The DOI matches its Crossref record; 25 of the 26 references it cites were found in a registry or an index.
An Iron-Regulated Ferric Reductase Associated with the Absorption of Dietary Iron
Abstract
The ability of intestinal mucosa to absorb dietary ferric iron is attributed to the presence of a brush-border membrane reductase activity that displays adaptive responses to iron status. We have isolated a complementary DNA, Dcytb (for duodenal cytochrome b), which encoded a putative plasma membrane di-heme protein in mouse duodenal mucosa. Dcytb shared between 45 and 50% similarity to the cytochrome b561 family of plasma membrane reductases, was highly expressed in the brush-border membrane of duodenal enterocytes, and induced ferric reductase activity when expressed in Xenopus oocytes and cultured cells. Duodenal expression levels of Dcytb messenger RNA and protein were regulated by changes in physiological modulators of iron absorption. Thus, Dcytb provides an important element in the iron absorption pathway.
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
“Iron homeostasis and bioavailability to either the host or invading pathogens is tightly regulated through coordination of hepcidin, iron binding proteins and several enzymes involved in iron metabolism (McKie et al., 2001; Nemeth et al., 2004).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as McKie et al., 2001
In the citing paper
“The uptake of ionic NHI in contrast, is a sequential process that is well characterized: Following the reduction of ferric iron by DCYTB (for duodenal cytochrome B) at the luminal surface of enterocytes (ENT), it is DMT1 (for divalent metal transporter-1) that imports iron into the cytoplasm (Gunshin et al., 1997;McKie et al., 2001).”
From Iron in infection and immunity (2020) · cites this paper as McKie et al., 2001
In the citing paper
“When systemic iron levels in the blood stream are low, expression of DMT1 (divalent metal transporter 1, also called NRAMP2 as well as SLC11A2) and DcytB (duodenal membrane associated cytochrome-b) ferrireductase increases on the surface of intestinal enterocytes on the luminal side enabling the reduction of Fe3+ into its ferrous form (Fe2+) which can then be taken up by DMT1 (McKie et al., 2001).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as McKie et al., 2001
In the citing paper
“At either location, Dmt1 only accepts ferrous iron along with other divalent cations, such as copper or manganese, and co-localizes with an iron reductase [152, 177].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [152]
In the citing paper
“To overcome the low availability of Fe2+, duodenal cytochrome b (DCYTB) enzymes that are present within the apical membrane of enterocytes are able to reduce any soluble Fe3+ to Fe2+ before DMT1‐mediated Fe2+ import. 14 , 15”
From The battle for iron in enteric infections (2020) · cites this paper as [14]
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 [14]
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 [13]
In the citing paper
“It must be reduced to ferrous (Fe 2ϩ ) iron, either chemically or through the action of a brush border ferrireductase such as duodenal cytochrome B (CYBRD1, also known as DCYTB), a cytochrome B561 homolog that may use ascorbic acid as a cofactor.53”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [53]
In the citing paper
“CYBRD1 was one of 2 iron transport-related molecules discovered by McKie through a very productive RNA subtraction approach.53,54”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [53]
In the citing paper
“IRP1-knockout mice survived with insignificant effects on iron homeostasis in kidney and brown fat that highly express IRP1 (55, 200).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [200]
In the citing paper
“IRP2-knockout mice showed abnormal induction of ferritin expression, resulting in iron misregulation in intestinal mucosa and the CNS (55, 200).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [200]
In the citing paper
“IRP2 was also sensitive to iron levels, whereas IRP1 was not, suggesting that IRP2 is the predominant posttranscriptional regulator of key genes involved iron homeostasis (200).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [200]
In the citing paper
“IRP2 was also sensitive to iron levels, whereas IRP1 was not, suggesting that IRP2 is the predominant posttranscriptional regulator of key genes involved iron homeostasis (200).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [200]
In the citing paper
“IRP1-knockout mice misregulate iron in specific tissues, namely in brown fat and kidney, whereas IRP2-knockout mice exhibit aberrant management of iron in multiple tissues.”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [200]
Citations
Cites
