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Mammalian iron transport
Open accessAbstract
Iron is essential for basic cellular processes but is toxic when present in excess. Consequently, iron transport into and out of cells is tightly regulated. Most iron is delivered to cells bound to plasma transferrin via a process that involves transferrin receptor 1, divalent metal-ion transporter 1 and several other proteins. Non-transferrin-bound iron can also be taken up efficiently by cells, although the mechanism is poorly understood. Cells can divest themselves of iron via the iron export protein ferroportin in conjunction with an iron oxidase. The linking of an oxidoreductase to a membrane permease is a common theme in membrane iron transport. At the systemic level, iron transport is regulated by the liver-derived peptide hepcidin which acts on ferroportin to control iron release to the plasma.
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“During periods of high iron requirement, such as in iron deficiency or pregnancy, its levels are reduced to increase duodenal iron absorption and release from macrophages (Anderson and Vulpe, 2009).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Anderson and Vulpe, 2009
In the citing paper
“Transferrin transfers iron to cells through transferrin receptor 1 (TfR1) found on the surface of most body cells, and via transferrin receptor 2 (TfR2) expressed mainly in hepatocytes (Anderson and Vulpe, 2009; Caza and Kronstad, 2013).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Anderson and Vulpe, 2009
In the citing paper
“Transferrin-Transferrin receptor (TfR1) interaction triggers cell-mediated endocytosis of the complex and iron bound on transferrin dissociates within endosomes at a low pH (~5.5) since apotransferrin binds iron with a higher affinity at physiological pH relative to a low pH (Bali and Aisen, 1992; Anderson and Vulpe, 2009).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Anderson and Vulpe, 2009
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Cites
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,836
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
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
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
Identification of the haemoglobin scavenger receptor
Kristiansen, M., Graversen, J. H., Jacobsen, C., Sonne, O., Hoffman, H.-J., Law, S. K. A., & Moestrup, S. K. (2001) · Nature · doi:10.1038/35051594 · Cited by 1,712
Pigeon, C., Ilyin, G., Courselaud, B., Leroyer, P., Turlin, B., Brissot, P., & Loréal, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008923200 · Cited by 1,697
Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
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
Dysmetabolic Hyperferritinemia: All Iron Overload Is Not Hemochromatosis
Makker, J. S., Hanif, A., Bajantri, B., & Chilimuri, S. S. (2015) · Case Reports in Gastroenterology · doi:10.1159/000373883 · Cited by 1,353
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
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
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
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214
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
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
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
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084
Self-citationThe role of iron regulatory proteins in mammalian iron homeostasis and disease
Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055
Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026
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
C ERULOPLASMIN M ETABOLISM AND F UNCTION
Hellman, N. E., & Gitlin, J. D. (2002) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.22.012502.114457 · Cited by 954
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
LRP: a multifunctional scavenger and signaling receptor
Herz, J., & Strickland, D. K. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13992 · Cited by 908
LRP: a multifunctional scavenger and signaling receptor
Herz, J., & Strickland, D. K. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113992 · Cited by 908
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
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
Qiu, A., Jansen, M., Sakaris, A., Min, S. H., Chattopadhyay, S., Tsai, E., Sandoval, C., Zhao, R., Akabas, M. H., & Goldman, I. D. (2006) · Cell · doi:10.1016/j.cell.2006.09.041 · Cited by 847
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
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
BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism
Andriopoulos Jr, B., Corradini, E., Xia, Y., Faasse, S. A., Chen, S., Grgurevic, L., Knutson, M. D., Pietrangelo, A., Vukicevic, S., Lin, H. Y., et al. (2009) · Nature Genetics · doi:10.1038/ng.335 · Cited by 769
Identification of an Intestinal Heme Transporter
Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S., Laftah, A. H., Takeuchi, K., Halliday, N., Khan, Y., Warley, A., McCann, F. E., Hider, R. C., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.025 · Cited by 755
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
Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P., & Koenig, M. (2001) · Nature Genetics · doi:10.1038/84818 · Cited by 738
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
Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)
Peyssonnaux, C., Zinkernagel, A. S., Schuepbach, R. A., Rankin, E., Vaulont, S., Haase, V. H., Nizet, V., & Johnson, R. S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31370 · Cited by 639
Mitoferrin is essential for erythroid iron assimilation
Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624
Forging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623
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
Self-citationA role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
Wang, R.-H., Li, C., Xu, X., Zheng, Y., Xiao, C., Zerfas, P., Cooperman, S., Eckhaus, M., Rouault, T., Mishra, L., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.010 · Cited by 614
Binding of apotransferrin to K562 cells: explanation of the transferrin cycle.
