The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Iron Homeostasis
Abstract
Iron is needed by all mammalian cells but is toxic in excess. Specialized transport mechanisms conduct iron across cellular membranes. These are regulated to ensure homeostasis both systemically in living organisms and within individual cells. Over the past decade, major advances have been made in identifying and characterizing the proteins involved in the transport, handling, and homeostatic regulation of iron. Molecular understanding of these processes has provided important insights into the pathophysiology of human iron disorders.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
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
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
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
Iron, brain ageing and neurodegenerative disorders
Zecca, L., Youdim, M. B. H., Riederer, P., Connor, J. R., & Crichton, R. R. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1537 · Cited by 1,801
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
Self-citationPigeon, C., Ilyin, G., Courselaud, B., Leroyer, P., Turlin, B., Brissot, P., & Loréal, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008923200 · Cited by 1,697
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
Self-citationMcKie, 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
Research works printed but not linked: 70
- 10.1182/blood-2005-02-0716 · DOI · Paper page
- 10.1182/blood-2006-02-003681 · DOI · Paper page
- 10.1172/JCI200524356 · DOI · Paper page
- 10.1073/pnas.95.3.1148 · DOI · Paper page
- 10.1371/journal.pbio.0020050 · DOI
- 10.1182/blood-2005-10-4269 · DOI
- 10.1182/blood-2005-06-2477 · DOI
- 10.1182/blood-2004-07-2966 · DOI
- 10.1038/5979 · DOI · Paper page
- 10.1016/j.cmet.2005.10.003 · DOI
- 10.1182/blood.V61.4.799.799 · DOI
- 10.1056/NEJM198407263110402 · DOI
- Bernstein SE, 1987, J. Lab. Clin. Med., 110, 690
- 10.1182/blood.V96.3.1113 · DOI
- 10.1007/s100380200049 · DOI
- 10.1182/blood.V96.13.4071 · DOI
- 10.1016/0006-8993(94)91436-2 · DOI
- 10.1182/blood.V89.1.1 · DOI · Paper page
- 10.1016/j.cell.2004.08.014 · DOI · Paper page
- 10.1073/pnas.80.11.3494 · DOI · Paper page
- Neckers LM, 1984, J. Immunol., 133, 2437, 10.4049/jimmunol.133.5.2437 · DOI
- 10.4049/jimmunol.172.11.6709 · DOI · Paper page
- 10.1097/00007890-199801150-00003 · DOI
- 10.1038/nature03104 · DOI · Paper page
- 10.1016/S0896-6273(03)00126-0 · DOI · Paper page
- 10.1002/jcp.20095 · DOI
- 10.1042/BJ20031187 · DOI
- 10.1074/jbc.M005435200 · DOI
- Barisani D, 1995, Am. J. Physiol., 269, G570
- Randell EW, 1994, J. Biolog. Chem., 269, 16046, 10.1016/S0021-9258(17)33971-6 · DOI
- 10.1152/ajpgi.2000.279.6.G1265 · DOI
- 10.1182/blood-2002-07-2108 · DOI
- 10.1093/jn/133.5.1549S · DOI
- 10.1182/blood-2002-07-2006 · DOI
- 10.1016/0092-8674(91)90312-M · DOI · Paper page
- 10.1073/pnas.88.22.10109 · DOI
- 10.1073/pnas.95.9.4924 · DOI · Paper page
- 10.1196/annals.1306.001 · DOI · Paper page
- 10.1038/sj.emboj.7600041 · DOI · Paper page
- 10.1038/84859 · DOI · Paper page
- 10.1038/ng0906-967 · DOI