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
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-citationMcKie, 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
Self-citationA ferric-chelate reductase for iron uptake from soils
Robinson, N. J., Procter, C. M., Connolly, E. L., & Guerinot, M. L. (1999) · Nature · doi:10.1038/17800 · Cited by 1,271
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
Dancis, A., Roman, D. G., Anderson, G. J., Hinnebusch, A. G., & Klausner, R. D. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.9.3869 · Cited by 358
Identification and characterization of a second mouse Nramp gene
Gruenheid, S., Cellier, M. F., Vidal, S. M., & Gros, P. (1995) · Genomics · doi:10.1016/0888-7543(95)80053-o · Cited by 287
Georgatsou, E., & Alexandraki, D. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.5.3065-3073.1994 · Cited by 233
Trinder, D., Oates, P. S., Thomas, C., Sadleir, J., & Morgan, E. H. (2000) · Gut · doi:10.1136/gut.46.2.270 · Cited by 231
Crystal, R. G. (1997) · Nature Medicine · doi:10.1038/nm0497-383 · Cited by 204
Research works printed but not linked: 5
- Male mice (6 to 9 weeks old) of the CD-1 strain were used for experimental manipulations of iron status. Hypoxia iron deficiency and iron loading were carried out as described previously (10). Hypotransferrinemic mice were bred and maintained as described previously (16). Animal procedures were approved by the U.K. Home Office. Total RNA was extracted from tissues and Northern blotting was carried out as previously described (10). The above-described 114-bp fragment of Dcytb was used as the probe. We carried out reverse transcription on 10 μg of total RNA from each tissue using 100 U of Superscript II (Gibco) and 100 nM random hexamers (Pharmacia) and following the manufacturer's instructions. PCR was performed in a PTC 200 thermal cycler (MJ Research Waltham MA) with 0.5 U of Taq polymerase (Supertaq HT Biotechnology Cambridge) 200 μM deoxynucleoside triphosphate (Fermentas Hanover MD) and gene-specific primers (sequences available on request) at a concentration of 10 μM. Products were compared after 20 25 and 30 cycles. The products shown in Fig. 2D are after 20 [GAPDH (glyceraldehyde phosphate dehydrogenase) and Dcytb] and 30 cycles (gp91- phox ). The data shown were reproducible in independent experiments on individual mice from each group. In situ hybridizations were carried out as previously described (10).
- Simpson R. J., J. Nutr. 126, 1858 (1996).
- Simpson R. J., et al., Clin. Sci. 96, 16P (1999).
- Georgatsou E., Alexandraki D., Mol. Cell. Biol. 14, 3065 (1994).
- Roman D. G., et al., Mol. Cell. Biol. 13, 4342 (1993).
Cited by
Sorted by citations
Items 201–300 of 998
Lesjak, M. M., Hoque, R., Balesaria, S., Skinner, V. O., Debnam, E. S., Srai, S. K., & Sharp, P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102900 · Cited by 112
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-citationDupic, F., Fruchon, S., Bensaid, M., Loréal, O., Brissot, P., Borot, N., Roth, M., & Coppin, H. (2002) · Gut · doi:10.1136/gut.51.5.648 · Cited by 115
The Multifaceted Regulation of Mitochondria in Ferroptosis
Wu, H., Wang, F., Ta, N., Zhang, T., & Gao, W. (2021) · Life · doi:10.3390/life11030222 · Cited by 111
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 116
Ji, C., & Kosman, D. J. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13040 · Cited by 109
Role of iron in the pathogenesis of respiratory disease
Ali, M. K., Kim, R., Karim, R., Mayall, J., Martin, K. L., Shahandeh, A., Abbasian, F., Starkey, M. R., Loustaud-Ratti, V., Johnstone, D. M., et al. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.05.003 · Cited by 114
The Involvement of a Multicopper Oxidase in Iron Uptake by the Green Algae Chlamydomonas reinhardtii
Herbik, A., Bölling, C., & Buckhout, T. J. (2002) · PLANT PHYSIOLOGY · doi:10.1104/pp.013060 · Cited by 109
Frazer, D. M., Inglis, H. R., Wilkins, S. J., Millard, K. N., Steele, T. M., McLaren, G. D., McKie, A. T., Vulpe, C. D., & Anderson, G. J. (2004) · Gut · doi:10.1136/gut.2003.037416 · Cited by 109
Self-citationThe iron cycle and oxidative stress in the lung
Turi, J. L., Yang, F., Garrick, M. D., Piantadosi, C. A., & Ghio, A. J. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.12.008 · Cited by 111
Molecular and Functional Roles of Duodenal Cytochrome B (Dcytb) in Iron Metabolism
Latunde-Dada, G. O., der Westhuizen, J. V., Vulpe, C. D., Anderson, G. J., Simpson, R. J., & McKie, A. T. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0574 · Cited by 107
Self-citationMetal transporters and disease
Andrews, N. C. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00307-1 · Cited by 110
The zebrafish mutant gene chardonnay (cdy) encodes divalent metal transporter 1 (DMT1).
