Regulation of cellular iron metabolism

Anemia of Chronic Disease

Weiss, G., & Goodnough, L. T. (2005) · New England Journal of Medicine · doi:10.1056/nejmra041809 · Cited by 3,800

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

Disorders of Iron Metabolism

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

Two to tango: Regulation of Mammalian iron metabolism

Hentze, M. W., Muckenthaler, M. U., Galy, B., & Camaschella, C. (2010) · Cell · doi:10.1016/j.cell.2010.06.028 · Cited by 2,120

Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron

Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877

Iron, brain ageing and neurodegenerative disorders

Zecca, L., Youdim, M. B. H., Riederer, P., Connor, J. R., & Crichton, R. R. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1537 · Cited by 1,801

Identification of the haemoglobin scavenger receptor

Kristiansen, M., Graversen, J. H., Jacobsen, C., Sonne, O., Hoffman, H.-J., Law, S. K. A., & Moestrup, S. K. (2001) · Nature · doi:10.1038/35051594 · Cited by 1,712

Structure, function, and formation of biological iron-sulfur clusters

Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438

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

The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition

Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355

The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis

Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275

A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism

Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267

Regulation of ferritin genes and protein

Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173

Function and biogenesis of iron-sulphur proteins

Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167

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

The role of iron regulatory proteins in mammalian iron homeostasis and disease

Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055

Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury

Mori, K., Lee, H. T., Rapoport, D., Drexler, I. R., Foster, K., Yang, J., Schmidt-Ott, K. M., Chen, X., Li, J. Y., Weiss, S., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23056 · Cited by 954

Nramp 2 is mutated in the anemic Belgrade ( b ) rat: Evidence of a role for Nramp2 in endosomal iron transport

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

Ferritins: A family of molecules for iron storage, antioxidation and more

Arosio, P., Ingrassia, R., & Cavadini, P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.004 · Cited by 886

High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin

Tanno, T., Bhanu, N. V., Oneal, P. A., Goh, S.-H., Staker, P., Lee, Y. T., Moroney, J. W., Reed, C. H., Luban, N. L., Wang, R.-H., et al. (2007) · Nature Medicine · doi:10.1038/nm1629 · Cited by 854

The heme synthesis and degradation pathways: role in oxidant sensitivity

Ryter, S. W., & Tyrrell, R. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00223-3 · Cited by 825

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

Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells

Ohgami, R. S., Campagna, D. R., Greer, E. L., Antiochos, B., McDonald, A., Chen, J., Sharp, J. J., Fujiwara, Y., Barker, J. E., & Fleming, M. D. (2005) · Nature Genetics · doi:10.1038/ng1658 · Cited by 775

BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism

Andriopoulos Jr, B., Corradini, E., Xia, Y., Faasse, S. A., Chen, S., Grgurevic, L., Knutson, M. D., Pietrangelo, A., Vukicevic, S., Lin, H. Y., et al. (2009) · Nature Genetics · doi:10.1038/ng.335 · Cited by 769

Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network

Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701

Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease

Duce, J. A., Tsatsanis, A., Cater, M. A., James, S., Robb, E. L., Wikhe, K., Leong, S. L., Perez, K. A., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 695

A Cell-Surface Receptor for Lipocalin 24p3 Selectively Mediates Apoptosis and Iron Uptake

Devireddy, L. R., Gazin, C., Zhu, X., & Green, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.10.027 · Cited by 672

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

Mitoferrin is essential for erythroid iron assimilation

Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624

Forging a field: the golden age of iron biology.

Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623

Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo

Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620

A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression

Wang, R.-H., Li, C., Xu, X., Zheng, Y., Xiao, C., Zerfas, P., Cooperman, S., Eckhaus, M., Rouault, T., Mishra, L., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.010 · Cited by 614

The transferrin receptor: role in health and disease

Ponka, P., & Lok, C. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00070-9 · Cited by 609

The Role of Hepcidin in Iron Metabolism

Nemeth, E., & Ganz, T. (2009) · Acta Haematologica · doi:10.1159/000243791 · Cited by 607

Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo

Rankin, E. B., Biju, M. P., Liu, Q., Unger, T. L., Rha, J., Johnson, R. S., Simon, M. C., Keith, B., & Haase, V. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30117 · Cited by 596

JunD Reduces Tumor Angiogenesis by Protecting Cells from Oxidative Stress

Gerald, D., Berra, E., Frapart, Y. M., Chan, D. A., Giaccia, A. J., Mansuy, D., Pouysségur, J., Yaniv, M., & Mechta-Grigoriou, F. (2004) · Cell · doi:10.1016/j.cell.2004.08.025 · Cited by 588

Lack of the bone morphogenetic protein BMP6 induces massive iron overload

Meynard, D., Kautz, L., Darnaud, V., Canonne-Hergaux, F., Coppin, H., & Roth, M.-P. (2009) · Nature Genetics · doi:10.1038/ng.320 · Cited by 587

Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells

Liuzzi, J. P., Aydemir, F., Nam, H., Knutson, M. D., & Cousins, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606424103 · Cited by 577

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

Binding and uptake of H-ferritin are mediated by human transferrin receptor-1

Li, L., Fang, C. J., Ryan, J. C., Niemi, E. C., Lebrón, J. A., Björkman, P. J., Arase, H., Torti, F. M., Torti, S. V., Nakamura, M. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913192107 · Cited by 558

The Serine Protease Matriptase-2 (TMPRSS6) Inhibits Hepcidin Activation by Cleaving Membrane Hemojuvelin

Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J., & Camaschella, C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.012 · Cited by 555

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

Tissue-Specific Regulation of Iron Metabolism and Heme Synthesis: Distinct Control Mechanisms in Erythroid Cells

Ponka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544

Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol

Richardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536

A cytosolic iron chaperone that delivers iron to ferritin

Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536

Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice

LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., et al. (2001) · Nature Genetics · doi:10.1038/84859 · Cited by 509

HIF-2α, but not HIF-1α, promotes iron absorption in mice

Mastrogiannaki, M., Matak, P., Keith, B., Simon, M. C., Vaulont, S., & Peyssonnaux, C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38499 · Cited by 502

Identification of the receptor scavenging hemopexin-heme complexes

Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473

Suppression of hepcidin during anemia requires erythropoietic activity

Pak, M., Lopez, M. A., Gabayan, V., Ganz, T., & Rivera, S. (2006) · Blood · doi:10.1182/blood-2006-06-028787 · Cited by 472

Regulation of iron acquisition and storage: consequences for iron-linked disorders

De Domenico, I., McVey Ward, D., & Kaplan, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2295 · Cited by 464

Acute postnatal ablation of Hif-2 α results in anemia

Gruber, M., Hu, C.-J., Johnson, R. S., Brown, E. J., Keith, B., & Simon, M. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608382104 · Cited by 457

Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway

Cohen, L. A., Gutierrez, L., Weiss, A., Leichtmann-Bardoogo, Y., Zhang, D.-L., Crooks, D. R., Sougrat, R., Morgenstern, A., Galy, B., Hentze, M. W., et al. (2010) · Blood · doi:10.1182/blood-2009-11-253815 · Cited by 452

Iron regulates phosphorylation of Smad1/5/8 and gene expression of Bmp6, Smad7, Id1, and Atoh8 in the mouse liver

Kautz, L., Meynard, D., Monnier, A., Darnaud, V., Bouvet, R., Wang, R.-H., Deng, C., Vaulont, S., Mosser, J., Coppin, H., et al. (2008) · Blood · doi:10.1182/blood-2008-03-143354 · Cited by 437

An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis

Salahudeen, A. A., Thompson, J. W., Ruiz, J. C., Ma, H.-W., Kinch, L. N., Li, Q., Grishin, N. V., & Bruick, R. K. (2009) · Science · doi:10.1126/science.1176326 · Cited by 432

Intestinal Hypoxia-Inducible Transcription Factors Are Essential for Iron Absorption following Iron Deficiency

Shah, Y. M., Matsubara, T., Ito, S., Yim, S.-H., & Gonzalez, F. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.012 · Cited by 431

Control of iron homeostasis by an iron-regulated ubiquitin ligase

Vashisht, A. A., Zumbrennen, K. B., Huang, X., Powers, D. N., Durazo, A., Sun, D., Bhaskaran, N., Persson, A., Uhlen, M., Sangfelt, O., et al. (2009) · Science · doi:10.1126/science.1176333 · Cited by 429

Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: Implications for regulation and cellular function

Hubert, N., & Hentze, M. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192423399 · Cited by 428

Cytokine-mediated regulation of iron transport in human monocytic cells

Ludwiczek, S., Aigner, E., Theurl, I., & Weiss, G. (2003) · Blood · doi:10.1182/blood-2002-08-2459 · Cited by 420

Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver

Gunshin, H., Fujiwara, Y., Custodio, A. O., DiRenzo, C., Robine, S., & Andrews, N. C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24356 · Cited by 419

Nramp2 is mutated in the anemic Belgrade (b) rat : evidence of a role for Nramp2 in endosomal iron transport

Flemming (1998) · Medical Entomology and Zoology · Cited by 412

Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis.

Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408

A Heme Export Protein Is Required for Red Blood Cell Differentiation and Iron Homeostasis

Keel, S. B., Doty, R. T., Yang, Z., Quigley, J. G., Chen, J., Knoblaugh, S., Kingsley, P. D., De Domenico, I., Vaughn, M. B., Kaplan, J., et al. (2008) · Science · doi:10.1126/science.1151133 · Cited by 404

TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens

Peyssonnaux, C., Zinkernagel, A. S., Datta, V., Lauth, X., Johnson, R. S., & Nizet, V. (2006) · Blood · doi:10.1182/blood-2005-06-2259 · Cited by 379

Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system

Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377

Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.

The Tübingen 2000 Screen Consortium, Wingert, R. A., Galloway, J. L., Barut, B., Foott, H., Fraenkel, P., Axe, J. L., Weber, G. J., Dooley, K., Davidson, A. J., et al. (2005) · Nature · doi:10.1038/nature03887 · Cited by 370

Scara5 Is a Ferritin Receptor Mediating Non-Transferrin Iron Delivery

Li, J. Y., Paragas, N., Ned, R. M., Qiu, A., Viltard, M., Leete, T., Drexler, I. R., Chen, X., Sanna‐Cherchi, S., Mohammed, F., et al. (2009) · Developmental Cell · doi:10.1016/j.devcel.2008.12.002 · Cited by 366

Regulation of Mitochondrial Iron Import through Differential Turnover of Mitoferrin 1 and Mitoferrin 2

Paradkar, P. N., Zumbrennen, K. B., Paw, B. H., Ward, D. M., & Kaplan, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01685-08 · Cited by 362

Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects

Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352

Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells

Tanno, T., Porayette, P., Sripichai, O., Noh, S.-J., Byrnes, C., Bhupatiraju, A., Lee, Y. T., Goodnough, J. B., Harandi, O., Ganz, T., et al. (2009) · Blood · doi:10.1182/blood-2008-12-195503 · Cited by 352

The endocytic receptor megalin binds the iron transporting neutrophil‐gelatinase‐associated lipocalin with high affinity and mediates its cellular uptake

Hvidberg, V., Jacobsen, C. B., Strong, R. K., Cowland, J. B., Moestrup, S. K., & Borregaard, N. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.031 · Cited by 351

Coordinated Regulation of Iron-Controlling Genes, H-Ferritin and IRP2 , by c-MYC

Wu, K., Polack, A., & Dalla‐Favera, R. (1999) · Science · doi:10.1126/science.283.5402.676 · Cited by 328

Interaction of the Hereditary Hemochromatosis Protein HFE with Transferrin Receptor 2 Is Required for Transferrin-Induced Hepcidin Expression

Gao, J., Chen, J., Kramer, M., Tsukamoto, H., Zhang, A.-S., & Enns, C. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.01.010 · Cited by 326

ER Stress Controls Iron Metabolism Through Induction of Hepcidin

Vecchi, C., Montosi, G., Zhang, K., Lamberti, I., Duncan, S. A., Kaufman, R. J., & Pietrangelo, A. (2009) · Science · doi:10.1126/science.1176639 · Cited by 310

Alcohol Metabolism-mediated Oxidative Stress Down-regulates Hepcidin Transcription and Leads to Increased Duodenal Iron Transporter Expression

Harrison-Findik, D. D., Schafer, D., Klein, E., Timchenko, N. A., Kulaksiz, H., Clemens, D. L., Fein, E., Andriopoulos, B., Pantopoulos, K., & Gollan, J. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602098200 · Cited by 308

Structure of Dual Function Iron Regulatory Protein 1 Complexed with Ferritin IRE-RNA

Walden, W. E., Selezneva, A. I., Dupuy, J., Volbeda, A., Fontecilla-Camps, J. C., Theil, E. C., & Volz, K. W. (2006) · Science · doi:10.1126/science.1133116 · Cited by 305

The centennial of the Fenton reaction

Koppenol, W. H. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90168-t · Cited by 302

A Mammalian Siderophore Synthesized by an Enzyme with a Bacterial Homolog Involved in Enterobactin Production

Devireddy, L. R., Hart, D. O., Goetz, D. H., & Green, M. R. (2010) · Cell · doi:10.1016/j.cell.2010.04.040 · Cited by 295

Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency

Sanchez, M., Galy, B., Muckenthaler, M. U., & Hentze, M. W. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1222 · Cited by 294

Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis

Tong, W.-H., & Rouault, T. A. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.003 · Cited by 294

Molecular control of vertebrate iron homeostasis by iron regulatory proteins

Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287

Cytosolic Monothiol Glutaredoxins Function in Intracellular Iron Sensing and Trafficking via Their Bound Iron-Sulfur Cluster

Mühlenhoff, U., Molik, S., Godoy, J. R., Uzarska, M. A., Richter, N., Seubert, A., Zhang, Y., Stubbe, J., Pierrel, F., Herrero, E., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.001 · Cited by 282

A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression

Zhang, D.-L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., & Rouault, T. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.006 · Cited by 281

Early Embryonic Lethality of H Ferritin Gene Deletion in Mice

Ferreira, C., Bucchini, D., Martin, M.-E., Levi, S., Arosio, P., Grandchamp, B., & Beaumont, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3021 · Cited by 275

Megalin-dependent cubilin-mediated endocytosis is a major pathway for the apical uptake of transferrin in polarized epithelia

Kozyraki, R., Fyfe, J. C., Verroust, P. J., Jacobsen, C. B., Dautry‐Varsat, A., Gburek, J., Willnow, T. E., Christensen, E., & Moestrup, S. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211291398 · Cited by 271

Hepatitis C virus–induced oxidative stress suppresses hepcidin expression through increased histone deacetylase activity

Miura, K., Taura, K., Kodama, Y., Schnabl, B., & Brenner, D. A. (2008) · Hepatology · doi:10.1002/hep.22486 · Cited by 270

The importance of non-transferrin bound iron in disorders of iron metabolism

Breuer, W., Hershko, C., & Cabantchik, Z. I. (2000) · Transfusion Science · doi:10.1016/s0955-3886(00)00087-4 · Cited by 268

Mammalian Tissue Oxygen Levels Modulate Iron-Regulatory Protein Activities in Vivo

Meyron‐Holtz, E. G., Ghosh, M. C., & Rouault, T. A. (2004) · Science · doi:10.1126/science.1103786 · Cited by 250

Human Iron−Sulfur Cluster Assembly, Cellular Iron Homeostasis, and Disease

Ye, H., & Rouault, T. A. (2010) · Biochemistry · doi:10.1021/bi1004798 · Cited by 247

Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts

Ye, H., Jeong, S. Y., Ghosh, M. C., Kovtunovych, G., Silvestri, L., Ortillo, D., Uchida, N., Tisdale, J. F., Camaschella, C., & Rouault, T. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40372 · Cited by 246

C/EBPα Regulates Hepatic Transcription of Hepcidin, an Antimicrobial Peptide and Regulator of Iron Metabolism

Courselaud, B., Pigeon, C., Inoue, Y., Inoue, J., Gonzalez, F. J., Leroyer, P., Gilot, D., Boudjema, K., Guguen-Guillouzo, C., Brissot, P., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202653200 · Cited by 245

