The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Inactivation of the Friedreich ataxia mouse gene leads to early embryonic lethality without iron accumulation
Abstract
Friedreich ataxia (FRDA), the most common autosomal recessive ataxia, is caused in almost all cases by homozygous intronic expansions resulting in the loss of frataxin, a mitochondrial protein conserved through evolution, and involved in mitochondrial iron homeostasis. Yeast knockout models, and histological and biochemical data from patient heart biopsies or autopsies indicate that the frataxin defect causes a specific iron-sulfur protein deficiency and mitochondrial iron accumulation leading to the pathological changes. Affected human tissues are rarely available to further examine this hypothesis. To study the mechanism of the disease, we generated a mouse model by deletion of exon 4 leading to inactivation of the Frda gene product. We show that homozygous deletions cause embryonic lethality a few days after implantation, demonstrating an important role for frataxin during early development. These results suggest that the milder phenotype in humans is due to residual frataxin expression associated with the expansion mutations. Surprisingly, in the frataxin knockout mouse, no iron accumulation was observed during embryonic resorption, suggesting that cell death could be due to a mechanism independent of iron accumulation.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In the citing paper
“Studies in the liver demonstrated that C/EBPα plays a role in the iron-mediated regulation of hepcidin mRNA (58).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [58]
In the citing paper
“levels of C/EBPα transcription factor in murine liver are doubled in response to iron loading,”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [58]
In the citing paper
“mice deficient in C/EBPα exhibited lower levels of hepcidin mRNA,”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [58]
In the citing paper
“suggesting that C/EBPα modulates hepcidin transcription (58).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [58]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
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
Lantos, P. L. (1985) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.48.5.496 · Cited by 1,156
Clinical and Genetic Abnormalities in Patients with Friedreich's Ataxia
Dürr, A., Cossee, M., Agid, Y., Campuzano, V., Mignard, C., Penet, C., Mandel, J.-L., Brice, A., & Koenig, M. (1996) · New England Journal of Medicine · doi:10.1056/nejm199610173351601 · Cited by 1,071
Harding, A. E. (1981) · Brain · doi:10.1093/brain/104.3.589 · Cited by 929
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
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
Schrank, B., Götz, R., Gunnersen, J. M., Ure, J., Toyka, K. V., Smith, A. G., & Sendtner, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9920 · Cited by 661
Filla, A., Michele, G. D., Cavalcanti, F., Pianese, L., Monticelli, A., Campanella, G., & Cocozza, S. (1996) · PubMed Central · Cited by 487
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
Research works printed but not linked: 1
- Dierich, A. and Dollé, P. (1997) In Klug, S. and Thiel, R. (eds), Methods in Developmental Toxicology and Biology. Blackwell Science, Oxford, UK, pp. 111-123.
Cited by
Sorted by citations
Trinucleotide Repeat Disorders
Orr, H. T., & Zoghbi, H. Y. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.113042 · Cited by 1,394
Diseases of Unstable Repeat Expansion: Mechanisms and Common Principles
Gatchel, J. R., & Zoghbi, H. Y. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1691 · Cited by 802
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
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 605
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
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
Davies, V. J., Hollins, A. J., Piechota, M. J., Yip, W., Davies, J. R., White, K. E., Nicols, P. P., Boulton, M. E., & Votruba, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm079 · Cited by 449
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
The Role of Mitochondrial DNA Copy Number in Mammalian Fertility1
Wai, T., Ao, A., Zhang, X., Cyr, D. G., Dufort, D., & Shoubridge, E. A. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.109.080887 · Cited by 443
Iron uptake and metabolism in the new millennium
Dunn, L., Rahmanto, Y. S., & Richardson, D. R. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.12.003 · Cited by 423
Iron homeostasis: insights from genetics and animal models
Andrews, N. C. (2000) · Nature Reviews Genetics · doi:10.1038/35042073 · Cited by 425
Oxidative stress, mitochondrial dysfunction and cellular stress response in Friedreich's ataxia
Calabrese, V., Lodi, R., Tonon, C., D’Agata, V., Sapienza, M. A., Scapagnini, G., Mangiameli, A., Pennisi, G., Stella, A. M. G., & Butterfield, D. A. (2005) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2005.03.012 · Cited by 411