Donovan, A. (2002) · Blood · doi:10.1182/blood-2002-04-1169 · Cited by 106
Cellular and mitochondrial iron homeostasis in vertebrates
Chen, C., & Paw, B. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.003 · Cited by 111
Prebiotics and Iron Bioavailability—Is There a Connection?
Yeung, C. K., Glahn, R. E., Welch, R. M., & Miller, D. D. (2005) · Journal of Food Science · doi:10.1111/j.1365-2621.2005.tb09984.x · Cited by 105
Rychtarcikova, Z., Lettlova, S., Tomkova, V., Korenkova, V., Langerova, L., Simonova, E., Zjablovskaja, P., Alberich-Jorda, M., Neuzil, J., & Truksa, J. (2017) · Oncotarget · doi:10.18632/oncotarget.14093 · Cited by 100
Evaluating Shigella flexneri Pathogenesis in the Human Enteroid Model
Ranganathan, S., Doucet, M., Grassel, C. L., Delaine-Elias, B., Zachos, N. C., & Barry, E. M. (2019) · Infection and Immunity · doi:10.1128/iai.00740-18 · Cited by 105
Identification of a Steap3 endosomal targeting motif essential for normal iron metabolism
Lambe, T., Simpson, R. J., Dawson, S., Bouriez‐Jones, T., Crockford, T. L., Lepherd, M. L., Latunde-Dada, G. O., Robinson, H., Raja, K. B., Campagna, D. R., et al. (2008) · Blood · doi:10.1182/blood-2007-11-120402 · Cited by 103
Self-citationAnemia of Chronic Diseases: Wider Diagnostics—Better Treatment?
Wiciński, M., Liczner, G., Cadelski, K., Kołnierzak, T., Nowaczewska, M., & Malinowski, B. (2020) · Nutrients · doi:10.3390/nu12061784 · Cited by 122
Molecular control of iron metabolism
Andrews, N. C. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.10.004 · Cited by 109
Iron absorption and iron status are reduced after Roux-en-Y gastric bypass
Manuel Ruz, O., Fernando Carrasco, N., Rojas, P., Codoceo, J., Inostroza, J., Annabella Rebolledo, A., Basfi-fer, K., Csendes, A., Papapietro, K., Pizarro, F., et al. (2009) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2009.27699 · Cited by 103
Regulation of iron pathways in response to hypoxia
Chepelev, N. L., & Willmore, W. G. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.023 · Cited by 106
The role of Dcytb in iron metabolism: an update
McKie, A. T. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361239 · Cited by 101
Self-citationDoes Ceruloplasmin Defend Against Neurodegenerative Diseases?
