An overview of molecular basis of iron metabolism regulation and the associated pathologies
Open accessAbstract
Iron is essential for several vital biological processes. Its deficiency or overload drives to the development of several pathologies. To maintain iron homeostasis, the organism controls the dietary iron absorption by enterocytes, its recycling by macrophages and storage in hepatocytes. These processes are mainly controlled by hepcidin, a liver-derived hormone which synthesis is regulated by iron levels, inflammation, infection, anemia and erythropoiesis. Besides the systemic regulation of iron metabolism mediated by hepcidin, cellular regulatory processes also occur. Cells are able to regulate themselves the expression of the iron metabolism-related genes through different post-transcriptional mechanisms, such as the alternative splicing, microRNAs, the IRP/IRE system and the proteolytic cleavage. Whenever those mechanisms are disturbed, due to genetic or environmental factors, iron homeostasis is disrupted and iron related pathologies may arise.
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?
The HIF and NRF2 pathways are related with anemia.
“Furthermore, the hypoxia inducible factor (HIF) and the nuclear factor-erythroid 2-related factor 2 (NRF2) pathways are related with anemia (Lee et al., 2004;Silva and Faustino, 2015).”
From Identification of Candidate Signature Genes and Key Regulators Associated With Trypanotolerance in the Sheko Breed (2019) · cites this paper as Silva and Faustino, 2015
Section 4.1.4, “Anemia and erythropoiesis” (page unavailable), links anemia-related hypoxia to HIF-2 regulation of erythropoietin. Our copy does not establish the claimed NRF2–anemia relationship; searches for NRF2 and Nrf2 found no relevant passage. (LLM, conf=0.85)
Experimental — accuracy not yet measured
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
MicroRNAs: small RNAs with a big role in gene regulation
He, L., & Hannon, G. J. (2004) · Nature Reviews Genetics · doi:10.1038/nrg1379 · Cited by 5,910 · see citing works
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180 · 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
Weiss, G., & Goodnough, L. T. (2005) · New England Journal of Medicine · doi:10.1056/nejmra041809 · Cited by 3,800 · 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
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
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 · cited 4× · see citing works
“The hypoferremia commonly associated with the infection is one of the several innate and adaptive responses of the immune system [70].”
BackgroundInfluentialExpansion of the eukaryotic proteome by alternative splicing
Nilsen, T. W., & Graveley, B. R. (2010) · Nature · doi:10.1038/nature08909 · Cited by 2,172 · 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
Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130 · 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
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
Ambros, V. (2001) · Cell · doi:10.1016/s0092-8674(01)00616-x · Cited by 1,704 · see citing works
Structure, function, and formation of biological iron-sulfur clusters
Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438 · cited 1× · see citing works
“During iron de fi ciency, IRP1 binds to IRE through a cavity on its structure, while under iron overload that same cavity is occupied by the 4Fe – 4S cluster and unavailable to bind to the IRE [137,138].”
BackgroundHepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
Nemeth, E., Valore, E. V., Territo, M., Schiller, G., Lichtenstein, A., & Ganz, T. (2003) · Blood · doi:10.1182/blood-2002-10-3235 · Cited by 1,417 · see citing works
RNA‐binding proteins and post‐transcriptional gene regulation
Glisovic, T., Bachorik, J. L., Yong, J., & Dreyfuss, G. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.004 · Cited by 1,398 · 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
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214 · see citing works
Haas, J. D., & Brownlie, T. (2001) · The Journal of Nutrition · doi:10.1093/jn/131.2.676s · Cited by 1,186 · see citing works
Trophic macrophages in development and disease
Pollard, J. W. (2009) · Nature Reviews Immunology · doi:10.1038/nri2528 · Cited by 1,178 · see citing works
Iron Biology in Immune Function, Muscle Metabolism and Neuronal Functioning
Beard, J. L. (2001) · Journal of Nutrition · doi:10.1093/jn/131.2.568s · Cited by 1,136 · 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
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
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 · cited 1× · see citing works
“The activated receptors induce the phosphorylation of cytosolic SMADs 1, 5 and 8 [71,73,74].”
BackgroundHeme 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
Interleukin-6 induces hepcidin expression through STAT3
Wrighting, D. M., & Andrews, N. C. (2006) · Blood · doi:10.1182/blood-2006-06-027631 · Cited by 983 · 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
High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
Tanno, T., Bhanu, N. V., Oneal, P. A., Goh, S.-H., Staker, P., Lee, Y. T., Moroney, J. W., Reed, C. H., Luban, N. L., Wang, R.-H., et al. (2007) · Nature Medicine · doi:10.1038/nm1629 · Cited by 854 · see citing works
The biology and therapeutic targeting of the proprotein convertases
Seidah, N. G., & Prat, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3699 · Cited by 819 · 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
Iron-Oxidizing Bacteria: An Environmental and Genomic Perspective
Emerson, D., Fleming, E. J., & McBeth, J. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.112408.134208 · Cited by 797 · see citing works
Global prevalence of putative haemochromatosis mutations.
Merryweather‐Clarke, A. T., Pointon, J. J., Shearman, J. R., & Robson, K. (1997) · Journal of Medical Genetics · doi:10.1136/jmg.34.4.275 · Cited by 785 · see citing works
Lee, P. J., Jiang, B.-H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., & Choi, A. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5375 · Cited by 782 · see citing works
Hemochromatosis and Iron-Overload Screening in a Racially Diverse Population
Adams, P. C., Reboussin, D. M., Barton, J. C., McLaren, C. E., Eckfeldt, J. H., McLaren, G. D., Dawkins, F. W., Acton, R. T., Harris, E. L., Gordeuk, V. R., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa041534 · Cited by 770 · 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
Dowdle, W. E., Nyfeler, B., Nagel, J., Elling, R. A., Liu, S., Triantafellow, E., Menon, S., Wang, Z., Honda, A., Pardee, G., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3053 · Cited by 759 · 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
Crichton, R. R., & CHARLOTEAUX‐WAUTERS, M. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb11155.x · Cited by 682 · 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
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
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
Hereditary Hemochromatosis: Pathogenesis, Diagnosis, and Treatment
Pietrangelo, A. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.06.013 · Cited by 615 · see citing works
Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo
Rankin, E. B., Biju, M. P., Liu, Q., Unger, T. L., Rha, J., Johnson, R. S., Simon, M. C., Keith, B., & Haase, V. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30117 · Cited by 596 · see citing works
The mammalian basic helix–loop–helix/PAS family of transcriptional regulators
Kewley, R. J., Whitelaw, M. L., & Chapman‐Smith, A. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00211-5 · Cited by 590 · 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
Current Production and Metal Oxide Reduction by Shewanella oneidensis MR-1 Wild Type and Mutants
Bretschger, O., Obraztsova, A., Sturm, C. A., Chang, I. S., Gorby, Y. A., Reed, S. B., Culley, D. E., Reardon, C. L., Barua, S., Romine, M. F., et al. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.01087-07 · Cited by 577 · 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
Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10812 · Cited by 568 · see citing works
H <sub>2</sub> -rich fluids from serpentinization: Geochemical and biotic implications
Sleep, N. H., Meibom, A., Fridriksson, T., Coleman, R. G., & Bird, D. K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405289101 · Cited by 568 · 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
Regulation of hepcidin transcription by interleukin-1 and interleukin-6
Lee, P. L., Peng, H., Gelbart, T., Wang, L., & Beutler, E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409808102 · Cited by 542 · see citing works
A cytosolic iron chaperone that delivers iron to ferritin
Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536 · see citing works
Bekri, S., Gual, P., Anty, R., Luciani, N., Dahman, M., Ramesh, B., Iannelli, A., Staccini–Myx, A., Casanova, D., Ben Amor, I., et al. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.07.007 · Cited by 496 · see citing works
Mammalian iron metabolism and its control by iron regulatory proteins
Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works
Feder, J. N., Tsuchihashi, Z., Irrinki, A., Lee, V. K., Mapa, F. A., Morikang, E., Prass, C. E., Starnes, S. M., Wolff, R. K., Parkkila, S., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14025 · Cited by 471 · see citing works
Regulators of iron balance in humans [see comments]
Finch, C. (1994) · Blood · doi:10.1182/blood.v84.6.1697.1697 · Cited by 455 · see citing works
The origin of membrane bioenergetics
Lane, N., & Martin, W. F. (2012) · Cell · doi:10.1016/j.cell.2012.11.050 · Cited by 452 · see citing works
Prevalence and outcomes of anemia in geriatrics: a systematic review of the literature
Beghé, C., Wilson, A., & Ershler, W. B. (2004) · The American Journal of Medicine · doi:10.1016/j.amjmed.2003.12.009 · Cited by 450 · see citing works
Kautz, L., Meynard, D., Monnier, A., Darnaud, V., Bouvet, R., Wang, R.-H., Deng, C., Vaulont, S., Mosser, J., Coppin, H., et al. (2008) · Blood · doi:10.1182/blood-2008-03-143354 · Cited by 437 · see citing works
An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis
Salahudeen, A. A., Thompson, J. W., Ruiz, J. C., Ma, H.-W., Kinch, L. N., Li, Q., Grishin, N. V., & Bruick, R. K. (2009) · Science · doi:10.1126/science.1176326 · Cited by 432 · 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
Hubert, N., & Hentze, M. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192423399 · Cited by 428 · see citing works
Non‐Specific Serum Iron in Thalassaemia: an Abnormal Serum Iron Fraction of Potential Toxicity
Hershko, C., Graham, G. M., Bates, G. W., & Rachmilewitz, E. A. (1978) · British Journal of Haematology · doi:10.1111/j.1365-2141.1978.tb03662.x · Cited by 421 · see citing works
Non-transferrin-bound iron in plasma or serum from patients with idiopathic hemochromatosis
Grootveld, M. C., Bell, J. D., Halliwell, B. B., Aruoma, O. I., Bomford, A. B., & Sadler, P. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83758-9 · Cited by 404 · see citing works
A human mitochondrial ferritin encoded by an intronless gene
Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400 · see citing works
Hunter, H. N., Fulton, D. B., Ganz, T., & Vogel, H. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205305200 · Cited by 400 · see citing works
The Role of Hemoglobin Denaturation and Band 3 Clustering in Red Blood Cell Aging
Low, P. S., Waugh, S. M., Zinke, K., & Drenckhahn, D. (1985) · Science · doi:10.1126/science.2578228 · Cited by 395 · see citing works
Hepcidin—a regulator of intestinal iron absorption and iron recycling by macrophages
GANZ, T. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.08.020 · Cited by 393 · see citing works
Clark, S. F. (2008) · Nutrition in Clinical Practice · doi:10.1177/0884533608314536 · Cited by 380 · see citing works
Identification of a hypoxia response element in the transferrin receptor gene
Lok, C. N., & Ponka, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24147 · Cited by 380 · see citing works
Tanno, T., Porayette, P., Sripichai, O., Noh, S.-J., Byrnes, C., Bhupatiraju, A., Lee, Y. T., Goodnough, J. B., Harandi, O., Ganz, T., et al. (2009) · Blood · doi:10.1182/blood-2008-12-195503 · Cited by 352 · see citing works
Hypoxic regulation of erythropoiesis and iron metabolism
Haase, V. H. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00174.2010 · 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
Siderophore uptake in bacteria and the battle for iron with the host; a bird’s eye view
Chu, B. C. H., Garcia-Herrero, A., Johanson, T. H., Krewulak, K. D., Lau, C. K. Y., Peacock, R. S., Slavinskaya, Z., & Vogel, H. J. (2010) · BioMetals · doi:10.1007/s10534-010-9361-x · Cited by 339 · see citing works
Casey, J. L., Koeller, D. M., Ramin, V. C., Klausner, R. D., & Harford, J. B. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08544.x · Cited by 338 · see citing works
Iron/sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity
Roche, B., Aussel, L., Ezraty, B., Mandin, P., Py, B., & Barras, F. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.010 · Cited by 335 · see citing works
Hepcidin-Induced Endocytosis of Ferroportin Is Dependent on Ferroportin Ubiquitination
Qiao, B., Sugianto, P., Fung, E., del-Castillo-Rueda, A., Moran-Jimenez, M.-J., Ganz, T., & Nemeth, E. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.03.018 · Cited by 334 · see citing works
Gao, J., Chen, J., Kramer, M., Tsukamoto, H., Zhang, A.-S., & Enns, C. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.01.010 · Cited by 326 · see citing works
Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis
Silvestri, L., Pagani, A., & Camaschella, C. (2008) · Blood · doi:10.1182/blood-2007-07-100677 · Cited by 311 · see citing works
Truksa, J., Peng, H., Lee, P., & Beutler, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603124103 · Cited by 309 · see citing works
Rivera, S., Nemeth, E., Gabayan, V., Lopez, M. A., Farshidi, D., & Ganz, T. (2005) · Blood · doi:10.1182/blood-2005-04-1766 · Cited by 308 · see citing works
Iron-dependent regulation of the divalent metal ion transporter
Gunshin, H., Allerson, C. R., Polycarpou-Schwarz, M., Rofts, A., Rogers, J. T., Kishi, F., Hentze, M. W., Rouault, T. A., Andrews, N. C., & Hediger, M. A. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03189-1 · Cited by 305 · see citing works
Frey, P. A., & Reed, G. H. (2012) · ACS Chemical Biology · doi:10.1021/cb300323q · Cited by 299 · see citing works
Iron Regulates the Intracellular Degradation of Iron Regulatory Protein 2 by the Proteasome
Guo, B., Phillips, J. D., Yu, Y., & Leibold, E. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21645 · Cited by 287 · see citing works
Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287 · see citing works
Zhang, D.-L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., & Rouault, T. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.006 · Cited by 281 · see citing works
Role of hypoxia-inducible factor-1 in transcriptional activation of ceruloplasmin by iron deficiency
Mukhopadhyay, C. K., Mazumder, B., & Fox, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000636200 · Cited by 274 · see citing works
Lin, L., Valore, E. V., Nemeth, E., Goodnough, J. B., Gabayan, V., & Ganz, T. (2007) · Blood · doi:10.1182/blood-2007-04-087593 · Cited by 267 · see citing works
Direct interorganellar transfer of iron from endosome to mitochondrion
Sheftel, A. D., Zhang, A., Brown, C. M., Shirihai, O. S., & Ponka, P. (2007) · Blood · doi:10.1182/blood-2007-01-068148 · Cited by 266 · see citing works
Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis
Vokurka, M., Krijt, J., Šulc, K., & Nečas, E. (2006) · Physiological Research · doi:10.33549/physiolres.930841 · Cited by 263 · see citing works
Erythrocyte Aging: A More than Superficial Resemblance to Apoptosis?
