Targeting iron metabolism in drug discovery and delivery
Open accessAbstract
Iron fulfils a central role in many essential biochemical processes in human physiology; thus, proper processing of iron is crucial. Although iron metabolism is subject to relatively strict physiological control, numerous disorders, such as cancer and neurodegenerative diseases, have recently been linked to deregulated iron homeostasis. Consequently, iron metabolism constitutes a promising and largely unexploited therapeutic target for the development of new pharmacological treatments for these diseases. Several iron metabolism-targeted therapies are already under clinical evaluation for haematological disorders, and these and newly developed therapeutic agents are likely to have substantial benefit in the clinical management of iron metabolism-associated diseases, for which few efficacious treatments are currently available.
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
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?
Although several approaches to restore aberrant FPN function have been evaluated in clinical trials, none have thus far succeeded.
“Although several approaches to restore aberrant FPN function have been evaluated in clinical trials 16-18 , none have thus far succeeded.”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [18]
In preclinical models of anemia of inflammation, hepcidin antagonists decreased hepcidin expression, an effect verified in clinical trials for some compounds.
“In preclinical models of anemia of inflammation, hepcidin antagonists decreased hepcidin expression, an effect verified in clinical trials for some compounds.133”
From Iron metabolism and iron disorders revisited in the hepcidin era (2020) · cites this paper as [133]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
RETRACTED ARTICLE: Cerebrospinal fluid ferritin in glioblastoma: Evidence for tumor synthesis
Sato, Y., Honda, Y., Asoh, T., Ōizumi, K., Ohshima, Y., & Honda, E. (1998) · Journal of Neuro-Oncology · doi:10.1023/a:1006078521790 · Cited by 31 · see citing works
RetractedFerroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691 · see citing works
Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713 · see citing works
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works
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 · see citing works
Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732 · see citing works
A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, R., Ellis, M. C., Fullan, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0896-399 · Cited by 3,664 · see citing works
Ferroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398 · see citing works
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333 · see citing works
LXXIII.—Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · J. Chem. Soc., Trans. · doi:10.1039/ct8946500899 · Cited by 3,179 · see citing works
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 · see citing works
Stadtman, E. R. (1992) · Science · doi:10.1126/science.1355616 · Cited by 2,701 · see citing works
Nemeth, 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 · see citing works
A conserved family of prolyl-4-hydroxylases that modify HIF
Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549 · see citing works
The role of iron and reactive oxygen species in cell death
Dixon, S. J., & Stockwell, B. R. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1416 · Cited by 2,381 · see citing works
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168 · see citing works
Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084 · see citing works
Salvati, A., Pitek, A. S., Monopoli, M. P., Prapainop, K., Bombelli, F. B., Hristov, D. R., Kelly, P. M., Åberg, C., Mahon, E., & Dawson, K. A. (2013) · Nature Nanotechnology · doi:10.1038/nnano.2012.237 · Cited by 1,912 · see citing works
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877 · see citing works
The role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819 · see citing works
Jones, M., Ibels, L. S., Schenkel, B., & Zagari, M. J. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.00450.x · Cited by 1,812 · see citing works
M2 microglia and macrophages drive oligodendrocyte differentiation during CNS remyelination
Miron, V. E., Boyd, A., Zhao, J.-W., Yuen, T. J., Ruckh, J. M., Shadrach, J. L., van Wijngaarden, P., Wagers, A. J., Williams, A., Franklin, R. J. M., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3469 · Cited by 1,788 · see citing works
Identification of the haemoglobin scavenger receptor
Kristiansen, M., Graversen, J. H., Jacobsen, C., Sonne, O., Hoffman, H.-J., Law, S. K. A., & Moestrup, S. K. (2001) · Nature · doi:10.1038/35051594 · Cited by 1,712 · see citing works
Camaschella, C. (2015) · New England Journal of Medicine · doi:10.1056/nejmra1401038 · Cited by 1,678 · see citing works
Positional 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 · see citing works
Zanganeh, S., Hutter, G., Spitler, R., Lenkov, O., Mahmoudi, M., Shaw, A., Pajarinen, J. S., Nejadnik, H., Goodman, S., Moseley, M., et al. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.168 · Cited by 1,647 · see citing works
Mitochondrial ROS in cancer: initiators, amplifiers or an Achilles' heel?
Sabharwal, S. S., & Schumacker, P. T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3803 · Cited by 1,643 · see citing works
Iron and cancer: more ore to be mined
Torti, S. V., & Torti, F. M. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3495 · Cited by 1,621 · see citing works
Oxidation of tartaric acid in presence of iron
Fenton, H. J. H. (1894) · Journal of the Chemical Society (Resumed) · Cited by 1,498 · see citing works
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 · see citing works
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 · see citing works
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324 · see citing works
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 · see citing works
Oxidative stress inhibits distant metastasis by human melanoma cells
Piskounova, E., Agathocleous, M., Murphy, M. M., Hu, Z., Huddlestun, S. E., Zhao, Z., Leitch, A. M., Johnson, T. M., DeBerardinis, R. J., & Morrison, S. J. (2015) · Nature · doi:10.1038/nature15726 · Cited by 1,269 · see citing works
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 · see citing works
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 · see citing works
pH and the recycling of transferrin during receptor-mediated endocytosis.
Dautry‐Varsat, A., Ciechanover, A. J., & Lodish, H. F. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.8.2258 · Cited by 1,178 · see citing works
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 · see citing works
Ferrostatins Inhibit Oxidative Lipid Damage and Cell Death in Diverse Disease Models
Skouta, R., Dixon, S. J., Wang, J., Dunn, D. E., Orman, M., Shimada, K., Rosenberg, P. A., Lo, D. C., Weinberg, J. M., Linkermann, A., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja411006a · Cited by 1,146 · see citing works
Identification of erythroferrone as an erythroid regulator of iron metabolism
Kautz, L., Jung, G., Valore, E. V., Rivella, S., Nemeth, E., & Ganz, T. (2014) · Nature Genetics · doi:10.1038/ng.2996 · Cited by 1,127 · see citing works
Self-citationSynchronized renal tubular cell death involves ferroptosis
Linkermann, A., Skouta, R., Himmerkus, N., Mulay, S. R., Dewitz, C., De Zen, F., Prokai, A., Zuchtriegel, G., Krombach, F., Welz, P.-S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415518111 · Cited by 1,126 · see citing works
Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122 · see citing works
Borgna‐Pignatti, C., Rugolotto, S., Stefano, P. D., Zhao, H., Cappellini, M. D., Vecchio, G. C. D., Romeo, M. A., Forni, G. L., Gamberini, M. R., Ghilardi, R., et al. (2004) · PubMed · Cited by 1,119 · see citing works
An 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 · see citing works
Sindrilaru, A., Peters, T., Wieschalka, S., Baican, C., Baican, A., Peter, H., Hainzl, A., Schatz, S., Qi, Y., Schlecht, A., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44490 · Cited by 1,100 · see citing works
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084 · see citing works
Stadtman, E. R. (2006) · Free Radical Research · doi:10.1080/10715760600918142 · Cited by 1,056 · see citing works
Bacterial Iron Sources: From Siderophores to Hemophores
Wandersman, C., & Delepelaire, P. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123811 · Cited by 1,056 · see citing works
Local proliferation dominates lesional macrophage accumulation in atherosclerosis
Robbins, C. S., Hilgendorf, I., Weber, G. F., Theurl, I., Iwamoto, Y., Figueiredo, J.-L., Gorbatov, R., Sukhova, G. K., Gerhardt, L. M. S., Smyth, D., et al. (2013) · Nature Medicine · doi:10.1038/nm.3258 · Cited by 1,041 · see citing works
Dorsomorphin inhibits BMP signals required for embryogenesis and iron metabolism
Yu, P. B., Hong, C. C., Sachidanandan, C., Babitt, J. L., Deng, D. Y., Hoyng, S. A., Lin, H. Y.-F., Bloch, K. D., & Peterson, R. T. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.54 · Cited by 1,039 · see citing works
Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026 · see citing works
Heme oxygenase 1 is required for mammalian iron reutilization
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10919 · Cited by 1,016 · see citing works
Mutations in HFE2 cause iron overload in chromosome 1q–linked juvenile hemochromatosis
Papanikolaou, G., Samuels, M. E., Ludwig, E. H., MacDonald, M. L. E., Franchini, P. L., Dubé, M.-P., Andres, L., MacFarlane, J., Sakellaropoulos, N., Politou, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1274 · Cited by 974 · see citing works
