Mitoferrin is essential for erythroid iron assimilation

Effective targeted gene ‘knockdown’ in zebrafish

Nasevicius, A., & Ekker, S. C. (2000) · Nature Genetics · doi:10.1038/79951 · Cited by 2,485

Balancing Acts

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

Iron–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

The gene mutated in adult-onset type II citrullinaemia encodes a putative mitochondrial carrier protein

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

GATA-1 and Erythropoietin Cooperate to Promote Erythroid Cell Survival by Regulating bcl-xL Expression

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

Iron–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

Molecular identification of spadetail: regulation of zebrafish trunk and tail mesoderm formation by T-box genes

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

Endosome Traffic Modulates Pro-Inflammatory Signal Transduction in CD4+ T Cells—Implications for the Pathogenesis of Systemic Lupus Erythematosus

Park, J. S., & Perl, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310749 · 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

Hypoxia induces erythroid‐specific 5‐aminolevulinate synthase expression in human erythroid cells through transforming growth factor‐β signaling

Kaneko, K., Furuyama, K., Aburatani, H., & Shibahara, S. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06878.x · Cited by 14

Identification and Characterization of an Inhibitory Metal Ion-binding Site in Ferrochelatase

Hunter, G. A., & Ferreira, G. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.174243 · Cited by 14

Metal Homeostasis in Plant Mitochondria

Vigani, G., & Hanikenne, M. (2018) · Wiley eBooks · doi:10.1002/9781119312994.apr0547 · Cited by 14

Ferroptosis and pyroptosis: Mediating mechanisms of the cGAS/STING pathway and therapeutic strategies in heart failure

Zhang, Z., Yang, Z., Wang, S., Wang, X., & Mao, J. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102932 · Cited by 13

Targeting Mitochondrial Metal Dyshomeostasis for the Treatment of Neurodegeneration

Liddell, J. R. (2015) · Neurodegenerative Disease Management · doi:10.2217/nmt.15.19 · Cited by 13

Cellular Iron Physiology

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

Melanosomes in pigmented epithelia maintain eye lens transparency during zebrafish embryonic development

Takamiya, M., Xu, F., Suhonen, H., Gourain, V., Yang, L., Ho, N. Y., Helfen, L., Schröck, A., Etard, C., Grabher, C., et al. (2016) · Scientific Reports · doi:10.1038/srep25046 · Cited by 13

NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis

Cai, K., & Markley, J. L. (2018) · Molecules · doi:10.3390/molecules23092213 · Cited by 15

Ferroptosis as an Emerging Target in Diabetic Osteoporosis

Li, C., Gong, H., Zhang, Y., Shi, P., Liu, S., & Zhang, Q. (2025) · The FASEB Journal · doi:10.1096/fj.202500415r · Cited by 13

Mössbauer Study and Modeling of Iron Import and Trafficking in Human Jurkat Cells

Jhurry, N. D., Chakrabarti, M., McCormick, S. P., Gohil, V. M., & Lindahl, P. A. (2013) · Biochemistry · doi:10.1021/bi401015t · Cited by 12

Prime Real Estate: Metals, Cofactors and MICOS

Medlock, A. E., Hixon, J. C., Bhuiyan, T., & Cobine, P. A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.892325 · Cited by 12

Influence of mitochondrial and systemic iron levels in heart failure pathology

Lupu, M., Tudor, D. V., & Filip, G. A. (2019) · Heart Failure Reviews · doi:10.1007/s10741-019-09788-z · Cited by 13

Molecular basis of hereditary iron homeostasis defects

Horváthová, M., Ponka, P., & Divoký, V. (2010) · Hematology · doi:10.1179/102453310x12583347009810 · Cited by 12

The peculiar properties of mitochondrial carriers of the SLC25 family

Kunji, E. R. S., Mavridou, V., King, M. S., Cimadamore‐Werthein, C., Baron, S. J., Jones, S. A., King, A. C., Springett, R., Chand, D., Palmer, S. M., et al. (2025) · Biochemical Journal · doi:10.1042/bcj20253171 · Cited by 15

Trace and essential elements as vital components to improve the performance of the male reproductive system: Implications in cell signaling pathways

Morabbi, A., & Karimian, M. (2024) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2024.127403 · Cited by 13

Electromagnetic fields regulate iron metabolism in living organisms: A review of effects and mechanism