Wang, B., & Wang, X. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180508113025 · Cited by 104
Hereditary Causes of Disturbed Iron Homeostasis in the Central Nervous System
Ponka, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.022 · Cited by 99
Dupic, F., Fruchon, S., Bensaid, M., Borot, N., Radosavljevic, M., Loreal, O., Brissot, P., Gilfillan, S., Bahram, S., Coppin, H., et al. (2002) · Gastroenterology · doi:10.1053/gast.2002.31877 · Cited by 99
McCarthy, R. C., & Kosman, D. J. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00031 · Cited by 100
Intestinal HIF2α promotes tissue-iron accumulation in disorders of iron overload with anemia
Anderson, E. R., Taylor, M. J., Xue, X., Ramakrishnan, S. K., Martin, A. S., Xie, L., Bredell, B. X., Gardenghi, S., Rivella, S., & Shah, Y. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314197110 · Cited by 101
Quercetin and iron metabolism: What we know and what we need to know
Xiao, L., Luo, G., Tang, Y., & Yao, P. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.02.022 · Cited by 105
Genetics of iron regulation and the possible role of iron in Parkinson's disease
Rhodes, S. L., & Ritz, B. R. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.07.001 · Cited by 103
Cuproptosis: mechanisms and nanotherapeutic strategies in cancer and beyond
Mao, L., Lu, J., Wen, X., Song, Z., Sun, C., Zhao, Y., Huang, F., Chen, S., Jiang, D., Che, W., et al. (2025) · Chemical Society Reviews · doi:10.1039/d5cs00083a · Cited by 104
The Ins and Outs of Iron Homeostasis
Donovan, A., Roy, C. N., & Andrews, N. C. (2006) · Physiology · doi:10.1152/physiol.00052.2005 · Cited by 101
Iron Absorption in Drosophila melanogaster
Mandilaras, K., Pathmanathan, T., & Missirlis, F. (2013) · Nutrients · doi:10.3390/nu5051622 · Cited by 102
Skjørringe, T., Møller, L. B., & Moos, T. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00169 · Cited by 104
Role of Intestinal HIF-2α in Health and Disease
Ramakrishnan, S. K., & Shah, Y. M. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105202 · Cited by 100
You, L., Yu, P., Dong, T., Guo, W., Chang, S., Zheng, B., Ci, Y., Wang, F., Yu, P., Gao, G., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05043-w · Cited by 99
Hereditary hemochromatosis in the post- HFE era
Olynyk, J. K., Trinder, D., Ramm, G. A., Britton, R. S., & Bacon, B. R. (2008) · Hepatology · doi:10.1002/hep.22507 · Cited by 97
Iron metabolism: current facts and future decisions
Tandara, L., & Salamunić, I. (2012) · Biochemia Medica · doi:10.11613/bm.2012.034 · Cited by 102
An, Y., Zhu, J., Liu, F., Deng, J., Meng, X., Liu, G., Wu, H., Fan, A., Wang, Z., & Zhao, Y. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b10954 · Cited by 95
Sheikh, N., Dudás, J., & Ramadori, G. P. (2007) · Laboratory Investigation · doi:10.1038/labinvest.3700553 · Cited by 97
Noncanonical role of transferrin receptor 1 is essential for intestinal homeostasis
Chen, A. C., Donovan, A., Ned, R. M., & Andrews, N. C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1511701112 · Cited by 98
Burkhart, A., Skjørringe, T., Johnsen, K. B., Siupka, P., Thomsen, L. B., Nielsen, M. S., Thomsen, L. L., & Moos, T. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9582-7 · Cited by 98
Coad, J. E., & Conlon, C. A. (2011) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32834be6fd · Cited by 102
Recent advances in disorders of iron metabolism: mutations, mechanisms and modifiers
Roy, C. N. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.20.2181 · Cited by 96
Seiwert, N., Wecklein, S., Demuth, P., Hasselwander, S., Kemper, T. A., Schwerdtle, T., Brunner, T., & Fahrer, J. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02950-8 · Cited by 94
