The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Mitochondria and Iron: current questions
Open accessAbstract
INTRODUCTION: Mitochondria are cellular organelles that perform numerous bioenergetic, biosynthetic, and regulatory functions and play a central role in iron metabolism. Extracellular iron is taken up by cells and transported to the mitochondria, where it is utilized for synthesis of cofactors essential to the function of enzymes involved in oxidation-reduction reactions, DNA synthesis and repair, and a variety of other cellular processes. Areas covered: This article reviews the trafficking of iron to the mitochondria and normal mitochondrial iron metabolism, including heme synthesis and iron-sulfur cluster biogenesis. Much of our understanding of mitochondrial iron metabolism has been revealed by pathologies that disrupt normal iron metabolism. These conditions affect not only iron metabolism but mitochondrial function and systemic health. Therefore, this article also discusses these pathologies, including conditions of systemic and mitochondrial iron dysregulation as well as cancer. Literature covering these areas was identified via PubMed searches using keywords: Iron, mitochondria, Heme Synthesis, Iron-sulfur Cluster, and Cancer. References cited by publications retrieved using this search strategy were also consulted. Expert commentary: While much has been learned about mitochondrial and its iron, key questions remain. Developing a better understanding of mitochondrial iron and its regulation will be paramount in developing therapies for syndromes that affect mitochondrial iron.
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.
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
Weiss, G., & Goodnough, L. T. (2005) · New England Journal of Medicine · doi:10.1056/nejmra041809 · Cited by 3,800
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
Mitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803 · cited 2×
“ber of mitochondria per cell is dependent on cellular metabolic requirements and tissue types [4].”
BackgroundHeme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
The energetics of genome complexity.
Lane, N., & Martin, W. (2010) · Nature · doi:10.1038/nature09486 · Cited by 1,289
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
Mitoferrin is essential for erythroid iron assimilation
Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624
Structure of the human voltage-dependent anion channel
Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., Vonrhein, C., Griesinger, C., Zweckstetter, M., & Zeth, K. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808115105 · Cited by 588
A cytosolic iron chaperone that delivers iron to ferritin
Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536
Iron and cancer: recent insights
Manz, D. H., Blanchette, N. L., Paul, B. T., Torti, F. M., & Torti, S. V. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13008 · Cited by 507 · cited 3×
“ted that cancer cells exhibit higher iron retention than their nonmalignant counterparts [11,167].”
BackgroundSelf-citationLane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399 · cited 12×
“Once iron is transported through the outer mitochondrial membrane (OMM) and into the intermembrane space (IMS), it is transferred through the inner mitochondrial membrane (IMM) and into the mitochondrial matrix by mitoferrins (MFRN) and associated regulatory proteins (i.e. ATP Binding Cassette Subfamily B Member 10 [A…”
BackgroundInfluentialLouandre, C., Marcq, I., Bouhlal, H., Lachaier, E., Godin, C., Saidak, Z., François, C., Chatelain, D., Debuysscher, V., Barbare, J.-C., et al. (2015) · Cancer Letters · doi:10.1016/j.canlet.2014.11.014 · Cited by 374
Favaro, E., Ramachandran, A., McCormick, R., Gee, H., Blancher, C., Crosby, M., Devlin, C., Blick, C., Buffa, F., Li, J.-L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010345 · Cited by 324
Guernsey, D. L., Jiang, H., Campagna, D. R., Evans, S. C., Ferguson, M., Kellogg, M. D., Lachance, M., Matsuoka, M., Nightingale, M., Rideout, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.359 · Cited by 244
An iron regulatory gene signature predicts outcome in breast cancer
Miller, L. D., Coffman, L. G., Chou, J. W., Black, M. A., Bergh, J., D'Agostino, R., Torti, S. V., & Torti, F. M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1870 · Cited by 202 · cited 2×
“S cluster biogenesis and mitochondrial iron trafficking, were among 16 genes identified as an Iron Regulatory Gene Signature [166].”
BackgroundMaturation of cytosolic and nuclear iron–sulfur proteins
Netz, D. J. A., Mascarenhas, J., Stehling, O., Pierik, A. J., & Lill, R. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.11.005 · Cited by 184
Mitochondrial Ferritin: A New Player in Iron Metabolism
Drysdale, J., Arosio, P., Invernizzi, R., Cazzola, M., Volz, A., Corsi, B., Biasiotto, G., & Levi, S. (2002) · Blood Cells, Molecules, and Diseases · doi:10.1006/bcmd.2002.0577 · Cited by 180
Rauen, U., Springer, A., Weisheit, D., Petrat, F., Korth, H., de Groot, H., & Sustmann, R. (2007) · ChemBioChem · doi:10.1002/cbic.200600311 · Cited by 121
Langlois d'Estaintot, B., Santambrogio, P., Granier, T., Gallois, B., Chevalier, J. M., Précigoux, G., Levi, S., & Arosio, P. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.04.036 · Cited by 113
Taketani, S., Kohno, H., Okuda, M., Furukawa, T., & Tokunaga, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37318-0 · Cited by 88
Farhan, S. M. K., Wang, J., Robinson, J. F., Lahiry, P., Siu, V. M., Prasad, C., Kronick, J. B., Ramsay, D. A., Rupar, C. A., & Hegele, R. A. (2014) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.46 · Cited by 76
Congenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9
Schmitz-Abe, K., Ciesielski, S. J., Schmidt, P. J., Campagna, D. R., Rahimov, F., Schilke, B. A., Cuijpers, M., Rieneck, K., Lausen, B., Linenberger, M. L., et al. (2015) · Blood · doi:10.1182/blood-2015-09-659854 · Cited by 75
Cited by
The role of zinc, copper, manganese and iron in neurodegenerative diseases
Mezzaroba, L., Alfieri, D. F., Colado Simão, A. N., & Vissoci Reiche, E. M. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.07.007 · Cited by 524
Iron Metabolism in Obesity and Metabolic Syndrome
González-Domínguez, Á., Visiedo-García, F. M., Domínguez-Riscart, J., González-Domínguez, R., Mateos, R. M., & Lechuga-Sancho, A. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155529 · Cited by 227
Why cells need iron: a compendium of iron utilisation
Teh, M. R., Armitage, A. E., & Drakesmith, H. (2024) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2024.04.015 · Cited by 114
Smoking-induced iron dysregulation in the lung
Zhang, W. Z., Butler, J. J., & Cloonan, S. M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.024 · Cited by 62
Black, B., Lee, C., Horianopoulos, L. C., Jung, W. H., & Kronstad, J. W. (2021) · PLOS Pathogens · doi:10.1371/journal.ppat.1009661 · Cited by 51
Metadata
- Authors
- Paul, B. T., Manz, D. H., Torti, F. M., & Torti, S. V.
- Venue
- Expert Review of Hematology
- Publisher
- Informa UK Limited
- Published
- 2016-12-12
- Volume
- 10
- Issue
- 1
- Pages
- 65-79
- ISSN
- 1747-4086 (ISSN-L)
- 1747-4094
- OpenAlex
- W2559410759
- Cited by
- 423
- References
- 23
- FWCI
- 9.22
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
