Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease

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 · see citing works

The ferritins: molecular properties, iron storage function and cellular regulation

Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667 · see citing works

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 · see citing works

Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy

Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084 · see citing works

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 · see citing works

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 · see citing works

Function and biogenesis of iron-sulphur proteins

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

An iron-regulated ferric reductase associated with the absorption of dietary iron

McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., et al. (2001) · Science · doi:10.1126/science.1057206 · Cited by 1,101 · see citing works

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 · see citing works

The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation

Bryan, H. K., Olayanju, A., Goldring, C. E., & Park, B. K. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.11.016 · Cited by 1,026 · see citing works

Mineralization in ferritin: an efficient means of iron storage

Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815 · see citing works

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 · see citing works

Frataxin is Reduced in Friedreich Ataxia Patients and is Associated with Mitochondrial Membranes

Campuzano, V., Montermini, L., Lutz, Y., Cova, L., Hindelang, C., Jiralerspong, S., Trottier, Y., Kish, S. J., Faucheux, B. A., Trouillas, P., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.11.1771 · Cited by 739 · see citing works

Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits

Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., & Koenig, M. (2001) · Nature Genetics · doi:10.1038/84818 · Cited by 738 · 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

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 · see citing works

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins

Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699 · see citing works

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 · see citing works

Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases

Lill, R., & Mühlenhoff, U. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162653 · Cited by 595 · see citing works

A Disulfide Relay System in the Intermembrane Space of Mitochondria that Mediates Protein Import

Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., & Herrmann, J. M. (2005) · Cell · doi:10.1016/j.cell.2005.04.011 · Cited by 557 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

The role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism

Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 501 · see citing works

Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin

Koutníková, H., Campuzano, V., Foury, F., Dollé, P., Cazzalini, O., & Koenig, M. (1997) · Nature Genetics · doi:10.1038/ng0897-345 · Cited by 473 · see citing works

Heme in pathophysiology: a matter of scavenging, metabolism and trafficking across cell membranes

Chiabrando, D., Vinchi, F., Fiorito, V., Mercurio, S., & Tolosano, E. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00061 · Cited by 455 · see citing works

Friedreich's ataxia: Pathology, pathogenesis, and molecular genetics

Koeppen, A. H. (2011) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2011.01.010 · Cited by 447 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis

Sheftel, A. D., Stehling, O., Pierik, A. J., Elsässer, H.-P., Mühlenhoff, U., Webert, H., Hobler, A., Hannemann, F., Bernhardt, R., & Lill, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004250107 · Cited by 406 · see citing works

Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: Protection against reactive oxygen and nitrogen species‐induced cell injury

Zhu, H., Itoh, K., Yamamoto, M. P., Zweier, J. L., & Li, Y. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.04.058 · Cited by 394 · see citing works

Iron–sulfur cluster biogenesis and human disease

Rouault, T. A., & Tong, W. H. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.05.008 · Cited by 387 · see citing works

Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation

Cossee, M. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.8.1219 · Cited by 377 · see citing works

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 · see citing works

Iron−Sulfur Cluster Biosynthesis. Characterization of Frataxin as an Iron Donor for Assembly of [2Fe-2S] Clusters in ISU-Type Proteins

Yoon, T., & Cowan, J. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja027967i · Cited by 353 · see citing works

Mitochondria as a Therapeutic Target in Heart Failure

Bayeva, M., Gheorghiade, M., & Ardehali, H. (2012) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2012.08.1021 · Cited by 336 · see citing works

Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease

Rouault, T. A. (2012) · Disease Models & Mechanisms · doi:10.1242/dmm.009019 · Cited by 332 · see citing works

Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage

Arosio, P., & Levi, S. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.02.005 · Cited by 320 · see citing works

Lysosomes in iron metabolism, ageing and apoptosis

Kurz, T., Terman, A., Gustafsson, B., & Brunk, U. T. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0394-y · Cited by 302 · see citing works

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 · see citing works

Iron Regulates the Intracellular Degradation of Iron Regulatory Protein 2 by the Proteasome

Guo, B., Phillips, J. D., Yu, Y., & Leibold, E. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21645 · Cited by 287 · see citing works

Human Frataxin Is an Allosteric Switch That Activates the Fe−S Cluster Biosynthetic Complex

Tsai, C.-L., & Barondeau, D. P. (2010) · Biochemistry · doi:10.1021/bi1013062 · Cited by 282 · see citing works

Frataxin-mediated Iron Delivery to Ferrochelatase in the Final Step of Heme Biosynthesis

Yoon, T., & Cowan, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400107200 · Cited by 281 · see citing works

Mutations in Iron-Sulfur Cluster Scaffold Genes NFU1 and BOLA3 Cause a Fatal Deficiency of Multiple Respiratory Chain and 2-Oxoacid Dehydrogenase Enzymes

Cameron, J. M., Janer, A., Levandovskiy, V., MacKay, N., Rouault, T. A., Tong, W.-H., Ogilvie, I. M., Shoubridge, E. A., & Robinson, B. H. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.08.011 · Cited by 278 · see citing works

Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions

Shi, R., Proteau, A., Villarroya, M., Moukadiri, I., Zhang, L., Trempe, J., Matte, A., Armengod, M. ‐., & Cygler, M. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000354 · Cited by 270 · see citing works

Direct interorganellar transfer of iron from endosome to mitochondrion

Sheftel, A. D., Zhang, A., Brown, C. M., Shirihai, O. S., & Ponka, P. (2007) · Blood · doi:10.1182/blood-2007-01-068148 · Cited by 266 · see citing works

The active role of vitamin C in mammalian iron metabolism: Much more than just enhanced iron absorption!

Lane, D. J. R., & Richardson, D. R. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.007 · Cited by 264 · see citing works

Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS

Adinolfi, S., Iannuzzi, C., Prischi, F., Pastore, C., Iametti, S., Martin, S. R., Bonomi, F., & Pastore, A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1579 · Cited by 256 · see citing works

Nrf1 and Nrf2 Regulate Rat Glutamate-Cysteine Ligase Catalytic Subunit Transcription Indirectly via NF-κB and AP-1

Yang, H., Magilnick, N., Lee, C., Kalmaz, D. M., Ou, X., Chan, J. Y., & Lu, S. C.-L. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5933-5946.2005 · Cited by 250 · see citing works

Physiologic implications of metal-ion transport by ZIP14 and ZIP8

Jenkitkasemwong, S., Wang, C., Mackenzie, B., & Knutson, M. D. (2012) · BioMetals · doi:10.1007/s10534-012-9526-x · Cited by 245 · see citing works

The pathogenesis of Friedreich ataxia and the structure and function of frataxin

Pandolfo, M., & Pastore, A. (2009) · Journal of Neurology · doi:10.1007/s00415-009-1003-2 · Cited by 242 · see citing works

The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria

Adam, A. C., Bornhövd, C., Prokisch, H., Neupert, W., & Hell, K. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600905 · Cited by 240 · see citing works

