In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations
Open accessAbstract
Type IV hemochromatosis is associated with dominant mutations in the SLC40A1 gene encoding ferroportin (FPN). Known as the “ferroportin disease,” this condition is typically characterized by high serum ferritin, reduced transferrin saturation, and macrophage iron loading. Previously FPN expression in vitro has been shown to cause iron deficiency in human cell lines and mediate iron export from Xenopus oocytes. We confirm these findings by showing that expression of human FPN in a human cell line results in an iron deficiency because of a 3-fold increased export of iron. We show that FPN mutations A77D, V162Δ, and G490D that are associated with a typical pattern of disease in vivo cause a loss of iron export function in vitro but do not physically or functionally impede wild-type FPN. These mutants may, therefore, lead to disease by haploinsufficiency. By contrast the variants Y64N, N144D, N144H, Q248H, and C326Y, which can be associated with greater transferrin saturation and more prominent iron deposition in liver parenchyma in vivo, retained iron export function in vitro. Because FPN is a target for negative feedback in iron homeostasis, we postulate that the latter group of mutants may resist inhibition, resulting in a permanently “turned on” iron exporter.
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?
Several hereditary hemochromatosis mutations in FPN directly coordinate Co2+ in the C domain, including C326S/F/Y and H507R.
“Several hereditary hemochromatosis mutations in FPN directly coordinate Co 2+ in the C domain, including C326S/F/Y 13,29-31 and H507R 32 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [30]
The Introduction identifies C326Y as a disease-associated FPN mutation, and the Discussion reports its iron-export function. The paper does not establish that C326Y directly coordinates Co²⁺ in the C domain, and it does not address C326S, C326F, or H507R. (LLM, conf=0.86)
Experimental — accuracy not yet measuredSeveral FPN mutations decrease hepcidin binding to FPN, including N144H/D/T, C326S/F/Y, Y333H, Y501C, D504N and H507R.
“Several FPN mutations decrease hepcidin binding to FPN, including N144H/D/T 34-36 , C326S/F/Y 13,29-31 , Y333H 37 , Y501C 7,38 , D504N 7,39 and H507R 32 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [30]
The Discussion proposes that N144H and N144D might prevent FPN from interacting with hepcidin, but presents this as a possibility, not a measured decrease in binding. The Introduction lists N144T as a disease-associated mutation without linking it to hepcidin binding. In the citing sentence, this source is attached to the N144H/D/T group, not the later mutations. (LLM, conf=0.88)
Experimental — accuracy not yet measuredMutations in SLC40A1 can cause hemochromatosis by rendering the transporter insensitive to hepcidin regulation.
“Finally, mutations in the gene encoding ferroportin (SLC40A1) can cause hemochromatosis by rendering the transporter insensitive to hepcidin regulation.158,162”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [162]
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
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
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
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
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
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
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
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
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
Bridle, K. R., Frazer, D. M., Wilkins, S. J., Dixon, J. L., Purdie, D. M., Crawford, D. H., Subramaniam, V. N., Powell, L. W., Anderson, G. J., & Ramm, G. A. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12602-5 · Cited by 620 · 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
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
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
Cytokine-mediated regulation of iron transport in human monocytic cells
Ludwiczek, S., Aigner, E., Theurl, I., & Weiss, G. (2003) · Blood · doi:10.1182/blood-2002-08-2459 · Cited by 420 · see citing works
Hepcidin is decreased in TFR2 hemochromatosis
Nemeth, E., Roetto, A., Garozzo, G., Ganz, T., & Camaschella, C. (2004) · Blood · doi:10.1182/blood-2004-08-3042 · Cited by 396 · see citing works
Pietrangelo, A. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2003.08.003 · Cited by 380 · see citing works
The discovery of the new haemochromatosis gene
Brissot, P. (2003) · Journal of Hepatology · doi:10.1016/s0168-8278(03)00142-9 · Cited by 313 · see citing works
