The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Functional properties of human ferroportin, a cellular iron exporter reactive also with cobalt and zinc
Open accessAbstract
Iron homeostasis is achieved by regulating the intestinal absorption of the metal and its recycling by macrophages. Iron export from enterocytes or macrophages to blood plasma is thought to be mediated by ferroportin under the control of hepcidin. Although ferroportin was identified over a decade ago, little is understood about how it works. We expressed in Xenopus oocytes a human ferroportin-enhanced green fluorescent protein fusion protein and observed using confocal microscopy its exclusive plasma-membrane localization. As a first step in its characterization, we established an assay to detect functional expression of ferroportin by microinjecting oocytes with 55 Fe and measuring efflux. Ferroportin expression increased the first-order rate constants describing 55 Fe efflux up to 300-fold over control. Ferroportin-mediated 55 Fe efflux was saturable, temperature-dependent (activation energy, E a ≈ 17 kcal/mol), maximal at extracellular pH ≈ 7.5, and inactivated at extracellular pH < 6.0. We estimated that ferroportin reacts with iron at its intracellular aspect with apparent affinity constant < 10 −7 M. Ferroportin expression also stimulated efflux of 65 Zn and 57 Co but not of 64 Cu, 109 Cd, or 54 Mn. Hepcidin treatment of oocytes inhibited efflux of 55 Fe, 65 Zn, and 57 Co. Whereas hepcidin administration in mice resulted in a marked hypoferremia within 4 h, we observed no effect on serum zinc levels in those same animals. We conclude that ferroportin is an iron-preferring cellular metal-efflux transporter with a narrow substrate profile that includes cobalt and zinc. Whereas hepcidin strongly regulated serum iron levels in the mouse, we found no evidence that ferroportin plays an important role in zinc homeostasis.
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
“The exported species is almost certainly ferrous iron [12] but the energetics of iron export is not yet well characterized.”
From Hepcidin-Ferroportin Interaction Controls Systemic Iron Homeostasis (2021) · cites this paper as [12]
In the citing paper
“The smaller ion Mn 2+ was previously found not to be effluxed by FPN in oocytes 83 , but appears to be transported in liposomes.”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [83]
Citations
Cites
Lodish, H. F. (1986) · Cited by 5,650
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-citationNemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650
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
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
Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122
Self-citationTransport and Diffusion Across Cell Membranes
Stein, W. D., & Lieb, W. R. (1986) · Elsevier eBooks · doi:10.1016/b978-0-12-664660-3.x5001-7 · Cited by 1,029
Regulation of Iron Metabolism by Hepcidin
Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Nemeth E, 2006, Haematologica, 91, 727
Cited by
Sorted by citations
Drakesmith, H., Nemeth, E., & Ganz, T. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.006 · Cited by 638
Self-citationManganese Is Essential for Neuronal Health
Horning, K. J., Caito, S. W., Tipps, K. G., Bowman, A. B., & Aschner, M. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034419 · Cited by 623
Hepcidin-Ferroportin Interaction Controls Systemic Iron Homeostasis
Nemeth, E., & Ganz, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126493 · Cited by 540
“The exported species is almost certainly ferrous iron [12] but the energetics of iron export is not yet well characterized.”
