Cited by 107Genetic Neurodegenerative DiseasesMitochondrial Function and PathologyRedox biology and oxidative stress

The DOI matches its Crossref record; 101 of the 101 references it cites were found in a registry or an index.

Does oxidative stress contribute to the pathology of Friedreich's ataxia? A radical question

Armstrong, Jeffrey S., Khdour, Omar, Hecht, Sidney M.·2010·The FASEB Journal

Open this paper in CoChat — free account

Abstract

Friedreich's ataxia (FRDA) is a hereditary neurodegenerative disease that frequently culminates in cardiac failure at an early age. FRDA is believed to arise from reduced synthesis of the mitochondrial iron chaperone frataxin due to impaired gene transcription, which leads to mitochondrial iron accumulation, dysfunction of mitochondrial Fe‐S containing enzymes, and increased Fenton‐mediated free radical production. Recent reports have challenged this generally accepted hypothesis, by suggesting that the oxidative stress component in FRDA is minimal and thereby questioning the benefit of antioxidant therapeutic strategies. We suggest that this apparent paradox results from the radically divergent chemistries of the participating reactive oxygen species (ROS), the major cellular subcompartments involved and the overall cellular responses to ROS. In this review, we consider these factors and conclude that oxidative stress does constitute a major contributing factor to FRDA pathology. This reaffirms the idea that the rational design of specific small molecule multifunctional antioxidants will benefit FRDA patients.—Armstrong, J. S., Khdour, O., Hecht, S. M. Does oxidative stress contribute to the pathology of Friedreich's ataxia? A radical question. FASEBJ. 24, 2152–2163 (2010). www.fasebj.org

