Mitochondrial iron metabolism and its role in neurodegeneration

Free radicals in biology and medicine

Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works

Free Radicals in Biology and Medicine

Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990 · see citing works

Alzheimer’s disease

Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · see citing works

The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen

Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626 · see citing works

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120 · see citing works

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 · see citing works

Balancing Acts

Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736 · see citing works

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447 · see citing works

The effect of age on the non-haemin iron in the human brain

Hallgren, B., & Sourander, P. (1958) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1958.tb12607.x · Cited by 1,427 · see citing works

Iron accumulation in Alzheimer disease is a source of redox-generated free radicals

Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357 · see citing works

Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial

Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988 · see citing works

Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria

Cadenas, E., Boveris, A., Ragan, C. I., & Stoppani, A. O. M. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90035-2 · Cited by 855 · see citing works

The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1

Herrero-Mendez, A., Almeida, A., Fernández, E., Maestre, C., Moncada, S., & Bolaños, J. P. (2009) · Nature Cell Biology · doi:10.1038/ncb1881 · Cited by 844 · 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

Intramuscular desferrioxamine in patients with Alzheimer's disease

MCLACHLAN, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)92978-b · Cited by 764 · 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

Rapid Restoration of Cognition in Alzheimer's Transgenic Mice with 8-Hydroxy Quinoline Analogs Is Associated with Decreased Interstitial Aβ

Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., Volitakis, I., Liu, X., Smith, J. P., Perez, K., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.018 · Cited by 672 · 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

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 · 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

Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 567 · see citing works

An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript

Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., Leiter, L., McPhee, J., Sarang, S. S., Utsuki, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207435200 · Cited by 551 · see citing works

Labile iron pool: the main determinant of cellular response to oxidative stress

Kruszewski, M. K. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.004 · Cited by 529 · see citing works

Intracellular iron transport and storage: from molecular mechanisms to health implications

Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526 · see citing works

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 · see citing works

Biosynthesis of heme in mammals

Ajioka, R. S., Phillips, J. D., & Kushner, J. P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.005 · Cited by 493 · 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

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

Assay of metabolic superoxide production in Escherichia coli.

Imlay, J. A., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89596-9 · Cited by 420 · see citing works

Divalent metal transporter 1 (DMT1) contributes to neurodegeneration in animal models of Parkinson's disease

Salazar, J., Mena, N., Hunot, S., Prigent, A., Alvarez-Fischer, D., Arredondo, M., Duyckaerts, C., Sazdovitch, V., Zhao, L., Garrick, L. M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804373105 · Cited by 409 · 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

A human mitochondrial ferritin encoded by an intronless gene

Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400 · 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

Regional distribution of iron and iron‐regulatory proteins in the brain in aging and Alzheimer's disease

Connor, J. R., Snyder, B. S., Beard, J. L., Fine, R. E., & Mufson, E. J. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310214 · Cited by 374 · see citing works

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 · see citing works

Iron Toxicity in Diseases of Aging: Alzheimer's Disease, Parkinson's Disease and Atherosclerosis

Altamura, S., & Muckenthaler, M. U. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1010 · Cited by 369 · see citing works

Alzheimer's disease, metal ions and metal homeostatic therapy

Zatta, P., Drago, D., Bolognin, S., & Sensi, S. L. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.05.002 · Cited by 369 · 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

Identification of a mammalian mitochondrial porphyrin transporter

Krishnamurthy, P. C., Du, G., Fukuda, Y., Sun, D., Sampath, J., Mercer, K. E., Wang, J., Sosa‐Pineda, B., Murti, K. G., & Schuetz, J. D. (2006) · Nature · doi:10.1038/nature05125 · Cited by 358 · see citing works

Platelet mitochondria function in Parkinson's disease

Krige, D., Carroll, M. T., Cooper, J. A. D., MARSDEN, C. D., & Schapira, A. H. V. (1992) · Annals of Neurology · doi:10.1002/ana.410320612 · Cited by 358 · see citing works