Bosman, G., Willekens, F., & Werre, J. (2005) · Cellular Physiology and Biochemistry · doi:10.1159/000087725 · Cited by 253 · see citing works
The liver-specific microRNA miR-122 controls systemic iron homeostasis in mice
Castoldi, M., Spasić, M. V., Altamura, S., Elmén, J., Lindow, M., Kiss, J., Stolte, J., Sparla, R., D’Alessandro, L. A., Klingmüller, U., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44883 · Cited by 246 · see citing works
Kulaksiz, H., Theilig, F., Bachmann, S., Gehrke, S. G., Rost, D., Janetzko, A., Cetin, Y., & Stremmel, W. (2005) · Journal of Endocrinology · doi:10.1677/joe.1.05729 · Cited by 241 · see citing works
Valore, E. V., & Ganz, T. (2008) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.07.009 · Cited by 234 · see citing works
Gross, C. N., Irrinki, A., Feder, J. N., & Enns, C. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.22068 · Cited by 227 · see citing works
Schito, L., Rey, S., Tafani, M., Zhang, H., Wong, C. C.-L., Russo, A., Russo, M. A., & Semenza, G. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214019109 · Cited by 224 · see citing works
Xia, Y. Y., Babitt, J. L., Sidis, Y., Chung, R. T., & Lin, H. Y.-F. (2008) · Blood · doi:10.1182/blood-2007-09-111567 · Cited by 223 · see citing works
Samaniego, F., Chin, J., Iwaï, K., Rouault, T. A., & Klausner, R. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47367-x · Cited by 219 · see citing works
Discovery of Genes Essential for Heme Biosynthesis through Large-Scale Gene Expression Analysis
Nilsson, R., Schultz, I. J., Pierce, E. L., Soltis, K. A., Naranuntarat, A., Ward, D. M., Baughman, J. M., Paradkar, P. N., Kingsley, P. D., Culotta, V., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.012 · Cited by 213 · see citing works
Role of ferritin alterations in human breast cancer cells
Shpyleva, S., Tryndyak, V., Kovalchuk, O., Starlard‐Davenport, A., Chekhun, V. F., Beland, F. A., & Pogribny, I. P. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-0849-4 · Cited by 206 · see citing works
Patel, B. N., Dunn, R. J., & David, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4305 · Cited by 202 · see citing works
Advances in Quantitative Hepcidin Measurements by Time-of-Flight Mass Spectrometry
Swinkels, D. W., Girelli, D., Laarakkers, C. M., Kroot, J. J., Campostrini, N., Kemna, E., & Tjalsma, H. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002706 · Cited by 202 · 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
Hou, W., Tian, Q., Zheng, J., & Bonkovsky, H. L. (2009) · Hepatology · doi:10.1002/hep.23401 · Cited by 199 · see citing works
The role of transferrin in the mechanism of cellular iron uptake
Thorstensen, K., & Romslo, I. (1990) · Biochemical Journal · doi:10.1042/bj2710001 · Cited by 194 · see citing works
Ashby, D. R., Gale, D. P., Busbridge, M., Murphy, K. G., Duncan, N. D., Cairns, T. D., Taube, D. H., Bloom, S. R., Tam, F. W. K., Chapman, R., et al. (2010) · Haematologica · doi:10.3324/haematol.2009.013136 · Cited by 191 · cited 1× · see citing works
“However, it was reported that the administration of erythropoietin to healthy individuals lowered the levels of circulatory hepcidin, while no immediate changes of iron levels were detected [114].”
BackgroundPathology of hepatic iron overload
Deugnier, Y. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4755 · Cited by 187 · see citing works
The role of the iron responsive element in the control of ferroportin1/IREG1/MTP1 gene expression
Lymboussaki, A., Pignatti, E., Montosi, G., Garuti, C., Haile, D. J., & Pietrangelo, A. (2003) · Journal of Hepatology · doi:10.1016/s0168-8278(03)00408-2 · Cited by 177 · see citing works
Nramp1 promotes efficient macrophage recycling of iron following erythrophagocytosis in vivo
Soe-Lin, S., Apte, S. S., Andriopoulos, B., Andrews, M. C., Schranzhofer, M., Kahawita, T., Garcia-Santos, D., & Ponka, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900808106 · Cited by 167 · see citing works
The FBXL5-IRP2 Axis Is Integral to Control of Iron Metabolism In Vivo
Moroishi, T., Nishiyama, M., Takeda, Y., Iwaï, K., & Nakayama, K. I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.011 · Cited by 163 · see citing works
Casanovas, G., Mleczko-Sanecka, K., Altamura, S., Hentze, M. W., & Muckenthaler, M. U. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0447-2 · Cited by 161 · see citing works
Pathology of dietary carbonyl iron overload in rats.
Park, C. H., Bacon, B. R., Brittenham, G., & Tavill, A. S. (1987) · PubMed · Cited by 151 · see citing works
Zhang, A., West, A. P., Wyman, A. E., Björkman, P. J., & Enns, C. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506207200 · Cited by 149 · see citing works
Sham, R. L., Phatak, P. D., West, C., Lee, P., Andrews, C., & Beutler, E. (2005) · Blood Cells, Molecules, and Diseases · doi:10.1016/j.bcmd.2004.12.002 · Cited by 146 · see citing works
Alternative mRNA polyadenylation in eukaryotes: an effective regulator of gene expression
Lutz, C. S., & Moreira, A. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.47 · Cited by 145 · see citing works
Hypoxia induced downregulation of hepcidin is mediated by platelet derived growth factor BB
Sonnweber, T., Nachbaur, D., Schroll, A., Nairz, M., Seifert, M., Demetz, E., Haschka, D., Mitterstiller, A.-M., Kleinsasser, A., Burtscher, M., et al. (2014) · Gut · doi:10.1136/gutjnl-2013-305317 · Cited by 145 · see citing works
Hepcidin expression and iron transport in alveolar macrophages
Nguyen, N.-B., Callaghan, K. D., Ghio, A. J., Haile, D. J., & Yang, F. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00484.2005 · Cited by 143 · see citing works
Alternative Splicing Regulates the Subcellular Localization of Divalent Metal Transporter 1 Isoforms
Tabuchi, M., Tanaka, N., Nishida-Kitayama, J., Ohno, H., & Kishi, F. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-03-0165 · Cited by 141 · cited 1× · see citing works
“On the other hand, DMT1B does not have the IRE, thus it does not respond to iron, and it is expressed mainly by blood cells [132].”