Zhen, C., Zhang, G., Wang, S., Wang, J., Fang, Y., & Shang, P. (2024) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2024.03.001 · Cited by 12

Mitochondrial Dysfunctions: Genetic and Cellular Implications Revealed by Various Model Organisms

Stańczyk, M., Szubart, N., Maślanka, R., & Zadrąg‐Tęcza, R. (2024) · Genes · doi:10.3390/genes15091153 · Cited by 12

Fighting ischemia-reperfusion injury: Focusing on mitochondria-derived ferroptosis

Tian, L., Liu, Q., Guo, H. W., Zang, H., & Li, Y. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101974 · Cited by 15

Synaptic Activity Regulates Mitochondrial Iron Metabolism to Enhance Neuronal Bioenergetics

Tena‐Morraja, P., Riqué‐Pujol, G., Müller‐Sánchez, C., Reina, M., Martínez-Estrada, O. M., & Soriano, F. X. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020922 · Cited by 11

Mitoferrin-1 Promotes Proliferation and Abrogates Protein Oxidation via the Glutathione Pathway in Glioblastoma

Ali, M. Y., Griguer, C. E., Flor, S., & Oliva, C. R. (2023) · Antioxidants · doi:10.3390/antiox12020349 · Cited by 11

Gfi1aa and Gfi1b set the pace for primitive erythroblast differentiation from hemangioblasts in the zebrafish embryo

Moore, C., Richens, J. L., Hough, Y., Ucanok, D., Malla, S., Sang, F., Chen, Y., Elworthy, S., Wilkinson, R. N., & Gering, M. (2018) · Blood Advances · doi:10.1182/bloodadvances.2018020156 · Cited by 12

Iron deficiency anemia, anemia of chronic disorders and iron overload

Pippard, M. J. (2011) · Elsevier eBooks · doi:10.1016/b978-0-7020-3147-2.00011-0 · Cited by 13

Blood co-expression modules identify potential modifier genes of diabetes and lung function in cystic fibrosis

Pineau, F., Caimmi, D. P., Magalhães, M., Fremy, E., Mohamed, A., Mély, L., Leroy, S., Murris, M., Claustres, M., Chiron, R., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0231285 · Cited by 11

Emerging role of tumor microenvironmental nutrients and metabolic molecules in ferroptosis: Mechanisms and clinical implications

Li, D., Zhang, Z., & Wang, L. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117406 · Cited by 10

The Emerging Role of RNA N6-Methyladenosine Modification in Pancreatic Cancer

Hu, X., Lei, X., Guo, J., Fu, W., Sun, W. Y., Lu, Q., Su, W., Xu, Q., & Tu, K. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.927640 · Cited by 10

Antagonistic roles of the ERK and p38 MAPK signalling pathways in globin expression, haem biosynthesis and iron uptake1

Mardini, L., Gasiorek, J. J., Derjuga, A., Carrière, L., Schranzhofer, M., Paw, B. H., Ponka, P., & Blank, V. (2010) · Biochemical Journal · doi:10.1042/bj20100541 · Cited by 10

Studying disorders of vertebrate iron and heme metabolism using zebrafish

van der Vorm, L. N., & Paw, B. H. (2016) · Methods in cell biology · doi:10.1016/bs.mcb.2016.10.008 · Cited by 10

Strong correlation of ferrochelatase enzymatic activity with Mitoferrin-1 mRNA in lymphoblasts of patients with protoporphyria

Phillips, J. D., Farrell, C., Wang, Y., Singal, A. K., Anderson, K. E., Balwani, M., Bissell, M., Bonkovsky, H. L., Seay, T., Paw, B. H., et al. (2018) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2018.10.005 · Cited by 10

Recent Endeavors on Molecular Imaging for Mapping Metals in Biology

Gao, J., Chen, Y., Guo, Z., & He, W. (2020) · Biophysics Reports · doi:10.1007/s41048-020-00118-7 · Cited by 11

Proteins of Iron Homeostasis

Srai, S. K., & Sharp, P. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_1 · Cited by 11

Induction of the mitochondrial permeability transition (MPT) by micromolar iron: Liberation of calcium is more important than NAD(P)H oxidation

Gáll, J., Škrha, J., Buchal, R., Sedláčková, E., Verébová, K., & Pláteník, J. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.05.008 · Cited by 10

The role of hepcidin, GDF15, and mitoferrin-1 in iron metabolism of polycythemia vera and essential thrombocytosis patients

