Towards a structural understanding of Friedreich’s ataxia: the solution structure of frataxin

Musco, Giovanna; Stier, Gunter; Kolmerer, Bernhard; Adinolfi, Salvatore; Martin, Stephen; Frenkiel, Tom; Gibson, Toby; Pastore, Annalisa

doi:10.1016/s0969-2126(00)00158-1

Cited by 166Genetic Neurodegenerative DiseasesProtein Structure and DynamicsEnzyme Structure and Function

Towards a structural understanding of Friedreich’s ataxia: the solution structure of frataxin

Open access

Musco, Giovanna, Stier, Gunter, Kolmerer, Bernhard, Adinolfi, Salvatore, Martin, Stephen, Frenkiel, Tom, Gibson, Toby, Pastore, Annalisa·2000·Structure

DOI 10.1016/s0969-2126(00)00158-1

Open this paper in CoChat — free account Open PDF

Abstract

Background Lesions in the gene for frataxin, a nuclear-encoded mitochondrial protein, cause the recessively inherited condition Friedreich's ataxia. It is thought that the condition arises from disregulation of mitochondrial iron homeostasis, with concomitant oxidative damage leading to neuronal death. Very little is, as yet, known about the biochemical function of frataxin. Results Here, we show that the mature form of recombinant frataxin behaves in solution as a monodisperse species that is composed of a 15-residue-long unstructured N terminus and an evolutionarily conserved C-terminal region that is able to fold independently. The structure of the C-terminal domain consists of a stable seven-stranded antiparallel beta sheet packing against a pair of parallel helices. The structure is compact with neither grooves nor cavities, features that are typical of iron-binding modules. Exposed evolutionarily conserved residues cover a broad area and all cluster on the beta-sheet face of the structure, suggesting that this is a functionally important surface. The effect of two clinically occurring mutations on the fold was checked experimentally. When the mature protein was titrated with iron, no tendency to iron-binding or to aggregation was observed. Conclusions Knowledge of the frataxin structure provides important guidelines as to the nature of the frataxin binding partner. The absence of all the features expected for an iron-binding activity, the large conserved area on its surface and lack of evidence for iron-binding activity strongly support an indirect involvement of frataxin in iron metabolism. The effects of point mutations associated with Friedreich's ataxia can be rationalised by knowledge of the structure and suggest possible models for the occurrence of the disease in compound heterozygous patients.

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

Crossref · 10.1016/s0969-2126(00)00158-1

Cites

51 of 51 references verified0 citation errors · 0 not checkable

Statistics

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?

