Crystal Structure of Human Frataxin

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,961

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616

Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230

Three-dimensional tracking of axonal projections in the brain by magnetic resonance imaging

Mori, S., Crain, B. J., Chacko, V. P., & van Zijl, P. C. M. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199902)45:2 · Cited by 3,513

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

Crystallographic Computing 6

Flack, H. D., Párkányi, L., & Simon, K. (1993) · doi:10.1093/oso/9780198557883.001.0001 · Cited by 2,003

A Hot Spot of Binding Energy in a Hormone-Receptor Interface

Clackson, T., & Wells, J. A. (1995) · Science · doi:10.1126/science.7529940 · Cited by 1,987

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 34

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

Frataxin Structure and Function

Castro, I. H., Pignataro, M. F., Sewell, K. E., Espeche, L. D., Herrera, M. G., Noguera, M. E., Daín, L., Nadra, A. D., Arán, M., Smal, C., et al. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-28151-9_13 · Cited by 37

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

Discovery of a Novel Small Molecule Inhibitor Targeting the Frataxin/Ubiquitin Interaction via Structure-Based Virtual Screening and Bioassays

Lavecchia, A., Giovanni, C. D., Cerchia, C., Russo, A., Russo, G., & Novellino, E. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3017199 · Cited by 32

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

Crystal structure of Escherichia coli YfhJ protein, a member of the ISC machinery involved in assembly of iron–sulfur clusters

Shimomura, Y., Takahashi, Y., Kakuta, Y., & Fukuyama, K. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20481 · Cited by 31

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

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 31

Structure of the autophagic E2 enzyme Atg10

Hong, S., Kim, B.-W., Kim, J., & Song, H. K. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912034166 · Cited by 30

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

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

The Structure of the Complex between Yeast Frataxin and Ferrochelatase

Söderberg, C. A. G., Gillam, M. E., Ahlgren, E.-C., Hunter, G. A., Gakh, O., Isaya, G., Ferreira, G. C., & Al‐Karadaghi, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.701128 · Cited by 28

Architectural Features of Human Mitochondrial Cysteine Desulfurase Complexes from Crosslinking Mass Spectrometry and Small-Angle X-Ray Scattering

Cai, K., Frederick, R. O., Dashti, H., & Markley, J. L. (2018) · Structure · doi:10.1016/j.str.2018.05.017 · Cited by 27

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

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

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

Friedreich ataxia

Pandolfo, M. (2011) · Handbook of clinical neurology · doi:10.1016/b978-0-444-51892-7.00017-6 · Cited by 26

Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone

Sun, G., Gargus, J. J., Ta, D. T., & Vickery, L. E. (2003) · Journal of Human Genetics · doi:10.1007/s10038-003-0048-9 · Cited by 26

Cardiolipin-deficient cells have decreased levels of the iron–sulfur biogenesis protein frataxin

Li, Y., Lou, W., Grevel, A., Böttinger, L., Liang, Z., Ji, J., Patil, V. A., Liu, J., Ye, C., Hüttemann, M., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013960 · Cited by 26

The Molecular Basis of Iron-induced Oligomerization of Frataxin and the Role of the Ferroxidation Reaction in Oligomerization

Söderberg, C. A. G., Rajan, S. S., Shkumatov, A. V., Gakh, O., Schaefer, S., Ahlgren, E.-C., Svergun, D. I., Isaya, G., & Al‐Karadaghi, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442285 · Cited by 25

Quantitative proteomics in Friedreich's ataxia B-lymphocytes: A valuable approach to decipher the biochemical events responsible for pathogenesis

Télot, L., Rousseau, E., Lesuisse, E., Garcia, C., Morlet, B., Léger, T., Camadro, J., & Serre, V. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.01.010 · Cited by 25

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

Human Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region

Faraj, S. E., González‐Lebrero, R. M., Román, E. A., & Santos, J. (2016) · Scientific Reports · doi:10.1038/srep20782 · Cited by 24