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 239 · see citing works

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

Ye, H., & Rouault, T. A. (2010) · Biochemistry · doi:10.1021/bi1004798 · Cited by 238 · see citing works

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 220 · see citing works

Impaired Nuclear Nrf2 Translocation Undermines the Oxidative Stress Response in Friedreich Ataxia

Paupe, V., Dassa, E. P., Gonçalves, S., Auchère, F., Lönn, M. E., Holmgren, A., & Rustin, P. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004253 · Cited by 218 · see citing works

Mammalian Iron Homeostasis in Health and Disease: Uptake, Storage, Transport, and Molecular Mechanisms of Action

Lawen, A., & Lane, D. J. R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4271 · Cited by 217 · see citing works

Iron –sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery

Maio, N., & Rouault, T. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.009 · Cited by 215 · see citing works

The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation

Sheftel, A. D., Wilbrecht, C., Stehling, O., Niggemeyer, B., Elsässer, H., Mühlenhoff, U., & Lill, R. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0772 · Cited by 213 · see citing works

Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant

Huang, M. L.-H., Becker, E. M., Whitnall, M., Rahmanto, Y. S., Ponka, P., & Richardson, D. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906784106 · Cited by 212 · see citing works

Splice Mutation in the Iron-Sulfur Cluster Scaffold Protein ISCU Causes Myopathy with Exercise Intolerance

Mochel, F., Knight, M. A., Tong, W.-H., Hernandez, D. G., Ayyad, K., Taivassalo, T., Andersen, P. M., Singleton, A., Rouault, T. A., Fischbeck, K. H., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2007.12.012 · Cited by 208 · see citing works

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 · see citing works

Activation of the HIF Prolyl Hydroxylase by the Iron Chaperones PCBP1 and PCBP2

Nandal, A., Ruiz, J. C., Subramanian, P., Ghimire-Rijal, S., Sinnamon, R. A., Stemmler, T. L., Bruick, R. K., & Philpott, C. C. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.015 · Cited by 204 · see citing works

The diverse roles of J-proteins, the obligate Hsp70 co-chaperone

Craig, E. A., Huang, P., Aron, R., & Andrew, A. J. (2006) · Springer eBooks · doi:10.1007/s10254-005-0001-0 · Cited by 198 · see citing works

Out of Balance—Systemic Iron Homeostasis in Iron-Related Disorders

Steinbicker, A. U., & Muckenthaler, M. U. (2013) · Nutrients · doi:10.3390/nu5083034 · Cited by 196 · see citing works

Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis

Shi, Y., Ghosh, M. C., Kovtunovych, G., Crooks, D. R., & Rouault, T. A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.11.002 · Cited by 194 · see citing works

A Specific Role of the Yeast Mitochondrial Carriers Mrs3/4p in Mitochondrial Iron Acquisition under Iron-limiting Conditions

Mühlenhoff, U., Stadler, J. A., Richhardt, N., Seubert, A., Eickhorst, T., Schweyen, R. J., Lill, R., & Wiesenberger, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307847200 · Cited by 193 · see citing works

Each Member of the Poly-r(C)-binding Protein 1 (PCBP) Family Exhibits Iron Chaperone Activity toward Ferritin

Leidgens, S., Zumbrennen‐Bullough, K. B., Shi, H., Li, F., Shakoury‐Elizeh, M., Yabe‐Wada, T., Subramanian, P., Hsu, E., Natarajan, N., Nandal, A., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.460253 · Cited by 193 · see citing works

VDAC1: from structure to cancer therapy

Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 192 · see citing works

Frataxin: a protein in search for a function

Pastore, A., & Puccio, H. M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12220 · Cited by 191 · see citing works

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 · see citing works

Molecular Chaperones HscA/Ssq1 and HscB/Jac1 and Their Roles in Iron-Sulfur Protein Maturation

Vickery, L. E., & Cupp‐Vickery, J. R. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701322298 · Cited by 188 · see citing works

Maturation of cytosolic and nuclear iron–sulfur proteins

Netz, D. J. A., Mascarenhas, J., Stehling, O., Pierik, A. J., & Lill, R. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.11.005 · Cited by 184 · see citing works

Structural bases for the interaction of frataxin with the central components of iron–sulphur cluster assembly

Prischi, F., Konarev, P. V., Iannuzzi, C., Pastore, C., Adinolfi, S., Martin, S. R., Svergun, D. I., & Pastore, A. (2010) · Nature Communications · doi:10.1038/ncomms1097 · Cited by 184 · see citing works

Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols

Parent, A., Elduque, X., Cornu, D., Belot, L., Caër, J. L., Grandas, A., Tolédano, M. B., & D’Autréaux, B. (2015) · Nature Communications · doi:10.1038/ncomms6686 · Cited by 176 · see citing works

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 · see citing works

Deletion of the Mitochondrial Carrier Genes MRS3 andMRS4 Suppresses Mitochondrial Iron Accumulation in a Yeast Frataxin-deficient Strain

Foury, F., & Roganti, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111789200 · Cited by 171 · see citing works

Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur Proteins

Stehling, O., Mascarenhas, J., Vashisht, A. A., Sheftel, A. D., Niggemeyer, B., Rösser, R., Pierik, A. J., Wohlschlegel, J. A., & Lill, R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.06.015 · Cited by 170 · see citing works

Mitochondrial Ferritin Expression in Adult Mouse Tissues

Santambrogio, P., Biasiotto, G., Sanvito, F., Olivieri, S., Arosio, P., & Levi, S. (2007) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.7a7273.2007 · Cited by 169 · see citing works

Hypoxia‐mediated biological control

Cassavaugh, J. M., & Lounsbury, K. M. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22956 · Cited by 169 · see citing works

Cochaperone Binding to LYR Motifs Confers Specificity of Iron Sulfur Cluster Delivery

Maio, N., Singh, A., Uhrigshardt, H., Saxena, N., Tong, W.-H., & Rouault, T. A. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.015 · Cited by 167 · see citing works

Frataxin Deficiency Leads to Defects in Expression of Antioxidants and Nrf2 Expression in Dorsal Root Ganglia of the Friedreich's Ataxia YG8R Mouse Model

Shan, Y., Schoenfeld, R. A., Hayashi, G., Napoli, E., Akiyama, T., Carstens, M. I., Carstens, E. E., Pook, M. A., & Cortopassi, G. A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4537 · Cited by 159 · see citing works

Human Frataxin Activates Fe–S Cluster Biosynthesis by Facilitating Sulfur Transfer Chemistry

Bridwell‐Rabb, J., Fox, N. G., Tsai, C.-L., Winn, A. M., & Barondeau, D. P. (2014) · Biochemistry · doi:10.1021/bi500532e · Cited by 158 · see citing works

Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis

Chen, W., Dailey, H. A., & Paw, B. H. (2010) · Blood · doi:10.1182/blood-2009-12-259614 · Cited by 157 · see citing works

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 · see citing works

Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury

Uchiyama, A., Kim, J.-S., Kon, K., Jaeschke, H., Ikejima, K., Watanabe, S., & Lemasters, J. J. (2008) · Hepatology · doi:10.1002/hep.22498 · Cited by 154 · see citing works