Integrity signals

Registry

Crossref · 10.1096/fj.09-143222

Cites

101 of 101 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Three-dimensional tracking of axonal projections in the brain by magnetic resonance imaging
Mori, S., Crain, B. J., Chacko, V. P., & van Zijl, P. C. M. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199902)45:2 · Cited by 3,513
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010
Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601
Oxidative Phosphorylation at the fin de siècle
Saraste, M. (1999) · Science · doi:10.1126/science.283.5407.1488 · Cited by 1,345
The measurement and mechanism of lipid peroxidation in biological systems
Gutteridge, J. M. C., & Halliwell, B. B. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90206-q · Cited by 1,297
Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
Turrens, J. F., Alexandre, A., & Lehninger, A. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90293-0 · Cited by 1,214
Aconitase and mitochondrial iron–sulphur protein deficiency in Friedreich ataxia
Rötig, A., de Lonlay, P., Chretien, D., Foury, F., Koenig, M., Sidi, D., Munnich, A., & Rustin, P. (1997) · Nature Genetics · doi:10.1038/ng1097-215 · Cited by 991
Architecture of succinate dehydrogenase and reactive oxygen species generation
Yankovskaya, V., Horsefield, R., Törnroth, S., Luna-Chavez, C., Miyoshi, H., Léger, C., Byrne, B., Cecchini, G., & Iwata, S. (2003) · Science · doi:10.1126/science.1079605 · Cited by 927
NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer
Hayes, J. D., & McMahon, M. J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.12.008 · Cited by 870
Superoxide in Apoptosis
Cai, J., & Jones, D. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11401 · Cited by 765
Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions
Catalá, A. (2009) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2008.09.004 · Cited by 745
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
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
Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711
Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 696
The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex.
Trumpower, B. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38410-8 · Cited by 598
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.
Zheng, L., White, R. H., Cash, V. L., Jack, R. F., & Dean, D. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2754 · Cited by 597
Superoxide sensitivity of the Escherichia coli aconitase.
Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55001-8 · Cited by 514
Role of glutathione depletion and reactive oxygen species generation in apoptotic signaling in a human B lymphoma cell line
Armstrong, J. S., Steinauer, K. K., Hornung, B., Irish, J. M., Lecane, P. S., Birrell, G. W., Peehl, D. M., & Knox, S. J. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400959 · Cited by 507
Self-citation
S-glutathionylation in protein redox regulation
Dalle‐Donne, I., Rossi, R., Giustarini, D., Colombo, R., & Milzani, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.014 · Cited by 506
Redox control and oxidative stress in yeast cells
Herrero, E., Ros, J., Bellí, G., & Cabiscol, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.12.004 · Cited by 505
Mitochondrial Oxygen Radical Generation and Leak: Sites of Production in States 4 and 3, Organ Specificity, and Relation to Aging and Longevity
Barja, G. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005427919188 · Cited by 494
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
Histone deacetylase inhibitors reverse gene silencing in Friedreich's ataxia
Herman, D., Jenssen, K., Burnett, R., Soragni, E., Perlman, S. L., & Gottesfeld, J. M. (2006) · Nature Chemical Biology · doi:10.1038/nchembio815 · Cited by 442
The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
Wong, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.3.425 · Cited by 374
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
Deficit of in vivo mitochondrial ATP production in patients with Friedreich ataxia
Lodi, R., Cooper, J. A. D., Bradley, J. L., Manners, D. N., Styles, P., Taylor, D. J., & Schapira, A. H. V. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11492 · Cited by 352
Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue
Wilson, R. B., & Roof, D. M. (1997) · Nature Genetics · doi:10.1038/ng0897-352 · Cited by 345
Oxidative stress in patients with Friedreich ataxia
Schulz, J. B., Dehmer, T., Schöls, L. J., Mende, H. E., Hardt, C., Vorgerd, M., Bürk, K., Matson, W. R., DICHGANS, J., Beal, M. F., et al. (2000) · Neurology · doi:10.1212/wnl.55.11.1719 · Cited by 305
The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron–sulfur cluster N2
Genova, M. L., Ventura, B., Giuliano, G., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02850-2 · Cited by 301
Structures and Proton-Pumping Strategies of Mitochondrial Respiratory Enzymes
Schultz, B. E., & Chan, S. I. (2001) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.30.1.23 · Cited by 299
High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function.
Mårtensson, J., Lai, J. C. K., & Meister, A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.18.7185 · Cited by 282
The Yeast Frataxin Homologue Mediates Mitochondrial Iron Efflux
Radisky, D. C., Babcock, M. C., & Kaplan, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4497 · Cited by 277
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
Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia
Adamec, J., Rusnak, F., Owen, W. G., Naylor, S., Benson, L. M., Gacy, A. M., & Isaya, G. (2000) · The American Journal of Human Genetics · doi:10.1086/303056 · Cited by 255
Intracellular generation of reactive oxygen species by mitochondria
Nohl, H., Gille, L., & Staniek, K. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.12.002 · Cited by 251
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