Klausner, R. D., Ashwell, G., van Renswoude, J., Harford, J. B., & Bridges, K. R. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.8.2263 · Cited by 604
Stoichiometric and site characteristics of the binding of iron to human transferrin
Aisen, P., Leibman, A., & Zweier, J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62337-9 · Cited by 601
Lack of the bone morphogenetic protein BMP6 induces massive iron overload
Meynard, D., Kautz, L., Darnaud, V., Canonne-Hergaux, F., Coppin, H., & Roth, M.-P. (2009) · Nature Genetics · doi:10.1038/ng.320 · Cited by 587
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
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
Structure of the human transferrin receptor-transferrin complex
Cheng, Y., Zak, O., Aisen, P., Harrison, S. C., & Walz, T. (2004) · Cell · doi:10.1016/s0092-8674(04)00130-8 · Cited by 571
Targeted 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
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
A cytosolic iron chaperone that delivers iron to ferritin
Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536
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 Metabolism and the IRE/IRP Regulatory System: An Update
Pantopoulos, K. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.001 · Cited by 520
LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., et al. (2001) · Nature Genetics · doi:10.1038/84859 · Cited by 509
Biosynthesis of heme in mammals
Ajioka, R. S., Phillips, J. D., & Kushner, J. P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.005 · Cited by 493
Oudit, 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
Identification of the receptor scavenging hemopexin-heme complexes
Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473
The macrophage scavenger receptor CD163
Fabriek, B. O., Dijkstra, C. D., & van den Berg, T. K. (2005) · Immunobiology · doi:10.1016/j.imbio.2005.05.010 · Cited by 456
Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences
Crichton, R. (2001) · doi:10.1002/0470845791 · Cited by 453
CD163: a regulated hemoglobin scavenger receptor with a role in the anti‐inflammatory response
Moestrup, S. K., & Møller, H. J. (2004) · Annals of Medicine · doi:10.1080/07853890410033171 · Cited by 444
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
Iron–sulphur cluster biogenesis and mitochondrial iron homeostasis
Rouault, T. A., & Tong, W.-H. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1620 · Cited by 432
Gruenheid, S., Pinner, E., Desjardins, M., & Gros, P. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.4.717 · Cited by 428
Hemopexin: structure, function, and regulation
Tolosano, E., & Altruda, F. (2002) · DNA and Cell Biology · doi:10.1089/104454902753759717 · Cited by 426
Identification of a Human Heme Exporter that Is Essential for Erythropoiesis
Quigley, J. G., Yang, Z., Worthington, M., Phillips, J. D., Sabo, K. M., Sabath, D. E., Berg, C. L., Sassa, S., Wood, B. L., & Abkowitz, J. L. (2004) · Cell · doi:10.1016/j.cell.2004.08.014 · Cited by 423
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
Flemming (1998) · Medical Entomology and Zoology · Cited by 412
Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408
A Heme Export Protein Is Required for Red Blood Cell Differentiation and Iron Homeostasis
Keel, S. B., Doty, R. T., Yang, Z., Quigley, J. G., Chen, J., Knoblaugh, S., Kingsley, P. D., De Domenico, I., Vaughn, M. B., Kaplan, J., et al. (2008) · Science · doi:10.1126/science.1151133 · Cited by 404
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 399
Hepcidin—a regulator of intestinal iron absorption and iron recycling by macrophages
GANZ, T. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.08.020 · Cited by 393
Identification of a hypoxia response element in the transferrin receptor gene
Lok, C. N., & Ponka, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24147 · Cited by 380
Transferrin Receptor Induction by Hypoxia
Tacchini, L., Bianchi, L., Bernelli-Zazzera, A., & Cairo, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24142 · Cited by 379
Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377
(2004) · ASM Press eBooks · doi:10.1128/9781555816544 · Cited by 369
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
The role of ceruloplasmin in iron metabolism.