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 · see citing works

Monothiol CGFS Glutaredoxins and BolA-like Proteins: [2Fe-2S] Binding Partners in Iron Homeostasis

Li, H., & Outten, C. E. (2012) · Biochemistry · doi:10.1021/bi300393z · Cited by 148 · see citing works

Frataxin and Mitochondrial FeS Cluster Biogenesis

Stemmler, T. L., Lesuisse, E., Pain, D., & Dancis, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.118679 · Cited by 145 · see citing works

Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis

Pondarré, C., Campagna, D. R., Antiochos, B., Sikorski, L., Mulhern, H. L., & Fleming, M. D. (2006) · Blood · doi:10.1182/blood-2006-04-015768 · Cited by 140 · see citing works

Iron chaperones PCBP1 and PCBP2 mediate the metallation of the dinuclear iron enzyme deoxyhypusine hydroxylase

Frey, A. G., Nandal, A., Park, J. H., Smith, P. M., Yabe‐Wada, T., Ryu, M., Ghosh, M. C., Lee, J., Rouault, T. A., Park, M. H., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402732111 · Cited by 136 · see citing works

Chaperone protein involved in transmembrane transport of iron

Yanatori, I., Yasui, Y., Tabuchi, M., & Kishi, F. (2014) · Biochemical Journal · doi:10.1042/bj20140225 · Cited by 134 · see citing works

Lysosome-related Organelles as Mediators of Metal Homeostasis

Blaby, C., & Merchant, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.592618 · Cited by 134 · see citing works

Poly(C)-binding proteins as transcriptional regulators of gene expression

Choi, H. S., Hwang, C. K., Song, K. Y., Law, P., Wei, L., & Loh, H. H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.136 · Cited by 131 · see citing works

The MCK mouse heart model of Friedreich's ataxia: Alterations in iron-regulated proteins and cardiac hypertrophy are limited by iron chelation

Whitnall, M., Rahmanto, Y. S., Šuťák, R., Xu, X., Becker, E., Mikhael, M., Ponka, P., & Richardson, D. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804261105 · Cited by 122 · see citing works

Assembly of Fe/S proteins in bacterial systems

Blanc, B., Gerez, C., & de Choudens, S. O. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.009 · Cited by 118 · see citing works

The LYR Factors SDHAF1 and SDHAF3 Mediate Maturation of the Iron-Sulfur Subunit of Succinate Dehydrogenase

Na, U., Yu, W., Cox, J. E., Bricker, D. K., Brockmann, K., Rutter, J. P., Thummel, C. S., & Winge, D. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.05.014 · Cited by 114 · see citing works

Cytosolic Iron-Sulfur Cluster Assembly (CIA) System: Factors, Mechanism, and Relevance to Cellular Iron Regulation

Sharma, A. K., Pallesen, L. J., Spang, R. J., & Walden, W. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.122218 · Cited by 107 · see citing works

Coming into View: Eukaryotic Iron Chaperones and Intracellular Iron Delivery

Philpott, C. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.326876 · Cited by 106 · see citing works

Mitochondrial Mayhem: The Mitochondrion as a Modulator of Iron Metabolism and Its Role in Disease

Huang, M. L.-H., Lane, D. J. R., & Richardson, D. R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3921 · Cited by 103 · see citing works

Frataxin deficiency alters heme pathway transcripts and decreases mitochondrial heme metabolites in mammalian cells

Schoenfeld, R. A., Napoli, E., Wong, A., Zhan, S. S., Reutenauer, L., Morin, D., Buckpitt, A. R., Taroni, F., Lönnerdal, B., Ristow, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi393 · Cited by 103 · see citing works

Two routes of iron accumulation in astrocytes: ascorbate-dependent ferrous iron uptake via the divalent metal transporter (DMT1) plus an independent route for ferric iron

Lane, D. J. R., Robinson, S. R., Czerwinska, H., Bishop, G. M., & Lawen, A. (2010) · Biochemical Journal · doi:10.1042/bj20101317 · Cited by 101 · see citing works

Effector Role Reversal during Evolution: The Case of Frataxin in Fe–S Cluster Biosynthesis

Bridwell‐Rabb, J., Iannuzzi, C., Pastore, A., & Barondeau, D. P. (2012) · Biochemistry · doi:10.1021/bi201628j · Cited by 96 · see citing works

Evolution of Mitochondrial Chaperones Utilized in Fe-S Cluster Biogenesis

Schilke, B. A., Williams, B. L., Knieszner, H., Pukszta, S., D’Silva, P., Craig, E. A., & Marszałek, J. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.069 · Cited by 96 · see citing works

Frataxin Directly Stimulates Mitochondrial Cysteine Desulfurase by Exposing Substrate-binding Sites, and a Mutant Fe-S Cluster Scaffold Protein with Frataxin-bypassing Ability Acts Similarly

Pandey, A., Gordon, D. M., Pain, J., Stemmler, T. L., Dancis, A., & Pain, D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525857 · Cited by 94 · see citing works

Involvement of ABC7 in the biosynthesis of heme in erythroid cells: interaction of ABC7 with ferrochelatase

Taketani, S., Kakimoto, K., Ueta, H., Masaki, R., & Furukawa, T. (2003) · Blood · doi:10.1182/blood-2002-04-1212 · Cited by 94 · see citing works

Binding of Yeast Frataxin to the Scaffold for Fe-S Cluster Biogenesis, Isu

Wang, T., & Craig, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800399200 · Cited by 94 · see citing works

Special delivery: distributing iron in the cytosol of mammalian cells

Philpott, C. C., & Ryu, M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00173 · Cited by 93 · see citing works

Frataxin Deficiency Leads to Reduced Expression and Impaired Translocation of NF-E2-Related Factor (Nrf2) in Cultured Motor Neurons

Doria, V., Petrini, S., Travaglini, L., Priori, C., Piermarini, E., Petrillo, S., Carletti, B., Bertini, E., & Piemonte, F. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14047853 · Cited by 92 · see citing works

Identification of nonferritin mitochondrial iron deposits in a mouse model of Friedreich ataxia

Whitnall, M., Rahmanto, Y. S., Huang, M. L. H., Saletta, F., Lok, H. C., Gutiérrez, L., Lázaro, F. J., Fleming, A. J., Pierre, T. G. S., Mikhael, M., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215349109 · Cited by 91 · see citing works

Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron–sulfur cluster biogenesis

Uhrigshardt, H., Singh, A., Kovtunovych, G., Ghosh, M. C., & Rouault, T. A. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq301 · Cited by 91 · see citing works

Mitochondrial ABC transporters function: The role of ABCB10 (ABC-me) as a novel player in cellular handling of reactive oxygen species

Liesa, M., Qiu, W., & Shirihai, O. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.07.013 · Cited by 87 · see citing works

Iron Regulatory Protein 1 Sustains Mitochondrial Iron Loading and Function in Frataxin Deficiency