Impact of Drosophila Models in the Study and Treatment of Friedreich’s Ataxia

Monnier, V., Llorens, J. V., & Navarro, J. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071989 · Cited by 23

Exploring iron-binding to human frataxin and to selected Friedreich ataxia mutants by means of NMR and EPR spectroscopies

Bellanda, M., Maso, L., Doni, D., Bortolus, M., Rosa, E. D., Lunardi, F., Alfonsi, A., Noguera, M. E., Herrera, M. G., Santos, J., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.07.007 · Cited by 23

Expression and one-step purification of recombinant Arabidopsis thaliana frataxin homolog (AtFH)

Maliandi, M. V., Busi, M. V., Clemente, M., Zabaleta, E. J., Araya, A., & Gomez‐Casati, D. F. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.06.007 · Cited by 23

Iron Pathophysiology in Friedreich’s Ataxia

Li, K. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_7 · Cited by 22

Iron metabolism in insect disease vectors: Mining the Anopheles gambiae translated protein database

Winzerling, J. J., & Pham, D. Q. ‐. (2006) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2006.01.006 · Cited by 23

Correlation of 2J couplings with protein secondary structure

Schmidt, J. M., Hua, Y., & Löhr, F. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22672 · Cited by 21

The kinetics of folding of frataxin

Bonetti, D., Toto, A., Giri, R., Morrone, A., Sanfelice, D., Pastore, A., Temussi, P. A., Gianni, S., & Brunori, M. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp54055c · Cited by 20

Characterization of human frataxin missense variants in cancer tissues

Petrosino, M., Pasquo, A., Novak, L., Toto, A., Gianni, S., Mantuano, E., Veneziano, L., Minicozzi, V., Pastore, A., Puglisi, R., et al. (2019) · Human Mutation · doi:10.1002/humu.23789 · Cited by 20

Key Players and Their Role During Mitochondrial Iron–Sulfur Cluster Biosynthesis

Rawat, S., & Stemmler, T. L. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002143 · Cited by 19

A structural approach to trinucleotide expansion diseases

Masino, L., & Pastore, A. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00582-2 · Cited by 19

The displacement of frataxin from the mitochondrial cristae correlates with abnormal respiratory supercomplexes formation and bioenergetic defects in cells of Friedreich ataxia patients

Doni, D., Rigoni, G., Palumbo, E., Baschiera, E., Peruzzo, R., Rosa, E. D., Caicci, F., Passerini, L., Bettio, D., Russo, A., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202000524rr · Cited by 19

Friedreich Ataxia: An Update on Animal Models, Frataxin Function and Therapies

González‐Cabo, P., Llorens, J. V., Palau, F., & Moltó, M. D. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-90-481-2813-6_17 · Cited by 19

Mitochondrial damage and senescence phenotype of cells derived from a novel frataxin G127V point mutation mouse model of Friedreich's ataxia

Fil, D., Chacko, B. K., Conley, R. L., Ouyang, X., Zhang, J., Darley-Usmar, V. M., Zuberi, A. R., Lutz, C. M., Напиерала, М., & Napierala, J. S. (2020) · Disease Models & Mechanisms · doi:10.1242/dmm.045229 · Cited by 17

Frataxin mRNA Isoforms in FRDA Patients and Normal Subjects: Effect of Tocotrienol Supplementation

Abruzzo, P. M., Marini, M., Bolotta, A., Malisardi, G., Manfredini, S., Ghezzo, A., Pini, A., Tasco, G., & Casadio, R. (2013) · BioMed Research International · doi:10.1155/2013/276808 · Cited by 17

Computational analysis of human disease-associated genes and their protein products

Sreekumar, K. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00186-6 · Cited by 17

Iron-induced oligomerization of human FXN81-210 and bacterial CyaY frataxin and the effect of iron chelators

Ahlgren, E.-C., Fekry, M., Wiemann, M., Söderberg, C. A. G., Bernfur, K., Gakh, O., Rasmussen, M. I., Højrup, P., Emanuelsson, C. S., Isaya, G., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0188937 · Cited by 16