Hepcidin negatively regulates iron efflux by binding Fpn and triggering its internalization and subsequent degradation.
“It negatively regulates iron efflux by binding Fpn and triggering its internalization and subsequent degradation (215).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [215]
Fpn is posttranslationally regulated by the peptide hormone hepcidin.
“Fpn is posttranslationally regulated by a peptide hormone, hepcidin (215).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [215]
Overexpression of Fpn accelerates export of cytosolic iron.
“Over-expression of Fpn accelerates export of cytosolic iron (215)”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [215]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
Thompson, J. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.24.4876 · Cited by 39,119 · see citing works
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502 · see citing works
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 3,479 · see citing works
WHAT IF: A molecular modeling and drug design program
Vriend, G. (1990) · Journal of Molecular Graphics · doi:10.1016/0263-7855(90)80070-v · Cited by 3,476 · see citing works
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 · see citing works
Torsion angle dynamics for NMR structure calculation with the new program Dyana
Güntert, P., Mumenthaler, C., & Kurt Wüthrich, A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1284 · Cited by 2,781 · see citing works
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667 · see citing works
Recognition of errors in three‐dimensional structures of proteins
Sippl, M. J. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340170404 · Cited by 2,156 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Frataxin is Reduced in Friedreich Ataxia Patients and is Associated with Mitochondrial Membranes
Campuzano, V., Montermini, L., Lutz, Y., Cova, L., Hindelang, C., Jiralerspong, S., Trottier, Y., Kish, S. J., Faucheux, B. A., Trouillas, P., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.11.1771 · Cited by 739 · see citing works
The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699 · see citing works
The relationship between trinucleotide (GAA) repeat length and clinical features in Friedreich ataxia.
Filla, A., Michele, G. D., Cavalcanti, F., Pianese, L., Monticelli, A., Campanella, G., & Cocozza, S. (1996) · PubMed Central · Cited by 487 · see citing works
Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
Koutníková, H., Campuzano, V., Foury, F., Dollé, P., Cazzalini, O., & Koenig, M. (1997) · Nature Genetics · doi:10.1038/ng0897-345 · Cited by 473 · see citing works
Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin 1 1Edited by P. E. Wright
Nilges, M., Macías, M. J., O’Donoghue, S. I., & Oschkinat, H. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1044 · Cited by 427 · see citing works
Mutation of a Putative Mitochondrial Iron Transporter Gene (ABC7) in X-Linked Sideroblastic Anemia and Ataxia (XLSA/A)
Allikmets, R. L., Raskind, W. H., Hutchinson, A. A., Schueck, N. D., Dean, M. C., & Koeller, D. M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.5.743 · Cited by 406 · see citing works
Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
Foury, F., & Cazzalini, O. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00734-5 · Cited by 378 · see citing works
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 · see citing works
Effect of idebenone on cardiomyopathy in Friedreich's ataxia: a preliminary study
Rustin, P., von Kleist-Retzow, J., Chantrel-Groussard, K., Sidi, D., Münnich, A., & Rötig, A. (1999) · The Lancet · doi:10.1016/s0140-6736(99)01341-0 · Cited by 348 · see citing works
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 · see citing works
Mapping of mutation causing Friedreich's ataxia to human chromosome 9
Chamberlain, S., Shaw, J., Rowland, A., Wallis, J., South, S., Nakamura, Y., von Gabain, A., Farrall, M., & Williamson, R. (1988) · Nature · doi:10.1038/334248a0 · Cited by 317 · see citing works
Transverse Relaxation-Optimized Spectroscopy (TROSY) for NMR Studies of Aromatic Spin Systems in 13C-Labeled Proteins
Pervushin, K. V., Riek, R., Wider, G., & Kurt Wüthrich, A. (1998) · Journal of the American Chemical Society · doi:10.1021/ja980742g · Cited by 311 · see citing works
Immunohistochemical and subcellular localization of parkin protein: Absence of protein in autosomal recessive juvenile parkinsonism patients
Shimura, H., Hattori, N., Kubo, S., Yoshikawa, M., Kitada, T., Matsumine, H., Asakawa, S., Minoshima, S., Yamamura, Y., Shimizu, N., et al. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199905)45:5 · Cited by 282 · see citing works
The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site.
Chiancone, E., Ilari, A., Stefanini, S., & Tsernoglou, D. (2000) · Nature Structural Biology · doi:10.1038/71236 · Cited by 279 · see citing works
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 · see citing works
Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein
Jiang, J., Zhang, Y., Krainer, A. R., & Xu, R.-M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3572 · Cited by 253 · see citing works
The Cardiomyopathy of Friedreich's Ataxia Morphological Observations in 3 Cases
Lamarche, J. B., Côté, M., & Lemieux, B. (1980) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100022927 · Cited by 189 · see citing works
The complex pathology of trinucleotide repeats
Reddy, P. S., & Housman, D. E. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80009-9 · Cited by 187 · see citing works
Friedreich's ataxia protein: phylogenetic evidence for mitochondrial dysfunction
