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Molecular control of vertebrate iron homeostasis by iron regulatory proteins

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Wallander, Michelle L., Leibold, Elizabeth A., Eisenstein, Richard S.·2006·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

DOI 10.1016/j.bbamcr.2006.05.004PMC PMC2291536

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Abstract

Both deficiencies and excesses of iron represent major public health problems throughout the world. Understanding the cellular and organismal processes controlling iron homeostasis is critical for identifying iron-related diseases and in advancing the clinical treatments for such disorders of iron metabolism. Iron regulatory proteins (IRPs) 1 and 2 are key regulators of vertebrate iron metabolism. These RNA binding proteins post-transcriptionally control the stability or translation of mRNAs encoding proteins involved in iron homeostasis thereby controlling the uptake, utilization, storage or export of iron. Recent evidence provides insight into how IRPs selectively control the translation or stability of target mRNAs, how IRP RNA binding activity is controlled by iron-dependent and iron-independent effectors, and the pathological consequences of dysregulation of the IRP system.

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Textbook of Medical Physiology
Guyton, A. C., & Hall, J. E. (1966) · Annals of Internal Medicine · doi:10.7326/0003-4819-64-6-1363_2 · Cited by 9,760
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513
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
Balancing Acts
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
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
Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 ( USF2 ) knockout mice
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
Iron deficiency and reduced work capacity: A critical review of the research to determine a causal relationship
Haas, J. D., & Brownlie, T. (2001) · The Journal of Nutrition · doi:10.1093/jn/131.2.676s · Cited by 1,186
Iron Biology in Immune Function, Muscle Metabolism and Neuronal Functioning
Beard, J. L. (2001) · Journal of Nutrition · doi:10.1093/jn/131.2.568s · Cited by 1,163

Show all 307 references

Research works printed but not linked: 1

Laufberger, 1937, Sur la cristallisation de la ferritine, Bull. Soc. Chim. Biol., 19, 1575

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Self-citation
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Authors: Wallander, M. L., Leibold, E. A., & Eisenstein, R. S.
Affiliations: University of Utah (US)
University of Wisconsin–Madison (US)
Corresponding author: Eisenstein, Richard S.
ORCID: Wallander, Michelle L.
Leibold, Elizabeth A.
Eisenstein, Richard S.
Venue: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher: Elsevier BV
Published: 2006-07
Volume: 1763
Issue: 7
Pages: 668-689
ISSN: 0167-4889 (ISSN-L)
DOI: 10.1016/j.bbamcr.2006.05.004
PMC: PMC2291536
OpenAlex: W2121798267
Cited by: 287
References: 307
Citations by year: 2026: 4 · 2025: 7 · 2024: 8 · 2023: 7 · 2022: 7 · 2021: 14 · 2020: 13 · 2019: 6 · 2018: 11 · 2017: 6 · 2016: 12 · 2015: 11 · 2014: 19 · 2013: 18 · 2012: 22
FWCI: 2.94
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2574 d)
Locations: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (GM 45201, R01GM045201)
National Institute of Diabetes and Digestive and Kidney Diseases (DK 66600, R56DK066600, DK47219, R01DK066600)
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, iron regulatory proteins, iron regulatory protein 1, IRP2, RNA-binding proteins, post-transcriptional regulation, mRNA stability, translational regulation, iron metabolism disorders, iron deficiency, iron overload
MeSH terms: Animals, Homeostasis, Iron, Vertebrates, Iron-Regulatory Proteins

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Molecular control of vertebrate iron homeostasis by iron regulatory proteins

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