Iron-Sulfur Cluster Complex Assembly in the Mitochondria of Arabidopsis thaliana

Armas, A. M., Balparda, M., Terenzi, A., Busi, M. V., Pagani, M. A., & Gomez‐Casati, D. F. (2020) · Plants · doi:10.3390/plants9091171 · Cited by 16

A structural and functional homolog supports a general role for frataxin in cellular iron chemistry

Qi, W., & Cowan, J. A. (2009) · Chemical Communications · doi:10.1039/b911975b · Cited by 16

Protein Mutations and Stability, a Link with Disease: The Case Study of Frataxin

Puglisi, R. (2022) · Biomedicines · doi:10.3390/biomedicines10020425 · Cited by 15

Simultaneous Quantification of Mitochondrial Mature Frataxin and Extra-Mitochondrial Frataxin Isoform E in Friedreich’s Ataxia Blood

Wang, Q., Laboureur, L., Weng, L., Eskenazi, N., Hauser, L. A., Mesaros, C., Lynch, D. R., & Blair, I. A. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.874768 · Cited by 15

A novel deletion–insertion mutation identified in exon 3 of FXN in two siblings with a severe Friedreich ataxia phenotype

Evans‐Galea, M. V., Corben, L. A., Hasell, J., Galea, C. A., Fahey, M. C., du Sart, D., & Delatycki, M. B. (2011) · Neurogenetics · doi:10.1007/s10048-011-0296-3 · Cited by 15

Identification of two frataxin isoforms in Zea mays: Structural and functional studies

Buchensky, C., Sánchez, M., Carrillo, M., Palacios, Ò., Capdevila, M., Dominguez-Vera, J. M., Busi, M. V., Atrian, S., Pagani, M. A., & Gomez‐Casati, D. F. (2017) · Biochimie · doi:10.1016/j.biochi.2017.06.011 · Cited by 15

Effects of Fe2+/Fe3+ Binding to Human Frataxin and Its D122Y Variant, as Revealed by Site-Directed Spin Labeling (SDSL) EPR Complemented by Fluorescence and Circular Dichroism Spectroscopies

Doni, D., Passerini, L., Audran, G., Marque, S. R. A., Schulz, M., Santos, J., Costantini, P., Bortolus, M., & Carbonera, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249619 · Cited by 14

Interaction of frataxin, an iron binding protein, with IscU of Fe–S clusters biogenesis pathway and its upregulation in AmpB resistant Leishmania donovani

Zaidi, A., Singh, K. P., Anwar, S., Suman, S. S., Equbal, A., Singh, K., Dikhit, M. R., Bimal, S., Pandey, K., Das, P. K., et al. (2015) · Biochimie · doi:10.1016/j.biochi.2015.05.016 · Cited by 14

Mechanisms of iron and copper–frataxin interactions

Han, T.-H.-L., Camadro, J., Santos, R., Lesuisse, E., Chahine, J. E. H., & Duong, N.-T. H. (2017) · Metallomics · doi:10.1039/c7mt00031f · Cited by 14

Relationship between activity and stability: Design and characterization of stable variants of human frataxin

Castro, I. H., Bringas, M., Doni, D., Noguera, M. E., Capece, L., Arán, M., Blaustein, M., Costantini, P., & Santos, J. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108491 · Cited by 13

A Dynamic Model of the Proteins that Form the Initial Iron-Sulfur Cluster Biogenesis Machinery in Yeast Mitochondria

Amela, I., Delicado, P., Gómez, A., Querol, E., & Cedano, J. A. (2013) · The Protein Journal · doi:10.1007/s10930-013-9475-4 · Cited by 13

Gain of local structure in an amphipathic peptide does not require a specific tertiary framework

Román, E. A., Rosi, P. E., Lebrero, M. C. G., Wuilloud, R., Flecha, F. L. G., Delfino, J., & Santos, J. (2010) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.22789 · Cited by 9

A helix–coil transition induced by the metal ion interaction with a grafted iron-binding site of the CyaY protein family