BackgroundIron–sulphur clusters in nucleic acid processing enzymes
White, M. F., & Dillingham, M. S. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.11.004 · Cited by 136 · see citing works
Matriptase-2 (TMPRSS6): a proteolytic regulator of iron homeostasis
Ramsay, A. J., Hooper, J. D., Folgueras, A. R., Velasco, G., & López-Otı́n, C. (2009) · Haematologica · doi:10.3324/haematol.2008.001867 · Cited by 132 · see citing works
Pantaleo, A., Giribaldi, G., Mannu, F., Arese, P., & Turrini, F. (2008) · Autoimmunity Reviews · doi:10.1016/j.autrev.2008.03.017 · Cited by 130 · see citing works
miR-320 targets transferrin receptor 1 (CD71) and inhibits cell proliferation
Schaar, D. G., Medina, D. J., Moore, D. F., STRAIR, R. K., & Ting, Y. (2009) · Experimental Hematology · doi:10.1016/j.exphem.2008.10.002 · Cited by 130 · see citing works
Characterization and Expression of Iron Regulatory Protein 2 (IRP2)
Guo, B., Brown, F. M., Phillips, J. D., Yu, Y., & Leibold, E. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16529 · Cited by 129 · see citing works
Pancreatic β-cells express hepcidin, an iron-uptake regulatory peptide
Kulaksiz, H., Fein, E., Redecker, P., Stremmel, W., Adler, G., & Cetin, Y. (2008) · Journal of Endocrinology · doi:10.1677/joe-07-0528 · Cited by 129 · see citing works
HFE interacts with the BMP type I receptor ALK3 to regulate hepcidin expression
Wu, X.-G., Wang, Y., Wu, Q., Cheng, W. H., Liu, W., Zhao, Y., Mayeur, C., Schmidt, P. J., Yu, P. B., Wang, F., et al. (2014) · Blood · doi:10.1182/blood-2014-01-552281 · Cited by 129 · see citing works
Charlton, R. W., & Bothwell, T. H. (1983) · Annual Review of Medicine · doi:10.1146/annurev.me.34.020183.000415 · Cited by 126 · see citing works
Conrad, M. E., & Jn, U. (2000) · New England Journal of Medicine · doi:10.1056/nejm200004273421716 · Cited by 125 · see citing works
ROS mediate the hypoxic repression of the hepcidin gene by inhibiting C/EBPα and STAT-3
Choi, S.-O., Cho, Y.-S., Kim, H.-L., & Park, J.-W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.137 · Cited by 122 · see citing works
Iron-Responsive miR-485-3p Regulates Cellular Iron Homeostasis by Targeting Ferroportin
Sangokoya, C., Doss, J. F., & Chi, J. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003408 · Cited by 122 · see citing works
Ramey, G., Deschemin, J., & Vaulont, S. (2009) · Haematologica · doi:10.3324/haematol.2008.003541 · Cited by 122 · see citing works
Caco-2 Intestinal Epithelial Cells Absorb Soybean Ferritin by μ2 (AP2)-Dependent Endocytosis
SanMartín, C. D., Garri, C., Pizarro, F., Walter, T., Theil, E. C., & Núñez, M. T. (2008) · Journal of Nutrition · doi:10.1093/jn/138.4.659 · Cited by 121 · see citing works
Mechanism for phosphatidylserine-dependent erythrophagocytosis in mouse liver
Lee, S.-J., Park, S., Jung, M.-Y., Bae, S. M., & Kim, I.-S. (2011) · Blood · doi:10.1182/blood-2010-10-313239 · Cited by 119 · see citing works
Walling, C. T., Partch, R. E., & Weil, T. M. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.140 · Cited by 116 · see citing works
Walsh, A. J., Dixon, J. L., Ramm, G. A., Hewett, D. G., Lincoln, D. J., Anderson, G. J., Subramaniam, V. N., Dodemaide, J., Cavanaugh, J. A., Bassett, M. L., et al. (2006) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2006.07.009 · Cited by 115 · see citing works
Kono, S. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00007-7 · Cited by 105 · see citing works
Truksa, J., Lee, P. L., & Beutler, E. (2008) · Blood · doi:10.1182/blood-2008-05-160184 · Cited by 104 · see citing works
Hou, W., Tian, Q., Steuerwald, N., Schrum, L. W., & Bonkovsky, H. L. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.06.001 · Cited by 103 · see citing works
Is solubility in vitro a reliable predictor of iron bioavailability?
Miller, D. D., & Berner, L. A. (1989) · Biological Trace Element Research · doi:10.1007/bf02925446 · Cited by 103 · see citing works
Ferritin L and H Subunits Are Differentially Regulated on a Post-transcriptional Level
Sammarco, M. C., Ditch, S., Banerjee, A., & Grabczyk, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703456200 · Cited by 102 · see citing works
Iron storage disease: Facts, fiction and progress
Beutler, E. (2007) · Blood Cells, Molecules, and Diseases · doi:10.1016/j.bcmd.2007.03.009 · Cited by 101 · see citing works
Iron regulatory proteins control a mucosal block to intestinal iron absorption
Galy, B., Ferring-Appel, D., Becker, C., Gretz, N., Gröne, H.-J., Schümann, K., & Hentze, M. W. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.026 · Cited by 98 · see citing works
Disturbance of plasma and platelet thrombospondin levels in sickle cell disease
Browne, P., Mosher, D. F., Steinberg, M. H., & Hebbel, R. P. (1996) · American Journal of Hematology · doi:10.1002/(sici)1096-8652(199604)51:4 · Cited by 97 · see citing works
Lin, L., Nemeth, E., Goodnough, J. B., Thapa, D. R., Gabayan, V. R., & Ganz, T. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.06.023 · Cited by 95 · see citing works
Intestinal Iron Absorption: Regulation by Dietary & Systemic Factors
Sharp, P. (2010) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831/a000029 · Cited by 95 · see citing works
Processing of microRNA primary transcripts requires heme in mammalian cells
Weitz, S. H., Gong, M., Barr, I., Weiss, S., & Guo, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309915111 · Cited by 91 · see citing works
Andolfo, I., Falco, L. D., Asci, R., Russo, R., Colucci, S., Gorrese, M., Zollo, M., & Iolascon, A. (2010) · Haematologica · doi:10.3324/haematol.2009.020685 · Cited by 90 · see citing works
Joshi, H. P., Subramanian, I. V., Schnettler, E. K., Ghosh, G., Rupaimoole, R., Evans, C., Saluja, M., Jing, Y., Ivan, C., Roy, S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317242111 · Cited by 87 · see citing works
Micromanaging Iron Homeostasis
Yoshioka, Y., Kosaka, N., Ochiya, T., & Kato, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.356717 · Cited by 86 · see citing works
Larson, J. A., Howie, H. L., & So, M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04169.x · Cited by 85 · see citing works
Oxidation-induced ferritin turnover in microglial cells: role of proteasome
Mehlhase, J., Sandig, G., Pantopoulos, K., & Grune, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.025 · Cited by 84 · see citing works
Yeh, K., YEH, M. K. Y., Mims, L., & Glass, J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90298.2008 · Cited by 84 · see citing works
Haem and folate transport by proton-coupled folate transporter/haem carrier protein 1 (SLC46A1)
Laftah, A. H., Latunde-Dada, G. O., Fakih, S., Hider, R. C., Simpson, R. J., & McKie, A. T. (2008) · British Journal Of Nutrition · doi:10.1017/s0007114508066762 · Cited by 84 · see citing works
Guillemot, J., Canuel, M., Essalmani, R., Prat, A., & Seidah, N. G. (2013) · Hepatology · doi:10.1002/hep.26297 · Cited by 83 · see citing works
Zhang, A.-S., Yang, F., Wang, J., Tsukamoto, H., & Enns, C. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.027318 · Cited by 83 · see citing works
Zhang, A., Gao, J., Koeberl, D. D., & Enns, C. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.109488 · Cited by 80 · see citing works
Hepatocyte-targeted HFE and TFR2 control hepcidin expression in mice
Gao, J., Chen, J., Domenico, I. D., Koeller, D. M., Harding, C. O., Fleming, R. E., Koeberl, D. D., & Enns, C. A. (2010) · Blood · doi:10.1182/blood-2009-09-245209 · Cited by 79 · see citing works
Studies on erythropoiesis. VII. The role of the kidney in the production of erythropoietin.
