J., & de Sousa, M. A. B. (2019) · Pharmaceuticals · doi:10.3390/ph12030122 · Cited by 8
“sensing and hepcidin signaling [43], thus contributing to the prevention of inappropriate iron accumulation.”
BackgroundInfluentialIron Metabolism and Related Disorders
Hoda, K., Bowlus, C. L., Chu, T. W., & Gruen, J. R. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00106-3 · Cited by 8
Paterson, A. C., & Pietrangelo, A. (2011) · Elsevier eBooks · doi:10.1016/b978-0-7020-3398-8.00005-2 · Cited by 9
In vitro binding of HFE to the cation-independent mannose-6 phosphate receptor
Schimanski, L. M., Drakesmith, H., Sweetland, E., Bastin, J. M., Rezgui, D., Edelmann, M. J., Kessler, B. M., Merryweather‐Clarke, A. T., Robson, K., & Townsend, A. (2009) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2009.03.010 · Cited by 8
Actualités du métabolisme du fer
Beaumont, C. (2009) · La Revue de Médecine Interne · doi:10.1016/j.revmed.2009.09.020 · Cited by 8
Hepcidin Regulation by Bone Morphogenetic Protein Signaling and Iron Homeostasis
Rodova, M., & Kim, S. (2016) · Journal of Nutrition & Food Sciences · doi:10.4172/2155-9600.1000521 · Cited by 7
“[43], demonstrated that HFE binds both transferrin receptor 1 (TfR1) and transferrin receptor 2 (TfR2) [44] on the cell membrane.”
BackgroundTransferrin receptor 2 is emerging as a major player in the control of iron metabolism
Calzolari, A., Oliviero, I., & Testa, U. (2007) · Open Life Sciences · doi:10.2478/s11535-007-0007-0 · Cited by 7
Михайлова, С. В., Babenko, V. N., Voevoda, M. I., & Ромащенко, А. Г. (2010) · Genetic Testing and Molecular Biomarkers · doi:10.1089/gtmb.2009.0203 · Cited by 6
“HFE interacts with transferrin receptor 2 (TfR2) (Griffiths and Cox, 2003; Goswami and Andrews, 2006) expressed in a smaller number of cells than TfR1 (Vogt et al. , 2003).”
InfluentialHepcidin production in response to iron is controlled by monocyte-derived humoral factors
Sasaki, Y., Shimonaka, Y., Ikuta, K., Hosoki, T., Sasaki, K., Torimoto, Y., Kanada, H., Moriguchi, Y., & Kohgo, Y. (2013) · International Journal of Hematology · doi:10.1007/s12185-013-1476-8 · Cited by 6
Hereditäre Hämochromatose, Alpha-1-Antitrypsin-Mangel und Morbus Wilson
Zhou, H. J., & Hp, F. (2007) · Der Pathologe · doi:10.1007/s00292-007-0954-2 · Cited by 6
Plasma Iron and Iron Delivery to the Tissues
Graham, R. M., Chua, A. C. G., & Trinder, D. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_7 · Cited by 6
“Also, HFE maintains its interaction with TFR2 which contains mutations leading to TFR2-associated hemochromatosis in vivo [ 119 ] .”
