The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Crystal Structure of Human Frataxin
Open accessAbstract
Friedreich's ataxia, an autosomal recessive neurodegenerative disorder characterized by progressive gait and limb ataxia, cardiomyopathy, and diabetes mellitus, is caused by decreased frataxin production or function. The structure of human frataxin, which we have determined at 1.8-A resolution, reveals a novel protein fold. A five-stranded, antiparallel beta sheet provides a flat platform, which supports a pair of parallel alpha helices, to form a compact alphabeta sandwich. A cluster of 12 acidic residues from the first helix and the first strand of the large sheet form a contiguous anionic surface on the protein. The overall protein structure and the anionic patch are conserved in eukaryotes, including animals, plants, and yeast, and in prokaryotes. Additional conserved residues create an extended 1008-A(2) patch on a distinct surface of the protein. Side chains of disease-associated mutations either contribute to the anionic patch, help create the second conserved surface, or point toward frataxin's hydrophobic core. These structural findings predict potential modes of protein-protein and protein-iron binding.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Exogenous Fpn expressed in Xenopus oocytes served as a ferrous iron exporter (72).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [72]
In the citing paper
“Simultaneous studies characterized Fpn, which is abundantly expressed on the basolateral membrane of polarized enterocytes in the duodenum, in the cytosol of reticuloendothelial cells, and on the basal surface of syncytiotrophoblasts of the placenta (1, 72, 198).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [72]
In the citing paper
“Fpn (also termed Ireg1, MTP1) was originally identified by positional cloning to identify the causative gene for hypochromic anemia of “weissherbst” mutant zebrafish (72).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [72]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[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
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
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
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
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
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159
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
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
Mineralization in ferritin: an efficient means of iron storage
Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815
Carson, M. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891007240 · Cited by 809
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
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
Cossee, M. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.8.1219 · Cited by 377
Wong, A. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.3.425 · Cited by 374
Deficit of in vivo mitochondrial ATP production in patients with Friedreich ataxia
Lodi, R., Cooper, J. A. D., Bradley, J. L., Manners, D. N., Styles, P., Taylor, D. J., & Schapira, A. H. V. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11492 · Cited by 352
Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue
Wilson, R. B., & Roof, D. M. (1997) · Nature Genetics · doi:10.1038/ng0897-352 · Cited by 345
Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia
Bradley, J. L. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.2.275 · Cited by 339
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
Sakamoto, N., Chastain, P. D., Parniewski, P., Ohshima, K., Pandolfo, M., Griffith, J. D., & Wells, R. D. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80474-8 · Cited by 313
Knight, S. A. B., Sepuri, N. B. V., Pain, D., & Dancis, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18389 · Cited by 173
Blass, J. P., Kark, R. A. P., Menon, N. K., & Harris, S. E. (1976) · New England Journal of Medicine · doi:10.1056/nejm197607082950202 · Cited by 130
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
Branda, S. S., Cavadini, P., Adamec, J., Kalousek, F., Taroni, F., & Isaya, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22763 · Cited by 107
Gordon, D. M., Shi, Q., Dancis, A., & Pain, D. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.12.2255 · Cited by 46
Atypical Friedreich ataxia phenotype associated with a novel missense mutation in the X25 gene
Michele, G. D., Filla, A., Cavalcanti, F., Tammaro, A., Monticelli, A., Pianese, L., Salle, F. D., Perretti, A., Santoro, L., Caruso, G., et al. (2000) · Neurology · doi:10.1212/wnl.54.2.496 · Cited by 27
Gray, J. V., & Johnson, K. J. (1997) · Nature Genetics · doi:10.1038/ng0897-323 · Cited by 5
Cited by
Sorted by citations
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
Sazanov, L. A., & Hinchliffe, P. (2006) · Science · doi:10.1126/science.1123809 · Cited by 763
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
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
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
Yoon, T., & Cowan, J. A. (2003) · Journal of the American Chemical Society · doi:10.1021/ja027967i · Cited by 353
Metadata
- Authors
- Dhe-Paganon, S., Shigeta, R., Chi, Y.-I., Ristow, M., & Shoelson, S. E.
- Affiliations
- Joslin Diabetes Center (US)
- Corresponding author
- Shoelson, Steven E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 275
- Issue
- 40
- Pages
- 30753-30756
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2105822562
- Cited by
- 226
- References
- 32
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 6 · 2023: 6 · 2022: 9 · 2021: 6 · 2020: 10 · 2019: 10 · 2018: 7 · 2017: 8 · 2016: 4 · 2015: 9 · 2014: 10 · 2013: 14 · 2012: 3
- FWCI
- 8.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Joslin Diabetes Center
- Universität zu Köln
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (DK4312, DK07260, T32DK007260)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- frataxin, Friedreich's ataxia, protein crystal structure, novel protein fold, anionic surfaces, disease-associated mutations, protein-protein interaction, hydrophobic core
- MeSH terms
- Frataxin, Amino Acid Sequence, Cloning, Molecular, Friedreich Ataxia, Humans, Iron, Models, Molecular, Molecular Sequence Data, Protein Binding, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Protein Structure, Secondary, Protein Folding, Phosphotransferases (Alcohol Group Acceptor), Crystallography, X-Ray, 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
