The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells
Open accessAbstract
The reduction of iron is an essential step in the transferrin (Tf) cycle, which is the dominant pathway for iron uptake by red blood cell precursors. A deficiency in iron acquisition by red blood cells leads to hypochromic, microcytic anemia. Using a positional cloning strategy, we identified a gene, six-transmembrane epithelial antigen of the prostate 3 (Steap3), responsible for the iron deficiency anemia in the mouse mutant nm1054. Steap3 is expressed highly in hematopoietic tissues, colocalizes with the Tf cycle endosome and facilitates Tf-bound iron uptake. Steap3 shares homology with F(420)H(2):NADP(+) oxidoreductases found in archaea and bacteria, as well as with the yeast FRE family of metalloreductases. Overexpression of Steap3 stimulates the reduction of iron, and mice lacking Steap3 are deficient in erythroid ferrireductase activity. Taken together, these findings indicate that Steap3 is an endosomal ferrireductase required for efficient Tf-dependent iron uptake in erythroid cells.
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
“The freed ferric iron is then reduced to its bio-active ferrous form, Fe2+ by the ferrireductase STEAP3 (six-transmembrane epithelial antigen of prostate 3) and shuttled into the cytosol from the endosome by DMT1 (Fleming et al., 1997; Gunshin et al., 1997; Ohgami et al., 2005; Figure 1).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Ohgami et al., 2005
In the citing paper
“At either location, Dmt1 only accepts ferrous iron along with other divalent cations, such as copper or manganese, and co-localizes with an iron reductase [152, 177].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [177]
In the citing paper
“Liberated inorganic iron is then reduced by the ferrireductase STEAP3 to Fe 2ϩ , 10 which is the substrate for transmembrane transport by divalent metal transporter 1 (DMT1 or SLC11A2, formerly called NRAMP2, DCT1).”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [10]
In the citing paper
“Both STEAP3 and DMT1 were discovered through positional cloning of genes altered in rodents carrying spontaneous mutations impairing iron transport.10,11”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [10]
In the citing paper
“Amino acid and serum depletion activate autophagy, resulting in ferritin degradation, which sensitized cells to H2O2-induced oxidative stress because of an increased “labile iron” pool, which caused ROS production via the Fenton reaction (226).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [226]
In the citing paper
“Lysosome-mediated ferritin degradation uses the autophagy system under particular conditions (173, 226) and iron chelator treatment (165)”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [226]
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
The Pfam Protein Families Database
Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,075
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166
The Pfam protein families database
Bateman, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh121 · Cited by 3,127
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
Self-citationAn iron-regulated ferric reductase associated with the absorption of dietary iron
McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., et al. (2001) · Science · doi:10.1126/science.1057206 · Cited by 1,101
Fleming, M. D., Romano, M. A., Su, M. A., Garrick, L. M., Garrick, M. D., & Andrews, N. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.1148 · Cited by 936
Self-citationPonka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544
Ross, J. S., Sheehan, C. E., Fisher, H. A. �., Kaufman, R. P., Kaur, P., Gray, K., Webb, I. J., Gray, G. S., Mosher, R. E., & Kallakury, B. (2003) · PubMed · Cited by 502
Flemming (1998) · Medical Entomology and Zoology · Cited by 412
STEAP: A prostate-specific cell-surface antigen highly expressed in human prostate tumors