Lane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399
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
Iron-Sulfur Protein Biogenesis in Eukaryotes: Components and Mechanisms
Lill, R., & Mühlenhoff, U. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104538 · Cited by 365
Yoon, T., & Cowan, J. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja027967i · Cited by 353
Neurodegenerative disorders associated with diabetes mellitus
Ristow, M. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0552-1 · Cited by 355
The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
Mühlenhoff, U. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.17.2025 · Cited by 326
Eid, R., Arab, N. T. T., & Greenwood, M. T. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.12.002 · Cited by 297
Clinical features and molecular genetics of autosomal recessive cerebellar ataxias
Fogel, B. L., & Perlman, S. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70054-6 · Cited by 299
Mitochondrial iron–sulfur protein biogenesis and human disease
Stehling, O., Wilbrecht, C., & Lill, R. (2014) · Biochimie · doi:10.1016/j.biochi.2014.01.010 · Cited by 272
Friedreich Ataxia: Neuropathology Revised
Koeppen, A. H., & Mazurkiewicz, J. E. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31827e5762 · Cited by 273
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
Idebenone and reduced cardiac hypertrophy in Friedreich's ataxia
HAUSSE, A., Aggoun, Y., Bonnet, D., Sidi, D., Münnich, A., Rötig, A., & Rustin, P. (2002) · Heart · doi:10.1136/heart.87.4.346 · Cited by 251
Al‐Mahdawi, S., Pinto, R. M., Varshney, D., Lawrence, L., Lowrie, M. B., Hughes, S., Webster, Z., Blake, J. C., Cooper, J. A. D., King, R. H. M., et al. (2006) · Genomics · doi:10.1016/j.ygeno.2006.06.015 · Cited by 240
Identification of Frataxin as a regulator of ferroptosis
Du, J., Zhou, Y., Li, Y., Xia, J., Chen, Y., Chen, S., Wang, X., Sun, W., Wang, T., Ren, X., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101483 · Cited by 243
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
Crystal Structure of Human Frataxin
Dhe-Paganon, S., Shigeta, R., Chi, Y.-I., Ristow, M., & Shoelson, S. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000407200 · Cited by 226
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
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
Maio, N., & Rouault, T. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.009 · Cited by 222
Simon, D., Seznec, H., Gansmuller, A., Carelle, N., Weber, P., Metzger, D., Rustin, P., Koenig, M., & Puccio, H. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4549-03.2004 · Cited by 205
Singh, N., Haldar, S., Tripathi, A. K., Horback, K., Wong, J., Sharma, D., Beserra, A., Suda, S., Anbalagan, C., Dev, S., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4931 · Cited by 208
Pathways to motor incoordination: the inherited ataxias
Taroni, F., & DiDonato, S. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1474 · Cited by 207
Autosomal recessive cerebellar ataxias
Palau, F., & Espinós, C. (2006) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-1-47 · Cited by 201
Mitochondrial Iron in Human Health and Disease
Ward, D. M., & Cloonan, S. M. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114742 · Cited by 208
Friedreich Ataxia: Molecular Mechanisms, Redox Considerations, and Therapeutic Opportunities
Santos, R., Lefevre, S. D., Sliwa, D., Seguin, A., Camadro, J., & Lesuisse, E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3015 · 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
Trinucleotide repeats and neurodegenerative disease
Everett, C. M. (2004) · Brain · doi:10.1093/brain/awh278 · Cited by 182
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 186
Iron Overload, Oxidative Stress, and Ferroptosis in the Failing Heart and Liver
Mancardi, D., Mezzanotte, M., Arrigo, E., Barinotti, A., & Roetto, A. (2021) · Antioxidants · doi:10.3390/antiox10121864 · Cited by 188
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
Miranda, C. J., Santos, M. M., Ohshima, K., Smith, J., Li, L., Bunting, M., Cossée, M., Koenig, M., Sequeiros, J., Kaplan, J., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02251-2 · Cited by 172
Self-citationFriedreich ataxia- pathogenesis and implications for therapies
Delatycki, M. B., & Bidichandani, S. I. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104606 · Cited by 168
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 167
Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis
Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 165
Hypoxia Rescues Frataxin Loss by Restoring Iron Sulfur Cluster Biogenesis
Ast, T., Meisel, J. D., Patra, S., Wang, H., Grange, R. M. H., Kim, S. H., Calvo, S. E., Orefice, L. L., Nagashima, F., Ichinose, F., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.045 · Cited by 160
Friedreich Ataxia: current status and future prospects
Bürk, K. (2017) · Cerebellum & Ataxias · doi:10.1186/s40673-017-0062-x · Cited by 162
