The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Abstract
Although disorders of iron metabolism are prevalent, iron transport remains poorly understood. To address this problem, we undertook a positional cloning strategy to identify the causative mutation in mice with microcytic anaemia (mk). Homozygous mk/mk mice have microcytic, hypochromic anaemia due to severe defects in intestinal iron absorption and erythroid iron utilization. We report the identification of a strong candidate gene for mk, and suggest that the phenotype is a consequence of a missense mutation in Nramp2 (ref. 5), a previously identified gene of unknown function. Nramp2 is homologous to Nramp1, a gene activa in host defense. If Nramp2 is mk, as the cumulative evidence suggests, our findings have broad implications for the understanding of iron transport and resistance to intracellular pathogens.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The freed ferric iron is then reduced to its bio-active ferrous form, Fe2+ by the ferrireductase STEAP3 (six-transmembrane epithelial antigen of prostate 3) and shuttled into the cytosol from the endosome by DMT1 (Fleming et al., 1997; Gunshin et al., 1997; Ohgami et al., 2005; Figure 1).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Fleming et al., 1997
In the citing paper
“However, inorganic iron uptake from the gastrointestinal lumen by enterocytes depends upon the divalent metal transporter protein 1 (DMT1 or NRAMP2), which is not able to import Fe3+. 12 , 13 , 14”
From The battle for iron in enteric infections (2020) · cites this paper as [12]
In the citing paper
“Liberated inorganic iron is then reduced by the ferrireductase STEAP3 to Fe 2ϩ , 10 which is the substrate for transmembrane transport by divalent metal transporter 1 (DMT1 or SLC11A2, formerly called NRAMP2, DCT1).”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [12]
In the citing paper
“In spite of these obstacles and entirely by chance, the first mammalian transmembrane iron transporter was discovered simultaneously in 2 laboratories, located within a city block of each other in Boston, using singularly modern techniques.12,13”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [12]
In the citing paper
“Interestingly, the clinical phenotype of patients with DMT1 mutations differs slightly from the corresponding mouse model, mk. 12”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [12]
In the citing paper
“Unlike TfR1, TfR2 does not contain an IRE in its mRNA and does not appear to be regulated in an iron-dependent manner (90, 315).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [90]
In the citing paper
“Studies of TfR2 expression in a mouse model for hemochromatosis revealed that TfR2 was not downregulated in conditions of iron overload (90), supporting the absence of an iron-mediated posttranscriptional regulatory mechanism.”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [90]
In the citing paper
“Interestingly, iron accumulation in the liver in type 1 HH results in the downregulation of TfR1, but in the case of TfR2, it is continually expressed even during HH-mediated iron loading (90).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [90]
In the citing paper
“In addition, TfR2 does not appear to be regulated by iron concentrations, for it lacks IRE in its mRNA and is not inducible by iron deficiency (90).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [90]
Citations
Cites
Goffeau, A., Barrell, B. G., Bussey, H., Davis, R. W., Dujon, B., Feldmann, H., Galibert, F., Hoheisel, J. D., Jacq, C., Johnston, M., et al. (1996) · Science · doi:10.1126/science.274.5287.546 · Cited by 4,423
Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786
DNA methylation and the frequency of CpG in animal DNA
Bird, A. P. (1980) · Nucleic Acids Research · doi:10.1093/nar/8.7.1499 · Cited by 1,175
The I.M.A.G.E. Consortium: An Integrated Molecular Analysis of Genomes and Their Expression
Lennon, G., Auffray, C., Polymeropoulos, M. H., & Soares, M. B. (1996) · Genomics · doi:10.1006/geno.1996.0177 · Cited by 1,123
Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg
Vidal, S. M., Malo, D., Vogan, K., Skamene, E., & Gros, P. (1993) · Cell · doi:10.1016/0092-8674(93)90135-d · Cited by 1,104
Harding, A. E. (1981) · Brain · doi:10.1093/brain/104.3.589 · Cited by 929
Homozygosity Mapping: A Way to Map Human Recessive Traits with the DNA of Inbred Children
Lander, E. S., & Botstein, D. (1987) · Science · doi:10.1126/science.2884728 · Cited by 885
The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.
Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670
Dancis, A., Yuan, D. S., Haile, D., Askwith, C., Eide, D., Moehle, C., Kaplan, J., & Klausner, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90345-x · Cited by 659
Vidal, S., Tremblay, M. L., Govoni, G., Gauthier, S., Sebastiani, G., Malo, D., Skamene, E., Olivier, M., Jothy, S., & Gros, P. (1995) · The Journal of experimental medicine · doi:10.1084/jem.182.3.655 · Cited by 603
Research works printed but not linked: 2
- McFarland, E.C. & Russell, E.S. Microcytic anemia (mk) has been located close to Ca on chromosome 15. Mouse News Letter 53, 35 (1975).
- Weinberg, E.D. The iron-withholding defense system. ASM News 59, 559–562 (1993).
Cited by
Sorted by citations
Items 301–400 of 1,000
Pinner, E., Gruenheid, S., Raymond, M., & Gros, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.28933 · Cited by 115
Zebrafish in the sea of mineral (iron, zinc, and copper) metabolism
Zhao, L., Xia, Z., & Wang, F. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00033 · Cited by 119
Molecular Mechanism of Nramp-Family Transition Metal Transport
Bozzi, A. T., & Gaudet, R. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166991 · Cited by 117
Kuhn, D. E., Baker, B. D., Lafuse, W. P., & Zwilling, B. S. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.66.1.113 · Cited by 113
Iron: A New Target for Pharmacological Intervention in Neurodegenerative Diseases
Whitnall, M., & Richardson, D. R. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.008 · Cited by 113
Dysregulation of iron and copper homeostasis in nonalcoholic fatty liver
Aigner, E. S. (2014) · World Journal of Hepatology · doi:10.4254/wjh.v7.i2.177 · Cited by 116
Dietary iron induces rapid changes in rat intestinal divalent metal transporter expression
Yeh, K., YEH, M. K. Y., Watkins, J. A., Rodriguez‐Paris, J., & Glass, J. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.279.5.g1070 · Cited by 113
Kanbay, M., Perazella, M. A., Kasapoğlu, B., Köroğlu, M., & Covic, A. C. (2009) · Blood Purification · doi:10.1159/000245041 · Cited by 114
Identification and Localization of Divalent Metal Transporter-1 (DMT-1) in Term Human Placenta
Georgieff, M. K., Wobken, J. D., Welle, J., Burdo, J. R., & Connor, J. R. (2000) · Placenta · doi:10.1053/plac.2000.0566 · Cited by 113
Moos, T., & Morgan, E. H. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02142.x · Cited by 113
Dupic, F., Fruchon, S., Bensaid, M., Loréal, O., Brissot, P., Borot, N., Roth, M., & Coppin, H. (2002) · Gut · doi:10.1136/gut.51.5.648 · Cited by 115
The Ceruloplasmin Homolog Hephaestin and the Control of Intestinal Iron Absorption
Anderson, G. J., Frazer, D. M., McKie, A. T., & Vulpe, C. D. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0576 · Cited by 111
Pelizzoni, I., Macco, R., Morini, M. F., Zacchetti, D., Grohovaz, F., & Codazzi, F. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00652.x · Cited by 111
Tchernitchko, D., Bourgeois, M., Martin, M., & Beaumont, C. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630449 · Cited by 111
Metal transporters and disease
Andrews, N. C. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00307-1 · Cited by 110
Self-citationFleming, M. D., Campagna, D. R., Haslett, J. N., Trenor, C. C., & Andrews, N. C. (2001) · Genes & Development · doi:10.1101/gad.873001 · Cited by 110
Self-citationMolecular and Functional Roles of Duodenal Cytochrome B (Dcytb) in Iron Metabolism
Latunde-Dada, G. O., der Westhuizen, J. V., Vulpe, C. D., Anderson, G. J., Simpson, R. J., & McKie, A. T. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0574 · Cited by 107
Molecular control of iron metabolism
Andrews, N. C. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.10.004 · Cited by 109
Self-citationFrazer, D. M., Inglis, H. R., Wilkins, S. J., Millard, K. N., Steele, T. M., McLaren, G. D., McKie, A. T., Vulpe, C. D., & Anderson, G. J. (2004) · Gut · doi:10.1136/gut.2003.037416 · Cited by 109
Zoller, H., Theurl, I., Koch, R., Kaser, A., & Weiss, G. (2002) · Blood Cells, Molecules, and Diseases · doi:10.1006/bcmd.2002.0587 · Cited by 106
The zebrafish mutant gene chardonnay (cdy) encodes divalent metal transporter 1 (DMT1).