Ravia, J. J., Stephen, R. M., Ghishan, F. K., & Collins, J. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506727200 · Cited by 96
Hereditary hemochromatosis is reflected in the iron isotope composition of blood
Krayenbuehl, P., Walczyk, T., Schoenberg, R., von Blanckenburg, F., & Schulthess, G. (2005) · Blood · doi:10.1182/blood-2004-07-2807 · Cited by 98
Millard, K. N., Frazer, D. M., Wilkins, S. J., & Anderson, G. J. (2004) · Gut · doi:10.1136/gut.2003.031153 · Cited by 93
Molecular pathogenesis of iron overload
Trinder, D., Fox, C., Vautier, G., & Olynyk, J. K. (2002) · Gut · doi:10.1136/gut.51.2.290 · Cited by 93
Prion Protein Regulates Iron Transport by Functioning as a Ferrireductase
Singh, A., Haldar, S., Horback, K., Tom, C. M., Zhou, L., Meyerson, H. J., & Singh, N. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130218 · Cited by 93
Su, D., May, J. M., Koury, M. J., & Asard, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606543200 · Cited by 93
Iron metabolism and the role of the iron-regulating hormone hepcidin in health and disease
Daher, R., Manceau, H., & Karim, Z. (2017) · La Presse Médicale · doi:10.1016/j.lpm.2017.10.006 · Cited by 92
Fe(III)‐mediated cellular toxicity
Chamnongpol, S., Dodson, W., Cromie, M. J., Harris, Z. L., & Groisman, E. A. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03041.x · Cited by 93
Advances in iron chelation: an update
Heli, H., Mirtorabi, S., & Karimian, K. (2011) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.569493 · Cited by 92
A general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 97
Iron Homeostasis and Metabolism: Two Sides of a Coin
Venkataramani, V. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_3 · Cited by 96
Glei, M., Klenow, S., Sauer, J., Wegewitz, U. E., Richter, K. K., & Pool-Zobel, B. L. (2005) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.08.006 · Cited by 90
Iron Metabolism and Ferroptosis in Physiological and Pathological Pregnancy
Zhang, Y., Lu, Y., & Jin, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169395 · Cited by 94
The SLC40 basolateral iron transporter family (IREG1/ferroportin/MTP1)
McKie, A. T., & Barlow, D. J. (2004) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-003-1102-3 · Cited by 89
Self-citationIron Homeostasis in the Lungs—A Balance between Health and Disease
Neves, J., Haider, T., Gassmann, M., & Muckenthaler, M. U. (2019) · Pharmaceuticals · doi:10.3390/ph12010005 · Cited by 94
Silicon dioxide nanoparticle exposure affects small intestine function in an in vitro model
Guo, Z., Martucci, N. J., Liu, Y., Yoo, E., Tako, E., & Mahler, G. J. (2018) · Nanotoxicology · doi:10.1080/17435390.2018.1463407 · Cited by 91
Guo, Q., Qian, C., Wang, X., & Qian, Z. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01436-x · Cited by 91
Molecular Mechanisms and Regulation of Iron Transport
Chung, J., & Wessling‐Resnick, M. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609332 · Cited by 86
Mechanisms of Haem and Non-Haem Iron Absorption: Lessons from Inherited Disorders of Iron Metabolism
Anderson, G. J., Frazer, D. M., McKie, A. T., Vulpe, C. D., & Smith, A. (2005) · BioMetals · doi:10.1007/s10534-005-3708-8 · Cited by 90
Self-citationYeh, K., YEH, M. K. Y., Mims, L., & Glass, J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90298.2008 · Cited by 85
Zimmermann, M. B., Troesch, B., Biebinger, R., Egli, I. M., Zeder, C., & Hurrell, R. F. (2009) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2009.28129 · Cited by 84
Iron, oxidative stress, and redox signaling in the cardiovascular system
