Cited by 255Mitochondrial Function and PathologyGenetic Neurodegenerative DiseasesNeurological diseases and metabolism

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia

Open access

Adamec, Jiri, Rusnak, Frank, Owen, Whyte G., Naylor, Stephen, Benson, Linda M., Gacy, A. Marquis, Isaya, Grazia·2000·The American Journal of Human Genetics

DOI 10.1086/303056PMC PMC1287515

Open this paper in CoChat — free account

Abstract

Frataxin deficiency is the primary cause of Friedreich ataxia (FRDA), an autosomal recessive cardiodegenerative and neurodegenerative disease. Frataxin is a nuclear-encoded mitochondrial protein that is widely conserved among eukaryotes. Genetic inactivation of the yeast frataxin homologue (Yfh1p) results in mitochondrial iron accumulation and hypersensitivity to oxidative stress. Increased iron deposition and evidence of oxidative damage have also been observed in cardiac tissue and cultured fibroblasts from patients with FRDA. These findings indicate that frataxin is essential for mitochondrial iron homeostasis and protection from iron-induced formation of free radicals. The functional mechanism of frataxin, however, is still unknown. We have expressed the mature form of Yfh1p (mYfh1p) in Escherichia coli and have analyzed its function in vitro. Isolated mYfh1p is a soluble monomer (13,783 Da) that contains no iron and shows no significant tendency to self-associate. Aerobic addition of ferrous iron to mYfh1p results in assembly of regular spherical multimers with a molecular mass of approximately 1. 1 MDa (megadaltons) and a diameter of 13+/-2 nm. Each multimer consists of approximately 60 subunits and can sequester >3,000 atoms of iron. Titration of mYfh1p with increasing iron concentrations supports a stepwise mechanism of multimer assembly. Sequential addition of an iron chelator and a reducing agent results in quantitative iron release with concomitant disassembly of the multimer, indicating that mYfh1p sequesters iron in an available form. In yeast mitochondria, native mYfh1p exists as monomer and a higher-order species with a molecular weight >600,000. After addition of (55)Fe to the medium, immunoprecipitates of this species contain >16 atoms of (55)Fe per molecule of mYfh1p. We propose that iron-dependent self-assembly of recombinant mYfh1p reflects a physiological role for frataxin in mitochondrial iron sequestration and bioavailability.

Integrity signals

Registry

Crossref · 10.1086/303056

Cites

34 of 34 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

We couldn’t retrieve this paper’s full text, 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?

Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.
Matsudaira, P. T. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61070-1 · Cited by 4,951
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
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
At least six nucleotides preceding the AUG initiator codon enhance translation in mammalian cells
Kozak, M. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90418-9 · Cited by 1,182
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
Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
Babcock, M., de Silva, D., Oaks, R., Davis-Kaplan, S., Jiralerspong, S., Montermini, L., Pandolfo, M., & Kaplan, J. (1997) · Science · doi:10.1126/science.276.5319.1709 · Cited by 921
Online Mendelian Inheritance in Man 'OMIM'.
Amladi, S. (2007) · PubMed · Cited by 871
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
Radicals r'aging
Wallace, D. C., & Melov, S. (1998) · Nature Genetics · doi:10.1038/448 · Cited by 548
Biomolecular Imaging with the Atomic Force Microscope
Hansma, H. G., & Hoh, J. H. (1994) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.23.060194.000555 · Cited by 540

