The DOI matches its Crossref record; 109 of the 110 references it cites were found in a registry or an index.
Ironing out Ferroportin
Open accessAbstract
Maintaining physiologic iron concentrations in tissues is critical for metabolism and host defense. Iron absorption in the duodenum, recycling of iron from senescent erythrocytes, and iron mobilization from storage in macrophages and hepatocytes constitute the major iron flows into plasma for distribution to tissues, predominantly for erythropoiesis. All iron transfer to plasma occurs through the iron exporter ferroportin. The concentration of functional membrane-associated ferroportin is controlled by its ligand, the iron-regulatory hormone hepcidin, and fine-tuned by regulatory mechanisms serving iron homeostasis, oxygen utilization, host defense, and erythropoiesis. Fundamental questions about the structure and biology of ferroportin remain to be answered.
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In the citing paper
“Aberrant ferroportin activity can lead to diseases of iron overload, like hemochromatosis, or iron limitation anemias 2 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“In mammals, iron levels are regulated by the action of hepcidin, a peptide hormone, on ferroportin (FPN), the only known iron efflux transporter 2-4 (Fig. 1a).”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
The cited source says what the claim attributes to it.
In the citing paper
“The cryo-EM density map of FPN enabled building of an atomic model of FPN regions important for iron transport and hepcidin binding 2,7 , and a portion of the intracellular loop 3 (ICL3) important in hepcidin-induced FPN internalization 8-10 (Extended Data Fig. 5).”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
In the citing paper
“The expression of FPN is tightly regulated at the transcriptional, posttranscriptional, and posttranslational levels.8”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
In the citing paper
“In duodenal enterocytes, transcription of the Fpn gene, which encodes ferroportin, is regulated by iron and hypoxia to increase the absorption of dietary iron during iron deficiency and anemia.8,54”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
In the citing paper
“Taken together, these data support that FPN expression is tightly controlled at both transcriptional and/or the translational levels,8,68,69 which allow multiple and diverse physiological effects to influence FPN activity at its various sites of expression.”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
In the citing paper
“On average, humans ingest 20–25 mg of iron/day, the majority of which is inorganic iron (85%–90%), followed by haem‐bound iron (10%–15%).”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“In mammals, excretion of iron is not extensively regulated; instead, iron homeostasis is achieved mainly by regulating intestinal absorption in the duodenum, 9 and possibly in the colon to some extent. 10”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“However, only ~ 1 mg iron is absorbed per day, because of both poor iron bioavailability and tightly regulated iron homeostasis. 9 , 11”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“In conditions of iron accumulation, the production of HAMP is stimulated, and, as a result, iron is subsequently trapped within enterocytes and macrophages, respectively inhibiting iron export to circulation or preventing recycling of iron derived from red blood cells. 9”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In the citing paper
“The iron regulatory hormone hepcidin limits iron fluxes to the bloodstream by promoting degradation of the iron exporter ferroportin in target cells.”
From Pharmacological Targeting of the Hepcidin/Ferroportin Axis (2016) · cites this paper as Drakesmith et al., 2015
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Citations
Cites
2 retracted
RETRACTED: The Hepcidin-Binding Site on Ferroportin Is Evolutionarily Conserved
Domenico, I. D., Nemeth, E., Nelson, J. M., Phillips, J. D., Ajioka, R. S., Kay, M. S., Kushner, J. P., Ganz, T., Ward, D. M., & Kaplan, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.002 · Cited by 127
Self-citationRetractedDomenico, I. D., Lo, E., Yang, B., Korolnek, T., Hamza, I., Ward, D. M., & Kaplan, J. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.09.008 · Cited by 27
RetractedExploring the full spectrum of macrophage activation
Mosser, D. M., & Edwards, J. P. (2008) · Nature Reviews Immunology · doi:10.1038/nri2448 · Cited by 9,144
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
Self-citationPositional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
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
Flagged first, then by citations
1 of the 110 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Altamura, 2011, Mouse models for ferroportin with impaired hepcidin regulation, Am. J. Hematol., 86, E42
- Preza, 2011, Minihepcidins are rationally designed small peptides that mimic hepcidin activity in mice and may be useful for the treatment of iron overload, J. Clin. Invest., 121, 4880, 10.1172/JCI57693 · DOI · Paper page
Cited by
Sorted by citations
Ferroptosis: Mechanisms and links with diseases
Yan, H.-F., Zou, T., Tuo, Q.-Z., Xu, S., Li, H., Belaidi, A. A., & Lei, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00428-9 · Cited by 1,471
A Red carpet for iron metabolism
Muckenthaler, M. U., Rivella, S., Hentze, M. W., & Galy, B. (2017) · Cell · doi:10.1016/j.cell.2016.12.034 · Cited by 1,319
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 1,170
Iron homeostasis and oxidative stress: An intimate relationship
Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 960
Loss of ferroportin induces memory impairment by promoting ferroptosis in Alzheimer’s disease
Bao, W.-D., Pang, P., Zhou, X.-T., Hu, F., Xiong, W., Chen, K., Wang, J., Wang, F., Xie, D., Ya⁃zhuo, H. U., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00685-9 · Cited by 682
Metadata
- Authors
- Drakesmith, H., Nemeth, E., & Ganz, T.
- Affiliations
- University of Oxford (GB)
- University of California, Los Angeles (US)
- Corresponding author
- Ganz, Tomas
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 22
- Issue
- 5
- Pages
- 777-787
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4635047
- OpenAlex
- W2174098335
- Cited by
- 638
- References
- 110
- Citations by year
- 2026: 35 · 2025: 64 · 2024: 68 · 2023: 76 · 2022: 75 · 2021: 67 · 2020: 86 · 2019: 52 · 2018: 54 · 2017: 33 · 2016: 24 · 2015: 1
- FWCI
- 5.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK065029, R01DK090554, R01DK107309)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- ferroportin, hepcidin, iron homeostasis, iron absorption, erythropoiesis, iron recycling, iron storage, iron export, membrane protein structure, host defense, oxygen utilization
- MeSH terms
- Ferroportin, Animals, Erythrocytes, Erythropoiesis, Homeostasis, Humans, Iron, Macrophages, Hepatocytes, Cation Transport Proteins, Hepcidins
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