The DOI matches its Crossref record; 109 of the 110 references it cites were found in a registry or an index.
Ironing out Ferroportin
Open accessAbstract
Maintaining physiologic iron concentrations in tissues is critical for metabolism and host defense. Iron absorption in the duodenum, recycling of iron from senescent erythrocytes, and iron mobilization from storage in macrophages and hepatocytes constitute the major iron flows into plasma for distribution to tissues, predominantly for erythropoiesis. All iron transfer to plasma occurs through the iron exporter ferroportin. The concentration of functional membrane-associated ferroportin is controlled by its ligand, the iron-regulatory hormone hepcidin, and fine-tuned by regulatory mechanisms serving iron homeostasis, oxygen utilization, host defense, and erythropoiesis. Fundamental questions about the structure and biology of ferroportin remain to be answered.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Aberrant ferroportin activity can lead to diseases of iron overload, like hemochromatosis, or iron limitation anemias 2 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“In mammals, iron levels are regulated by the action of hepcidin, a peptide hormone, on ferroportin (FPN), the only known iron efflux transporter 2-4 (Fig. 1a).”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
The cited source says what the claim attributes to it.
In the citing paper
“The cryo-EM density map of FPN enabled building of an atomic model of FPN regions important for iron transport and hepcidin binding 2,7 , and a portion of the intracellular loop 3 (ICL3) important in hepcidin-induced FPN internalization 8-10 (Extended Data Fig. 5).”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
In the citing paper
“The expression of FPN is tightly regulated at the transcriptional, posttranscriptional, and posttranslational levels.8”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
In the citing paper
“In duodenal enterocytes, transcription of the Fpn gene, which encodes ferroportin, is regulated by iron and hypoxia to increase the absorption of dietary iron during iron deficiency and anemia.8,54”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
In the citing paper
“Taken together, these data support that FPN expression is tightly controlled at both transcriptional and/or the translational levels,8,68,69 which allow multiple and diverse physiological effects to influence FPN activity at its various sites of expression.”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
In the citing paper
“On average, humans ingest 20–25 mg of iron/day, the majority of which is inorganic iron (85%–90%), followed by haem‐bound iron (10%–15%).”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“In mammals, excretion of iron is not extensively regulated; instead, iron homeostasis is achieved mainly by regulating intestinal absorption in the duodenum, 9 and possibly in the colon to some extent. 10”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“However, only ~ 1 mg iron is absorbed per day, because of both poor iron bioavailability and tightly regulated iron homeostasis. 9 , 11”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“In conditions of iron accumulation, the production of HAMP is stimulated, and, as a result, iron is subsequently trapped within enterocytes and macrophages, respectively inhibiting iron export to circulation or preventing recycling of iron derived from red blood cells. 9”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“The iron regulatory hormone hepcidin limits iron fluxes to the bloodstream by promoting degradation of the iron exporter ferroportin in target cells.”