ALBAYRAK, C., Tarkun, P., Ateşoğlu, E. B., ERALDEMİR, C., Özsoy, Ö. D., Demirsoy, E. T., Mehtap, Ö., & Gedük, A. (2019) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.3906/sag-1803-13 · Cited by 9

Long non-coding RNA ZFAS1 promotes ferroptosis by regulating the miR-185-5p/SLC25A28 axis in clear cell renal cell carcinoma

Tao, Q., Li, Y., Zhang, W., Zhang, M., Li, X., Jin, H., Zheng, J., & Li, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140602 · Cited by 10

Endogenous small molecule effectors in GATA transcription factor mechanisms governing biological and pathological processes

Liao, R., & Bresnick, E. H. (2024) · Experimental Hematology · doi:10.1016/j.exphem.2024.104252 · Cited by 12

Mitoferrin2 is a synthetic lethal target for chromosome 8p deleted cancers

Krieg, S., Rohde, T. D., Rausch, T., Butthof, L., Wendler-Link, L., Eckert, C., Breuhahn, K., Galy, B., Korbel, J. O., Billmann, M., et al. (2024) · Genome Medicine · doi:10.1186/s13073-024-01357-w · Cited by 14

Iron transport by proteoliposomes containing mitochondrial F1Fo ATP synthase isolated from rat heart

Kim, M.-S., & Song, E. (2010) · Biochimie · doi:10.1016/j.biochi.2010.01.014 · Cited by 9

A role for iron deficiency in dopaminergic neurodegeneration

Yien, Y. Y., & Paw, B. H. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601976113 · Cited by 9

Splitting the functions of Rim2, a mitochondrial iron/pyrimidine carrier

Knight, S. A. B., Yoon, H., Pandey, A. K., Pain, J., Pain, D., & Dancis, A. (2019) · Mitochondrion · doi:10.1016/j.mito.2018.12.005 · Cited by 9

ABCs of erythroid mitochondrial iron uptake

Andrews, N. C. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909137106 · Cited by 9

Iron homeostasis in a mouse model of thalassemia intermedia is altered between adolescence and adulthood

Sanyear, C., Butthep, P., Eamsaard, W., Fucharoen, S., Svasti, S., & Masaratana, P. (2020) · PeerJ · doi:10.7717/peerj.8802 · Cited by 9

Fighting ferroptosis: Protective effects of dexmedetomidine on vital organ injuries

Tian, L., Liu, Q., Wang, X., Chen, S., & Li, Y. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122949 · Cited by 8

Ferroptosis in Cerebral Ischemia/Reperfusion Injury: Mechanistic Drivers and Therapeutic Frontiers

Song, C., Liu, Z., Tang, J., & Huang, Y. (2026) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s580170 · Cited by 13

Optical Imaging Opportunities to Inspect the Nature of Cytosolic Iron Pools

Hider, R. C., Pourzand, C., Ma, Y., & Cilibrizzi, A. (2023) · Molecules · doi:10.3390/molecules28186467 · Cited by 8

Low-Iron Diet-Induced Fatty Liver Development Is Microbiota Dependent and Exacerbated by Loss of the Mitochondrial Iron Importer Mitoferrin2

Klag, K. A., Bell, R. S., Jia, X., Seguin, A., Maschek, J. A., Bronner, M. P., Cox, J. E., Round, J. L., & Ward, D. M. (2024) · Nutrients · doi:10.3390/nu16121804 · Cited by 9

Cancer Therapeutic Potential and Prognostic Value of the SLC25 Mitochondrial Carrier Family: A Review

Gao, R., Zhou, D., Qiu, X., Zhang, J., Luo, D., Yang, X., Qian, C., & Liu, Z. (2024) · Cancer Control · doi:10.1177/10732748241287905 · Cited by 16

Comparative hematopoiesis and signal transduction in model organisms

Gautam, D. K., Chimata, A. V., Gutti, R. K., & Paddibhatla, I. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30287 · Cited by 8

Iron and mitochondria in the susceptibility, pathogenesis and progression of COPD

Faherty, L., Kenny, S., & Cloonan, S. M. (2023) · Clinical Science · doi:10.1042/cs20210504 · Cited by 9

Erythroid Iron Metabolism

Ponka, P., & Sheftel, A. D. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_10 · Cited by 8

Transethnic meta-analysis suggests genetic variation in the HEME pathway influences potassium response in patients treated with hydrochlorothiazide