Vazquez, D. S., Agudelo, W. A., Yone, Á., Vizioli, N. M., Arán, M., Flecha, F. L. G., Lebrero, M. C. G., & Santos, J. (2014) · Dalton Transactions · doi:10.1039/c4dt02796e · Cited by 13

The role of the N-terminal tail for the oligomerization, folding and stability of human frataxin

Faraj, S., Venturutti, L., Román, E. A., Marino-Buslje, C., Mignone, A., Tosatto, S., Delfino, J., & Santos, J. (2013) · FEBS Open Bio · doi:10.1016/j.fob.2013.07.004 · Cited by 12

Fe-S Protein Synthesis in Green Algae Mitochondria

Gomez‐Casati, D. F., Busi, M. V., Barchiesi, J., Pagani, M. A., Marchetti, N., & Terenzi, A. (2021) · Plants · doi:10.3390/plants10020200 · Cited by 12

Mitochondrial iron metabolism in plants: frataxin comes into play

Murgia, I., Tarantino, D., & Soave, C. (2009) · Plant and Soil · doi:10.1007/s11104-009-0038-6 · Cited by 12

Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis

Falb, N., Patil, G., Furtmüller, P. G., Gabler, T., & Hofbauer, S. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.07.024 · Cited by 11

Structural characterization of metal binding to a cold-adapted frataxin

Noguera, M. E., Román, E. A., Rigal, J. B., Cousido-Siah, A., Mitschler, A., PODJARNY, A. D., & Santos, J. (2015) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1251-9 · Cited by 11

Insights on the conformational dynamics of human frataxin through modifications of loop-1

Noguera, M. E., Arán, M., Smal, C., Vazquez, D. S., Herrera, M. G., Román, E. A., Alaimo, N., Gallo, M. L., & Santos, J. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.10.022 · Cited by 10

Friedreich Ataxia

Muthuswamy, S., & Agarwal, S. (2015) · The Neurologist · doi:10.1097/nrl.0000000000000054 · Cited by 10

Drosophila melanogaster frataxin: protein crystal and predicted solution structure with identification of the iron-binding regions

Rodrigues, A. V., Batelu, S., Hinton, T. V., Rotondo, J., Thompson, L., Brunzelle, J. S., & Stemmler, T. L. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322011639 · Cited by 9

On the Effect of Sodium Chloride and Sodium Sulfate on Cold Denaturation

Pica, A., & Graziano, G. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133550 · Cited by 9

Biophysical characterisation of the recombinant human frataxin precursor

Castro, I. H., Ferrari, A., Herrera, M. G., Noguera, M. E., Maso, L., Benini, M., Rufini, A., Testi, R., Costantini, P., & Santos, J. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12376 · Cited by 9

Identification of a novel missense mutation in Friedreich's ataxia – FXNW 168R

Clark, E. M., Strawser, C. J., Schadt, K. A., & Lynch, D. R. (2019) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.728 · Cited by 8

NMR assignments of a stable processing intermediate of human frataxin

Kondapalli, K. C., Bencze, K. Z., Dizin, E., Cowan, J. A., & Stemmler, T. L. (2010) · Biomolecular NMR Assignments · doi:10.1007/s12104-010-9209-x · Cited by 8

Micronutrients (Metals and Iodine)

Litwack, G. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-383864-3.00019-3 · Cited by 10

Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin

Faraj, S. E., Noguera, M. E., Delfino, J. M., & Santos, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-39429-2 · Cited by 8

Friedreich's ataxia

Cooper, J. A. D., & Bradley, J. L. (2002) · International review of neurobiology · doi:10.1016/s0074-7742(02)53006-3 · Cited by 8

Selection of synthetic proteins to modulate the human frataxin function

Pignataro, M. F., Herrera, M. G., Fernández, N., Arán, M., Gentili, H., Battaglini, F., & Santos, J. (2022) · Biotechnology and Bioengineering · doi:10.1002/bit.28263 · Cited by 5