From Pharmacological Targeting of the Hepcidin/Ferroportin Axis (2016) · cites this paper as Drakesmith et al., 2015
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
2 retracted
RETRACTED: The Hepcidin-Binding Site on Ferroportin Is Evolutionarily Conserved
Domenico, I. D., Nemeth, E., Nelson, J. M., Phillips, J. D., Ajioka, R. S., Kay, M. S., Kushner, J. P., Ganz, T., Ward, D. M., & Kaplan, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.002 · Cited by 127
Self-citationRetractedDomenico, I. D., Lo, E., Yang, B., Korolnek, T., Hamza, I., Ward, D. M., & Kaplan, J. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.09.008 · Cited by 27
RetractedExploring the full spectrum of macrophage activation
Mosser, D. M., & Edwards, J. P. (2008) · Nature Reviews Immunology · doi:10.1038/nri2448 · Cited by 9,144
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803
Self-citationPositional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422
Dysmetabolic Hyperferritinemia: All Iron Overload Is Not Hemochromatosis
Makker, J. S., Hanif, A., Bajantri, B., & Chilimuri, S. S. (2015) · Case Reports in Gastroenterology · doi:10.1159/000373883 · Cited by 1,353
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275
A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267
Nicolas, G., Bennoun, M., Devaux, I., Beaumont, C., Grandchamp, B., Kahn, A., & Vaulont, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151179498 · Cited by 1,233
Flagged first, then by citations
1 of the 110 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Altamura, 2011, Mouse models for ferroportin with impaired hepcidin regulation, Am. J. Hematol., 86, E42
- Preza, 2011, Minihepcidins are rationally designed small peptides that mimic hepcidin activity in mice and may be useful for the treatment of iron overload, J. Clin. Invest., 121, 4880, 10.1172/JCI57693 · DOI · Paper page
Cited by
Sorted by citations
Items 301–400 of 631
Serum hepcidin / ferroportin levels in bipolar disorder and schizophrenia
Altun, İ. K., Atagün, M. İ., Erdogan, A. R., Yenilmez, D., Yusifova, A., Şenat, A., & Erel, Ö. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126843 · Cited by 19
Liu, W., Pan, P.-Y., Sun, Y., Wang, J., Zhou, H., Xie, X., Duan, Z., Dong, H.-Y., Chen, W., Zhang, L.-D., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2021.794735 · Cited by 19
Tokumoto, M., Lee, J.-Y., Fujiwara, Y., & Satoh, M. (2023) · Toxics · doi:10.3390/toxics11070641 · Cited by 18
Biology of the iron efflux transporter, ferroportin
Rishi, G., & Subramaniam, V. N. (2020) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2020.10.005 · Cited by 19
He, X., Lin, S., Chen, L., Huang, Y., Hu, J., & Sun, N. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c11046 · Cited by 17
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
Systemic iron homeostasis in female athletes: hepcidin, exercise and sex influence
Barba‐Moreno, L., Alfaro-Magallanes, V. M., Calderón, F. J., & Peinado, A. (2020) · Archivos de medicina del deporte: revista de la Federación Española de Medicina del Deporte y de la Confederación Iberoamericana de Medicina del Deporte · doi:10.18176/archmeddeporte.0009 · Cited by 17
The Emerging Role of Ferroptosis in Liver Cancers
Casini, A., Leone, S., Vaccaro, R., Vivacqua, G., Ceci, L., Pannarale, L., Franchitto, A., Onori, P., Gaudio, E., & Mancinelli, R. (2022) · Life · doi:10.3390/life12122128 · Cited by 17