JACOBSON, L. O., Goldwasser, E., Fried, W. I., & Lf, P. (1957) · PubMed · Cited by 76 · see citing works
Roetto, A., Cunto, F. D., Pellegrino, R. M., Hirsch, E., Azzolino, O., Bondi, A., Defilippi, I., Carturan, S., Miniscalco, B., Riondato, F., et al. (2010) · Blood · doi:10.1182/blood-2009-09-240960 · Cited by 74 · see citing works
Enns, C. A., Ahmed, R., Wang, J., Ueno, A., Worthen, C., Tsukamoto, H., & Zhang, A.-S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060534 · Cited by 69 · see citing works
2-Oxoglutarate-dependent oxygenases control hepcidin gene expression
Braliou, G. G., Falzacappa, M. V. V., Chachami, G., Casanovas, G., Muckenthaler, M. U., & Simos, G. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2007.12.021 · Cited by 67 · see citing works
Iron Homeostasis Regulates the Activity of the MicroRNA Pathway through Poly(C)-Binding Protein 2
Li, Y., Lin, L., Li, Z., Ye, X., Xiong, K., Aryal, B., Xu, Z., Paroo, Z., Liu, Q., He, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.021 · Cited by 65 · see citing works
Neogenin Interacts with Matriptase-2 to Facilitate Hemojuvelin Cleavage
Enns, C. A., Ahmed, R., & Zhang, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.363937 · Cited by 64 · see citing works
DeRusso, P. A., Philpott, C. C., Iwaï, K., Mostowski, H. S., Klausner, R. D., & Rouault, T. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.26.15451 · Cited by 64 · see citing works
miR-214 Regulates Lactoferrin Expression and Pro-Apoptotic Function in Mammary Epithelial Cells ,
Liao, Y., Du, X., & Lönnerdal, B. L. (2010) · Journal of Nutrition · doi:10.3945/jn.110.124289 · Cited by 62 · see citing works
Influence of microRNA on the Maintenance of Human Iron Metabolism
Davis, M. R., & Clarke, S. L. (2013) · Nutrients · doi:10.3390/nu5072611 · Cited by 62 · see citing works
A New Case of Human Atransferrinemia with a Previously Undescribed Mutation in the Transferrin Gene
Aslan, D., Crain, K., & Beutler, E. (2007) · Acta Haematologica · doi:10.1159/000112726 · Cited by 51 · see citing works
Rishi, G., Crampton, E. M., Wallace, D. F., & Subramaniam, V. N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077267 · Cited by 49 · see citing works
Growth differentiation factor 15 in patients with congenital dyserythropoietic anaemia (CDA) type II
Casanovas, G., Swinkels, D. W., Altamura, S., Schwarz, K., Laarakkers, C. M., Gross, H.-J., Wiesneth, M., Heimpel, H., & Muckenthaler, M. U. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0751-5 · Cited by 46 · see citing works
Gagliardo, B., Kubat, N. J., Faye, A., Jaouen, M., Durel, B., Deschemin, J., Canonne‐Hergaux, F., Sari, M., & Vaulont, S. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2008.09.018 · Cited by 45 · see citing works
Lawless, M. W., Mankan, A. K., White, M., O’Dwyer, M. J., & Norris, S. (2007) · BMC Cell Biology · doi:10.1186/1471-2121-8-30 · Cited by 44 · see citing works
Evidence that iron stores regulate iron absorption— a setpoint theory
Gavin, M. W., McCarthy, D., & Garry, P. (1994) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/59.6.1376 · Cited by 43 · see citing works
Zumbrennen‐Bullough, K. B., Wu, Q., Core, A. B., Canali, S., Chen, W., Theurl, I., Meynard, D., & Babitt, J. L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.577387 · Cited by 43 · see citing works
Inamura, K., Matsuzaki, Y., Uematsu, N., Honda, A., Tanaka, N., & Uchida, K. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.06.003 · Cited by 41 · see citing works
Liao, Y., & Lönnerdal, B. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.07.019 · Cited by 40 · see citing works
Ferroportin1: a new iron export molecule?
Le, N. T. V., & Richardson, D. R. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00104-2 · Cited by 37 · see citing works
Patel, N., Varghese, J., Masaratana, P., Latunde-Dada, G. O., Jacob, M., Simpson, R. J., & McKie, A. T. (2013) · British Journal of Haematology · doi:10.1111/bjh.12649 · Cited by 36 · see citing works
Processing of hemojuvelin requires retrograde trafficking to the Golgi in HepG2 cells
Maxson, J. E., Enns, C. A., & Zhang, A. (2008) · Blood · doi:10.1182/blood-2008-08-174565 · Cited by 35 · see citing works
Asci, R., Vallefuoco, F., Andolfo, I., Bruno, M., Falco, L. D., & Iolascon, A. (2013) · Neuroscience Research · doi:10.1016/j.neures.2013.09.003 · Cited by 31 · see citing works
Ferritin as an Iron Concentrator and Chelator Target
Liu, X., & Theil, E. C. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1345.016 · Cited by 31 · see citing works
Brown, P. J., & Johnson, P. M. (1981) · Placenta · doi:10.1016/s0143-4004(81)80034-3 · Cited by 29 · see citing works
Shpyleva, S., Pogribna, M., Cozart, C. R., Bryant, M., Muskhelishvili, L., Tryndyak, V., Ross, S. A., Beland, F. A., & Pogribny, I. P. (2014) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2014.06.012 · Cited by 24 · see citing works
Relation of ferroxidase (ceruloplasmin) to iron absorption.
Brittin, G. M., & Chee, Q. T. (1969) · PubMed · Cited by 24 · see citing works
Differential HFE Gene Expression Is Regulated by Alternative Splicing in Human Tissues
Martins, R., Silva, B. D. R., Proença, D., & Faustino, P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017542 · Cited by 21 · see citing works
Self-citationTransferrin and Cellular Iron Exchange
Young, S. P., & Bomford, A. B. (1984) · Clinical Science · doi:10.1042/cs0670273 · Cited by 21 · see citing works
Sánchez, M., Bruguera, M., Rodés, J., & Oliva, R. (2001) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2000.0346 · Cited by 20 · see citing works
Martins, R., Proença, D., Silva, B. D. R., Barbosa, C., Silva, A. L., Faustino, P., & Romão, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035461 · Cited by 19 · see citing works
Self-citationProtective role of calreticulin in HFE hemochromatosis
Pinto, J. P., Ramos, P., de Almeida, S. F., Oliveira, S. J., Breda, L., Michalak, M., Porto, G., Rivella, S., & de Sousa, M. A. B. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.014 · Cited by 18 · see citing works
The hereditary hyperferritinemia–cataract syndrome: a family study
Alvarez-Coca, J., Moreno‐Carralero, M., Martínez-Pérez, J., Méndez, M., García-Ros, M., & Morán‐Jiménez, M. (2010) · European Journal of Pediatrics · doi:10.1007/s00431-010-1251-2 · Cited by 14 · see citing works
Oxygen Sensing Heme Proteins: Monoxygenases, Myoglobin and Hemoglobin
GUNSALUS, I. C., Sligar, S. G., Nordlund, T. M., & Frauenfelder, H. (1977) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-9035-4_3 · Cited by 10 · see citing works
Silva, B. D. R., Ferreira, J. T., Santos, V., Baldaia, C., Serejo, F., & Faustino, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.07.017 · Cited by 4 · see citing works
Self-citation
Flagged first, then by citations
1 of the 193 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
The interaction between ferroptosis and inflammatory signaling pathways
Chen, Y., Fang, Z., Yi, X., Wei, X., & Jiang, D. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05716-0 · Cited by 589 · see citing works
Iron and cancer: recent insights
Manz, D. H., Blanchette, N. L., Paul, B. T., Torti, F. M., & Torti, S. V. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13008 · Cited by 507 · see citing works
Advances in pathogenesis and therapeutic strategies for osteoporosis
Song, S., Guo, Y., Yang, Y., & Fu, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108168 · Cited by 476 · see citing works
On Iron Metabolism and Its Regulation
Vogt, A. S., Arsiwala, T., Mohsen, M. O., Vogel, M., Manolova, V., & Bachmann, M. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094591 · Cited by 473 · see citing works
Eid, R., Arab, N. T. T., & Greenwood, M. T. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.12.002 · Cited by 286 · see citing works
The vicious cycle of vitamin a deficiency: A review