BackgroundSelf-citationStructure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms
Billesbølle, C. B., Azumaya, C. M., Kretsch, R. C., Powers, A. S., Gonen, S., Schneider, S., Arvedson, T., Dror, R. O., Cheng, Y., & Manglik, A. (2020) · Nature · doi:10.1038/s41586-020-2668-z · Cited by 344
Dietary Cadmium Intake and Its Effects on Kidneys
Satarug, S. (2018) · Toxics · doi:10.3390/toxics6010015 · Cited by 347
Aschemeyer, S., Qiao, B., Stefanova, D., Valore, E. V., Sek, A. C., Ruwe, T. A., Vieth, K. R., Jung, G., Casu, C., Rivella, S., et al. (2018) · Blood · doi:10.1182/blood-2017-05-786590 · Cited by 325
Self-citationCadmium and Lead Exposure, Nephrotoxicity, and Mortality
Satarug, S., Gobe, G. C., Vesey, D. A., & Phelps, K. R. (2020) · Toxics · doi:10.3390/toxics8040086 · Cited by 243
Chen, L.-L., Fan, Y.-G., Zhao, L.-X., Zhang, Q., & Wang, Z.-Y. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106301 · Cited by 200
Iron homeostasis: An anthropocentric perspective
Coffey, R., & Ganz, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.781823 · Cited by 194
Self-citationIntersection of Iron and Copper Metabolism in the Mammalian Intestine and Liver
Doğuer, Ç., Ha, J., & Collins, J. F. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170045 · Cited by 225
Iron transport proteins: Gateways of cellular and systemic iron homeostasis
Knutson, M. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.786632 · Cited by 177
Direct Cell Radiolabeling for in Vivo Cell Tracking with PET and SPECT Imaging
Gawne, P. J., Man, F., Blower, P. J., & de Rosales, R. T. M. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00767 · Cited by 168
McCarthy, R. C., & Kosman, D. J. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1771-4 · Cited by 163
Ng, S., Norwitz, S. G., & Norwitz, E. R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133283 · Cited by 162
Influence of iron metabolism on manganese transport and toxicity
Ye, Q., Park, J. E., Gugnani, K. S., Betharia, S., Pino‐Figueroa, A. J., & Kim, J. (2017) · Metallomics · doi:10.1039/c7mt00079k · Cited by 155
Xin, Y., Gao, H., Wang, J., Qiang, Y., Imam, M. U., Li, Y., Wang, J., Zhang, R., Zhang, H., Yu, Y., et al. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.25 · Cited by 147
Bjørklund, G., Aaseth, J., Skalny, A. V., Suliburska, J., Геннадиевна, С. М., Nikonorov, A. А., & Tinkov, A. A. (2017) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2017.02.005 · Cited by 129
Taniguchi, R., Kato, H. E., Font, J., Deshpande, C. N., Wada, M., Ito, K., Ishitani, R., Jormakka, M., & Nureki, O. (2015) · Nature Communications · doi:10.1038/ncomms9545 · Cited by 120
Placental iron transport: The mechanism and regulatory circuits
Sangkhae, V., & Nemeth, E. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.001 · Cited by 119
Self-citationManganese transporter Slc30a10 controls physiological manganese excretion and toxicity
Mercadante, C. J., Prajapati, M., Conboy, H. L., Dash, M. E., Herrera, C., Pettiglio, M. A., Cintrón-Rivera, L. G., Salesky, M., Rao, D. B., & Bartnikas, T. B. (2019) · Journal of Clinical Investigation · doi:10.1172/jci129710 · Cited by 110
Jacobo‐Estrada, T., Santoyo-Sánchez, M. P., Thévenod, F., & Barbier, O. C. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071590 · Cited by 103
Macrophages: central regulators of iron balance
Gammella, E., Buratti, P., Cairo, G., & Recalcati, S. (2014) · Metallomics · doi:10.1039/c4mt00104d · Cited by 100
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
Recent Advances in the Role of SLC39A/ZIP Zinc Transporters In Vivo
Takagishi, T., Hara, T., & Fukada, T. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122708 · Cited by 97
Thévenod, F., Fels, J., Lee, W., & Zarbock, R. (2019) · BioMetals · doi:10.1007/s10534-019-00176-6 · Cited by 88