Srivastava, N. K., Mukherjee, S., & Mishra, V. N. (2023) · Clinical Nutrition ESPEN · doi:10.1016/j.clnesp.2023.10.006 · Cited by 17
Iron metabolism in patients with Graves’ hyperthyroidism
Fischli, S., von Wyl, V., Trummler, M., Konrad, D., Wueest, S., Ruefer, A., Heering, K., Streuli, R., Steuer, C., Bernasconi, L., et al. (2017) · Clinical Endocrinology · doi:10.1111/cen.13450 · Cited by 18
The role of heparin, heparanase and heparan sulfates in hepcidin regulation
Asperti, M., Denardo, A., Gryzik, M., Arosio, P., & Poli, M. (2019) · Vitamins and hormones · doi:10.1016/bs.vh.2019.01.008 · Cited by 17
Ghadimi, D., Hassan, M. F. Y., Fölster‐Holst, R., Röcken, C., Ebsen, M., de Vrese, M., & Heller, K. J. (2019) · Immunobiology · doi:10.1016/j.imbio.2019.11.009 · Cited by 17
Role of a Tyrosine Radical in Human Ceruloplasmin Catalysis
Tian, S., Jones, S. M., & Solomon, E. I. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00953 · Cited by 17
Role of iron homeostasis in the heart
Ying, H., Shen, Z., Wang, J., & Zhou, B. (2021) · Herz · doi:10.1007/s00059-021-05039-w · Cited by 17
A detrimental role of NLRP6 in host iron metabolism during Salmonella infection
Deng, Q., Yang, S., Sun, L., Huang, K., Dong, K., Zhu, Y., Cao, Y. C., Li, Y., Wu, S., & Huang, R. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102217 · Cited by 17
Akhtar, T., Ali, G., & Sheikh, N. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8675275 · Cited by 17
Iron from the gut: the role of divalent metal transporter 1
Okazaki, Y. (2023) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.23-47 · Cited by 18
Mammalian SLC39A13 promotes ER/Golgi iron transport and iron homeostasis in multiple compartments
Li, H., Cui, Y., Hu, Y., Zhao, M., Li, K., Pang, X., Sun, F., & Zhou, B. (2024) · Nature Communications · doi:10.1038/s41467-024-55149-2 · Cited by 16
Cardiac injury caused by iron overload in thalassemia
Fu, C., & Yang, X. Y. (2025) · Frontiers in Pediatrics · doi:10.3389/fped.2025.1514722 · Cited by 16
Perioperative iron deficiency anaemia
Shah, A., Acheson, A. G., & Sinclair, R. C. F. (2023) · BJA Education · doi:10.1016/j.bjae.2023.06.001 · Cited by 16
Sousa, R. A. L. D., Yehia, A., & Abulseoud, O. A. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1237153 · Cited by 16
Nrf2--a hidden bridge linking cancer stem cells to ferroptosis
Li, Y., Tuerxun, H., Liu, X., Zhao, Y., Wen, S., Li, Y., Cao, J., & Zhao, Y. (2023) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2023.104105 · Cited by 16
Tziastoudi, M., Pissas, G., Golfinopoulos, S., Filippidis, G., Dousdampanis, P., Eleftheriadis, T., & Stefanidis, I. (2023) · Life · doi:10.3390/life13122338 · Cited by 16
Bone marrow stromal cell-derived hepcidin has antimicrobial and immunomodulatory activities
Krepuska, M., Mayer, B., Vitale-Cross, L. A., Myneni, V. D., Boyajian, M. K., Németh, K., Szalayova, I., Cho, T. H., MCCLAIN-CALDWELL, I., Gingerich, A. D., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-54227-1 · Cited by 16
González, D. A. S., Cheli, V. T., Rosenblum, S. L., Denaroso, G., & Paez, P. M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102118 · Cited by 16
Qu, Y., Li, N., Xu, M., Zhang, D., Xie, J., & Wang, J. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03658-1 · Cited by 16
Paying the Iron Price: Liver Iron Homeostasis and Metabolic Disease
Ameka, M., & Hasty, A. H. (2022) · Comprehensive physiology · doi:10.1002/cphy.c210039 · Cited by 17