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 · see citing works
Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
Roetto, A., Papanikolaou, G., Politou, M., Alberti, F., Girelli, D., Christakis, J., Loukopoulos, D., & Camaschella, C. (2003) · Nature Genetics · doi:10.1038/ng1053 · Cited by 860 · see citing works
Iron homeostasis in host defence and inflammation
Ganz, T., & Nemeth, E. (2015) · Nature Reviews Immunology · doi:10.1038/nri3863 · Cited by 843 · see citing works
The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22
Camaschella, C., Roetto, A., Calì, A., De Gobbi, M., Garozzo, G., Carella, M., Majorano, N., Totaro, A., & Gasparini, P. (2000) · Nature Genetics · doi:10.1038/75534 · Cited by 803 · see citing works
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. (2005) · Nature Genetics · doi:10.1038/ng1658 · Cited by 775 · see citing works
BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism
Andriopoulos Jr, B., Corradini, E., Xia, Y., Faasse, S. A., Chen, S., Grgurevic, L., Knutson, M. D., Pietrangelo, A., Vukicevic, S., Lin, H. Y., et al. (2009) · Nature Genetics · doi:10.1038/ng.335 · Cited by 769 · see citing works
Intramuscular desferrioxamine in patients with Alzheimer's disease
MCLACHLAN, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)92978-b · Cited by 764 · see citing works
The Steap proteins are metalloreductases
Ohgami, R. S., Campagna, D. R., McDonald, A., & Fleming, M. D. (2006) · Blood · doi:10.1182/blood-2006-02-003681 · Cited by 744 · see citing works
Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA)
Finberg, K. E., Heeney, M. M., Campagna, D. R., Aydınok, Y., Pearson, H. A., Hartman, K. R., Mayo, M. M., Samuel, S. M., Strouse, J. J., Markianos, K., et al. (2008) · Nature Genetics · doi:10.1038/ng.130 · Cited by 675 · see citing works
Leibold, E. A., & Munro, H. N. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.7.2171 · Cited by 671 · see citing works
HSPB1 as a novel regulator of ferroptotic cancer cell death
Sun, X., Ou, Z., Xie, M., Kang, R., Fan, Y., Niu, X., Wang, H., Cao, L., & Tang, D. (2015) · Oncogene · doi:10.1038/onc.2015.32 · Cited by 666 · see citing works
Kroner, A., Greenhalgh, A. D., Zarruk, J. G., Passos dos Santos, R., Gaestel, M., & David, S. (2014) · Neuron · doi:10.1016/j.neuron.2014.07.027 · Cited by 655 · see citing works
Hexameric Structure and Assembly of the Interleukin-6/IL-6 α-Receptor/gp130 Complex
Boulanger, M. J., Chow, D., Brevnova, E. E., & García, K. C. (2003) · Science · doi:10.1126/science.1083901 · Cited by 647 · see citing works
Molecular Cloning of Transferrin Receptor 2
Kawabata, H., Yang, R., Hirama, T., Vuong, P. T., Kawano, S., Gombart, A. F., & Koeffler, H. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20826 · Cited by 646 · see citing works
Macrophage subsets in atherosclerosis
Chinetti, G., Colin, S., & Staels, B. (2014) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2014.173 · Cited by 640 · see citing works
Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)
Peyssonnaux, C., Zinkernagel, A. S., Schuepbach, R. A., Rankin, E., Vaulont, S., Haase, V. H., Nizet, V., & Johnson, R. S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31370 · Cited by 639 · see citing works
Regulated necrosis: disease relevance and therapeutic opportunities
Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630 · see citing works
Mitoferrin is essential for erythroid iron assimilation
Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624 · see citing works
Targeting Chelatable Iron as a Therapeutic Modality in Parkinson's Disease
Devos, D., Moreau, C., Devedjian, J. C., Kluza, J., Pétrault, M., Laloux, C., Jonneaux, A., Ryckewaert, G., Garçon, G., Rouaix, N., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5593 · Cited by 622 · see citing works
The Biochemistry of Desferrioxamine and its Relation to Iron Metabolism
Keberle, H. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1965.tb54077.x · Cited by 615 · see citing works
Herz, J., Clouthier, D. E., & Hammer, R. E. (1992) · Cell · doi:10.1016/0092-8674(92)90511-a · Cited by 611 · see citing works
Stoichiometric and site characteristics of the binding of iron to human transferrin
Aisen, P., Leibman, A., & Zweier, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62337-9 · Cited by 601 · see citing works
The Molecular Mechanism of Action of Artemisinin—The Debate Continues
O’Neill, P. M., Barton, V., & Ward, S. A. (2010) · Molecules · doi:10.3390/molecules15031705 · Cited by 597 · see citing works
Lack of the bone morphogenetic protein BMP6 induces massive iron overload
Meynard, D., Kautz, L., Darnaud, V., Canonne-Hergaux, F., Coppin, H., & Roth, M.-P. (2009) · Nature Genetics · doi:10.1038/ng.320 · Cited by 587 · see citing works
The serine protease TMPRSS6 is required to sense iron deficiency
Du, X., She, E., Gelbart, T., Truksa, J., Lee, P., Xia, Y., Khovananth, K., Mudd, S., Mann, N., Moresco, E. M. Y., et al. (2008) · Science · doi:10.1126/science.1157121 · Cited by 578 · see citing works
Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells
Liuzzi, J. P., Aydemir, F., Nam, H., Knutson, M. D., & Cousins, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606424103 · Cited by 577 · see citing works
Transferrin receptor is necessary for development of erythrocytes and the nervous system
Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574 · see citing works
Binding and uptake of H-ferritin are mediated by human transferrin receptor-1
Li, L., Fang, C. J., Ryan, J. C., Niemi, E. C., Lebrón, J. A., Björkman, P. J., Arase, H., Torti, F. M., Torti, S. V., Nakamura, M. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913192107 · Cited by 558 · see citing works
Autosomal-dominant hemochrom-atosis is associated with a mutation in the ferroportin (SLC11A3) gene
Montosi, G., Donovan, A., Totaro, A., Garuti, C., Pignatti, E., Cassanelli, S., Trenor, C. C., Gasparini, P., Andrews, N. C., & Pietrangelo, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113468 · Cited by 557 · see citing works
Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J., & Camaschella, C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.012 · Cited by 555 · see citing works
Autosomal-dominant hemochrom-atosis is associated with a mutation in the ferroportin (SLC11A3) gene
Montosi, G., Donovan, A., Totaro, A., Garuti, C., Pignatti, E., Cassanelli, S., Trenor, C. C., Gasparini, P., Andrews, N. C., & Pietrangelo, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13468 · Cited by 555 · see citing works
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
The biology and chemistry of high-valent iron–oxo and iron–nitrido complexes
Hohenberger, J., Ray, K., & Meyer, K. (2012) · Nature Communications · doi:10.1038/ncomms1718 · Cited by 545 · see citing works
Wiley, D. T., Webster, P. C., Gale, A., & Davis, M. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307152110 · Cited by 521 · see citing works
�ber die Katalyse des Hydroperoxydes
Haber, F., & Weiss, J. (1932) · Die Naturwissenschaften · doi:10.1007/bf01504715 · Cited by 513 · see citing works
Scortegagna, M., Ding, K., Oktay, Y., Gaur, A., Thurmond, F., Yan, L.-J., Marck, B. T., Matsumoto, A. M., Shelton, J. M., Richardson, J. A., et al. (2003) · Nature Genetics · doi:10.1038/ng1266 · Cited by 496 · see citing works
Iron metabolism in the CNS: implications for neurodegenerative diseases
Rouault, T. A. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3453 · Cited by 496 · see citing works
A mutation in SLC11A3 is associated with autosomal dominant hemochromatosis
Njajou, O. T., Vaessen, N., Joosse, M., Berghuis, B., van Dongen, J. W. F., Breuning, M. H., Snijders, P. J. L. M., Rutten, W. P. F., Sandkuijl, L. A., Oostra, B. A., et al. (2001) · Nature Genetics · doi:10.1038/90038 · Cited by 492 · see citing works
Philippidis, P., Mason, J. C., Evans, B. J., Nadra, I., Taylor, K. M., Haskard, D. O., & Landis, R. C. (2004) · Circulation Research · doi:10.1161/01.res.0000109414.78907.f9 · Cited by 476 · see citing works
Identification of the receptor scavenging hemopexin-heme complexes
Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473 · see citing works
A histochemical study of iron, transferrin, and ferritin in Alzheimer's diseased brains
Connor, J. R., Menzies, S. L., Martin, S. M. S., & Mufson, E. J. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310111 · Cited by 468 · see citing works
Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway
Cohen, L. A., Gutierrez, L., Weiss, A., Leichtmann-Bardoogo, Y., Zhang, D.-L., Crooks, D. R., Sougrat, R., Morgenstern, A., Galy, B., Hentze, M. W., et al. (2010) · Blood · doi:10.1182/blood-2009-11-253815 · Cited by 452 · see citing works
Ferroportin and Iron Regulation in Breast Cancer Progression and Prognosis
Pinnix, Z. K., Miller, L. D., Wang, W., D’Agostino, R., Kute, T., Willingham, M. C., Hatcher, H., Tesfay, L., Sui, G., Di, X., et al. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3001127 · Cited by 448 · see citing works
CD169 + macrophages provide a niche promoting erythropoiesis under homeostasis and stress
Chow, A., Huggins, M., Ahmed, J., Hashimoto, D., Lucas, D., Kunisaki, Y., Pinho, S., Leboeuf, M., Noizat, C., van Rooijen, N., et al. (2013) · Nature Medicine · doi:10.1038/nm.3057 · Cited by 433 · see citing works
Shah, Y. M., Matsubara, T., Ito, S., Yim, S.-H., & Gonzalez, F. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.012 · Cited by 431 · see citing works
Identification of a Human Heme Exporter that Is Essential for Erythropoiesis
Quigley, J. G., Yang, Z., Worthington, M., Phillips, J. D., Sabo, K. M., Sabath, D. E., Berg, C. L., Sassa, S., Wood, B. L., & Abkowitz, J. L. (2004) · Cell · doi:10.1016/j.cell.2004.08.014 · Cited by 423 · see citing works
Chemical agents and related occupations.