Wiseman, E., Barel-Dadon, S., & Reifen, R. (2017) · Critical reviews in food science and nutrition · doi:10.1080/10408398.2016.1160362 · Cited by 215 · see citing works
Effectiveness of probiotics, prebiotics, and prebiotic‐like components in common functional foods
Peng, M., Tabashsum, Z., Anderson, M., Truong, A., Houser, A., Padilla, J., Akmel, A., Bhatti, J., Rahaman, S. O., & Biswas, D. (2020) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12565 · Cited by 258 · see citing works
A Short Review of Iron Metabolism and Pathophysiology of Iron Disorders
Yiannikourides, A., & Latunde-Dada, G. O. (2019) · Medicines · doi:10.3390/medicines6030085 · Cited by 265 · see citing works
Possible Side Effects of Polyphenols and Their Interactions with Medicines
Duda‐Chodak, A., & Tarko, T. (2023) · Molecules · doi:10.3390/molecules28062536 · Cited by 244 · see citing works
Iron Metabolism in Obesity and Metabolic Syndrome
González-Domínguez, Á., Visiedo-García, F. M., Domínguez-Riscart, J., González-Domínguez, R., Mateos, R. M., & Lechuga-Sancho, A. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155529 · Cited by 227 · see citing works
Pajarillo, E. A. B., Lee, E.-S., & Kang, D. (2021) · Animal nutrition · doi:10.1016/j.aninu.2021.03.005 · Cited by 227 · see citing works
New Insights into the Role of Ferritin in Iron Homeostasis and Neurodegenerative Diseases
Zhang, N., Yu, X., Xie, J., & Xu, H. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02277-7 · Cited by 218 · see citing works
Criteria for Iron Deficiency in Patients With Heart Failure
Masini, G., Graham, F. J., Pellicori, P., Cleland, J. G. F., Cuthbert, J. J., Kazmi, S., Inciardi, R. M., & Clark, A. L. (2022) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2021.11.039 · Cited by 193 · see citing works
Molecular Mechanisms of Ferroptosis and Relevance to Cardiovascular Disease
Xie, L., Fefelova, N., Pamarthi, S. H., & Gwathmey, J. K. (2022) · Cells · doi:10.3390/cells11172726 · Cited by 191 · see citing works
Hudak, L., Jaraisy, A., Haj, S., & Muhsen, K. (2016) · Helicobacter · doi:10.1111/hel.12330 · Cited by 184 · see citing works
Association between the gut microbiota and mineral metabolism
Skrypnik, K., & Suliburska, J. (2017) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.8724 · Cited by 182 · see citing works
Iron bioavailability from food fortification to precision nutrition. A review
Blanco-Rojo, R., & Vaquero, M. P. (2018) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2018.04.015 · Cited by 181 · see citing works
Zhao, T., Guo, X., & Sun, Y. (2021) · Aging and Disease · doi:10.14336/ad.2020.0912 · Cited by 176 · see citing works
A promising new approach to cancer therapy: Targeting iron metabolism in cancer stem cells
El-Hout, M., Santos, L. D., Hamaï, A., & Mehrpour, M. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.07.009 · Cited by 170 · see citing works
Smith, E. M., & Tangpricha, V. (2015) · Current Opinion in Endocrinology Diabetes and Obesity · doi:10.1097/med.0000000000000199 · Cited by 158 · 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
Morris, G., Berk, M., Carvalho, A. F., Maes, M. H. J., Walker, A. J., & Puri, B. K. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.12.036 · Cited by 154 · see citing works
Environmental Enteropathy: Elusive but Significant Subclinical Abnormalities in Developing Countries
Watanabe, K., & Petri, W. A. (2016) · EBioMedicine · doi:10.1016/j.ebiom.2016.07.030 · Cited by 139 · see citing works
Iron and restless legs syndrome: treatment, genetics and pathophysiology
Connor, J. R., Patton, S. M., Oexle, K., & Allen, R. P. (2016) · Sleep Medicine · doi:10.1016/j.sleep.2016.07.028 · Cited by 137 · see citing works
Cell Death Pathways: a Novel Therapeutic Approach for Neuroscientists
Morris, G., Walker, A. J., Berk, M., Maes, M. H. J., & Puri, B. K. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0793-y · Cited by 129 · see citing works
Kalinowski, D. S., Stefani, C., Toyokuni, S., Ganz, T., Anderson, G. J., Subramaniam, V. N., Trinder, D., Olynyk, J. K., Chua, A. C. G., Jansson, P. J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.026 · Cited by 129 · see citing works
Advanced approaches for improving bioavailability and controlled release of anthocyanins
Shen, Y., Zhang, N., Tian, J., Xin, G., Liu, L., Sun, X., & Li, B. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.11.031 · Cited by 122 · see citing works
Wu, W., Yang, Y., Sun, N., Bao, Z., & Lin, S. (2020) · Food Research International · doi:10.1016/j.foodres.2020.108976 · Cited by 105 · see citing works
Ferroptosis and Its Multifaceted Roles in Cerebral Stroke
Zhang, Y., Lu, X., Tai, B., Li, W., & Li, T. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.615372 · Cited by 108 · see citing works
Lovett, B., & Leger, R. J. S. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.funk-0001-2016 · Cited by 105 · see citing works
Iron and Neurodegeneration: Is Ferritinophagy the Link?
Biasiotto, G., Lorenzo, D. D., Archetti, S., & Zanella, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9473-y · Cited by 104 · see citing works
Ferritinophagy drives uropathogenic<i>Escherichia coli</i>persistence in bladder epithelial cells
Bauckman, K. A., & Mysorekar, I. U. (2016) · Autophagy · doi:10.1080/15548627.2016.1160176 · Cited by 100 · see citing works
Iron homeostasis imbalance and ferroptosis in brain diseases
Long, H., Zhu, W., Wei, L., & Zhao, J. (2023) · MedComm · doi:10.1002/mco2.298 · Cited by 104 · see citing works
Iron Metabolism, Calcium, Magnesium and Trace Elements: A Review
Rolić, T., Yazdani, M., Mandić, S., & Distante, S. (2024) · Biological Trace Element Research · doi:10.1007/s12011-024-04289-z · Cited by 102 · see citing works
Jing, X., Lin, J., Du, T., Jiang, Z., Li, T., Wang, G., Liu, X., Cui, X., & Sun, K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.594509 · Cited by 101 · see citing works
González, A., Gálvez, N., Martín, J., Reyes, F., Pérez-Victoria, I., & Dominguez-Vera, J. M. (2017) · Food Chemistry · doi:10.1016/j.foodchem.2017.02.008 · Cited by 100 · see citing works
Excess iron: considerations related to development and early growth
Wessling‐Resnick, M. (2017) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.155879 · Cited by 100 · see citing works
Quercetin attenuates neurotoxicity induced by iron oxide nanoparticles
Bardestani, A., Ebrahimpour, S., Esmaeili, A., & Esmaeili, A. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-021-01059-0 · Cited by 105 · see citing works
Highly biodegradable and bioactive Fe-Pd-bredigite biocomposites prepared by selective laser melting
Gao, C., Meng, Y., Li, S., Feng, P., Peng, S., & Shuai, C. (2019) · Journal of Advanced Research · doi:10.1016/j.jare.2019.06.001 · Cited by 97 · see citing works
Ferroptosis in life: To be or not to be
Xu, L., Liu, Y., Chen, X., Zhong, H., & Wang, Y. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114241 · Cited by 98 · see citing works
Ferroptosis: Biological Rust of Lipid Membranes
Hassannia, B., Coillie, S. V., & Berghe, T. V. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8175 · Cited by 92 · see citing works
Toxic and essential metals: metabolic interactions with the gut microbiota and health implications
Zhu, Q., Chen, B., Zhang, F., Zhang, B., Guo, Y., Pang, M., Huang, L., & Wang, T. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1448388 · Cited by 100 · see citing works
Jing, X., Du, T., Li, T., Yang, X., Wang, G., Liu, X., Jiang, Z., & Cui, X. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16581 · Cited by 92 · see citing works
Iron in Health and Disease: An Update
Lal, A. (2019) · The Indian Journal of Pediatrics · doi:10.1007/s12098-019-03054-8 · Cited by 92 · see citing works
Valent, P., Büsche, G., Theurl, I., Uras, I. Z., Germing, U., Stauder, R., Sotlar, K., Füreder, W., Bettelheim, P., Pfeilstöcker, M., et al. (2018) · Haematologica · doi:10.3324/haematol.2018.192518 · Cited by 86 · see citing works
Could Alzheimer’s Disease Originate in the Periphery and If So How So?
