The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor 1 1Edited by I. A. Wilson
Abstract
HFE is a class I major histocompatibility complex (MHC)-related protein that is mutated in patients with the iron overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR), the receptor used by cells to obtain iron in the form of diferric transferrin (Fe-Tf). Previous studies demonstrated that HFE and Fe-Tf can bind simultaneously to TfR to form a ternary complex, and that membrane-bound or soluble HFE binding to cell surface TfR results in a reduction in the affinity of TfR for Fe-Tf. We studied the inhibition by soluble HFE of the interaction between soluble TfR and Fe-Tf using radioactivity-based and biosensor-based assays. The results demonstrate that HFE inhibits the TfR:Fe-Tf interaction by binding at or near the Fe-Tf binding site on TfR, and that the Fe-Tf:TfR:HFE ternary complex consists of one Fe-Tf and one HFE bound to a TfR homodimer.
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Mitochondrial ferritin genes do not have IRE in both human and mouse.
“mitochondrial ferritin genes do not have IRE in both the human and the mouse (74, 182).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [182]
Cites
A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, R., Ellis, M. C., Fullan, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0896-399 · Cited by 3,664 · see citing works
Proteins: Structures and Molecular Properties
Creighton, T. E. (1986) · Medical Entomology and Zoology · Cited by 2,652 · see citing works
Antigen Recognition By Class-I Restricted T Lymphocyte
Townsend, A., & Bodmer, H. C. (1989) · Annual Review of Immunology · doi:10.1146/annurev.iy.07.040189.003125 · Cited by 1,192 · see citing works
Feder, J. N., Penny, D. M., Irrinki, A., Lee, V. K., Lebrón, J. A., Watson, N., Tsuchihashi, Z., Sigal, E., Bjorkman, P. J., & Schatzman, R. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1472 · Cited by 827 · see citing works
Self-citationGlobal prevalence of putative haemochromatosis mutations.
Merryweather‐Clarke, A. T., Pointon, J. J., Shearman, J. R., & Robson, K. (1997) · Journal of Medical Genetics · doi:10.1136/jmg.34.4.275 · Cited by 785 · see citing works
The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
Richardson, D. R., & Ponka, P. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(96)00014-7 · Cited by 706 · see citing works
Lebrón, J., Bennett, M. J., Vaughn, D., Chirino, A., Snow, P., Mintier, G., Feder, J., & Bjorkman, P. (1998) · Cell · doi:10.1016/s0092-8674(00)81151-4 · Cited by 636 · see citing works
Self-citationBiospecific interaction analysis using biosensor technology
Malmqvist, M. (1993) · Nature · doi:10.1038/361186a0 · Cited by 534 · see citing works
Feder, J. N., Tsuchihashi, Z., Irrinki, A., Lee, V. K., Mapa, F. A., Morikang, E., Prass, C. E., Starnes, S. M., Wolff, R. K., Parkkila, S., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14025 · Cited by 471 · see citing works
Aisen, P., Wessling‐Resnick, M., & Leibold, E. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80033-7 · Cited by 424 · see citing works
Waheed, A., Parkkila, S., Zhou, X. Y., Tomatsu, S., Tsuchihashi, Z., Feder, J. N., Schatzman, R. C., Britton, R. S., Bacon, B. R., & Sly, W. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12384 · Cited by 380 · see citing works
Parkkila, S., Waheed, A., Britton, R. S., Bacon, B. R., Zhou, X. Y., Tomatsu, S., Fleming, R. E., & Sly, W. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13198 · Cited by 336 · see citing works
Crystal Structure of the Ectodomain of Human Transferrin Receptor
Lawrence, C. M., Ray, S., Babyonyshev, M., Galluser, R., Borhani, D. W., & Harrison, S. C. (1999) · Science · doi:10.1126/science.286.5440.779 · Cited by 315 · see citing works
Gross, C. N., Irrinki, A., Feder, J. N., & Enns, C. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.22068 · Cited by 227 · see citing works
Proteins: Structures and Molecular Properties
Wood, E. (1985) · Biochemical Education · doi:10.1016/0307-4412(85)90028-7 · Cited by 213 · see citing works
Roy, C. N., Penny, D. M., Feder, J. N., & Enns, C. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.9022 · Cited by 206 · see citing works
The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes
Young, S. P., Bomford, A. B., & Williams, R. J. R. (1984) · Biochemical Journal · doi:10.1042/bj2190505 · Cited by 176 · see citing works
Salter–Cid, L., Brunmark, A. B., Li, Y., Leturcq, D. J., Peterson, P. A., Jackson, M. R., & Yang, Y. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5434 · Cited by 152 · see citing works
Physical characterization of the transferrin receptor in human placentae.
