The DOI matches its Crossref record; 208 of the 208 references it cites were found in a registry or an index.
Regulation of cellular iron metabolism
Open accessAbstract
Iron is an essential but potentially hazardous biometal. Mammalian cells require sufficient amounts of iron to satisfy metabolic needs or to accomplish specialized functions. Iron is delivered to tissues by circulating transferrin, a transporter that captures iron released into the plasma mainly from intestinal enterocytes or reticuloendothelial macrophages. The binding of iron-laden transferrin to the cell-surface transferrin receptor 1 results in endocytosis and uptake of the metal cargo. Internalized iron is transported to mitochondria for the synthesis of haem or iron-sulfur clusters, which are integral parts of several metalloproteins, and excess iron is stored and detoxified in cytosolic ferritin. Iron metabolism is controlled at different levels and by diverse mechanisms. The present review summarizes basic concepts of iron transport, use and storage and focuses on the IRE (iron-responsive element)/IRP (iron-regulatory protein) system, a well known post-transcriptional regulatory circuit that not only maintains iron homoeostasis in various cell types, but also contributes to systemic iron balance.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“IRPs, in addition to modulating ferritin and TfR1 levels can regulate the mRNAs or other proteins required for iron utilization (erythroid 5-aminolevulanata synthase), iron uptake (DMT1) and export (FPN1).DMT1 mRNA has IRE in its 3 ' UTR and is upregulated by iron deficiency while the other two proteins have IREs in their 5 ' UTR and are therefore upregulated under high iron conditions”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Conversely, when iron concentration is high, IRPs are inactivated resulting in degradation of TfR1 mRNA while translation of ferritin mRNA occurs.Thus when iron levels exceed the cellular needs, the IRE/IRP switch minimizes iron uptake and promotes iron storage”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
The cited source says what the claim attributes to it.
In the citing paper
“When iron is depleted, IRE-IRP interaction at the 3 ' UTR of TfR1 stabilizes mRNA, while imposing a steric blockade to ferritin mRNA translation.As a result, TfR1 is upregulated and stimulates acquisition of iron from plasma Tf to counteract low iron levels.Simultaneously ferritin synthesis is inhibited as storage of iron is not needed.”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
The cited source says what the claim attributes to it.
In the citing paper
“However, in erythroid progenitor cells which require high amounts of iron for heme synthesis, TfR1 stability is uncoupled from iron supply and TfR1 level is transcriptionally regulated by erythroid active element in its promoter region (Wang and Pantopoulos, 2011).”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
In the citing paper
“Iron homoeostasis is needed to maintain normal physiological brain function, whereas misregulation of iron homoeostasis can cause neurotoxicity through different mechanisms.”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [3]
In the citing paper
“Iron homoeostasis is needed to maintain normal physiological brain function, whereas misregulation of iron homoeostasis can cause neurotoxicity through different mechanisms.”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [3]
In the citing paper
“Circulating hepcidin (panel) regulates systemic iron homoeostasis by interacting with ferroportin when iron is abundant, which results in ferroportin internalisation and degradation, thereby blocking iron exportation from cells.3”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [3]
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
Items 201–208 of 208
Iron Regulatory Protein 2 is Involved in Brain Copper Homeostasis
Mueller, C., Magaki, S., Schrag, M., Ghosh, M. C., & Kirsch, W. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1136 · Cited by 14
Ghosh, M. C., Ollivierre, H., Cooperman, S. S., & Rouault, T. A. (2006) · Nature Genetics · doi:10.1038/ng0906-969 · Cited by 12
Ferritin does not donate its iron for haem synthesis in macrophages
Mikhael, M., Sheftel, A. D., & Ponka, P. (2010) · Biochemical Journal · doi:10.1042/bj20100346 · Cited by 11
In vivo role(s) of the iron regulatory proteins (IRP) 1 and 2 in aseptic local inflammation
Viatte, L., Gröne, H.-J., Hentze, M. W., & Galy, B. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0494-8 · Cited by 11
Comment to: Hepcidin: from discovery to differential diagnosis. Haematologica 2008; 93:90-7
Olsson, K. S., & Norrby, A. (2008) · Haematologica · doi:10.3324/haematol.12814 · Cited by 10
Is the iron donor lipocalin 2 implicated in the pathophysiology of hereditary hemochromatosis?†
Huang, H., Akira, S., & Santos, M. M. (2008) · Hepatology · doi:10.1002/hep.22699 · Cited by 9
Interaction of iron regulatory protein-1 (IRP-1) with ATP/ADP maintains a non-IRE-binding state
Popović, Z., & Templeton, D. M. (2010) · Biochemical Journal · doi:10.1042/bj20100111 · Cited by 9
(1998) · PubMed
Flagged first, then by citations
Cited by
Sorted by citations
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373
Review on iron and its importance for human health.
Abbaspour, N., Hurrell, R. F., & Kelishadi, R. (2014) · Europe PMC (PubMed Central) · Cited by 1,886
The role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819
A Review of Micronutrients and the Immune System–Working in Harmony to Reduce the Risk of Infection
Gombart, A. F., Pierre, A., & Maggini, S. (2020) · Nutrients · doi:10.3390/nu12010236 · Cited by 1,358
Redox- and non-redox-metal-induced formation of free radicals and their role in human disease
Valko, M., Jomová, K., Rhodes, C. J., Kuča, K., & Musílek, K. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1579-5 · Cited by 1,062
Metadata
- Authors
- Wang, J., & Pantopoulos, K.
- Affiliations
- Jewish General Hospital (CA)
- Corresponding author
- Pantopoulos, Kostas
- ORCID
- Pantopoulos, Kostas
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2011-02-24
- Volume
- 434
- Issue
- 3
- Pages
- 365-381
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC3048577
- OpenAlex
- W2158115535
- Cited by
- 986
- References
- 208
- Citations by year
- 2026: 38 · 2025: 41 · 2024: 54 · 2023: 72 · 2022: 69 · 2021: 70 · 2020: 71 · 2019: 72 · 2018: 67 · 2017: 64 · 2016: 56 · 2015: 67 · 2014: 77 · 2013: 76 · 2012: 60
- FWCI
- 10.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochemical Journal (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research (MOP-86514)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- iron homeostasis, transferrin, transferrin receptor 1, iron absorption, endocytosis, mitochondrial iron transport, haem synthesis, iron-sulfur clusters, ferritin, iron storage, post-transcriptional regulation
- MeSH terms
- Animals, Biological Transport, Ferritins, Humans, Iron, Mitochondria, Neoplasms, Oxidation-Reduction, RNA, Messenger, Transferrin, Response Elements, Iron-Regulatory Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