Structural basis of ion transport and inhibition in ferroportin
Pan, Y., Ren, Z., Gao, S., Shen, J., Wang, L., Xu, Z., Yu, Y., Bachina, P., Zhang, H., Fan, X., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19458-6 · Cited by 81
Iron, hepcidin, and the metal connection
Loréal, O., Cavey, T., Bardou‐Jacquet, E., Guggenbuhl, P., Ropert, M., & Brissot, P. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00128 · Cited by 78
Iron and manganese transport in mammalian systems
Liu, Q., Barker, S., & Knutson, M. D. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118890 · Cited by 78
Wang, S. C., Davejan, P. M., Hendargo, K. J., Javadi-Razaz, I., Chou, A., Yee, D. C., Ghazi, F., Lam, K. J. K., Conn, A. M., Madrigal, A. A., et al. (2020) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2020.183277 · Cited by 74
Calcium is an essential cofactor for metal efflux by the ferroportin transporter family
Deshpande, C. N., Ruwe, T. A., Shawki, A., Xin, V., Vieth, K. R., Valore, E. V., Qiao, B., Ganz, T., Nemeth, E., Mackenzie, B., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05446-4 · Cited by 57
Self-citationIron and Cadmium Entry Into Renal Mitochondria: Physiological and Toxicological Implications
Thévenod, F., Lee, W., & Garrick, M. D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00848 · Cited by 60
Catapano, A., Cimmino, F., Petrella, L., Pizzella, A., D’Angelo, M., Ambrosio, K., Marino, F., Sabbatini, A., Petrelli, M. D., Paolini, B., et al. (2025) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2025.109888 · Cited by 70
Ferroportin deficiency impairs manganese metabolism in flatiron mice
Seo, Y. A., & Wessling‐Resnick, M. (2015) · The FASEB Journal · doi:10.1096/fj.14-262592 · Cited by 55
Interactions between iron and manganese in neurotoxicity
Bjørklund, G., Dadar, M., Peana, M., Rahaman, M. S., & Aaseth, J. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02652-2 · Cited by 57
Shan, Z., Wei, Z., & Shaikh, Z. A. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.07.017 · Cited by 56
Christenson, E. T., Gallegos, A. S., & Banerjee, A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.817478 · Cited by 51
From zinc homeostasis to disease progression: Unveiling the neurodegenerative puzzle
Fan, Y., Wu, T.-Y., Zhao, L., Jia, R., Hang, R., Hou, W., & Wang, Z. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.107039 · Cited by 49
Impact of ferroptosis on preeclampsia: A review
Shan, Y., Guan, C., Wang, J., Qi, W., Chen, A., & Liu, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115466 · Cited by 47
Hamp1 but not Hamp2 regulates ferroportin in fish with two functionally distinct hepcidin types
Neves, J. V., Ramos, M. F., Moreira, A. C., Silva, T., Gomes, M. S., & Rodrigues, P. (2017) · Scientific Reports · doi:10.1038/s41598-017-14933-5 · Cited by 41
Ferroportin disease mutations influence manganese accumulation and cytotoxicity
Choi, E., Nguyen, T., Iwase, S., & Seo, Y. A. (2018) · The FASEB Journal · doi:10.1096/fj.201800831r · Cited by 37
Iron-responsive-like elements and neurodegenerative ferroptosisPreprint
Rogers, J. T., & Cahill, C. M. (2020) · Learning & Memory · doi:10.1101/lm.052282.120 · Cited by 41
Distribution of manganese and other biometals in flatiron mice
Seo, Y. A., Elkhader, J. A., & Wessling‐Resnick, M. (2015) · BioMetals · doi:10.1007/s10534-015-9904-2 · Cited by 34
Metal Toxicity – An Introduction
Crichton, R. R. (2016) · Royal Society of Chemistry eBooks · doi:10.1039/9781782623892-00001 · Cited by 37
A neurodegeneration gene, WDR45, links impaired ferritinophagy to iron accumulation
Aring, L., Choi, E., Kopera, H. C., Lanigan, T. M., Iwase, S., Klionsky, D. J., & Seo, Y. A. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15548 · Cited by 37
Investigational therapies for renal disease-induced anemia
