The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Mitoferrin is essential for erythroid iron assimilation
Abstract
Iron has a fundamental role in many metabolic processes, including electron transport, deoxyribonucleotide synthesis, oxygen transport and many essential redox reactions involving haemoproteins and Fe-S cluster proteins. Defective iron homeostasis results in either iron deficiency or iron overload. Precise regulation of iron transport in mitochondria is essential for haem biosynthesis, haemoglobin production and Fe-S cluster protein assembly during red cell development. Here we describe a zebrafish mutant, frascati (frs), that shows profound hypochromic anaemia and erythroid maturation arrest owing to defects in mitochondrial iron uptake. Through positional cloning, we show that the gene mutated in the frs mutant is a member of the vertebrate mitochondrial solute carrier family (SLC25) that we call mitoferrin (mfrn). mfrn is highly expressed in fetal and adult haematopoietic tissues of zebrafish and mouse. Erythroblasts generated from murine embryonic stem cells null for Mfrn (also known as Slc25a37) show maturation arrest with severely impaired incorporation of 55Fe into haem. Disruption of the yeast mfrn orthologues, MRS3 and MRS4, causes defects in iron metabolism and mitochondrial Fe-S cluster biogenesis. Murine Mfrn rescues the defects in frs zebrafish, and zebrafish mfrn complements the yeast mutant, indicating that the function of the gene may be highly conserved. Our data show that mfrn functions as the principal mitochondrial iron importer essential for haem biosynthesis in vertebrate erythroblasts.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“For example, SLC25A37 encodes mitoferrin-1, an important iron introducer for the synthesis of heme and iron–sulfur clusters in erythroblast mitochondria”
From Red Blood Cells as Potential Repositories of MicroRNAs in the Circulatory System (2020) · cites this paper as Shaw et al., 2006
In the citing paper
“The mitoferrin transporters (Mitoferrin1 and Mitoferrin2) are responsible for the mitochondrial import of iron (Shaw et al., 2006; Troadec et al., 2011; Chung et al., 2014).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Shaw et al., 2006
In the citing paper
“Mitoferrin was originally discovered in yeast (called MRS3/MRS4 16 ) and in a mutant zebrafish.17”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [17]
In the citing paper
“Interestingly, mutations in mitoferrin result in a clinical disorder that is very similar to erythropoietic protoporphyria caused by ferrochelatase mutations.17”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [17]
In the citing paper
“The mitochondrial iron importer was recently identified as mitoferrin (also known as SLC25A37), a transmembrane protein that plays a critical role in supplying iron to ferrochelatase for insertion into protoporphyrin IX.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [17]
Citations
Cites
Effective targeted gene ‘knockdown’ in zebrafish
Nasevicius, A., & Ekker, S. C. (2000) · Nature Genetics · doi:10.1038/79951 · Cited by 2,485
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
Transplantation and in vivo imaging of multilineage engraftment in zebrafish bloodless mutants
Traver, D., Paw, B. H., Poss, K. D., Penberthy, W. T., Lin, S., & Zon, L. I. (2003) · Nature Immunology · doi:10.1038/ni1007 · Cited by 800
Self-citationIron–sulphur cluster biogenesis and mitochondrial iron homeostasis
Rouault, T. A., & Tong, W.-H. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1620 · Cited by 432