Gibson, T. J., Koonin, E. V., Musco, G., Pastore, A., & Peer Bork, B. (1996) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)20054-2 · Cited by 159 · see citing works
Self-citation
Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion.
Bidichandani, S. I., Ashizawa, T., & Patel, P. I. (1997) · Europe PMC (PubMed Central) · Cited by 141 · see citing works
Handbook of cerebellar diseases
Lechtenberg, R. J. (1993) · M. Dekker eBooks · Cited by 128 · see citing works
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 · see citing works
Floating stereospecific assignment revisited: Application to an 18 kDa protein and comparison with J-coupling data
Folmer, R. H. A., Hilbers, C. W., Konings, R. N. H., & Nilges, M. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018670623695 · Cited by 110 · see citing works
Molecular Pathogenesis of Friedreich Ataxia
Pandolfo, M. (1999) · Archives of Neurology · doi:10.1001/archneur.56.10.1201 · Cited by 108 · see citing works
Knock‐out of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants
Li, D. S., Ohshima, K., Jiralerspong, S., Bojanowski, M. W., & Pandolfo, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00896-0 · Cited by 77 · see citing works
The correlation of clinical phenotype in Friedreich ataxia with the site of point mutations in the FRDA gene
Forrest, S., Knight, M. A., Delatycki, M. B., Paris, D. B. B. P., Williamson, R., King, J. O., Yeung, L., Nassif, N. T., & Nicholson, G. A. (1998) · Neurogenetics · doi:10.1007/s100480050037 · Cited by 70 · see citing works
Mitochondrial intermediate peptidase and the yeast frataxin homolog together maintain mitochondrial iron homeostasis in Saccharomyces cerevisiae
Branda, S. S. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.6.1099 · Cited by 64 · see citing works
Friedreich ataxia in Italian families: genetic homogeneity and linkage disequilibrium with the marker loci D9S5 and D9S15.
Pandolfo, M., Sirugo, G., Antonelli, A., Weitnauer, L., Ferretti, L., Leone, M. A., Dones, I., Cerino, A., Fujita, R., & Hanauer, A. (1990) · Europe PMC (PubMed Central) · Cited by 46 · see citing works
Maturation of Frataxin Within Mammalian and Yeast Mitochondria: One-Step Processing by Matrix Processing Peptidase
Gordon, D. M., Shi, Q., Dancis, A., & Pain, D. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.12.2255 · Cited by 46 · see citing works
Deciphering the cause of Friedreich ataxia
Kœnig, M., & Mandel, J. (1997) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(97)80090-6 · Cited by 40 · see citing works
Two-Dimensional NMR Experiments for the Assignment of Aromatic Side Chains in13C-labeled Proteins
Prompers, J. J., Groenewegen, A., Hilbers, C. W., & Pepermans, H. A. M. (1998) · Journal of Magnetic Resonance · doi:10.1006/jmre.1997.1277 · Cited by 29 · see citing works
Genetic recombination events which position the Friedreich ataxia locus proximal to the D9S15/D9S5 linkage group on chromosome 9q.
Chamberlain, S., Farrall, M., Shaw, J., Wilkes, D. C., Carvajal, J. J., Hillermann, R., Doudney, K., Harding, A. E., Williamson, R., & Sirugo, G. (1993) · Europe PMC (PubMed Central) · Cited by 28 · see citing works
Letter to the Editor: Assignment of the 1H, 15N, and 13C resonances of the C-terminal domain of frataxin, the protein responsible for Friedreich ataxia
Musco, G., de Tommasi, T., Stier, G., Kolmerer, B., Bottomley, M. J., Adinolfi, S., Muskett, F. W., Gibson, T. J., Frenkiel, T. A., & Pastore, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008398832619 · Cited by 19 · see citing works
Self-citation
Rapp-Hodgkin syndrome with palmoplantar keratoderma, glossy tongue, congenital absence of lingual frenum and of sublingual caruncles: Newly recognized findings
Kantaputra, P. N., Pruksachatkunakorn, C., & Vanittanakom, P. (1998) · American Journal of Medical Genetics · doi:10.1002/(sici)1096-8628(19981012)79:5 · Cited by 18 · see citing works
Mutation of a Putative Mitochondrial Iron Transporter Gene (ABC7) in X-Linked Sideroblastic Anemia and Ataxia (XLSA/A)
Allikmets, R. L., Raskind, W. H., Hutchinson, A. A., Schueck, N. D., Dean, M. C., & Koeller, D. M. (1999) · Pediatric Research · doi:10.1203/00006450-199904020-00805 · Cited by 15 · see citing works
Abnormalities of Antioxidant Metabolism in a Case of Friedreich's Disease
Helveston, W. R., Cibula, J. E., Hurd, R. W., Uthman, B. M., & Wilder, B. J. (1996) · Clinical Neuropharmacology · doi:10.1097/00002826-199619030-00010 · Cited by 15 · see citing works
Determination of the Dipolar Interaction of23Na in Solution by Triple-Quantum Relaxation Time Measurements
Eliav, U., & Navon, G. (1998) · Journal of Magnetic Resonance · doi:10.1006/jmre.1997.1278 · Cited by 10 · see citing works
A jack bean protein similar to pea seed ferritin and unrelated to concanavalin A is the only iron storage protein in jack bean seeds, although concanavalin A can form ferritin-like iron cores in vitro
Briat, J., Massenet, O., & Laulhère, J. P. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80097-7 · Cited by 9 · see citing works
A rapid screening for steroid 21-hydroxylase mutations in patients with congenital adrenal hyperplasia
Kapelari, K., Ghanaati, Z., Wollmann, H. A., Ventz, M., Ranke, M. B., Kofler, R., & Peters, H. (1999) · Human Mutation · doi:10.1002/(sici)1098-1004(1999)13:6 · Cited by 8 · see citing works
Chemical and Mössbauer spectroscopic evidence that iron-containing concanavalin A is a ferritin.
Yariv, J., Kalb, A. J., Helliwell, J. R., Papiz, M. Z., Bauminger, E. R., & Nowik, I. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68270-5 · Cited by 7 · see citing works