Del‐Aguila, J. L., Cooper‐DeHoff, R. M., Chapman, A. B., Gums, J. G., Beitelshees, A. L., Bailey, K. R., Turner, S. T., Johnson, J. A., & Boerwinkle, E. (2014) · The Pharmacogenomics Journal · doi:10.1038/tpj.2014.46 · Cited by 8

Establishment of a cell model of X-linked sideroblastic anemia using genome editing

Kaneko, K., Kubota, Y., Nomura, K., Hayashimoto, H., Chida, T., Yoshino, N., Wayama, M., Ogasawara, K., Nakamura, Y., Tooyama, I., et al. (2018) · Experimental Hematology · doi:10.1016/j.exphem.2018.06.002 · Cited by 8

Unlocking mitochondrial drug targets: The importance of mitochondrial transport proteins

Hoogstraten, C. A., Schirris, T. J. J., & Rüssel, F. G. M. (2024) · Acta Physiologica · doi:10.1111/apha.14150 · Cited by 7

Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release

Gillam, M. E., Hunter, G. A., & Ferreira, G. C. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.02.015 · Cited by 7

New Insights into the Evolution and Gene Structure of the Mitochondrial Carrier Family Unveiled by Analyzing the Frequent and Conserved Intron Positions

Monné, M., Cianciulli, A., Panaro, M. A., Calvello, R., Grassi, A., Palmieri, L., Mitolo, V., & Palmieri, F. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad051 · Cited by 7

Cardiolipin deficiency leads to the destabilization of mitochondrial magnesium channel MRS2 in Barth syndrome

Joshi, A., & Gohil, V. M. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad153 · Cited by 7

The Therapeutic Potential of Targeting Ferroptosis in the Treatment of Mitochondrial Cardiomyopathies and Heart Failure

Cantrell, A. C., Zeng, H., & Chen, J. (2023) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001496 · Cited by 8

Murine mutants in the study of systemic iron metabolism and its disorders: An update on recent advances

Bartnikas, T. B., Fleming, M. D., & Schmidt, P. J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.011 · Cited by 7

Iron kinetics and laboratory assessment

Doig, K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-323-53045-3.00017-9 · Cited by 7

Iron and metabolic rewiring in cancer

Ciscar, M., Rodríguez-Santana, C., & Santana-Codina, N. (2026) · Oncogenesis · doi:10.1038/s41389-025-00595-w · Cited by 11

The Hepatic Porphyrias: Revealing the Complexities of a Rare Disease

Balogun, O., & Nejak‐Bowen, K. N. (2023) · Seminars in Liver Disease · doi:10.1055/s-0043-1776760 · Cited by 8

Erythropoiesis in Teleost Fishes: The Fantastic Biological Process

Zhong, A., & Yan, X. (2024) · Reviews in Aquaculture · doi:10.1111/raq.12960 · Cited by 6

Lytic regulated cell death in aquaculture fish

Xia, X., He, B., Zhang, X., Cheng, Z., Liu, M., Wei, X., Jiang, J., & Hu, J. (2021) · Reviews in Aquaculture · doi:10.1111/raq.12533 · Cited by 6

Can Iron Play a Crucial Role in Maintaining Cardiovascular Health in the 21st Century?

Szklarz, M., Gontarz-Nowak, K., Matuszewski, W., & Bandurska-Stankiewicz, E. M. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph191911990 · Cited by 6

Iron-loaded extracellular vesicles: angel or demon?

Chen, H., & Tang, Y. (2023) · Free Radical Research · doi:10.1080/10715762.2023.2191813 · Cited by 6

Cooperative contributions of the klf1 and klf17 genes in zebrafish primitive erythropoiesis

Suzuki, H., Ogawa, T., Fujita, S., Sone, R., & Kawahara, A. (2023) · Scientific Reports · doi:10.1038/s41598-023-39196-1 · Cited by 6

Role of iron overload and ferroptosis in heart disease

Cai, Z., Min, J., Wang, H., Fang, X., & Wang, F. (2019) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2019-0242 · Cited by 6

Leukemia‐associated transcription factor mllt3 is important for primitive erythroid development in zebrafish embryogenesis

Germanò, G., Porazzi, P., & Felix, C. A. (2022) · Developmental Dynamics · doi:10.1002/dvdy.477 · Cited by 6