(2012) · PubMed Central · Cited by 420 · see citing works
Gunshin, H., Fujiwara, Y., Custodio, A. O., DiRenzo, C., Robine, S., & Andrews, N. C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24356 · Cited by 419 · see citing works
Flemming (1998) · Medical Entomology and Zoology · Cited by 412 · see citing works
Salazar, J., Mena, N., Hunot, S., Prigent, A., Alvarez-Fischer, D., Arredondo, M., Duyckaerts, C., Sazdovitch, V., Zhao, L., Garrick, L. M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804373105 · Cited by 409 · see citing works
Ferritin: A Versatile Building Block for Bionanotechnology
Jutz, G., van Rijn, P., de Miranda, B. S., & Böker, A. (2015) · Chemical Reviews · doi:10.1021/cr400011b · Cited by 407 · see citing works
A Heme Export Protein Is Required for Red Blood Cell Differentiation and Iron Homeostasis
Keel, S. B., Doty, R. T., Yang, Z., Quigley, J. G., Chen, J., Knoblaugh, S., Kingsley, P. D., De Domenico, I., Vaughn, M. B., Kaplan, J., et al. (2008) · Science · doi:10.1126/science.1151133 · Cited by 404 · see citing works
Takeda, K., Ho, V. C., Takeda, H., Duan, L.-J., Nagy, A., & Fong, G.-H. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00425-06 · Cited by 401 · see citing works
Ligand-targeted particulate nanomedicines undergoing clinical evaluation: Current status
van der Meel, R., Vehmeijer, L. J. C., Kok, R. J., Storm, G., & van Gaal, E. V. B. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2013.08.012 · Cited by 398 · see citing works
Somatic<i>HIF2A</i>Gain-of-Function Mutations in Paraganglioma with Polycythemia
Zhuang, Z., Yang, C., Lorenzo, F., Merino, M., Fojo, T., Kebebew, E., Popovic, V., Stratakis, C. A., Prchal, J. T., & Pacak, K. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1205119 · Cited by 397 · see citing works
Macrophage polarization and plasticity in health and disease
Biswas, S. K., Chittezhath, M., Shalova, I. N., & Lim, J.-Y. (2012) · Immunologic Research · doi:10.1007/s12026-012-8291-9 · Cited by 396 · see citing works
Taher, A. T., Musallam, K. M., Karimi, M., El-Beshlawy, A. M., Belhoul, K., Daar, S., Saned, M., El-Chafic, A.-H., Fasulo, M. R., & Cappellini, M. D. (2009) · Blood · doi:10.1182/blood-2009-09-243154 · Cited by 390 · see citing works
Eaton, J. W., & Qian, M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00772-4 · Cited by 389 · see citing works
Wang, C., Jenkitkasemwong, S., Duarte, S., Sparkman, B. K., Shawki, A., Mackenzie, B., & Knutson, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.367284 · Cited by 381 · see citing works
Transferrin Receptor Induction by Hypoxia
Tacchini, L., Bianchi, L., Bernelli-Zazzera, A., & Cairo, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24142 · Cited by 379 · see citing works
Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377 · see citing works
Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)
McDonough, M. A., Li, V., Flashman, E., Chowdhury, R., Mohr, C., Liénard, B. M. R., Zondlo, J., Oldham, N. J., Clifton, I. J., Lewis, J. K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601283103 · Cited by 366 · see citing works
Urrutia, P., Aguirre, P., Esparza, A., Tapia, V., Mena, N. P., Arredondo, M., González‐Billault, C., & Núñez, M. T. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12244 · Cited by 364 · see citing works
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works
Scavenger receptor CD163, a Jack-of-all-trades and potential target for cell-directed therapy
Gorp, H. V., Delputte, P., & Nauwynck, H. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.02.008 · Cited by 358 · see citing works
Scara5 Is a Ferritin Receptor Mediating Non-Transferrin Iron Delivery
Li, J. Y., Paragas, N., Ned, R. M., Qiu, A., Viltard, M., Leete, T., Drexler, I. R., Chen, X., Sanna‐Cherchi, S., Mohammed, F., et al. (2009) · Developmental Cell · doi:10.1016/j.devcel.2008.12.002 · Cited by 355 · see citing works
Binding of a Cytosolic Protein to the Iron-Responsive Element of Human Ferritin Messenger RNA
Rouault, T. A., Hentze, M. W., Caughman, S. W., Harford, J. B., & Klausner, R. D. (1988) · Science · doi:10.1126/science.3413484 · Cited by 351 · see citing works
Preferential Iron Trafficking Characterizes Glioblastoma Stem-like Cells
Schonberg, D. L., Miller, T. E., Wu, Q., Flavahan, W. A., Das, N. K., Hale, J. S., Hubert, C. G., Mack, S. C., Jarrar, A., Karl, R. T., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.09.002 · Cited by 347 · see citing works
The Transferrin Receptor Modulates Hfe-Dependent Regulation of Hepcidin Expression
Schmidt, P. J., Toran, P. T., Giannetti, A. M., Bjorkman, P. J., & Andrews, N. C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.016 · Cited by 345 · see citing works
Structure–activity relationship study of bone morphogenetic protein (BMP) signaling inhibitors
Cuny, G. D., Yu, P. B., Laha, J. K., Xing, X., Liu, J.-F., Lai, C. S. C., Deng, D. Y., Sachidanandan, C., Bloch, K. D., & Peterson, R. T. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.06.052 · Cited by 343 · see citing works
Transferrin and Iron in Normal, Alzheimer's Disease, and Parkinson's Disease Brain Regions
Loeffler, D. A., Connor, J. R., Juneau, P. L., Snyder, B. S., Kanaley, L., DeMaggio, A. J., Nguyen, H., Brickman, C. M., & LeWitt, P. A. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65020710.x · Cited by 334 · see citing works
Percy, M. J., Zhao, Q., Flores, A., Harrison, C., Lappin, T. R. J., Maxwell, P. H., McMullin, M. F., & Lee, F. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508423103 · Cited by 330 · see citing works
Ayton, S., Faux, N. G., Bush, A. I., Initiative, A. D. N., Weiner, M. W., Aisen, P. S. S., Petersen, R. C., Jack, C. R., Jagust, W., Trojanowki, J. Q., et al. (2015) · Nature Communications · doi:10.1038/ncomms7760 · Cited by 330 · see citing works
Iron-Chelation Therapy with Oral Deferiprone in Patients with Thalassemia Major
Olivieri, N. F., Brittenham, G. M., Matsui, D. M., Berkovitch, M., Blendis, L. M., Cameron, R., MCCLELLAND, R. A., Liu, P. P., Templeton, D. M., & Koren, G. (1995) · New England Journal of Medicine · doi:10.1056/nejm199504063321404 · Cited by 323 · see citing works
Coronary Intraplaque Hemorrhage Evokes a Novel Atheroprotective Macrophage Phenotype