Deciphering ferroptosis in critical care: mechanisms, consequences, and therapeutic opportunities
Tan, R., Chen, G., Yan, Y., Guo, H., Han, X., Zhu, Q., & Du, Q. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1511015 · Cited by 15
Szulc, A., & Woźniak, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26209902 · Cited by 17
Ferroptosis in liver fibrosis and its potential intervention strategy
Zhu, W., Fu, L., Cui, Y., Tang, Y., Liu, K., Shi, L., Gao, Y., Li, M., & Huang, L. (2025) · Cell Biology and Toxicology · doi:10.1007/s10565-025-10111-w · Cited by 17
Ferroptosis plays a novel role in nonalcoholic steatohepatitis pathogenesis
Xiong, F., Zhou, Q., Huang, X., Cao, P., & Wang, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1055793 · Cited by 15
Ferroptosis in early brain injury after subarachnoid hemorrhage: review of literature
Kang, J., Tian, S., Zhang, L., & Yang, G. (2024) · Chinese Neurosurgical Journal · doi:10.1186/s41016-024-00357-4 · Cited by 15
Wang, Y., Li, X., Qu, T., Huang, F., Xu, J., Gao, H., & Zhang, S. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.173118 · Cited by 15
Targeting Ferroptosis as an Advance Strategy in Cancer Therapy
Muluh, T. A., Fu, Q., Ai, X., Wang, C., Chen, W., Zheng, X., Wang, W., Wang, M., Shu, X., & Ying, Y. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2024.0608 · Cited by 15
Qiu, R., Alikhanyan, K., Volk, N., Marques, O., Mertens, C., Agarvas, A. R., Singh, S., Pepperkok, R., Altamura, S., & Muckenthaler, M. U. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101644 · Cited by 16
Yang, P., Xu, H., Zhang, Z., Yang, L., Kuang, H., & Aguilar, Z. P. (2018) · IET Nanobiotechnology · doi:10.1049/iet-nbt.2017.0152 · Cited by 14
Ferroptosis: Reviewing CRC with the Third Eye
Liu, X., Tuerxun, H., Li, Y., Li, Y., He, Y., & Zhao, Y. (2022) · Journal of Inflammation Research · doi:10.2147/jir.s389290 · Cited by 15
Atypical artificial cells: Novel biomimetic materials for combating cancer
Ren, Z., Wan, Q., Zhu, Y., Li, L., Wang, K., Zhao, F., Jiao, K., Tang, M., Tay, F. R., Wan, M., et al. (2024) · Interdisciplinary materials · doi:10.1002/idm2.12199 · Cited by 15
Burz, C. C., Cismaru, C. A., Pop, V. S., & Bojan, A. S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.80940 · Cited by 17
Bolotta, A., Abruzzo, P. M., Baldassarro, V. A., Ghezzo, A., Scotlandi, K., Marini, M., & Zucchini, C. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7623023 · Cited by 14
Impact of natural neuromedin‐B receptor variants on iron metabolism
Rametta, R., Dongiovanni, P., Baselli, G., Pelusi, S., Meroni, M., Fracanzani, A. L., Busti, F., Castagna, A., Scarlini, S., Corradini, E., et al. (2019) · American Journal of Hematology · doi:10.1002/ajh.25679 · Cited by 14
Tybl, E., Gunshin, H., Gupta, S., Barrientos, T., Bonadonna, M., Nos, F. C., Palais, G., Karim, Z., Sánchez, M., Andrews, N. C., et al. (2020) · HemaSphere · doi:10.1097/hs9.0000000000000459 · Cited by 14
The Role of Copper in the Regulation of Ferroportin Expression in Macrophages
Jończy, A., Mazgaj, R., Smuda, E., Żelazowska, B., Kopeć, Z., Starzyński, R. R., & Lipiński, P. (2021) · Cells · doi:10.3390/cells10092259 · Cited by 18
Iron in Porphyrias: Friend or Foe?
Buzzetti, E., Ventura, P., & Corradini, E. (2022) · Diagnostics · doi:10.3390/diagnostics12020272 · Cited by 17
Iron in infectious diseases friend or foe?: The role of gut microbiota
Aksoyalp, Z. Ş., Temel, A., & Erdoğan, B. R. (2022) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2022.127093 · Cited by 15