Roeser, H. P., Lee, G. R., Nacht, S., & Cartwright, G. E. (1970) · Journal of Clinical Investigation · doi:10.1172/jci106460 · Cited by 365
Iron-Sulfur Protein Biogenesis in Eukaryotes: Components and Mechanisms
Lill, R., & Mühlenhoff, U. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104538 · Cited by 365
Paradkar, P. N., Zumbrennen, K. B., Paw, B. H., Ward, D. M., & Kaplan, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01685-08 · Cited by 362
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
ROLE OF ABCG2/BCRP IN BIOLOGY AND MEDICINE
Krishnamurthy, P., & Schuetz, J. D. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141238 · Cited by 357
De Domenico, I., Ward, D. M., di Patti, M. C. B., Jeong, S. Y., David, S., Musci, G., & Kaplan, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601735 · Cited by 350
Aisen, P. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.007 · Cited by 345
Hepcidin: from discovery to differential diagnosis
Kemna, E., Tjalsma, H., Willems, H. L., & Swinkels, D. W. (2007) · Haematologica · doi:10.3324/haematol.11705 · Cited by 318
Crystal Structure of the Ectodomain of Human Transferrin Receptor
Lawrence, C. M., Ray, S., Babyonyshev, M., Galluser, R., Borhani, D. W., & Harrison, S. C. (1999) · Science · doi:10.1126/science.286.5440.779 · Cited by 315
Intracellular Copper Transport in Mammals
Prohaska, J. R., & Gybina, A. A. (2004) · Journal of Nutrition · doi:10.1093/jn/134.5.1003 · Cited by 307
Iron-dependent regulation of the divalent metal ion transporter
Gunshin, H., Allerson, C. R., Polycarpou-Schwarz, M., Rofts, A., Rogers, J. T., Kishi, F., Hentze, M. W., Rouault, T. A., Andrews, N. C., & Hediger, M. A. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03189-1 · Cited by 305
Genetic Evidence that Ferric Reductase Is Required for Iron Uptake in Saccharomyces cerevisiae
Dancis, A., Klausner, R. D., Hinnebusch, A. G., & Barriocanal, J. G. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.5.2294-2301.1990 · Cited by 304
Iron trafficking in the mitochondrion: novel pathways revealed by disease
Napier, I. A., Ponka, P., & Richardson, D. R. (2004) · Blood · doi:10.1182/blood-2004-10-3856 · Cited by 291
Bekri, S., Kispál, G., Lange, H., Fitzsimons, E. J., Tolmie, J., Lill, R., & Bishop, D. F. (2000) · Blood · doi:10.1182/blood.v96.9.3256 · Cited by 281
Decreased Liver Hepcidin Expression in the Hfe Knockout Mouse
Ahmad, K. A., Ahmann, J. R., Migas, M. C., Waheed, A., Britton, R. S., Bacon, B. R., Sly, W. S., & Fleming, R. E. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0575 · Cited by 276
Direct interorganellar transfer of iron from endosome to mitochondrion
Sheftel, A. D., Zhang, A., Brown, C. M., Shirihai, O. S., & Ponka, P. (2007) · Blood · doi:10.1182/blood-2007-01-068148 · Cited by 274
Fleming, R. E., Migas, M. C., Holden, C. C., Waheed, A., Britton, R. S., Tomatsu, S., Bacon, B. R., & Sly, W. S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040548097 · Cited by 273
The role of transporters in cellular heme and porphyrin homeostasis
Krishnamurthy, P. C., Xie, T., & Schuetz, J. D. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.02.001 · Cited by 268
Craven, C. M., Alexander, J., Eldridge, M., Kushner, J. P., Bernstein, S., & Kaplan, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3457 · Cited by 259
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
Sec15 Is an Effector for the Rab11 GTPase in Mammalian Cells
Zhang, X.-M., Ellis, S., Sriratana, A., Mitchell, C. A., & Rowe, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402264200 · Cited by 257
Mammalian Tissue Oxygen Levels Modulate Iron-Regulatory Protein Activities in Vivo
Meyron‐Holtz, E. G., Ghosh, M. C., & Rouault, T. A. (2004) · Science · doi:10.1126/science.1103786 · Cited by 250
Targeted mutagenesis of the murine transferrin receptor-2 gene produces hemochromatosis
Fleming, R. E., Ahmann, J. R., Migas, M. C., Waheed, A., Koeffler, H. P., Kawabata, H., Britton, R. S., Bacon, B. R., & Sly, W. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162360699 · Cited by 247
Response to Iron Deprivation in Saccharomyces cerevisiae
Philpott, C. C., & Protchenko, O. (2008) · Eukaryotic Cell · doi:10.1128/ec.00354-07 · Cited by 246
Inorganic Biochemistry of Iron Metabolism: From Molecular Mechanisms to Clinical Consequences
Crichton, R. R. (2001) · Cited by 244
MDB: the Metalloprotein Database and Browser at The Scripps Research Institute
Castagnetto, J. M. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.379 · Cited by 236
Trinder, D., Oates, P. S., Thomas, C., Sadleir, J., & Morgan, E. H. (2000) · Gut · doi:10.1136/gut.46.2.270 · Cited by 231
Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 224
Bernstein, S. E. (1987) · PubMed · Cited by 222
TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis
Chen, T. T., Li, L., Chung, D.-H., Allen, C. D. C., Torti, S. V., Torti, F. M., Cyster, J. G., Chen, C.-Y., Brodsky, F. M., Niemi, E. C., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042433 · Cited by 219
Natural-resistance-associated macrophage protein 1 is an H+/bivalent cation antiporter
GOSWAMI, T., BHATTACHARJEE, A., BABAL, P., SEARLE, S., MOORE, E., LI, M., & BLACKWELL, J. M. (2001) · Biochemical Journal · doi:10.1042/bj3540511 · Cited by 218
Role of the hypoxia inducible factors HIF in iron metabolism
Peyssonnaux, C., Nizet, V., & Johnson, R. S. (2008) · Cell Cycle · doi:10.4161/cc.7.1.5145 · Cited by 217
Increased Susceptibility in Hp Knockout Mice During Acute Hemolysis
Lim, S. K., Kim, H., Lim, S. K., bin Ali, A., Lim, Y. K., Wang, Y., Chong, S. M., Costantini, F. D., & Baumman, H. (1998) · Blood · doi:10.1182/blood.v92.6.1870 · Cited by 215
Pondarré, C., Antiochos, B., Campagna, D. R., Clarke, S. L., Greer, E. L., Deck, K. M., McDonald, A. A., Han, A., Medlock, A. E., Kutok, J. L., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl012 · Cited by 212
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
The orchestration of body iron intake: how and where do enterocytes receive their cues?
Frazer, D. M., & Anderson, G. J. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00039-1 · Cited by 211
Self-citationHaptoglobin: function and polymorphism.
Wassell, J. (2000) · PubMed · Cited by 204
Melefors, Ö., Goossen, B., Johansson, H. E., Stripecke, R., Gray, N. K., & Hentze, M. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53414-1 · Cited by 200
Characterization of non-transferrin-bound iron clearance by rat liver.
Wright, T. L., Brissot, P., L, W., & Weisiger, R. A. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67473-3 · Cited by 196
Hepcidin excess induces the sequestration of iron and exacerbates tumor-associated anemia
Rivera, S., Liu, L., Nemeth, E., Gabayan, V., Sorensen, O. E., & Ganz, T. (2005) · Blood · doi:10.1182/blood-2004-08-3375 · Cited by 196
Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195
The role of transferrin in the mechanism of cellular iron uptake
Thorstensen, K., & Romslo, I. (1990) · Biochemical Journal · doi:10.1042/bj2710001 · Cited by 194
Picard, V., Govoni, G. R., Jabado, N., & Gros, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005387200 · 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
Cellular regulation and molecular interactions of the ferritins
Hintze, K. J., & Theil, E. C. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5285-y · Cited by 184
A new role for the transferrin receptor in the release of iron from transferrin
Bali, P. K., Zak, O., & Aisen, P. (1991) · Biochemistry · doi:10.1021/bi00216a003 · Cited by 182
Breuer, W., Shvartsman, M., & Cabantchik, Z. I. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.010 · Cited by 175
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
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
Transferrin receptors and iron uptake during erythroid cell development
Iacopetta, B. J., Morgan, E. H., & Yeoh, G. C. (1982) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(82)90547-8 · Cited by 164
Koorts, A. M., & Viljoen, M. (2007) · Archives of Physiology and Biochemistry · doi:10.1080/13813450701318583 · Cited by 164
Unexpected role of ceruloplasmin in intestinal iron absorption
Cherukuri, S., Potla, R., Sarkar, J., Nurko, S., Harris, Z. L., & Fox, P. L. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.003 · Cited by 163
Modification of iron regulation by the inflammatory response
WEISS, G. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.09.001 · Cited by 161
Aceruloplasminemia: An Inherited Neurodegenerative Disease with Impairment of Iron Homeostasis
XU, X., PIN, S., GATHINJI, M., FUCHS, R., & HARRIS, Z. L. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.024 · Cited by 160
Molecular and Cellular Iron Transport
(2002) · CRC Press eBooks · doi:10.1201/9780824744175.fmatt1 · Cited by 150
Defective Recovery and Severe Renal Damage After Acute Hemolysis in Hemopexin-Deficient Mice
Tolosano, E., Hirsch, E., Patrucco, E., Camaschella, C., Navone, R., Silengo, L., & Altruda, F. (1999) · Blood · doi:10.1182/blood.v94.11.3906 · Cited by 149
The Heme Oxygenase System: Update 2005
Maines, M. D. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1761 · Cited by 146
Crusade for iron: iron uptake in unicellular eukaryotes and its significance for virulence
Šuťák, R., Lesuisse, E., Tachezy, J., & Richardson, D. R. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.03.005 · Cited by 145
Foot, N. J., Dalton, H. E., Shearwin-Whyatt, L. M., Dorstyn, L., Tan, S.-S., Yang, B., & Kumar, S. (2008) · Blood · doi:10.1182/blood-2008-04-150953 · Cited by 143
Domenico, I. D., Lo, E., Ward, D. M., & Kaplan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900453106 · Cited by 143
Sibille, J., Kondo, H. G., & Aisen, P. (1988) · Hepatology · doi:10.1002/hep.1840080218 · Cited by 139
Nature of nontransferrin‐bound iron
Hider, R. C. (2002) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2002.0320s1050.x · Cited by 139
The Macrophage Cell Surface Glyceraldehyde-3-phosphate Dehydrogenase Is a Novel Transferrin Receptor
Raje, C. I., Kumar, S., Harle, A. S., Nanda, J. S., & Raje, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608328200 · Cited by 139