Morris, G., Berk, M., Maes, M. H. J., & Puri, B. K. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1092-y · Cited by 83 · see citing works
Iron and zinc exploitation during bacterial pathogenesis
Ma, L. M., Terwilliger, A. L., & Maresso, A. W. (2015) · Metallomics · doi:10.1039/c5mt00170f · Cited by 83 · 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
Iron, Oxidative Stress, and Metabolic Dysfunction—Associated Steatotic Liver Disease
Gensluckner, S., Wernly, B., Datz, C., & Aigner, E. S. (2024) · Antioxidants · doi:10.3390/antiox13020208 · Cited by 81 · see citing works
Bruzzese, A., Martino, E. A., Mendicino, F., Lucia, E., Olivito, V., Bova, C., Filippelli, G., Capodanno, I., Neri, A., Morabito, F., et al. (2023) · European Journal Of Haematology · doi:10.1111/ejh.13935 · Cited by 76 · see citing works
Conjugated polymer based fluorescent probes for metal ions
Pak, Y. L., Wang, Y., & Xu, Q. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213745 · Cited by 71 · see citing works
D-Glyceraldehyde-3-Phosphate Dehydrogenase Structure and Function
White, M. R., & Garcin, E. D. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-46503-6_15 · Cited by 71 · see citing works
Molecular Genetics of Secondary Chemistry in Metarhizium Fungi
Donzelli, B. G. G., & Krasnoff, S. B. (2016) · Advances in genetics · doi:10.1016/bs.adgen.2016.01.005 · Cited by 66 · see citing works
Zayed, M. F., Eisa, W. H., El-Kousy, S. M., Mleha, W. K., & Kamal, N. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.02.042 · Cited by 65 · 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
A Review of the Role of Curcumin in Metal Induced Toxicity
Smirnova, E., Moniruzzaman, M., Chin, S., Sureshbabu, A., Karthikeyan, A., Do, K., & Min, T. (2023) · Antioxidants · doi:10.3390/antiox12020243 · Cited by 64 · see citing works
The Effect of Multispecies Probiotic Supplementation on Iron Status in Rats
Skrypnik, K., Bogdański, P., SCHMIDT, M. T., & Suliburska, J. (2019) · Biological Trace Element Research · doi:10.1007/s12011-019-1658-1 · Cited by 62 · see citing works
Relationship between Hepatitis C Virus Infection and Iron Overload
Zou, D., & Sun, W. (2017) · Chinese Medical Journal · doi:10.4103/0366-6999.202737 · Cited by 60 · see citing works
Linking Cancer Metabolic Dysfunction and Genetic Instability through the Lens of Iron Metabolism
Petronek, M. S., Spitz, D. R., Buettner, G. R., & Allen, B. G. (2019) · Cancers · doi:10.3390/cancers11081077 · Cited by 61 · see citing works
Factors Affecting Gut Microbiome in Daily Diet
Su, Q., & Liu, Q. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.644138 · Cited by 60 · see citing works
Cellular sensing and transport of metal ions: implications in micronutrient homeostasis
Bird, A. J. (2015) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2015.08.002 · Cited by 58 · see citing works
Tarifeño-Saldivia, E., Aguilar, A., Contreras, D., Mercado, L. A., Lange, B. M., Márquez, K., Henríquez, A., Riquelme-Vidal, C., & Boltaña, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01296 · Cited by 58 · see citing works
Frataxin and the molecular mechanism of mitochondrial iron-loading in Friedreich's ataxia
Chiang, S., Kovačević, Ž., Sahni, S., Lane, D. J. R., Merlot, A. M., Kalinowski, D. S., Huang, M. L. H., & Richardson, D. R. (2016) · Clinical Science · doi:10.1042/cs20160072 · Cited by 58 · see citing works
Corte‐Rodríguez, M., Blanco‐González, E., Bettmer, J., & Montes‐Bayón, M. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b03438 · Cited by 58 · see citing works
Rosito, M., Testi, C., Parisi, G., Cortese, B., Baiocco, P., & Angelantonio, S. D. (2020) · Antioxidants · doi:10.3390/antiox9080700 · Cited by 58 · see citing works
Proprotein convertases: Key players in inflammation-related malignancies and metastasis
Siegfried, G., Descarpentrie, J., Évrard, S., & Khatib, A. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.12.027 · Cited by 55 · see citing works
Regulation of Ferroptosis Pathway by Ubiquitination
Wang, X., Wang, Y., Li, Z., Qin, J., & Wang, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.699304 · Cited by 54 · see citing works
Iron and inflammation – the gut reaction
Verma, S., & Cherayil, B. J. (2017) · Metallomics · doi:10.1039/c6mt00282j · Cited by 50 · see citing works
Iron Pathways and Iron Chelation Approaches in Viral, Microbial, and Fungal Infections
Chhabra, R., Saha, A., Chamani, A., Schneider, N., Shah, R., & Nanjundan, M. (2020) · Pharmaceuticals · doi:10.3390/ph13100275 · Cited by 51 · see citing works
He, H., Yang, Q., Zhang, Z., Wu, Z., Liu, D., Liao, Z., Yin, D., & He, M. L. (2018) · Food & Function · doi:10.1039/c7fo02057k · Cited by 47 · see citing works
Nascimento, C. S., Alves, É. A. R., de Melo, C. P., Corrêa‐Oliveira, R., & Calzavara-Silva, C. E. (2021) · Nanomedicine · doi:10.2217/nnm-2021-0255 · Cited by 46 · see citing works
bu, X., & Wang, L. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5480 · Cited by 49 · see citing works
Rushdi, M. I., Basak, R., Das, P., Ahamed, T., & Bhattacharjee, S. (2023) · Journal of Hazardous Materials Advances · doi:10.1016/j.hazadv.2023.100287 · Cited by 44 · see citing works
Simão, M., Gavaia, P. J., Camacho, A. B., Porto, G., Pinto, I., Ea, H., & Cancela, M. L. (2019) · BioFactors · doi:10.1002/biof.1520 · Cited by 44 · see citing works
Endocrine effects of duodenal–jejunal exclusion in obese patients with type 2 diabetes mellitus
Kaválková, P., Mráz, M., Trachta, P., Kloučková, J., Cinkajzlová, A., Lacinová, Z., Haluzíková, D., Beneš, M., Vlasáková, Z., Burda, V., et al. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0206 · Cited by 41 · see citing works
Moksnes, M. R., Graham, S. E., Wu, K.-H., Hansen, A. F., Taliun, S. A. G., Zhou, W., Thorstensen, K., Fritsche, L. G., Gill, D., Mason, A. M., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03529-z · Cited by 40 · see citing works
Ferroptosis—A Novel Mechanism With Multifaceted Actions on Stroke
Fang, X., Ding, S.-Y., Du, X., Wang, J.-H., & Li, X. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.881809 · Cited by 40 · see citing works
Mekonnen, Y. A., Gültas, M., Effa, K., Hanotte, O., & Schmitt, A. O. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.01095 · Cited by 37 · see citing works
“…to overcome the shortage of oxygen, stressassociated, HIF, and NRF2 related pathways play a critical role in the production of red blood cells in which hemoglobin acts as oxygen repository for red blood cells and other cells (Chan et al., 2001; Sangokoya et al., 2010; Silva and Faustino, 2015).”