Martelli, A., Schmucker, S., Reutenauer, L., Mathieu, J. R. R., Peyssonnaux, C., Karim, Z., Puy, H., Galy, B., Hentze, M. W., & Puccio, H. M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.01.010 · Cited by 82 · see citing works

Acidic residues of yeast frataxin have an essential role in Fe–S cluster assembly

Foury, F., Pastore, A., & Trincal, M. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400881 · Cited by 81 · see citing works

Iron Homeostasis and Its Interaction with Prolyl Hydroxylases

Mole, D. R. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2790 · Cited by 80 · see citing works

Normal and Friedreich Ataxia Cells Express Different Isoforms of Frataxin with Complementary Roles in Iron-Sulfur Cluster Assembly

Gakh, O., Bedekovics, T., Duncan, S. F., Smith, D. Y., Berkholz, D. S., & Isaya, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145144 · Cited by 76 · see citing works

Excess Capacity of the Iron Regulatory Protein System

Wang, W., Di, X., D'Agostino, R. B., Torti, S. V., & Torti, F. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703167200 · Cited by 75 · see citing works

Human frataxin: iron and ferrochelatase binding surface

Bencze, K. Z., Yoon, T., Millán‐Pacheco, C., Bradley, P. B., Pastor, N., Cowan, J. A., & Stemmler, T. L. (2007) · Chemical Communications · doi:10.1039/b703195e · Cited by 75 · see citing works

The LYR Protein Mzm1 Functions in the Insertion of the Rieske Fe/S Protein in Yeast Mitochondria

Atkinson, A. E., Smith, P. M., Fox, J. L., Cui, T.-Z., Khalimonchuk, O., & Winge, D. R. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05673-11 · Cited by 75 · see citing works

Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization

Becker, E., Greer, J. M., Ponka, P., & Richardson, D. R. (2002) · Blood · doi:10.1182/blood.v99.10.3813 · Cited by 74 · see citing works

Structure–Function Analysis of Friedreich’s Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe–S Assembly Complex

Bridwell‐Rabb, J., Winn, A. M., & Barondeau, D. P. (2011) · Biochemistry · doi:10.1021/bi200895k · Cited by 72 · see citing works

Mortalin – a multipotent chaperone regulating cellular processes ranging from viral infection to neurodegeneration

Flachbartova, Z., & Kováčech, B. (2013) · Acta Virologica · doi:10.4149/av_2013_01_3 · Cited by 71 · see citing works

The diverse roles of J-proteins, the obligate Hsp70 co-chaperone

Craig, E. A., Huang, P., Aron, R., & Andrew, A. (2006) · Springer eBooks · doi:10.1007/s10254-005-0001-8 · Cited by 69 · see citing works

Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin

Condò, I., Malisan, F., Guccini, I., Serio, D., Rufini, A., & Testi, R. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddp592 · Cited by 68 · see citing works

Mitoferrin-2-dependent Mitochondrial Iron Uptake Sensitizes Human Head and Neck Squamous Carcinoma Cells to Photodynamic Therapy

Hung, H., Schwartz, J. M., Maldonado, E. N., Lemasters, J. J., & Nieminen, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422667 · Cited by 67 · see citing works

Evidence for mitochondrial localization of divalent metal transporter 1 (DMT1)

Wolff, N. A., Ghio, A. J., Garrick, L. M., Garrick, M. D., Zhao, L., Fenton, R. A., & Thévenod, F. (2014) · The FASEB Journal · doi:10.1096/fj.13-240564 · Cited by 66 · see citing works

Abcb10 Role in Heme Biosynthesis In Vivo: Abcb10 Knockout in Mice Causes Anemia with Protoporphyrin IX and Iron Accumulation

Yamamoto, M., Arimura, H., Fukushige, T., Minami, K., Nishizawa, Y., Tanimoto, A., Kanekura, T., Nakagawa, M., Akiyama, S., & Furukawa, T. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00865-13 · Cited by 65 · see citing works

Transferrin iron uptake is stimulated by ascorbate via an intracellular reductive mechanism

Lane, D. J. R., Chikhani, S., Richardson, V., & Richardson, D. R. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.010 · Cited by 63 · see citing works

Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe–S cluster synthesis

Pandey, A., Ramesh, G., Yoon, H., Dancis, A., & Pain, D. (2012) · Biochemical Journal · doi:10.1042/bj20120951 · Cited by 62 · see citing works

The superfamily of mitochondrial Complex1_LYR motif-containing (LYRM) proteins

Angerer, H. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130116 · Cited by 59 · see citing works

Non-transferrin Iron Reduction and Uptake Are Regulated by Transmembrane Ascorbate Cycling in K562 Cells

Lane, D. J. R., & Lawen, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800713200 · Cited by 56 · see citing works

Fixing frataxin: ‘ironing out’ the metabolic defect in F riedreich's ataxia

Anzovino, A., Lane, D. J. R., Huang, M. L. H., & Richardson, D. R. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12470 · Cited by 55 · see citing works

The Role of CyaY in Iron Sulfur Cluster Assembly on the E. coli IscU Scaffold Protein

Iannuzzi, C., Adinolfi, S., Howes, B. D., García‐Serres, R., Clémancey, M., Latour, J., Smulevich, G., & Pastore, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021992 · Cited by 55 · see citing works

The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis

Sheftel, A. D., & Lill, R. (2008) · Annals of Medicine · doi:10.1080/07853890802322229 · Cited by 48 · see citing works

HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis

Shan, Y., & Cortopassi, G. A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr582 · Cited by 47 · see citing works

A structural model for glutathione-complexed iron–sulfur cluster as a substrate for ABCB7-type transporters

Qi, W., Li, J., & Cowan, J. A. (2014) · Chemical Communications · doi:10.1039/c3cc48239a · Cited by 45 · see citing works

Mechanism of glutaredoxin—ISU [2Fe–2S] cluster exchange

Qi, W., & Cowan, J. A. (2011) · Chemical Communications · doi:10.1039/c0cc05079b · Cited by 44 · see citing works

Iron regulatory protein-1 protects against mitoferrin-1-deficient porphyria

Chung, J., Anderson, S. A., Gwynn, B., Deck, K. M., Chen, M. J., Langer, N. B., Shaw, G. C., Huston, N. C., Boyer, L. F., Datta, S., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.547778 · Cited by 39 · see citing works

The Glutamate Aspartate Transporter (GLAST) Mediates l-Glutamate-Stimulated Ascorbate-Release Via Swelling-Activated Anion Channels in Cultured Neonatal Rodent Astrocytes

Lane, D. J. R., & Lawen, A. (2012) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-012-9404-8 · Cited by 35 · see citing works

Iron chaperones for mitochondrial Fe–S cluster biosynthesis and ferritin iron storage

Subramanian, P., Rodrigues, A. V., Ghimire-Rijal, S., & Stemmler, T. L. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.01.003 · Cited by 31 · see citing works

Iron transport in K562 cells: a kinetic study using native gel electrophoresis and 59Fe autoradiography