Anderson, G. J., & Frazer, D. M. (2005) · Seminars in Liver Disease · doi:10.1055/s-2005-923314 · Cited by 138
Self-citationFrazer, D. M., Vulpe, C. D., McKie, A. T., Wilkins, S. J., Trinder, D., Cleghorn, G. J., & Anderson, G. J. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.4.g931 · Cited by 137
Self-citationCourville, P., Chaloupka, R., & Cellier, M. F. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-193 · Cited by 134
Sendamarai, A. K., Ohgami, R. S., Fleming, M. D., & Lawrence, C. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801318105 · Cited by 134
Pietrangelo, A. (2004) · Hepatology · doi:10.1002/hep.20007 · Cited by 128
Randell, E. W., Parkes, J. G., Olivieri, N. F., & Templeton, D. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33971-6 · Cited by 127
Iron-regulatory proteins: molecular biology and pathophysiological implications
Cairo, G., & Recalcati, S. (2007) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399407000531 · Cited by 124
Mims, M. P., & Prchal, J. T. (2005) · Hematology · doi:10.1080/10245330500093419 · Cited by 123
Investigation of a role for reduction in ferric iron uptake by mouse duodenum
Raja, K. B., Simpson, R. J., & Peters, T. J. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(92)90129-y · Cited by 121
Ceruloplasmin/hephaestin knockout mice model morphologic and molecular features of AMD
Hadziahmetovic, M., Dentchev, T., Song, Y., Haddad, N., He, X., Hahn, P., Pratico, D., Wen, R., Harris, Z. L., Lambris, J. D., et al. (2008) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.07-1472 · Cited by 121
The Testicular Iron Shuttle: A “Nurse” Function of the Sertoli Cells
Sylvester, S. R., & Griswold, M. D. (1994) · Journal of Andrology · doi:10.1002/j.1939-4640.1994.tb00468.x · Cited by 120
Iron accumulation in the liver of male patients with Wilson's disease
Shiono, Y., Wakusawa, S., Hayashi, H., Takikawa, T., Yano, M., Okada, T., Mabuchi, H., Kono, S., & Miyajima, H. (2001) · The American Journal of Gastroenterology · doi:10.1111/j.1572-0241.2001.05269.x · Cited by 120
Copper 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
Studies on familial hypotransferrinemia: unique clinical course and molecular pathology.
Hayashi, A., Wada, Y., Suzuki, T., & Shimizu, A. (1993) · Europe PMC (PubMed Central) · Cited by 117
Thorstensen, K., & Romslo, I. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68384-x · 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
Recent advances in mammalian haem transport
Latunde-Dada, G. O., Simpson, R. J., & McKie, A. T. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.005 · Cited by 113
Tchernitchko, D., Bourgeois, M., Martin, M., & Beaumont, C. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630449 · Cited by 111
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
Self-citationIRON AND PROTEIN KINETICS STUDIED BY MEANS OF DOUBLY LABELED HUMAN CRYSTALLINE TRANSFERRIN*
Katz, J. H. (1961) · Journal of Clinical Investigation · doi:10.1172/jci104440 · Cited by 108
Rice, A. E., Mendez, M. J., Hokanson, C. A., Rees, D. C., & Björkman, P. J. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.063 · Cited by 102
Pietrangelo, A. (2005) · Seminars in Liver Disease · doi:10.1055/s-2005-923316 · Cited by 102
Johnson, M. B., Chen, J., Murchison, N., Green, F. A., & Enns, C. A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0798 · Cited by 102
Wilson, M. T., & Reeder, B. J. (2007) · Experimental Physiology · doi:10.1113/expphysiol.2007.039735 · 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
Wallace, D. F. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4690 · Cited by 101
A mutation in Sec15l1 causes anemia in hemoglobin deficit (hbd) mice
Lim, J. E., Jin, O., Bennett, C. M., Morgan, K. J., Wang, F., Trenor, C. C., Fleming, M. D., & Andrews, N. C. (2005) · Nature Genetics · doi:10.1038/ng1659 · Cited by 99
Deaglio, 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 94
Transferrin binding and iron uptake in mouse hepatocytes
Cole, E. S., & Glass, J. (1983) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(83)90122-2 · Cited by 93
Millard, K. N., Frazer, D. M., Wilkins, S. J., & Anderson, G. J. (2004) · Gut · doi:10.1136/gut.2003.031153 · Cited by 93
Self-citationCasey, J. L., Jeso, B. D., Rao, K., Klausner, R. D., & Harford, J. B. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.6.1787 · Cited by 92
Trinder, D. (1996) · Hepatology · doi:10.1053/jhep.1996.v23.pm0008675172 · Cited by 91
Jordan, I., & Kaplan, J. (1994) · Biochemical Journal · doi:10.1042/bj3020875 · Cited by 88
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
Trinder, D., Zak, O., & Aisen, P. (1996) · Hepatology · doi:10.1002/hep.510230631 · Cited by 84
Pandolfo, M. (2003) · Seminars in Pediatric Neurology · doi:10.1016/s1071-9091(03)00025-1 · Cited by 81
Anemia of the Belgrade rat: evidence for defective membrane transport of iron
Bowen, B., & Morgan, E. (1987) · Blood · doi:10.1182/blood.v70.1.38.38 · Cited by 79
Friedreich's Ataxia: From Disease Mechanisms to Therapeutic Interventions
Lodi, R., Tonon, C., Calabrese, V., & Schapira, A. H. V. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.438 · Cited by 79
Molecular and Cellular Iron Transport
Templeton, D. M. (2002) · CRC Press eBooks · doi:10.1201/9780824744175 · Cited by 78
nm1054: a spontaneous, recessive, hypochromic, microcytic anemia mutation in the mouse
Ohgami, R. S., Campagna, D. R., Antiochos, B., Wood, E., Sharp, J. J., Barker, J. E., & Fleming, M. D. (2005) · Blood · doi:10.1182/blood-2005-01-0379 · Cited by 74
Mok, H., Jelinek, J., Pai, S., Cattanach, B. M., Prchal, J. T., Youssoufian, H., & Schumacher, A. (2004) · Development · doi:10.1242/dev.01081 · Cited by 73
Genetic variation in Mon1a affects protein trafficking and modifies macrophage iron loading in mice
Wang, F., Paradkar, P. N., Custodio, Á. O., Ward, D. M., Fleming, M. D., Campagna, D. R., Roberts, K. A., Boyartchuk, V., Dietrich, W. F., Kaplan, J., et al. (2007) · Nature Genetics · doi:10.1038/ng2059 · Cited by 72
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
Regulation of Transferrin Function and Expression: Review and Update
Lok, C., & Loh, T. T. (1998) · Neurosignals · doi:10.1159/000014542 · Cited by 72
Lam-Yuk-Tseung, S., & Gros, P. (2006) · Biochemistry · doi:10.1021/bi052307m · Cited by 72
Inman, R. S., Coughlan, M. M., & Wessling-Resnick, M. (1994) · Biochemistry · doi:10.1021/bi00205a022 · Cited by 70
Regulation of transferrin gene expression
Zakin, M. M. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.14.1426763 · Cited by 67
Chapter 6 Iron Homeostasis and Erythropoiesis
Wrighting, D. M., & Andrews, N. C. (2008) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(07)00006-3 · Cited by 59
The mechanisms of iron uptake by fetal rat hepatocytes in culture
Trinder, D., Morgan, E. H., & Baker, E. (1986) · Hepatology · doi:10.1002/hep.1840060508 · Cited by 58
Ultrastructural sequences during liver iron overload in genetic hemochromatosis
Iancu, T. C., Deugnier, Y., Halliday, J. W., Powell, L. W., & Brissot, P. (1997) · Journal of Hepatology · doi:10.1016/s0168-8278(97)80079-7 · Cited by 57
Wilkins, S. J., Frazer, D. M., Millard, K. N., McLaren, G. D., & Anderson, G. J. (2005) · Blood · doi:10.1182/blood-2005-07-2614 · Cited by 56