Hereditary Hemochromatosis in Adults without Pathogenic Mutations in the Hemochromatosis Gene
Pietrangelo, A., Montosi, G., Totaro, A., Garuti, C., Conte, D., Cassanelli, S., Fraquelli, M., Sardini, C., Vasta, F., & Gasparini, P. (1999) · New England Journal of Medicine · doi:10.1056/nejm199909023411003 · Cited by 265 · see citing works
Kawabata, H., Fleming, R. E., Gui, D., Moon, S. Y., Saitoh, T., O’Kelly, J., Umehara, Y., Wano, Y., SAID, J. W., & Koeffler, H. P. (2004) · Blood · doi:10.1182/blood-2004-04-1416 · Cited by 238 · see citing works
Gordeuk, V. R., Caleffi, A., Corradini, E., Ferrara, F., Jones, R. A., Castro, O., Onyekwere, O., Kittles, R., Pignatti, E., Montosi, G., et al. (2003) · Blood Cells, Molecules, and Diseases · doi:10.1016/s1079-9796(03)00164-5 · Cited by 198 · see citing works
Devalia, V., Carter, K., Walker, A. P., Perkins, S. J., Worwood, M., May, A. M., & Dooley, J. S. (2002) · Blood · doi:10.1182/blood-2001-11-0132 · Cited by 188 · see citing works
Novel mutation in ferroportin1 is associated with autosomal dominant hemochromatosis
Wallace, D. F., Pedersen, P. L., Dixon, J. L., Stephenson, P. M., Searle, J. W., Powell, L. W., & Subramaniam, V. N. (2002) · Blood · doi:10.1182/blood.v100.2.692 · Cited by 173 · see citing works
Hetet, G., Devaux, I., Soufir, N., Grandchamp, B., & Beaumont, C. (2003) · Blood · doi:10.1182/blood-2003-02-0439 · Cited by 134 · see citing works
Ferroportin 1 (SCL40A1) variant associated with iron overload in African-Americans
Beutler, E., Barton, J. C., Felitti, V. J., Gelbart, T., West, C., Lee, P. L., Waalen, J., & Vulpe, C. D. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00165-7 · Cited by 129 · see citing works
The hemochromatosis protein HFE inhibits iron export from macrophages
Drakesmith, H., Sweetland, E., Schimanski, L., Edwards, J., Cowley, D., Ashraf, M., Bastin, J., & Townsend, A. R. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242614699 · Cited by 128 · see citing works
Self-citationA valine deletion of ferroportin 1: a common mutation in hemochromatosis type 4?
Roetto, A., Merryweather‐Clarke, A. T., Daraio, F., Livesey, K., Pointon, J. J., Barbabietola, G., Piga, A. G., Mackie, P. H., Robson, K., & Camaschella, C. (2002) · Blood · doi:10.1182/blood-2002-03-0693 · Cited by 102 · see citing works
Self-citationDeaglio, S., Capobianco, A., Calı̀, A., Bellora, F., Alberti, F., Righi, L., Sapino, A., Camaschella, C., & Malavasi, F. (2002) · Blood · doi:10.1182/blood-2002-01-0076 · Cited by 86 · see citing works
The SLC40 basolateral iron transporter family (IREG1/ferroportin/MTP1)
McKie, A. T., & Barlow, D. J. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1102-3 · Cited by 86 · see citing works
Arden, K. E., Wallace, D. F., Dixon, J. L., Summerville, L., Searle, J. W., Anderson, G. J., Ramm, G. A., Powell, L. W., & Subramaniam, V. N. (2003) · Gut · doi:10.1136/gut.52.8.1215 · Cited by 84 · see citing works
Wallace, D. F., Clark, R. M., Harley, H. A. J., & Subramaniam, V. N. (2004) · Journal of Hepatology · doi:10.1016/j.jhep.2003.12.008 · Cited by 83 · see citing works
Novel mutation in ferroportin 1 gene is associated with autosomal dominant iron overload
Jouanolle, A., Douabin-Gicquel, V., Halimi, C., Loréal, O., Fergelot, P., Delacour, T., de Lajarte‐Thirouard, A., Turlin, B., Gall, J. L., Cadet, E., et al. (2003) · Journal of Hepatology · doi:10.1016/s0168-8278(03)00148-x · Cited by 79 · see citing works
Genotypic and phenotypic heterogeneity of African Americans with primary iron overload
Barton, J. C., Acton, R. T., Rivers, C. A., Bertoli, L. F., Gelbart, T., West, C., & Beutler, E. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00166-9 · Cited by 68 · see citing works
Recent advances in understanding haemochromatosis: a transition state
Robson, K., Merryweather-Clarke, A. T., Cadet, E., Viprakasit, V., Zaahl, M. G., Pointon, J. J., Weatherall, D. J., & Rochette, J. (2004) · Journal of Medical Genetics · doi:10.1136/jmg.2004.020644 · Cited by 61 · see citing works
Self-citation(2003) · PubMed · Cited by 59 · see citing works
Ferroportin mutation in autosomal dominant hemochromatosis: loss of function, gain in understanding
Fleming, R. E., & Sly, W. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13739 · Cited by 54 · see citing works
Davies, P. S., & Enns, C. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400537200 · Cited by 47 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [18]18. Njajou OT, Vaessen N, Joosse M, et al. A muta- tion in SLC11A3 is associated with autosomal dominant hemochromatosis. Nat Genet. 2001;28: 213-214.