HDAC Inhibitors Correct Frataxin Deficiency in a Friedreich Ataxia Mouse Model
Rai, M., Soragni, E., Jenssen, K., Burnett, R., Herman, D., Coppola, G., Geschwind, D. H., Gottesfeld, J. M., & Pandolfo, M. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001958 · Cited by 224
Frataxin activates mitochondrial energy conversion and oxidative phosphorylation
Ristow, M., Pfister, M. F., Yee, A. J., Schubert, M., Michael, L., Zhang, C., Ueki, K., Michael, M. D., Lowell, B. B., & Kahn, C. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220403797 · Cited by 221
Friedreich ataxia: the oxidative stress paradox
Seznec, H., Simon, D., Bouton, C., Reutenauer, L., Hertzog, A., Golik, P., Procaccio, V., Patel, M., Drapier, J.-C., Koenig, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi042 · Cited by 219
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
Iron–sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer
Fontecave, M., & de Choudens, S. O. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.12.014 · Cited by 215
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
Effect of Glutathione Depletion on Sites and Topology of Superoxide and Hydrogen Peroxide Production in Mitochondria
Han, D., Canali, R., Rettori, D., & Kaplowitz, N. (2003) · Molecular Pharmacology · doi:10.1124/mol.64.5.1136 · Cited by 211
Localization at Complex I and Mechanism of the Higher Free Radical Production of Brain Nonsynaptic Mitochondria in the Short-Lived Rat Than in the Longevous Pigeon
Barja, G., & Herrero, A. (1998) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1020592719405 · Cited by 203
Autosomal recessive cerebellar ataxias
Palau, F., & Espinós, C. (2006) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-1-47 · Cited by 201
Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
Cavadini, P. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.3.217 · Cited by 197
Disabled early recruitment of antioxidant defenses in Friedreich's ataxia
Chantrel-Groussard, K. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.19.2061 · Cited by 189
Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
Gakh, O., Park, S., Liu, G., Macomber, L., Imlay, J. A., Ferreira, G. C., & Isaya, G. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi461 · Cited by 184
Iron–sulfur protein maturation in human cells: evidence for a function of frataxin
Stehling, O., Elsässer, H.-P., Brückel, B., Mühlenhoff, U., & Lill, R. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh324 · Cited by 176
Mitochondrial Production of Hydrogen Peroxide Regulation by Nitric Oxide and the Role of Ubisemiquinone
Boveris, A., & Cadenas, E. (2000) · IUBMB Life · doi:10.1080/713803732 · Cited by 171
Coenzyme Q 10 and vitamin E deficiency in Friedreich’s ataxia: predictor of efficacy of vitamin E and coenzyme Q 10 therapy
Cooper, J. A. D., Korlipara, L. V. P., Hart, P. E., Bradley, J. L., & Schapira, A. H. V. (2008) · European Journal of Neurology · doi:10.1111/j.1468-1331.2008.02318.x · Cited by 163
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
Actin Glutathionylation Increases in Fibroblasts of Patients with Friedreich's Ataxia
Pastore, A., Tozzi, G., Gaeta, L. M., Bertini, E., Serafini, V., Cesare, S. D., Bonetto, V., Casoni, F., Carrozzo, R., Federici, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301872200 · Cited by 161
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 154
Frataxin interacts functionally with mitochondrial electron transport chain proteins
González-Cabo, P., Vázquez-Manrique, R. P., García-Gimeno, M. A., Sanz, P., & Palau, F. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi214 · Cited by 140
Production of Superoxide Anions by Keratinocytes Initiates P. acnes-Induced Inflammation of the Skin
Grange, P., Chéreau, C., Raingeaud, J., Nicco, C., Weill, B. J., Dupin, N., & Batteux, F. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000527 · Cited by 140
Cell functions impaired by frataxin deficiency are restored by drug-mediated iron relocation
Kakhlon, O., Manning, H., Breuer, W. V., Melamed‐Book, N., Lu, C., Cortopassi, G. A., Münnich, A., & Cabantchik, Z. I. (2008) · Blood · doi:10.1182/blood-2008-06-161919 · Cited by 131
Iron Binding and Oxidation Kinetics in Frataxin CyaY of Escherichia coli
Bou‐Abdallah, F., Adinolfi, S., Pastore, A., Laue, T. M., & Chasteen, N. D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.072 · Cited by 129
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
Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase
Koutníková, H. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.9.1485 · Cited by 122
Permeability of bilayer lipid membranes for superoxide (O2−) radicals
Gus'kova, R. A., Ivanov, I. I., Koltover, V. K., Akhobadze, V. V., & Rubin, A. (1984) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(84)90409-7 · Cited by 112
Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia
Anderson, P. R., Kirby, K., Orr, W. C., Hilliker, A. J., & Phillips, J. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709691105 · Cited by 105
Hypersensitivity to oxygen and shortened lifespan in a Drosophila mitochondrial complex II mutant
Walker, D. W., Hájek, P., Muffat, J., Knoepfle, D., Cornelison, S., Attardi, G., & Benzer, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607918103 · Cited by 105
Reduction of Caenorhabditis elegans frataxin increases sensitivity to oxidative stress, reduces lifespan, and causes lethality in a mitochondrial complex II mutant
Vázquez‐Manrique, R. P., González‐Cabo, P., Ros, S., Aziz, H., Baylis, H. A., & Palau, F. (2005) · The FASEB Journal · doi:10.1096/fj.05-4212fje · Cited by 104
Recombinant human erythropoietin: effects on frataxin expression in vitro
Sturm, B., Stupphann, D., Kaun, C., Boesch, S., Schranzhofer, M., Wojta, J., Goldenberg, H., & Scheiber‐Mojdehkar, B. (2005) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2005.01568.x · Cited by 103
The Use of Transgenic and Mutant Mice to Study Oxygen Free Radical Metabolism