The Relevance of Iron in the Pathogenesis of Parkinson's Disease

Götz, M. E., Double, K. L., Gerlach, M., Youdim, M. B. H., & RIEDERERE, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.017 · Cited by 342 · see citing works

Iron misregulation in the brain: a primary cause of neurodegenerative disorders

Ke, Y., & Qian, Z. (2003) · The Lancet Neurology · doi:10.1016/s1474-4422(03)00353-3 · Cited by 339 · see citing works

Iron-melanin complex in substantia nigra of parkinsonian brains: an x-ray microanalysis

Jellinger, K., Kienzl, E., Rumpelmair, G., Riederer, P., Stachelberger, H., Ben‐Shachar, D., & Youdim, M. B. H. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08362.x · Cited by 313 · see citing works

The human counterpart of zebrafish shiraz shows sideroblastic-like microcytic anemia and iron overload

Camaschella, C., Campanella, A., De Falco, L., Boschetto, L., Merlini, R., Silvestri, L., Levi, S., & Iolascon, A. (2007) · Blood · doi:10.1182/blood-2007-02-072520 · Cited by 306 · see citing works

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 301 · see citing works

Aluminium, iron, zinc and copper influence the in vitro formation of amyloid fibrils of Aβ42 in a manner which may have consequences for metal chelation therapy in Alzheimer's disease

House, E., Collingwood, J., Khan, A., Korchazkina, O., Berthon, G., & Exley, C. (2004) · Journal of Alzheimer's Disease · doi:10.3233/jad-2004-6310 · Cited by 294 · see citing works

Metal-Responsive Transcription Factors That Regulate Iron, Zinc, and Copper Homeostasis in Eukaryotic Cells

Rutherford, J. C., & Bird, A. J. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.1.1-13.2004 · Cited by 293 · see citing works

Transferrin receptor 2: Continued expression in mouse liver in the face of iron overload and in hereditary hemochromatosis

Fleming, R. E., Migas, M. C., Holden, C. C., Waheed, A., Britton, R. S., Tomatsu, S., Bacon, B. R., & Sly, W. S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040548097 · Cited by 273 · see citing works

Individual dopaminergic neurons show raised iron levels in Parkinson disease

Oakley, A. E., Collingwood, J. F., Dobson, J., Love, G., Perrott, H. R., Edwardson, J. A., Elstner, M., & Morris, C. M. (2007) · Neurology · doi:10.1212/01.wnl.0000262033.01945.9a · Cited by 273 · 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

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 246 · see citing works

Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., YOSHIMASU, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 246 · see citing works

Neuroprotection by a novel brain permeable iron chelator, VK-28, against 6-hydroxydopamine lession in rats

Shachar, D. B., Kahana, N., Kampel, V., Warshawsky, A., & Youdim, M. B. H. (2004) · Neuropharmacology · doi:10.1016/j.neuropharm.2003.09.005 · Cited by 246 · see citing works

Diferric transferrin regulates transferrin receptor 2 protein stability

Johnson, M. B., & Enns, C. A. (2004) · Blood · doi:10.1182/blood-2004-06-2477 · Cited by 230 · see citing works

Neuromelanin associated redox-active iron is increased in the substantia nigra of patients with Parkinson's disease

Faucheux, B. A., Martin, M., Beaumont, C., Hauw, J., Agid, Y., & Hirsch, E. C. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01923.x · Cited by 229 · see citing works

The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.