BackgroundPhysiopathologie et génétique de l'hémochromatose HFE de type 1
Loréal, O., Ropert, M., Mosser, A., Déhais, V., Deugnier, Y., David, V., Brissot, P., & Jouanolle, A. (2007) · La Presse Médicale · doi:10.1016/j.lpm.2007.03.038 · Cited by 7
Bacon, B. R., Adams, P. C., Kowdley, K. V., Powell, L. W., & Tavill, A. S. (2011) · Cited by 6
A HAMP promoter bioassay system for identifying chemical compounds that modulate hepcidin expression
Kawabata, H., Uchiyama, T., Sakamoto, S., Kanda, J., Oishi, S., Fujii, N., Tomosugi, N., Kadowaki, N., & Takaori‐Kondo, A. (2015) · Experimental Hematology · doi:10.1016/j.exphem.2015.01.005 · Cited by 5
The Systems Biology of Bone Morphogenetic Proteins
Sampath, K. T. (2017) · Springer eBooks · doi:10.1007/978-3-319-47507-3_2 · Cited by 5
Liver Disease in Iron Overload
Guindi, M. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-42873-6.00011-1 · Cited by 4
Dietzen, D. J., & Diab, Y. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817962-8.00026-3 · Cited by 6
Métabolisme du fer : physiologie et pathologie
Beaumont, C., & Girot, R. (2010) · Encyclopédie médico-chirurgicale. Hématologie · doi:10.1016/s1155-1984(10)49948-3 · Cited by 7
Ścibior, A., Hus, I., Mańko, J., & Jawniak, D. (2020) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2020.126550 · Cited by 5
Microcytic anaemias in childhood and iron‐refractory iron deficiency anaemia
Pippard, M. J. (2017) · British Journal of Haematology · doi:10.1111/bjh.14558 · Cited by 5
“…transferrin stabilises TFR2 (Johnson & Enns, 2004) and, by displacing of HFE from binding to transferrin receptor 1, makes HFE available to interact with the BMP receptor complex (Goswami & Andrews, 2006), allowing hepcidin synthesis to be sensitive to circulating transferrin saturation.”
BackgroundLiu, S., Tsyplenkova, S., Charlebois, E., Wallace, D. F., Subramaniam, V. N., Fillebeen, C., & Pantopoulos, K. (2026) · Blood · doi:10.1182/blood.2025030054 · Cited by 4
Silva, B. D. R., Ferreira, J. T., Santos, V., Baldaia, C., Serejo, F., & Faustino, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.07.017 · Cited by 4
Pietrangelo, A., & Torbenson, M. S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-7020-6697-9.00004-2 · Cited by 4
Kallianpur, A. R., Wen, W., Erwin, A., Clifford, D. B., Hulgan, T., & Robbins, G. K. (2020) · PLoS ONE · doi:10.1371/journal.pone.0239758 · Cited by 4
“Though the precise mechanisms of action of HFE are still not well understood, its role in regulating monocytemacrophage iron content is well established; overall, HFE C282Y homozygosity results in systemic intracellular iron loading of cells other than macrophage-monocytes, due to a combination of unregulated gut iron…”
BackgroundIron Metabolism and Related Disorders
Ginzburg, Y. Z., & Finberg, K. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-812535-9.00012-1 · Cited by 4
Surcharges héréditaires en fer
Brissot, P., Bardou‐Jacquet, E., Latournerie, M., Ropert, M., Island, M., Loréal, O., & Jouanolle, A. (2009) · Pathologie Biologie · doi:10.1016/j.patbio.2009.10.011 · Cited by 5
The Central Role of the Liver in Iron Storage and Regulation of Systemic Iron Homeostasis
Rouault, T. A., Gordeuk, V. R., & Anderson, G. J. (2009) · Wiley eBooks · doi:10.1002/9780470747919.ch16 · Cited by 4
Domenico, I. D., & Kushner, J. P. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.05.020 · Cited by 4
Enns, C. A., Jue, S. F., & Zhang, A.-S. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111142 · Cited by 3
“Additional investigations indicate that hepatic hepcidin expression also depends on the HFE/TfR2 interaction (38, 39), the HFE/ALK3 interaction (40), the NEO1/ALK3 interaction (30, 41), and the formation of HFE/TfR2/HJV complex (42).”
Role and regulation of iron metabolism in erythropoiesis and disease
Arvedson, T., & Sasu, B. J. (2009) · Birkhäuser Basel eBooks · doi:10.1007/978-3-7643-8698-6_15 · Cited by 4
Transferrin Receptor 2 in Canine Testicular Tumors: An Emerging Key Role in Seminomas
Leandri, R., Buonocore, S., & Power, K. (2025) · Animals · doi:10.3390/ani15020264 · Cited by 3
Marques, O., Rosa, A., Leite, L., Faustino, P., Rêma, A., da Silva, B. M., Porto, G., & Lopes, C. (2016) · Cancer Microenvironment · doi:10.1007/s12307-016-0191-4 · Cited by 3
“Hemojuvelin [12, 13], involved in signal communication upon binding of the Bmp ligands, and whose interaction leads to the activation of hepcidin transcription [14–16].”