Schmid, H., & JELKMANN, W. E. B. (2016) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2016.1182981 · Cited by 33
Vadolas, J., Ng, G. Z., Kysenius, K., Crouch, P. J., Dames, S., Eisermann, M., Nualkaew, T., Vilcassim, S., Schaeper, U., & Grigoriadis, G. (2021) · British Journal of Haematology · doi:10.1111/bjh.17428 · Cited by 32
Unice, K. M., Kerger, B. D., Paustenbach, D. J., Finley, B. L., & Tvermoes, B. E. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.04.001 · Cited by 31
Hepcidin Attenuates Zinc Efflux in Caco-2 Cells
Hennigar, S. R., & McClung, J. P. (2016) · Journal of Nutrition · doi:10.3945/jn.116.237081 · Cited by 31
Pyle, C. J., Azad, A., Papp, A. C., Sadée, W., Knoell, D. L., & Schlesinger, L. S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112375 · Cited by 32
Mechanisms and Regulation of Intestinal Iron Transport
Collins, J. F., Flores, S. R., Wang, X., & Anderson, G. J. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00060-8 · Cited by 30
Low-molecular-mass iron in healthy blood plasma is not predominately ferric citrate
Dziuba, N., Hardy, J., & Lindahl, P. A. (2018) · Metallomics · doi:10.1039/c8mt00055g · Cited by 28
Comparative genomics and metagenomics of the metallomes
Zhang, Y., Ying, H., & Xu, Y. (2019) · Metallomics · doi:10.1039/c9mt00023b · Cited by 29
Modulation of Adverse Health Effects of Environmental Cadmium Exposure by Zinc and Its Transporters
Ćirović, A., Ćirović, A., Yimthiang, S., Vesey, D. A., & Satarug, S. (2024) · Biomolecules · doi:10.3390/biom14060650 · Cited by 29
Structures of ferroportin in complex with its specific inhibitor vamifeport
Lehmann, E. F., Liziczai, M., Drożdżyk, K., Altermatt, P., Langini, C., Manolova, V., Sundström, H., Dürrenberger, F., Dutzler, R., & Manatschal, C. (2023) · eLife · doi:10.7554/elife.83053 · Cited by 25
Cavey, T., Ropert, M., de Tayrac, M., Bardou‐Jacquet, E., Island, M., Leroyer, P., Bendavid, C., Brissot, P., & Loréal, O. (2015) · BioMetals · doi:10.1007/s10534-015-9862-8 · Cited by 28
Human ferroportin mediates proton-coupled active transport of iron
Li, S., Yang, Y., & Li, W. (2020) · Blood Advances · doi:10.1182/bloodadvances.2020001864 · Cited by 25
Zavala-Guevara, I. P., Ortega-Romero, M., Narváez-Morales, J., Jacobo‐Estrada, T., Lee, W., Mendoza, L. A., Thévenod, F., & Barbier, O. C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147262 · Cited by 25
Membrane Transporters Involved in Iron Trafficking: Physiological and Pathological Aspects
Pasquadibisceglie, A., di Patti, M. C. B., Musci, G., & Polticelli, F. (2023) · Biomolecules · doi:10.3390/biom13081172 · Cited by 26
Fenton Reaction in vivo and in vitro. Possibilities and Limitations
Muranov, K. O. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924140074 · Cited by 26
Differential cytolocation and functional assays of the two major human SLC30A8 (ZnT8) isoforms
Carvalho, S., Molina‐López, J., Parsons, D. S., Corpe, C. P., Maret, W., & Högstrand, C. (2017) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2017.06.001 · Cited by 24
Sheldon, J. R., Himmel, L. E., Kunkle, D. E., Monteith, A. J., Maloney, K. N., & Skaar, E. P. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010809 · Cited by 27
Iron-laden macrophage-mediated paracrine profibrotic signaling induces lung fibroblast activation
Li, Y., Du, X., Hu, Y., Wang, D., Duan, L., Zhang, H., Zhang, R., Xu, Y., Zhou, R., Zhang, X., et al. (2024) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00675.2023 · Cited by 25
Thévenod, F., Herbrechter, R., Schlabs, C., Pethe, A., Lee, W., Wolff, N. A., & Roussa, E. (2023) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00020.2023 · Cited by 23
The Availability of Iron Is Involved in the Murine Experimental Toxoplasma gondii Infection Outcome
Oliveira, M., Coutinho, L. B., Almeida, M. P. O., Briceño, M. P. P., Araújo, E. C. B., & Silva, N. M. (2020) · Microorganisms · doi:10.3390/microorganisms8040560 · Cited by 20