Boyle, J. J., Harrington, H. A., Piper, E., Elderfield, K., Stark, J., Landis, R. C., & Haskard, D. O. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080431 · Cited by 319 · see citing works
Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins
Rajagopal, A., Rao, A. U., Amigo, J., Tian, M., Upadhyay, S. K., Hall, C., Uhm, S., Mathew, M. K., Fleming, M. D., Paw, B. H., et al. (2008) · Nature · doi:10.1038/nature06934 · Cited by 316 · see citing works
Allosteric inhibition of hypoxia inducible factor-2 with small molecules
Scheuermann, T. H., Li, Q., Ma, H.-W., Key, J., Zhang, L., Chen, R., Garcia, J. A., Naidoo, J., Longgood, J., Frantz, D. E., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1185 · Cited by 315 · see citing works
Stadler, N., Lindner, R. A., & Davies, M. J. (2004) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000124892.90999.cb · Cited by 310 · see citing works
Iron traffics in circulation bound to a siderocalin (Ngal)–catechol complex
Bao, G., Clifton, M., Hoette, T. M., Mori, K., Deng, S.-X., Qiu, A., Viltard, M., Williams, D., Paragas, N., Leete, T., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.402 · Cited by 307 · see citing works
MRI of Tumor-Associated Macrophages with Clinically Applicable Iron Oxide Nanoparticles
Daldrup-Link, H. E., Golovko, D. M., Ruffell, B., DeNardo, D. G., Castaneda, R., Ansari, C., Rao, J., Tikhomirov, G. A., Wendland, M. F., Corot, C., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-3420 · Cited by 302 · see citing works
Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency
Sanchez, M., Galy, B., Muckenthaler, M. U., & Hentze, M. W. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1222 · Cited by 294 · see citing works
HIF prolyl hydroxylase inhibitors for the treatment of renal anaemia and beyond
Maxwell, P. H., & Eckardt, K. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2015.193 · Cited by 286 · see citing works
A missense mutation in TFRC, encoding transferrin receptor 1, causes combined immunodeficiency
Jabara, H. H., Boyden, S. E., Chou, J., Ramesh, N., Massaad, M. J., Benson, H., Bainter, W., Fraulino, D., Rahimov, F., Sieff, C., et al. (2016) · Nature Genetics · doi:10.1038/ng.3465 · Cited by 279 · see citing works
Kovtunovych, G., Eckhaus, M., Ghosh, M. C., Ollivierre, H., & Rouault, T. A. (2010) · Blood · doi:10.1182/blood-2010-03-272138 · Cited by 273 · see citing works
Vinchi, F., Costa da Silva, M., Ingoglia, G., Petrillo, S., Brinkman, N., Zuercher, A., Cerwenka, A., Tolosano, E., & Muckenthaler, M. U. (2016) · Blood · doi:10.1182/blood-2015-08-663245 · Cited by 269 · see citing works
Taylor, M., Qu, A., Anderson, E. R., Matsubara, T., Martin, A., Gonzalez, F. J., & Shah, Y. M. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.03.007 · Cited by 265 · see citing works
Provenzano, R., Besarab, A., Wright, S., Dua, S., Zeig, S., Nguyen, P., Poole, L., Saikali, K. G., Saha, G. C., Hemmerich, S., et al. (2016) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2015.12.020 · Cited by 265 · see citing works
Biodegradation of Iron Oxide Nanocubes: High-Resolution In Situ Monitoring
Lartigue, L., Alloyeau, D., Kolosnjaj‐Tabi, J., Javed, Y., Guardia, P., Riedinger, A., Péchoux, C., Pellegrino, T., Wilhelm, C., & Gazeau, F. (2013) · ACS Nano · doi:10.1021/nn305719y · Cited by 263 · see citing works
Iron deposits in multiple sclerosis and Alzheimer's disease brains
LeVine, S. M. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00470-8 · Cited by 258 · see citing works
Phase I Study of a Systemically Delivered p53 Nanoparticle in Advanced Solid Tumors
Senzer, N. N., Nemunaitis, J. J., Nemunaitis, D., Bedell, C., Edelman, G. M., Barve, M. A., Nunan, R., Pirollo, K. F., Rait, A. S., & Chang, E. H. (2013) · Molecular Therapy · doi:10.1038/mt.2013.32 · Cited by 250 · see citing works
The iron redox and hydrolysis chemistry of the ferritins
Bou‐Abdallah, F. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.03.021 · Cited by 250 · see citing works
Ferroportin1 deficiency in mouse macrophages impairs iron homeostasis and inflammatory responses
Zhang, Z., Zhang, F., An, P., Guo, X., Shen, Y., Tao, Y., Wu, Q., Zhang, Y., Yu, Y., Ning, B., et al. (2011) · Blood · doi:10.1182/blood-2011-01-330324 · Cited by 250 · see citing works
Jenkitkasemwong, S., Wang, C.-Y., Coffey, R., Zhang, W., Chan, A., Biel, T., Kim, J.-S., Hojyo, S., Fukada, T., & Knutson, M. D. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.002 · Cited by 245 · see citing works
Heme oxygenase–1 deficiency: The first autopsy case
Kawashima, A., Oda, Y., Yachie, A., Koizumi, S., & Nakanishi, I. (2002) · Human Pathology · doi:10.1053/hupa.2002.30217 · Cited by 245 · see citing works
White, C., Yuan, X., Schmidt, P. J., Bresciani, E., Samuel, T. K., Campagna, D. R., Hall, C., Bishop, K. S., Calicchio, M. L., Lapierre, A., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.005 · Cited by 237 · see citing works
Structure of the haptoglobin–haemoglobin complex
Andersen, C. B. F., Torvund-Jensen, M., Nielsen, M. J., Oliveira, C. L. P., Hersleth, H.-P., Andersen, N. H., Pedersen, J. S., Andersen, G. R., & Moestrup, S. K. (2012) · Nature · doi:10.1038/nature11369 · Cited by 236 · see citing works
Habashy, H. O., Powe, D. G., Staka, C. M., Rakha, E. A., Ball, G., Green, A. R., Aleskandarany, M., Paish, E. C., Douglas Macmillan, R., Nicholson, R. I., et al. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-009-0345-x · Cited by 236 · see citing works
Fernández‐Real, J. M., McClain, D. A., & Manco, M. (2015) · Diabetes Care · doi:10.2337/dc14-3082 · Cited by 235 · see citing works
Preza, G. C., Ruchala, P., Pinon, R., Ramos, E., Qiao, B., Peralta, M. A., Sharma, S., Waring, A., Ganz, T., & Nemeth, E. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57693 · Cited by 234 · see citing works
Tiainen, S., Tumelius, R., Rilla, K. J., Hämäläinen, K. M., Tammi, M., Tammi, R., Kosma, V., Oikari, S., & Auvinen, P. (2014) · Histopathology · doi:10.1111/his.12607 · Cited by 234 · see citing works
Kong, S. M. Y., Chan, B. K. K., Park, J., Hill, K. J., Aitken, J. B., Cottle, L., Farghaian, H., Cole, A. R., Lay, P. A., Sue, C. M., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu099 · Cited by 233 · see citing works
Nanoparticles for Imaging: top or Flop?