A Combined Spectroscopic and In Silico Approach to Evaluate the Interaction of Human Frataxin with Mitochondrial Superoxide Dismutase

Doni, D., Meggiolaro, M., Santos, J., Audran, G., Marque, S. R. A., Costantini, P., Bortolus, M., & Carbonera, D. (2021) · Biomedicines · doi:10.3390/biomedicines9121763 · Cited by 5

Modelling Protein Plasticity: The Example of Frataxin and Its Variants

Botticelli, S., Penna, G. L., Nobili, G., Rossi, G. C., Stellato, F., & Morante, S. (2022) · Molecules · doi:10.3390/molecules27061955 · Cited by 5

Thermodynamic Stabilization of Human FrataxinPreprint

Núñez‐Franco, R., Torres-Mozas, Á., Navo, C. D., Schedlbauer, A., Azkargorta, M., Iloro, I., Elortza, F., Ortega, G., Millet, Ó., Peccati, F., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.08.556816 · Cited by 5

Frataxin is essential for zebrafish embryogenesis and pronephros formation

Ercanbrack, W. S., Dungan, A., Gaul, E., Ramirez, M., DelVecchio, A. J., Grass, C., & Wingert, R. A. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1496244 · Cited by 4

Life and death of Yfh1: how cool is cold denaturation

Temussi, P. A., Martin, S. R., & Pastore, A. (2025) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583524000180 · Cited by 4

Probing protein stability: towards a computational atomistic, reliable, affordable, and improvable model

Nobili, G., Botticelli, S., Penna, G. L., Morante, S., Rossi, G. C., & Salina, G. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1122269 · Cited by 4

Protein structure determination using a Riemannian approach

Wei, X., Li, Z., Li, S., Peng, X., & Zhao, Q. B. (2019) · FEBS Letters · doi:10.1002/1873-3468.13688 · Cited by 4

A Highly Conserved Iron-Sulfur Cluster Assembly Machinery between Humans and Amoeba Dictyostelium discoideum: The Characterization of Frataxin

Olmos, J., Pignataro, M. F., dos Santos, A. B. B., Bringas, M., Klinke, S., Kamenetzky, L., Velázquez, F., & Santos, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186821 · Cited by 4

Friedreich Ataxia

Pandolfo, M. (2007) · Springer eBooks · doi:10.1007/3-540-33336-3_4 · Cited by 3

Friedreich ataxia

Pandolfo, M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19176-3.00041-8 · Cited by 3

Structure of Respiratory Complex I: “Minimal” Bacterial and “De luxe” Mammalian Versions

Sazanov, L. A. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781788010405-00025 · Cited by 3

Structural and Functional Characterization of CreFH1, the Frataxin Homolog from Chlamydomonas reinhardtii

Terenzi, A., Pagani, M. A., Gomez‐Casati, D. F., & Busi, M. V. (2022) · Plants · doi:10.3390/plants11151931 · Cited by 3

An In Silico Analysis of Genetic Variants and Structural Modeling of the Human Frataxin Protein in Friedreich’s Ataxia

Conceição, L. M. A. D., Cabral, L. M., Pereira, G. R. C., & Mesquita, J. F. D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25115796 · Cited by 5

Genome-Wide Identification, Characterization and Expression Profiling of Potato (Solanum tuberosum) Frataxin (FH) Gene

Kurt, F., Filiz, E., Yildiz, K., & Akbudak, M. A. (2023) · Genes · doi:10.3390/genes14020468 · Cited by 2

Searching for Frataxin Function: Exploring the Analogy with Nqo15, the Frataxin-like Protein of Respiratory Complex I from Thermus thermophilus

Doni, D., Cavallari, E., Noguera, M. E., Gentili, H., Cavion, F., Parisi, G. D., Fornasari, M. S., Sartori, G., Santos, J., Bellanda, M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031912 · Cited by 2