Show all 34 references

Sorted by citations

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
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804
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
Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol
Richardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536
Ferritin, iron homeostasis, and oxidative damage1,2 1Guest Editor: Mario Comporti 2This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.
Arosio, P., & Levi, S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00842-0 · Cited by 553
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
Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases
Trushina, E. V., & McMurray, C. T. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2006.10.056 · Cited by 451
Mitochondrial processing peptidases
Gakh, O., Cavadini, P., & Isaya, G. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(02)00265-3 · Cited by 436
Self-citation
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
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
Frataxin Acts as an Iron Chaperone Protein to Modulate Mitochondrial Aconitase Activity
Bulteau, A.-L., O’Neill, H. A., Kennedy, M. C., Ikeda‐Saito, M., Isaya, G., & Szweda, L. I. (2004) · Science · doi:10.1126/science.1098991 · Cited by 372
Self-citation
Brain iron pathways and their relevance to Parkinson's disease
Berg, D., Gerlach, M., Youdim, M. B. H., Double, K. L., Zecca, L., Riederer, P., & Becker, G. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00608.x · Cited by 362
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
Neurodegenerative disorders associated with diabetes mellitus
Ristow, M. (2004) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0552-1 · Cited by 355
An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
Gerber, J., Mühlenhoff, U., & Lill, R. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor918 · Cited by 334
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
Iron trafficking in the mitochondrion: novel pathways revealed by disease
Napier, I. A., Ponka, P., & Richardson, D. R. (2004) · Blood · doi:10.1182/blood-2004-10-3856 · Cited by 291
Mitochondria and degenerative disorders
Orth, M., & Schapira, A. H. V. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1425 · Cited by 281
Oxidative stress and signal transduction in Saccharomyces cerevisiae: insights into ageing, apoptosis and diseases
Costa, V. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(01)00012-7 · Cited by 282
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
Oxidative Stress and the Homeodynamics of Iron Metabolism
Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247
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
Iron use for haeme synthesis is under control of the yeast frataxin homologue (Yfh1)
Lesuisse, E. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg096 · 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
Transcription of the Yeast Iron Regulon Does Not Respond Directly to Iron but Rather to Iron-Sulfur Cluster Biosynthesis
Chen, O. S., Crisp, R. J., Valachovic, M., Bard, M., Winge, D. R., & Kaplan, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403209200 · Cited by 202
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
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
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
Frataxin: a protein in search for a function
Pastore, A., & Puccio, H. M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12220 · Cited by 191
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
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
Self-citation
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
Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols
Parent, A., Elduque, X., Cornu, D., Belot, L., Caër, J. L., Grandas, A., Tolédano, M. B., & D’Autréaux, B. (2015) · Nature Communications · doi:10.1038/ncomms6686 · Cited by 176
Mitochondrial Control of Iron Homeostasis
Foury, F., & Talibi, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005804200 · Cited by 174
Deletion of the Mitochondrial Carrier Genes MRS3 andMRS4 Suppresses Mitochondrial Iron Accumulation in a Yeast Frataxin-deficient Strain
Foury, F., & Roganti, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111789200 · Cited by 171
The Structure and Function of Frataxin
Bencze, K. Z., Kondapalli, K. C., Cook, J. D., McMahon, S., Millán‐Pacheco, C., Pastor, N., & Stemmler, T. L. (2006) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230600846058 · Cited by 164
Yeast Frataxin Sequentially Chaperones and Stores Iron by Coupling Protein Assembly with Iron Oxidation
Park, S., Gakh, O., O’Neill, H. A., Mangravita, A., Nichol, H., Ferreira, G. C., & Isaya, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303158200 · Cited by 169
Self-citation
Yeast Frataxin Solution Structure, Iron Binding, and Ferrochelatase Interaction ,
He, Y., Alam, S. L., Proteasa, S. V., Zhang, Y., Lesuisse, E., Dancis, A., & Stemmler, T. L. (2004) · Biochemistry · doi:10.1021/bi0488193 · Cited by 157
The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
Huynen, M. A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.21.2463 · Cited by 157
Mammalian Frataxin Controls Sulfur Production and Iron Entry during de Novo Fe 4 S 4 Cluster Assembly
Colin, F., Martelli, A., Clémancey, M., Latour, J.-M., Gambarelli, S., Zeppieri, L., Birck, C., Page, A., Puccio, H., & Ollagnier de Choudens, S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja308736e · Cited by 148
Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis
Chen, O. S., Hemenway, S., & Kaplan, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192449599 · Cited by 152
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
Dysregulation of cellular iron metabolism in Friedreich ataxia: from primary iron-sulfur cluster deficit to mitochondrial iron accumulation
Martelli, A., & Puccio, H. M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00130 · Cited by 148
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
Human frataxin maintains mitochondrial iron homeostasis in Saccharomyces cerevisiae
Cavadini, P. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.17.2523 · Cited by 141
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
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
A structural approach to understanding the iron-binding properties of phylogenetically different frataxins
Adinolfi, S. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.16.1865 · Cited by 133
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
Monomeric Yeast Frataxin Is an Iron-Binding Protein
Cook, J. D., Bencze, K. Z., Janković, A., Crater, A. K., Busch, C. N., Bradley, P. B., Stemmler, A. J., Spaller, M. R., & Stemmler, T. L. (2006) · Biochemistry · doi:10.1021/bi060424r · Cited by 129
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
Self-citation
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
Self-citation
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
Assembly of Fe/S proteins in bacterial systems
Blanc, B., Gerez, C., & de Choudens, S. O. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.009 · Cited by 123
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
Mitochondrial functional interactions between frataxin and Isu1p, the iron–sulfur cluster scaffold protein, in Saccharomyces cerevisiae