(2001) · Nature Structural Biology · doi:10.1038/84152 · Cited by 227 · see citing works

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 222 · 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

Human ferrochelatase is an iron-sulfur protein

Dailey, H. A., Finnegan, M. G., & Johnson, M. K. (1994) · Biochemistry · doi:10.1021/bi00168a003 · Cited by 216 · see citing works

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 213 · see citing works

Heme as a Magnificent Molecule with Multiple Missions: Heme Determines Its Own Fate and Governs Cellular Homeostasis

Furuyama, K., Kaneko, K., & V., P. D. V. (2007) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.213.1 · Cited by 210 · see citing works

Expression of the iron transporter ferroportin in synaptic vesicles and the blood-brain barrier

Wu, L. J.-C., Leenders, A. G. M., Cooperman, S., Meyron-Holtz, E., Smith, S., Land, W., Tsai, R. Y. L., Berger, U. V., Sheng, Z.-H., & Rouault, T. A. (2004) · Brain Research · doi:10.1016/j.brainres.2003.10.066 · Cited by 210 · see citing works

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 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

Iron–sulfur proteins in health and disease

Sheftel, A. D., Stehling, O., & Lill, R. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.12.006 · Cited by 203 · see citing works

Human Ind1, an Iron-Sulfur Cluster Assembly Factor for Respiratory Complex I

Sheftel, A. D., Stehling, O., Pierik, A. J., Netz, D. J. A., Kerscher, S., Elsässer, H., Wittig, I., Balk, J., Brandt, U., & Lill, R. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00817-09 · Cited by 201 · see citing works

Interaction of neuromelanin and iron in substantia nigra and other areas of human brain

Zecca, L., Shima, T., Stroppolo, A., Goj, C., Battiston, G. A., Gerbasi, R., Sarna, T., & Swartz, H. M. (1996) · Neuroscience · doi:10.1016/0306-4522(96)00047-4 · Cited by 197 · see citing works

Mitochondrial complex I and II activities of lymphocytes and platelets in Parkinson's disease

Yoshino, H., Nakagawa-Hattori, Y., Kondo, T., & Mizuno, Y. (1992) · Journal of Neural Transmission - Parkinsons Disease and Dementia Section · doi:10.1007/bf02257619 · Cited by 195 · see citing works

A novel transferrin/TfR2-mediated mitochondrial iron transport system is disrupted in Parkinson's disease

Mastroberardino, P. G., Hoffman, E. K., Horowitz, M. P., Betarbet, R., Taylor, G., Cheng, D., Na, H. M., Gutekunst, C.-A., Gearing, M., Trojanowski, J. Q., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.02.009 · Cited by 195 · see citing works

The role of iron in mitochondrial function

Levi, S., & Rovida, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.008 · Cited by 195 · see citing works

Reduction of iron‐regulated amyloid precursor protein and β‐amyloid peptide by (–)‐epigallocatechin‐3‐gallate in cell cultures: implications for iron chelation in Alzheimer's disease

Reznichenko, L., Amit, T., Zheng, H., Avramovich‐Tirosh, Y., Youdim, M. B. H., Weinreb, O., & Mandel, S. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03770.x · Cited by 189 · see citing works

Iron metabolism in Parkinsonian syndromes

Berg, D., & Hochstrasser, H. (2006) · Movement Disorders · doi:10.1002/mds.21020 · Cited by 185 · see citing works

Three Histidine Residues of Amyloid-β Peptide Control the Redox Activity of Copper and Iron

Nakamura, M., Shishido, N., Nunomura, A., Smith, M. A., Perry, G. L., Hayashi, Y., Nakayama, K., & Hayashi, T. (2007) · Biochemistry · doi:10.1021/bi701079z · Cited by 184 · see citing works

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 181 · see citing works

Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis

Nie, G., Sheftel, A. D., Kim, S. F., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-07-2722 · Cited by 179 · 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

The iron–sulphur protein Ind1 is required for effective complex I assembly

Bych, K., Kerscher, S., Netz, D. J. A., Pierik, A. J., Zwicker, K., Huynen, M. A., Lill, R., Brandt, U., & Balk, J. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.98 · Cited by 167 · see citing works

Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia

Campanella, A., Rovelli, E., Santambrogio, P., Cozzi, A., Taroni, F., & Levi, S. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn308 · Cited by 162 · see citing works

RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload

Cavadini, P., Biasiotto, G., Poli, M., Levi, S., Verardi, R., Zanella, I., Derosas, M., Ingrassia, R., Corrado, M., & Arosio, P. (2006) · Blood · doi:10.1182/blood-2006-08-041632 · Cited by 155 · see citing works

In Vitro Studies of Ferritin Iron Release and Neurotoxicity

Double, K. L., Maywald, M., Schmittel, M., Riederer, P. F., & Gerlach, M. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70062492.x · Cited by 152 · see citing works

Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones

Shan, Y., Napoli, E., & Cortopassi, G. A. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm038 · Cited by 152 · see citing works

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 145 · see citing works

Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia

Li, K., Besse, E. K., Ha, D., Kovtunovych, G., & Rouault, T. A. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn127 · Cited by 141 · see citing works

Differences in the RNA binding sites of iron regulatory proteins and potential target diversity.

Butt, J., Kim, H. Y., Basilion, J. P., Cohen, S., Iwaï, K., Philpott, C. C., Altschul, S. F., Klausner, R. D., & Rouault, T. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4345 · Cited by 139 · see citing works

Therapeutic targets and potential of the novel brain‐ permeable multifunctional iron chelator–monoamine oxidase inhibitor drug, M‐30, for the treatment of Alzheimer's disease¹

Avramovich‐Tirosh, Y., Amit, T., Bar‐Am, O., Zheng, H., Fridkin, M., & Youdim, M. B. H. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04258.x · Cited by 130 · see citing works

Characterization and Expression of Iron Regulatory Protein 2 (IRP2)

Guo, B., Brown, F. M., Phillips, J. D., Yu, Y., & Leibold, E. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16529 · Cited by 129 · see citing works

Physical Evidence that Yeast Frataxin Is an Iron Storage Protein

Gakh, O., Adamec, J., Gacy, A. M., Twesten, R. D., Owen, W. G., & Isaya, G. (2002) · Biochemistry · doi:10.1021/bi025566+ · Cited by 128 · see citing works

Role of hepcidin in murine brain iron metabolism

Wang, S.-M., Fu, L.-L., Duan, X.-L., Crooks, D., Yu, P., Qian, Z., Di, X.-J., Li, J., Rouault, T. A., & Chang, Y. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0167-3 · Cited by 127 · see citing works

Distribution of the iron‐regulating protein hepcidin in the murine central nervous system

Zechel, S., Huber‐Wittmer, K., & Halbach, O. V. B. U. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20991 · Cited by 124 · see citing works

Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria

Zhang, A., Sheftel, A. D., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-06-2226 · Cited by 119 · see citing works

Iron‐induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo

Aloria, K., Schilke, B. A., Andrew, A. J., & Craig, E. A. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400272 · Cited by 104 · see citing works

Original Papers: ON THE OCCURRENCE OF ABNORMAL DEPOSITS OF IRON IN THE BRAIN IN PARKINSONISM WITH SPECIAL REFERENCE TO ITS LOCALISATION.

Lhermitte, J., Kraus, W. M., & McAlpine, D. (1924) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.s1-5.19.195 · Cited by 103 · see citing works

Cellular iron transport

Garrick, M. D., & Garrick, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.018 · Cited by 102 · see citing works

Transferrin Receptor 2: Evidence for Ligand-induced Stabilization and Redirection to a Recycling Pathway

Johnson, M. B., Chen, J., Murchison, N., Green, F. A., & Enns, C. A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0798 · Cited by 101 · see citing works

Disturbance of iron metabolism in Parkinson’s disease — ultrasonography as a biomarker

Berg, D., Hochstrasser, H., Schweitzer, K. J., & Rieß, O. (2006) · Neurotoxicity Research · doi:10.1007/bf03033302 · Cited by 98 · see citing works

Neuroprotective Mechanism of Mitochondrial Ferritin on 6-Hydroxydopamine–Induced Dopaminergic Cell Damage: Implication for Neuroprotection in Parkinson's Disease