Flagged first, then by citations

2 of the 53 references couldn’t be matched to a known paper.

Sorted by citations

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 · see citing works
Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., & Koenig, M. (2001) · Nature Genetics · doi:10.1038/84818 · Cited by 738 · see citing works
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
Iron−Sulfur Cluster Biosynthesis. Characterization of Frataxin as an Iron Donor for Assembly of [2Fe-2S] Clusters in ISU-Type Proteins
Yoon, T., & Cowan, J. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja027967i · Cited by 353 · see citing works
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 · see citing works
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 287 · see citing works
Frataxin-mediated Iron Delivery to Ferrochelatase in the Final Step of Heme Biosynthesis
Yoon, T., & Cowan, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400107200 · Cited by 281 · see citing works
Mitochondria and degenerative disorders
Orth, M., & Schapira, A. H. V. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1425 · Cited by 278 · see citing works
Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions
Shi, R., Proteau, A., Villarroya, M., Moukadiri, I., Zhang, L., Trempe, J., Matte, A., Armengod, M. ‐., & Cygler, M. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000354 · Cited by 270 · see citing works
Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
Adinolfi, S., Iannuzzi, C., Prischi, F., Pastore, C., Iametti, S., Martin, S. R., Bonomi, F., & Pastore, A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1579 · Cited by 256 · see citing works
Self-citation
The pathogenesis of Friedreich ataxia and the structure and function of frataxin
Pandolfo, M., & Pastore, A. (2009) · Journal of Neurology · doi:10.1007/s00415-009-1003-2 · Cited by 242 · see citing works
Self-citation
Characterization of disease-associated single amino acid polymorphisms in terms of sequence and structure properties 1 1Edited by J. Thornton
Ferrer‐Costa, C., Orozco, M., & de la Cruz, X. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5255 · Cited by 211 · see citing works
Brain Iron Homeostasis: From Molecular Mechanisms To Clinical Significance and Therapeutic Opportunities
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 205 · see citing works
Autosomal recessive cerebellar ataxias
Palau, F., & Espinós, C. (2006) · Orphanet Journal of Rare Diseases · doi:10.1186/1750-1172-1-47 · Cited by 198 · see citing works
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 · see citing works
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 191 · see citing works
Frataxin: a protein in search for a function
Pastore, A., & Puccio, H. M. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12220 · Cited by 191 · see citing works
Self-citation
Structural bases for the interaction of frataxin with the central components of iron–sulphur cluster assembly
Prischi, F., Konarev, P. V., Iannuzzi, C., Pastore, C., Adinolfi, S., Martin, S. R., Svergun, D. I., & Pastore, A. (2010) · Nature Communications · doi:10.1038/ncomms1097 · Cited by 186 · see citing works
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 · see citing works
Mitochondrial Control of Iron Homeostasis
Foury, F., & Talibi, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005804200 · Cited by 176 · see citing works
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 · see citing works
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 165 · see citing works
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 · see citing works
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 · see citing works
The in vivo mitochondrial two-step maturation of human frataxin
Schmucker, S., Argentini, M., Calmels, N., Martelli, A., & Puccio, H. M. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn244 · Cited by 150 · see citing works
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 · see citing works
Compound heterozygous FXN mutations and clinical outcome in friedreich ataxia
Galea, C. A., Huq, A. J., Lockhart, P. J., Tai, G., Corben, L. A., Yiu, E. M., Gurrin, L. C., Lynch, D. R., Gelbard, S., Dürr, A., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24595 · Cited by 146 · see citing works
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 · see citing works
Understanding the molecular mechanisms of Friedreich's ataxia to develop therapeutic approaches
Schmucker, S., & Puccio, H. M. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq165 · Cited by 142 · see citing works
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 · see citing works
Self-citation
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 · see citing works