Nanobodies as tools for studying human frataxin biology

Pignataro, M. F., Fernández, N. B., Garay-Alvarez, A., Pavan, M. F., Molina, R., Muñoz, I. G., Grossi, J., Noguera, M., Vila, A., García, A. E., et al. (2026) · Communications Biology · doi:10.1038/s42003-025-09458-x · Cited by 2

Metalochaperonas: escoltas personales en el tráfico intracelular de iones metálicos

Gómez, M. E. B., Espinoza-Guillén, A., Blum, S. E. C., & Behrens, N. B. (2015) · Educación Química · doi:10.1016/s0187-893x(15)72095-1 · Cited by 2

Molecular Diagnosis of Friedreich Ataxia Using Analysis of GAA Repeats and FXN Gene Exons in Population from Western India

Potdar, P. D., & Raghu, A. (2013) · Asian Journal of Neuroscience · doi:10.1155/2013/909767 · Cited by 2

Animal Models of Friedreich Ataxia

Pandolfo, M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00065-2 · Cited by 2

Iron Proteins for Storage & Transport & Their Synthetic Analogs

Lewin, A. C., Brun, N. E. L., & Moore, G. R. (2005) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0107 · Cited by 2

Characterization of Arabidopsis thaliana FRATAXIN HOMOLOG in heme catabolism

Zhang, J., Zhou, Y., Qianyi, D., Xu, X., Wang, X., Wang, J., & Liu, L. (2024) · Biochimie · doi:10.1016/j.biochi.2024.12.010 · Cited by 1

Integration of Evolutionary Analysis With RFdiffusion for De Novo Design of Aggregation‐Resistant Frataxin

Kırboğa, K. K., & Küçüksille, E. U. (2026) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.70114 · Cited by 1

Thermodynamic Preference of Fe 2+ for a C-Terminal Coordination Site in Human Frataxin Revealed by Multiscale Simulations

Kırboğa, K. K., & Küçüksille, E. U. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6c00960 · Cited by 1

Friedreich Ataxia

Pandolfo, M. (2003) · Elsevier eBooks · doi:10.1016/b978-012566652-7/50020-4 · Cited by 1

Micronutrients (Metals and Iodine)

Litwack, G. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85718-5.00018-2 · Cited by 1

Remodelling the surface of thioredoxin from Escherichia coli by grafting an iron-binding site from the CyaY protein family

Vazquez, D. S., Agudelo, W. A., Ferrer‐Sueta, G., Giraudo, L., Lebrero, M. C. G., Arán, M., & Santos, J. (2022) · Dalton Transactions · doi:10.1039/d2dt02599j · Cited by 1

Hydrophilic Domain of Respiratory Complex I fromThermus thermophilus

Sazanov, L. A. (2011) · Wiley eBooks · doi:10.1002/9781119951438.eibc0666 · Cited by 1

PROTEIN FOLDING AND DISEASE THE MITOCHONDRIAL PROTEIN FRATAXIN

Correia, A. R. (2010) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)

Characterization of poly (rc) binding protein (pcbp2) and frataxin

Ghimire-Rijal, S. (2011) · Human Biology

Friedreich's Ataxia and Diseases Associated with Expansion of Non‐Coding Triplets

Crichton, R. R., & Ward, R. J. (2005) · doi:10.1002/0470022574.ch6

Chapter 7 Friedreich Ataxia

Pandolfo, M. (2007) · Blue books of neurology · doi:10.1016/s1877-184x(09)70081-4

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

Musco, G., Stier, G., Kolmerer, B., Adinolfi, S., Martin, S., Frenkiel, T., Gibson, T., & Pastore, A. (2000) · Structure · doi:10.1016/s0969-2126(00)00158-1 · Cited by 166

Structure studies of human frataxin and its higher order structures: implication in Friedreich's ataxia

Ahlgren, E.-C., & Al-Karadaghi, S. (2010) · Lund University Publications (Lund University) · doi:10.1111/j.1742-4658.2010.07680.x

Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family

Cho, S.-J., Lee, M. G., Yang, J. K., Lee, J. Y., Song, H. K., & Suh, S. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160270897 · Cited by 127

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

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 43