Erythropoietin mediates hepcidin expression in hepatocytes through EPOR signaling and regulation of C/EBPα

Pinto, J. P., Ribeiro, S., Pontes, H., Thowfeequ, S., Tosh, D., Carvalho, F. D., & Porto, G. (2008) · Blood · doi:10.1182/blood-2007-08-106195 · Cited by 239

Ferroportin‐mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome

De Domenico, I., Vaughn, M. B., Li, L., Bagley, D., Musci, G., Ward, D. M., & Kaplan, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601409 · Cited by 235

Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2

Cooperman, S. S., Meyron-Holtz, E. G., Olivierre-Wilson, H., Ghosh, M. C., McConnell, J. P., & Rouault, T. A. (2005) · Blood · doi:10.1182/blood-2004-12-4703 · Cited by 235

Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria

Chen, W., Paradkar, P. N., Li, L., Pierce, E. L., Langer, N. B., Takahashi‐Makise, N., Hyde, B. B., Shirihai, O. S., Ward, D. M., Kaplan, J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904519106 · Cited by 230

The Chelatable Iron Pool in Living Cells: A Methodically Defined Quantity

Petrat, F. M., de GROOT, H., Sustmann, R., & Rauen, U. (2002) · Biological Chemistry · doi:10.1515/bc.2002.051 · Cited by 230

Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)

Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 224

TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis

Chen, T. T., Li, L., Chung, D.-H., Allen, C. D. C., Torti, S. V., Torti, F. M., Cyster, J. G., Chen, C.-Y., Brodsky, F. M., Niemi, E. C., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042433 · Cited by 219

Friedreich ataxia: the oxidative stress paradox

Seznec, H., Simon, D., Bouton, C., Reutenauer, L., Hertzog, A., Golik, P., Procaccio, V., Patel, M., Drapier, J.-C., Koenig, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi042 · Cited by 219

Discovery of Genes Essential for Heme Biosynthesis through Large-Scale Gene Expression Analysis

Nilsson, R., Schultz, I. J., Pierce, E. L., Soltis, K. A., Naranuntarat, A., Ward, D. M., Baughman, J. M., Paradkar, P. N., Kingsley, P. D., Culotta, V., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.012 · Cited by 217

Trafficking of Heme and Porphyrins in Metazoa

Severance, S., & Hamza, I. (2009) · Chemical Reviews · doi:10.1021/cr9001116 · Cited by 215

The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron–sulfur cluster biogenesis

Pondarré, C., Antiochos, B., Campagna, D. R., Clarke, S. L., Greer, E. L., Deck, K. M., McDonald, A. A., Han, A., Medlock, A. E., Kutok, J. L., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl012 · Cited by 212

H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties

Epsztejn, S., Glickstein, H., Picard, V., Slotki, I. N., Breuer, W., Beaumont, C., & Cabantchik, Z. I. (1999) · Blood · doi:10.1182/blood.v94.10.3593.422k26_3593_3603 · Cited by 209

Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia

Cazzola, M., Invernizzi, R., Bergamaschi, G., Levi, S., Corsi, B., Travaglino, E., Rolandi, V., Biasiotto, G., Drysdale, J., & Arosio, P. (2003) · Blood · doi:10.1182/blood-2002-07-2006 · Cited by 205

Managed care for viruses

Crystal, R. G. (1997) · Nature Medicine · doi:10.1038/nm0497-383 · Cited by 204

Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum

Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195

Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing

Zimmer, M., Ebert, B. L., Neil, C., Brenner, K., Papaioannou, I., Melas, A., Tolliday, N., Lamb, J., Pantopoulos, K., Golub, T., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.12.004 · Cited by 191

Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis

Netz, D. J. A., Stümpfig, M., Doré, C., Mühlenhoff, U., Pierik, A. J., & Lill, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.432 · Cited by 189

Selective Translational Control of the Alzheimer Amyloid Precursor Protein Transcript by Iron Regulatory Protein-1

Cho, H.-H., Cahill, C. M., Vanderburg, C. R., Scherzer, C. R., Wang, B., Huang, X., & Rogers, J. T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149161 · Cited by 188

The molecular defect in hypotransferrinemic mice

Trenor, C. C., Campagna, D. R., Sellers, V. M., Andrews, N. C., & Fleming, M. D. (2000) · Blood · doi:10.1182/blood.v96.3.1113 · Cited by 187

The 5′-untranslated region of Parkinson's disease α-synuclein messengerRNA contains a predicted iron responsive element

Friedlich, A. L., Tanzi, R. E., & Rogers, J. T. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4001937 · Cited by 184

Specific iron chelators determine the route of ferritin degradation

De Domenico, I., Ward, D. M., & Kaplan, J. (2009) · Blood · doi:10.1182/blood-2009-05-224188 · Cited by 176

Iron–sulfur protein maturation in human cells: evidence for a function of frataxin

Stehling, O., Elsässer, H.-P., Brückel, B., Mühlenhoff, U., & Lill, R. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh324 · Cited by 176

Intracellular labile iron

Breuer, W., Shvartsman, M., & Cabantchik, Z. I. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.010 · Cited by 175

The Cfd1–Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol

Netz, D. J. A., Pierik, A. J., Stümpfig, M., Mühlenhoff, U., & Lill, R. (2007) · Nature Chemical Biology · doi:10.1038/nchembio872 · Cited by 174

Regulation of Hepcidin and Iron-Overload Disease

Lee, P. L., & Beutler, E. (2009) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092205 · Cited by 174