Self-citation
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Iron−Sulfur Cluster Biosynthesis: Toward an Understanding of Cellular Machinery and Molecular Mechanism
Mansy, S. S., & Cowan, J. A. (2004) · Accounts of Chemical Research · doi:10.1021/ar0301781 · Cited by 105 · 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
Friedreich's ataxia: Past, present and future
Marmolino, D. (2011) · Brain Research Reviews · doi:10.1016/j.brainresrev.2011.04.001 · Cited by 103 · see citing works
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 · see citing works
Self-citation
Molecular and cellular bases of iron metabolism in humans
Васильевич, М. И., Suhodolo, I. V., Prokopieva, V. D., & Klimenteva, T. K. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916060018 · Cited by 100 · see citing works
Ferredoxin Competes with Bacterial Frataxin in Binding to the Desulfurase IscS*
Yan, R., Konarev, P. V., Iannuzzi, C., Adinolfi, S., Roche, B., Kelly, G. P., Simon, L., Martin, S. R., Py, B., Barras, F., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.480327 · Cited by 92 · see citing works
Self-citation
Acidic residues of yeast frataxin have an essential role in Fe–S cluster assembly
Foury, F., Pastore, A., & Trincal, M. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400881 · Cited by 81 · see citing works
Self-citation
Friedreich ataxia
Pandolfo, M. (2003) · Seminars in Pediatric Neurology · doi:10.1016/s1071-9091(03)00025-1 · Cited by 81 · see citing works
Variable-Temperature Electrospray Ionization for Temperature-Dependent Folding/Refolding Reactions of Proteins and Ligand Binding
McCabe, J. W., Shirzadeh, M., Walker, T. E., Lin, C.-W., Jones, B. J., Wysocki, V. H., Barondeau, D. P., Clemmer, D. E., Laganowsky, A. D., & Russell, D. H. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c00870 · Cited by 80 · see citing works
Friedreich Ataxia: Clinical Features and New Developments
Keita, M., McIntyre, K., Rodden, L. N., Schadt, K. A., & Lynch, D. R. (2022) · Neurodegenerative Disease Management · doi:10.2217/nmt-2022-0011 · Cited by 79 · see citing works
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 · see citing works
Normal and Friedreich Ataxia Cells Express Different Isoforms of Frataxin with Complementary Roles in Iron-Sulfur Cluster Assembly
Gakh, O., Bedekovics, T., Duncan, S. F., Smith, D. Y., Berkholz, D. S., & Isaya, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145144 · Cited by 76 · see citing works
Human frataxin: iron and ferrochelatase binding surface
Bencze, K. Z., Yoon, T., Millán‐Pacheco, C., Bradley, P. B., Pastor, N., Cowan, J. A., & Stemmler, T. L. (2007) · Chemical Communications · doi:10.1039/b703195e · Cited by 75 · see citing works
Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization
Becker, E., Greer, J. M., Ponka, P., & Richardson, D. R. (2002) · Blood · doi:10.1182/blood.v99.10.3813 · Cited by 74 · see citing works
Structure–Function Analysis of Friedreich’s Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe–S Assembly Complex
Bridwell‐Rabb, J., Winn, A. M., & Barondeau, D. P. (2011) · Biochemistry · doi:10.1021/bi200895k · Cited by 72 · see citing works
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 · see citing works
THE MOLECULAR BASIS
Pandolfo, M. (2002) · Cited by 70 · see citing works
Iron Metabolism and Mitochondrial Abnormalities in Friedreich Ataxia
Pandolfo, M. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0591 · Cited by 65 · see citing works
Understanding the binding properties of an unusual metal‐binding protein − a study of bacterial frataxin
Pastore, C., Franzese, M., Sica, F., Temussi, P., & Pastore, A. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05946.x · Cited by 64 · see citing works
Self-citation
Functional and molecular characterization of the frataxin homolog from Arabidopsis thaliana,
Busi, M. V., Zabaleta, E. J., Araya, A., & Gomez‐Casati, D. F. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.003 · Cited by 64 · see citing works
Dynamics, stability and iron‐binding activity of frataxin clinical mutants
Correia, A. R., Pastore, C., Adinolfi, S., Pastore, A., & Gomes, C. M. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06512.x · Cited by 63 · see citing works
Self-citation
Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly
Cai, K., Frederick, R. O., Tonelli, M., & Markley, J. L. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.03.007 · Cited by 61 · see citing works
The First Cellular Models Based on Frataxin Missense Mutations That Reproduce Spontaneously the Defects Associated with Friedreich Ataxia