Enns, C. A., & Sussman, H. H. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68700-4 · Cited by 88 · see citing works
Lebrón, J. A., & Björkman, P. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2842 · Cited by 83 · see citing works
Self-citationAnderson, G. J. (1996) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.1996.tb00029.x · Cited by 31 · see citing works
Crystallization and X-ray diffraction studies of a soluble form of the human transferrin receptor
Borhani, D. W., & Harrison, S. C. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90255-5 · Cited by 27 · see citing works
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Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122 · see citing works
Targeted Drug Delivery via the Transferrin Receptor-Mediated Endocytosis Pathway
Qian, Z., Li, H., Sun, H., & Ho, K. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.4.561 · Cited by 1,021 · see citing works
Hereditary Hemochromatosis — A New Look at an Old Disease
Pietrangelo, A. (2004) · New England Journal of Medicine · doi:10.1056/nejmra031573 · Cited by 992 · see citing works
The roles of iron in health and disease
Lieu, P. T., Heiskala, M. K., Peterson, P. A., & Yang, Y. M. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(00)00006-6 · Cited by 813 · see citing works
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804 · see citing works
Daniels‐Wells, T. R., Delgado, T., Rodríguez, J. A., Helguera, G. F., & Penichet, M. L. (2006) · Clinical Immunology · doi:10.1016/j.clim.2006.06.010 · Cited by 630 · see citing works
Structure of the human transferrin receptor-transferrin complex
Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571 · see citing works
Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526 · see citing works
Viral infection and iron metabolism
Drakesmith, H., & Prentice, A. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1930 · Cited by 469 · see citing works
Transferrin/transferrin receptor‐mediated drug delivery
Li, H., & Qian, Z. (2002) · Medicinal Research Reviews · doi:10.1002/med.10008 · Cited by 441 · see citing works
The Transferrin Receptor Modulates Hfe-Dependent Regulation of Hepcidin Expression
Schmidt, P. J., Toran, P. T., Giannetti, A. M., Bjorkman, P. J., & Andrews, N. C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.016 · Cited by 345 · see citing works
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 338 · see citing works
Self-citationAisen, P. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.007 · Cited by 329 · see citing works
Gallium and its competing roles with iron in biological systems.
Chitambar, C. (2016) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2016.04.027 · Cited by 243 · see citing works
Lin, L., Valore, E. V., Nemeth, E., Goodnough, J. B., Gabayan, V., & Ganz, T. (2007) · Blood · doi:10.1182/blood-2007-04-087593 · Cited by 267 · see citing works
Digenic inheritance of mutations in HAMP and HFE results in different types of haemochromatosis
Merryweather‐Clarke, A. T. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg225 · Cited by 262 · see citing works
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 · see citing works
Self-citationMolecular Mechanisms of Hepcidin Regulation: Implications for the Anemia of CKD
Babitt, J. L., & Lin, H. Y.-F. (2010) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2009.12.030 · Cited by 236 · see citing works
Molecular Pharmacology of the Interaction of Anthracyclines with Iron
Xu, X., Persson, H. L., & Richardson, D. R. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.013383 · Cited by 235 · see citing works
Genes that modify the hemochromatosis phenotype in mice
Levy, J. E., Montross, L. K., & Andrews, N. C. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9635 · Cited by 212 · see citing works
D’Alessio, F., Hentze, M. W., & Muckenthaler, M. U. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.06.015 · Cited by 200 · see citing works