Evolution of the iron-responsive element

Piccinelli, P., & Samuelsson, T. (2007) · RNA · doi:10.1261/rna.464807 · Cited by 168

Nramp1 promotes efficient macrophage recycling of iron following erythrophagocytosis in vivo

Soe-Lin, S., Apte, S. S., Andriopoulos, B., Andrews, M. C., Schranzhofer, M., Kahawita, T., Garcia-Santos, D., & Ponka, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900808106 · Cited by 167

ZRT/IRT-like Protein 14 (ZIP14) Promotes the Cellular Assimilation of Iron from Transferrin

Zhao, N., Gao, J., Enns, C. A., & Knutson, M. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143248 · Cited by 166

Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis

Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 165

Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation

Biederbick, A., Stehling, O., Rösser, R., Niggemeyer, B., Nakai, Y., Elsässer, H.-P., & Lill, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00112-06 · Cited by 164

A novel eukaryotic factor for cytosolic Fe–S cluster assembly

Roy, A., Solodovnikova, N., Nicholson, T., Antholine, W. E., & Walden, W. E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg455 · Cited by 160

Bacillus subtilis aconitase is an RNA-binding protein

Amaro, C. A., & Sonenshein, A. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10412 · Cited by 159

Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases

Tang, Y., & Guest, J. R. (1999) · Microbiology · doi:10.1099/00221287-145-11-3069 · Cited by 158

Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis

Shi, Y., Ghosh, M. C., Tong, W.-H., & Rouault, T. A. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp239 · Cited by 155

Crystal Structure of Human Iron Regulatory Protein 1 as Cytosolic Aconitase

Dupuy, J., Volbeda, A., Carpentier, P., Darnault, C., Moulis, J., & Fontecilla-Camps, J. C. (2006) · Structure · doi:10.1016/j.str.2005.09.009 · Cited by 150

Dre2, a Conserved Eukaryotic Fe/S Cluster Protein, Functions in Cytosolic Fe/S Protein Biogenesis

Zhang, Y., Lyver, E. R., Nakamaru‐Ogiso, E., Yoon, H., Amutha, B., Lee, D., Bi, E., Ohnishi, T., Daldal, F., Pain, D., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00642-08 · Cited by 148

Iron regulatory proteins secure mitochondrial iron sufficiency and function

Galy, B., Ferring-Appel, D., Sauer, S. W., Kaden, S., Lyoumi, S., Puy, H., Kölker, S., Gröne, H.-J., & Hentze, M. W. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.06.007 · Cited by 147

The aconitase family: three structural variations on a common theme

Gruer, M. J., Artymiuk, P. J., & Guest, J. R. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10069-4 · Cited by 144

Oxygen and Iron Regulation of Iron Regulatory Protein 2

Hanson, E. S., Rawlins, M. L., & Leibold, E. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302798200 · Cited by 140

Nature of nontransferrin‐bound iron

Hider, R. C. (2002) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2002.0320s1050.x · Cited by 139

Intestinal Ferritin H Is Required for an Accurate Control of Iron Absorption

Vanoaica, L., Darshan, D., Richman, L., Schümann, K., & Kühn, L. C. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.003 · Cited by 137

Localized Unfolding at the Junction of Three Ferritin Subunits

Takagi, H., Shi, D., Ha, Y., Allewell, N. M., & Theil, E. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18685 · Cited by 130

The Essential WD40 Protein Cia1 Is Involved in a Late Step of Cytosolic and Nuclear Iron-Sulfur Protein Assembly

Balk, J., Netz, D. J. A., Tepper, K., Pierik, A. J., & Lill, R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.10833-10841.2005 · Cited by 129

Nitrogen monoxide (NO)-mediated iron release from cells is linked to NO-induced glutathione efflux via multidrug resistance-associated protein 1

Watts, R., Hawkins, C. L., Ponka, P., & Richardson, D. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602515103 · Cited by 128

Iron Regulatory Proteins: From Molecular Mechanisms to Drug Development

Recalcati, S., Minotti, G., & Cairo, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2983 · Cited by 127

Brain iron homeostasis, the choroid plexus, and localization of iron transport proteins

Rouault, T. A., Zhang, D., & Jeong, S. Y. (2009) · Metabolic Brain Disease · doi:10.1007/s11011-009-9169-y · Cited by 126

Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development

Smith, S., Ghosh, M. C., Ollivierre, H., Tong, W. H., & Rouault, T. A. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.12.006 · Cited by 123

ROS mediate the hypoxic repression of the hepcidin gene by inhibiting C/EBPα and STAT-3

Choi, S.-O., Cho, Y.-S., Kim, H.-L., & Park, J.-W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.137 · Cited by 122

Cross-talk between the mitogen activated protein kinase and bone morphogenetic protein/hemojuvelin pathways is required for the induction of hepcidin by holotransferrin in primary mouse hepatocytes

Ramey, G., Deschemin, J., & Vaulont, S. (2009) · Haematologica · doi:10.3324/haematol.2008.003541 · Cited by 122

Assessment of Chelatable Mitochondrial Iron by Using Mitochondrion‐Selective Fluorescent Iron Indicators with Different Iron‐Binding Affinities

Rauen, U., Springer, A., Weisheit, D., Petrat, F., Korth, H., de Groot, H., & Sustmann, R. (2007) · ChemBioChem · doi:10.1002/cbic.200600311 · Cited by 121

Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit

Zhang, Y., Mikhael, M., Xu, D., Li, Y., Soe-Lin, S., Ning, B., Li, W., Nie, G., Zhao, Y., & Ponka, P. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3129 · Cited by 120

Mitochondrial ferritin

Levi, S., & Arosio, P. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.10.020 · Cited by 120

Iron-Refractory Iron Deficiency Anemia

Finberg, K. E. (2009) · Seminars in Hematology · doi:10.1053/j.seminhematol.2009.06.006 · Cited by 119

Modulation of Cellular Iron Metabolism by Hydrogen Peroxide

Caltagirone, A., Weiß, G., & Pantopoulos, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100245200 · Cited by 118

Iron-Mediated Degradation of IRP2, an Unexpected Pathway Involving a 2-Oxoglutarate-Dependent Oxygenase Activity

Wang, J., Chen, G., Muckenthaler, M. U., Galy, B., Hentze, M. W., & Pantopoulos, K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.954-965.2004 · Cited by 116

Iron Regulation and the Cell Cycle

Sánchez, M., Galy, B., Dandekar, T., Bengert, P., Vainshtein, Y., Stolte, J., Muckenthaler, M. U., & Hentze, M. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603876200 · Cited by 111

Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis

Stehling, O., Netz, D. J. A., Niggemeyer, B., Rösser, R., Eisenstein, R. S., Puccio, H. M., Pierik, A. J., & Lill, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00545-08 · Cited by 107

Diversity and distribution of hemerythrin-like proteins in prokaryotes

French, C. E., Bell, J. M., & Ward, F. B. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.01011.x · Cited by 103

ER Stress-Inducible Factor CHOP Affects the Expression of Hepcidin by Modulating C/EBPalpha Activity

Oliveira, S. J., Pinto, J. P., Picarote, G., Costa, V. M., Carvalho, F. D., Rangel, M., de Sousa, M. A. B., & de Almeida, S. F. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006618 · Cited by 101

Myeloperoxidase-derived Hypochlorous Acid Antagonizes the Oxidative Stress-mediated Activation of Iron Regulatory Protein 1

Mütze, S., Hebling, U., Stremmel, W., Wang, J., Arnhold, J., Pantopoulos, K., & Mueller, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307159200 · Cited by 101

Roles of the Mammalian Cytosolic Cysteine Desulfurase, ISCS, and Scaffold Protein, ISCU, in Iron-Sulfur Cluster Assembly

Li, K., Tong, W.-H., Hughes, R. M., & Rouault, T. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600582200 · Cited by 97

Iron‐responsive degradation of iron‐regulatory protein 1 does not require the Fe–S cluster

Clarke, S. L., Vasanthakumar, A., Anderson, S. A., Pondarré, C., Koh, C. M., Deck, K. M., Pitula, J. S., Epstein, C. J., Fleming, M. D., & Eisenstein, R. S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600954 · Cited by 97

Severity of Neurodegeneration Correlates with Compromise of Iron Metabolism in Mice with Iron Regulatory Protein Deficiencies

Smith, S., Cooperman, S. S., LaVaute, T. M., Tresser, N. J., Ghosh, M. C., Meyron‐Holtz, E. G., Land, W., Ollivierre, H., Jortner, B. S., Switzer, R., et al. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.006 · Cited by 94

Evidence for a lack of a direct transcriptional suppression of the iron regulatory peptide hepcidin by hypoxia-inducible factors

Volke, M., Gale, D. P., Maegdefrau, U., Schley, G., Klanke, B., Bosserhoff, A.-K., Maxwell, P. H., Eckardt, K.-U., & Warnecke, C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007875 · Cited by 93

Tempol-mediated activation of latent iron regulatory protein activity prevents symptoms of neurodegenerative disease in IRP2 knockout mice

Ghosh, M. C., Tong, W.-H., Zhang, D., Ollivierre, H., Singh, A., Krishna, M. C., Mitchell, J. B., & Rouault, T. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805361105 · Cited by 91

Remodeling the regulation of iron metabolism during erythroid differentiation to ensure efficient heme biosynthesis

Schranzhofer, M., Schifrer, M., Cabrera, J. A., Kopp, S., Chiba, P., Beug, H., & Müllner, E. W. (2006) · Blood · doi:10.1182/blood-2005-05-1809 · Cited by 89

S-Nitrosylation of IRP2 Regulates Its Stability via the Ubiquitin-Proteasome Pathway

Kim, S.-W., Wing, S. S., & Ponka, P. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.330-337.2004 · Cited by 87

Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage #

Darshan, D., Vanoaica, L., Richman, L., Beermann, F., & Kühn, L. C. (2009) · Hepatology · doi:10.1002/hep.23058 · Cited by 86

Iron feeding induces ferroportin 1 and hephaestin migration and interaction in rat duodenal epithelium

Yeh, K., YEH, M. K. Y., Mims, L., & Glass, J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90298.2008 · Cited by 85

Neuroferritinopathy: a neurodegenerative disorder associated with L-ferritin mutation

Levi, S., Cozzi, A., & Arosio, P. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.08.021 · Cited by 84

Oxidation-induced ferritin turnover in microglial cells: role of proteasome

Mehlhase, J., Sandig, G., Pantopoulos, K., & Grune, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.025 · Cited by 84

Iron transport and the kidney

Smith, C. P., & Thévenod, F. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.10.010 · Cited by 80

A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis

Song, D., & Lee, F. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708077200 · Cited by 79

Disruption of ferroportin 1 regulation causes dynamic alterations in iron homeostasis and erythropoiesis in polycythaemia mice