Gudjoncik, A., Guénancia, C., Zeller, M., Cottin, Y., Vergely, C., & Rochette, L. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400036 · Cited by 87
Intestinal Iron Homeostasis and Colon Tumorigenesis
Xue, X., & Shah, Y. M. (2013) · Nutrients · doi:10.3390/nu5072333 · Cited by 85
Scheers, N., Rossander-Hulthén, L., Torsdottir, I., & Sandberg, A. (2015) · European Journal of Nutrition · doi:10.1007/s00394-015-0857-6 · Cited by 76
Transplasma membrane electron transport: enzymes involved and biological function
Ly, J. D., & Lawen, A. (2003) · Redox Report · doi:10.1179/135100003125001198 · Cited by 82
Factors Affecting Iron Absorption and Mitigation Mechanisms: A review
Dasa, F., & Abera, T. (2018) · International Journal of Agricultural Science and Food Technology · doi:10.17352/2455-815x.000033 · Cited by 94
Stromal cell-derived receptor 2 and cytochrome b561 are functional ferric reductases
Vargas, J. D. H., Herpers, B., McKie, A. T., Gledhill, S., McDonnell, J. M., van den Heuvel, M., Davies, K. E., & Ponting, C. P. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(03)00242-5 · Cited by 82
Self-citationIron Homeostasis and Its Interaction with Prolyl Hydroxylases
Mole, D. R. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2790 · Cited by 80
The Families of Zinc (SLC30 and SLC39) and Copper (SLC31) Transporters
Schweigel‐Röntgen, M. (2014) · Current topics in membranes · doi:10.1016/b978-0-12-800223-0.00009-8 · Cited by 82
Tsubaki, M., Takeuchi, F., & Nakanishi, N. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.08.015 · Cited by 81
Molecular aspects of iron absorption and HFE expression
Parkkila, S., Niemelä, O. J., Britton, R. S., Fleming, R. E., Waheed, A., Bacon, B. R., & Sly, W. S. (2001) · Gastroenterology · doi:10.1053/gast.2001.29617 · Cited by 79
Role of Dietary Flavonoids in Iron Homeostasis
Lesjak, M. M., & Srai, S. K. (2019) · Pharmaceuticals · doi:10.3390/ph12030119 · Cited by 87
Iron Homeostasis and Nutritional Iron Deficiency1–3
Theil, E. C. (2011) · Journal of Nutrition · doi:10.3945/jn.110.127639 · Cited by 81
Intestinal iron uptake in the European flounder (Platichthys flesus)
Bury, N. R., Grosell, M., Wood, C. M., Högstrand, C., Wilson, R. W., Rankin, J. C., Busk, M., Lecklin, T., & Jensen, F. B. (2001) · Journal of Experimental Biology · doi:10.1242/jeb.204.21.3779 · Cited by 80
Effects of Microcystin-LR on the Microstructure and Inflammation-Related Factors of Jejunum in Mice
Cao, L., Huang, F., Massey, I. Y., Wen, C., Zheng, S., Xu, S., & Yang, F. (2019) · Toxins · doi:10.3390/toxins11090482 · Cited by 79
Smith, C. P., & Thévenod, F. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.10.010 · Cited by 80
Quercetin–iron chelates are transported via glucose transporters
Vlachodimitropoulou, E., Sharp, P., & Naftalin, R. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.01.005 · Cited by 78
A possible role for secreted ferritin in tissue iron distribution
Meyron‐Holtz, E. G., Moshe-Belizowski, S., & Cohen, L. A. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0582-0 · Cited by 78
Mesías, M., Seiquer, I., & Navarro, M. P. (2013) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2011.564333 · Cited by 86
Zumbrennen‐Bullough, K. B., & Babitt, J. L. (2013) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gft443 · Cited by 82
Cooper, C. A., Handy, R. D., & Bury, N. R. (2006) · Aquatic Toxicology · doi:10.1016/j.aquatox.2006.06.008 · Cited by 77
Effects of copper on the expression of metal transporters in human intestinal Caco‐2 cells
Tennant, J. P., Stansfield, M., Yamaji, S., Srai, S. K., & Sharp, P. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03253-2 · Cited by 75
The role of hepatic transferrin receptor 2 in the regulation of iron homeostasis in the body