Alves, F. M., Lane, D. J. R., Nguyen, T. P. M., Bush, A. I., & Ayton, S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02088-5 · Cited by 197 · see citing works
Iron homeostasis: An anthropocentric perspective
Coffey, R., & Ganz, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.781823 · Cited by 189 · see citing works
The liver: conductor of systemic iron balance
Meynard, D., Babitt, J. L., & Lin, H. Y.-F. (2013) · Blood · doi:10.1182/blood-2013-06-427757 · Cited by 178 · see citing works
Iron homeostasis: new tales from the crypt
Roy, C. N., & Enns, C. A. (2000) · Blood · doi:10.1182/blood.v96.13.4020 · Cited by 175 · see citing works
Iron uptake and transport across physiological barriers
Duck, K. A., & Connor, J. R. (2016) · BioMetals · doi:10.1007/s10534-016-9952-2 · Cited by 176 · see citing works
Widera, A., Norouziyan, F., & Shen, W. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.07.004 · Cited by 173 · see citing works
Iron refractory iron deficiency anemia
Falco, L. D., Sánchez, M., Silvestri, L., Kannengiesser, C., Muckenthaler, M. U., Iolascon, A., Gouya, L., Camaschella, C., & Beaumont, C. (2013) · Haematologica · doi:10.3324/haematol.2012.075515 · Cited by 182 · see citing works
Mechanisms of Iron Accumulation in Hereditary Hemochromatosis
Fleming, R. E., & Sly, W. S. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.081501.155838 · Cited by 172 · see citing works
The Regulation of Cellular Iron Metabolism
Chua, A. C. G., Graham, R. M., Trinder, D., & Olynyk, J. K. (2007) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701428257 · Cited by 168 · see citing works
HFE gene: Structure, function, mutations, and associated iron abnormalities
Barton, J. C., Edwards, C. Q., & Acton, R. T. (2015) · Gene · doi:10.1016/j.gene.2015.10.009 · Cited by 160 · see citing works
Carter, C. J. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.07.007 · Cited by 148 · see citing works
Waheed, A., Grubb, J. H., Zhou, X., Tomatsu, S., Fleming, R. E., Costaldi, M. E., Britton, R. S., Bacon, B. R., & Sly, W. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042701499 · Cited by 148 · see citing works
HFE and Transferrin Directly Compete for Transferrin Receptor in Solution and at the Cell Surface
Giannetti, A. M., & Björkman, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401467200 · Cited by 143 · see citing works
Self-citationBone Morphogenetic Protein Signaling Is Impaired in an Hfe Knockout Mouse Model of Hemochromatosis
Corradini, E., Garuti, C., Montosi, G., Ventura, P., Andriopoulos, B., Lin, H. Y.-F., Pietrangelo, A., & Babitt, J. L. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.06.057 · Cited by 140 · see citing works
McKie, A. T., & Simpson, R. J. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_6 · Cited by 132 · see citing works
Localisation of proteins of iron metabolism in the human placenta and liver
Bastin, J. M., Drakesmith, H., REES, M. C. P., Sargent, I. L., & Townsend, A. (2006) · British Journal of Haematology · doi:10.1111/j.1365-2141.2006.06216.x · Cited by 130 · see citing works
The hemochromatosis protein HFE inhibits iron export from macrophages
Drakesmith, H., Sweetland, E., Schimanski, L., Edwards, J., Cowley, D., Ashraf, M., Bastin, J., & Townsend, A. R. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242614699 · Cited by 128 · see citing works
Jung, C. (2000) · Journal of Molecular Recognition · doi:10.1002/1099-1352(200011/12)13:6 · Cited by 245 · see citing works
West, A. P., Giannetti, A. M., Herr, A. B., Bennett, M. J., Nangiana, J. S., Pierce, J. R., Weiner, L. P., Snow, P. M., & Björkman, P. J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5048 · Cited by 125 · see citing works
Self-citationHFE Gene Variants Affect Iron in the Brain1–3
Nandar, W., & Connor, J. R. (2011) · Journal of Nutrition · doi:10.3945/jn.110.130351 · Cited by 125 · see citing works