Hubert, R., Vivanco, I., Chen, E., Rastegar, S., Leong, K., Mitchell, S. C., Madraswala, R., Zhou, Y., Kuo, J., Raitano, A. B., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14523 · Cited by 353
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 779
Role of carbonic anhydrases in ferroptosis-resistance
Li, Z., Jiang, L., & Toyokuni, S. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108440 · Cited by 24
Stathopoulou, M. G., Kanoni, S., Papanikolaou, G. V., Antonopoulou, S., Nomikos, T., & Dedoussis, G. V. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-398397-8.00009-5 · Cited by 25
van Aerts, R. M. M., van Deursen, C. T. B. M., & Koek, G. H. (2015) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2015.06.043 · Cited by 25
Feng, R., Wang, D., Li, T., Liu, X., Peng, T., Liu, M., Ren, G., Xu, H., Luo, H., Lu, D., et al. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.89368 · Cited by 23
McKenzie, C. W., Preston, C. C., Finn, R., Eyster, K. M., Faustino, R. S., & Lee, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-31743-5 · Cited by 24
Zhou, D., Zhang, Y., Mamtawla, G., Wan, S., Gao, X., Zhang, L., Li, G., & Wang, X. (2020) · Medical Oncology · doi:10.1007/s12032-020-01439-w · Cited by 23
The Usefulness of STEAP Proteins in Prostate Cancer Clinical Practice
Rocha, S. M., Barroca-Ferreira, J., Passarinha, L. A., Socorro, S., & Maia, C. J. (2021) · Exon Publications eBooks · doi:10.36255/exonpublications.prostatecancer.steap.2021 · Cited by 23
Halcrow, P. W., Kumar, N., Afghah, Z., Fischer, J. P., Khan, N., Chen, X., Meucci, O., & Geiger, J. D. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15583 · Cited by 23
Research progress of iron metabolism in retinal diseases
Li, C., Xiao, C., Tao, H., & Tang, X. (2023) · Advances in Ophthalmology Practice and Research · doi:10.1016/j.aopr.2023.02.001 · Cited by 23
Yu, B., Liu, J., Cai, Z., Wang, H., Feng, X., Zhang, T., Ma, R., Gu, Y., & Zhang, J. (2023) · Poultry Science · doi:10.1016/j.psj.2023.102793 · Cited by 23
Steere, A. N., Chasteen, N. D., Miller, B., Smith, V. C., MacGillivray, R. T. A., & Mason, A. B. (2012) · Biochemistry · doi:10.1021/bi3001038 · Cited by 23
Pathophysiology of the Belgrade rat
Veuthey, T., & Wessling‐Resnick, M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00082 · Cited by 23
The iron islands: Erythroblastic islands and iron metabolism
Yeo, J. H., Colonne, C. K., Tasneem, N., Cosgriff, M. P., & Fraser, S. T. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.10.019 · Cited by 25
Chen, X., Huang, Z., Zhou, B., Wang, H., Jia, G., Liu, G., & Zhao, H. (2014) · Endocrine · doi:10.1007/s12020-014-0230-1 · Cited by 23
The role of duodenal cytochrome b in intestinal iron absorption remains unclear
Frazer, D. M., Wilkins, S. J., Vulpe, C. D., & Anderson, G. J. (2005) · Blood · doi:10.1182/blood-2005-07-2923 · Cited by 23
Abdizadeh, H., & Atılgan, C. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp05107j · Cited by 22
Zhang, D., Liu, H., Wang, W., Xu, G., Yin, C., & Wang, S. (2022) · Cancer Biology & Therapy · doi:10.1080/15384047.2022.2136465 · Cited by 22
Mesenchymal stem cells and ferroptosis: Clinical opportunities and challenges
Cui, M., Chen, F., Shao, L., Wei, C., Zhang, W., Sun, W., & Wang, J. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e25251 · Cited by 22
Trafficking regulator of GLUT4-1 (TRARG1) is a GSK3 substrate
Duan, X., Norris, D. M., Humphrey, S. J., Yang, P., Cooke, K. C., Bultitude, W. P., Parker, B. L., Conway, O. J., Burchfield, J. G., Krycer, J. R., et al. (2022) · Biochemical Journal · doi:10.1042/bcj20220153 · Cited by 23
A ferrireductase fills the gap in the transferrin cycle
McKie, A. T. (2005) · Nature Genetics · doi:10.1038/ng1105-1159 · Cited by 22
Molecular regulation of hepatic expression of iron regulatory hormone hepcidin
Oates, P. S., & Ahmed, U. (2007) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2007.04950.x · Cited by 22
Ferroptosis-related genes involved in animal reproduction: An Overview