Ferroportin depletes iron needed for cell cycle progression in head and neck squamous cell carcinoma
Belvin, B. R., & Lewis, J. P. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2022.1025434 · Cited by 14
Liu, J., Yang, B. V., Wang, Y., Wu, Y., Fan, B., Zhu, S., Song, E., & Song, Y. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.113587 · Cited by 14
Banerjee, S., Lu, S., Jain, A. S., Wang, I., Tao, H., Srinivasan, S., Nemeth, E., & He, P. (2024) · Blood · doi:10.1182/blood.2024023829 · Cited by 13
Self-citationVamifeport: Monography of the First Oral Ferroportin Inhibitor
Pilo, F., & Angelucci, E. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13185524 · Cited by 13
Wang, M., Zheng, C., Zhou, F., Xie, Y., Zhang, X., Peng, C., & Wang, L. (2024) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.16826 · Cited by 13
Hepcidin Is a Valuable Therapeutic Target for Colorectal Cancer
Frascatani, R., Colella, M., & Monteleone, G. (2024) · Cancers · doi:10.3390/cancers16234068 · 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
Berezovsky, B., Frýdlová, J., Gurieva, I., Rogalsky, D. W., Vokurka, M., & Krijt, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23115899 · Cited by 13
Zheng, J., Wang, J., Ma, H., Shen, M., Qian, Z., & Bao, Y.-X. (2022) · Redox Report · doi:10.1080/13510002.2022.2088011 · Cited by 13
Structural basis of ferroportin inhibition by minihepcidin PR73
Wilbon, A. S., Shen, J., Ruchala, P. P., Zhou, M., & Pan, Y. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3001936 · Cited by 13
Mice overexpressing hepcidin suggest ferroportin does not play a major role in Mn homeostasis
Jin, L. J., Frazer, D. M., Lu, Y., Wilkins, S. J., Ayton, S., Bush, A. I., & Anderson, G. J. (2019) · Metallomics · doi:10.1039/c8mt00370j · Cited by 13
Iron metabolism, ferroptosis and cancer
Вартанян, А. А. (2017) · Russian Journal of Biotherapy · doi:10.17650/1726-9784-2017-16-3-14-20 · Cited by 13
Associated Effect of SLC40A1 and TMPRSS6 Polymorphisms on Iron Overload
Duca, L., Granata, F., Pierro, E. D., Brancaleoni, V., Graziadei, G., & Nava, I. (2022) · Metabolites · doi:10.3390/metabo12100919 · Cited by 12
Zheng, H., Yang, F., Deng, K., Wei, J., Liu, Z., Zheng, Y., & Xu, H. (2023) · Medicine · doi:10.1097/md.0000000000033225 · Cited by 12
Uguen, K., Tertre, M. L., Tchernitchko, D., Elbahnsi, A., Maestri, S., Gourlaouen, I., Férec, C., Ka, C., Callebaut, I., & Gac, G. L. (2024) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2024.100335 · Cited by 12
The role of iron in normal and impaired testicular function
Harrer, A., Meyron‐Holtz, E. G., & Meinhardt, A. (2025) · Andrology · doi:10.1111/andr.70068 · Cited by 12
Bajbouj, K., Shafarin, J., Muhammad, J. S., Ali, A., Unnikannan, H., Suleiman, B., Al-Jabi, N., Menon, K., & Hamad, M. A. (2020) · Immunobiology · doi:10.1016/j.imbio.2020.151995 · Cited by 12
Zhang, T., Luo, L., He, Q., Xiao, S., Li, Y., Chen, J., Qin, T., Xiao, Z., & Ge, Q. (2024) · European journal of medical research · doi:10.1186/s40001-024-01809-4 · Cited by 12
Role of the kidneys in the redistribution of heme-derived iron during neonatal hemolysis in mice
Bednarz, A., Lipiński, P., Starzyński, R. R., Tomczyk, M., Nowak, W. N., Mucha, O., Ogórek, M., Pierzchała, O., Jończy, A., Staroń, R., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-47414-y · Cited by 12
Is brain iron trafficking part of the physiology of the amyloid precursor protein?