Donovan, A. (2002) · Blood · doi:10.1182/blood-2002-04-1169 · Cited by 106
Cellular and mitochondrial iron homeostasis in vertebrates
Chen, C., & Paw, B. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.003 · Cited by 111
Kim, D., Kim, K., Choi, B., Youn, P., Ryu, D., Klaassen, C. D., & Park, J. (2006) · Archives of Toxicology · doi:10.1007/s00204-006-0160-7 · Cited by 106
Iron and inflammatory bowel disease
Oldenburg, B., Koningsberger, J. C., Henegouwen, G. P. V. B., van Asbeck, B. S., & Marx, J. J. M. (2001) · Alimentary Pharmacology & Therapeutics · doi:10.1046/j.1365-2036.2001.00930.x · Cited by 106
Heme and FLVCR-related transporter families SLC48 and SLC49
Khan, A. A., & Quigley, J. G. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.07.013 · Cited by 105
Iron Status in Mice Carrying a Targeted Disruption of Lactoferrin
Ward, P. P., Mendoza-Meneses, M., Cunningham, G. A., & Conneely, O. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.178-185.2003 · Cited by 108
Crossgrove, J. S. (2003) · NeuroToxicology · doi:10.1016/j.neuro.2003.10.005 · Cited by 104
The role of labile iron pool in cardiovascular diseases.
Kruszewski, M. K. (2004) · Acta Biochimica Polonica · doi:10.18388/abp.2004_3585 · Cited by 104
Kalinowski, D. S., Sharpe, P. C., Bernhardt, P. V., & Richardson, D. R. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm7012562 · Cited by 104
Richardson, D. R. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.026 · Cited by 104
Mitochondrial Mayhem: The Mitochondrion as a Modulator of Iron Metabolism and Its Role in Disease
Huang, M. L.-H., Lane, D. J. R., & Richardson, D. R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3921 · Cited by 103
Metal ion transporters in mammals: structure, function and pathological implications
Rolfs, A., & Hediger, M. A. (1999) · The Journal of Physiology · doi:10.1111/j.1469-7793.1999.0001r.x · Cited by 103
Iron transport by Nramp2/DMT1: pH regulation of transport by 2 histidines in transmembrane domain 6
Lam-Yuk-Tseung, S., Govoni, G. R., Forbes, J., & Gros, P. (2003) · Blood · doi:10.1182/blood-2002-07-2108 · Cited by 104
Erikson, K. M., & Aschner, M. (2005) · NeuroToxicology · doi:10.1016/j.neuro.2005.07.003 · Cited by 103
Mechanisms of Manganese-Induced Rat Pheochromocytoma (PC12) Cell Death and Cell Differentiation
Roth, J. A., Horbinski, C., Higgins, D. M., Lein, P. J., & Garrick, M. D. (2002) · NeuroToxicology · doi:10.1016/s0161-813x(01)00077-8 · Cited by 102
Garrick, M. D., & Garrick, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.018 · Cited by 105
Genetic regulation of macrophage activation: understanding the function of Nramp1 (=Ity/Lsh/Bcg)
Blackwell, J. M., & Searle, S. (1999) · Immunology Letters · doi:10.1016/s0165-2478(98)00127-8 · Cited by 102
Quercetin and iron metabolism: What we know and what we need to know
Xiao, L., Luo, G., Tang, Y., & Yao, P. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.02.022 · Cited by 105
Han, M., Xu, R., Wang, S., Yang, N., Ni, S., Zhang, Q. H., Xu, Y., Zhang, X., Zhang, C., Wei, Y., et al. (2018) · Neoplasia · doi:10.1016/j.neo.2018.04.002 · Cited by 101
Wyllie, S., Seu, P., & Goss, J. A. (2002) · Microbes and Infection · doi:10.1016/s1286-4579(02)01548-4 · Cited by 101
Touret, N., Furuya, W., Forbes, J., Gros, P., & Grinstein, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212374200 · Cited by 101
The SLC31 (Ctr) copper transporter family
Petris, M. J. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1092-1 · Cited by 101
Canonne‐Hergaux, F., Fleming, M. D., Levy, J. E., Gauthier, S., Ralph, T., Picard, V., Andrews, N. C., & Gros, P. (2000) · PubMed · doi:10.1182/blood.v96.12.3964.h8003964_3964_3970 · Cited by 101
Self-citationResearch on the Mechanisms of Plant Enrichment and Detoxification of Cadmium