Huang, T., Carlson, E. J., Raineri, I., Gillespie, A. M., Kozy, H. M., & Epstein, C. J. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07820.x · Cited by 101
Assembly of Human Frataxin Is a Mechanism for Detoxifying Redox-Active Iron
O’Neill, H. A., Gakh, O., Park, S., Cui, J., Mooney, S. M., Sampson, M., Ferreira, G. C., & Isaya, G. (2004) · Biochemistry · doi:10.1021/bi048459j · Cited by 98
Frataxin, Iron–Sulfur Clusters, Heme, ROS, and Aging
Napoli, E., Taroni, F., & Cortopassi, G. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.506 · Cited by 96
Unique Iron Binding and Oxidation Properties of Human Mitochondrial Ferritin: A Comparative Analysis with Human H-chain Ferritin
Bou‐Abdallah, F., Santambrogio, P., Levi, S., Arosio, P., & Chasteen, N. D. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.007 · Cited by 96
Reduction of Hydrophilic Ubiquinones by the Flavin in Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) and Production of Reactive Oxygen Species
King, M. S., Sharpley, M. S., & Hirst, J. (2009) · Biochemistry · doi:10.1021/bi802282h · Cited by 95
Frataxin knockdown causes loss of cytoplasmic iron–sulfur cluster functions, redox alterations and induction of heme transcripts
Lu, C., & Cortopassi, G. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.09.010 · Cited by 94
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
The Ferroxidase Activity of Yeast Frataxin
Park, S., Gakh, O., Mooney, S. M., & Isaya, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206711200 · Cited by 88
Glutathione-dependent redox status of frataxin-deficient cells in a yeast model of Friedreich's ataxia
Auchère, F., Santos, R., Planamente, S., Lesuisse, E., & Camadro, J. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn178 · Cited by 87
Decreased expression of genes involved in sulfur amino acid metabolism in frataxin-deficient cells
Tan, G. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg187 · Cited by 86
Oxidative stress and protease dysfunction in the yeast model of Friedreich ataxia
Bulteau, A., Dancis, A., Gareil, M., Montagne, J.-J., Camadro, J., & Lesuisse, E. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.02.014 · Cited by 84
Frataxin expression rescues mitochondrial dysfunctions in FRDA cells
Tan, G. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.19.2099 · Cited by 82
Manganese superoxide dismutase induction by iron is impaired in Friedreich ataxia cells
Jiralerspong, S., Ge, B., Hudson, T. J., & Pandolfo, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03140-4 · Cited by 80
Friedreich's Ataxia: From Disease Mechanisms to Therapeutic Interventions
Lodi, R., Tonon, C., Calabrese, V., & Schapira, A. H. V. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.438 · Cited by 79
Frataxin deficiency enhances apoptosis in cells differentiating into neuroectoderm
Santos, M. M. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.18.1935 · Cited by 79
Friedreich's Ataxia, No Changes in Mitochondrial Labile Iron in Human Lymphoblasts and Fibroblasts
Sturm, B., Bistrich, U., Schranzhofer, M., Sarsero, J. P., Rauen, U., Scheiber-Mojdehkar, B., de Groot, H., Ioannou, P., & Petrat, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408717200 · Cited by 73
Structure of Frataxin Iron Cores: An X-ray Absorption Spectroscopic Study
Nichol, H., Gakh, O., O’Neill, H. A., Pickering, I. J., Isaya, G., & George, G. N. (2003) · Biochemistry · doi:10.1021/bi027021l · Cited by 68
The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin
Zanella, I., Derosas, M., Corrado, M., Cocco, E., Cavadini, P., Biasiotto, G., Poli, M., Verardi, R., & Arosio, P. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.11.006 · Cited by 60
Quality of potent Mn porphyrin-based SOD mimics and peroxynitrite scavengers for pre-clinical mechanistic/therapeutic purposes
Reboucas, J. S., Spasojević, I., & Batinic̈‐Haberle, I. (2008) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2008.08.005 · Cited by 59
Multicellular models of Friedreich ataxia
Puccio, H. M. (2009) · Journal of Neurology · doi:10.1007/s00415-009-1004-1 · Cited by 58
Impaired respiration is positively correlated with decreased life span in Caenorhabditis elegans models of Friedreich Ataxia
Zarse, K., Schulz, T. J., Birringer, M., & Ristow, M. (2007) · The FASEB Journal · doi:10.1096/fj.06-6994com · Cited by 58
Partial Correction of Sensitivity to Oxidant Stress in Friedreich Ataxia Patient Fibroblasts by Frataxin-Encoding Adeno-Associated Virus and Lentivirus Vectors
Fleming, J., Spinoulas, A., Zheng, M., Cunningham, S. C., Ginn, S. L., McQuilty, R. C., Rowe, P. B., & Alexander, I. E. (2005) · Human Gene Therapy · doi:10.1089/hum.2005.16.947 · Cited by 42
N-terminal iron-mediated self-cleavage of human frataxin: regulation of iron binding and complex formation with target proteins
Yoon, T., Dizin, E., & Cowan, J. A. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0205-2 · Cited by 41
Frataxin deficiency and mitochondrial dysfunction
Pandolfo, M. (2002) · Mitochondrion · doi:10.1016/s1567-7249(02)00039-9 · Cited by 39
Intreactions between superoxide and nitric oxide Implications in DNA damage and mutagenesis
Grisham, M. B. (1997) · Frontiers in bioscience · doi:10.2741/a182 · Cited by 39
Functional studies of frataxin
Isaya, G., O'Neill, H., Gakh, O., Park, S., Mantcheva, R., & Mooney, S. (2004) · Acta Paediatrica · doi:10.1111/j.1651-2227.2004.tb03061.x · Cited by 37
The chemical form of mitochondrial iron in Friedreich’s ataxia
Popescu, B. F. G., Pickering, I. J., George, G. N., & Nichol, H. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.03.004 · Cited by 36
Frataxin and frataxin deficiency in Friedreich's ataxia
Wilson, R. B. (2003) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(02)00432-x · Cited by 32
Mitochondrial superoxide anion production and release into intermembrane space
Han, D., Antunes, F., Daneri, F., & Cadenas, E. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)49341-x · Cited by 28