Kobayashi, K., Sinasac, D. S., Iijima, M., Boright, A. P., Begum, L., Lee, J. R., Yasuda, T., Ikeda, S., Hirano, R., Terazono, H., et al. (1999) · Nature Genetics · doi:10.1038/9667 · Cited by 418
Gregory, T. C., Yu, C., Ma, A. I., Orkin, S. H., Blobel, G. A., & Weiss, M. J. (1999) · Blood · doi:10.1182/blood.v94.1.87.413k41_87_96 · Cited by 385
Self-citationIron–sulfur-protein biogenesis in eukaryotes
Lill, R., & Mühlenhoff, U. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.01.006 · Cited by 333
Griffin, K. J. P., Amacher, S. L., Kimmel, C. B., & Kimelman, D. (1998) · Development · doi:10.1242/dev.125.17.3379 · Cited by 327
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 291
Characterization of zebrafish mutants with defects in embryonic hematopoiesis
Ransom, D. G., Haffter, P., Odenthal, J., Brownlie, A., Vogelsang, E., Kelsh, R. N., Brand, M., van Eeden, F. J. M., Furutani-Seiki, M., Granato, M., et al. (1996) · Development · doi:10.1242/dev.123.1.311 · Cited by 271
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 625
The BET Protein BRD2 Cooperates with CTCF to Enforce Transcriptional and Architectural Boundaries
Hsu, S. C., Gilgenast, T. G., Bartman, C., Edwards, C. R., Stonestrom, A. J., Huang, P., Emerson, D. J., Evans, P., Werner, M. T., Keller, C. A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.027 · Cited by 143
Iron metabolism and its contribution to cancer (Review)
Chen, Y., Fan, Z., Yang, Y., & Gu, C. (2019) · International Journal of Oncology · doi:10.3892/ijo.2019.4720 · Cited by 146
Ironing out mechanisms of iron homeostasis and disorders of iron deficiency
Koleini, N., Shapiro, J. S., Geier, J., & Ardehali, H. (2021) · Journal of Clinical Investigation · doi:10.1172/jci148671 · Cited by 161
Physiological and pathological roles of mitochondrial SLC25 carriers
Gutiérrez‐Aguilar, M., & Baines, C. P. (2013) · Biochemical Journal · doi:10.1042/bj20121753 · Cited by 140
Chaperone protein involved in transmembrane transport of iron
Yanatori, I., Yasui, Y., Tabuchi, M., & Kishi, F. (2014) · Biochemical Journal · doi:10.1042/bj20140225 · Cited by 139
The genetics of essential metal homeostasis during development
Kambe, T., Weaver, B. P., & Andrews, G. K. (2008) · genesis · doi:10.1002/dvg.20382 · Cited by 140
Rb intrinsically promotes erythropoiesis by coupling cell cycle exit with mitochondrial biogenesis
Sankaran, V. G., Orkin, & Walkley, C. R. (2008) · Genes & Development · doi:10.1101/gad.1627208 · Cited by 133
Francia, R. D., Crisci, S., Monaco, A. D., Cafiero, C., Re, A., Iaccarino, G., Filippi, R. D., Frigeri, F., Corazzelli, G., Micera, A., et al. (2021) · Cancers · doi:10.3390/cancers13050966 · Cited by 143
Courville, P., Chaloupka, R., & Cellier, M. F. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-193 · Cited by 134
Iron and Porphyrin Trafficking in Heme Biogenesis
Schultz, I. J., Chen, C., Paw, B. H., & Hamza, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.119503 · Cited by 131
Self-citationErythroid Heme Biosynthesis and Its DisordersPreprint
Dailey, H. A., & Meissner, P. N. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011676 · Cited by 130
Snx3 Regulates Recycling of the Transferrin Receptor and Iron Assimilation
Chen, C., Garcia-Santos, D., Ishikawa, Y., Seguin, A., Li, L., Fegan, K. H., Hildick-Smith, G. J., Shah, D. I., Cooney, J. D., Chen, W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.013 · Cited by 125
Self-citationFerecatu, I., Gonçalves, S., Golinelli‐Cohen, M., Clémancey, M., Martelli, A., Riquier, S., Guittet, É., Latour, J., Puccio, H. M., Drapier, J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.548438 · Cited by 125