- [29]29. Pietrangelo A, Montosi G, Totaro A, et al. Heredi- tary hemochromatosis in adults without patho- genic mutations in the hemochromatosis gene. N Engl J Med. 1999;341:725-732.
Cited by
Sorted by citations
Regulation of Iron Metabolism by Hepcidin
Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756 · see citing works
Drakesmith, H., Nemeth, E., & Ganz, T. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.006 · Cited by 638 · see citing works
Self-citationForging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623 · see citing works
Regulation of iron acquisition and storage: consequences for iron-linked disorders
De Domenico, I., McVey Ward, D., & Kaplan, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2295 · Cited by 464 · see citing works
The Molecular Mechanism of Hepcidin-mediated Ferroportin Down-Regulation
De Domenico, I., Ward, D. M., Langelier, C., Vaughn, M. B., Nemeth, E., Sundquist, W. I., Ganz, T., Musci, G., & Kaplan, J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0060 · Cited by 434 · 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
Molecular control of iron transport
Ganz, T. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006070802 · Cited by 353 · see citing works
Aschemeyer, S., Qiao, B., Stefanova, D., Valore, E. V., Sek, A. C., Ruwe, T. A., Vieth, K. R., Jung, G., Casu, C., Rivella, S., et al. (2018) · Blood · doi:10.1182/blood-2017-05-786590 · Cited by 325 · see citing works
Delaby, C., Pilard, N., Gonçalves, A. S., Beaumont, C., & Canonne-Hergaux, F. (2005) · Blood · doi:10.1182/blood-2005-06-2398 · Cited by 283 · see citing works
Autocrine formation of hepcidin induces iron retention in human monocytes
Theurl, I., Theurl, M., Seifert, M., Mair, S., Nairz, M., Rumpold, H., Zoller, H., Bellmann-Weiler, R., Niederegger, H., Talasz, H., et al. (2008) · Blood · doi:10.1182/blood-2007-05-090019 · Cited by 275 · see citing works
Powell, L. W., Seckington, R. C., & Deugnier, Y. (2016) · The Lancet · doi:10.1016/s0140-6736(15)01315-x · Cited by 266 · see citing works
Resistance to hepcidin is conferred by hemochromatosis-associated mutations of ferroportin
Drakesmith, H., Schimanski, L. M., Ormerod, E., Merryweather-Clarke, A. T., Viprakasit, V., Edwards, J. P., Sweetland, E., Bastin, J. M., Cowley, D., Chinthammitr, Y., et al. (2005) · Blood · doi:10.1182/blood-2005-02-0561 · Cited by 264 · see citing works
Self-citationThe molecular basis of ferroportin-linked hemochromatosis
De Domenico, I., Ward, D. M., Nemeth, E., Vaughn, M. B., Musci, G., Ganz, T., & Kaplan, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503804102 · Cited by 230 · see citing works
An essential cell-autonomous role for hepcidin in cardiac iron homeostasis
Lakhal-Littleton, S., Wolna, M., Chung, Y. J., Christian, H. C., Heather, L. C., Brescia, M., Ball, V., Diaz, R., Santos, A., Biggs, D., et al. (2016) · eLife · doi:10.7554/elife.19804 · Cited by 184 · see citing works
Ferroportin disease: pathogenesis, diagnosis and treatment
Pietrangelo, A. (2017) · Haematologica · doi:10.3324/haematol.2017.170720 · Cited by 151 · see citing works
The Iron Efflux Protein Ferroportin Regulates the Intracellular Growth of<i>Salmonella enterica</i>
Chlosta, S., Fishman, D. S., Harrington, L., Johnson, E. E., Knutson, M. D., Wessling-Resnick, M., & Cherayil, B. J. (2006) · Infection and Immunity · doi:10.1128/iai.74.5.3065-3067.2006 · Cited by 145 · see citing works
Ferroportin disease: a systematic meta-analysis of clinical and molecular findings
Mayr, R., Janecke, A. R., Schranz, M., Griffiths, W. J. H., Vogel, W., Pietrangelo, A., & Zoller, H. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.05.016 · Cited by 133 · see citing works
Mitchell, C. J., Shawki, A., Ganz, T., Nemeth, E., & Mackenzie, B. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00348.2013 · Cited by 132 · see citing works
The flatiron mutation in mouse ferroportin acts as a dominant negative to cause ferroportin disease.