Mechanism for Multiple Ligand Recognition by the Human Transferrin Receptor
Giannetti, A. M., Snow, P. M., Zak, O., & Björkman, P. J. (2003) · PLoS Biology · doi:10.1371/journal.pbio.0000051 · Cited by 122 · see citing works
Fillebeen, C., Charlebois, E., Wagner, J., Katsarou, A., Mui, J., Vali, H., Garcia‐Santos, D., Ponka, P., Presley, J. F., & Pantopoulos, K. (2018) · Blood · doi:10.1182/blood-2018-05-850404 · Cited by 120 · see citing works
Hepcidin modulation in human diseases: From research to clinic
Piperno, A., Mariani, R., Trombini, P., & Girelli, D. (2009) · World Journal of Gastroenterology · doi:10.3748/wjg.15.538 · Cited by 115 · see citing works
Transferrin Receptors TfR1 and TfR2 Bind Transferrin through Differing Mechanisms
Kleven, M. D., Jue, S. F., & Enns, C. A. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00006 · Cited by 112 · see citing works
BMP/Smad signaling is not enhanced in Hfe-deficient mice despite increased Bmp6 expression
Kautz, L., Meynard, D., Besson‐Fournier, C., Darnaud, V., Saati, T. A., Coppin, H., & Roth, M. (2009) · Blood · doi:10.1182/blood-2009-02-206771 · Cited by 110 · see citing works
Regulation of iron absorption in Hfe mutant mice
Ajioka, R. S., Levy, J. E., Andrews, N. C., & Kushner, J. P. (2002) · Blood · doi:10.1182/blood-2001-11-0037 · Cited by 95 · see citing works
Gardenghi, S., Grady, R. W., & Rivella, S. (2010) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2010.08.003 · Cited by 96 · see citing works
Transferrin-modified chitosan nanoparticles for targeted nose-to-brain delivery of proteins
Gabold, B., Adams, F., Brameyer, S., Jung, K., Ried, C. L., Merdan, T., & Merkel, O. M. (2022) · Drug Delivery and Translational Research · doi:10.1007/s13346-022-01245-z · Cited by 93 · see citing works
A general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 92 · see citing works
Bone morphogenic proteins in iron homeostasis
Xiao, X., Alfaro-Magallanes, V. M., & Babitt, J. L. (2020) · Bone · doi:10.1016/j.bone.2020.115495 · Cited by 88 · see citing works
Hereditary Hemochromatosis Since Discovery of the HFE Gene
Lyon, E., & Frank, E. L. (2001) · Clinical Chemistry · doi:10.1093/clinchem/47.7.1147 · Cited by 87 · see citing works
Uncommon Mutations and Polymorphisms in the Hemochromatosis Gene
Pointon, J. J., Wallace, D. F., Merryweather‐Clarke, A. T., & Robson, K. (2000) · Genetic Testing · doi:10.1089/10906570050114867 · Cited by 87 · see citing works
Chen, J., Chloupková, M., Gao, J., Arvedson, T., & Enns, C. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706720200 · Cited by 81 · see citing works
Intestinal expression of genes involved in iron absorption in humans
Rolfs, A., Bonkovsky, H. L., Kohlroser, J. G., McNeal, K., Sharma, A. K., Berger, U. V., & Hediger, M. A. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00371.2001 · Cited by 82 · see citing works
Molecular aspects of iron absorption and HFE expression
Parkkila, S., Niemelä, O. J., Britton, R. S., Fleming, R. E., Waheed, A., Bacon, B. R., & Sly, W. S. (2001) · Gastroenterology · doi:10.1053/gast.2001.29617 · Cited by 78 · see citing works
Townsend, A., & Drakesmith, H. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07885-6 · Cited by 79 · see citing works
Zumbrennen‐Bullough, K. B., & Babitt, J. L. (2013) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gft443 · Cited by 80 · see citing works
Lipiński, P., Styś, A., & Starzyński, R. R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1018-1 · Cited by 73 · see citing works
Beyond the Signal Sequence: Protein Routing in Health and Disease
Castro-Fernández, C., Maya‐Núñez, G., & Conn, P. M. (2004) · Endocrine Reviews · doi:10.1210/er.2004-0010 · Cited by 73 · see citing works
Herrmann, T., Muckenthaler, M., van der Hoeven, F., Brennan, K., Gehrke, S. G., Hubert, N., Sergi, C., Gröne, H.-J., Kaiser, I., Gosch, I., et al. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0508-x · Cited by 69 · see citing works