Shi, Z.-H., Nie, G., Duan, X.-L., Rouault, T. A., Wu, W.-S., Ning, B., Zhang, N., Chang, Y.-Z., & Zhao, B.-L. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3018 · Cited by 98 · see citing works

Divalent metal transporter 1 is involved in amyloid precursor protein processing and Aβ generation

Zheng, W. H., Xin, N., Chi, Z., Zhao, B.-L., Zhang, J., Li, J., & Wang, Z. (2009) · The FASEB Journal · doi:10.1096/fj.09-135749 · Cited by 95 · see citing works

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 93 · see citing works

Non-transferrin-bound iron reaches mitochondria by a chelator-inaccessible mechanism: biological and clinical implications

Shvartsman, M., Kikkeri, R. V., Shanzer, A., & Cabantchik, Z. I. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00054.2007 · Cited by 78 · see citing works

Restoration of Nigrostriatal Dopamine Neurons in Post-MPTP Treatment by the Novel Multifunctional Brain-Permeable Iron Chelator-Monoamine Oxidase Inhibitor Drug, M30

Gal, S., Zheng, H., Fridkin, M., & Youdim, M. B. H. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9070-9 · Cited by 75 · see citing works

nm1054: a spontaneous, recessive, hypochromic, microcytic anemia mutation in the mouse

Ohgami, R. S., Campagna, D. R., Antiochos, B., Wood, E., Sharp, J. J., Barker, J. E., & Fleming, M. D. (2005) · Blood · doi:10.1182/blood-2005-01-0379 · Cited by 74 · see citing works

In vivo detection of iron and neuromelanin by transcranial sonography – a new approach for early detection of substantia nigra damage

Berg, D. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-005-0447-5 · Cited by 73 · see citing works

The Heme Synthesis Defect of Mutants Impaired in Mitochondrial Iron-Sulfur Protein Biogenesis Is Caused by Reversible Inhibition of Ferrochelatase

Lange, H., Mühlenhoff, U., Denzel, M. S., Kispál, G., & Lill, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403721200 · Cited by 66 · see citing works

Oligodendrogenesis: the role of iron

Badaracco, M. E., Siri, M. V. R., & Pasquini, J. M. (2010) · BioFactors · doi:10.1002/biof.90 · Cited by 63 · see citing works

M30, a novel multifunctional neuroprotective drug with potent iron chelating and brain selective monoamine oxidase-ab inhibitory activity for Parkinson’s disease

Gal, S., Fridkin, M., Amit, T., Zheng, H., & Youdim, M. B. H. (2006) · Parkinson’s Disease and Related Disorders · doi:10.1007/978-3-211-45295-0_68 · Cited by 58 · see citing works

An oxidative stress‐mediated positive‐feedback iron uptake loop in neuronal cells

Núñez‐Millacura, C., Tapia, V., Muñoz, P., Maccioni, R. B., & Núñez, M. T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00971.x · Cited by 50 · see citing works

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 · 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

Iron as a cause of Parkinson disease – a myth or a well established hypothesis?

Friedman, A., Gałązka-Friedman, J., & Koziorowski, D. (2009) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(09)70817-x · Cited by 43 · see citing works

Chronic ferritin expression within murine dopaminergic midbrain neurons results in a progressive age-related neurodegeneration

Kaur, D., Rajagopalan, S., Chinta, S., Kumar, J., Di Monte, D., Cherny, R. A., & Andersen, J. K. (2007) · Brain Research · doi:10.1016/j.brainres.2006.03.006 · Cited by 36 · see citing works

A High-Throughput Drug Screen Targeted to the 5′Untranslated Region of Alzheimer Amyloid Precursor Protein mRNA

Bandyopadhyay, S., Ni, J., Ruggiero, A., Walshe, K., Rogers, M. S., Chattopadhyay, N., Glicksman, M. A., & Rogers, J. T. (2006) · SLAS DISCOVERY · doi:10.1177/1087057106287271 · Cited by 33 · see citing works

Overexpression of Mitochondrial Ferritin Sensitizes Cells to Oxidative Stress Via an Iron-Mediated Mechanism