Kiessling, F., Mertens, M. E., Grimm, J., & Lammers, T. (2014) · Radiology · doi:10.1148/radiol.14131520 · Cited by 228 · see citing works
Self-citationArezes, J., Jung, G., Gabayan, V., Valore, E., Ruchala, P., Gulig, P. A., Ganz, T., Nemeth, E., & Bulut, Y. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2014.12.001 · Cited by 227 · see citing works
Macrophages support pathological erythropoiesis in polycythemia vera and β-thalassemia
Ramos, P., Casu, C., Gardenghi, S., Breda, L., Crielaard, B. J., Guy, E., Marongiu, M. F., Gupta, R., Levine, R. L., Abdel-Wahab, O., et al. (2013) · Nature Medicine · doi:10.1038/nm.3126 · Cited by 227 · see citing works
Self-citationModulation of iron transport proteins in human colorectal carcinogenesis
Brookes, M. J., Hughes, S., Turner, F. E., Reynolds, G., Sharma, N., Ismail, T., Berx, G., McKie, A. T., Hotchin, N., Anderson, G. J., et al. (2006) · Gut · doi:10.1136/gut.2006.094060 · Cited by 226 · see citing works
Reducing TMPRSS6 ameliorates hemochromatosis and β-thalassemia in mice
Guo, S., Casu, C., Gardenghi, S., Booten, S. L., Aghajan, M., Peralta, R. Q., Watt, A., Freier, S., Monia, B. P., & Rivella, S. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66969 · Cited by 224 · see citing works
Self-citationAntibody-based PET imaging of amyloid beta in mouse models of Alzheimer’s disease
Sehlin, D., Fang, X. T., Cato, L., Antoni, G., Lannfelt, L., & Syvänen, S. (2016) · Nature Communications · doi:10.1038/ncomms10759 · Cited by 223 · see citing works
Boyle, J. J., Johns, M. S., Kämpfer, T., Nguyen, A. T., Gamé, L., Schaer, D. J., Mason, J. C., & Haskard, D. O. (2011) · Circulation Research · doi:10.1161/circresaha.111.247577 · Cited by 220 · see citing works
Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload
Mims, M. P., Guan, Y., Pospı́šilová, D., Priwitzerova, M., Indrák, K., Ponka, P., Divoký, V., & Prchal, J. T. (2005) · Blood · doi:10.1182/blood-2004-07-2966 · Cited by 219 · see citing works
TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis
Chen, T. T., Li, L., Chung, D.-H., Allen, C. D. C., Torti, S. V., Torti, F. M., Cyster, J. G., Chen, C.-Y., Brodsky, F. M., Niemi, E. C., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042433 · Cited by 219 · see citing works
STEAP Proteins: From Structure to Applications in Cancer Therapy
Gomes, I. M., Maia, C. J., & Santos, C. R. A. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0281 · Cited by 215 · see citing works
Minihepcidins prevent iron overload in a hepcidin-deficient mouse model of severe hemochromatosis
Ramos, E., Ruchala, P., Goodnough, J. B., Kautz, L., Preza, G. C., Nemeth, E., & Ganz, T. (2012) · Blood · doi:10.1182/blood-2012-07-440743 · Cited by 213 · see citing works
Multi-Copper Oxidases and Human Iron Metabolism
Vashchenko, G., & MacGillivray, R. T. A. (2013) · Nutrients · doi:10.3390/nu5072289 · Cited by 212 · see citing works
Hervault, A., Dunn, A. E., Lim, M., Boyer, C. A., Mott, D. M., Maenosono, S., & Thanh, N. T. K. (2016) · Nanoscale · doi:10.1039/c5nr07773g · Cited by 212 · see citing works
Ehrnstorfer, I. A., Geertsma, E. R., Pardon, E., Steyaert, J., & Dutzler, R. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2904 · Cited by 210 · see citing works
The pivotal role of astrocytes in the metabolism of iron in the brain
Dringen, R., Bishop, G. M., Koeppe, M., Dang, T. N., & Robinson, S. R. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9375-0 · Cited by 209 · see citing works
Wallace, D. F., Summerville, L., Crampton, E. M., Frazer, D. M., Anderson, G. J., & Subramaniam, V. N. (2009) · Hepatology · doi:10.1002/hep.23198 · Cited by 206 · see citing works
Schmidt, P. J., Toudjarska, I., Sendamarai, A. K., Racie, T., Milstein, S., Bettencourt, B. R., Hettinger, J., Bumcrot, D., & Fleming, M. D. (2013) · Blood · doi:10.1182/blood-2012-09-453977 · Cited by 204 · see citing works
Iron Is a Sensitive Biomarker for Inflammation in Multiple Sclerosis Lesions
Mehta, V. B., Pei, W., Yang, G., Li, S., Swamy, E., Boster, A. L., Schmalbrock, P., & Pitt, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057573 · Cited by 202 · see citing works
An iron regulatory gene signature predicts outcome in breast cancer
Miller, L. D., Coffman, L. G., Chou, J. W., Black, M. A., Bergh, J., D'Agostino, R., Torti, S. V., & Torti, F. M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1870 · Cited by 202 · see citing works
The Transferrin Receptor: A Potential Molecular Imaging Marker for Human Cancer
Högemann, D., Bos, E., Blondet, C., Sato, F., Abé, T., Josephson, L., Weissleder, R., Gaudet, J., Sgroi, D. C., Peters, P. J., et al. (2003) · Neoplasia · doi:10.1016/s1476-5586(03)80034-9 · Cited by 201 · see citing works
D’Alessio, F., Hentze, M. W., & Muckenthaler, M. U. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.06.015 · Cited by 200 · see citing works
The mitochondrial heme exporter FLVCR1b mediates erythroid differentiation
Chiabrando, D., Marro, S. G., Mercurio, S., Giorgi, C., Petrillo, S., Vinchi, F., Fiorito, V., Fagoonee, S., Camporeale, A., Turco, E., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci62422 · Cited by 198 · see citing works
Effects of a single course of deferoxamine in neuroblastoma patients.
Donfrancesco, A., Deb, G., Dominici, C., Pileggi, D., Castello, M. A., & Helson, L. (1990) · PubMed · Cited by 196 · see citing works
Transferrin therapy ameliorates disease in β-thalassemic mice
Li, H., Rybicki, A. C., Suzuka, S. M., von Bonsdorff, L., Breuer, W., Hall, C. B., Cabantchik, Z. I., Bouhassira, E. E., Fabry, M. E., & Ginzburg, Y. Z. (2010) · Nature Medicine · doi:10.1038/nm.2073 · Cited by 192 · see citing works
Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice
Gunshin, H., Starr, C. N., DiRenzo, C., Fleming, M. D., Jin, J., Greer, E. L., Sellers, V. M., Galica, S. M., & Andrews, N. C. (2005) · Blood · doi:10.1182/blood-2005-02-0716 · Cited by 188 · see citing works
Leptin Increases the Expression of the Iron Regulatory Hormone Hepcidin in HuH7 Human Hepatoma Cells
Chung, B., Matak, P., McKie, A. T., & Sharp, P. (2007) · Journal of Nutrition · doi:10.1093/jn/137.11.2366 · Cited by 186 · see citing works
Hepcidin regulation in prostate and its disruption in prostate cancer
Tesfay, L., Clausen, K. A., Kim, J. W., Hegde, P., Wang, X., Miller, L. D., Deng, Z., Blanchette, N., Arvedson, T., Miranti, C. K., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2465 · Cited by 186 · see citing works
Raha, A. A., Vaishnav, R., Friedland, R. P., Bomford, A. B., & Raha‐Chowdhury, R. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-55 · Cited by 179 · see citing works
Kovačević, Ž., Chikhani, S., Lovejoy, D. B., & Richardson, D. R. (2011) · Molecular Pharmacology · doi:10.1124/mol.111.073627 · Cited by 178 · see citing works
Structure–function analysis of a novel member of the LIV‐1 subfamily of zinc transporters, ZIP14
Taylor, K. M., Morgan, H. E., JOHNSON, A., & Nicholson, R. I. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.006 · Cited by 176 · see citing works
Hojyo, S., Fukada, T., Shimoda, S., Ohashi, W., Bin, B.-H., Koseki, H., & Hirano, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018059 · Cited by 175 · see citing works
A novel inflammatory pathway mediating rapid hepcidin-independent hypoferremia
Guida, C., Altamura, S., Klein, F. A., Galy, B., Boutros, M., Ulmer, A. J., Hentze, M. W., & Muckenthaler, M. U. (2015) · Blood · doi:10.1182/blood-2014-08-595256 · Cited by 173 · see citing works
Understanding Local Macrophage Phenotypes In Disease: Modulating macrophage function to treat cancer
Bronte, V., & Murray, P. J. (2015) · Nature Medicine · doi:10.1038/nm.3794 · Cited by 172 · see citing works
Brigandi, R. A., Johnson, B. M., Oei, C., Westerman, M. E., Olbina, G., de Zoysa, J., Roger, S. D., Sahay, M., Cross, N., McMahon, L. P., et al. (2016) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2015.11.021 · Cited by 170 · see citing works
Canonne-Hergaux, F., Zhang, A.-S., Ponka, P., & Gros, P. (2001) · Blood · doi:10.1182/blood.v98.13.3823 · Cited by 169 · see citing works