Calmels, N., Schmucker, S., Wattenhofer‐Donzé, M., Martelli, A., Vaucamps, N., Reutenauer, L., Messaddeq, N., Bouton, C., Koenig, M., & Puccio, H. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006379 · Cited by 59 · see citing works
Iron Dysregulation in Friedreich Ataxia
Wilson, R. B. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.005 · Cited by 59 · see citing works
Friedreich’s Ataxia Variants I154F and W155R Diminish Frataxin-Based Activation of the Iron–Sulfur Cluster Assembly Complex
Tsai, C.-L., Bridwell‐Rabb, J., & Barondeau, D. P. (2011) · Biochemistry · doi:10.1021/bi200666h · Cited by 58 · see citing works
Integration of genome data and protein structures: prediction of protein folds, protein interactions and ‘molecular phenotypes’ of single nucleotide polymorphisms
Sunyaev, S. R., Lathe, W. C., & Peer Bork, B. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00175-5 · Cited by 57 · see citing works
Supramolecular Assemblies of Human Frataxin are Formed via Subunit–Subunit Interactions Mediated by a Non-conserved Amino-terminal Region
O’Neill, H. A., Gakh, O., & Isaya, G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.074 · Cited by 57 · see citing works
Fixing frataxin: ‘ironing out’ the metabolic defect in Friedreich's ataxia
Anzovino, A., Lane, D., Huang, L.-H. M., & Richardson, D. R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12470 · Cited by 54 · see citing works
Biogenesis of iron–sulfur proteins in eukaryotes: components, mechanism and pathology
Gerber, J., & Lill, R. (2002) · Mitochondrion · doi:10.1016/s1567-7249(02)00041-7 · Cited by 54 · see citing works
The Molecular Basis of Friedreich Ataxia
Pandolfo, M. (2002) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0117-6_5 · Cited by 52 · see citing works
Making iron-sulfur cluster: structure, regulation and evolution of the bacterial ISC system
Baussier, C., Fakroun, S., Aubert, C., Dubrac, S., Mandin, P., Py, B., & Barras, F. (2020) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2020.01.001 · Cited by 51 · see citing works
Molecular basis of Friedreich ataxia
Pandolfo, M. (2001) · Movement Disorders · doi:10.1002/mds.1162 · Cited by 49 · see citing works
Omaveloxolone: an activator of Nrf2 for the treatment of Friedreich ataxia
Profeta, V., McIntyre, K., Wells, M., Park, C. C., & Lynch, D. R. (2023) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2023.2173063 · Cited by 46 · see citing works
Exploring frataxin function
Busi, M. V., & Gomez‐Casati, D. F. (2011) · IUBMB Life · doi:10.1002/iub.577 · Cited by 46 · see citing works
Bacterial IscU is a well folded and functional single domain protein
Adinolfi, S., Rizzo, F. M., Masino, L., Nair, M. M., Martin, S. R., Pastore, A., & Temussi, P. A. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04112.x · Cited by 46 · see citing works
Self-citation
The NMR contribution to protein–protein networking in Fe–S protein maturation
Banci, L., Camponeschi, F., Ciofi‐Baffoni, S., & Piccioli, M. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1552-x · Cited by 45 · see citing works
Mapping iron binding sites on human frataxin: implications for cluster assembly on the ISU Fe–S cluster scaffold protein
Huang, J., Dizin, E., & Cowan, J. A. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0369-4 · Cited by 45 · see citing works
Conformational stability of human frataxin and effect of Friedreich's ataxia-related mutations on protein folding
Correia, A. R., Adinolfi, S., Pastore, A., & Gomes, C. M. (2006) · Biochemical Journal · doi:10.1042/bj20060345 · Cited by 45 · see citing works
Self-citation
Friedreich Ataxia: Detection of GAA Repeat Expansions and Frataxin Point Mutations
Pandolfo, M. (2006) · Humana Press eBooks · doi:10.1385/1-59745-088-x:197 · Cited by 44 · see citing works
Frataxin interacts with Isu1 through a conserved tryptophan in its β-sheet
Leidgens, S., Smet, S. D., & Foury, F. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp495 · Cited by 44 · see citing works
The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress
Crack, J. C., Balasiny, B. K., Bennett, S. P., Rolfe, M. D., Froes, A. V. T. D. V., MacMillan, F., Green, J. D., Cole, J. A., & Brun, N. E. L. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c12407 · Cited by 42 · see citing works
Recent Advances in the Elucidation of Frataxin Biochemical Function Open Novel Perspectives for the Treatment of Friedreich’s Ataxia
Monfort, B., Want, K., Gervason, S., & D’Autréaux, B. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.838335 · Cited by 42 · see citing works
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 · see citing works
Iron-binding activity in yeast frataxin entails a trade off with stability in the α1/β1 acidic ridge region
Correia, A. R., Wang, T., Craig, E. A., & Gomes, C. M. (2009) · Biochemical Journal · doi:10.1042/bj20091612 · Cited by 40 · see citing works
