The roles of iron in health and disease

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

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

Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion

Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786

Disorders of Iron Metabolism

Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130

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

A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation

McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422

Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress.

Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292

Regulating the fate of mRNA: the control of cellular iron metabolism

Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210

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

Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg

Vidal, S. M., Malo, D., Vogan, K., Skamene, E., & Gros, P. (1993) · Cell · doi:10.1016/0092-8674(93)90135-d · Cited by 1,104

Clinical and Genetic Abnormalities in Patients with Friedreich's Ataxia

Dürr, A., Cossee, M., Agid, Y., Campuzano, V., Mignard, C., Penet, C., Mandel, J.-L., Brice, A., & Koenig, M. (1996) · New England Journal of Medicine · doi:10.1056/nejm199610173351601 · Cited by 1,071

Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia

DEXTER, D. T., CARAYON, A., JAVOY-AGID, F., AGID, Y., WELLS, F. R., DANIEL, S. E., LEES, A. J., JENNER, P., & MARSDEN, C. D. (1991) · Brain · doi:10.1093/brain/114.4.1953 · Cited by 1,043

Serum Transferrin Receptor and Its Ratio to Serum Ferritin in the Diagnosis of Iron Deficiency

Punnonen, K., Irjala, K., & Rajamäki, A. (1997) · Blood · doi:10.1182/blood.v89.3.1052 · Cited by 859

The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding

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

The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22

Camaschella, C., Roetto, A., Calì, A., De Gobbi, M., Garozzo, G., Carella, M., Majorano, N., Totaro, A., & Gasparini, P. (2000) · Nature Genetics · doi:10.1038/75534 · Cited by 803

Iron-Responsive Elements: Regulatory RNA Sequences That Control mRNA Levels and Translation

Casey, J. L., Hentze, M. W., Koeller, D. M., Caughman, S. W., Rouault, T. A., Klausner, R. D., & Harford, J. B. (1988) · Science · doi:10.1126/science.2452485 · Cited by 709

STRUCTURE, FUNCTION, AND DIVERSITY OF CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULES

Bjorkman, P. J., & Parham, P. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.001345 · Cited by 700

Transferrin receptor is necessary for development of erythrocytes and the nervous system

Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574

Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux

Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10812 · Cited by 568

Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis

Collawn, J. F., Stangel, M., Kuhn, L. A., Esekogwu, V., Jing, S., Trowbridge, I. S., & Tainer, J. A. (1990) · Cell · doi:10.1016/0092-8674(90)90509-d · Cited by 518

The Hemochromatosis Founder Mutation in HLA-H Disrupts β2-Microglobulin Interaction and Cell Surface Expression

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

Stimulation of lipid peroxidation and hydroxyl-radical generation by the contents of human atherosclerotic lesions

Smith, C., Mitchinson, M. J., Aruoma, O. I., & Halliwell, B. (1992) · Biochemical Journal · doi:10.1042/bj2860901 · Cited by 455

Regulators of iron balance in humans [see comments]

Finch, C. (1994) · Blood · doi:10.1182/blood.v84.6.1697.1697 · Cited by 455

Identification of a hypoxia response element in the transferrin receptor gene

Lok, C. N., & Ponka, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24147 · Cited by 380

Iron regulates ferritin mRNA translation through a segment of its 5′-untranslated region.

Aziz, N., & Munro, H. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8478 · Cited by 368

Transferrin and Iron in Normal, Alzheimer's Disease, and Parkinson's Disease Brain Regions

Loeffler, D. A., Connor, J. R., Juneau, P. L., Snyder, B. S., Kanaley, L., DeMaggio, A. J., Nguyen, H., Brickman, C. M., & LeWitt, P. A. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65020710.x · Cited by 334

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

IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F.

Muckenthaler, M., Gray, N. K., & Hentze, M. W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80282-8 · Cited by 297

Mutation in the iron responsive element of the L ferritin mRNA in a family with dominant hyperferritinaemia and cataract

Beaumont, C., Leneuve, P., Devaux, I., Scoazec, J.-Y., Berthier, M., Loiseau, M.-N., Grandchamp, B., & Bonneau, D. (1995) · Nature Genetics · doi:10.1038/ng1295-444 · Cited by 293

The Yeast Frataxin Homologue Mediates Mitochondrial Iron Efflux

Radisky, D. C., Babcock, M. C., & Kaplan, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4497 · Cited by 277

Mechanism of increased iron absorption in murine model of hereditary hemochromatosis: Increased duodenal expression of the iron transporter DMT1

Fleming, R. E., Migas, M. C., Zhou, X., Jiang, J., Britton, R. S., Brunt, E. M., Tomatsu, S., Waheed, A., Bacon, B. R., & Sly, W. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3143 · Cited by 269

Increased basal ganglia iron levels in Huntington disease

Bartzokis, G., Cummings, J., Perlman, S., Hance, D. B., & Mintz, J. (1999) · Archives of Neurology · doi:10.1001/archneur.56.5.569 · Cited by 183

The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor 1 1Edited by I. A. Wilson

Lebrón, J. A., West, A. P., & Bjorkman, P. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3252 · Cited by 182

Use of desferrioxamine in the treatment of aceruloplasminemia

Miyajima, H., Takahashi, Y., Kamata, T., Shimizu, H., Sakai, N., & Gitlin, J. D. (1997) · Annals of Neurology · doi:10.1002/ana.410410318 · Cited by 173

Regulation of iron metabolism in the acute‐phase response: interferon γ and tumour necrosis factor α induce hypoferraemia, ferritin production and a decrease in circulating transferrin receptors in cancer patients

Feelders, Vreugdenhil, Eggermont, Kuiper‐Kramer, Eijk, V., & Swaak (1998) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.1998.00323.x · Cited by 172

Duodenal metal-transporter (DMT-1, NRAMP-2) expression in patients with hereditary haemochromatosis

Zoller, H., Pietrangelo, A., Vogel, W., & Weiss, G. (1999) · The Lancet · doi:10.1016/s0140-6736(98)11179-0 · Cited by 167

Modulation of iron metabolism in monocyte cell line U937 by inflammatory cytokines: changes in transferrin uptake, iron handling and ferritin mRNA.

Fahmy, M., & Young, S. P. (1993) · Biochemical Journal · doi:10.1042/bj2960175 · Cited by 150

Inappropriately high iron regulatory protein activity in monocytes of patients with genetic hemochromatosis

Cairo, G., Recalcati, S., Montosi, G., Castrusini, E., Conte, D., & Pietrangelo, A. (1997) · Blood · doi:10.1182/blood.v89.7.2546 · Cited by 96

Essential metals in health and disease

Jomova, K., Makova, M., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., Rhodes, C. J., & Valko, M. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110173 · Cited by 1,121

The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer

Kalinowski, D. S., & Richardson, D. R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.2 · Cited by 721

An Iron Delivery Pathway Mediated by a Lipocalin

Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651

Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases

Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554

Molecular mechanisms of ferroptosis and their involvement in brain diseases

Costa, I., Barbosa, D. J., Benfeito, S., Silva, V., Chavarria, D., Borges, F., Remião, F., & Silva, R. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108373 · Cited by 402