Kim, B., Ahn, S. H., Bae, S. J., Kim, E. H., Lee, S., Kim, H., Choe, J. W., Koh, J., & Kim, G. S. (2012) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1692 · Cited by 168 · see citing works
Development of Tridentate Iron Chelators: From Desferrithiocin to ICL670
Nick, H., Acklin, P., Lattmann, R., Buehlmayer, P., Hauffe, S., Schupp, J., & Alberti, D. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033457610 · Cited by 167 · see citing works
The molecular basis of hepcidin-resistant hereditary hemochromatosis
Fernandes, A. O., Preza, G. C., Phung, Y., Domenico, I. D., Kaplan, J., Ganz, T., & Nemeth, E. (2009) · Blood · doi:10.1182/blood-2008-03-146134 · Cited by 166 · see citing works
Hu, H., Hang, J.-J., Han, T., Zhuo, M., Jiao, F., & Wang, L.-W. (2016) · Tumor Biology · doi:10.1007/s13277-015-4741-z · Cited by 162 · see citing works
Deletion of Macrophage LDL Receptor–Related Protein Increases Atherogenesis in the Mouse
Overton, C. D., Yancey, P. G., Major, A. S., Linton, M. F., & Fazio, S. (2007) · Circulation Research · doi:10.1161/01.res.0000260204.40510.aa · Cited by 159 · see citing works
Shawki, A., Anthony, S., Nose, Y., Engevik, M. A., Niespodzany, E. J., Barrientos, T., Öhrvik, H., Worrell, R. T., Thiele, D. J., & Mackenzie, B. (2015) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00160.2015 · Cited by 156 · see citing works
Jiang, Y., Oliver, P. L., Davies, K. E., & Platt, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507599200 · Cited by 154 · see citing works
Erythroferrone contributes to recovery from anemia of inflammation
Kautz, L., Jung, G., Nemeth, E., & Ganz, T. (2014) · Blood · doi:10.1182/blood-2014-06-584607 · Cited by 152 · see citing works
Minihepcidin peptides as disease modifiers in mice affected by β-thalassemia and polycythemia vera
Casu, C., Oikonomidou, P. R., Chen, H., Nandi, V., Ginzburg, Y., Prasad, P., Fleming, R. E., Shah, Y. M., Valore, E. V., Nemeth, E., et al. (2016) · Blood · doi:10.1182/blood-2015-10-676742 · Cited by 148 · see citing works
Self-citationAnaemia in inflammatory rheumatic diseases
Weiss, G., & Schett, G. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2012.183 · Cited by 146 · see citing works
An anemia of Alzheimer's disease
Faux, N. G., Rembach, A., Wiley, J. S., Ellis, K. A., Ames, D. J., Fowler, C. J., Martins, R. N., Pertile, K. K., Rumble, R. L., Trounson, B. O., et al. (2014) · Molecular Psychiatry · doi:10.1038/mp.2013.178 · Cited by 141 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [224]Hartman CS AKB-6548, a new hypoxia-inducible factor prolyl hydroxylase inhibitor increases hemoglobin while decreasing ferritin in a 28-day, phase 2a dose escalation study in stage 3 and 4 chronic kidney disease patients with anemia Proceedings of the American Society of Nephrology Kidney Week 2011
Cited by
Sorted by citations
Ferroptosis is a type of autophagy-dependent cell death
Zhou, B., Liu, J., Kang, R., Klionsky, D. J., Kroemer, G., & Tang, D. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.03.002 · Cited by 1,071 · see citing works
Iron metabolism and iron disorders revisited in the hepcidin era
Camaschella, C., Nai, A., & Silvestri, L. (2020) · Haematologica · doi:10.3324/haematol.2019.232124 · Cited by 734 · see citing works
The tumor suppressor protein p53 and the ferroptosis network
Kang, R., Kroemer, G., & Tang, D. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.074 · Cited by 701 · see citing works
Brissot, P., Pietrangelo, A., Adams, P. C., de Graaff, B., McLaren, C. E., & Loréal, O. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2018.16 · Cited by 430 · see citing works
FTH1 Inhibits Ferroptosis Through Ferritinophagy in the 6-OHDA Model of Parkinson's Disease
Tian, Y., Lü, J., Hao, X., Li, H., Zhang, G., Liu, X., Li, X., Zhao, C., Kuang, W., Chen, D., et al. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00929-z · Cited by 425 · see citing works
Torti, S. V., Manz, D. H., Paul, B. T., Blanchette-Farra, N., & Torti, F. M. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082117-051732 · Cited by 426 · see citing works
Transferrin receptor 1 in cancer: a new sight for cancer therapy.
Shen, Y., Li, X., Dong, D., Zhang, B., Xue, Y., & Shang, P. (2018) · Europe PMC (PubMed Central) · Cited by 357 · see citing works
Structure 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 · see citing works
Iron deficiency anaemia: pathophysiology, assessment, practical management
Kumar, A., Sharma, E., Marley, A., Samaan, M., & Brookes, M. (2022) · BMJ Open Gastroenterology · doi:10.1136/bmjgast-2021-000759 · Cited by 351 · see citing works
The epigenetic regulators and metabolic changes in ferroptosis-associated cancer progression
Wu, Y., Zhang, S.-W., Gong, X., Tam, S., Xiao, D., Liu, S., & Tao, Y. (2020) · Molecular Cancer · doi:10.1186/s12943-020-01157-x · Cited by 341 · see citing works
Emerging mechanisms and targeted therapy of ferroptosis in cancer
Wang, H., Cheng, Y., Mao, C., Liu, S., Xiao, D., Huang, J. X., & Tao, Y. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.03.022 · Cited by 320 · see citing works
Iron metabolism: pathophysiology and pharmacology
Roemhild, K., von Maltzahn, F., Weiskirchen, R., Knüchel, R., von Stillfried, S. F., & Lammers, T. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.05.001 · Cited by 315 · see citing works
Self-citationIron Deficiency in Heart Failure
von Haehling, S., Ebner, N., Evertz, R., Ponikowski, P. P., & Anker, S. D. (2018) · JACC Heart Failure · doi:10.1016/j.jchf.2018.07.015 · Cited by 305 · see citing works
Xue, C., Li, M., Zhao, Y., Zhou, J., Hu, Y., Cai, K.-Y., Zhao, Y., Yu, S., & Luo, Z. Y. (2020) · Science Advances · doi:10.1126/sciadv.aax1346 · Cited by 302 · see citing works
Wang, Y., Lei, Y., Ding, J. P., & Chen, Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010095 · Cited by 297 · see citing works
Iron and Alzheimer’s Disease: From Pathogenesis to Therapeutic Implications
Liu, J., Fan, Y., Yang, Z., Wang, Z., & Guo, C. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00632 · Cited by 286 · see citing works
Dynamic O-GlcNAcylation coordinates ferritinophagy and mitophagy to activate ferroptosis
Yu, F. D., Zhang, Q., Liu, H., Liu, J., Yang, S., Luo, X., Liu, W., Zheng, H., Liu, Q., Cui, Y., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00390-6 · Cited by 287 · see citing works
Iron Metabolism and Immune Regulation
Ni, S., Yuan, Y., Kuang, Y., & Li, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.816282 · Cited by 266 · see citing works
Stem Cell Factor SOX2 Confers Ferroptosis Resistance in Lung Cancer via Upregulation of SLC7A11
Wang, X., Chen, Y., Wang, X., Tian, H., Wang, Y., Jin, J., Shan, Z., Liu, Y., Cai, Z., Tong, X., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-0567 · Cited by 265 · see citing works
Hepcidin and Anemia: A Tight Relationship
Pagani, A., Nai, A., Silvestri, L., & Camaschella, C. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01294 · Cited by 256 · see citing works
Heme: emergent roles of heme in signal transduction, functional regulation and as catalytic centres
Shimizu, T., Lengálová, A., Martínek, V., & Martínková, M. (2019) · Chemical Society Reviews · doi:10.1039/c9cs00268e · Cited by 235 · see citing works
Classical and Nonclassical Intercellular Communication in Senescence and Ageing
Fafián‐Labora, J., & O’Loghlen, A. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.05.003 · Cited by 230 · see citing works
Babitt, J. L., Eisenga, M. F., Haase, V. H., Kshirsagar, A. V., Levin, A., Locatelli, F., Małyszko, J., Swinkels, D. W., Tarng, D., Cheung, M., et al. (2021) · Kidney International · doi:10.1016/j.kint.2021.03.020 · Cited by 222 · see citing works
Fighting age-related orthopedic diseases: focusing on ferroptosis
Ru, Q., Li, Y., Xie, W., Ding, Y., Chen, L., Xu, G., Wu, Y., & Wang, F. (2023) · Bone Research · doi:10.1038/s41413-023-00247-y · Cited by 206 · see citing works
Iron homeostasis in host and gut bacteria – a complex interrelationship
Seyoum, Y., Baye, K., & Humblot, C. (2021) · Gut Microbes · doi:10.1080/19490976.2021.1874855 · Cited by 196 · see citing works