Tangled web of interactions among proteins involved in iron–sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Kim, J. H., Bothe, J. R., Alderson, T. R., & Markley, J. L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.020 · Cited by 37 · see citing works
Of the vulnerability of orphan complex proteins: The case study of the E. coli IscU and IscS proteins
Prischi, F., Pastore, C., Carroni, M., Iannuzzi, C., Adinolfi, S., Temussi, P., & Pastore, A. (2010) · Protein Expression and Purification · doi:10.1016/j.pep.2010.05.003 · Cited by 37 · see citing works
Self-citation
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 · see citing works
The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX
Adinolfi, S., Puglisi, R., Crack, J. C., Iannuzzi, C., Piaz, F. D., Konarev, P. V., Svergun, D. I., Martin, S. R., Brun, N. E. L., & Pastore, A. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00097 · Cited by 34 · see citing works
Self-citation
The MotA transcription factor from bacteriophage T4 contains a novel DNA‐binding domain: the ‘double wing’ motif
Li, N., Sickmier, E. A., Zhang, R., Joachimiak, A., & White, S. W. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02809.x · Cited by 34 · see citing works
Frataxin Is Localized to Both the Chloroplast and Mitochondrion and Is Involved in Chloroplast Fe-S Protein Function in Arabidopsis
Turowski, V. R., Aknin, C., Maliandi, M. V., Buchensky, C., Leaden, L., Peralta, D. A., Busi, M. V., Araya, A., & Gomez‐Casati, D. F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141443 · Cited by 33 · see citing works
Highly specific ubiquitin-competing molecules effectively promote frataxin accumulation and partially rescue the aconitase defect in Friedreich ataxia cells
Rufini, A., Cavallo, F., Condò, I., Fortuni, S., Martino, G. D., Incani, O., Venere, A. D., Benini, M., Massaro, D. S., Arcuri, G., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.12.011 · Cited by 32 · see citing works
Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU
Blauenburg, B., Mielcarek, A., Altegoer, F., Fage, C. D., Linne, U., Bange, G., & Marahiel, M. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158749 · Cited by 33 · see citing works
Human frataxin, the Friedreich ataxia deficient protein, interacts with mitochondrial respiratory chain
Doni, D., Cavion, F., Bortolus, M., Baschiera, E., Muccioli, S., Tombesi, G., d’Ettorre, F., Ottaviani, D., Marchesan, E., Leanza, L., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06320-y · Cited by 32 · see citing works
Iron chaperones for mitochondrial Fe–S cluster biosynthesis and ferritin iron storage
Subramanian, P., Rodrigues, A. V., Ghimire-Rijal, S., & Stemmler, T. L. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.01.003 · Cited by 31 · see citing works
Protein Stability and Dynamics Modulation: The Case of Human Frataxin
Román, E. A., Faraj, S. E., Gallo, M. L., Salvay, A. G., Ferreiro, D. U., & Santos, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045743 · Cited by 31 · see citing works
Pathophysiogical and therapeutic progress in Friedreich ataxia
Puccio, H. M., Anheim, M., & Tranchant, C. (2014) · Revue Neurologique · doi:10.1016/j.neurol.2014.03.008 · Cited by 29 · see citing works
The alteration of the C‐terminal region of human frataxin distorts its structural dynamics and function
Faraj, S. E., Román, E. A., Arán, M., Gallo, M. L., & Santos, J. (2014) · FEBS Journal · doi:10.1111/febs.12869 · Cited by 29 · see citing works
Clinical use of frataxin measurement in a patient with a novel deletion in the FXN gene
Saccà, F., Marsili, A., Puorro, G., Antenora, A., Pane, C., Tessa, A., Scoppettuolo, P., Nesti, C., Morra, V. B., Michele, G. D., et al. (2012) · Journal of Neurology · doi:10.1007/s00415-012-6770-5 · Cited by 28 · see citing works
Molecular Defects in Friedreich’s Ataxia: Convergence of Oxidative Stress and Cytoskeletal Abnormalities
Smith, F. M., & Kosman, D. J. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.569293 · Cited by 27 · see citing works
Variation in protein Cα‐related one‐bond J couplings
Schmidt, J. M., Howard, M. J., Maestre-Martínez, M., Pérez, C., & Löhr, F. (2008) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.2337 · Cited by 27 · see citing works
His86 from the N-Terminus of Frataxin Coordinates Iron and Is Required for Fe–S Cluster Synthesis
Gentry, L. E., Thacker, M. A., Doughty, R., Timkovich, R., & Busenlehner, L. S. (2013) · Biochemistry · doi:10.1021/bi400443n · Cited by 26 · see citing works
Friedreich ataxia
Pandolfo, M. (2011) · Handbook of clinical neurology · doi:10.1016/b978-0-444-51892-7.00017-6 · Cited by 26 · see citing works