Yang, G., Zheng, M., Tan, A.-J., Liu, Y., Feng, D., & Lv, S. (2021) · Biology · doi:10.3390/biology10060544 · Cited by 100
Intestinal HIF2α promotes tissue-iron accumulation in disorders of iron overload with anemia
Anderson, E. R., Taylor, M. J., Xue, X., Ramakrishnan, S. K., Martin, A. S., Xie, L., Bredell, B. X., Gardenghi, S., Rivella, S., & Shah, Y. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314197110 · Cited by 101
The Ins and Outs of Iron Homeostasis
Donovan, A., Roy, C. N., & Andrews, N. C. (2006) · Physiology · doi:10.1152/physiol.00052.2005 · Cited by 101
Self-citationDupic, F., Fruchon, S., Bensaid, M., Borot, N., Radosavljevic, M., Loreal, O., Brissot, P., Gilfillan, S., Bahram, S., Coppin, H., et al. (2002) · Gastroenterology · doi:10.1053/gast.2002.31877 · Cited by 99
Wang, X., Zhang, M., Flores, S. R. L., Woloshun, R. R., Yang, C., Yin, L., Xiang, P., Xu, X., Garrick, M. D., Vidyasagar, S., et al. (2019) · Molecular Therapy · doi:10.1016/j.ymthe.2019.01.003 · Cited by 99
Hereditary Causes of Disturbed Iron Homeostasis in the Central Nervous System
Ponka, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.022 · Cited by 99
Role of Intestinal HIF-2α in Health and Disease
Ramakrishnan, S. K., & Shah, Y. M. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105202 · Cited by 100
Seeking Candidate Mutations That Affect Iron Homeostasis
Lee, P. L., Gelbart, T., West, C., Halloran, C., & Beutler, E. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0586 · Cited by 98
Sacher, A., Cohen, A., & Nelson, N. (2001) · Journal of Experimental Biology · doi:10.1242/jeb.204.6.1053 · Cited by 98
The natural resistance-associated macrophage protein and susceptibility to intracellular pathogens
Bellamy, R. (1999) · Microbes and Infection · doi:10.1016/s1286-4579(99)80010-0 · Cited by 96
Iron-Sensing Proteins that Regulate Hepcidin and Enteric Iron Absorption
Knutson, M. D. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104801 · Cited by 96
Expression of the iron transporter DMT1 in kidney from normal and anemic mk mice
Canonne‐Hergaux, F., & Gros, P. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00405.x · Cited by 96
Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers
Roy, C. N. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.20.2181 · Cited by 96
Ferroportin1 and hephaestin are involved in the nigral iron accumulation of 6‐OHDA‐lesioned rats
Wang, J., Jiang, H. F., & Xie, J. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05515.x · Cited by 95
Divalent metal transporter 1 is involved in amyloid precursor protein processing and Aβ generation
Zheng, W. H., Xin, N., Chi, Z., Zhao, B.-L., Zhang, J., Li, J., & Wang, Z. (2009) · The FASEB Journal · doi:10.1096/fj.09-135749 · Cited by 95
Cadmium Absorption and Its Relationship to Divalent Metal Transporter-1 in the Pregnant Rat
Leazer, T. M. (2002) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2002.9505 · Cited by 95
Regulation of iron absorption in Hfe mutant mice
Ajioka, R. S., Levy, J. E., Andrews, N. C., & Kushner, J. P. (2002) · Blood · doi:10.1182/blood-2001-11-0037 · Cited by 95
Self-citationThe role of iron in T cell development and autoimmunity
Bowlus, C. L. (2003) · Autoimmunity Reviews · doi:10.1016/s1568-9972(02)00143-x · Cited by 95
Functional Expression of Nramp1 In Vitro in the Murine Macrophage Line RAW264.7
Govoni, G. R., Canonne‐Hergaux, F., Pfeifer, C. G., Marcus, S. L., Mills, S. D., Hackam, D. J., Grinstein, S., Malo, D., Finlay, B. B., & Gros, P. (1999) · Infection and Immunity · doi:10.1128/iai.67.5.2225-2232.1999 · Cited by 97
The Thlaspi caerulescens NRAMP homologue TcNRAMP3 is capable of divalent cation transport
