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
Ferroptosis turns 10: Emerging mechanisms, physiological functions, and therapeutic applications
Stockwell, B. R. (2022) · Cell · doi:10.1016/j.cell.2022.06.003 · Cited by 3,211
Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130
Self-citationHentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
Self-citationPositional 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-citationHepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
Ganz, T. (2003) · Blood · doi:10.1182/blood-2003-03-0672 · Cited by 1,544
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
A Red carpet for iron metabolism
Muckenthaler, M. U., Rivella, S., Hentze, M. W., & Galy, B. (2017) · Cell · doi:10.1016/j.cell.2016.12.034 · Cited by 1,319
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275
Self-citationA 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
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
Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122
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
Papanikolaou, G., & Pantopoulos, K. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.06.021 · Cited by 1,070
Trace elements in human physiology and pathology. Copper
Tapiero, H., Townsend, D. M., & Tew, K. D. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(03)00012-x · Cited by 1,046
Targeted Drug Delivery via the Transferrin Receptor-Mediated Endocytosis Pathway
Qian, Z., Li, H., Sun, H., & Ho, K. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.4.561 · Cited by 1,035
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
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
Self-citationIron homeostasis and oxidative stress: An intimate relationship
Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 960
Severe iron deficiency anemia in transgenic mice expressing liver hepcidin
Nicolas, G., Bennoun, M., Porteu, A., Mativet, S., Beaumont, C., Grandchamp, B., Sirito, M., Sawadogo, M., Kahn, A., & Vaulont, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072632499 · Cited by 880
Casari, G., Fusco, M. D., Ciarmatori, S., Zeviani, M., Mora, M., Fernández‐Silva, P., Michele, G. D., Filla, A., Cocozza, S., Marconi, R., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81203-9 · Cited by 826
The roles of iron in health and disease
Lieu, P. T., Heiskala, M. K., Peterson, P. A., & Yang, Y. M. (2001) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(00)00006-6 · Cited by 829
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804
Ohgami, R. S., Campagna, D. R., Greer, E. L., Antiochos, B., McDonald, A., Chen, J., Sharp, J. J., Fujiwara, Y., Barker, J. E., & Fleming, M. D. (2005) · Nature Genetics · doi:10.1038/ng1658 · Cited by 775
Self-citationThe 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
Self-citationGrotz, N., Fox, T. C., Connolly, E. L., Park, W. D., Guerinot, M. L., & Eide, D. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.12.7220 · Cited by 735
Variations in the NRAMP1 Gene and Susceptibility to Tuberculosis in West Africans
Bellamy, R., Ruwende, C., Corrah, T., McAdam, K. P. W. J., Whittle, H. C., & Hill, A. V. S. (1998) · New England Journal of Medicine · doi:10.1056/nejm199803053381002 · Cited by 738
The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer
Kalinowski, D. S., & Richardson, D. R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.2 · Cited by 721
Ponka, P. (1999) · The American Journal of the Medical Sciences · doi:10.1097/00000441-199910000-00004 · Cited by 661
I RON R EGULATORY P ROTEINS AND THE M OLECULAR C ONTROL OF M AMMALIAN I RON M ETABOLISM
Eisenstein, R. S. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.627 · Cited by 655
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 661
Andrews, N. C., & Schmidt, P. J. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.164337 · Cited by 671
Self-citationWeinstein, D. A., Roy, C. N., Fleming, M. D., Loda, M. F., Wolfsdorf, J. I., & Andrews, N. C. (2002) · Blood · doi:10.1182/blood-2002-04-1260 · Cited by 632
Self-citationEmerging mechanisms for heavy metal transport in plants
Williams, L. E., Pittman, J. K., & Hall, J. L. (2000) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(00)00133-4 · Cited by 644
Manganese: Recent advances in understanding its transport and neurotoxicity
Aschner, M., Guilarte, T. R., Schneider, J. S., & Zheng, W. (2007) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2007.03.001 · Cited by 639
Forging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623
Self-citationHereditary Hemochromatosis: Pathogenesis, Diagnosis, and Treatment
Pietrangelo, A. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.06.013 · Cited by 615
Mechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598
The transferrin receptor: role in health and disease
Ponka, P., & Lok, C. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00070-9 · Cited by 609
Leishmaniasis: Current Status of Vaccine Development
Handman, E. (2001) · Clinical Microbiology Reviews · doi:10.1128/cmr.14.2.229-243.2001 · Cited by 595
Transferrin receptor is necessary for development of erythrocytes and the nervous system
Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574
Self-citationTargeted 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
Role of iron in carcinogenesis: cancer as a ferrotoxic disease
Toyokuni, S. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2008.01001.x · Cited by 552
Involvement of NRAMP1 from Arabidopsis thaliana in iron transport
Curie, C., Alonso, J. M., Jean, M. L., Ecker, J. R., & Briat, J. (2000) · Biochemical Journal · doi:10.1042/bj3470749 · Cited by 561
Labile iron pool: the main determinant of cellular response to oxidative stress
Kruszewski, M. K. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.004 · Cited by 538
Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526
Nutritive metal uptake in teleost fish
Bury, N. R., Walker, P., & Glover, C. N. (2002) · Journal of Experimental Biology · doi:10.1242/jeb.00068 · Cited by 522
Regulation of iron transport and the role of transferrin
Gkouvatsos, K., Papanikolaou, G., & Pantopoulos, K. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.10.013 · Cited by 518
The NRAMP family of metal-ion transporters
Nevo, Y., & Nelson, N. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.007 · Cited by 526
Iron Deficiency and Erythropoiesis: New Diagnostic Approaches
Brugnara, C. (2003) · Clinical Chemistry · doi:10.1373/49.10.1573 · Cited by 511
Brain barrier systems: a new frontier in metal neurotoxicological research
Zheng, W., Aschner, M., & Ghersi‐Egea, J. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/s0041-008x(03)00251-5 · Cited by 513
HIF-2α, but not HIF-1α, promotes iron absorption in mice
Mastrogiannaki, M., Matak, P., Keith, B., Simon, M. C., Vaulont, S., & Peyssonnaux, C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38499 · Cited by 502
Cailliatte, R., Schikora, A., Briat, J., Mari, S., & Curie, C. (2010) · The Plant Cell · doi:10.1105/tpc.109.073023 · Cited by 508
NEW INSIGHTS INTO ERYTHROPOIESIS: The Roles of Folate, Vitamin B 12 , and Iron
Koury, M. J., & Ponka, P. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.24.012003.132306 · Cited by 518
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
Iron Homeostasis and the Inflammatory Response
Wessling-Resnick, M. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104804 · Cited by 480
Overview of iron metabolism in health and disease
Dev, S., & Babitt, J. L. (2017) · Hemodialysis International · doi:10.1111/hdi.12542 · Cited by 499
Kozłowski, H., Janicka-Kłos, A., Brasuń, J., Gaggelli, E., Valensin, D., & Valensin, G. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.05.011 · Cited by 481
Altered selectivity in an Arabidopsis metal transporter
Rogers, E. E., Eide, D. J., & Guerinot, M. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.210214197 · Cited by 467
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
The role of iron in cell cycle progression and the proliferation of neoplastic cells
Le, N. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00068-9 · Cited by 453
Canonne-Hergaux, F., Gruenheid, S., Ponka, P., & Gros, P. (1999) · Blood · doi:10.1182/blood.v93.12.4406 · Cited by 451
Huang, X. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.023 · Cited by 446
Lactoferrin: Multifunctional roles of lactoferrin: a critical overview
Ward, P. P., Paz, E., & Conneely, O. M. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5369-8 · Cited by 443
Transferrin/transferrin receptor‐mediated drug delivery
Li, H., & Qian, Z. (2002) · Medicinal Research Reviews · doi:10.1002/med.10008 · Cited by 447
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
Brissot, P., Pietrangelo, A., Adams, P. C., de Graaff, B., McLaren, C. E., & Loréal, O. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2018.16 · Cited by 430
Hubert, N., & Hentze, M. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192423399 · Cited by 428
Aisen, P., Wessling‐Resnick, M., & Leibold, E. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80033-7 · Cited by 426
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
Gunshin, H., Fujiwara, Y., Custodio, A. O., DiRenzo, C., Robine, S., & Andrews, N. C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24356 · Cited by 419
Self-citationIron uptake and metabolism in the new millennium