Zohn, I. E., De Domenico, I., Pollock, A., Ward, D. M., Goodman, J. F., Liang, X., Sanchez, A. J., Niswander, L., & Kaplan, J. (2007) · Blood · doi:10.1182/blood-2007-01-066068 · Cited by 104 · see citing works
Regulation of growth differentiation factor 15 expression by intracellular iron
Lakhal, S., Talbot, N. P., Crosby, A., Stoepker, C., Townsend, A. R. M., Robbins, P. A., Pugh, C. W., Ratcliffe, P. J., & Mole, D. R. (2009) · Blood · doi:10.1182/blood-2008-07-170431 · Cited by 95 · see citing works
Hepcidin and Ferroportin: The New Players in Iron Metabolism
De Domenico, I., Ward, D., & Kaplan, J. (2011) · Seminars in Liver Disease · doi:10.1055/s-0031-1286058 · Cited by 71 · see citing works
Evidence for the multimeric structure of ferroportin.
De Domenico, I., Ward, D. M., Musci, G., & Kaplan, J. (2007) · Blood · doi:10.1182/blood-2006-06-032516 · Cited by 72 · see citing works
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 · see citing works
Mayr, R., Griffiths, W. J. H., Hermann, M., McFarlane, I., Halsall, D. J., Finkenstedt, A., Douds, A., Davies, S. E., Janecke, A. R., Vogel, W., et al. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.02.064 · Cited by 64 · see citing works
Vlasveld, L. T., Janssen, R., Bardou-Jacquet, E., Venselaar, H., Hamdi-Roze, H., Drakesmith, H., & Swinkels, D. W. (2019) · Pharmaceuticals · doi:10.3390/ph12030132 · Cited by 57 · see citing works
Self-citationA structural model of human ferroportin and of its iron binding site
Bonaccorsi di Patti, M. C., Polticelli, F., Cece, G., Cutone, A., Felici, F., Persichini, T., & Musci, G. (2014) · The FEBS Journal · doi:10.1111/febs.12825 · Cited by 44 · see citing works
The ferroportin Q248H mutation protects from anemia, but not malaria or bacteremia
Muriuki, J. M., Mentzer, A. J., Band, G., Gilchrist, J. J., Carstensen, T., Lule, S. A., Goheen, M. M., Joof, F., Kimita, W., Mogire, R., et al. (2019) · Science Advances · doi:10.1126/sciadv.aaw0109 · Cited by 29 · see citing works
- Authors
- Schimanski, L. M., Drakesmith, H., Merryweather-Clarke, A. T., Viprakasit, V., Edwards, J. P., Sweetland, E., Bastin, J. M., Cowley, D., Chinthammitr, Y., Robson, K. J. H., & Townsend, A. R. M.
- Affiliations
- Siriraj Hospital (TH)
- From the Molecular Immunology Group, Weatherall Institute of Molecular Medicine, Oxford, United Kingdom; the MRC Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, Oxford, United Kingdom; the Department of Paediatrics, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok, Thailand; and the Department of Internal Medicine, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok, Thailand.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2005-05-15
- Volume
- 105
- Issue
- 10
- Pages
- 4096-4102
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2128704908
- Cited by
- 212
- References
- 36
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 2 · 2023: 10 · 2022: 4 · 2021: 7 · 2020: 8 · 2019: 4 · 2018: 5 · 2017: 9 · 2016: 13 · 2015: 7 · 2014: 6 · 2013: 10 · 2012: 8
- FWCI
- 13.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- 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
- ferroportin, SLC40A1, iron export, iron deficiency, haploinsufficiency, iron homeostasis, transferrin saturation, serum ferritin, iron overload
- MeSH terms
- Iron Deficiencies, Ferroportin, Cell Line, Ferritins, Hemochromatosis, Humans, Iron, Mutation, Phenotype, Protein Binding, Receptors, Transferrin, Antigens, CD, Cation Transport Proteins, Intracellular Space
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