Tumor Abnormality-Oriented Nanomedicine Design
Zhou, Q., Xiang, J., Qiu, N., Wang, Y., Piao, Y., Shao, S., Tang, J., Zhou, Z., & Shen, Y. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00062 · Cited by 194 · see citing works
FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster
Wang, H., Shi, H., Rajan, M., Canarie, E. R., Hong, S., Simoneschi, D., Pagano, M., Bush, M. F., Stoll, S., Leibold, E. A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.02.011 · Cited by 185 · see citing works
Shang, Y., Luo, M., Yao, F., Wang, S., Yuan, Z., & Yang, Y. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109633 · Cited by 181 · see citing works
Torti, S. V., & Torti, F. M. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2017 · Cited by 176 · see citing works
Iron Deficiency in Heart Failure: Mechanisms and Pathophysiology
Alnuwaysir, R. I. S., Hoes, M. F., van Veldhuisen, D. J., van der Meer, P., & Beverborg, N. G. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm11010125 · Cited by 170 · see citing works
Nanomedicine and macroscale materials in immuno-oncology
Sun, Q., Barz, M., Geest, B. G. D., Diken, M., Hennink, W. E., Kiessling, F. M., Lammers, T., & Shi, Y. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00473k · Cited by 153 · see citing works
Self-citationIron Homeostasis Disorder and Alzheimer’s Disease
Peng, Y., Chang, X., & Lang, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212442 · Cited by 143 · see citing works
Pharmacological Targeting of Microglial Activation: New Therapeutic Approach
Liu, C., Wang, X., Liu, C., & Zhang, H. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00514 · Cited by 141 · see citing works
Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities
Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 143 · see citing works
Zhou, Z., Ni, K., Deng, H., & Chen, X. S. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.06.006 · Cited by 139 · see citing works
Su, G.-H., Xiao, Y., You, C., Zheng, R., Zhao, S., Sun, S., Zhou, J.-Y., Lin, L., Wang, H., Shao, Z., et al. (2023) · Science Advances · doi:10.1126/sciadv.adf0837 · Cited by 139 · see citing works
Hepcidin agonists as therapeutic tools
Casu, C., Nemeth, E., & Rivella, S. (2018) · Blood · doi:10.1182/blood-2017-11-737411 · Cited by 131 · see citing works
Self-citationHepcidin and the BMP-SMAD pathway: An unexpected liaison
Silvestri, L., Nai, A., Dulja, A., & Pagani, A. (2019) · Vitamins and hormones · doi:10.1016/bs.vh.2019.01.004 · Cited by 125 · see citing works
Anaemia, Iron Deficiency and Heart Failure in 2020: Facts and Numbers
Chopra, V., & Anker, S. D. (2020) · ESC Heart Failure · doi:10.1002/ehf2.12797 · Cited by 124 · see citing works
Anticancer mechanisms of metformin: A review of the current evidence
Zhao, B., Luo, J., Yu, T., Zhou, L., Lv, H., & Shang, P. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117717 · Cited by 124 · see citing works
Yang, H., Yao, X., Liu, Y., Shen, X., Li, M., & Luo, Z. Y. (2023) · ACS Nano · doi:10.1021/acsnano.3c04632 · Cited by 120 · see citing works
Huang, G., Xiang, Z., Wu, H., He, Q., Dou, R., Lin, Z., Yang, C., Huang, S., Song, J., Di, Z., et al. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.69454 · Cited by 117 · see citing works
Iron: An Essential Element of Cancer Metabolism
Hsu, M. Y., Mina, E., Roetto, A., & Porporato, P. E. (2020) · Cells · doi:10.3390/cells9122591 · Cited by 116 · see citing works
Katsarou, A., & Pantopoulos, K. (2018) · Pharmaceuticals · doi:10.3390/ph11040127 · Cited by 115 · see citing works
Iron Deficiency and Iron Deficiency Anemia: Potential Risk Factors in Bone Loss
Yang, J., Li, Q., Feng, Y., & Zeng, Y. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24086891 · Cited by 125 · see citing works
Recent Progress in Fluorescent Sensors for Drug-Induced Liver Injury Assessment
Chen, J., Huang, D., She, M., Wang, Z., Chen, X., Liu, P., Zhang, S., & Li, J. (2021) · ACS Sensors · doi:10.1021/acssensors.0c02343 · Cited by 111 · see citing works
Lin, K., Xie, A., Rutter, J. C., Ahn, Y.-R., Lloyd-Cowden, J. M., Nichols, A., Soderquist, R. S., Koves, T. R., Muoio, D. M., MacIver, N. J., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.011 · Cited by 102 · see citing works
Hepcidin, an emerging and important player in brain iron homeostasis
Vela, D. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1399-5 · Cited by 104 · see citing works
Ferroptosis regulation through Nrf2 and implications for neurodegenerative diseases
Xiang, Y., Song, X., & Long, D. (2024) · Archives of Toxicology · doi:10.1007/s00204-023-03660-8 · Cited by 109 · see citing works
Advances in the Chemical Biology of Desferrioxamine B
Codd, R., Richardson‐Sanchez, T., Telfer, T. J., & Gotsbacher, M. P. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00851 · Cited by 103 · see citing works
Alterations in Cellular Iron Metabolism Provide More Therapeutic Opportunities for Cancer
Zhou, L., Zhao, B., Zhang, L., Wang, S., Dong, D., Lv, H., & Shang, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051545 · Cited by 102 · see citing works
Autophagy-Dependent Ferroptosis in Cancer
Chen, F., Cai, X., Kang, R., Liu, J., & Tang, D. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0202 · Cited by 101 · see citing works
Targeting ferroptosis as a vulnerability in pulmonary diseases
Yang, L., Cao, L., Zhang, X., & Chu, B. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05070-7 · Cited by 97 · see citing works
Differential regulation of hepcidin in cancer and non-cancer tissues and its clinical implications
Vela, D., & Vela‐Gaxha, Z. (2018) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.273 · Cited by 94 · see citing works
Zhu, J., Dai, P., Liu, F., Li, Y., Qin, Y., Yang, Q., Tian, R., Fan, A., Medeiros, S. F., Wang, Z., et al. (2020) · Nano Letters · doi:10.1021/acs.nanolett.0c00502 · Cited by 93 · see citing works
Yang, J., Zhang, J., Ding, C., Dong, D., & Shang, P. (2017) · Biological Trace Element Research · doi:10.1007/s12011-017-1161-5 · Cited by 88 · see citing works
Ehsani, S. (2020) · Biology Direct · doi:10.1186/s13062-020-00275-2 · Cited by 87 · see citing works
Hirayama, T., Niwa, M., Hirosawa, S., & Nagasawa, H. (2020) · ACS Sensors · doi:10.1021/acssensors.0c01445 · Cited by 90 · see citing works
Weber, S., Parmon, A., Kurrle, N., Schnütgen, F., & Serve, H. L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.627662 · Cited by 86 · see citing works
Feng, Q., Fang, W., Guo, Y., Hu, P., & Shi, J. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c08032 · Cited by 83 · see citing works
The crosstalk between mitochondrial quality control and metal-dependent cell death
Zhou, Q.-Y., Ren, C., Li, J., Wang, L., Duan, Y., Yao, R.-Q., Tian, Y., & Yao, Y.-M. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06691-w · Cited by 83 · see citing works
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 · see citing works
Li, J., Zheng, S., Fan, Y., & Tan, K. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06144-w · Cited by 82 · see citing works
Lv, H., Zhen, C., Liu, J., & Shang, P. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5021983 · Cited by 80 · see citing works
Iron metabolism gene expression and prognostic features of hepatocellular carcinoma
Shen, Y., Li, X., Zhao, B., Xue, Y., Wang, S., Chen, X., Yang, J., Lv, H., & Shang, P. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27184 · Cited by 79 · see citing works
Ge, C., Zhang, S., Mu, H., Shaojun, Z., Tan, Z., Huang, X., Chen, X., Zou, J., Zhu, Y., Dong, F., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.774957 · Cited by 77 · see citing works
Brain metabolism in Alzheimer’s disease: biological mechanisms of exercise
Xu, L., Liu, R., Qin, Y., & Wang, T. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00364-y · Cited by 78 · see citing works
Ferroptosis: Biochemistry and Biology in Cancers
Shi, Z., Zhang, L., Zheng, J., Sun, H., & Shao, C. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.579286 · Cited by 74 · see citing works
The role of iron homeostasis and iron-mediated ROS in cancer.