BackgroundIron Deficiency and Anemia 10 Years After Roux-en-Y Gastric Bypass for Severe Obesity
Sandvik, J., Bjerkan, K. K., Græslie, H., Hoff, D. A. L., Johnsen, G., Klöckner, C. A., Mårvik, R., Nymo, S., Hyldmo, Å. A., & Kulseng, B. E. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.679066 · Cited by 37 · see citing works
Modulating Iron for Metabolic Support of TB Host Defense
Phelan, J. J., Basdeo, S. A., Tazoll, S. C., McGivern, S., Saborido, J. R., & Keane, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02296 · Cited by 37 · see citing works
Valenzuela‐Muñoz, V., Valenzuela‐Miranda, D., Gonçalves, A. T., Novoa, B., Figueras, A. J., & Gallardo‐Escárate, C. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735058 · Cited by 36 · see citing works
Fefelova, N., Wongjaikam, S., Pamarthi, S. H., Siri‐Angkul, N., Comollo, T. W., Kumari, A., Garg, V., Ivessa, A., Chattipakorn, S. C., Chattipakorn, N., et al. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-00990-7 · Cited by 35 · see citing works
Lombardi, G., Perego, S., Sansoni, V., & Banfi, G. (2016) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2016.09.017 · Cited by 34 · see citing works
Unraveling the interplay between iron homeostasis, ferroptosis and extramedullary hematopoiesis
Fernández-García, V., González-Ramos, S., Martín‐Sanz, P., Castrillo, A., & Boscá, L. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106386 · Cited by 34 · see citing works
The role of iron in pulmonary pathology
Khiroya, H., & Turner, A. M. (2015) · Multidisciplinary Respiratory Medicine · doi:10.1186/s40248-015-0031-2 · Cited by 35 · see citing works
Wang, Z., Li, J., Benin, B. M., Yu, B., Bunge, S. D., Abeydeera, N., Huang, S. D., & Kim, M. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00656 · Cited by 33 · see citing works
Iron, Heme Synthesis and Erythropoietic Porphyrias: A Complex Interplay
Poli, A., Schmitt, C., Moulouel, B., Mirmiran, A., Puy, H., Lefèbvre, T., & Gouya, L. (2021) · Metabolites · doi:10.3390/metabo11120798 · Cited by 33 · see citing works
Understanding the Intricacies of Iron Overload Associated with β-Thalassemia: A Comprehensive Review
Basu, S., Rahaman, M., Dolai, T. K., Shukla, P. C., & Chakravorty, N. (2023) · Thalassemia Reports · doi:10.3390/thalassrep13030017 · Cited by 31 · see citing works
Low Serum Hepcidin in Patients with Autoimmune Liver Diseases
Lyberopoulou, A., Chachami, G., Gatselis, N., Kyratzopoulou, E., Saitis, A., Gabeta, S., Eliades, P., Paraskeva, E., Zachou, K., Koukoulis, G. Κ., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135486 · Cited by 32 · see citing works
Iron accumulation and lipid peroxidation: implication of ferroptosis in diabetic cardiomyopathy
Yan, X., Xie, Y., Liu, H., Huang, M., Yang, Z., Dong-qing, A., & Jiang, G. (2023) · Diabetology & Metabolic Syndrome · doi:10.1186/s13098-023-01135-5 · Cited by 32 · see citing works
Dietary sources of iron and vitamin B12: Is this the missing link in colorectal carcinogenesis?
Banjari, I., & Hjartåker, A. (2018) · Medical Hypotheses · doi:10.1016/j.mehy.2018.05.003 · Cited by 30 · see citing works
Increased DMT1 and FPN1 expression with enhanced iron absorption in ulcerative colitis human colon
Minor, E. A., Kupec, J. T., Nickerson, A. J., Narayanan, K., & Rajendran, V. M. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00128.2019 · Cited by 29 · see citing works
Evliyaoğlu, E., Kilercioğlu, S., Yılmaz, H. A., Turchini, G. M., Paolucci, M., Clark, T. D., Demirkale, İ., & Eroldoğan, O. T. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2021.737884 · Cited by 30 · see citing works
Raffield, L. M., Louie, T., Sofer, T., Jain, D., Ipp, E., Taylor, K. D., Papanicolaou, G., Avilés-Santa, L. M., Lange, L. A., Laurie, C. C., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx082 · Cited by 31 · see citing works
Angelucci, E., Cianciulli, P., Finelli, C., Mecucci, C., Voso, M. T., & Tura, S. (2017) · Leukemia Research · doi:10.1016/j.leukres.2017.10.001 · Cited by 28 · see citing works
Huang, C., Ma, W., Luo, Q., Shi, L., Xia, Y., Lao, C., Liu, W., Zou, Y., Cheng, A., Shi, R., et al. (2019) · Aging · doi:10.18632/aging.102433 · Cited by 27 · see citing works
Ojha, N. K., & Lole, K. S. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2715-0 · Cited by 27 · see citing works
Dong, W., Tan, Y., Qi, Q., Yang, B. V., Zhu, Q., Xu, L., Liu, Z., Song, E., & Song, Y. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00350 · Cited by 27 · see citing works
KCa(H2O)2[FeIII(CN)6]⋅H2O Nanoparticles as an Antimicrobial Agent against Staphylococcus aureus
Wang, Z., Yu, B., Alamri, H. M., Yarabarla, S., Kim, M., & Huang, S. D. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201713177 · Cited by 27 · see citing works
- Authors
- Silva, B., & Faustino, P.
- Affiliations
- National Institute of Health Dr. Ricardo Jorge (PT)
- Corresponding author
- Faustino, Paula
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 1852
- Issue
- 7
- Pages
- 1347-1359
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2076768785
- Cited by
- 300
- References
- 193
- Citations by year
- 2026: 17 · 2025: 24 · 2024: 27 · 2023: 40 · 2022: 25 · 2021: 31 · 2020: 24 · 2019: 30 · 2018: 23 · 2017: 21 · 2016: 28 · 2015: 9 · 2012: 1
- FWCI
- 4.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion)
- Funders
- Fundação para a Ciência e a Tecnologia
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- iron metabolism, iron homeostasis, hepcidin, iron absorption, enterocytes, inflammation, anemia, erythropoiesis, post-transcriptional regulation, alternative splicing, microRNA, proteolytic cleavage
- MeSH terms
- Animals, Humans, Iron, Iron Metabolism Disorders, Iron-Binding Proteins, Iron-Regulatory Proteins
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