Vyoral, D., & Petrák, J. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(98)00039-1 · Cited by 27 · see citing works

Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone

Sun, G., Gargus, J. J., Ta, D. T., & Vickery, L. E. (2003) · Journal of Human Genetics · doi:10.1007/s10038-003-0048-9 · Cited by 26 · see citing works

Biochemistry of cardiomyopathy in the mitochondrial disease Friedreich's ataxia

Lane, D. J. R., Huang, M. L. H., Ting, S., Sivagurunathan, S., & Richardson, D. R. (2013) · Biochemical Journal · doi:10.1042/bj20130079 · Cited by 23 · see citing works

Effect of ascorbate in the reduction of transferrin-associated iron in endocytic vesicles

Escobar, A., Gaete, V., & N��ez, M. T. (1992) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762681 · Cited by 20 · see citing works

Key Players and Their Role During Mitochondrial Iron–Sulfur Cluster Biosynthesis

Rawat, S., & Stemmler, T. L. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002143 · Cited by 19 · see citing works

The Lure of a LYR: The Logistics of Iron Sulfur Cluster Delivery

Lane, D. J. R., Merlot, A. M., & Richardson, D. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.02.011 · Cited by 8 · see citing works

Ferroptosis: machinery and regulation

Chen, X., Li, J., Kang, R., Klionsky, D. J., & Tang, D. (2021) · Autophagy · doi:10.1080/15548627.2020.1810918 · Cited by 2,099 · see citing works

A Red carpet for iron metabolism

Muckenthaler, M. U., Rivella, S., Hentze, M. W., & Galy, B. (2017) · Cell · doi:10.1016/j.cell.2016.12.034 · Cited by 1,319 · see citing works

Loss of ‘homeostatic’ microglia and patterns of their activation in active multiple sclerosis

Zrzavy, T., Hametner, S., Wimmer, I., Butovsky, O., Weiner, H. L., & Lassmann, H. (2017) · Brain · doi:10.1093/brain/awx113 · Cited by 684 · see citing works

Ferritinophagy via NCOA4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis

Mancias, J. D., Pontano Vaites, L., Nissim, S., Biancur, D. E., Kim, A. J., Wang, X., Liu, Y., Goessling, W., Kimmelman, A. C., & Harper, J. W. (2015) · eLife · doi:10.7554/elife.10308 · Cited by 552 · see citing works

On Iron Metabolism and Its Regulation

Vogt, A. S., Arsiwala, T., Mohsen, M. O., Vogel, M., Manolova, V., & Bachmann, M. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094591 · Cited by 473 · see citing works

Mitochondria and Iron: current questions

Paul, B. T., Manz, D. H., Torti, F. M., & Torti, S. V. (2016) · Expert Review of Hematology · doi:10.1080/17474086.2016.1268047 · Cited by 429 · see citing works

Iron homeostasis in plants – a brief overview

Connorton, J. M., Balk, J., & Rodríguez-Celma, J. (2017) · Metallomics · doi:10.1039/c7mt00136c · Cited by 420 · see citing works

Iron–sulfur cluster biogenesis and trafficking in mitochondria

Braymer, J. J., & Lill, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.787101 · Cited by 389 · see citing works

Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism

Ding, K., Liu, C., Li, L., Yang, M., Jiang, N., Luo, S., & Sun, L. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002533 · Cited by 396 · see citing works

Metformin induces Ferroptosis by inhibiting UFMylation of SLC7A11 in breast cancer

Yang, J., Zhou, Y., Xie, S., Wang, J., Li, Z., Chen, L., Mao, M., Chen, C., Huang, A., Chen, Y., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02012-7 · Cited by 386 · see citing works

Iron catalysis of lipid peroxidation in ferroptosis: Regulated enzymatic or random free radical reaction?

Stoyanovsky, D. A., Tyurina, Y. Y., Shrivastava, I. H., Bahar, İ., Tyurin, V. A., Protchenko, O. V., Jadhav, S., Bolevich, S., Kozlov, A. V., Vladimirov, Y. A., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.008 · Cited by 374 · see citing works

Mitochondria and microbiota dysfunction in COVID-19 pathogenesis

Saleh, J., Peyssonnaux, C., Singh, K. K., & Edeas, M. A. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.06.008 · Cited by 304 · see citing works

Iron and Alzheimer’s Disease: An Update on Emerging Mechanisms

Lane, D. J. R., Ayton, S., & Bush, A. I. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179944 · Cited by 278 · see citing works

Altered Iron Metabolism and Impact in Cancer Biology, Metastasis, and Immunology

Brown, R. A. M., Richardson, K. L., Kabir, T. D., Trinder, D., Ganß, R., & Leedman, P. J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00476 · Cited by 279 · see citing works

Iron as a central player and promising target in cancer progression

Jung, M., Mertens, C., Tomat, E., & Brüne, B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020273 · Cited by 268 · 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

The emerging role of ferroptosis in intestinal disease

Xu, S., He, Y., Lin, L., Chen, P., Chen, M., & Zhang, S. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03559-1 · Cited by 263 · see citing works

Autophagy mediates an amplification loop during ferroptosis

Lee, S., Hwang, N., Seok, B. G., Lee, S., Lee, S., & Chung, S. W. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05978-8 · Cited by 240 · see citing works

Antioxidants Mediate Both Iron Homeostasis and Oxidative Stress

Imam, M. U., Zhang, S., Ma, J., Wang, H., & Wang, F. (2017) · Nutrients · doi:10.3390/nu9070671 · Cited by 226 · see citing works

Ferroptosis: Opportunities and Challenges in Myocardial Ischemia‐Reperfusion Injury

Zhao, W., Zhou, Y., Xu, T., & Wu, Q. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9929687 · Cited by 212 · see citing works

Iron homeostasis in host and gut bacteria – a complex interrelationship

Seyoum, Y., Baye, K., & Humblot, C. (2021) · Gut Microbes · doi:10.1080/19490976.2021.1874855 · Cited by 196 · see citing works

Iron bioavailability from food fortification to precision nutrition. A review

Blanco-Rojo, R., & Vaquero, M. P. (2018) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2018.04.015 · Cited by 181 · see citing works

The Aging of Iron Man

Ashraf, A., Clark, M., & So, P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00065 · Cited by 158 · see citing works

Gallium-Based Liquid Metal Particles for Therapeutics

Xie, W., Allioux, F., Ou, J. Z., Miyako, E., Tang, S., & Kalantar‐Zadeh, K. (2020) · Trends in biotechnology · doi:10.1016/j.tibtech.2020.10.005 · Cited by 154 · see citing works

Ferroptosis in hepatocellular carcinoma: mechanisms and targeted therapy

Ajoolabady, A., Tang, D., Kroemer, G., & Ren, J. T. (2022) · British Journal of Cancer · doi:10.1038/s41416-022-01998-x · Cited by 154 · see citing works

Ferroptosis: mechanisms and implications for cancer development and therapy response

dos Santos, A. F., Fazeli, G., da Silva, T. N. X., & Angeli, J. P. F. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.04.005 · Cited by 151 · see citing works