Gan, J., Gu, T., Hong, L., & Cai, G. (2022) · Theriogenology · doi:10.1016/j.theriogenology.2022.02.022 · Cited by 22
Chen, X., Hu, S., Han, Y., Cai, Y., Lu, T., Hu, X., Chu, Y., Zhou, X., & Wang, X. (2023) · Clinical and Experimental Medicine · doi:10.1007/s10238-023-00996-4 · Cited by 21
Acyl-CoA binding protein and epidermal barrier function
Bloksgaard, M., Neess, D., Færgeman, N. J., & Mandrup, S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.09.013 · Cited by 21
Ponka, P., Tenenbein, M., & Eaton, J. W. (2014) · Elsevier eBooks · doi:10.1016/b978-0-444-59453-2.00041-x · Cited by 20
Yoo, S. K., Cheong, J., & Kim, H. Y. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.8456 · Cited by 22
STEAP Proteins: Roles in disease biology and potential for therapeutic intervention
Cai, Q., Jing, C., Wang, X., Xing, X., & Liu, W. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142797 · Cited by 20
Balušíková, K., Neubauerová, J., Dostalikova‐Cimburova, M., Horák, J., & Kovár̆, J. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9926-y · Cited by 20
Waki, H., & Tontonoz, P. (2007) · Cell · doi:10.1016/j.cell.2007.04.022 · Cited by 21
Role of Macromolecular Crowding on Stability and Iron Release Kinetics of Serum Transferrin
Kumar, S., Sharma, D., & Kumar, R. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b05702 · Cited by 21
Iron deficiency anaemia and iron overload
Worwood, M., & May, A. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-7020-3408-4.00009-6 · Cited by 20
Loss of rapid transferrin receptor recycling due to a mutation in Sec15l1 in hbd mice
Garrick, M. D., & Garrick, L. M. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.09.032 · Cited by 20
Zhang, A., Canonne‐Hergaux, F., Gruenheid, S., Gros, P., & Ponka, P. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.04.014 · Cited by 20
Cardiac iron metabolism during aging – Role of inflammation and proteolysis
Walter, S., Mertens, C., Muckenthaler, M. U., & Ott, C. (2023) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2023.111869 · Cited by 19
Fe(III) Is Essential for Porcine Embryonic Development via Mitochondrial Function Maintenance
Zhao, M., Liang, S., Kim, S.-H., Cui, X., & Kim, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130791 · Cited by 19
Yadav, N., Kannan, D., Patil, S., Singh, S., & Lochab, B. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c00632 · Cited by 18
Host and microbiota derived extracellular vesicles: Crucial players in iron homeostasis
Daou, Y., Falabrègue, M., Pourzand, C., Peyssonnaux, C., & Edeas, M. A. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.985141 · Cited by 19
Massaiu, I., Campodonico, J., Mapelli, M., Salvioni, E., Valerio, V., Moschetta, D., Myasoedova, V. A., Cappellini, M. D., Pompilio, G., Poggio, P., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032887 · Cited by 18
Ponka, P., Tenenbein, M., & Eaton, J. W. (2007) · Elsevier eBooks · doi:10.1016/b978-012369413-3/50085-9 · Cited by 19
Involvement of 101F6, a Homologue of Cytochrome b561, in the Reduction of Ferric Ions
Mizutani, A., Sanuki, R., Kakimoto, K., Kojo, S., & Taketani, S. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm185 · Cited by 18
Iron Metabolism and Muscle Aging: Where Ferritinophagy Meets Mitochondrial Quality Control
Lorenzo, R. D., Marzetti, E., Coelho‐Júnior, H. J., Calvani, R., Pesce, V., Landi, F., Leeuwenburgh, C., & Picca, A. (2025) · Cells · doi:10.3390/cells14090672 · Cited by 18
Zhou, B., Li, J., Wu, A., Wang, X., Cheng, L., Yang, G., Gao, D., & Zhu, C. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1587986 · Cited by 18
The role of magnetic nanoparticles in dark fermentation
Hidalgo, D., Martín-Marroquín, J. M., & Corona, F. (2023) · Biomass Conversion and Biorefinery · doi:10.1007/s13399-023-04103-1 · Cited by 18
Forston, M. D., Wei, G. Z., Chariker, J. H., Stephenson, T., Andres, K. R., Glover, C., Rouchka, E. C., Whittemore, S. R., & Hetman, M. (2023) · Scientific Reports · doi:10.1038/s41598-023-48425-6 · Cited by 17
Xia, P., Köberle, M., & Ghashghaeinia, M. (2024) · Antioxidants · doi:10.3390/antiox13080968 · Cited by 17
Treating incurable non-communicable diseases by targeting iron metabolism and ferroptosis
Ni, R., Jiang, J., Wang, F., & Min, J. (2025) · Science China Life Sciences · doi:10.1007/s11427-024-2787-y · Cited by 19
Targeting mineral metabolism in cancer: Insights into signaling pathways and therapeutic strategies
Bhatnagar, K., Raju, S., Patki, N., Motiani, R. K., & Chaudhary, S. (2025) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2025.02.011 · Cited by 17
Louvel, H. ̈., Kanai, T., Atomi, H., & Reeve, J. N. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01594.x · Cited by 17
Batool, M., Berghausen, E. M., Zierden, M., Vantler, M., SCHERMULY, R. T., Baldus, S. E., Rosenkranz, S., & ten Freyhaus, H. (2020) · Basic Research in Cardiology · doi:10.1007/s00395-020-00826-8 · Cited by 17
Role for copper in the cellular and regulatory effects of heme-hemopexin
Smith, A., Rish, K. R., Lovelace, R., Hackney, J. F., & Helston, R. M. (2008) · BioMetals · doi:10.1007/s10534-008-9178-z · Cited by 17
Iron acquisition inLeishmaniaand its crucial role in infection
NIU, Q., Li, S., Chen, D., CHEN, Q., & Chen, J. (2016) · Parasitology · doi:10.1017/s0031182016000858 · Cited by 17
Self-citationSTEAP4 expression in CNS resident cells promotes Th17 cell-induced autoimmune encephalomyelitis
Zhao, J., Liao, Y., Miller-Little, W. A., Xiao, J., Liu, C., Li, X., Li, X., & Kang, Z. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02146-7 · Cited by 16
Wei, Q., Xue, C., Li, M., Wei, J., Zheng, L., Chen, S., Duan, Y., Deng, H., Tang, F., Xiong, W., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-023-2474-4 · Cited by 16
Insights into the pathogenesis of gestational and hepatic diseases: the impact of ferroptosis
You, Y., Qian, Z., Jiang, Y., Chen, L., Wu, D., Liu, L., Zhang, F., Ning, X., Zhang, Y., & Xiao, J. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1482838 · Cited by 18
Duan, W.-L., Gu, L., Guo, A., Wang, X.-J., Ding, Y.-Y., Zhang, P., Zhang, B., Li, Q., & Yang, L. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5544 · Cited by 18
Impact of TET2 deficiency on iron metabolism in erythroblasts
Inokura, K., Fujiwara, T., Saito, K., Iino, T., Hatta, S., Okitsu, Y., Fukuhara, N., Onishi, Y., Ishizawa, K., Shimoda, K., et al. (2017) · Experimental Hematology · doi:10.1016/j.exphem.2017.01.002 · Cited by 16
Differential Expression and Function of Stamp Family Proteins in Adipocyte Differentiation
Sikkeland, J., & Saatcioglu, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068249 · Cited by 16
Iron as a Therapeutic Target in HFE-Related Hemochromatosis: Usual and Novel Aspects
Loréal, O., Cavey, T., Robin, F., Kenawi, M., Guggenbuhl, P., & Brissot, P. (2018) · Pharmaceuticals · doi:10.3390/ph11040131 · Cited by 17
Subha Palaneeswari, M. (2013) · JOURNAL OF CLINICAL AND DIAGNOSTIC RESEARCH · doi:10.7860/jcdr/2013/6420.3273 · Cited by 19
Iron-deficiency anemia secondary to mutations in genes controlling hepcidin
Cau, M., Melis, M. A., Congiu, R., & Galanello, R. (2010) · Expert Review of Hematology · doi:10.1586/ehm.10.2 · Cited by 16
Du, L., Zhang, Y., Luo, J., He, C., Lang, J., & Cao, X. (2026) · Experimental Hematology and Oncology · doi:10.1186/s40164-025-00737-1 · Cited by 15
Yuan, J., Li, Z., Lin, Z., Yao, S., Han, Y., Fu, Q., & Liu, J. (2022) · Microbes and Infection · doi:10.1016/j.micinf.2022.104999 · Cited by 15
Deng, L., Zeng, S., Yi, Q., & Song, L. (2023) · PeerJ · doi:10.7717/peerj.15136 · Cited by 15
Kim, S. Y., Tang, M., Lu, T., Chih, S. Y., & Li, W. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149045 · Cited by 17
Zhou, J., Bu, D.-R., Zhao, X. F., Wu, F., Chen, X.-Q., Shi, H., Yao, C., Du, A., & Yang, Y. (2020) · Parasites & Vectors · doi:10.1186/s13071-020-3911-z · Cited by 15
DNA Methylation-Driven Genes for Developing Survival Nomogram for Low-Grade Glioma
Guo, Y., Li, Y., Li, J., Tao, W., & Dong, W. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2021.629521 · Cited by 15
Zhang, Q., Steensma, D. P., Yang, J., Dong, T., & Wu, M. X. (2018) · Leukemia · doi:10.1038/s41375-018-0204-z · Cited by 16
Glanfield, A., McManus, D. P., Smyth, D. J., Lovas, E. M., Loukas, A. C., Gobert, G. N., & Jones, M. K. (2010) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000884 · Cited by 15
Singh, A. K., Mohan, M. L., Isaac, A. O., Luo, X., Petrák, J., Vyoral, D., & Singh, N. (2009) · PLoS ONE · doi:10.1371/annotation/194f4e44-20f0-48eb-bbe9-14e21d18909b · Cited by 15
Petriaggi, L., Giorgio, E., Natali, G. A. E. P. G., Galeano, C., Furtado, S. R., Faniello, M. C., Costanzo, F. S., Biamonte, F., & Battaglia, A. M. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl39675 · Cited by 14
NCOA4-mediated ferritinophagy: emerging role and novel therapeutic target in precision oncology
Chen, D., Jiang, X., Duan, T., Tian, Y., Zhang, J., Wang, X., & Tan, J. (2026) · Autophagy · doi:10.1080/15548627.2026.2656779 · Cited by 14
Zhao, J., Liu, Z., Zheng, X., Gao, H., & Li, L. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.753680 · Cited by 14
Role of Mitochondrial Iron Uptake in Acetaminophen Hepatotoxicity
Hu, J., Nieminen, A., Zhong, Z., & Lemasters, J. J. (2024) · Livers · doi:10.3390/livers4030024 · Cited by 14
RBC-GEM: A genome-scale metabolic model for systems biology of the human red blood cell
Haiman, Z. B., Key, A., D’Alessandro, A., & Palsson, B. Ø. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1012109 · Cited by 14
Direct thermodynamic and kinetic measurements of Fe2+ and Zn2+ binding to human serum transferrin
Terpstra, T., McNally, J., Han, T.-H.-L., Duong, N.-T. H., Chahine, J. E. H., & Bou‐Abdallah, F. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.03.007 · Cited by 14
Rish, K. R., Swartzlander, R., Sadikot, T., Berridge, M. V., & Smith, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.003 · Cited by 14
The Roles of DMT1 in Inflammatory and Degenerative Diseases
Liu, H., Li, M., Deng, Y. X., Hou, Y., Hou, L., Zhang, X., Zheng, Z., Guo, F., & Sun, K. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04687-x · Cited by 14
Cytoplasmic and Nuclear Localization of TCTP in Normal and Cancer Cells
Ma, Y.-P., & Zhu, W.-L. (2012) · Biochemistry Research International · doi:10.1155/2012/871728 · Cited by 13
Human STEAP3 mutations with no phenotypic red cell changes
Liu, D., Yi, S., Zhang, X., Fang, P., Zheng, C., Lin, L., Cai, R., Ye, Y., Zhou, Y., Liang, Y., et al. (2015) · Blood · doi:10.1182/blood-2015-09-670174 · Cited by 13
Sun, L., Lin, X., Pornprasert, S., Lü, X., Ran, B., & Lin, Y. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173513 · Cited by 13
The Placental Ferroxidase Zyklopen Is Not Essential for Iron Transport to the Fetus in Mice
Helman, S. L., Wilkins, S. J., McKeating, D. R., Perkins, A. V., Whibley, P. E., Cuffe, J. S. M., Simmons, D. G., Fuqua, B. K., Vulpe, C. D., Wallace, D. F., et al. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab174 · Cited by 13
Membrane-Bound Flavocytochrome MsrQ Is a Substrate of the Flavin Reductase Fre in Escherichia coli
Caux‐Thang, C., Guigliarelli, B., Vivès, C., Biaso, F., Horeau, M., Hassoune, H., Petit-Härtlein, I., Juillan‐Binard, C., Torelli, S., Fieschi, F., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00613 · Cited by 13
Taleb, M., Maillet, I., Bert, M. L., & Mura, C. (2022) · Blood · doi:10.1182/blood.2021014493 · Cited by 13
Muckenthaler, M. U., & Lill, R. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_2 · Cited by 13
Regulation of heme biosynthesis and transport in metazoa
Sun, F., Cheng, Y., & Chen, C. (2015) · Science China Life Sciences · doi:10.1007/s11427-015-4885-5 · Cited by 14
Mithen, R. F. (2007) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831.77.3.205 · Cited by 13
Dubey, Y., Mansuri, S., & Kanvah, S. (2024) · Journal of Materials Chemistry B · doi:10.1039/d4tb00353e · Cited by 12
Kasakura, K., Kawakami, Y., Jacquet, A., & Kawakami, T. (2022) · The Journal of Immunology · doi:10.4049/jimmunol.2200276 · Cited by 12