Arieh, S. V.-B., Zimerman, B., Smorodinsky, N. I., Yaacubovicz, M., Schechter, C., Bačík, I., Gibbs, J., Bennink, J. R., Yewdell, J. W., Coligan, J. E., et al. (2001) · Journal of Virology · doi:10.1128/jvi.75.21.10557-10562.2001 · Cited by 67 · see citing works
Cureton, D. K., Harbison, C. E., Cocucci, E., Parrish, C. R., & Kirchhausen, T. L. (2012) · Journal of Virology · doi:10.1128/jvi.07194-11 · Cited by 65 · see citing works
Barton, J. C., & Acton, R. T. (2017) · Journal of Diabetes Research · doi:10.1155/2017/9826930 · Cited by 65 · see citing works
Nandar, W., Neely, E. B., Unger, E., & Connor, J. R. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.02.009 · Cited by 64 · see citing works
Hemochromatosis gene modifies course of hepatitis C viral infection
Pietrangelo, A. (2003) · Gastroenterology · doi:10.1016/s0016-5085(03)00275-0 · Cited by 60 · see citing works
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 · see citing works
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 · see citing works
Liu, Y., Lee, S. Y., Neely, E. B., Nandar, W., Moyo, M., Simmons, Z., & Connor, J. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.170944 · Cited by 52 · see citing works
Ramos, P., Guy, E. C., Chen, N., Proenca, C. C., Gardenghi, S., Casu, C., Follenzi, A., van Rooijen, N., Grady, R. W., de Sousa, M. A. B., et al. (2010) · Blood · doi:10.1182/blood-2010-09-307462 · Cited by 53 · see citing works
HFE inhibits type I IFNs signaling by targeting the SQSTM1-mediated MAVS autophagic degradation
Liu, J., Wu, X., Wang, H., Wei, J., Wu, Q., Wang, X., Yan, Y., Cui, J., Min, J., Wang, F., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1804683 · Cited by 52 · see citing works
Giannetti, A. M., Halbrooks, P. J., Mason, A. B., Vogt, T. M., Enns, C. A., & Björkman, P. J. (2005) · Structure · doi:10.1016/j.str.2005.07.016 · Cited by 52 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Arieh, S. V.-B., Laham-Karam, N., Schechter, C., Yewdell, J. W., Coligan, J. E., & Ehrlich, R. L. (2003) · Blood · doi:10.1182/blood-2002-07-2158 · Cited by 52 · see citing works
Function of the hemochromatosis protein HFE: Lessons from animal models
Pantopoulos, K. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.6893 · Cited by 49 · see citing works
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 · see citing works
Ramalingam, T. S., West, A. P., Lebrón, J. A., Nangiana, J. S., Hogan, T. H., Enns, C. A., & Björkman, P. J. (2000) · Nature Cell Biology · doi:10.1038/35046611 · Cited by 49 · see citing works
Self-citationRetractedDavies, P. S., & Enns, C. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400537200 · Cited by 47 · see citing works
Heterotypic interactions between transferrin receptor and transferrin receptor 2
Vogt, T. M., Blackwell, A. D., Giannetti, A. M., Björkman, P. J., & Enns, C. A. (2003) · Blood · doi:10.1182/blood-2002-09-2742 · Cited by 47 · see citing works
Hepatic macrophage iron aggravates experimental alcoholic steatohepatitis
Xiong, S., She, H., Zhang, A., Wang, J., Mkrtchyan, H., Dynnyk, A., Gordeuk, V. R., French, S. W., Enns, C. A., & Tsukamoto, H. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90327.2008 · Cited by 45 · see citing works
Enns, C. A. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.020303.x · Cited by 45 · see citing works
Gac, G. L., Dupradeau, F., Mura, C., Jacolot, S., Scotet, V., Esnault, G., Mercier, A., Rochette, J., & Férec, C. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00036-6 · Cited by 44 · see citing works
Wilson disease: At the crossroads between genetics and epigenetics—A review of the evidence
Kieffer, D. A., & Medici, V. (2017) · Liver Research · doi:10.1016/j.livres.2017.08.003 · Cited by 43 · see citing works
Structural Allostery and Binding of the Transferrin·Receptor Complex
Xu, G., Liu, R., Zak, O., Aisen, P., & Chance, M. R. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500095-mcp200 · Cited by 43 · see citing works