Erythroid cell mitochondria receive endosomal iron by a “kiss-and-run” mechanism
Hamdi, A., Roshan, T., Kahawita, T. M., Mason, A. B., Sheftel, A. D., & Ponka, P. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.008 · Cited by 124
Lv, H., & Shang, P. (2018) · Metallomics · doi:10.1039/c8mt00048d · Cited by 127
Mupo, A., Seiler, M., Sathiaseelan, V., Pance, A., Yang, Y., Agrawal, A. A., Iorio, F., Bautista, R., Pacharne, S., Tzelepis, K., et al. (2016) · Leukemia · doi:10.1038/leu.2016.251 · Cited by 128
Molecular Mediators Governing Iron-Copper Interactions
Güleç, Ş., & Collins, J. F. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161215 · Cited by 122
Systemic iron homeostasis and erythropoiesis
Papanikolaou, G. V., & Pantopoulos, K. (2017) · IUBMB Life · doi:10.1002/iub.1629 · Cited by 128
Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis
Kardon, J. R., Yien, Y. Y., Huston, N. C., Branco, D. S., Hildick-Smith, G. J., Rhee, K. Y., Paw, B. H., & Baker, T. A. (2015) · Cell · doi:10.1016/j.cell.2015.04.017 · Cited by 118
Self-citationOptical/electrochemical methods for detecting mitochondrial energy metabolism
Ji, W., Tang, X. X., Du, W., Lu, Y., Wang, N., Wu, Q., Wei, W., Liu, J., Yu, H., Ma, B., et al. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01610a · Cited by 124
Self-citationMitochondrial iron accumulation with age and functional consequences
Seo, A. Y., Xu, J., Servais, S., Hofer, T., Marzetti, E., Wohlgemuth, S. E., Knutson, M. D., Chung, H. Y., & Leeuwenburgh, C. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00418.x · Cited by 127
A comprehensive joint analysis of the long and short RNA transcriptomes of human erythrocytes.
Doss, J. F., Corcoran, D. L., Jima, D. D., Telen, M. J., Dave, S. S., & Chi, J.-T. (2015) · BMC Genomics · doi:10.1186/s12864-015-2156-2 · Cited by 113
Jain, A., & Zoncu, R. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101481 · Cited by 122
Qian, Z., & Ke, Y. (2019) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12521 · Cited by 118
Iron: An Essential Element of Cancer Metabolism
Hsu, M. Y., Mina, E., Roetto, A., & Porporato, P. E. (2020) · Cells · doi:10.3390/cells9122591 · Cited by 119
Mitochondrial iron metabolism and neurodegenerative diseases
Cheng, R., Dhorajia, V. V., Kim, J., & Kim, Y. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.11.003 · Cited by 121
The essential nature of iron usage and regulation
Kaplan, J., & Ward, D. M. (2013) · Current Biology · doi:10.1016/j.cub.2013.05.033 · Cited by 115
Self-citationWhy 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
Lymphoblastoid Cell Lines in Pharmacogenomic Discovery and Clinical Translation
Wheeler, H. E., & Dolan, M. E. (2011) · Pharmacogenomics · doi:10.2217/pgs.11.121 · Cited by 118
Molecular Mechanism of Nramp-Family Transition Metal Transport
Bozzi, A. T., & Gaudet, R. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166991 · Cited by 117
Exploring whole-genome duplicate gene retention with complex genetic interaction analysis
Kuzmin, E., VanderSluis, B., Ba, A. N. N., Wang, W., Koch, E. N., Ušaj, M., Khmelinskii, A., Ušaj, M. M., van Leeuwen, J. S., Kraus, O. Z., et al. (2020) · Science · doi:10.1126/science.aaz5667 · Cited by 112
Vest, K. E., Leary, S. C., Winge, D. R., & Cobine, P. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470674 · Cited by 112
The Multifaceted Regulation of Mitochondria in Ferroptosis
Wu, H., Wang, F., Ta, N., Zhang, T., & Gao, W. (2021) · Life · doi:10.3390/life11030222 · Cited by 111
Froschauer, E. M., Schweyen, R. J., & Wiesenberger, G. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.03.004 · Cited by 110
Identification of the Mitochondrial Heme Metabolism Complex
Medlock, A. E., Shiferaw, M. T., Marcero, J. R., Vashisht, A. A., Wohlschlegel, J. A., Phillips, J. D., & Dailey, H. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135896 · Cited by 110
Cellular and mitochondrial iron homeostasis in vertebrates
Chen, C., & Paw, B. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.003 · Cited by 111
Self-citationHuman Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis
Stehling, O., Netz, D. J. A., Niggemeyer, B., Rösser, R., Eisenstein, R. S., Puccio, H. M., Pierik, A. J., & Lill, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00545-08 · Cited by 107
Sirtuins' control of autophagy and mitophagy in cancer
Aventaggiato, M., Vernucci, E., Barreca, F., Russo, M. A., & Tafani, M. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107748 · Cited by 103
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
Congenital Sideroblastic Anemias: Iron and Heme Lost in Mitochondrial Translation
Fleming, M. D. (2011) · Hematology · doi:10.1182/asheducation-2011.1.525 · Cited by 103
Regulation of iron pathways in response to hypoxia
Chepelev, N. L., & Willmore, W. G. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.023 · Cited by 106
Targeted deletion of the mouse Mitoferrin1 gene: from anemia to protoporphyria
Troadec, M.-B., Warner, D., Wallace, J., Thomas, K., Spangrude, G. J., Phillips, J., Khalimonchuk, O., Paw, B. H., Ward, D. M., & Kaplan, J. (2011) · Blood · doi:10.1182/blood-2010-11-319483 · Cited by 97
Alterations in Cellular Iron Metabolism Provide More Therapeutic Opportunities for Cancer
Zhou, L., Zhao, B., Zhang, L., Wang, S., Dong, D., Lv, H., & Shang, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051545 · Cited by 102
Shi, X., Reinstadler, B. M., Shah, H., To, T., Byrne, K., Summer, L. C., Calvo, S. E., Goldberger, O., Doench, J. G., Mootha, V. K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30126-9 · Cited by 104
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 103
Mitochondrial involvement in genetically determined transition metal toxicity
Mehta, R., Templeton, D. M., & O'Brien, P. J. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.05.011 · Cited by 104
Iron transport in the kidney: implications for physiology and cadmium nephrotoxicity
Thévenod, F., & Wolff, N. A. (2015) · Metallomics · doi:10.1039/c5mt00215j · Cited by 101
Jouihan, H. A., Cobine, P. A., Cooksey, R. C., Hoagland, E. A., Boudina, S., Abel, E. D., Winge, D. R., & McClain, D. A. (2008) · Molecular Medicine · doi:10.2119/2007-00114.jouihan · Cited by 103
Garrick, M. D., & Garrick, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.018 · Cited by 105
Mrs3p, Mrs4p, and Frataxin Provide Iron for Fe-S Cluster Synthesis in Mitochondria
Zhang, Y., Lyver, E. R., Knight, S. A. B., Pain, D., Lesuisse, E., & Dancis, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604246200 · Cited by 98
Iron–sulfur cluster biosynthesis and trafficking – impact on human disease conditions
Wachnowsky, C., Fidai, I., & Cowan, J. A. (2017) · Metallomics · doi:10.1039/c7mt00180k · Cited by 99
Compartmentalization of iron between mitochondria and the cytosol and its regulation
Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95
H+-Coupled Divalent Metal-Ion Transporter-1
Shawki, A., Knight, P. B., Maliken, B. D., Niespodzany, E. J., & Mackenzie, B. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394316-3.00005-3 · Cited by 100
Heme metabolism and erythropoiesis
Chung, J., Chen, C., & Paw, B. H. (2012) · Current Opinion in Hematology · doi:10.1097/moh.0b013e328351c48b · Cited by 96
Self-citationThe human reticulocyte transcriptome
Goh, S., Josleyn, M. D., Lee, Y. T., Danner, R. L., Gherman, R. B., Cam, M. C., & Miller, J. L. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00247.2006 · Cited by 93
A Small Molecule Inhibitor of Redox-Regulated Protein Translocation into Mitochondria
Dabir, D. V., Hasson, S. A., Setoguchi, K., Johnson, M. E., Wongkongkathep, P., Douglas, C. J., Zimmerman, J., Damoiseaux, R. D., Teitell, M. A., & Koehler, C. M. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.03.006 · Cited by 92
Involvement of cytosolic and mitochondrial iron in iron overload cardiomyopathy: an update
Gordan, R., Wongjaikam, S., Gwathmey, J. K., Chattipakorn, N., Chattipakorn, S. C., & Xie, L. (2018) · Heart Failure Reviews · doi:10.1007/s10741-018-9700-5 · Cited by 92
Special delivery: distributing iron in the cytosol of mammalian cells
Philpott, C. C., & Ryu, M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00173 · Cited by 96
The Plant Mitochondrial Carrier Family: Functional and Evolutionary Aspects
Haferkamp, I., & Schmitz‐Esser, S. (2012) · Frontiers in Plant Science · doi:10.3389/fpls.2012.00002 · Cited by 100
A general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 97
Mitochondrial Atpif1 regulates haem synthesis in developing erythroblasts
Shah, D. I., Takahashi‐Makise, N., Cooney, J. D., Li, L., Schultz, I. J., Pierce, E. L., Narla, A., Seguin, A., Hattangadi, S. M., Medlock, A. E., et al. (2012) · Nature · doi:10.1038/nature11536 · Cited by 93
Self-citationDown the Iron Path: Mitochondrial Iron Homeostasis and Beyond
Dietz, J. V., Fox, J. L., & Khalimonchuk, O. (2021) · Cells · doi:10.3390/cells10092198 · Cited by 98
Redox Regulation of SCO Protein Function: Controlling Copper at a Mitochondrial Crossroad
Leary, S. C. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3116 · Cited by 89
Iron control of erythroid development by a novel aconitase-associated regulatory pathway
Bullock, G. C., Delehanty, L. L., Talbot, A.-L., Gonias, S. L., Tong, W.-H., Rouault, T. A., Dewar, B., Macdonald, J. M., Chruma, J. J., & Goldfarb, A. N. (2010) · Blood · doi:10.1182/blood-2009-10-251496 · Cited by 85
Iron and the heart: A paradigm shift from systemic to cardiomyocyte abnormalities
Paterek, A., Mackiewicz, U., & Ma̧czewski, M. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28820 · Cited by 88
Guo, Q., Qian, C., Wang, X., & Qian, Z. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01436-x · Cited by 91
Hartford, C. M., Duan, S., Delaney, S. M., Mi, S., Kistner, E. O., Lamba, J. K., Huang, R. S., & Dolan, M. E. (2008) · Blood · doi:10.1182/blood-2008-05-154302 · Cited by 84
Red Blood Cells as Potential Repositories of MicroRNAs in the Circulatory System
Sun, L., Yu, Y., Niu, B., & Wang, D. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00442 · Cited by 83
Zooming in and out of ferroptosis in human disease
Wang, X., Zhou, Y., Min, J., & Wang, F. (2023) · Frontiers of Medicine · doi:10.1007/s11684-023-0992-z · Cited by 85
Self-citationMechanisms of Pathogenesis in Drug Hepatotoxicity Putting the Stress on Mitochondria
Jones, D. P., Lemasters, J. J., Han, D., Boelsterli, U. A., & Kaplowitz, N. (2010) · Molecular Interventions · doi:10.1124/mi.10.2.7 · Cited by 83
Kesarwani, A. K., Ramirez, O., Gupta, A. K., Yang, X., Murthy, T., Minella, A. C., & Pillai, M. M. (2016) · Oncogene · doi:10.1038/onc.2016.279 · Cited by 86
Heme Levels Are Increased in Human Failing Hearts
Khechaduri, A., Bayeva, M., Chang, H., & Ardehali, H. (2013) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2013.02.012 · Cited by 80
Expression and putative role of mitochondrial transport proteins in cancer
Lytovchenko, O., & Kunji, E. R. S. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.03.006 · Cited by 80
Metzendorf, C., & Lind, M. (2010) · BMC Developmental Biology · doi:10.1186/1471-213x-10-68 · Cited by 82
Mitochondrial iron overload: causes and consequences
Rouault, T. A. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.02.004 · Cited by 80
A possible role for secreted ferritin in tissue iron distribution
Meyron‐Holtz, E. G., Moshe-Belizowski, S., & Cohen, L. A. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0582-0 · Cited by 78
Shvartsman, M., Kikkeri, R. V., Shanzer, A., & Cabantchik, Z. I. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00054.2007 · Cited by 78
Mitochondrial Metal Ion Transport in Cell Metabolism and Disease
Wang, X., An, P., Gu, Z., Luo, Y., & Luo, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147525 · Cited by 77
A π-Helix Switch Selective for Porphyrin Deprotonation and Product Release in Human Ferrochelatase
Medlock, A. E., Dailey, T. A., Ross, T. A., Dailey, H. A., & Lanzilotta, W. N. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.08.040 · Cited by 77
Recycling Iron in Normal and Pathological States
Beaumont, C., & Delaby, C. (2009) · Seminars in Hematology · doi:10.1053/j.seminhematol.2009.06.004 · Cited by 84
Recent advances in the understanding of inherited sideroblastic anaemia
Camaschella, C. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07290.x · Cited by 79
The mTORC1/4E-BP pathway coordinates hemoglobin production with L -leucine availability
Chung, J., Bauer, D. E., Ghamari, A., Nizzi, C. P., Deck, K. M., Kingsley, P. D., Yien, Y. Y., Huston, N. C., Chen, C., Schultz, I. J., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aaa5903 · Cited by 84
Self-citationFrom the discovery to molecular understanding of cellular iron-sulfur protein biogenesis
Lill, R. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0117 · Cited by 73
Ferroptosis: Biochemistry and Biology in Cancers
Shi, Z., Zhang, L., Zheng, J., Sun, H., & Shao, C. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.579286 · Cited by 76
Iron, oxidative stress and the example of solar ultraviolet a radiation.
Aroun, A., Zhong, J. L., Tyrrell, R. M., & Pourzand, C. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05204g · Cited by 74
Iron: Effect of Overload and Deficiency
Hider, R. C., & Kong, X. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_8 · Cited by 78
The influence of ferucarbotran on the chondrogenesis of human mesenchymal stem cells
Henning, T. D., Sutton, E. J., Kim, A. E., Golovko, D. M., Horvai, A., Ackerman, L. D., Sennino, B., McDonald, D. M., Lotz, J. C., & Daldrup-Link, H. E. (2009) · Contrast Media & Molecular Imaging · doi:10.1002/cmmi.276 · Cited by 74
Intracellular Trafficking of Porphyrins
Hamza, I. (2006) · ACS Chemical Biology · doi:10.1021/cb600442b · Cited by 74
Mitochondrial iron transport and homeostasis in plants
Jain, A., & Connolly, E. L. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00348 · Cited by 73
Mechanisms of divalent metal toxicity in affective disorders
Menon, A. V., Chang, J., & Kim, J. (2015) · Toxicology · doi:10.1016/j.tox.2015.11.001 · Cited by 77
Ferroptosis—A New Dawn in the Treatment of Organ Ischemia–Reperfusion Injury
Zhou, L., Han, S., Guo, J., Qiu, T., Zhou, J., & Shen, L. (2022) · Cells · doi:10.3390/cells11223653 · Cited by 75