Worthen, C., & Enns, C. A. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00034 · Cited by 80
Saini, R. K., Manoj, P., Shetty, N. P., Srinivasan, K., & Giridhar, P. (2014) · Nutrition Research · doi:10.1016/j.nutres.2014.07.003 · Cited by 80
Richardson, D. R., & Lok, H. C. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.12.009 · Cited by 76
Iron, hepcidin, and the metal connection
Loréal, O., Cavey, T., Bardou‐Jacquet, E., Guggenbuhl, P., Ropert, M., & Brissot, P. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00128 · Cited by 78
Fuzi, S. F. A., Koller, D., Bruggraber, S. F. A., Pereira, D. I. A., Dainty, J. R., & Mushtaq, S. (2017) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.161364 · Cited by 79
Oates, P. S. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i27.4281 · Cited by 76
Duodenal Cytochrome B Expression Stimulates Iron Uptake by Human Intestinal Epithelial Cells
Latunde-Dada, G. O., Simpson, R. J., & McKie, A. T. (2008) · Journal of Nutrition · doi:10.1093/jn/138.6.991 · Cited by 74
Self-citationDMT1 and FPN1 expression during infancy: developmental regulation of iron absorption
Leong, W.-I., Bowlus, C. L., Tallkvist, J., & Lönnerdal, B. L. (2003) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00107.2003 · Cited by 76
Uptake of ferrous iron by cultured rat astrocytes
Tulpule, K., Robinson, S. R., Bishop, G. M., & Dringen, R. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22217 · Cited by 75
Iron and ageing: an introduction to iron regulatory mechanisms
Levenson, C. W., & Tassabehji, N. M. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.03.001 · Cited by 74
Reduction-dependent siderophore assimilation in a model pennate diatom
Coale, T. H., Moosburner, M., Horák, A., Oborník, M., Barbeau, K. A., & Allen, A. E. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1907234116 · Cited by 75
Genes for iron metabolism influence circadian rhythms in Drosophila melanogaster
Mandilaras, K., & Missirlis, F. (2012) · Metallomics · doi:10.1039/c2mt20065a · Cited by 74
Siah, C. W., Trinder, D., & Olynyk, J. K. (2005) · Clinica Chimica Acta · doi:10.1016/j.cccn.2005.02.022 · Cited by 75
Metadata
- Authors
- McKie, A. T., Barrow, D., Latunde-Dada, G. O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., Peters, T. J., Raja, K. B., Shirali, S., Hediger, M. A., Farzaneh, F., & Simpson, R. J.
- Affiliations
- King's College London (GB)
- Brigham and Women's Hospital (US)
- Department of Clinical Biochemistry,
- Corresponding author
- McKie, Andrew T.
- ORCID
- Venue
- Science
- Published
- 2001-03-02
- Volume
- 291
- Issue
- 5509
- Pages
- 1755-1759
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2105749655
- Cited by
- 1,101
- References
- 26
- Citations by year
- 2026: 25 · 2025: 41 · 2024: 44 · 2023: 30 · 2022: 45 · 2021: 43 · 2020: 55 · 2019: 40 · 2018: 50 · 2017: 33 · 2016: 22 · 2015: 28 · 2014: 48 · 2013: 44 · 2012: 47
- FWCI
- 28.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Micronutrient Interactions and Effects
- Keywords
- ferric reductase, dietary iron absorption, duodenal cytochrome b, Dcytb, cytochrome b561, brush border membrane, duodenal enterocytes, Xenopus oocyte expression
- MeSH terms
- Amino Acid Sequence, Anemia, Animals, Hypoxia, Cell Line, Cloning, Molecular, Cytochrome b Group, Duodenum, Enzyme Induction, Ferric Compounds, Intestinal Absorption, Intestinal Mucosa, Male, Microvilli, Molecular Sequence Data, Nitroblue Tetrazolium, Oocytes, Oxidation-Reduction, Oxidoreductases, RNA, Messenger, Tetrazolium Salts, Thiazoles, Transfection, Xenopus, Up-Regulation, DNA, Complementary, Iron, Dietary, Enterocytes, 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