Bailey, D. K., & Kosman, D. J. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01684-z · Cited by 12
Ameka, M., & Hasty, A. H. (2020) · Immunometabolism · doi:10.20900/immunometab20200034 · Cited by 12
SLC39A13 Regulates Heart Function via Mitochondrial Iron Homeostasis Maintenance
Li, H., Wang, X., Zhang, Y., Yang, Y., Zhang, J. Z., & Zhou, B. (2025) · Circulation Research · doi:10.1161/circresaha.125.326201 · Cited by 12
Sato, M., Miyanishi, K., Tanaka, S., Sakurada, A., Sakamoto, H., Kawano, Y., Takada, K., Kobune, M., & Kato, J. (2018) · Canadian Journal of Gastroenterology and Hepatology · doi:10.1155/2018/2154361 · Cited by 11
Li, H., Hu, S.-M., Li, Y., Ciancio, G., Tadros, N. N., Tao, Y., Bai, Y.-J., & Shi, Y. (2022) · Annals of Translational Medicine · doi:10.21037/atm-22-5897 · Cited by 11
Pai, A. B., Digigow, R. G., Flühmann, B., & Wacker, M. G. (2023) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2023.04.025 · Cited by 11
Dziuba, N., Hardy, J., & Lindahl, P. A. (2019) · Metallomics · doi:10.1039/c9mt00152b · Cited by 11
Verma, S., Prescott, R. A., & Cherayil, B. J. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.2a1018-408rr · Cited by 11
Gao, S.-Q., Wang, X., Li, T., Gao, C.-C., Han, Y., Qiu, J.-Y., Miao, S.-H., Sun, Y., Zhao, R., Zheng, X., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.11.036 · Cited by 10
Iron metabolism in rheumatic diseases
Givian, A., Azizan, A., Jamshidi, A., Mahmoudi, M., & Farhadi, E. (2025) · Journal of Translational Autoimmunity · doi:10.1016/j.jtauto.2025.100267 · Cited by 10
Role of Iron Metabolism-Related Genes in Prenatal Development: Insights from Mouse Transgenic Models
Kopeć, Z., Starzyński, R. R., Jończy, A., Mazgaj, R., & Lipiński, P. (2021) · Genes · doi:10.3390/genes12091382 · Cited by 10
Kaushik, S. R., Sahu, S., Guha, H., Saha, S. T., Das, R., Kupa, R.-U., Kapfo, W., Deka, T., Basumatary, R., Thong, A., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.985538 · Cited by 10
Reassessing the safety concerns of utilizing blood donations from patients with hemochromatosis
Winters, A. C., Tremblay, D. A., Arinsburg, S. A., Mascarenhas, J. O., & Schiano, T. D. (2017) · Hepatology · doi:10.1002/hep.29521 · Cited by 10
Majore, S., di Patti, M. C. B., Valiante, M., Polticelli, F., Cortese, A., Bartolomeo, S. D., Bernardo, C. D., Muro, M. D., Faienza, F., Radio, F. C., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.11.006 · Cited by 10
Helgudóttir, S. S., Lichota, J., Burkhart, A., & Moos, T. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1241-3 · Cited by 10
Ferroportin disease: A novel SLC40A1 mutation
Ravasi, G., Pelucchi, S., Russo, A., Mariani, R., & Piperno, A. (2020) · Digestive and Liver Disease · doi:10.1016/j.dld.2020.03.013 · Cited by 10
Prions and prion diseases: Insights from the eye
Singh, N., Chaudhary, S., Ashok, A., & Lindner, E. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108200 · Cited by 10
Tortosa, V., Bonaccorsi di Patti, M. C., Brandi, V., Musci, G., & Polticelli, F. (2017) · Bio-Algorithms and Med-Systems · doi:10.1515/bams-2017-0029 · Cited by 9
Tan, Q., Huang, W., Zheng, Y., Li, M., Yi, T., & Yu, S. (2024) · Rheumatology & autoimmunity · doi:10.1002/rai2.12104 · Cited by 9
An Aptamer Glue Enables Hyperefficient Targeted Membrane Protein Degradation
Zhang, G., Zhang, C., Fu, T., Tan, W., & Wang, X. (2024) · JACS Au · doi:10.1021/jacsau.4c00260 · Cited by 9
Liu, J., Zhao, J., He, J., Li, Y., Xu, J., Xiao, C., Zhang, Y., Chen, H., Hu, Y., Fan, C., et al. (2025) · APOPTOSIS · doi:10.1007/s10495-025-02079-z · Cited by 9
Li, Z., Wang, L., Wu, X., Huang, R., & Yuan, Y. (2025) · JOR Spine · doi:10.1002/jsp2.70080 · Cited by 9
Ferroptosis and retinal ganglion cell death in glaucoma: Mechanisms and therapeutic approaches
Qin, M., He, X., Qiu, W., Peng, Y., Liao, Y., Zhao, J., Luo, L., & Zhang, Q. (2025) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2025.101355 · Cited by 9