Sorted by citations

The Role of Oxidative Stress and Hypoxia in Pancreatic Beta-Cell Dysfunction in Diabetes Mellitus
Gerber, P. A., & Rutter, G. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6755 · Cited by 654
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
Ferroptosis and Its Role in Diverse Brain Diseases
Weiland, A., Wang, Y., Wu, W., Lan, X., Han, X., Li, Q., & Wang, J. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1403-3 · Cited by 473
Dysregulation of Glutathione Homeostasis in Neurodegenerative Diseases
Johnson, W. M., Wilson‐Delfosse, A. L., & Mieyal, J. J. (2012) · Nutrients · doi:10.3390/nu4101399 · Cited by 367
Mild dehydration impairs cognitive performance and mood of men
Ganio, M. S., Armstrong, L. E., Casa, D. J., McDermott, B. P., Lee, E. C., Yamamoto, L. M., Marzano, S., Lopez, R. M., Jimenez, L., Le Bellego, L., et al. (2011) · British Journal of Nutrition · doi:10.1017/s0007114511002005 · Cited by 316

See all 107

Authors: Armstrong, J. S., Khdour, O., & Hecht, S. M.
Affiliations: Arizona State University (US)
Corresponding author: Armstrong, Jeffrey S.
ORCID: Khdour, Omar
Hecht, Sidney M.
Venue: The FASEB Journal
Publisher: Wiley
Published: 2010-03-10
Volume: 24
Issue: 7
Pages: 2152-2163
ISSN: 0892-6638 (ISSN-L)
1530-6860
DOI: 10.1096/fj.09-143222
OpenAlex: W2032253254
Cited by: 107
References: 101
Citations by year: 2025: 1 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 8 · 2019: 6 · 2018: 11 · 2017: 5 · 2016: 6 · 2015: 4 · 2014: 11 · 2013: 13 · 2012: 16
FWCI: 1.30
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The FASEB Journal (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: Friedreich's ataxia, oxidative stress, frataxin, mitochondrial iron accumulation, reactive oxygen species, Fenton reaction, antioxidant therapy, neurodegeneration, heart failure, gene transcription
MeSH terms: Frataxin, Energy Metabolism, Friedreich Ataxia, Humans, Iron-Sulfur Proteins, Oxidation-Reduction, Oxidative Stress, Iron-Binding Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Does oxidative stress contribute to the pathology of Friedreich's ataxia? A radical question

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks