The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
Open accessAbstract
Solute carrier family 11, member 2 (SLC11A2) is the only transmembrane iron transporter known to be involved in cellular iron uptake. It is widely expressed and has been postulated to play important roles in intestinal iron absorption, erythroid iron utilization, hepatic iron accumulation, placental iron transfer, and other processes. Previous studies have suggested that other transporters might exist, but their physiological significance remained uncertain. To define the activities of Slc11a2 in vivo, we inactivated the murine gene that encodes it globally and selectively. We found that fetal Slc11a2 is not needed for materno-fetal iron transfer but that Slc11a2 activity is essential for intestinal non-heme iron absorption after birth. Slc11a2 is also required for normal hemoglobin production during the development of erythroid precursors. However, hepatocytes and most other cells must have an alternative, as-yet-unknown, iron uptake mechanism. We previously showed that Slc11a2 serves as the primary portal for intestinal iron entry in hemochromatosis. However, inactivation of murine Hfe ameliorates the phenotype of animals lacking Slc11a2.
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.
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
“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 [13]
In the citing paper
“Mammals acquire ferrous (Fe2+) from the diet via a mechanism assisted by the divalent metal transporter ion transporter 1 (DMT1) expressed by duodenum enterocytes (12, 13).”
From Innate Nutritional Immunity (2018) · cites this paper as [12]
In the citing paper
“Surprisingly, however, most other cell types do not appear to require DMT1 for iron uptake.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [66]
In the citing paper
“Targeted disruption of the murine gene encoding DMT1 confirmed that DMT1 is the primary transmembrane iron transporter bringing dietary nonheme iron into intestinal epithelial cells and mediating iron uptake through the transferrin cycle in erythroid precursors.66”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [66]
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
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
Self-citationGoetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159
Self-citationTissue‐specific and inducible Cre‐mediated recombination in the gut epithelium
Marjou, F. E., Janssen, K., Chang, B. H., Li, M., Hindie, V., Chan, L., Louvard, D., Chambon, P., METZGER, D., & Robine, S. (2004) · genesis · doi:10.1002/gene.20042 · Cited by 1,087
Self-citationFleming, 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-citationBrodie, S. E. (1996) · Survey of Ophthalmology · doi:10.1016/s0039-6257(96)80075-0 · Cited by 770
An Iron Delivery Pathway Mediated by a Lipocalin
Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651
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-citationOudit, G. Y., Sun, H., Trivieri, M. G., Koch, S. E., Dawood, F., Ackerley, C., Yazdanpanah, M., Wilson, G. J., Schwartz, A., Liu, P. P., et al. (2003) · Nature Medicine · doi:10.1038/nm920 · Cited by 480
Canonne-Hergaux, F., Gruenheid, S., Ponka, P., & Gros, P. (1999) · Blood · doi:10.1182/blood.v93.12.4406 · Cited by 451
Research works printed but not linked: 2
- Canonne-Hergaux, 2000, Blood., 96, 3964
- Russell, 1970, Transplant. Proc., 2, 144
Cited by
Two to tango: Regulation of Mammalian iron metabolism
Hentze, M. W., Muckenthaler, M. U., Galy, B., & Camaschella, C. (2010) · Cell · doi:10.1016/j.cell.2010.06.028 · Cited by 2,120
Biomarkers of Nutrition for Development—Folate Review
Bailey, L. B., Stover, P. J., McNulty, H., Fenech, M. F., Gregory, J. F., Mills, J. L., Pfeiffer, C. M., Fazili, Z., Zhang, M., Ueland, P. M., et al. (2015) · Journal of Nutrition · doi:10.3945/jn.114.206599 · Cited by 1,173
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
Mechanisms controlling cellular and systemic iron homeostasis
Galy, B., Conrad, M., & Muckenthaler, M. U. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00648-1 · Cited by 862
Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701
Current understanding of iron homeostasis
Anderson, G. J., & Frazer, D. M. (2017) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.155804 · Cited by 688
Non-transferrin bound iron: a key role in iron overload and iron toxicity
Brissot, P., Ropert, M., Le Lan, C., & Loréal, O. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.07.014 · Cited by 654
Andrews, N. C., & Schmidt, P. J. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.164337 · Cited by 678
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
Self-citationMechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598
Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells
Liuzzi, J. P., Aydemir, F., Nam, H., Knutson, M. D., & Cousins, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606424103 · Cited by 577
The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
Dong, X., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T., & Xu, H. (2008) · Nature · doi:10.1038/nature07311 · Cited by 588
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
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
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
Overview of iron metabolism in health and disease
Dev, S., & Babitt, J. L. (2017) · Hemodialysis International · doi:10.1111/hdi.12542 · Cited by 507
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
Iron 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 425
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
Iron homeostasis during pregnancy
Fisher, A. L., & Nemeth, E. (2017) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.155812 · Cited by 432
Wang, C., Jenkitkasemwong, S., Duarte, S., Sparkman, B. K., Shawki, A., Mackenzie, B., & Knutson, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.367284 · Cited by 393
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
Iron Toxicity in Diseases of Aging: Alzheimer's Disease, Parkinson's Disease and Atherosclerosis
Altamura, S., & Muckenthaler, M. U. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1010 · Cited by 369
Metabolic crossroads of iron and copper
Collins, J. F., Prohaska, J. R., & Knutson, M. D. (2010) · Nutrition Reviews · doi:10.1111/j.1753-4887.2010.00271.x · Cited by 367
Scara5 Is a Ferritin Receptor Mediating Non-Transferrin Iron Delivery
Li, J. Y., Paragas, N., Ned, R. M., Qiu, A., Viltard, M., Leete, T., Drexler, I. R., Chen, X., Sanna‐Cherchi, S., Mohammed, F., et al. (2009) · Developmental Cell · doi:10.1016/j.devcel.2008.12.002 · Cited by 366
Self-citationTargeting 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
Biomarkers of Nutrition for Development (BOND)—Iron Review
Lynch, S. R., Pfeiffer, C. M., Georgieff, M., Brittenham, G. M., Fairweather‐Tait, S. J., Hurrell, R. F., McArdle, H. J., & Raiten, D. J. (2018) · Journal of Nutrition · doi:10.1093/jn/nxx036 · Cited by 367
Nose, Y., Kim, B., & Thiele, D. J. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.08.009 · Cited by 321
Anderson, G. J., & Vulpe, C. D. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0051-1 · Cited by 317
Harrison-Findik, D. D., Schafer, D., Klein, E., Timchenko, N. A., Kulaksiz, H., Clemens, D. L., Fein, E., Andriopoulos, B., Pantopoulos, K., & Gollan, J. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602098200 · Cited by 308
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
Iron traffics in circulation bound to a siderocalin (Ngal)–catechol complex
Bao, G., Clifton, M., Hoette, T. M., Mori, K., Deng, S.-X., Qiu, A., Viltard, M., Williams, D., Paragas, N., Leete, T., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.402 · Cited by 307
Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287
Substrate Profile and Metal-ion Selectivity of Human Divalent Metal-ion Transporter-1
Illing, A. C., Shawki, A., Cunningham, C. L., & Mackenzie, B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.364208 · Cited by 270
Waldvogel‐Abramowski, S., Waeber, G., Gassner, C., Buser, A. S., Frey, B. M., Favrat, B., & Tissot, J. (2014) · Transfusion Medicine and Hemotherapy · doi:10.1159/000362888 · Cited by 287
Hepcidin and Its Role in Regulating Systemic Iron Metabolism
Ganz, T. (2006) · Hematology · doi:10.1182/asheducation-2006.1.29 · Cited by 262
Iron and thiol redox signaling in cancer: an exquisite balance to escape ferroptosis
Toyokuni, S., Ito, F., Yamashita, K., Okazaki, Y., & Akatsuka, S. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.024 · Cited by 252
Mechanisms of heme iron absorption: Current questions and controversies
West, A. R., & Oates, P. S. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.4101 · Cited by 257
A precious metal: Iron, an essential nutrient for all cells
Cairo, G., Bernuzzi, F., & Recalcati, S. (2006) · Genes & Nutrition · doi:10.1007/bf02829934 · Cited by 262
Physiologic implications of metal-ion transport by ZIP14 and ZIP8
Jenkitkasemwong, S., Wang, C., Mackenzie, B., & Knutson, M. D. (2012) · BioMetals · doi:10.1007/s10534-012-9526-x · Cited by 251
Jenkitkasemwong, S., Wang, C.-Y., Coffey, R., Zhang, W., Chan, A., Biel, T., Kim, J.-S., Hojyo, S., Fukada, T., & Knutson, M. D. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.002 · Cited by 245
Xue, X., Ramakrishnan, S. K., Weisz, K. M., Triner, D. A., Xie, L., Attili, D., Pant, A., Győrffy, B., Zhan, M., Carter‐Su, C., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.015 · Cited by 249
Carter, A. M. (2012) · Physiological Reviews · doi:10.1152/physrev.00040.2011 · Cited by 246
Pregnancy and iron homeostasis: an update
Cao, C. Q., & O'Brien, K. O. (2013) · Nutrition Reviews · doi:10.1111/j.1753-4887.2012.00550.x · Cited by 239
The Role of Iron in Learning and Memory
Fretham, S. J. B., Carlson, E. S., & Georgieff, M. K. (2011) · Advances in Nutrition · doi:10.3945/an.110.000190 · Cited by 235
Regulation of iron acquisition and iron distribution in mammals
Ganz, T., & Nemeth, E. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.03.014 · Cited by 238
Pinilla-Tenas, J. J., Sparkman, B. K., Shawki, A., Illing, A. C., Mitchell, C. J., Zhao, N., Liuzzi, J. P., Cousins, R. J., Knutson, M. D., & Mackenzie, B. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00479.2010 · Cited by 228
Fuqua, B. K., Vulpe, C. D., & Anderson, G. J. (2012) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2012.03.015 · Cited by 241
Non-transferrin-bound iron transporters
Knutson, M. D. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.413 · Cited by 221
Anderson, E. R., & Shah, Y. M. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120016 · Cited by 264
Iron Imports. II. Iron uptake at the apical membrane in the intestine
Mackenzie, B., & Garrick, M. D. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00363.2005 · Cited by 211
Multi-Copper Oxidases and Human Iron Metabolism
Vashchenko, G., & MacGillivray, R. T. A. (2013) · Nutrients · doi:10.3390/nu5072289 · Cited by 223
Nramp1 phagocyte intracellular metal withdrawal defense
Cellier, M. F., Courville, P., & Campion, C. (2007) · Microbes and Infection · doi:10.1016/j.micinf.2007.09.006 · Cited by 203
Molecular mechanisms involved in intestinal iron absorption
Sharp, P. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4716 · Cited by 205
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
Adams, P. C., & Barton, J. C. (2010) · Blood · doi:10.1182/blood-2010-01-261875 · Cited by 191
Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice
Gunshin, H., Starr, C. N., DiRenzo, C., Fleming, M. D., Jin, J., Greer, E. L., Sellers, V. M., Galica, S. M., & Andrews, N. C. (2005) · Blood · doi:10.1182/blood-2005-02-0716 · Cited by 188
Self-citationH + ‐coupled nutrient, micronutrient and drug transporters in the mammalian small intestine
Thwaites, D. T., & Anderson, C. M. H. (2007) · Experimental Physiology · doi:10.1113/expphysiol.2005.029959 · Cited by 188
Iron homeostasis: An anthropocentric perspective
Coffey, R., & Ganz, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.781823 · Cited by 194
The Role of Fe, Zn, and Cu in Pregnancy
Grzeszczak, K., Kwiatkowski, S., & Kosik-Bogacka, D. I. (2020) · Biomolecules · doi:10.3390/biom10081176 · Cited by 210
Iron Is Essential for Neuron Development and Memory Function in Mouse Hippocampus
Carlson, E. S., Tkáč, I., Magid, R., O’Connor, M. B., Andrews, N. C., Schallert, T. J., Gunshin, H., Georgieff, M., & Petryk, A. (2009) · Journal of Nutrition · doi:10.3945/jn.108.096354 · Cited by 185
Self-citationAydemir, T. B., Chang, S.-M., Guthrie, G. J., Maki, A. B., Ryu, M., Karabıyık, A., & Cousins, R. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048679 · Cited by 183
Physiology and pathophysiology of iron in hemoglobin-associated diseases
Coates, T. D. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.039 · Cited by 187
Iron uptake and transport across physiological barriers
Duck, K. A., & Connor, J. R. (2016) · BioMetals · doi:10.1007/s10534-016-9952-2 · Cited by 182
Functional properties of multiple isoforms of human divalent metal-ion transporter 1 (DMT1)
Mackenzie, B., Takanaga, H., Hubert, N., Rolfs, A., & Hediger, M. A. (2007) · Biochemical Journal · doi:10.1042/bj20061290 · Cited by 173
Nam, H., Wang, C., Zhang, L., Zhang, W., Hojyo, S., Fukada, T., & Knutson, M. D. (2013) · Haematologica · doi:10.3324/haematol.2012.072314 · Cited by 170
The Regulation of Cellular Iron Metabolism
Chua, A. C. G., Graham, R. M., Trinder, D., & Olynyk, J. K. (2007) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701428257 · Cited by 172
ZRT/IRT-like Protein 14 (ZIP14) Promotes the Cellular Assimilation of Iron from Transferrin
Zhao, N., Gao, J., Enns, C. A., & Knutson, M. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143248 · Cited by 166
Skjørringe, T., Burkhart, A., Johnsen, K. B., & Moos, T. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00019 · Cited by 174
Steap Proteins: Implications for Iron and Copper Metabolism
Knutson, M. D. (2008) · Nutrition Reviews · doi:10.1111/j.1753-4887.2007.tb00311.x · Cited by 165
Absorption Mechanisms of Iron, Copper, and Zinc: An Overview
Nishito, Y., & Kambe, T. (2018) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.64.1 · Cited by 178
Intersection of Iron and Copper Metabolism in the Mammalian Intestine and Liver
Doğuer, Ç., Ha, J., & Collins, J. F. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170045 · Cited by 229
Iron transport proteins: Gateways of cellular and systemic iron homeostasis
Knutson, M. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.786632 · Cited by 178
Transferrin-Mediated Cellular Iron Delivery
Luck, A. N., & Mason, A. B. (2012) · Current topics in membranes · doi:10.1016/b978-0-12-394390-3.00001-x · Cited by 161
Ca2+ channel blockers reverse iron overload by a new mechanism via divalent metal transporter-1
Ludwiczek, S., Theurl, I., Muckenthaler, M. U., Jakab, M., Mair, S. M., Theurl, M., Kiss, J., Paulmichl, M., Hentze, M. W., Ritter, M., et al. (2007) · Nature Medicine · doi:10.1038/nm1542 · Cited by 160
Rose, P. P., Hanna, S. L., Spiridigliozzi, A., Wannissorn, N., Beiting, D. P., Ross, S. R., Hardy, R. W., Bambina, S., Heise, M. T., & Cherry, S. R. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.06.009 · Cited by 165
Shawki, A., Anthony, S., Nose, Y., Engevik, M. A., Niespodzany, E. J., Barrientos, T., Öhrvik, H., Worrell, R. T., Thiele, D. J., & Mackenzie, B. (2015) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00160.2015 · Cited by 164
Ng, S., Norwitz, S. G., & Norwitz, E. R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133283 · Cited by 166
Role of alcohol in the regulation of iron metabolism
Harrison-Findik, D. D. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i37.4925 · Cited by 156
Zhao, R., Min, S. H., Wang, Y., Puchulu‐Campanella, E., Low, P. S., & Goldman, I. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807665200 · Cited by 155
Hansen, J. B., Tonnesen, M., Madsen, A. N., Hagedorn, P., Friberg, J., Grunnet, L. G., Heller, R. S., Nielsen, A. Ø., Størling, J., Baeyens, L., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.09.001 · Cited by 162
Self-citationMammalian iron transporters: Families SLC11 and SLC40
Montalbetti, N., Simonin, A., Kovács, G., & Hediger, M. A. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.002 · Cited by 152
Iolascon, A., D’Apolito, M., Servedio, V., Cimmino, F., Piga, A. G., & Camaschella, C. (2005) · Blood · doi:10.1182/blood-2005-06-2477 · Cited by 144
Iron: the hard player in diabetes pathophysiology
Hansen, J. B., Moen, I. W., & Mandrup-Poulsen, T. R. (2014) · Acta Physiologica · doi:10.1111/apha.12256 · Cited by 146
A role for divalent metal transporter (DMT1) in mitochondrial uptake of iron and manganese
Wolff, N. A., Garrick, M. D., Zhao, L., Garrick, L. M., Ghio, A. J., & Thévenod, F. (2018) · Scientific Reports · doi:10.1038/s41598-017-18584-4 · Cited by 134
The genetics of essential metal homeostasis during development
Kambe, T., Weaver, B. P., & Andrews, G. K. (2008) · genesis · doi:10.1002/dvg.20382 · Cited by 140
McKie, A. T., & Simpson, R. J. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_6 · Cited by 133
Courville, P., Chaloupka, R., & Cellier, M. F. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-193 · Cited by 135
Beaumont, C. (2006) · Blood · doi:10.1182/blood-2005-10-4269 · Cited by 124
Comparative studies of duodenal and macrophage ferroportin proteins
Canonne-Hergaux, F., Donovan, A., Delaby, C., Wang, H.-J., & Gros, P. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00227.2005 · Cited by 124
Molecular Mediators Governing Iron-Copper Interactions
Güleç, Ş., & Collins, J. F. (2014) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071812-161215 · Cited by 122
Núñez, G., Sakamoto, K., & Soares, M. P. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800325 · Cited by 115
“Mammals acquire Fe from the diet via a mechanism assisted by the divalent metal transporter ion transporter 1 (DMT1) expressed by duodenum enterocytes (12, 13).”
BackgroundCopper and Iron Transport Across the Placenta: Regulation and Interactions
McArdle, H. J., Andersen, H. S., Jones, H. N., & Gambling, L. (2008) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2008.01658.x · Cited by 120
Placental iron transport: The mechanism and regulatory circuits
Sangkhae, V., & Nemeth, E. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.001 · Cited by 119
The gut in iron homeostasis: role of HIF-2 under normal and pathological conditions
Mastrogiannaki, M., Matak, P., & Peyssonnaux, C. (2013) · Blood · doi:10.1182/blood-2012-11-427765 · Cited by 116
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
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
Iron homeostasis in breast cancer
Marques, O., da Silva, B. M., Porto, G., & Lopes, C. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.01.029 · Cited by 115
Transferrin receptor 1-mediated iron uptake plays an essential role in hematopoiesis
Wang, S., He, X., Wu, Q., Jiang, L., Chen, L., Yu, Y., Zhang, P., Huang, X., Wang, J., Ju, Z., et al. (2019) · Haematologica · doi:10.3324/haematol.2019.224899 · Cited by 109
Metadata
- Authors
- Gunshin, H., Fujiwara, Y., Custodio, A. O., DiRenzo, C., Robine, S., & Andrews, N. C.
- Affiliations
- Boston Children's Hospital (US)
- Institut Curie (FR)
- Corresponding author
- Andrews, Nancy C.
- Venue
- Journal of Clinical Investigation
- Published
- 2005-04-21
- Volume
- 115
- Issue
- 5
- Pages
- 1258-1266
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W2135216513
- Cited by
- 419
- References
- 38
- Citations by year
- 2026: 9 · 2025: 18 · 2024: 16 · 2023: 20 · 2022: 21 · 2021: 15 · 2020: 14 · 2019: 17 · 2018: 19 · 2017: 17 · 2016: 17 · 2015: 12 · 2014: 25 · 2013: 33 · 2012: 23
- FWCI
- 14.62
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- American Gastroenterological Association
- National Institutes of Health (5k01dk002804-03)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK049216, R01 DK53813, K01 DK02804, P30 DK49216, R01DK053813)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P30HD018655, P30HD-18655)
- 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
- DMT1, ferroportin, intestinal iron absorption, erythropoiesis, placental iron transfer, hepatic iron deposition, iron transporters, hemochromatosis, HFE gene, knockout mice
- MeSH terms
- Solute Carrier Family 11, Member 2, Animals, Erythropoiesis, Female, Heterozygote, Homozygote, Intestine, Small, Iron, Liver, Mice, Transgenic, Placenta, Pregnancy, Promoter Regions, Genetic, Genes, Reporter, Integrases, Cation Transport Proteins, Iron-Binding Proteins, Mice
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.