BackgroundMolecular Regulation of Systemic Iron Metabolism
Ganz, T., & Vaulont, S. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_9 · Cited by 4
The Role of Hepcidin in Iron Homeostasis
Ganz, T. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-462-9_3 · Cited by 3
Managing anaemia of chronic kidney disease
Murphy, F. L. M., Bennett, L., & Jenkins, K. (2010) · British Journal of Nursing · doi:10.12968/bjon.2010.19.20.79681 · Cited by 3
Silvestri, L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801816-3.00037-6 · Cited by 2
Métabolisme du fer : impact de l’hypoactivité et mécanismes sous-jacents
Nay, K., Horeau, M., Loréal, O., & Derbré, F. (2021) · Cahiers de Nutrition et de Diététique · doi:10.1016/j.cnd.2021.01.002 · Cited by 2
Olynyk, J. K., Grainger, R., Currie, H., Ramm, L. E., & Ramm, G. A. (2023) · Scientific Reports · doi:10.1038/s41598-023-35028-4 · Cited by 2
Papel de la hepcidina en la patogenia de la hemocromatosis
Altés, A., & Fortó, J. A. (2009) · Gastroenterología y Hepatología · doi:10.1016/j.gastrohep.2009.01.180 · Cited by 2
A novel homozygous stop-codon mutation in human HFE responsible for nonsense-mediated mRNA decay
Padula, M. C., Martelli, G., Larocca, M., Rossano, R., & Olivieri, A. (2014) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2014.04.010 · Cited by 2
Loréal, O., Bardou‐Jacquet, E., Island, M., Fatih, N., Doyard, M., Détivaud, L., & Brissot, P. (2012) · Cahiers de Nutrition et de Diététique · doi:10.1016/j.cnd.2012.01.003 · Cited by 6
Hepcydyna — hormon wątrobowy kontrolujący homeostazę żelaza
Filipczyk, L., Król, P., & Wystrychowski, A. (2010) · Via Medica Journals · Cited by 2
Hepcidin and the Hormonal Control of Iron Homeostasis
Frazer, D. M., & Anderson, G. J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802168-2.00015-4 · Cited by 2
Bergasa, N. V. (2021) · Springer eBooks · doi:10.1007/978-1-4471-4715-2_11 · Cited by 2
Dancygier, H., Merle, U., Stremmel, W., & Niederau, C. (2009) · Springer eBooks · doi:10.1007/978-3-540-93842-2_6 · Cited by 2
The Central Role of the Liver in Iron Storage and Regulation of Systemic Iron Homeostasis
Rouault, T. A., Gordeuk, V. R., & Anderson, G. J. (2020) · Wiley eBooks · doi:10.1002/9781119436812.ch19 · Cited by 2
Normal iron absorption and metabolism
Barton, J. C., Edwards, C. Q., Phatak, P. D., Britton, R. S., & Bacon, B. R. (2010) · Cambridge University Press eBooks · doi:10.1017/cbo9780511777035.004 · Cited by 1
Metabolism of Iron Ions and Its Role in Regulating the Functions of Immune System Cells
Orlova, E. G., & Gorbunova, O. L. (2026) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093026020018 · Cited by 1
Jaroszewicz, J., Rogalska, M., & Flisiak, R. (2009) · Journal of Hepatology · doi:10.1016/s0168-8278(09)60620-6 · Cited by 1
Padula, M. C., Larocca, M., Rossano, R., & MARTELLI, G. B. G. (2012) · CINECA IRIS Institutional Research Information System (University of Basilicata) · Cited by 1
Hafez, M. H., Abdelhamid, Y., & Ahmed, A. I. (2010) · African Journal of Nephrology · doi:10.21804/14-1-763 · Cited by 1
Hemochromatosis Gene Mutation and Erythrocytosis
Várkonyi, J. (2018) · Haematology International Journal · doi:10.23880/hij-16000126 · Cited by 1
“It has been shown that both types of TfRs bind to HFE proteins and have role in iron sensing [7].”