Duodenal Cytochrome b (DCYTB) in Iron Metabolism: An Update on Function and Regulation

Lane, D. J. R., Bae, D.-H., Merlot, A. M., Sahni, S., & Richardson, D. R. (2015) · Nutrients · doi:10.3390/nu7042274 · Cited by 153 · see citing works

Iron Homeostasis Disorder and Alzheimer’s Disease

Peng, Y., Chang, X., & Lang, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212442 · Cited by 143 · see citing works

From Synthesis to Utilization: The Ins and Outs of Mitochondrial Heme

Swenson, S. A., Moore, C. M., Marcero, J. R., Medlock, A. E., Reddi, A. R., & Khalimonchuk, O. (2020) · Cells · doi:10.3390/cells9030579 · Cited by 148 · see citing works

Induction and application of ferroptosis in cancer therapy

Nie, Q. H., Hu, Y., Yu, X. H., Li, X., & Fang, X. (2022) · Cancer Cell International · doi:10.1186/s12935-021-02366-0 · Cited by 139 · see citing works

The Impact of Oxidative Stress on Ribosomes: From Injury to Regulation

Shcherbik, N., & Pestov, D. G. (2019) · Cells · doi:10.3390/cells8111379 · Cited by 137 · see citing works

A role for divalent metal transporter (DMT1) in mitochondrial uptake of iron and manganese

Wolff, N. A., Garrick, M. D., Zhao, L., Garrick, L. M., Ghio, A. J., & Thévenod, F. (2018) · Scientific Reports · doi:10.1038/s41598-017-18584-4 · Cited by 134 · see citing works

Revisiting nanoparticle technology for blood–brain barrier transport: Unfolding at the endothelial gate improves the fate of transferrin receptor-targeted liposomes

Johnsen, K. B., & Moos, T. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.11.032 · Cited by 132 · see citing works

Redox cycling metals: Pedaling their roles in metabolism and their use in the development of novel therapeutics

Kalinowski, D. S., Stefani, C., Toyokuni, S., Ganz, T., Anderson, G. J., Subramaniam, V. N., Trinder, D., Olynyk, J. K., Chua, A. C. G., Jansson, P. J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.026 · Cited by 129 · see citing works

Unraveling Cell Death Pathways during Malaria Infection: What Do We Know So Far?

Sena-dos-Santos, C., Braga-da-Silva, C., Marques, D., Pinheiro, J. A. D. S., Ribeiro‐dos‐Santos, Â., & Cavalcante, G. C. (2021) · Cells · doi:10.3390/cells10020479 · Cited by 130 · see citing works

Endometriosis: The Role of Iron Overload and Ferroptosis

Ng, S., Norwitz, S. G., Taylor, H. S., & Norwitz, E. R. (2020) · Reproductive Sciences · doi:10.1007/s43032-020-00164-z · Cited by 132 · see citing works

Iron metabolism and related genetic diseases: A cleared land, keeping mysteries

Brissot, P., & Loréal, O. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.11.009 · Cited by 126 · see citing works

Iron Acquisition in Mycobacterium tuberculosis

Chao, A., Sieminski, P. J., Owens, C. P., & Goulding, C. W. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00285 · Cited by 125 · see citing works

Inhibition of Glutaredoxin 5 predisposes Cisplatin-resistant Head and Neck Cancer Cells to Ferroptosis

Lee, J., You, J. H., Shin, D., & Roh, J. (2020) · Theranostics · doi:10.7150/thno.46903 · Cited by 127 · see citing works

Erythroid cell mitochondria receive endosomal iron by a “kiss-and-run” mechanism

Hamdi, A., Roshan, T., Kahawita, T. M., Mason, A. B., Sheftel, A. D., & Ponka, P. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.008 · Cited by 124 · see citing works

The significance, trafficking and determination of labile iron in cytosol, mitochondria and lysosomes

Lv, H., & Shang, P. (2018) · Metallomics · doi:10.1039/c8mt00048d · Cited by 123 · see citing works

Ferroptosis Mediated by Lipid Reactive Oxygen Species: A Possible Causal Link of Neuroinflammation to Neurological Disorders

Cheng, Y., Song, Y., Chen, H., Li, Q., Gao, Y. Z., Lu, G., & Luo, C. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/5005136 · Cited by 122 · see citing works

Iron and oxidative stress in cardiomyopathy in thalassemia

Berdoukas, V. A., Coates, T. D., & Cabantchik, Z. I. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.019 · Cited by 119 · see citing works

Protein networks in the maturation of human iron–sulfur proteins

Ciofi‐Baffoni, S., Nasta, V., & Banci, L. (2017) · Metallomics · doi:10.1039/c7mt00269f · Cited by 116 · see citing works

Role of iron in neurodegenerative diseases

Li, K., & Reichmann, H. (2016) · Journal of Neural Transmission · doi:10.1007/s00702-016-1508-7 · Cited by 118 · see citing works

Mitochondrial iron metabolism and neurodegenerative diseases

Cheng, R., Dhorajia, V. V., Kim, J., & Kim, Y. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.11.003 · Cited by 120 · see citing works

Why cells need iron: a compendium of iron utilisation

Teh, M. R., Armitage, A. E., & Drakesmith, H. (2024) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2024.04.015 · Cited by 114 · see citing works

The Multifaceted Regulation of Mitochondria in Ferroptosis

Wu, H., Wang, F., Ta, N., Zhang, T., & Gao, W. (2021) · Life · doi:10.3390/life11030222 · Cited by 111 · see citing works

Iron and Neurodegeneration: Is Ferritinophagy the Link?

Biasiotto, G., Lorenzo, D. D., Archetti, S., & Zanella, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9473-y · Cited by 104 · see citing works

Alterations in Cellular Iron Metabolism Provide More Therapeutic Opportunities for Cancer

Zhou, L., Zhao, B., Zhang, L., Wang, S., Dong, D., Lv, H., & Shang, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051545 · Cited by 102 · see citing works

Arsenite induces testicular oxidative stress in vivo and in vitro leading to ferroptosis

Meng, P., Zhang, S., Jiang, X., Cheng, S., Zhang, J., Cao, X., Qin, X., Zou, Z., & Chen, C. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.110360 · Cited by 101 · see citing works

Ferritinophagy: A novel insight into the double‐edged sword in ferritinophagy–ferroptosis axis and human diseases

Li, J., Feng, Y., Li, Y., He, P., Zhou, Q.-Y., Tian, Y., Yao, R.-Q., & Yao, Y.-M. (2024) · Cell Proliferation · doi:10.1111/cpr.13621 · Cited by 102 · see citing works

Quercetin attenuates neurotoxicity induced by iron oxide nanoparticles

Bardestani, A., Ebrahimpour, S., Esmaeili, A., & Esmaeili, A. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-021-01059-0 · Cited by 105 · see citing works

FDXR mutations cause sensorial neuropathies and expand the spectrum of mitochondrial Fe-S-synthesis diseases

