The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis
Open accessAbstract
Decreased expression of Yfh1p in the budding yeast, Saccharomyces cerevisiae , and the orthologous human gene frataxin results in respiratory deficiency and mitochondrial iron accumulation. The absence of Yfh1p decreases mitochondrial iron export. We demonstrate that decreased expression of Nfs1p, the yeast cysteine desulfurase that plays a central role in Fe-S cluster synthesis, also results in mitochondrial iron accumulation due to decreased export of mitochondrial iron. In the absence of Yfh1p, activity of Fe-S-containing enzymes (aconitase, succinate dehydrogenase) is decreased, whereas the activity of a non-Fe-S-containing enzyme (malate dehydrogenase) is unaffected. Aconitase protein was abundant even though the activity of aconitase was decreased in both aerobic and anaerobic conditions. These results demonstrate a direct role of Yfh1p in the formation of Fe-S clusters and indicate that mitochondrial iron export requires Fe-S cluster biosynthesis.
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
“Mouse T-cell immunoglobulin-domain and mucin-domain (TIM)-2 was identified as a ferritin H subunit receptor (48)”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [48]
In the citing paper
“Additional experiments also showed that ferritin L did not interact with TIM-2 (48).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [48]
In the citing paper
“Ferritin H incorporation was not observed in the absence of TIM-2 (48).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [48]
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
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
Daum, G., Böhni, P. C., & Schatz, G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33617-2 · Cited by 1,123
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
Self-citationThe 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
Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
Cabiscol, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003140200 · Cited by 418
CCC1 Is a Transporter That Mediates Vacuolar Iron Storage in Yeast
Li, L., Chen, O. S., Ward, D. M., & Kaplan, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103944200 · Cited by 354
Self-citationRespiratory 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
Oxidative Stress Promotes Specific Protein Damage inSaccharomyces cerevisiae
Cabiscol, E., Piulats, E., Echave, P., Herrero, E., & Ros, J. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61523-1 · 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
Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
Schilke, B. A., Voisine, C., Beinert, H., & Craig, E. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10206 · Cited by 284
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
Self-citationA mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
Lange, H., Kaut, A., Kispál, G., & Lill, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1050 · Cited by 272
Iron-Dependent Self-Assembly of Recombinant Yeast Frataxin: Implications for Friedreich Ataxia
Adamec, J., Rusnak, F., Owen, W. G., Naylor, S., Benson, L. M., Gacy, A. M., & Isaya, G. (2000) · The American Journal of Human Genetics · doi:10.1086/303056 · Cited by 255
Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase
Lapinskas, P. J., Cunningham, K. W., Liu, X. F., Fink, G. R., & Culotta, V. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1382 · Cited by 240
Dohrmann, P. R., Butler, G., Tamai, T. K., Dorland, S., Greene, J. R., Thiele, D. J., & Stillman, D. J. (1992) · Genes & Development · doi:10.1101/gad.6.1.93 · Cited by 220
Li, J., Kogan, M., Knight, S. A. B., Pain, D., & Dancis, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.33025 · Cited by 201
Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
Tong, W., & Rouault, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5692 · Cited by 194
Yamaguchi‐Iwai, Y., Ueta, R., Fukunaka, A., & Sasaki, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200949200 · Cited by 174
The Essential Role of Mitochondria in the Biogenesis of Cellular Iron-Sulfur Proteins
Lill, R., Diekert, K., Kaut, A., Lange, H., Pelzer, W., Prohl, C., & Kispál, G. (1999) · Biological Chemistry · doi:10.1515/bc.1999.147 · Cited by 156
Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
Foury, F. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00961-8 · Cited by 145
Munujos, P., Collcanti, J., González‐Sastre, F., & Gella, F.-J. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1360 · Cited by 126
Lutz, T., Westermann, B., Neupert, W., & Herrmann, J. M. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4527 · Cited by 125
Amberg, D. C., Botstein, D., & Beasley, E. M. (1995) · Yeast · doi:10.1002/yea.320111307 · Cited by 124
Adrenodoxin Reductase Homolog (Arh1p) of Yeast Mitochondria Required for Iron Homeostasis
Li, J., Saxena, S., Pain, D., & Dancis, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007198200 · Cited by 122
Chen, O. S., Schalinske, K. L., & Eisenstein Richard, S. (1997) · Journal of Nutrition · doi:10.1093/jn/127.2.238 · Cited by 110
Self-citation[18] Mitochondrial l-malate dehydrogenase of beef heart
Englard, S., & Siegel, L. (1969) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(69)13022-0 · Cited by 95
Brown, N. M., Anderson, S. A., Steffen, D. W., Carpenter, T. B., Kennedy, M. C., Walden, W. E., & Eisenstein, R. S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.26.15235 · Cited by 83
Chen, O. S., & Kaplan, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7626 · Cited by 77
Self-citationThe Aconitase Function of Iron Regulatory Protein 1
Narahari, J., Ma, R., Wang, M., & Walden, W. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910450199 · Cited by 66
YFH1‐mediated iron homeostasis is independent of mitochondrial respiration
Chen, O. S., & Kaplan, J. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03137-4 · Cited by 11
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
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, 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
Mühlenhoff, U., Gerber, J., Richhardt, N., & Lill, R. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg446 · Cited by 383
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
Metadata
- Authors
- Chen, O. S., Hemenway, S., & Kaplan, J.
- Affiliations
- University of Utah (US)
- ORCID
- Chen, Opal S.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2002-09-09
- Volume
- 99
- Issue
- 19
- Pages
- 12321-12326
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC129443
- OpenAlex
- W2039280518
- Cited by
- 152
- References
- 31
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 3 · 2022: 1 · 2021: 8 · 2020: 5 · 2019: 4 · 2018: 2 · 2017: 5 · 2015: 2 · 2014: 5 · 2013: 8 · 2012: 7
- FWCI
- 16.64
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 52380, R01DK052380)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- frataxin, iron-sulfur cluster assembly, mitochondrial iron accumulation, Saccharomyces cerevisiae, aconitase, succinate dehydrogenase, malate dehydrogenase, respiratory deficiency, cysteine desulfurase
- MeSH terms
- Frataxin, Aconitate Hydratase, Biological Transport, Active, Carrier Proteins, Fungal Proteins, Humans, Iron, Iron-Sulfur Proteins, Mitochondria, Oxidation-Reduction, RNA, Fungal, RNA, Messenger, Saccharomyces cerevisiae, Sulfurtransferases, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, 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