TLX1 (HOX11) Immortalization of Embryonic Stem Cell–Derived and Primary Murine Hematopoietic Progenitors

Hawley, R. G., Hawley, T. S., & Cantor, A. B. (2008) · Current Protocols in Stem Cell Biology · doi:10.1002/9780470151808.sc01f07s7 · Cited by 6

Heme Biosynthesis and Its Disorders

Fuller, S. J., & Wiley, J. S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-323-35762-3.00038-x · Cited by 6

Mitochondrial respiration supports cancer growth independent of OXPHOS

Chinopoulos, C. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189593 · Cited by 5

MitoNEET preserves muscle insulin sensitivity during iron overload by regulating mitochondrial iron, reactive oxygen species and fission

Tam, E., Nguyen, K. D., Sung, H. K., & Sweeney, G. (2024) · FEBS Journal · doi:10.1111/febs.17214 · Cited by 6

Haematometabolism rewiring in atherosclerotic cardiovascular disease

Yvan‐Charvet, L., Barouillet, T., & Borowczyk, C. (2025) · Nature Reviews Cardiology · doi:10.1038/s41569-024-01108-9 · Cited by 7

A new ferritin SjFer0 affecting the growth and development of Schistosoma japonicum

Zeng, F., Yi, C., Zhang, W., Cheng, S., Sun, C., Luo, F., Feng, Z., & Hu, W. (2022) · Parasites & Vectors · doi:10.1186/s13071-022-05247-1 · Cited by 5

Identification and Functional Analysis of Two Mitoferrins, CsMIT1 and CsMIT2, Participating in Iron Homeostasis in Cucumber

Małas, K., & Kabała, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24055050 · Cited by 5

Hsp90 and metal‐binding J‐protein family chaperones are not critically involved in cellular iron–sulfur protein assembly and iron regulation in yeast

Carvalho, F. A., Mühlenhoff, U., Braymer, J. J., Root, V., Stümpfig, M., Oliveira, C. C., & Lill, R. (2023) · FEBS Letters · doi:10.1002/1873-3468.14612 · Cited by 5

The Cellular Physiology of Iron

Anderson, G. J., & Vulpe, C. D. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-462-9_1 · Cited by 5

Association between Mitochondrial Bioenergetics and Radiation- Related Fatigue: A Possible Mechanism and Novel Target

Hsiao, C. P. (2015) · Archives in Cancer Research · doi:10.21767/2254-6081.100014 · Cited by 5

Disorders of iron metabolism

Dietzen, D. J., & Diab, Y. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-817962-8.00026-3 · Cited by 6

Métabolisme du fer : physiologie et pathologie

Beaumont, C., & Girot, R. (2010) · Encyclopédie médico-chirurgicale. Hématologie · doi:10.1016/s1155-1984(10)49948-3 · Cited by 7

[Iron metabolism, overview and recent insights].

Omar, S., Feki, M., & Kaabachi, N. (2006) · PubMed · Cited by 5

Energy Metabolism | Mitochondrial Transporters of the Solute Carrier 25 (SLC25) Superfamily

Palmieri, F. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00060-8 · Cited by 5

Research Progress on Ferroptosis Regulation of Female Reproduction

Wang, Z., Li, S., Xie, X., Zeng, X., Zhao, X., Wang, X., Jiang, D., & Kang, B. (2025) · Biological Trace Element Research · doi:10.1007/s12011-025-04818-4 · Cited by 5

RNA‐Based Biomarkers of Iron Metabolism in Dried Blood Spots for Detecting Recombinant Human Erythropoietin in Doping Control

Liu, X., Yan, T., Xu, Y., Zheng, X., & Wu, D. (2025) · Drug Testing and Analysis · doi:10.1002/dta.3870 · Cited by 4

Identification of ferroptosis-related genes as diagnostic biomarkers and therapeutic targets in sorafenib-resistant HCC via machine learning and experimental validation

Zhang, J., Geng, W., Sun, H., Chen, J., Fan, Y., & Tan, K. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115557 · Cited by 4

Exploring the Impact of Iron Overload on Mitochondrial DNA in β-Thalassemia: A Comprehensive Review

Narahari, J. M., Guruswamy, P., Jagadeesha, N. M., Shivashakar, K. K., Kumar, D. P., Narayana, P. S., Vishwanath, P. M., & Prashant, A. (2024) · Gene Expression · doi:10.14218/ge.2023.00128 · Cited by 4