Wei, W., Chai, T., Zhang, Y., Han, L., Xu, J., & Guan, Z. (2009) · Molecular Biotechnology · doi:10.1007/s12033-008-9088-x · Cited by 94
Seiwert, N., Wecklein, S., Demuth, P., Hasselwander, S., Kemper, T. A., Schwerdtle, T., Brunner, T., & Fahrer, J. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02950-8 · Cited by 94
H+-Coupled Divalent Metal-Ion Transporter-1
Shawki, A., Knight, P. B., Maliken, B. D., Niespodzany, E. J., & Mackenzie, B. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394316-3.00005-3 · Cited by 100
Molecular pathogenesis of iron overload
Trinder, D., Fox, C., Vautier, G., & Olynyk, J. K. (2002) · Gut · doi:10.1136/gut.51.2.290 · Cited by 93
Iron Homeostasis and Metabolism: Two Sides of a Coin
Venkataramani, V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_3 · Cited by 96
Ke, Y., Chang, Y. Z., Duan, X. L., Du, J. R., Zhu, L., Wang, K., Yang, X. D., Ho, K. P., & Qian, Z. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.06.002 · Cited by 92
A general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 97
Barton, J. C., Bertoli, L. F., & Rothenberg, B. E. (2000) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(00)70026-6 · Cited by 97
Expression of the DMT1 (NRAMP2/DCT1) iron transporter in mice with genetic iron overload disorders
Canonne‐Hergaux, F., Levy, J. E., Fleming, M. D., Montross, L. K., Andrews, N. C., & Gros, P. (2001) · Blood · doi:10.1182/blood.v97.4.1138 · Cited by 91
Self-citationAndolfo, 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
Abouhamed, M., Gburek, J., Liu, W., Torchalski, B., Wilhelm, A., Wolff, N. A., Christensen, E. I., Thévenod, F., & Smith, C. P. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00359.2005 · Cited by 90
Roth, J. A., Horbinski, C., Feng, L., Dolan, K. G., Higgins, D. M., & Garrick, M. D. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-20-07595.2000 · Cited by 90
Guo, Q., Qian, C., Wang, X., & Qian, Z. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01436-x · Cited by 91
Schranzhofer, M., Schifrer, M., Cabrera, J. A., Kopp, S., Chiba, P., Beug, H., & Müllner, E. W. (2006) · Blood · doi:10.1182/blood-2005-05-1809 · Cited by 89
Post‐transcriptional expression of DMT1 in the heart of rat
Ke, Y., Chen, Y. Y., Chang, Y. Z., Duan, X. L., Ho, K. P., Jiang, D. H., Wang, K., & Qian, Z. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10284 · Cited by 89
Gomes, M. S., & APPELBERG (1998) · Immunology · doi:10.1046/j.1365-2567.1998.00630.x · Cited by 89
Nrampl: a link between intracellular iron transport and innate resistance to intracellular pathogens
Barton, C. H., Biggs, T. E., Baker, S. T., Bowen, H., & Atkinson, P. G. P. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.66.5.757 · Cited by 88
Gruenheid, S. (2000) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(99)00049-1 · Cited by 87
S-Nitrosylation of IRP2 Regulates Its Stability via the Ubiquitin-Proteasome Pathway
Kim, S.-W., Wing, S. S., & Ponka, P. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.330-337.2004 · Cited by 87
Functional Expression Cloning and Characterization of SFT, a Stimulator of Fe Transport
Gutierrez, J. A., Yu, J., Rivera, S. B., & Wessling‐Resnick, M. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.4.895 · Cited by 87
Donker, A. E., Raymakers, R. A. P., Vlasveld, L. T., van Barneveld, T., Terink, R., Dors, N., Brons, P., Knoers, N. V. A. M., & Swinkels, D. W. (2014) · Blood · doi:10.1182/blood-2014-01-548776 · Cited by 88
Chawla, P., Bhandari, L., Sadh, P. K., & Kaushik, R. (2016) · Cereal Chemistry · doi:10.1094/cchem-05-16-0128-r · Cited by 86
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 89
Molecular Mechanisms and Regulation of Iron Transport
Chung, J., & Wessling‐Resnick, M. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609332 · Cited by 86