Ying, J., Lu, Z.-B., Fu, L., Tong, Y., Wang, Z., Li, W., & Mou, X. (2021) · PubMed Central · Cited by 74 · see citing works
Iron Deficiency in Heart Failure: A Scientific Statement from the Heart Failure Society of America
Beavers, C. J., Ambrosy, A. P., Butler, J., Davidson, B. T., Gale, S. E., Piña, I. L., Mastoris, I., Reza, N., Mentz, R. J., & Lewis, G. D. (2023) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2023.03.025 · Cited by 74 · see citing works
Spectrum of Restrictive and Infiltrative Cardiomyopathies
Pereira, N. L., Grogan, M. A., & Dec, G. W. (2018) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2018.01.017 · Cited by 71 · see citing works
Chen, Y., Deng, J., Liu, F., Dai, P., An, Y., Wang, Z., & Zhao, Y. (2019) · Advanced Healthcare Materials · doi:10.1002/adhm.201900366 · Cited by 70 · see citing works
Mitochondrial Iron Metabolism: The Crucial Actors in Diseases
Duan, G., Li, J., Duan, Y., Zheng, C., Guo, Q., Li, F., Zheng, J., Yu, J., Zhang, P., Wan, M., et al. (2022) · Molecules · doi:10.3390/molecules28010029 · Cited by 73 · see citing works
Efficient Iron and ROS Nanoscavengers for Brain Protection after Intracerebral Hemorrhage
Zhu, F., Zi, L., Yang, P., Yang, W., Zhong, R., Wang, Y., You, C., Li, Y., Tian, M., & Gu, Z. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c00491 · Cited by 68 · see citing works
Nanomedicine in Hepatocellular Carcinoma: A New Frontier in Targeted Cancer Treatment
Bakrania, A. K., Zheng, G., & Bhat, M. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics14010041 · Cited by 68 · see citing works
Small-Molecule Ferritin Degrader as a Pyroptosis Inducer
Chen, Y., Li, W., Kwon, S. C., Wang, Y., Li, Z., & Hu, Q. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c01852 · Cited by 67 · see citing works
Construction of a Plasmonic Chip for Metabolic Analysis in Cervical Cancer Screening and Evaluation
Shu, W., Wang, Y., Liu, C., Li, R., Pei, C., Lou, W., Lin, S., Di, W. J., & Wan, J. (2019) · Small Methods · doi:10.1002/smtd.201900469 · Cited by 66 · see citing works
Metal Ion Signaling in Biomedicine
Rodriguez, R., Müller, S., Colombeau, L., Solier, S., Sindikubwabo, F., & Cañeque, T. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00577 · Cited by 66 · see citing works
A Review on the Recent Advancements on Therapeutic Effects of Ions in the Physiological Environments
Awais, M., Aizaz, A., Nazneen, A., Bhatti, Q. U. A., Akhtar, M., Wadood, A., & Rehman, M. A. U. (2022) · Prosthesis · doi:10.3390/prosthesis4020026 · Cited by 65 · see citing works
Beneficial and Detrimental Roles of Heme Oxygenase-1 in the Neurovascular System
Choi, Y. K., & Kim, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137041 · Cited by 63 · see citing works
Mineral metabolism and ferroptosis in non-alcoholic fatty liver diseases
Ma, C., Li, H., Zhu, Z., Pang, C. H., & Pan, G. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115242 · Cited by 67 · see citing works
Hepcidin and its therapeutic potential in neurodegenerative disorders
Qian, Z., & Ke, Y. (2019) · Medicinal Research Reviews · doi:10.1002/med.21631 · Cited by 63 · see citing works
Bömer, N., Pávez, M., Beverborg, N. G., Cleland, J. G. F., van Veldhuisen, D. J., & van der Meer, P. (2022) · Journal of Internal Medicine · doi:10.1111/joim.13456 · Cited by 64 · see citing works
A mini-review and perspective on ferroptosis-inducing strategies in cancer therapy
Wang, S., Liao, H., Li, F., & Ling, D. (2019) · Chinese Chemical Letters · doi:10.1016/j.cclet.2019.03.025 · Cited by 63 · see citing works
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 · see citing works
Axonal iron transport in the brain modulates anxiety-related behaviors
Wang, Z., Zeng, Y., Yang, P., Jin, L.-Q., Xiong, W., Zhu, M., Zhang, J., He, X. B., & Zhu, X. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0371-x · Cited by 62 · see citing works
Developing New Cancer Nanomedicines by Repurposing Old Drugs
Yang, B., & Shi, J. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202004317 · Cited by 60 · see citing works
Metabolic Control of m6A RNA Modification
Kim, J., & Lee, G. (2021) · Metabolites · doi:10.3390/metabo11020080 · Cited by 56 · see citing works
Antiviral effects of ferric ammonium citrate
Wang, H., Li, Z., Niu, J., Xu, Y., Ma, L., Lu, A., Wang, X., Qian, Z., Huang, Z. W., Jin, X., et al. (2018) · Cell Discovery · doi:10.1038/s41421-018-0013-6 · Cited by 55 · see citing works
Faham, S., Golmohammadi, H., Ghavami, R., & Khayatian, G. (2019) · Analytica Chimica Acta · doi:10.1016/j.aca.2019.08.056 · Cited by 56 · see citing works
Qian, W., Liu, D., Han, Y., Liu, M., Liu, B., Ji, Q., Zhang, B., Mei, Q., Zhou, S., & Cheng, Y. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.02.025 · Cited by 55 · see citing works
Zhu, X., Zhang, H., & Mendell, J. T. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107895 · Cited by 55 · see citing works
Hydroxypyridinone-Based Iron Chelators with Broad-Ranging Biological Activities
Jiang, X., Zhou, T., Bai, R., & Xie, Y. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01480 · Cited by 54 · see citing works
Yang, J., Zhang, G., Dong, D., & Shang, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092608 · Cited by 54 · see citing works
Alcohol Exposure Induces Depressive and Anxiety-like Behaviors via Activating Ferroptosis in Mice
Xu, C., Xiong, Q., Tian, X., Liu, W., Sun, B., Ru, Q., & Shu, X. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213828 · Cited by 55 · see citing works
Yu, B., Liu, J., Cheng, J., Zhang, L., Song, C., Tian, X., Fan, Y., Lv, Y. M., & Zhang, X. (2021) · The Innovation · doi:10.1016/j.xinn.2021.100077 · Cited by 53 · see citing works
Ceruloplasmin Plays a Neuroprotective Role in Cerebral Ischemia
Ryan, F., Zarruk, J. G., Lößlein, L., & David, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00988 · Cited by 53 · see citing works
Procyanidins Boost the Neuroprotective Effect of Minocycline for Intracerebral Haemorrhage
Yuan, T., Wang, T., Zhang, J., Shi, S., Gu, Z., Li, Y., & Xu, J. (2023) · Advanced Functional Materials · doi:10.1002/adfm.202303379 · Cited by 50 · see citing works
Ru, Q., Li, Y., Zhang, F., Chen, L., Wu, Y., Min, J., & Wang, F. (2025) · Bone Research · doi:10.1038/s41413-024-00398-6 · Cited by 57 · see citing works
Choi, D.-H., Kwon, K.-C., Hwang, D.-J., Koo, J., Um, H.-S., Song, H., Kim, J., Jang, Y., & Cho, J. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02335-8 · Cited by 49 · see citing works
- Authors
- Crielaard, B. J., Lammers, T., & Rivella, S.
- Affiliations
- University Medical Center Groningen (NL)
- Utrecht University (NL)
- Children's Hospital of Philadelphia (US)
- Corresponding author
- Crielaard, Bart J.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2017-02-03
- Volume
- 16
- Issue
- 6
- Pages
- 400-423
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- PMC
- PMC5455971
- OpenAlex
- W2584260978
- Semantic Scholar
- 1e1ed22b40ae820d21446fbca090adacc01a21b1
- Cited by
- 352
- References
- 352
- Citations by year
- 2026: 19 · 2025: 38 · 2024: 37 · 2023: 51 · 2022: 58 · 2021: 39 · 2020: 33 · 2019: 38 · 2018: 32 · 2017: 6 · 2016: 1
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- green
- research.rug.nl
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Drug Discovery (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
- University of Twente Research Information (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RWTH Publications (RWTH Aachen) (submittedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, other-oa)
- University of Twente Research Information (submittedVersion, other-oa)
- Funders
- Eli Lilly and Company
- La Jolla Pharmaceutical Company
- Ionis Pharmaceuticals
- European Commission (HORIZON2020, 707229)
- Deutsche Forschungsgemeinschaft (309495, LA2937/1-2)
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK090554, R01DK095112)
- H2020 European Research Council (680882)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- iron metabolism, iron homeostasis, drug delivery, hematologic disorders, cancer, neurodegeneration, therapeutic target
- MeSH terms
- Animals, Homeostasis, Humans, Iron, Neoplasms, Drug Design, Drug Delivery Systems, Neurodegenerative Diseases, Drug Discovery, Molecular Targeted Therapy
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