Berggren, K. L., Agrawal, S., Fox, J. A., Hildenbrand, J. R. V., Nelson, R., Bush, A. I., & Fox, J. H. (2017) · Journal of Huntington s Disease · doi:10.3233/jhd-170242 · Cited by 9
Hinokitiol protects gastric injury from ethanol exposure via its iron sequestration capacity
Zhao, M., Qiao, C., Yang, S., Tang, Y., Sun, W., Sun, S., Guo, Q., Du, F., Zhang, N., Ning, T., et al. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176340 · Cited by 9
Ferroptosis defense mechanisms: The future and hope for treating osteosarcoma
Ma, Y., Cong, L., Shen, W., Yang, C., & Ye, K. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.4080 · Cited by 10
Phiwchai, I., Thongtem, T., Thongtem, S., & Pilapong, C. (2020) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-020-00951-0 · Cited by 10
Prognostic associations of plasma hepcidin in women with early breast cancer
Jerzak, K. J., Lohmann, A. E., Ennis, M., Nemeth, E., Ganz, T., & Goodwin, P. J. (2020) · Breast Cancer Research and Treatment · doi:10.1007/s10549-020-05903-z · Cited by 9
Self-citationSanyear, C., Butthep, P., Eamsaard, W., Fucharoen, S., Svasti, S., & Masaratana, P. (2020) · PeerJ · doi:10.7717/peerj.8802 · Cited by 9
Epigenetic Regulation of Ferroportin in Primary Cultures of the Rat Blood-Brain Barrier
Helgudóttir, S. S., Routhe, L. G., Burkhart, A., Jønsson, K., Pedersen, I. S., Lichota, J., & Moos, T. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01953-y · Cited by 9
Iron, Copper, and Selenium: Cancer's Thing for Redox BlingPreprint
Terzi, E. M., & Possemato, R. (2023) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041545 · Cited by 9
Molecular insights into placental iron transfer mechanisms and maternofetal regulation
Santhakumar, S., & Edison, E. S. (2023) · Archives of Gynecology and Obstetrics · doi:10.1007/s00404-023-07032-6 · Cited by 8
Hu, M., Zhou, J. F., Qiu, L., Song, R., Qin, X., Tan, Z., Wang, W., Liu, R., Li, Y., Mao, Y., et al. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.104555 · Cited by 8
Reference Values of Ceruloplasmin across the Adult Age Range in a Large Italian Healthy Population
Pelucchi, S., Risca, G., Lanzafame, C., Scollo, C. M., Garofalo, A. M., Martinez, D., Mariani, R., Botti, M., Capitoli, G., Rossi, F., et al. (2024) · The Journal of Applied Laboratory Medicine · doi:10.1093/jalm/jfae098 · Cited by 8
Dietary Iron Absorption: Biochemical and Nutritional Aspects
Frazer, D. M., Anderson, G. J., & Collins, J. F. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_6 · Cited by 8
Decoding the diet-inflammation nexus: ferroptosis as a therapeutic target
Zhang, Y., Liu, Y., Huang, Q., Wang, Z., Li, Y., Zhang, Q., & Lu, B. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2540044 · Cited by 10
Metadata
- Authors
- Drakesmith, H., Nemeth, E., & Ganz, T.
- Affiliations
- University of Oxford (GB)
- University of California, Los Angeles (US)
- Corresponding author
- Ganz, Tomas
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 22
- Issue
- 5
- Pages
- 777-787
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4635047
- OpenAlex
- W2174098335
- Cited by
- 638
- References
- 110
- Citations by year
- 2026: 35 · 2025: 64 · 2024: 68 · 2023: 76 · 2022: 75 · 2021: 67 · 2020: 86 · 2019: 52 · 2018: 54 · 2017: 33 · 2016: 24 · 2015: 1
- FWCI
- 5.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK065029, R01DK090554, R01DK107309)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- ferroportin, hepcidin, iron homeostasis, iron absorption, erythropoiesis, iron recycling, iron storage, iron export, membrane protein structure, host defense, oxygen utilization
- MeSH terms
- Ferroportin, Animals, Erythrocytes, Erythropoiesis, Homeostasis, Humans, Iron, Macrophages, Hepatocytes, Cation Transport Proteins, Hepcidins
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