Self-citationNramp1 equips macrophages for efficient iron recycling
Soe-Lin, S., Sheftel, A. D., Wasyluk, B., & Ponka, P. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.02.013 · Cited by 56
Uptake and subcellular processing of 59Fe-125I-labelled transferrin by rat liver
Morgan, E. H., Smith, G. D., & Peters, T. J. (1986) · Biochemical Journal · doi:10.1042/bj2370163 · Cited by 50
Pathogenesis of hereditary hemochromatosis
Fleming, R. E., Britton, R. S., Waheed, A., Sly, W. S., & Bacon, B. R. (2004) · Clinics in Liver Disease · doi:10.1016/j.cld.2004.06.004 · Cited by 48
The endocytosis of transferrin by rat intestinal epithelial cells
Anderson, G. J., Powell, L. W., & Halliday, J. W. (1994) · Gastroenterology · doi:10.1016/0016-5085(94)90600-9 · Cited by 45
Self-citationRobb, A., Ericsson, M., & Wessling‐Resnick, M. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00337.2004 · Cited by 45
The anemia of “haemoglobin-deficit” (hbd/hbd) mice is caused by a defect in transferrin cycling
Zhang, A., Sheftel, A. D., & Ponka, P. (2006) · Experimental Hematology · doi:10.1016/j.exphem.2006.02.004 · Cited by 44
Trinder, D., Morgan, E. H., & Baker, E. (1988) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(88)90375-6 · Cited by 44
White, R. A., Boydston, L. A., Brookshier, T. R., McNulty, S. G., Nsumu, N. N., Brewer, B. P., & Blackmore, K. (2005) · Genomics · doi:10.1016/j.ygeno.2005.09.015 · Cited by 42
Oshiro, S., Nakajima, H., Markello, T. C., Krasnewich, D. M., Bernardini, I. M., & Gahl, W. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80581-x · Cited by 41
Watkins, J. A., Altazan, J. D., Elder, P., Li, C. Y., Núñez, M. T., Cui, X. X., & Glass, J. (1992) · Biochemistry · doi:10.1021/bi00140a018 · Cited by 40
Effects of Cell Proliferation on the Uptake of Transferrin–Bound Iron by Human Hepatoma Cells
Lee, A. W. M., Oates, P. S., & Trinder, D. (2003) · Hepatology · doi:10.1053/jhep.2003.50422 · Cited by 38
Iron metabolism meets signal transduction
Anderson, G. J., & Frazer, D. M. (2006) · Nature Genetics · doi:10.1038/ng0506-503 · Cited by 37
Self-citationCharacterization of transferrin binding and specificity of the placental transferrin receptor
Tsunoo, H., & Sussman, H. H. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90005-x · Cited by 35
Research works printed but not linked: 1
- MacGillivray RTA, Mason AB (2001) Transferrins. In: Templeton DM (ed) Molecular and cellular iron transport. Marcel Dekker, New York, pp 41–69
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Metadata
- Authors
- Anderson, G. J., & Vulpe, C. D.
- Affiliations
- QIMR Berghofer Medical Research Institute (AU)
- Corresponding author
- Anderson, Gregory Jon
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2009-05-31
- Volume
- 66
- Issue
- 20
- Pages
- 3241-3261
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11115736
- OpenAlex
- W1981407334
- Cited by
- 317
- References
- 217
- Citations by year
- 2026: 6 · 2025: 25 · 2024: 21 · 2023: 21 · 2022: 24 · 2021: 17 · 2020: 14 · 2019: 18 · 2018: 16 · 2017: 14 · 2016: 9 · 2015: 16 · 2014: 20 · 2013: 23 · 2012: 33
- FWCI
- 3.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- iron transport, transferrin, transferrin receptor 1, DMT1, ferroportin, hepcidin, non-transferrin-bound iron, iron export, iron homeostasis, membrane transporters
- MeSH terms
- Animals, Biological Transport, Carrier Proteins, Gene Expression Regulation, Homeostasis, Iron, Macrophages, Mammals, Mitochondria, Models, Biological, Oxidoreductases, Hepatocytes, Antimicrobial Cationic Peptides, Erythroid Cells, Hepcidins
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 ›
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