In vitro reconstitution of transition metal transporters

Ongey, E. L., & Banerjee, A. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107589 · Cited by 5

Blood removal therapy in hereditary hemochromatosis induces a stress response resulting in improved genome integrity

Distante, S., Eikeland, J., Pawar, T., Skinnes, R., Høie, K., You, P., Mørkrid, L., & Eide, L. (2016) · Transfusion · doi:10.1111/trf.13588 · Cited by 4

Genome Evolutionary Dynamics Meets Functional Genomics: A Case Story on the Identification of SLC25A44

Darbani, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115669 · Cited by 4

Iron

Tenenbein, M., & Huang, X. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822946-0.00016-7 · Cited by 5

Iron-sulfur clusters: Basic building blocks for life

Lill, R. (2007) · Cited by 4

hem6: an ENU-induced recessive hypochromic microcytic anemia mutation in the mouse

Tian, M., Campagna, D. R., Woodward, L. S., Justice, M. J., & Fleming, M. D. (2008) · Blood · doi:10.1182/blood-2007-09-111500 · Cited by 4

The Central Role of the Liver in Iron Storage and Regulation of Systemic Iron Homeostasis

Rouault, T. A., Gordeuk, V. R., & Anderson, G. J. (2009) · Wiley eBooks · doi:10.1002/9780470747919.ch16 · Cited by 4

Role and regulation of iron metabolism in erythropoiesis and disease

Arvedson, T., & Sasu, B. J. (2009) · Birkhäuser Basel eBooks · doi:10.1007/978-3-7643-8698-6_15 · Cited by 4

Cellular Iron Homeostasis

Philpott, C. C., & Meyron‐Holtz, E. G. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_2 · Cited by 3

Protein iron transporters as potential therapeutic targets in cancer: A review

Banerjee, R., Bintee, B., Hegde, M., BharathwajChetty, B., Alqahtani, M. S., Abbas, M., Alqahtani, A., Sethi, G., Rangan, L., Ma, Z., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.146695 · Cited by 4

Characterization of a nucleus located mollusc mitoferrin and its response to OsHV-1 infection

Xin, L., Huang, B., Li, C., Bai, C.-M. C., & Wang, C. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.10.014 · Cited by 3

Cellular and Molecular Biology of Iron-Binding Proteins

Kalinowski, D. S., & Richardson, D. R. (2010) · CRC Press eBooks · doi:10.1201/9781420059984-c7 · Cited by 3

Targeted Disruption of the Mouse Mitoferrin (Slc25A37) Mitochondrial Solute Carrier Results in Defective Primitive and Definitive Erythropoiesis.

Paw, B. H., Gwynn, B., Langer, N. B., Shaw, G., Lambert, A. J., Boyer, L. A., Li, L., Stolte, J., Robledo, R. F., Sahr, K. E., et al. (2006) · Blood · doi:10.1182/blood.v108.11.265.265 · Cited by 6

Iron Does Not “Jiggle Free” in Mitochondria: Is Mitoferrin the Only Answer?.

Paw, B. H. (2008) · Blood · doi:10.1182/blood.v112.11.sci-27.sci-27

Abcb10 Physically Interacts with Mitoferrin1 to Enhance Its Stability for Heme Synthesis in the Erythroid Mitochondria

Chen, W., Li, L., Langer, N. B., Paradkar, P. N., Schultz, I. J., Hyde, B. B., Shirihai, O. S., Kaplan, J., & Paw, B. H. (2008) · Blood · doi:10.1182/blood.v112.11.530.530

Mitochondrial Iron Transport Via MFRN1 Is Required for Erythroid Cell Cycle Progression Even Under Iron-Replete Conditions Sufficient for Hemoglobinization

Perfetto, M., Danoff, A., Ishfaq, M., Mohideen, A., Chen, M., Stratman, A. N., Okawa, S., & Yien, Y. Y. (2024) · Blood · doi:10.1182/blood-2024-203047

Mitoferrin1 Transgenic Zebrafish Line Serves as a Model to Study Erythroid Cell Fate during Hematopoiesis

Amigo, J. D., Yu, M., dos Santos, C. O., Paradkar, P. N., Cooney, J. D., Kaplan, J., Weiss, M. J., Cantor, A. B., & Paw, B. H. (2008) · Blood · doi:10.1182/blood.v112.11.3576.3576 · Cited by 1