Mok, H., Jelinek, J., Pai, S., Cattanach, B. M., Prchal, J. T., Youssoufian, H., & Schumacher, A. (2004) · Development · doi:10.1242/dev.01081 · Cited by 73

Iron-Dependent Degradation of Apo-IRP1 by the Ubiquitin-Proteasome Pathway

Wang, J., Fillebeen, C., Chen, G., Biederbick, A., Lill, R., & Pantopoulos, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01111-06 · Cited by 72

Tumorigenic Properties of Iron Regulatory Protein 2 (IRP2) Mediated by Its Specific 73-Amino Acids Insert

Maffettone, C., Chen, G., Drozdov, I. A., Ouzounis, C. A., & Pantopoulos, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010163 · Cited by 68

A novel iron responsive element in the 3′UTR of human MRCKα

Čmejla, R., Petrák, J., & Čmejlová, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.155 · Cited by 67

Hypoxic up-regulation of erythroid 5-aminolevulinate synthase

Höfer, T., Wenger, R. H., Kramer, M. F., Ferreira, G. C., & Gassmann, M. (2002) · Blood · doi:10.1182/blood-2002-03-0773 · Cited by 66

Iron homeostasis in the brain: complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse

Galy, B., Hölter, S. M., Klopstock, T., Ferring–Appel, D., Becker, L., Kaden, S., Wurst, W., Gröne, H., & Hentze, M. W. (2006) · Nature Genetics · doi:10.1038/ng0906-967 · Cited by 62

Iron-Induced Expression of Bone Morphogenic Protein 6 in Intestinal Cells Is the Main Regulator of Hepatic Hepcidin Expression In Vivo

Arndt, S., Maegdefrau, U., Dorn, C., Schardt, K., Hellerbrand, C., & Bosserhoff, A. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.09.048 · Cited by 60

Identification of an Erythroid Active Element in the Transferrin Receptor Gene

Lok, C., & Ponka, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000944200 · Cited by 57

RNA Silencing of Mitochondrial m-Nfs1 Reduces Fe-S Enzyme Activity Both in Mitochondria and Cytosol of Mammalian Cells

Fosset, C., Chauveau, M.-J., Guillon, B., Canal, F., Drapier, J., & Bouton, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602979200 · Cited by 56

Overexpression of iron regulatory protein 1 suppresses growth of tumor xenografts

Chen, G., Fillebeen, C., Wang, J., & Pantopoulos, K. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl210 · Cited by 55

Iron and inflammation: cross-talk between pathways regulating hepcidin

Fleming, R. E. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0349-8 · Cited by 54

Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism

Ferring–Appel, D., Hentze, M. W., & Galy, B. (2008) · Blood · doi:10.1182/blood-2008-05-155093 · Cited by 53

Cysteine Oxidation Regulates the RNA-Binding Activity of Iron Regulatory Protein 2

由幸, 松., 直人, 篠., Romney, S. J., & Leibold, E. A. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00004-09 · Cited by 52

The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2

Bourdon, E., Kang, D., Ghosh, M. C., Drake, S. K., Wey, J. S., Levine, R. L., & Rouault, T. A. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00161-x · Cited by 51

Conditional Derepression of Ferritin Synthesis in Cells Expressing a Constitutive IRP1 Mutant

Wang, J., & Pantopoulos, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4638-4651.2002 · Cited by 49

Chronic expression of H-ferritin in dopaminergic midbrain neurons results in an age-related expansion of the labile iron pool and subsequent neurodegeneration: implications for Parkinson's disease

Kaur, D., Rajagopalan, S., & Andersen, J. K. (2009) · Brain Research · doi:10.1016/j.brainres.2009.08.043 · Cited by 48

Sustained Hydrogen Peroxide Induces Iron Uptake by Transferrin Receptor-1 Independent of the Iron Regulatory Protein/Iron-responsive Element Network

Andriopoulos, B., Hegedüsch, S., Mangin, J., Riedel, H.-D., Hebling, U., Wang, J., Pantopoulos, K., & Mueller, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702463200 · Cited by 48

A Phosphomimetic Mutation at Ser-138 Renders Iron Regulatory Protein 1 Sensitive to Iron-Dependent Degradation

Fillebeen, C., Chahine, D., Caltagirone, A., Segal, P., & Pantopoulos, K. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.19.6973-6981.2003 · Cited by 48

Redox control of iron regulatory proteins

Fillebeen, C., & Pantopoulos, K. (2002) · Redox Report · doi:10.1179/135100002125000136 · Cited by 44

Recycling of RNA Binding Iron Regulatory Protein 1 into an Aconitase after Nitric Oxide Removal Depends on Mitochondrial ATP

Bouton, C., Chauveau, M.-J., Lazereg, S., & Drapier, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203276200 · Cited by 44

Pathogenesis of Hyperferritinemia Cataract Syndrome

Roetto, A., Bosio, S., Gramaglia, E., Barilaro, M. R., Zecchina, G., & Camaschella, C. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0590 · Cited by 41

Maintaining Mammalian Iron and Oxygen Homeostasis

Salahudeen, A. A., & Bruick, R. K. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05038.x · Cited by 41

The Connectivity Map Links Iron Regulatory Protein-1–Mediated Inhibition of Hypoxia-Inducible Factor-2a Translation to the Anti-inflammatory 15-deoxy-Δ12,14-Prostaglandin J2