Ramazzotti, A., Vanmansart, V., & Foury, F. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01498-4 · Cited by 116
Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe–S proteins and induces oxidative stress
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
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
Self-citation
How Escherichia coli and Saccharomyces cerevisiae Build Fe/S Proteins
Barras, F., Loiseau, L., & Py, B. (2005) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(05)50002-x · Cited by 111
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
The expression of human mitochondrial ferritin rescues respiratory function infrataxin-deficient yeast
Campanella, A. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh232 · Cited by 109
Does oxidative stress contribute to the pathology of Friedreich's ataxia? A radical question
Armstrong, J. S., Khdour, O., & Hecht, S. M. (2010) · The FASEB Journal · doi:10.1096/fj.09-143222 · Cited by 107
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
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
Frataxin deficiency alters heme pathway transcripts and decreases mitochondrial heme metabolites in mammalian cells
Schoenfeld, R. A., Napoli, E., Wong, A., Zhan, S. S., Reutenauer, L., Morin, D., Buckpitt, A. R., Taroni, F., Lönnerdal, B., Ristow, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi393 · Cited by 103
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
Friedreich's ataxia: Past, present and future
Marmolino, D. (2011) · Brain Research Reviews · doi:10.1016/j.brainresrev.2011.04.001 · Cited by 106
Reduction in frataxin causes progressive accumulation of mitochondrial damage
Karthikeyan, G. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg349 · Cited by 102
Iron and its sensitive balance in the cell
Freitas, J. M. D., & Meneghini, R. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00066-5 · Cited by 101
Iron in neurodegenerative disorders
Berg, D., Becker, G., Riederer, P. F., & Rieß, O. (2002) · Neurotoxicity Research · doi:10.1080/1029842021000045444 · Cited by 98
Mrs3p, Mrs4p, and Frataxin Provide Iron for Fe-S Cluster Synthesis in Mitochondria
Zhang, Y., Lyver, E. R., Knight, S. A. B., Pain, D., Lesuisse, E., & Dancis, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604246200 · Cited by 98
FDXR mutations cause sensorial neuropathies and expand the spectrum of mitochondrial Fe-S-synthesis diseases
Paul, A., Drecourt, A., Petit, F., Deguine, D. D., Vasnier, C., Oufadem, M., Masson, C., Bonnet, C., Masmoudi, S., Mosnier, I., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.09.007 · Cited by 95
Mechanism of activation of the human cysteine desulfurase complex by frataxin
Patra, S., & Barondeau, D. P. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1909535116 · Cited by 90
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
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
Self-citation
Biogenesis of Iron–Sulfur Clusters and Their Role in DNA Metabolism
Shi, R., Hou, W., Wang, Z., & Xu, X. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.735678 · Cited by 91
The Role of Iron in Friedreich’s Ataxia: Insights From Studies in Human Tissues and Cellular and Animal Models
Llorens, J. V., Soriano, S., Calap-Quintana, P., González‐Cabo, P., & Moltó, M. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00075 · Cited by 87
Friedreich's Ataxia: Disease mechanisms, antioxidant and Coenzyme Q10therapy
Cooper, J. A. D., & Schapira, A. H. V. (2003) · BioFactors · doi:10.1002/biof.5520180219 · Cited by 86
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
The Structures of Frataxin Oligomers Reveal the Mechanism for the Delivery and Detoxification of Iron
Karlberg, T., Schagerlöf, U., Gakh, O., Park, S., Ryde, U., Lindahl, M., Leath, K., Garman, E., Isaya, G., & Al-Karadaghi, S. (2006) · Structure · doi:10.1016/j.str.2006.08.010 · Cited by 85
Self-citation
Mitochondrial dysfunction induced by frataxin deficiency is associated with cellular senescence and abnormal calcium metabolism
Bolinches-AmorÃ³s, A., Mollá, B., Pla‐Martín, D., Palau, F., & González‐Cabo, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00124 · Cited by 89
Frataxin expression rescues mitochondrial dysfunctions in FRDA cells
Tan, G. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.19.2099 · Cited by 82
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
Acidic residues of yeast frataxin have an essential role in Fe–S cluster assembly
Foury, F., Pastore, A., & Trincal, M. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400881 · Cited by 81
Mitochondrial ABC transporters
Lill, R., & Kispál, G. (2001) · Research in Microbiology · doi:10.1016/s0923-2508(01)01204-9 · Cited by 79
Frataxin promotes antioxidant defense in a thiol-dependent manner resulting in diminished malignant transformation in vitro
Shoichet, S. A. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.7.815 · Cited by 78
Friedreich's ataxia: Oxidative stress and cytoskeletal abnormalities
Sparaco, M., Gaeta, L. M., Santorelli, F. M., Passarelli, C., Tozzi, G., Bertini, E., Simonati, A., Scaravilli, F., Taroni, F., Duyckaerts, C. J., et al. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2009.08.052 · Cited by 76
Normal and Friedreich Ataxia Cells Express Different Isoforms of Frataxin with Complementary Roles in Iron-Sulfur Cluster Assembly
Gakh, O., Bedekovics, T., Duncan, S. F., Smith, D. Y., Berkholz, D. S., & Isaya, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145144 · Cited by 76
Self-citation
Human frataxin: iron and ferrochelatase binding surface
Bencze, K. Z., Yoon, T., Millán‐Pacheco, C., Bradley, P. B., Pastor, N., Cowan, J. A., & Stemmler, T. L. (2007) · Chemical Communications · doi:10.1039/b703195e · Cited by 75
Advancements in the pathophysiology of Friedreich’s Ataxia and new prospects for treatments
Babady, N. E., Carelle, N., Wells, R. D., Rouault, T. A., Hirano, M., Lynch, D. R., Delatycki, M. B., Wilson, R. B., Isaya, G., & Puccio, H. (2007) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2007.05.009 · Cited by 73
Self-citation
Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization
Becker, E., Greer, J. M., Ponka, P., & Richardson, D. R. (2002) · Blood · doi:10.1182/blood.v99.10.3813 · Cited by 74
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
Understanding the genetic and molecular pathogenesis of Friedreich’s ataxia through animal and cellular models
Martelli, A., Напиерала, М., & Puccio, H. M. (2012) · Disease Models & Mechanisms · doi:10.1242/dmm.008706 · Cited by 80
Friedreich?s ataxia: iron chelators that target the mitochondrion as a therapeutic strategy?
Richardson, D. R. (2003) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.12.2.235 · Cited by 71
Drosophila Frataxin: An Iron Chaperone during Cellular Fe−S Cluster Bioassembly
Kondapalli, K. C., Kok, N. M., Dancis, A., & Stemmler, T. L. (2008) · Biochemistry · doi:10.1021/bi800366d · Cited by 70
Routine preparation of air-dried negatively stained and unstained specimens on holey carbon support films: a review of applications
Harris, J. R., & Scheffler, D. (2002) · Micron · doi:10.1016/s0968-4328(01)00039-7 · Cited by 70
The complex clinical and genetic classification of inherited ataxias. II. Autosomal recessive ataxias
Donato, S. D., Gellera, C., & Mariotti, C. (2001) · Neurological Sciences · doi:10.1007/s100720100017 · Cited by 69