- 10.1126/science.1103786 · DOI
- 10.1086/321261 · DOI · Paper page
- 10.1111/j.1747-0285.2006.00328.x · DOI
- 10.1182/blood-2005-06-2259 · DOI · Paper page
- 10.1182/blood-2003-07-2524 · DOI · Paper page
- 10.1073/pnas.072632499 · DOI · Paper page
- 10.1182/blood-2004-12-4608 · DOI
- 10.1182/blood-2002-04-1260 · DOI · Paper page
- 10.1016/j.cmet.2005.10.010 · DOI · Paper page
- 10.1523/JNEUROSCI.4610-03.2004 · DOI
- 10.1182/blood-2002-04-1169 · DOI · Paper page
- 10.1038/35042073 · DOI · Paper page
- 10.1038/90038 · DOI · Paper page
- De Domenico I, 2006, Haematologica, 91, 92
- 10.1182/blood.V74.2.844.844 · DOI
- 10.1182/blood-2002-11-3453 · DOI
- 10.1182/blood-2003-01-0040 · DOI
- 10.1136/gut.52.4.610-a · DOI
- 10.1182/blood-2002-12-3926 · DOI
- 10.1016/S0140-6736(03)12602-5 · DOI · Paper page
- 10.1182/blood-2004-08-3042 · DOI · Paper page
- 10.1016/S0092-8674(00)81151-4 · DOI · Paper page
- 10.1086/515466 · DOI
- 10.1182/blood.V94.1.9.413a43_9_11 · DOI · Paper page
- 10.1182/blood.V96.13.4020 · DOI
- 10.1074/jbc.274.30.20826 · DOI · Paper page
- 10.1182/blood-2004-06-2481 · DOI
- 10.1182/blood-2004-06-2477 · DOI
- 10.1093/ajcn/67.5.972S · DOI · Paper page
Cited by
Glutaminolysis and transferrin regulate ferroptosis
Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069
Ferroptosis is an autophagic cell death process
Gao, M., Monian, P., Pan, Q., Zhang, W., Xiang, J., & Jiang, X. (2016) · Cell Research · doi:10.1038/cr.2016.95 · Cited by 1,899
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
Ferroptosis: Mechanisms and links with diseases
Yan, H.-F., Zou, T., Tuo, Q.-Z., Xu, S., Li, H., Belaidi, A. A., & Lei, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00428-9 · Cited by 1,471
The development of the concept of ferroptosis
Hirschhorn, T., & Stockwell, B. R. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.043 · Cited by 1,052
Probiotic Bacteria Reduce Salmonella Typhimurium Intestinal Colonization by Competing for Iron
Deriu, E., Liu, J. Z., Pezeshki, M., Edwards, R. A., Ochoa, R. J., Contreras, H., Libby, S. J., Fang, F. C., & Raffatellu, M. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.007 · Cited by 550
Copper and iron disorders of the brain
Madsen, E., & Gitlin, J. D. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.30.051606.094232 · Cited by 557
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554
Simcox, J. A., & McClain, D. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.007 · Cited by 545
Viral infection and iron metabolism
Drakesmith, H., & Prentice, A. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1930 · Cited by 469
Heme-mediated SPI-C induction promotes monocyte differentiation into iron-recycling macrophages
Haldar, M., Kohyama, M., So, A. Y.-L., KC, W., Wu, X., Briseño, C. G., Satpathy, A. T., Kretzer, N. M., Arase, H., Rajasekaran, N. S., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.069 · Cited by 431
“6 3 10(11) erythrocytes are recycled by the macrophage-dependent pathway, supplying the vast majority of the daily iron requirement (Andrews and Schmidt, 2007; Ganz, 2012; Pantopoulos et al., 2012; Bratosin et al., 1998).”