Zimmer, M., Lamb, J., Ebert, B. L., Lynch, M. C., Neil, C. R., Schmidt, E. V., Golub, T. R., & Iliopoulos, O. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2877 · Cited by 40

Activated macrophages induce hepcidin expression in HuH7 hepatoma cells

Matak, P., Chaston, T. B., Chung, B., Srai, S. K., McKie, A. T., & Sharp, P. (2009) · Haematologica · doi:10.3324/haematol.2008.003400 · Cited by 40

Nitric Oxide Inhibits the Degradation of IRP2

Wang, J., Chen, G., & Pantopoulos, K. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1347-1353.2005 · Cited by 38

Sodium Nitroprusside Promotes IRP2 Degradation via an Increase in Intracellular Iron and in the Absence of S Nitrosylation at C178

Wang, J., Fillebeen, C., Chen, G., Andriopoulos, B., & Pantopoulos, K. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1948-1954.2006 · Cited by 34

Evidence That Phosphorylation of Iron Regulatory Protein 1 at Serine 138 Destabilizes the [4Fe-4S] Cluster in Cytosolic Aconitase by Enhancing 4Fe-3Fe Cycling

Deck, K. M., Vasanthakumar, A., Anderson, S. A., Goforth, J. B., Kennedy, M. C., Antholine, W. E., & Eisenstein, R. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807717200 · Cited by 33

IRP1-independent alterations of cardiac iron metabolism in doxorubicin-treated mice

Corna, G., Galy, B., Hentze, M. W., & Cairo, G. (2006) · Journal of Molecular Medicine · doi:10.1007/s00109-006-0068-y · Cited by 32

Toll-like receptors mediate induction of hepcidin in mice infected with Borrelia burgdorferi

Koening, C. L., Miller, J. C., Nelson, J. M., Ward, D. M., Kushner, J. P., Bockenstedt, L. K., Weis, J. J., Kaplan, J., & Domenico, I. D. (2009) · Blood · doi:10.1182/blood-2009-03-209577 · Cited by 32

IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities

Fillebeen, C., Caltagirone, A., Martelli, A., Moulis, J., & Pantopoulos, K. (2005) · Biochemical Journal · doi:10.1042/bj20041623 · Cited by 30

Selective inhibition of the citrate-to-isocitrate reaction of cytosolic aconitase by phosphomimetic mutation of serine-711

Pitula, J. S., Deck, K. M., Clarke, S. L., Anderson, S. A., Vasanthakumar, A., & Eisenstein, R. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404308101 · Cited by 30

Redox control of iron regulatory protein 2 stability

Hausmann, A., Lee, J., & Pantopoulos, K. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.036 · Cited by 29

Systematic genomic screening and analysis of mRNA in untranslated regions and mRNA precursors: combining experimental and computational approaches.

Dandekar, T., Beyer, K., Bork, P., Kenealy, M.-R., Pantopoulos, K., Hentze, M. W., Sonntag-Buck, V., Flouriot, G., Gannon, F., & Schreiber, S. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.3.271 · Cited by 26

Human iron regulatory protein 2 is easily cleaved in its specific domain: consequences for the haem binding properties of the protein

Dycke, C., Bougault, C., Gaillard, J., Andrieu, J., Pantopoulos, K., & Moulis, J. (2007) · Biochemical Journal · doi:10.1042/bj20070983 · Cited by 25

Subcellular localization of iron regulatory proteins to Golgi and ER membranes

Patton, S. M., Piñero, D. J., Surguladze, N., Beard, J., & Connor, J. R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02570 · Cited by 23

Iron-independent Phosphorylation of Iron Regulatory Protein 2 Regulates Ferritin during the Cell Cycle

Wallander, M. L., Zumbrennen‐Bullough, K. B., Rodansky, E. S., Romney, S. J., & Leibold, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803005200 · Cited by 22

Iron-dependent degradation of IRP2 requires its C-terminal region and IRP structural integrity

Wang, J., Chen, G., Lee, J., & Pantopoulos, K. (2008) · BMC Molecular Biology · doi:10.1186/1471-2199-9-15 · Cited by 18

Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling

Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373

Review on iron and its importance for human health.

Abbaspour, N., Hurrell, R. F., & Kelishadi, R. (2014) · Europe PMC (PubMed Central) · Cited by 1,886

The role of iron in brain ageing and neurodegenerative disorders

Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819

A Review of Micronutrients and the Immune System–Working in Harmony to Reduce the Risk of Infection

Gombart, A. F., Pierre, A., & Maggini, S. (2020) · Nutrients · doi:10.3390/nu12010236 · Cited by 1,358

Redox- and non-redox-metal-induced formation of free radicals and their role in human disease

Valko, M., Jomová, K., Rhodes, C. J., Kuča, K., & Musílek, K. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1579-5 · Cited by 1,062

The Cellular Physiology of Iron

Anderson, G. J., & Vulpe, C. D. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-462-9_1 · Cited by 5

The transferrin receptor: a key function in iron metabolism.

Kühn, L. C. (1989) · PubMed · Cited by 21

Cellular Iron Metabolism and Regulation

Gao, G., Li, J., Zhang, Y., & Chang, Y.-Z. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_2 · Cited by 322

Effects of zinc deficiency on immune functions

Prasad, A. S. (2000) · The Journal of Trace Elements in Experimental Medicine · doi:10.1002/(sici)1520-670x(2000)13:1 · Cited by 87

Iron Metabolism and the IRE/IRP Regulatory System: An Update

Pantopoulos, K. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.001 · Cited by 505