Torrez, C. R. Z., Easley, A., Bouamar, H., Zheng, G., Gu, X., Yang, J., Chiu, Y., Chen, Y., Halff, G. A., Cigarroa, F. G., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-63368-2 · Cited by 12
Exploring the Fe(III) binding sites of human serum transferrin with EPR at 275 GHz
Mathies, G., Gast, P., Chasteen, N. D., Luck, A. N., Mason, A. B., & Groenen, E. J. J. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1229-z · Cited by 12
STAMPs at the Crossroads of Cancer and Nutrition
Lindstad, T., Jin, Y., Wang, L., Qu, S., & Saatcioglu, F. (2010) · Nutrition and Cancer · doi:10.1080/01635581.2010.509836 · Cited by 12
Olfactory ferric and ferrous iron absorption in iron-deficient rats
Kumara, V. M. R., & Wessling‐Resnick, M. (2012) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00004.2012 · Cited by 12
The requirement of iron transport for lymphocyte function
Lo, B. (2015) · Nature Genetics · doi:10.1038/ng.3478 · Cited by 12
Zhou, J. T., Zhao, H., Huang, Z., Ye, X., Zhang, L., Li, Q., Zhao, Z., Su, X., Liu, G., & Du, J. C. (2020) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2020.100741 · Cited by 12
Flaherty, M. M., Rish, K. R., Smith, A., & Crumbliss, A. L. (2007) · BioMetals · doi:10.1007/s10534-007-9112-9 · Cited by 12
Bossart, J., Rippl, A., Alston, A. E. B., Flühmann, B., Digigow, R. G., Buljan, M., Ayala‐Nunez, V., & Wick, P. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115404 · Cited by 11
Zhao, Z., Yu, P., Wang, Y., Hong, L., Qiao, H., Sun, C., Zhu, L., & Yang, P. (2024) · Cancer & Metabolism · doi:10.1186/s40170-024-00370-2 · Cited by 11
Myocardium-specific Isca1 knockout causes iron metabolism disorder and myocardial oncosis in rat
Ling, Y., Yang, X., Zhang, X., Guan, F., Qi, X., Dong, W., Liu, M., Ma, J., Jiang, X., Gao, K., et al. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120485 · Cited by 11
Noncoding RNAs in cancer ferroptosis: From biology to clinical opportunity
Shan, C., Liang, Y., Wang, K., & Li, P. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115053 · Cited by 11
Iron homeostasis and post-hemorrhagic hydrocephalus: a review
Pan, S., Hale, A. T., Lemieux, M., Raval, D. K., Garton, T. P., Sadler, B. E., Mahaney, K. B., & Strahle, J. M. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2023.1287559 · Cited by 11
Metadata
- Authors
- Ohgami, R. S., Campagna, D. R., Greer, E. L., Antiochos, B., McDonald, A., Chen, J., Sharp, J. J., Fujiwara, Y., Barker, J. E., & Fleming, M. D.
- Affiliations
- Harvard University (US)
- Takeda Oncology (United States) (US)
- Brigham and Women's Hospital (US)
- Emory University (US)
- Boston Children's Hospital (US)
- Jackson Laboratory (US)
- Corresponding author
- Fleming, Mark D
- ORCID
- Venue
- Nature Genetics
- Published
- 2005-10-16
- Volume
- 37
- Issue
- 11
- Pages
- 1264-1269
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- PMC
- PMC2156108
- OpenAlex
- W2069774708
- Cited by
- 775
- References
- 33
- Citations by year
- 2026: 35 · 2025: 48 · 2024: 48 · 2023: 60 · 2022: 52 · 2021: 47 · 2020: 41 · 2019: 28 · 2018: 41 · 2017: 23 · 2016: 22 · 2015: 31 · 2014: 28 · 2013: 30 · 2012: 45
- FWCI
- 16.60
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL074247)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK049216, R01DK027726)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Physical Sciences › Materials Science › Metals and Alloys › Iron and Steelmaking Processes
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- ferrireductase, STEAP3, erythroid cells, iron deficiency anemia, positional cloning, red blood cell precursors
- MeSH terms
- Amino Acid Sequence, Animals, Antigens, Neoplasm, Cells, Cultured, Erythrocytes, Female, Iron, Kidney, Male, Mice, Mutant Strains, Molecular Sequence Data, Oxidoreductases, Endosomes, Retroviridae, Subcellular Fractions, Transferrin, Blotting, Western, Sequence Homology, Amino Acid, Gene Targeting, Anemia, Iron-Deficiency, FMN Reductase, 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