Mechanisms of Haem and Non-Haem Iron Absorption: Lessons from Inherited Disorders of Iron Metabolism
Anderson, G. J., Frazer, D. M., McKie, A. T., Vulpe, C. D., & Smith, A. (2005) · BioMetals · doi:10.1007/s10534-005-3708-8 · Cited by 90
Large-scale, high-throughput screening for coagulation and hematologic phenotypes in mice*
Peters, L. L., Cheever, E. M., Ellis, H. R., Magnani, P. A., Svenson, K. L., Smith, R. V., & Bogue, M. A. (2002) · Physiological Genomics · doi:10.1152/physiolgenomics.00077.2002 · Cited by 85
Iron Is Hot: An Update on the Pathophysiology of Hemochromatosis
Andrews, N. C., & Levy, J. E. (1998) · Blood · doi:10.1182/blood.v92.6.1845.418k35_1845_1851 · Cited by 85
Self-citationZebrafish a genetic model for vertebrate organogenesis and human disorders
Paw, B. H. (2003) · Frontiers in bioscience · doi:10.2741/1092 · Cited by 87
Watts, R., Ponka, P., & Richardson, D. R. (2003) · Biochemical Journal · doi:10.1042/bj20021302 · Cited by 84
Iron Transport Across Biologic Membranes
Andrews, N. C., Fleming, M. D., & Gunshin, H. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1999.tb06934.x · Cited by 84
Self-citationGenetic Susceptibility to Tuberculosis
Bellamy, R. (2005) · Clinics in Chest Medicine · doi:10.1016/j.ccm.2005.02.006 · Cited by 83
Bauer, P., Thiel, T., Klatte, M., Bereczky, Z., Brumbarova, T., Hell, R., & Große, I. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.047233 · Cited by 85
Are There Common Biochemical and Molecular Mechanisms Controlling Manganism and Parkisonism
Roth, J. A. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8088-8 · Cited by 83
Stromal cell-derived receptor 2 and cytochrome b561 are functional ferric reductases
Vargas, J. D. H., Herpers, B., McKie, A. T., Gledhill, S., McDonnell, J. M., van den Heuvel, M., Davies, K. E., & Ponting, C. P. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(03)00242-5 · Cited by 82
Transplasma membrane electron transport: enzymes involved and biological function
Ly, J. D., & Lawen, A. (2003) · Redox Report · doi:10.1179/135100003125001198 · Cited by 82
Intestinal expression of genes involved in iron absorption in humans
Rolfs, A., Bonkovsky, H. L., Kohlroser, J. G., McNeal, K., Sharma, A. K., Berger, U. V., & Hediger, M. A. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00371.2001 · Cited by 82
Wetli, H. A., Buckett, P. D., & Wessling‐Resnick, M. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.08.005 · Cited by 81
Aschner, M., & Dorman, D. C. (2006) · Toxicological Reviews · doi:10.2165/00139709-200625030-00002 · Cited by 82
Metadata
- Authors
- Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C.
- Affiliations
- Brigham and Women's Hospital (US)
- Boston Children's Hospital (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Andrews, Nancy C.
- Venue
- Nature Genetics
- Published
- 1997-08
- Volume
- 16
- Issue
- 4
- Pages
- 383-386
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- OpenAlex
- W2082806735
- Cited by
- 1,159
- References
- 35
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 11 · 2023: 16 · 2022: 12 · 2021: 14 · 2020: 13 · 2019: 23 · 2018: 20 · 2017: 23 · 2016: 21 · 2015: 24 · 2014: 28 · 2013: 33 · 2012: 35
- FWCI
- 42.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- National Institutes of Health (1k08hl003600-01)
- National Heart, Lung, and Blood Institute (K08 HL03600)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- microcytic anemia, DMT1, iron transport, iron metabolism, intestinal iron absorption, missense mutations, positional cloning, NRAMP1, mice
- MeSH terms
- Frataxin, Animals, Friedreich Ataxia, Humans, Mitochondria, Phosphotransferases (Alcohol Group Acceptor), Iron-Binding 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