InfluentialThe chemistry and biology of ferroptosis
Stockwell, B. R., & Jiang, X. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.013 · Cited by 429
Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects
Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352
Iron metabolism in the anemia of chronic disease
Weiss, G. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.08.006 · Cited by 322
Mechanisms of Brain Iron Transport: Insight into Neurodegeneration and CNS Disorders
Mills, E., Dong, X.-P., Wang, F., & Xu, H. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.09.140 · Cited by 309
The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299
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
Jiao, Y., Wilkinson, J., Di, X., Wang, W., Hatcher, H., Kock, N. D., D'Agostino, R., Knovich, M. A., Torti, F. M., & Torti, S. V. (2009) · Blood · doi:10.1182/blood-2008-05-155952 · Cited by 266
Living with Iron (and Oxygen): Questions and Answers about Iron Homeostasis
Theil, E. C., & Goss, D. J. (2009) · Chemical Reviews · doi:10.1021/cr900052g · Cited by 265
NCOA4 deficiency impairs systemic iron homeostasis
Bellelli, R., Federico, G., Matte’, A., Colecchia, D., Iolascon, A., Chiariello, M., Santoro, M., De Franceschi, L., & Carlomagno, F. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.065 · Cited by 248
Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195
Miao, R., Fang, X., Zhang, Y., Wei, J., Zhang, Y., & Tian, J. (2023) · Cell Death & Disease · doi:10.1038/s41419-023-05708-0 · Cited by 192
Pharmacologic inhibition of hepcidin expression reverses anemia of chronic inflammation in rats
Theurl, I., Schroll, A., Sonnweber, T., Nairz, M., Theurl, M., Willenbacher, W., Eller, K., Wolf, D., Seifert, M., Sun, C. C., et al. (2011) · Blood · doi:10.1182/blood-2011-03-345066 · Cited by 189
Iron and Immunity: Immunological Consequences of Iron Deficiency and Overload
Cherayil, B. J. (2010) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-010-0095-9 · Cited by 170
Selective modulation of TLR4-activated inflammatory responses by altered iron homeostasis in mice
Wang, L., Harrington, L., Trebicka, E., Shi, H. N., Kagan, J. C., Hong, C. C., Lin, H. Y., Babitt, J. L., & Cherayil, B. J. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39939 · Cited by 162
Wang, L., Johnson, E. E., Shi, H. N., Walker, W. A., Wessling-Resnick, M., & Cherayil, B. J. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.4.2723 · Cited by 159
Minding metals: Tailoring multifunctional chelating agents for neurodegenerative disease
Perez, L. R., & Franz, K. J. (2010) · Dalton Trans. · doi:10.1039/b919237a · Cited by 156
Coupling Heme and Iron Metabolism via Ferritin H Chain
Gozzelino, R., & Soares, M. P. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5666 · Cited by 151
Nairz, M., Theurl, I., Schroll, A., Theurl, M., Fritsche, G., Lindner, E., Seifert, M., Crouch, M.-L. V., Hantke, K., Akira, S., et al. (2009) · Blood · doi:10.1182/blood-2009-05-223354 · Cited by 146
Intestinal Ferritin H Is Required for an Accurate Control of Iron Absorption
Vanoaica, L., Darshan, D., Richman, L., Schümann, K., & Kühn, L. C. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.003 · Cited by 137
Tacchini, L., Gammella, E., De Ponti, C., Recalcati, S., & Cairo, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800365200 · Cited by 132
Burden, R. J., Morton, K., Richards, T., Whyte, G. P., & Pedlar, C. R. (2015) · British Journal of Sports Medicine · doi:10.1136/bjsports-2014-093624 · Cited by 125
Iron-regulatory proteins: molecular biology and pathophysiological implications
Cairo, G., & Recalcati, S. (2007) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399407000531 · Cited by 124
Iron and innate antimicrobial immunity-depriving the pathogen, defending the host
Nairz, M., Dichtl, S., Schroll, A., Haschka, D., Tymoszuk, P., Theurl, I., & Weiss, G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.03.007 · Cited by 123
The effect of abnormal iron metabolism on osteoporosis
Che, J., Yang, J., Zhao, B., Zhang, G., Wang, L., Peng, S., & Shang, P. (2020) · Biological Trace Element Research · doi:10.1007/s12011-019-01867-4 · Cited by 113
Local iron homeostasis in the breast ductal carcinoma microenvironment
Marques, O., Porto, G., Rêma, A., Faria, F., Cruz Paula, A., Gomez-Lazaro, M., Silva, P., Martins da Silva, B., & Lopes, C. (2016) · BMC Cancer · doi:10.1186/s12885-016-2228-y · Cited by 90