Authors: Adamec, J., Rusnak, F., Owen, W. G., Naylor, S., Benson, L. M., Gacy, A. M., & Isaya, G.
Affiliations: University of Minnesota Rochester (US)
Mayo Clinic (US)
Corresponding author: Isaya, Grazia
ORCID: Naylor, Stephen
Isaya, Grazia
Venue: The American Journal of Human Genetics
Publisher: Elsevier BV
Published: 2000-09
Volume: 67
Issue: 3
Pages: 549-562
ISSN: 0002-9297 (ISSN-L)
DOI: 10.1086/303056
PMC: PMC1287515
OpenAlex: W2080731376
Cited by: 255
References: 34
Citations by year: 2026: 3 · 2025: 4 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 5 · 2020: 5 · 2019: 10 · 2018: 6 · 2017: 9 · 2016: 8 · 2015: 7 · 2014: 9 · 2013: 10 · 2012: 6
FWCI: 8.08
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4704 d)
Locations: The American Journal of Human Genetics (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG-15709, R01AG015709)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Keywords: frataxin, Friedreich's ataxia, mitochondrial iron homeostasis, iron sequestration, iron chelation, oxidative stress, iron bioavailability, recombinant protein expression
MeSH terms: Frataxin, Chromatography, Gel, Escherichia coli, Friedreich Ataxia, Homeostasis, Humans, Iron, Iron Chelating Agents, Microscopy, Electron, Mitochondria, Models, Biological, Molecular Sequence Data, Molecular Weight, Protein Binding, Recombinant Proteins, Saccharomyces cerevisiae, Solubility, Phosphotransferases (Alcohol Group Acceptor), Oxidative Stress, Microscopy, Atomic Force, Reducing Agents, Protein Structure, Quaternary, 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

Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia

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