Lomphithak, T., Helvacioglu, S., Armenia, I., Keshavan, S., Ovejero, J. G., Baldi, G., Ravagli, C., Grazú, V., & Fadeel, B. (2023) · Nanomaterials · doi:10.3390/nano13111719 · Cited by 23
Hepcidin: an important iron metabolism regulator in chronic kidney disease
Antunes, S. A., & Canziani, M. E. F. (2016) · Brazilian Journal of Nephrology · doi:10.5935/0101-2800.20160053 · Cited by 21
Carvalho, S., da Silva, R. B., Shawki, A., Castro, H., Lamy, M., Eide, D. J., Costa, V., Mackenzie, B., & Tomás, A. M. (2015) · Molecular Microbiology · doi:10.1111/mmi.12957 · Cited by 20
Self-citationCobalt in athletes: hypoxia and doping - new crossroads
Skalny, A. V., Zaitseva, I. P., Gluhcheva, Y. G., Skalny, A. A., Achkasov, E. E., Геннадиевна, С. М., & Tinkov, A. A. (2019) · Journal of Applied Biomedicine · doi:10.32725/jab.2018.003 · Cited by 20
Ye, Q., & Kim, J. (2016) · Metallomics · doi:10.1039/c6mt00080k · Cited by 20
Essential and non-essential trace elements among working populations in Ghana
Dartey, E., Berlinger, B., Weinbruch, S., Thomassen, Y., Odland, J. Ø., Brox, J. H., Nartey, V. K., Yeboah, F. A., & Ellingsen, D. G. (2017) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2017.08.014 · Cited by 20
Hackl, L., Zimmermann, M. B., Zeder, C., Parker, M., Johns, P. W., Hurrell, R. F., & Moretti, D. (2017) · Journal of Nutrition · doi:10.3945/jn.116.241778 · Cited by 18
Jonker, R., Deutz, N. E. P., Ligthart‐Melis, G. C., Zachria, A. J., Veley, E. A., Harrykissoon, R., & ENGELEN, M. P. K. J. (2018) · Clinical Nutrition · doi:10.1016/j.clnu.2018.07.018 · Cited by 18
Molecular Mechanisms for Iron Uptake and Homeostasis in Marine Eukaryotic Phytoplankton
Lampe, R. H., Coale, T. H., McQuaid, J. B., & Allen, A. E. (2024) · Annual Review of Microbiology · doi:10.1146/annurev-micro-041222-023252 · Cited by 15
Zhang, M., Wen, M., Xiong, Y., Zhang, L., & Tian, C. (2018) · Chinese Chemical Letters · doi:10.1016/j.cclet.2018.04.026 · Cited by 14
A potential role for zinc in restless legs syndrome
Chen, P., Bornhorst, J., Patton, S. M., Bagai, K., Nitin, R., Miah, M. R., Hare, D. J., Kysenius, K., Crouch, P. J., Xiong, L., et al. (2020) · SLEEP · doi:10.1093/sleep/zsaa236 · 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
Sánchez‐González, C., Rivas‐García, L., López-Chaves, C., Rodríguez‐Nogales, A., Algieri, F., Gálvez, J., Gómez-Aracena, J., Ramírez, L. V., Montes‐Bayón, M., Sanz‐Medel, A., et al. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.08.011 · Cited by 14
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
Gebeyew, K., Jiang, C., Gao, Q., Zhang, L., Zhu, H., Tian, Y., Wang, Q., Wei, Y., Tan, Z., & Han, X. (2022) · Animals · doi:10.3390/ani12111408 · Cited by 13
Baesler, J., Michaelis, V., Stiboller, M., Haase, H., Aschner, M., Schwerdtle, T., Stürzenbaum, S. R., & Bornhorst, J. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202001176 · 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
The Role of Cobalt in Human Health: A Brief Overview
Арыстангалиевна, Б. Г. (2024) · Медицинский журнал Западного Казахстана · doi:10.18502/wkmj.v66i1.15599 · Cited by 11
Satarug, S. (2025) · Biomolecules · doi:10.3390/biom15020183 · Cited by 12
Dziuba, N., Hardy, J., & Lindahl, P. A. (2019) · Metallomics · doi:10.1039/c9mt00152b · Cited by 11
Zhao, M., Liang, S., Guo, J., Choi, J., Kim, N., Lu, W., & Cui, X. (2016) · Microscopy and Microanalysis · doi:10.1017/s1431927616000040 · Cited by 10
Gut to brain: essential micronutrient and trace element manganese transport, function and toxicity
Zou, J., Yerramilli, R., & Aydemir, T. B. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1651151 · Cited by 9
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
Comparative analysis of the functional properties of human and mouse ferroportin