Structural diversity of class I MHC-like molecules and its implications in binding specificities
Hassan, M. I., & Ahmad, F. (2011) · Advances in protein chemistry and structural biology · doi:10.1016/b978-0-12-381262-9.00006-9 · Cited by 42 · see citing works
HFE gene variants, iron, and lipids: a novel connection in Alzheimer’s disease
Ali-Rahmani, F. G., Schengrund, C., & Connor, J. R. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00165 · Cited by 42 · see citing works
HFEgene in primary and secondary hepatic iron overload
Sebastiani, G. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4673 · Cited by 41 · see citing works
Ajioka, R. S., & Kushner, J. P. (2002) · Seminars in Hematology · doi:10.1053/shem.2002.35634 · Cited by 39 · see citing works
Mechanisms of HFE-induced regulation of iron homeostasis: Insights from the W81A HFE mutation
Zhang, A., Davies, P. S., Carlson, H. L., & Enns, C. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1233675100 · Cited by 38 · see citing works
Mysteries of the Transferrin-Transferrin Receptor 1 Interaction Uncovered
Richardson, D. R. (2004) · Cell · doi:10.1016/s0092-8674(04)00165-5 · Cited by 37 · see citing works
Livesey, K., Wimhurst, V. L. C., Carter, K., Worwood, M., Cadet, E., Rochette, J., Roberts, A. G., Pointon, J. J., Merryweather-Clarke, A. T., Bassett, M. L., et al. (2004) · Journal of Medical Genetics · doi:10.1136/jmg.2003.008805 · Cited by 36 · see citing works
Davies, P. S., Zhang, A., ANDERSON, E. L., Roy, C. N., Lampson, M. A., McGraw, T. E., & Enns, C. A. (2003) · Biochemical Journal · doi:10.1042/bj20030202 · Cited by 35 · see citing works
Cells under siege: Viral glycoprotein interactions at the cell surface
Bowden, T. A., Jones, E. Y., & Stuart, D. I. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.03.016 · Cited by 32 · see citing works
Regulation of Iron Absorption in Hemoglobinopathies
Rechavi, G., & Rivella, S. (2008) · Current Molecular Medicine · doi:10.2174/156652408786241401 · Cited by 32 · see citing works
Roy, C. N., Carlson, E. J., Anderson, E. L., Basava, A., Starnes, S. M., Feder, J. N., & Enns, C. A. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02173-6 · Cited by 33 · see citing works
Miquel, G., Nekaa, T., Kahn, P. H., Hémadi, M., & Chahine, J. E. H. (2004) · Biochemistry · doi:10.1021/bi048484p · Cited by 32 · see citing works
Biochemical and genetic defects underlying human congenital hypotransferrinemia
Goldwurm, S., Casati, C., Venturi, N., Strada, S., Santambrogio, P., Indraccolo, S., Arosio, P., Cazzola, M., Piperno, A., Masera, G., et al. (2000) · The Hematology Journal · doi:10.1038/sj.thj.6200063 · Cited by 30 · see citing works
WANG, J., CHEN, G., & PANTOPOULOS, K. (2003) · Biochemical Journal · doi:10.1042/bj20021607 · Cited by 28 · see citing works
- Authors
- Lebrón, J. A., West, A. P., & Bjorkman, P. J.
- Affiliations
- California Institute of Technology (US)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 294
- Issue
- 1
- Pages
- 239-245
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2061390170
- Cited by
- 182
- References
- 22
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 1 · 2022: 3 · 2021: 2 · 2020: 3 · 2018: 2 · 2017: 4 · 2016: 5 · 2015: 2 · 2014: 4 · 2013: 10 · 2012: 5
- Type
- book review
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM007616, GM07616)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- HFE gene, transferrin receptor 1, hereditary hemochromatosis, iron overload, transferrin, ternary complex, ligand-receptor interactions, iron absorption
- MeSH terms
- Hemochromatosis Protein, Binding, Competitive, Ferric Compounds, Hemochromatosis, HLA Antigens, Humans, Membrane Proteins, Protein Binding, Receptors, Transferrin, Recombinant Proteins, Transferrin, Biosensing Techniques, Histocompatibility Antigens Class I
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