Martelli, A., & Puccio, H. M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00130 · Cited by 148
PGC-1alpha Down-Regulation Affects the Antioxidant Response in Friedreich's Ataxia
Marmolino, D., Manto, M. U., Acquaviva, F., Vergara, P., Ravella, A., Monticelli, A., & Pandolfo, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010025 · Cited by 152
RNAi-mediated suppression of the mitochondrial iron chaperone, frataxin, in Drosophila
Anderson, P. R., Kirby, K., Hilliker, A. J., & Phillips, J. P. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi367 · Cited by 144
Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities
Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 149
Seznec, H. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh114 · Cited by 138
Solution Structure of the Bacterial Frataxin Ortholog, CyaY
Nair, M. M., Adinolfi, S., Pastore, C., Kelly, G. P., Temussi, P., & Pastore, A. (2004) · Structure · doi:10.1016/j.str.2004.08.012 · Cited by 138
The genetics of essential metal homeostasis during development
Kambe, T., Weaver, B. P., & Andrews, G. K. (2008) · genesis · doi:10.1002/dvg.20382 · Cited by 140
Adinolfi, S. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.16.1865 · Cited by 133
Frataxin deficiency in pancreatic islets causes diabetes due to loss of β cell mass
Ristow, M., Mulder, H., Pomplun, D., Schulz, T. J., Schmehl, K., Krause, A., Fex, M., Puccio, H. M., Müller, J., Isken, F., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18107 · 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
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
Friedreich Ataxia: From GAA Triplet–Repeat Expansion to Frataxin Deficiency
Patel, P. I., & Isaya, G. (2001) · The American Journal of Human Genetics · doi:10.1086/321283 · Cited by 126
Iron–sulfur cluster synthesis, iron homeostasis and oxidative stress in Friedreich ataxia
Vaubel, R. A., & Isaya, G. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.08.003 · Cited by 123
Causative role of oxidative stress in a Drosophila model of Friedreich ataxia
Llorens, J. V., Navarro, J. A., Martínez-Sebastián, M. J., Baylies, M. K., Schneuwly, S., Botella, J., & Moltó, M. D. (2006) · The FASEB Journal · doi:10.1096/fj.05-5709com · Cited by 123
Lynch, D. R., Farmer, J. M., Balcer, L. J., & Wilson, R. B. (2002) · Archives of Neurology · doi:10.1001/archneur.59.5.743 · Cited by 122
In vivo maturation of human frataxin
Condò, I., Ventura, N., Malisan, F., Rufini, A., Tomassini, B., & Testi, R. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm102 · Cited by 118
A non-essential function for yeast frataxin in iron-sulfur cluster assembly
Duby, G. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2635 · Cited by 117
Sandi, C., Pinto, R. M., Al‐Mahdawi, S., Ezzatizadeh, V., Barnes, G., Jones, S. E., Rusche, J. R., Gottesfeld, J. M., & Pook, M. A. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.02.016 · Cited by 118
Busi, M. V., Maliandi, M. V., Valdez, H., Clemente, M., Zabaleta, E. J., Araya, A., & Gomez‐Casati, D. F. (2006) · The Plant Journal · doi:10.1111/j.1365-313x.2006.02923.x · Cited by 115
Iron: A New Target for Pharmacological Intervention in Neurodegenerative Diseases
Whitnall, M., & Richardson, D. R. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.008 · Cited by 113
Two-step Processing of Human Frataxin by Mitochondrial Processing Peptidase
Cavadini, P., Adamec, J., Taroni, F., Gakh, O., & Isaya, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006539200 · Cited by 114
Friedreich ataxia: a paradigm for mitochondrial diseases
Puccio, H. M., & Koenig, M. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00298-8 · Cited by 111
Mitochondrial iron-sulfur cluster dysfunction in neurodegenerative disease
Isaya, G. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00029 · Cited by 109
Vyas, P. M., Tomamichel, W. J., Pride, P. M., Babbey, C. M., Wang, Q., Mercier, J., Martin, E. M., & Payne, R. M. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr554 · Cited by 115
Mammalian Fe–S cluster biogenesis and its implication in disease
Beilschmidt, L. K., & Puccio, H. M. (2014) · Biochimie · doi:10.1016/j.biochi.2014.01.009 · Cited by 113
Cardiomyopathy in Friedreich Ataxia
Payne, R. M., & Wagner, G. R. (2012) · Journal of Child Neurology · doi:10.1177/0883073812448535 · Cited by 106
Jauslin, M. L. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.24.3055 · Cited by 106
Friedreich's ataxia: Past, present and future
Marmolino, D. (2011) · Brain Research Reviews · doi:10.1016/j.brainresrev.2011.04.001 · Cited by 106
Mitochondrial iron metabolism and its role in diseases
Gao, J., Zhou, Q., Wu, D., & Chen, L. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.12.005 · Cited by 111
Reduction in frataxin causes progressive accumulation of mitochondrial damage
Karthikeyan, G. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg349 · Cited by 102
The role of oxidative stress in Friedreich's ataxia