Azucenas, C. R., Ruwe, T. A., Bonamer, J. P., Qiao, B., Ganz, T., Jormakka, M., Nemeth, E., & Mackenzie, B. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00063.2023 · Cited by 7
Self-citationA glance at…antioxidant and antiinflammatory properties of dietary cobalt
Glade, M. J., & Meguid, M. M. (2017) · Nutrition · doi:10.1016/j.nut.2017.08.009 · Cited by 8
Gluhcheva, Y., Pavlova, E., Petrova, E., Tinkov, A. A., Ajsuvakova, O. P., Геннадиевна, С. М., Владов, И., & Skalny, A. V. (2019) · Biological Trace Element Research · doi:10.1007/s12011-019-01790-8 · Cited by 8
Harrison‐Brown, M., Scholes, C. J., Field, C. J., McQuilty, R., Farah, S., Nizam, I., Kerr, D. R., & Kohan, L. (2019) · Clinical Toxicology · doi:10.1080/15563650.2019.1636993 · Cited by 8
Perinatal and early-life cobalt exposure impairs essential metal metabolism in immature ICR mice
Skalny, A. V., Gluhcheva, Y., Ajsuvakova, O. P., Pavlova, E., Petrova, E., Rashev, P. I., Владов, И., Shakieva, R. A., Aschner, M., & Tinkov, A. A. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.111973 · Cited by 8
Wong, M., Ahmed, A., Luo, W., Bowman, A. B., Tizabi, Y., Aschner, M., & Ferrer, B. (2025) · Biological Trace Element Research · doi:10.1007/s12011-025-04708-9 · Cited by 6
Trace metal nutrition and response to deficiency
Blaby, C., & Merchant, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-821430-5.00002-x · Cited by 6
Tertre, M. L., Elbahnsi, A., Ged, C., Uguen, K., Gourlaouen, I., Férec, C., Ka, C., Gac, G. L., & Callebaut, I. (2025) · The FASEB Journal · doi:10.1096/fj.202500790rr · Cited by 5
Ćirović, A., Milovanovic, P. D., & Satarug, S. (2026) · Biomedicines · doi:10.3390/biomedicines14020292 · Cited by 5
Structural insights into ferroportin mediated iron transport
Jormakka, M. (2023) · Biochemical Society Transactions · doi:10.1042/bst20230594 · Cited by 5
Domínguez, D., Montero, D., Robaina, L., Hamre, K., Terova, G., Karalazos, V., & Izquierdo, M. S. (2020) · Aquaculture Nutrition · doi:10.1111/anu.13057 · Cited by 5
Satarug, S. (2019) · MDPI eBooks · doi:10.3390/books978-3-03897-985-2 · Cited by 5
The Ferroxidase–Permease System for Transport of Iron Across Membranes: From Yeast to Humans
Amadei, M., Polticelli, F., Musci, G., & di Patti, M. C. B. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26030875 · Cited by 5
Metadata
- Authors
- Mitchell, C. J., Shawki, A., Ganz, T., Nemeth, E., & Mackenzie, B.
- Affiliations
- University of Cincinnati (US)
- University of California, Los Angeles (US)
- Corresponding author
- Mackenzie, Bryan
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2014-03-01
- Volume
- 306
- Issue
- 5
- Pages
- C450-C459
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- PMC
- PMC4042619
- OpenAlex
- W2068355995
- Cited by
- 132
- References
- 54
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 7 · 2023: 11 · 2022: 9 · 2021: 8 · 2020: 14 · 2019: 11 · 2018: 16 · 2017: 16 · 2016: 7 · 2015: 9 · 2014: 5
- FWCI
- 5.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK08271, R01DK080047, P30DK078392)
- David Geffen School of Medicine, University of California, Los Angeles
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Micronutrient Interactions and Effects
- Keywords
- ferroportin, iron efflux, metal transporters, iron homeostasis, hepcidin, zinc efflux, plasma membrane localization, substrate specificity, hypoferremia, zinc homeostasis
- MeSH terms
- Ferroportin, Animals, Biological Transport, Cell Membrane, Cobalt, Homeostasis, Humans, Hydrogen-Ion Concentration, Iron, Kinetics, Male, Mice, Inbred C57BL, Protein Binding, Recombinant Fusion Proteins, Temperature, Xenopus laevis, Zinc, Genes, Reporter, Microscopy, Confocal, Cation Transport Proteins, Green Fluorescent Proteins, Mice, 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