Paul, A., Drecourt, A., Petit, F., Deguine, D. D., Vasnier, C., Oufadem, M., Masson, C., Bonnet, C., Masmoudi, S., Mosnier, I., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.09.007 · Cited by 95 · see citing works

Impaired Transferrin Receptor Palmitoylation and Recycling in Neurodegeneration with Brain Iron Accumulation

Drecourt, A., Babdor, J., Dussiot, M., Petit, F., Goudin, N., Garfa-Traoré, M., Habarou, F., Bole-Feysot, C., Nitschké, P., Ottolenghi, C., et al. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2018.01.003 · Cited by 100 · see citing works

Neuronal Mitochondrial Dysfunction Activates the Integrated Stress Response to Induce Fibroblast Growth Factor 21

Restelli, L. M., Oettinghaus, B., Halliday, M., Ağca, C., Licci, M., Sironi, L., Savoia, C., Hench, J., Tolnay, M., Neutzner, A., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.023 · Cited by 96 · see citing works

Iron Metabolism and Brain Development in Premature Infants

Wang, Y., Wu, Y., Li, T., Wang, X., & Zhu, C. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00463 · Cited by 98 · see citing works

Compartmentalization of iron between mitochondria and the cytosol and its regulation

Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95 · see citing works

Simultaneous Fe ²⁺ /Fe ³⁺ imaging shows Fe ³⁺ over Fe ²⁺ enrichment in Alzheimer’s disease mouse brain

Wu, Y., Torabi, S.-F., Lake, R. J., Hong, S., Yu, Z., Wu, P., Yang, Z., Nelson, K., Guo, W., Pawel, G. T., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade7622 · Cited by 91 · see citing works

Iron and Copper Intracellular Chelation as an Anticancer Drug Strategy

Gaur, K., Vázquez-Salgado, A. M., Duran-Camacho, G., Dominguez-Martinez, I., Benjamín-Rivera, J. A., Fernández-Vega, L., Carmona‐Sarabia, L., García, A. C., Pérez-Deliz, F., Román, J. A. M., et al. (2018) · Inorganics · doi:10.3390/inorganics6040126 · Cited by 91 · see citing works

Regulation of Osteoblast Differentiation and Iron Content in MC3T3-E1 Cells by Static Magnetic Field with Different Intensities

Yang, J., Zhang, J., Ding, C., Dong, D., & Shang, P. (2017) · Biological Trace Element Research · doi:10.1007/s12011-017-1161-5 · Cited by 88 · see citing works

Down the Iron Path: Mitochondrial Iron Homeostasis and Beyond

Dietz, J. V., Fox, J. L., & Khalimonchuk, O. (2021) · Cells · doi:10.3390/cells10092198 · Cited by 89 · see citing works

Ferroptosis in lung cancer: a novel pathway regulating cell death and a promising target for drug therapy

Xing, N., Du, Q., Guo, S., Xiang, G., Zhang, Y., Meng, X., Li, X., & Wang, S. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01407-z · Cited by 88 · see citing works

The Role of Iron in Friedreich’s Ataxia: Insights From Studies in Human Tissues and Cellular and Animal Models

Llorens, J. V., Soriano, S., Calap-Quintana, P., González‐Cabo, P., & Moltó, M. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00075 · Cited by 87 · see citing works

Emerging Pathological Engagement of Ferroptosis in Gut Diseases

Gao, W., Zhang, T., & Wu, H. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4246255 · Cited by 87 · see citing works

Transferrin receptors

Guo, Q., Qian, C., Wang, X., & Qian, Z. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01436-x · Cited by 89 · see citing works

Impact of Solid‐State Fermentation (Aspergillus oryzae) on Functional Properties and Mineral Bioavailability of Black‐Eyed Pea (Vigna unguiculata) Seed Flour

Chawla, P., Bhandari, L., Sadh, P. K., & Kaushik, R. (2016) · Cereal Chemistry · doi:10.1094/cchem-05-16-0128-r · Cited by 86 · see citing works

Lipid Metabolism Regulates Oxidative Stress and Ferroptosis in RAS-Driven Cancers: A Perspective on Cancer Progression and Therapy

Bartolacci, C., Andreani, C., Elgammal, Y., & Scaglioni, P. P. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.706650 · Cited by 83 · see citing works

Iron and zinc exploitation during bacterial pathogenesis

Ma, L. M., Terwilliger, A. L., & Maresso, A. W. (2015) · Metallomics · doi:10.1039/c5mt00170f · Cited by 83 · see citing works

pH‐Sensitive Molecular‐Switch‐Containing Polymer Nanoparticle for Breast Cancer Therapy with Ferritinophagy‐Cascade Ferroptosis and Tumor Immune Activation

Zuo, T., Fang, T., Zhang, J., Yang, J., Xu, R., Wang, Z., Deng, H., & Shen, Q. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202100683 · Cited by 79 · see citing works

Nitric Oxide, Iron and Neurodegeneration

Liu, C., Liang, M. C., & Soong, T. W. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00114 · Cited by 79 · see citing works

Mitochondrial iron overload: causes and consequences

Rouault, T. A. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.02.004 · Cited by 78 · see citing works

Links Between Iron and Lipids: Implications in Some Major Human Diseases

Rockfield, S., Chhabra, R., Robertson, M., Rehman, N., Bisht, R., & Nanjundan, M. (2018) · Pharmaceuticals · doi:10.3390/ph11040113 · Cited by 78 · see citing works

High-Dose Vitamin C for Cancer Therapy

Mussa, A., Idris, R. A. M., Ahmed, N., Ahmad, S., Murtadha, A. H., Din, T. A. D. A. T., Yean, C. Y., Rahman, W. F. W. A., Lazim, N. M., Uskoković, V., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15060711 · Cited by 81 · see citing works

Iron chelation therapy

Bruzzese, A., Martino, E. A., Mendicino, F., Lucia, E., Olivito, V., Bova, C., Filippelli, G., Capodanno, I., Neri, A., Morabito, F., et al. (2023) · European Journal Of Haematology · doi:10.1111/ejh.13935 · Cited by 76 · see citing works

Time-course assessment of the aggregation and metabolization of magnetic nanoparticles

Rojas, J. M., Gavilán, H., del Dedo, V., Lorente-Sorolla, E., Sanz-Ortega, L., da Silva, G. B., Costo, R., Pérez-Yagüe, S., Talelli, M., Marciello, M., et al. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.05.047 · Cited by 76 · see citing works

Inhibiting Ferroptosis: A Novel Approach for Ulcerative Colitis Therapeutics

Huang, J., Zhang, J., Ma, J., Ma, J., Liu, J., Wang, F., & Tang, X. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9678625 · Cited by 73 · see citing works

The influence of microbiota on ferroptosis in intestinal diseases

Yao, T. S., & Li, L. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2263210 · Cited by 72 · see citing works