Lupoli, F., Vannocci, T., Longo, G., Niccolai, N., & Pastore, A. (2017) · FEBS Letters · doi:10.1002/1873-3468.12928 · Cited by 102
Inducible and reversible phenotypes in a novel mouse model of Friedreich’s Ataxia
Chandran, V., Gao, K., Swarup, V., Versano, R., Dong, H., Jordan, M. C., & Geschwind, D. H. (2017) · eLife · doi:10.7554/elife.30054 · Cited by 103
Central role and mechanisms of β‐cell dysfunction and death in friedreich ataxia–associated diabetes
Cnop, M., Igoillo‐Esteve, M., Rai, M., Corroller, A. B., Serroukh, Y. I. M., Depondt, C., Musuaya, A., Marhfour, I., Ladrière, L., Lopez, X. M., et al. (2012) · Annals of Neurology · doi:10.1002/ana.23698 · Cited by 108
GAA repeat instability in Friedreich ataxia YAC transgenic mice
Al‐Mahdawi, S., Pinto, R. M., Ruddle, P., Carroll, C. J., Webster, Z., & Pook, M. A. (2004) · Genomics · doi:10.1016/j.ygeno.2004.04.003 · Cited by 99
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
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
Modelling brain diseases in mice: the challenges of design and analysis
Watase, K., & Zoghbi, H. Y. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1045 · Cited by 94
Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers
Roy, C. N. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.20.2181 · Cited by 96
Mitochondrial pathophysiology in Friedreich's ataxia
González‐Cabo, P., & Palau, F. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12303 · Cited by 99
A Pool of Extramitochondrial Frataxin That Promotes Cell Survival
Condò, I., Ventura, N., Malisan, F., Tomassini, B., & Testi, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511960200 · Cited by 90
Long-lived C. elegans Mitochondrial mutants as a model for human mitochondrial-associated diseases
Ventura, N., Rea, S. L., & Testi, R. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.06.060 · Cited by 92
Reversible Axonal Dystrophy by Calcium Modulation in Frataxin-Deficient Sensory Neurons of YG8R Mice
Mollá, B., Muñoz-Lasso, D. C., Riveiro, F., Bolinches-Amorós, A., Pallardó, F. V., Fernandez-Vilata, A., de la Iglesia-Vayá, M., Palau, F., & González‐Cabo, P. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00264 · Cited by 87
Cytopathies involving mitochondrial complex II
Ackrell, B. A. C. (2002) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(02)00012-2 · Cited by 86
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
Kime, C., Kiyonari, H., Ohtsuka, S., Kohbayashi, E., Asahi, M., Yamanaka, S., Takahashi, M., & Tomoda, K. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.07.011 · Cited by 87
The mitochondrial protein frataxin prevents nuclear damage
Karthikeyan, G. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.11.1351 · Cited by 86
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
Molecular Mechanisms and Regulation of Iron Transport
Chung, J., & Wessling‐Resnick, M. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609332 · Cited by 86
Animal and cellular models of Friedreich ataxia
Perdomini, M., Hick, A., Puccio, H. M., & Pook, M. A. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12219 · Cited by 92
Frataxin expression rescues mitochondrial dysfunctions in FRDA cells
Tan, G. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.19.2099 · Cited by 82
The crosstalk between mitochondrial quality control and metal-dependent cell death
Zhou, Q.-Y., Ren, C., Li, J., Wang, L., Duan, Y., Yao, R.-Q., Tian, Y., & Yao, Y.-M. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06691-w · Cited by 90
Rescue of the Friedreich's ataxia knockout mouse by human YAC transgenesis
Pook, M. A., Al‐Mahdawi, S., Carroll, C. J., Cossée, M., Puccio, H. M., Lawrence, L., Clark, P. A., Lowrie, M. B., Bradley, J. L., Cooper, M. J., et al. (2001) · Neurogenetics · doi:10.1007/s100480100118 · Cited by 86
Metadata
- Authors
- Cossee, M.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2000-05-01
- Volume
- 9
- Issue
- 8
- Pages
- 1219-1226
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2114190171
- Cited by
- 377
- References
- 23
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 11 · 2023: 9 · 2022: 8 · 2021: 11 · 2020: 10 · 2019: 11 · 2018: 16 · 2017: 16 · 2016: 6 · 2015: 11 · 2014: 20 · 2013: 25 · 2012: 19
- FWCI
- 8.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Muscular Dystrophy Association
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- 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 › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- Friedreich's ataxia, frataxin, embryonic lethality, iron-sulfur proteins, mitochondrial iron homeostasis, iron accumulation, mouse model, cell death mechanisms
- MeSH terms
- Frataxin, Animals, Decidua, Embryo, Mammalian, Exons, Female, Fetal Death, Friedreich Ataxia, Genotype, Homozygote, Humans, Introns, Iron, Iron-Sulfur Proteins, Necrosis, Phenotype, Pregnancy, Apoptosis, Phosphotransferases (Alcohol Group Acceptor), Mice, Knockout, Iron-Binding Proteins, Mice
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