Lu, Z., Nie, G., Li, Y., Soe-Lin, S., Tao, Y., Cao, Y., Zhang, Z., Liu, N., Ponka, P., & Zhao, B. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2306 · Cited by 28 · see citing works

Physiological and pathological aspects of Aβ in iron homeostasis via 5'UTR in the APP mRNA and the therapeutic use of iron-chelators

Avramovich‐Tirosh, Y., Amit, T., Bar‐Am, O., Weinreb, O., & Youdim, M. B. H. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-s2-s2 · Cited by 27 · see citing works

Role of transferrin receptor 2 in hepatic accumulation of iron in patients with chronic hepatitis C

Mifuji, R., Kobayashi, Y., Ma, N., et al. (2006) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2005.04151.x · Cited by 20 · see citing works

Direct Interorganellar Transfer of Iron from Endosome to Mitochondrion.

Sheftel, A. D., Zhang, A., Brown, C. K., et al. (2006) · Blood · doi:10.1182/blood.v108.11.268.268 · Cited by 16 · see citing works

How Iron Controls Iron

Kühn, L. C. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.11.005 · Cited by 15 · see citing works

Role of rasagiline in treating Parkinson’s disease: effect on disease progression

Fernandez, H., & Malaty, I. A. (2009) · Therapeutics and Clinical Risk Management · doi:10.2147/tcrm.s4321 · Cited by 10 · see citing works

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 · see citing works

Repairing mitochondrial dysfunction in disease

Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works

Insulin Resistance and Neurodegeneration: Progress towards the Development of New Therapeutics for Alzheimer's Disease

de la Monte, S. M. (2017) · Drugs · doi:10.1007/s40265-016-0674-0 · Cited by 331 · 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

Cannabidiol normalizes caspase 3, synaptophysin, and mitochondrial fission protein DNM1L expression levels in rats with brain iron overload: implications for neuroprotection

da Silva, V. K., de Freitas, B. S., da Silva Dornelles, A., Nery, L. R., Falavigna, L., Ferreira, R. D. P., Bogo, M. R., Hallak, J. E. C., Zuardi, A. W., Crippa, J. A. S., et al. (2014) · Molecular Neurobiology · doi:10.1007/s12035-013-8514-7 · Cited by 91 · see citing works

Iron Pathophysiology in Alzheimer’s Diseases

Wang, T., Xu, S.-F., Fan, Y.-G., Li, L.-B., & Guo, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_5 · Cited by 64 · see citing works

Urinary metabolic phenotyping for Alzheimer’s disease

Kurbatova, N., Garg, M., Whiley, L., Chekmeneva, E., Jiménez, B., Gómez-Romero, M., Pearce, J., Kimhofer, T., D’Hondt, E., Soininen, H., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-78031-9 · Cited by 44 · see citing works

Disease-associated protein seeding suggests a dissociation between misfolded protein accumulation and neurodegeneration in prion disease

Alibhai, J. D., Diack, A. B., & Manson, J. C. (2017) · Prion · doi:10.1080/19336896.2017.1378289 · Cited by 5 · see citing works

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms

Yang, Y., & Wang, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170788 · Cited by 46 · see citing works

A Possible Neurodegeneration Mechanism Triggered by Diabetes

Farhadi, A., Vosough, M., Zhang, J., Tahamtani, Y., & Shahpasand, K. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.07.012 · Cited by 31 · see citing works

Temperature-Sensitive Paralytic Mutants Are Enriched For Those Causing Neurodegeneration in Drosophila

Palladino, M. J., Hadley, T. J., & Ganetzky, B. (2002) · Genetics · doi:10.1093/genetics/161.3.1197 · Cited by 98 · see citing works

Reactive oxygen species-mediated neurodegeneration is independent of the ryanodine receptor in Caernorhabditis elegans.

Young, L. E. A., & Williams, D. C. (2015) · PubMed · Cited by 3 · see citing works