Zhang, J., Li, X., Olmedo, M., Holdorf, A. D., Shang, Y., Artal-Sanz, M., Yilmaz, L. S., & Walhout, A. J. M. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.07.010 · Cited by 77
Leishmania-Mediated Inhibition of Iron Export Promotes Parasite Replication in Macrophages
Ben-Othman, R., Flannery, A. R., Miguel, D. C., Ward, D. M., Kaplan, J., & Andrews, N. W. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003901 · Cited by 76
Self-citationThompson, J. W., Salahudeen, A. A., Chollangi, S., Ruiz, J. C., Brautigam, C. A., Makris, T. M., Lipscomb, J. D., Tomchick, D. R., & Bruick, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308684 · Cited by 71
Kupffer cells modulate iron homeostasis in mice via regulation of hepcidin expression
Theurl, M., Theurl, I., Hochegger, K., Obrist, P., Subramaniam, N., van Rooijen, N., Schuemann, K., & Weiss, G. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0346-y · Cited by 69
Modulation of iron homeostasis in macrophages by bacterial intracellular pathogens
Pan, X., Tamilselvam, B., Hansen, E. J., & Daefler, S. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-64 · Cited by 69
Role of Ferroportin in Macrophage-Mediated Immunity
Johnson, E. E., Sandgren, A., Cherayil, B. J., Murray, M., & Wessling-Resnick, M. (2010) · Infection and Immunity · doi:10.1128/iai.00498-10 · Cited by 68
Nairz, M., Schroll, A., Haschka, D., Dichtl, S., Sonnweber, T., Theurl, I., Theurl, M., Lindner, E., Demetz, E., Aßhoff, M., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545569 · Cited by 67
The Repair of Skeletal Muscle Requires Iron Recycling through Macrophage Ferroportin
Corna, G., Caserta, I., Monno, A., Apostoli, P., Manfredi, A. A., Camaschella, C., & Rovere-Querini, P. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501417 · Cited by 63
The utility of iron chelators in the management of inflammatory disorders
Lehmann, C., Islam, S., Jarosch, S., Zhou, J., Hoskin, D., Greenshields, A., Al-Banna, N., Sharawy, N., Sczcesniak, A., Kelly, M., et al. (2015) · Mediators of Inflammation · doi:10.1155/2015/516740 · Cited by 54
“Due to their role in iron recycling from erythrocytes, iron loading in macrophages is particularly significant [31].”
BackgroundIron in intracellular infection: to provide or to deprive?
Silva-Gomes, S., Vale-Costa, S., Appelberg, R., & Gomes, M. S. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00096 · Cited by 51
Jian, N., Dowle, M., Horniblow, R. D., Tselepis, C., & Palmer, R. E. (2016) · Nanotechnology · doi:10.1088/0957-4484/27/46/46lt02 · Cited by 50
Weight loss, inflammatory markers, and improvements of iron status in overweight and obese children
Gong, L., Yuan, F., Teng, J., Li, X., Zheng, S., Lin, L., Deng, H., Ma, G., Sun, C., & Li, Y. (2014) · The Journal of Pediatrics · doi:10.1016/j.jpeds.2013.12.004 · Cited by 51
Charkoudian, L. K., Dentchev, T., Lukinova, N., Wolkow, N., Dunaief, J. L., & Franz, K. J. (2008) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2008.08.001 · Cited by 49
Function of the hemochromatosis protein HFE: Lessons from animal models
Pantopoulos, K. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.6893 · Cited by 49
Hsu, J. L., Manouvakhova, O. V., Clemons, K. V., Inayathullah, M., Tu, A. B., Sobel, R. A., Tian, A., Nazik, H., Pothineni, V. R., Pasupneti, S., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aag2616 · Cited by 38
Mineral Micronutrients in Asthma
Zajac, D. (2021) · Nutrients · doi:10.3390/nu13114001 · Cited by 33
Zhang, L., Li, X., Gu, Q., Zhu, Y., Zhao, H., Li, Y., & Zhang, Z. (2011) · Biological Trace Element Research · doi:10.1007/s12011-010-8725-y · Cited by 33
Davies, R., Clothier, B., Robinson, S. W., Edwards, R. E., Greaves, P., Luo, J., Gant, T. W., Chernova, T., & Smith, A. G. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700176r · Cited by 29
In vivo role(s) of the iron regulatory proteins (IRP) 1 and 2 in aseptic local inflammation
Viatte, L., Gröne, H.-J., Hentze, M. W., & Galy, B. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0494-8 · Cited by 11
Metadata
- Authors
- Andrews, N. C., & Schmidt, P. J.
- Venue
- Annual Review of Physiology
- Publisher
- Annual Reviews
- Published
- 2007-03-01
- Volume
- 69
- Issue
- 1
- Pages
- 69-85
- ISSN
- 0066-4278 (ISSN-L)
- 1545-1585
- OpenAlex
- W4213134081
- Cited by
- 642
- References
- 45
- FWCI
- 2.13
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.