TMEM14C is required for erythroid mitochondrial heme metabolism
Yien, Y. Y., Robledo, R. F., Schultz, I. J., Takahashi‐Makise, N., Gwynn, B., Bauer, D. E., Dass, A., Yi, G., Li, L., Hildick-Smith, G. J., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci76979 · Cited by 72
Self-citationYanatori, I., Richardson, D. R., Toyokuni, S., & Kishi, F. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.776021 · Cited by 69
Bruce, S. J., Gardiner, B., Burke, L. J., Gongora, M., Grimmond, S. M., & Perkins, A. C. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-365 · Cited by 70
Glycine and Folate Ameliorate Models of Congenital Sideroblastic Anemia
Fernández-Murray, J. P., Prykhozhij, S. V., Dufay, J. N., Steele, S. L., Gaston, D., Nasrallah, G. K., Coombs, A. J., Liwski, R., Fernandez, C. V., Berman, J. N., et al. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1005783 · Cited by 68
Hung, H., Schwartz, J. M., Maldonado, E. N., Lemasters, J. J., & Nieminen, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422667 · Cited by 67
The Role of Hepcidin in Iron Homeostasis and Anemia in Hemodialysis Patients
Eleftheriadis, T., Liakopoulos, V., Antoniadi, G., Kartsios, C., & Stefanidis, I. (2009) · Seminars in Dialysis · doi:10.1111/j.1525-139x.2008.00532.x · Cited by 66
Iron homeostasis: new players, newer insights
Edison, E. S., Bajel, A. R., & Chandy, M. (2008) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2008.01143.x · Cited by 71
The Interaction of Mitochondrial Iron with Manganese Superoxide Dismutase
Naranuntarat, A., Jensen, L. T., Pazicni, S., Penner-Hahn, J. E., & Culotta, V. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026773 · Cited by 66
Mitoferrin, Cellular and Mitochondrial Iron Homeostasis
Ali, M. Y., Oliva, C. R., Flor, S., & Griguer, C. E. (2022) · Cells · doi:10.3390/cells11213464 · Cited by 66
Metadata
- Authors
- 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., Trede, N. S., Barut, B. A., Zhou, Y., Minet, E., Donovan, A., Brownlie, A., Balzan, R., Weiss, M. J., Peters, L. L., Kaplan, J., Zon, L. I., & Paw, B. H.
- Affiliations
- Brigham and Women's Hospital (US)
- University of Utah (US)
- Boston Children's Hospital (US)
- Jackson Laboratory (US)
- University of Malta (MT)
- Children's Hospital of Philadelphia (US)
- Corresponding author
- Paw, Barry H.
- ORCID
- Venue
- Nature
- Published
- 2006-03
- Volume
- 440
- Issue
- 7080
- Pages
- 96-100
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1972998779
- Cited by
- 624
- References
- 30
- Citations by year
- 2026: 23 · 2025: 32 · 2024: 40 · 2023: 29 · 2022: 24 · 2021: 38 · 2020: 56 · 2019: 26 · 2018: 24 · 2017: 29 · 2016: 30 · 2015: 27 · 2014: 32 · 2013: 28 · 2012: 30
- FWCI
- 16.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (P01HL032262, R01HL075714)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK070838)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- heme biosynthesis, erythroblasts, erythroid maturation, hypochromic anemia, SLC25A37, iron-sulfur cluster assembly, iron homeostasis, positional cloning
- MeSH terms
- Anemia, Animals, Cell Differentiation, Erythroblasts, Gene Expression Regulation, Genetic Complementation Test, Heme, Homeostasis, Humans, Iron, Iron-Sulfur Proteins, Mitochondria, Molecular Sequence Data, Mutation, Phylogeny, Saccharomyces cerevisiae, Stem Cells, Zebrafish, Conserved Sequence, Iron Overload, Mitochondrial Proteins, Membrane Transport Proteins, Cation Transport Proteins, Saccharomyces cerevisiae Proteins, Zebrafish 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