Iron–sulfur clusters: from metals through mitochondria biogenesis to disease

Cardenas‐Rodriguez, M., Chatzi, A., & Tokatlidis, K. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1548-6 · Cited by 72 · see citing works

Emerging Regulatory Role of Nrf2 in Iron, Heme, and Hemoglobin Metabolism in Physiology and Disease

Kasai, S., Mimura, J., Ozaki, T., & Itoh, K. (2018) · Frontiers in Veterinary Science · doi:10.3389/fvets.2018.00242 · Cited by 71 · see citing works

D-Glyceraldehyde-3-Phosphate Dehydrogenase Structure and Function

White, M. R., & Garcin, E. D. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-46503-6_15 · Cited by 71 · see citing works

The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer

Yanatori, I., Richardson, D. R., Toyokuni, S., & Kishi, F. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.776021 · Cited by 69 · see citing works

Thrombopoietin receptor–independent stimulation of hematopoietic stem cells by eltrombopag

Kao, Y.-R., Chen, J., Narayanagari, S.-R., Todorova, T. I., Aivalioti, M. M., Ferreira, M. D. S., Ramos, P. M., Pallaud, C., Mantzaris, I., Shastri, A., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aas9563 · Cited by 69 · see citing works

Ferroptosis-related small-molecule compounds in cancer therapy: Strategies and applications

Yin, L., Liu, P., Jin, Y., Ning, Z., Yang, Y., & Gao, H. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114861 · Cited by 66 · see citing works

Role of ferroptosis pathways in neuroinflammation and neurological disorders: From pathogenesis to treatment

Mohan, S., Alhazmi, H. A., Hassani, R., Khuwaja, G., Maheshkumar, V. P., Aldahish, A. A., & Chidambaram, K. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e24786 · Cited by 67 · see citing works

Self-assembled nano-activator constructed ferroptosis-immunotherapy through hijacking endogenous iron to intracellular positive feedback loop

Xiong, H., Wang, C., Wang, Z., Lu, H., & Yao, J. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.03.007 · Cited by 66 · see citing works

Redox-Active Metal Ions and Amyloid-Degrading Enzymes in Alzheimer’s Disease

Kim, N., & Lee, H. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147697 · Cited by 67 · see citing works

Transferrin-targeted porous silicon nanoparticles reduce glioblastoma cell migration across tight extracellular space

Sheykhzadeh, S., Luo, M., Peng, B., White, J., Abdalla, Y., Tang, T., Mäkilä, E. M., Voelcker, N. H., & Tong, W. Y. (2020) · Scientific Reports · doi:10.1038/s41598-020-59146-5 · Cited by 66 · see citing works

Iron Brain Menace: The Involvement of Ferroptosis in Parkinson Disease

Lin, K.-J., Chen, S., Lin, K.-L., Liou, C., Lan, M., Chuang, Y., Wang, P., Lee, J., Wang, F., Lin, H., et al. (2022) · Cells · doi:10.3390/cells11233829 · Cited by 68 · see citing works

Gallium Maltolate Disrupts Tumor Iron Metabolism and Retards the Growth of Glioblastoma by Inhibiting Mitochondrial Function and Ribonucleotide Reductase

Chitambar, C. R., Al-Gizawiy, M. M., Alhajala, H. S., Pechman, K. R., Wereley, J. P., Wujek, R. T., Clark, P. A., Kuo, J. S., Antholine, W. E., & Schmainda, K. M. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-1009 · Cited by 64 · see citing works

Targeting the regulation of iron homeostasis as a potential therapeutic strategy for nonalcoholic fatty liver disease

Sui, Y., Geng, X., Wang, Z., Zhang, J., Yang, Y., & Meng, Z. (2024) · Metabolism · doi:10.1016/j.metabol.2024.155953 · Cited by 64 · see citing works

Effects of Iron-Oxide Nanoparticle Surface Chemistry on Uptake Kinetics and Cytotoxicity in CHO-K1 Cells

Hanot, C., Choi, Y., Anani, T., Soundarrajan, D. K., & David, A. E. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms17010054 · Cited by 63 · see citing works

Dysregulation of Neuronal Iron Homeostasis as an Alternative Unifying Effect of Mutations Causing Familial Alzheimer’s Disease

Lumsden, A. L., Rogers, J. T., Majd, S., Newman, M., Sutherland, G. T., Verdile, G., & Lardelli, M. T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00533 · Cited by 58 · see citing works

Iron and Cadmium Entry Into Renal Mitochondria: Physiological and Toxicological Implications

Thévenod, F., Lee, W., & Garrick, M. D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00848 · Cited by 59 · see citing works

Iron metabolism and ferroptosis in health and diseases: The crucial role of mitochondria in metabolically active tissues

Catapano, A., Cimmino, F., Petrella, L., Pizzella, A., D’Angelo, M., Ambrosio, K., Marino, F., Sabbatini, A., Petrelli, M. D., Paolini, B., et al. (2025) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2025.109888 · Cited by 65 · see citing works

Frataxin and the molecular mechanism of mitochondrial iron-loading in Friedreich's ataxia

Chiang, S., Kovačević, Ž., Sahni, S., Lane, D. J. R., Merlot, A. M., Kalinowski, D. S., Huang, M. L. H., & Richardson, D. R. (2016) · Clinical Science · doi:10.1042/cs20160072 · Cited by 58 · see citing works

Therapeutic potential of iron chelators on osteoporosis and their cellular mechanisms

Zhang, J., Zhao, H., Yao, G., Qiao, P., Li, L., & Wu, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111380 · Cited by 56 · see citing works

Iron-responsive element-binding protein 2 plays an essential role in regulating prostate cancer cell growth

Deng, Z., Manz, D. H., Torti, S. V., & Torti, F. M. (2017) · Oncotarget · doi:10.18632/oncotarget.19288 · Cited by 56 · see citing works

Iron robbery by intracellular pathogen via bacterial effector–induced ferritinophagy

Yan, Q., Zhang, W., Lin, M., Teymournejad, O., Budachetri, K., Lakritz, J., & Rikihisa, Y. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2026598118 · Cited by 54 · see citing works

Iron homeostasis in older adults: balancing nutritional requirements and health risks

Zeidan, R. S., Martenson, M. S., Tamargo, J. A., McLaren, C., Ezzati, A., Lin, Y., Yang, J. J., Yoon, H., McElroy, T., Collins, J. F., et al. (2024) · The journal of nutrition health & aging · doi:10.1016/j.jnha.2024.100212 · Cited by 59 · see citing works

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 · see citing works

Compartmentalization of iron between mitochondria and the cytosol and its regulation

Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95 · see citing works

Cellular and mitochondrial iron homeostasis in vertebrates

Chen, C., & Paw, B. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.003 · Cited by 106 · see citing works

Down the Iron Path: Mitochondrial Iron Homeostasis and Beyond

Dietz, J. V., Fox, J. L., & Khalimonchuk, O. (2021) · Cells · doi:10.3390/cells10092198 · Cited by 89 · see citing works

REVIEW ARTICLE The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis

Sheftel, A. D., & Lill, R. (2015)