Advances in iron homeostasis and ferromagnetic nanoparticles
Wang, J., An, P., Wang, H., Wu, Q., Fang, X., Min, J., & Wang, F. (2018) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/n972018-00707
Pietrangelo, A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-37591-7.00060-4 · Cited by 1
Hong, Y., Xu, Z., Zheng, Y., Liu, J., Huang, Z., Chen, J.-S., Zhang, Y., & Liu, B. (2023) · Journal of Biomedical Nanotechnology · doi:10.1166/jbn.2023.3705 · Cited by 1
Management of Renal Anemia in Children with Chronic Kidney Disease
Yorgin, P. D., & Zaritsky, J. J. (2011) · Springer eBooks · doi:10.1007/978-1-4614-0721-8_27 · Cited by 1
Classical and atypical HFE hemochromatosis
Barton, J. C., Edwards, C. Q., Phatak, P. D., Britton, R. S., & Bacon, B. R. (2010) · Cambridge University Press eBooks · doi:10.1017/cbo9780511777035.010 · Cited by 1
Sox2 function as a negative regulator to control HAMP expression
Song, B., Bian, Q., Shao, C., Liu, A.-A., Jing, W., Liu, R., Zhang, Y., Zhou, Y., Li, G., & Jin, G. (2015) · Biological Research · doi:10.1186/s40659-015-0013-z · Cited by 1
Cunnane, G. (2016) · Elsevier eBooks · doi:10.1016/b978-0-323-31696-5.00118-2 · Cited by 1
Pietrangelo, A., & Torbenson, M. S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-7020-8228-3.00004-1 · Cited by 1
Santrampurwala, N. (2016) · The University of Queensland · doi:10.14264/uql.2016.365 · Cited by 1
Molecular coordination of iron homeostasis by microRNA
Davis, M. (2013) · SHAREOK (University of Oklahoma; Oklahoma State University; Central Oklahoma University) · Cited by 1
Genetic Markers, Birth Characteristics, and Childhood Leukemia Risk
Kennedy, A. E. (2013) · doi:10.25148/etd.fi13120601
Mousavi, S. A., Mahmood, F. A., Aandahl, A., Knutsen, T. R., & Llohn, A. H. (2015) · BioMed Research International · doi:10.1155/2015/241784
“Some authors have proposed that increased transferrin saturation leads to dissociation of HFE protein from TfR1 which subsequently forms a complex with TfR2, which in turn upregulates hepatic hepcidin expression [25].”
BackgroundIlkovska, B., Trifunova, B. K., & Трифунов, Г. (2015) · Macedonian Medical Electronic Journal · doi:10.3889/mmej.2015.50010
“Иако точните молекуларни механизми се уште не се целосно разjaснети, овoj коскен морфогенетски протеински (BMP) рецепторен – комплекс, се поврзува со трансферински рецептори 1 и 2, најверојатно поврзувајќи ја чувствителноста за серумското железо со синтезата на хепцидин [97, 98].”
Crawford, D. H., Fletcher, L. M., Anderson, G. J., Kowdley, K. V., McCaughan, G. W., & Trautwein, C. (2008) · Hepatology · doi:10.1002/hep.22427
Regulation of hepcidin and iron homeostasis: progress and prospects
Barrios, M. F., Delgado, N. F., & Hernández-Ramírez, P. (2012) · Revista cubana de hematología, inmunología y hemoterapia
Metadata
- Authors
- Goswami, T., & Andrews, N. C.
- Affiliations
- Boston Children's Hospital (US)
- Corresponding author
- Andrews, Nancy C.
- ORCID
- Andrews, Nancy C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 281
- Issue
- 39
- Pages
- 28494-28498
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1983970155
- Cited by
- 352
- References
- 20
- Citations by year
- 2026: 6 · 2025: 2 · 2024: 1 · 2023: 6 · 2022: 4 · 2021: 15 · 2020: 13 · 2019: 12 · 2018: 12 · 2017: 18 · 2016: 16 · 2015: 16 · 2014: 18 · 2013: 31 · 2012: 17
- FWCI
- 19.02
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK53813, R01DK053813)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- hereditary hemochromatosis, HFE gene, transferrin receptor 2, transferrin receptor 1, protein-protein interaction, iron homeostasis, iron sensing, disease-associated mutations
- MeSH terms
- Hemochromatosis Protein, Animals, Hemochromatosis, Homeostasis, Humans, Iron, Membrane Proteins, Models, Biological, Mutation, Receptors, Transferrin, Histocompatibility Antigens Class I, Antigens, CD, 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