Dunn, L., Rahmanto, Y. S., & Richardson, D. R. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.12.003 · Cited by 423
Iron homeostasis: insights from genetics and animal models
Andrews, N. C. (2000) · Nature Reviews Genetics · doi:10.1038/35042073 · Cited by 425
Self-citationMolecular Basis of the Neurodegenerative Disorders
Martin, J. B. (1999) · New England Journal of Medicine · doi:10.1056/nejm199906243402507 · Cited by 422
Salazar, J., Mena, N., Hunot, S., Prigent, A., Alvarez-Fischer, D., Arredondo, M., Duyckaerts, C., Sazdovitch, V., Zhao, L., Garrick, L. M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804373105 · Cited by 409
Koskenkorva-Frank, T. S., Weiss, G., Koppenol, W. H., & Burckhardt, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.09.001 · Cited by 406
Mechanistic and regulatory aspects of intestinal iron absorption
Gulec, S., Anderson, G. J., & Collins, J. F. (2014) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00348.2013 · Cited by 406
Role of manganese in neurodegenerative diseases
Bowman, A. B., Kwakye, G. F., Hernández, E. H., & Aschner, M. (2011) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2011.08.144 · Cited by 400
Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377
DMT1: A mammalian transporter for multiple metals
Garrick, M. D., Dolan, K. G., Horbinski, C., Ghio, A. J., Higgins, D. M., Porubcin, M., Moore, E., Hainsworth, L. N., Umbreit, J. N., Conrad, M. E., et al. (2003) · BioMetals · doi:10.1023/a:1020702213099 · Cited by 378
Ferroportin-mediated iron transport: Expression and regulation
Ward, D. M., & Kaplan, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.03.004 · Cited by 373
Natural Resistance to Intracellular Infections
Jabado, N., Jankowski, A., Dougaparsad, S., Picard, V., Grinstein, S., & Gros, P. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.9.1237 · Cited by 372
Liver iron sensing and body iron homeostasis
Wang, C.-Y., & Babitt, J. L. (2019) · Blood · doi:10.1182/blood-2018-06-815894 · Cited by 360
Yanatori, I., & Kishi, F. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.020 · Cited by 371
The biological chemistry of lead
Godwin, H. A. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00194-0 · Cited by 359
Manganese in Health and Disease
Ávila, D. S., Puntel, R. L., & Aschner, M. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_7 · Cited by 378
MOLECULAR BIOLOGY OF CATION TRANSPORT IN PLANTS
Fox, T. C., & Guerinot, M. L. (1998) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.49.1.669 · Cited by 358
Metallostasis in Alzheimer's disease
Ayton, S., Lei, P., & Bush, A. I. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.558 · Cited by 359
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
Targeting iron metabolism in drug discovery and delivery
Crielaard, B. J., Lammers, T., & Rivella, S. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.248 · Cited by 352
Iron Metabolism in the Reticuloendothelial System
Knutson, M. D., & Wessling‐Resnick, M. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609210 · Cited by 360
Hepcidin, A New Iron Regulatory Peptide
Nicolas, G., Viatte, L., Bennoun, M., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0573 · Cited by 355
Iron misregulation in the brain: a primary cause of neurodegenerative disorders
Ke, Y., & Qian, Z. (2003) · The Lancet Neurology · doi:10.1016/s1474-4422(03)00353-3 · Cited by 341
Functional Expression of the Human hZIP2 Zinc Transporter
Gaither, L. A., & Eide, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5560 · Cited by 328
Manganese Dosimetry: Species Differences and Implications for Neurotoxicity
Aschner, M., Erikson, K. M., & Dorman, D. C. (2005) · Critical Reviews in Toxicology · doi:10.1080/10408440590905920 · Cited by 331
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
Varotto, C., Maiwald, D., Pesaresi, P., Jahns, P., Salamini, F., & Leister, D. (2002) · The Plant Journal · doi:10.1046/j.1365-313x.2002.01381.x · Cited by 320
Anderson, G. J., & Vulpe, C. D. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0051-1 · Cited by 317
Arabidopsis IRT2 gene encodes a root‐periphery iron transporter
Vert, G., Briat, J., & Curie, C. (2001) · The Plant Journal · doi:10.1046/j.1365-313x.2001.01018.x · Cited by 317
Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins
Rajagopal, A., Rao, A. U., Amigo, J., Tian, M., Upadhyay, S. K., Hall, C., Uhm, S., Mathew, M. K., Fleming, M. D., Paw, B. H., et al. (2008) · Nature · doi:10.1038/nature06934 · Cited by 316
Self-citationMetal ion transporters and homeostasis
Nelson, N. (1999) · The EMBO Journal · doi:10.1093/emboj/18.16.4361 · Cited by 320
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