The N‐terminus of mature human frataxin is intrinsically unfolded
Prischi, F., Giannini, C., Adinolfi, S., & Pastore, A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07381.x · Cited by 24 · see citing works
Self-citation
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 · see citing works
The pathogenesis of Friedreich ataxia and the structure and function of frataxin
Pandolfo, M., & Pastore, A. (2009) · Journal of Neurology · doi:10.1007/s00415-009-1003-2 · Cited by 242 · see citing works
Self-citation
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 · see citing works
Structural Basis of the Iron Storage Function of Frataxin from Single-Particle Reconstruction of the Iron-Loaded Oligomer
Schagerlöf, U., Elmlund, H., Gakh, O., Nordlund, G., Hebert, H., Lindahl, M., Isaya, G., & Al‐Karadaghi, S. (2008) · Biochemistry · doi:10.1021/bi800052m · Cited by 44 · see citing works

Authors: Musco, G., Stier, G., Kolmerer, B., Adinolfi, S., Martin, S., Frenkiel, T., Gibson, T., & Pastore, A.
Affiliations: European Molecular Biology Laboratory (DE)
Corresponding author: Pastore, Annalisa
ORCID: Musco, Giovanna
Adinolfi, Salvatore
Martin, Stephen
Frenkiel, Tom
Gibson, Toby
Pastore, Annalisa
Venue: Structure
Publisher: Elsevier BV
Published: 2000-07
Volume: 8
Issue: 7
Pages: 695-707
ISSN: 0969-2126 (ISSN-L)
DOI: 10.1016/s0969-2126(00)00158-1
OpenAlex: W2043666185
Cited by: 166
References: 53
Citations by year: 2026: 3 · 2025: 3 · 2024: 3 · 2023: 5 · 2022: 9 · 2021: 4 · 2020: 4 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 3 · 2015: 6 · 2014: 11 · 2013: 9 · 2012: 3
FWCI: 3.62
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, 4764 d)
Locations: Structure (publishedVersion)
PubMed (publishedVersion)
Institutional Research Information System University of Turin (University of Turin) (submittedVersion, other-oa)
Max Planck Institute for Plasma Physics (submittedVersion)
Max Planck Digital Library (submittedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion)
Scuola Normale Superiore di Pisa (submittedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords: Friedreich's ataxia, frataxin, protein solution structure, mitochondrial iron homeostasis, C-terminal domain, antiparallel beta-sheet, point mutations, compound heterozygosity, protein aggregation
MeSH terms: Frataxin, Amino Acid Sequence, Animals, Bacterial Proteins, Carrier Proteins, Circular Dichroism, Friedreich Ataxia, Fungal Proteins, Heterozygote, Humans, Iron, Ligands, Mitochondria, Models, Molecular, Molecular Sequence Data, Plant Proteins, Protein Conformation, Recombinant Fusion Proteins, Species Specificity, Structure-Activity Relationship, Helminth Proteins, Sequence Alignment, Point Mutation, Sequence Homology, Amino Acid, Protein Structure, Secondary, Phosphotransferases (Alcohol Group Acceptor), Oxidative Stress, Evolution, Molecular, Iron-Binding Proteins, Transferrin-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

Towards a structural understanding of Friedreich’s ataxia: the solution structure of frataxin

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks