The DOI matches its Crossref record; 108 of the 108 references it cites were found in a registry or an index.
The role of iron regulatory proteins in mammalian iron homeostasis and disease
Abstract
Iron regulatory proteins 1 and 2 (IRP1 and IRP2) are mammalian proteins that register cytosolic iron concentrations and post-transcriptionally regulate expression of iron metabolism genes to optimize cellular iron availability. In iron-deficient cells, IRPs bind to iron-responsive elements (IREs) found in the mRNAs of ferritin, the transferrin receptor and other iron metabolism transcripts, thereby enhancing iron uptake and decreasing iron sequestration. IRP1 registers cytosolic iron status mainly through an iron-sulfur switch mechanism, alternating between an active cytosolic aconitase form with an iron-sulfur cluster ligated to its active site and an apoprotein form that binds IREs. Although IRP2 is homologous to IRP1, IRP2 activity is regulated primarily by iron-dependent degradation through the ubiquitin-proteasomal system in iron-replete cells. Targeted deletions of IRP1 and IRP2 in animals have demonstrated that IRP2 is the chief physiologic iron sensor. The physiological role of the IRP-IRE system is illustrated by (i) hereditary hyperferritinemia cataract syndrome, a human disease in which ferritin L-chain IRE mutations interfere with IRP binding and appropriate translational repression, and (ii) a syndrome of progressive neurodegenerative disease and anemia that develops in adult mice lacking IRP2. The early death of mouse embryos that lack both IRP1 and IRP2 suggests a central role for IRP-mediated regulation in cellular viability.
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In the citing paper
“This gene also plays a major role for the development and proliferation of lymphocyte since defective T- and B-cell activation is caused by inadequate iron uptake (Rouault, 2006; Jabara et al., 2016).”
From Identification of Candidate Signature Genes and Key Regulators Associated With Trypanotolerance in the Sheko Breed (2019) · cites this paper as Rouault, 2006
In the citing paper
“The MIGA1 gene is associated with iron deficiency anemia and immunity (Moura et al., 2001; Rouault, 2006).”
From Identification of Candidate Signature Genes and Key Regulators Associated With Trypanotolerance in the Sheko Breed (2019) · cites this paper as Rouault, 2006
In the citing paper
“When iron levels normalize again, IRP1 regains its Fe-S cluster and aconitase activity. This results in increased ferritin translation and decreased TFR expression, resulting in reduced Fe uptake (Li et al., 2004; Rouault, 2006; Leipuviene and Theil, 2007; Sanchez et al., 2011; Figure 2).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Rouault, 2006
In the citing paper
“Interestingly, the hyperferritinemia-cataract syndrome that is caused by a mutation in a specific non-coding region of the FTL gene, the iron-responsive element (IRE), is not associated with iron accumulation in the brain but with the formation of ferritin crystals in the ocular lenses, resulting in cataracts in early adulthood [23, 83, 195].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [195]
In the citing paper
“IRPs sense free labile iron and control cellular iron homeostasis at the post-transcriptional level: Due to their ability to interact with iron-responsive elements (IREs) that are present in the non-coding mRNA sequences of Tfr1, Dmt1, Fpn1, FTH, and FTL chains, fluctuations in intracellular iron are promptly counterbalanced [179, 195].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [195]
In the citing paper
“One such mechanism to maintain cytosolic iron levels are the iron regulatory proteins (IRPs) 1 and 2 [5, 179, 195].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [195]
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 [69]
In the citing paper
“Therefore, high levels of IRP2 are usually indicative of decreased cellular iron bioavailability.”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [48]
In the citing paper
“While IRP2 can mediate the degradation of ferritin and ferroportin mRNA [48], this must be insufficient to prevent their biosynthesis in the context of senescent cells.”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [48]
In the citing paper
“and stabilizes TfR1 mRNA (via binding to 3′ IRE) increasing its expression to up-regulate cellular iron uptake [48].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [48]
In the citing paper
“In this situation, IRP1 usually loses its iron-sulfur cluster and aconitase activity and binds IREs with high affinity [48], [50].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [48]
Citations
Cites
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
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736
Structure, function, and formation of biological iron-sulfur clusters
Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438 · cited 1×
“Mammalian iron-sulfur cluster assembly Assembly of iron-sulfur clusters is a complex process involving many enzymes and scaffold protein”
BackgroundA 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
Regulating the fate of mRNA: the control of cellular iron metabolism
Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210
Leibold, E. A., & Munro, H. N. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.7.2171 · Cited by 671
I RON R EGULATORY P ROTEINS AND THE M OLECULAR C ONTROL OF M AMMALIAN I RON M ETABOLISM
Eisenstein, R. S. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.627 · Cited by 655
Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606 · cited 1×
“In aconitases, a cubane iron-sulfur cluster is ligated by three cysteines within the enzymatic active site cleft, and the fourth iron of the cubane cluster binds substrat”
BackgroundHentze, M. W., Caughman, S. W., Rouault, T. A., Barriocanal, J. G., Dancis, A., Harford, J. B., & Klausner, R. D. (1987) · Science · doi:10.1126/science.3685996 · Cited by 571
Cited by
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Qureshi, I., & Mehler, M. F. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05718.x · Cited by 23
Wojcik, K. A., Synowiec, E., Jiménez-García, M. P., Kamińska, A., Polakowski, P., Błasiak, J., Szaflik, J., & Szaflik, J. P. (2013) · BioMed Research International · doi:10.1155/2013/247438 · Cited by 23
Belko, N. V., Maltanava, H. M., Lugovski, A. P., Ferreira, R. A. S., Correia, S. F. H., Shabunya, P., Fatykhava, S., Tabolich, A., Kulahava, T. A., Bahdanava, A., et al. (2023) · Microchemical Journal · doi:10.1016/j.microc.2023.108744 · Cited by 22
Nahon, P., Charnaux, N., Friand, V., Prost‐Squarcioni, C., Ziol, M., Lievre, N., Trinchet, J., Beaugrand, M., Gattegno, L., Pessayre, D., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.011 · Cited by 22
The Structural Basis of Iron Sensing by the Human F‐box Protein FBXL5
Shu, C., Sung, M. W., Stewart, M. D., Igumenova, T. I., Tan, X., & Li, P. (2012) · ChemBioChem · doi:10.1002/cbic.201200043 · Cited by 22
Wallander, M. L., Zumbrennen‐Bullough, K. B., Rodansky, E. S., Romney, S. J., & Leibold, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803005200 · Cited by 22
Tapryal, N., Vishnu Vivek, G., & Mukhopadhyay, C. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592519 · Cited by 22
Shu, W., Baumann, B. H., Song, Y., Liu, Y., Wu, X., & Dunaief, J. L. (2019) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.19-28250 · Cited by 22
Gnana‐Prakasam, J. P., Zhang, M., Martin, P. M., Atherton, S. S., Smith, S. B., & Ganapathy, V. (2009) · Biochemical Journal · doi:10.1042/bj20082240 · Cited by 22
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Camponeschi, F., & Banci, L. (2018) · Pure and Applied Chemistry · doi:10.1515/pac-2018-0720 · Cited by 21
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Zhao, Y., Tan, M., Song, J., An, J., Yang, X., Li, W., Guo, Y., & Ji, E. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8520967 · Cited by 21
Yook, J., You, M., Kim, J., Toney, A. M., Fan, R., Puniya, B. L., Helikar, T., Vaulont, S., Deschemin, J., Okla, M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2109186118 · Cited by 21
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Waldern, J. M., Kumar, J., & Laederach, A. (2021) · Human Genetics · doi:10.1007/s00439-021-02395-9 · Cited by 22
Liu, D., Hu, Z., Lu, J., & Yi, C. (2024) · Antioxidants · doi:10.3390/antiox13070791 · Cited by 22
Fehringer, G., Liu, G., Pintilie, M., Sykes, J. R., Cheng, D., Liu, G., Chen, Z., Seymour, L., Der, S. D., Shepherd, F. A., et al. (2012) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-11-1123-t · Cited by 22
Mitophagy and iron: two actors sharing the stage in age-associated neuronal pathologies
Schiavi, A., Strappazzon, F., & Ventura, N. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111252 · Cited by 22
Chen, Y.-C., Wu, Y., & Wei, Y. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1067695 · Cited by 22
Aba, Ü., Maslak, İ. C., İpşir, C., Pehlivan, D., Warnock, N. I., Tumes, D. J., Cildir, G., & Erman, B. (2024) · Journal of Clinical Immunology · doi:10.1007/s10875-024-01658-0 · Cited by 20
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Tang, Q., Li, H., Hu, H., & Chen, L. (2023) · Dyes and Pigments · doi:10.1016/j.dyepig.2023.111634 · Cited by 19
Yang, X., Fang, H., Li, S., Chu, C., Zhang, Y., Yang, Y., He, W., Chen, Y., & Guo, Z. (2024) · Aggregate · doi:10.1002/agt2.641 · Cited by 20
Possible involvement of iron-induced oxidative insults in neurodegeneration
Asano, T., Koike, M., Sakata, S., Takeda, Y., Nakagawa, T., Hatano, T., Ohashi, S., Funayama, M., Yoshimi, K., Asanuma, M., et al. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.12.052 · Cited by 20
On the mechanism of iron sensing by IRP2: new players, new paradigms
Takahashi‐Makise, N., Ward, D. M., & Kaplan, J. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.261 · Cited by 20
Batista-Nascimento, L. S., Tolédano, M. B., Thiele, D. J., & Rodrigues‐Pousada, C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.12.018 · Cited by 20
Han, C., Huang, T., Liu, Q., Xu, H., Zhuang, Y., Li, J., Hu, J., Wang, A., & Xu, K. (2014) · Journal of Materials Chemistry C · doi:10.1039/c4tc01759e · Cited by 20
RetractedPang, Y. K., Gupta, G., Yang, C., Wang, H., Huynh, T., Abdullaev, Z., Pack, S., Percy, M. J., Lappin, T. R. J., Zhuang, Z., et al. (2018) · BMC Cancer · doi:10.1186/s12885-018-4127-x · Cited by 20
Translational control of the AZFa gene DDX3Y by 5′UTR exon-T extension
Jaroszynski, L. P., Zimmer, J., Fietz, D., Bergmann, M. M., Kliesch, S., & Vogt, P. H. (2010) · International Journal of Andrology · doi:10.1111/j.1365-2605.2010.01079.x · Cited by 20
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Xu, J., Shen, R., Qian, M., Zhou, Z., Xie, B., Jiang, Y. Q., Yu, Y., & Dong, W. (2025) · Journal of Integrative Neuroscience · doi:10.31083/jin25845 · Cited by 20
Ullah, Q., Khan, S. A., Arifuddin, M., Mohsin, M., Kausar, S., Fatema, N., & Ahmer, M. F. (2023) · Journal of Fluorescence · doi:10.1007/s10895-023-03514-7 · Cited by 19
Guerreiro, C. C., Silva, B. D. R., Crespo, Â. C., Marques, L., Costa, S., Timóteo, Â., Marcelino, E., Maruta, C., Vilares, A., Matos, M., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.07.017 · Cited by 19
Rhodes, D. A., Boyle, L. H., Boname, J. M., Lehner, P. J., & Trowsdale, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003421107 · Cited by 18
Haro, K. J., Sheth, A., & Scheinberg, D. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048841 · Cited by 19
Laparra, J. M., Tako, E., Glahn, R. P., & Miller, D. D. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf073470m · Cited by 19
Kundu, A., Pitchaimani, J., Madhu, V., Sakthivel, P., Ganesamoorthy, R., & Anthony, S. P. (2016) · Journal of Fluorescence · doi:10.1007/s10895-016-1976-z · Cited by 19
Chen, S.-C., & Olsthoorn, R. C. L. (2019) · Gene · doi:10.1016/j.gene.2019.06.012 · Cited by 19
Ahmadi, S., Dabbagh, H. A., Grieco, P., & Balalaie, S. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117696 · Cited by 19
Elevated serum iron level is a predictor of prognosis in ICU patients with acute kidney injury
Shu, J., Hu, Y., Yu, X., Chen, J.-X., Xu, W., & Pan, J. (2020) · BMC Nephrology · doi:10.1186/s12882-020-01965-9 · Cited by 19
Perng, V., Li, C., Klocke, C. R., Navazesh, S. E., Pinneles, D., Lein, P. J., & Ji, P. (2020) · Journal of Nutrition · doi:10.1093/jn/nxaa326 · Cited by 19
Liu, Q., Ren, B., Xie, K., Yan, Y., Liu, R., Lv, S., He, Q. G., Yang, B., & Li, L. (2020) · Nanoscale Advances · doi:10.1039/d0na00769b · Cited by 19
Yan, R., Guo, Z., Chen, X., Tang, L., Wang, M., & Miao, P. (2021) · The Analyst · doi:10.1039/d1an01451j · Cited by 19
Ding, Y., Yang, D., Xun, X., Wang, Z., Sun, P., Xu, D., He, P., Niu, H., & Jin, T. (2014) · International Journal of COPD · doi:10.2147/copd.s73042 · Cited by 19
Lin, X.-Y., Xue, R.-Y., Zhou, L., Zhang, Y.-S., Wang, H., Zhang, S., Li, S., Juhasz, A. L., Ma, L. Q., Zhou, D., et al. (2022) · Environment International · doi:10.1016/j.envint.2022.107664 · Cited by 18
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Crescenzi, E., Leonardi, A., & Pacifico, F. (2023) · Biology · doi:10.3390/biology12070989 · Cited by 20
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Skv, M., Abraham, S. M., Eshwari, O., Golla, K., Jhelum, P., Maity, S., & Komal, P. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-03989-w · Cited by 18
Casarrubea, D., Viatte, L., Hallas, T., Vasanthakumar, A., Eisenstein, R. S., Schümann, K., Hentze, M. W., & Galy, B. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1008-2 · Cited by 19
Synowiec, E., Pogorzelska, M., Błasiak, J., Szaflik, J., & Szaflik, J. P. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-1539-6 · Cited by 18
One-Step Synthesis of Nitrogen and Chlorine Co-Doped Carbon Quantum Dots for Detection of Fe3+
Zhong, Y., Chen, Q., Li, J., Pan, X., Han, Z., & Dong, W. (2017) · NANO · doi:10.1142/s1793292017501351 · Cited by 18
Jiao, Q., Du, X., Wei, J., Li, Y. H., & Jiang, H. F. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00020 · Cited by 18
A smart single molecular probe for Cu2+/Fe3+/Mg2+ by three-emission behaviors
Wang, F., Li, C., Song, L., Zhang, X., Wang, A., Zhou, L., Jia, C., Xu, J., & Chen, Y. (2019) · Dyes and Pigments · doi:10.1016/j.dyepig.2019.107667 · Cited by 18
Gao, Y., Ma, S.-Y., Ya, X., Gao, J., Han, S., Li, T., Gao, Y., & Zhao, B. (2020) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.151452 · Cited by 14
A novel treatment strategy to prevent Parkinson’s disease: focus on iron regulatory protein 1 (IRP1)
Berry, T. M., & Moustafa, A. A. (2021) · International Journal of Neuroscience · doi:10.1080/00207454.2021.1885403 · Cited by 17
Mallick, D., Biswal, B., Thirunavoukkarasu, M., Mohanty, R., & Bag, B. (2017) · New Journal of Chemistry · doi:10.1039/c7nj03364h · Cited by 18
Iron-dependent degradation of IRP2 requires its C-terminal region and IRP structural integrity
Wang, J., Chen, G., Lee, J., & Pantopoulos, K. (2008) · BMC Molecular Biology · doi:10.1186/1471-2199-9-15 · Cited by 18
Huang, X. B., Wu, J., Li, Q., Gu, S., Chen, Z., & Wang, K. (2017) · RSC Advances · doi:10.1039/c7ra09576g · Cited by 17
Pollak, Y., Mechlovich, D., Amit, T., Bar‐Am, O., Manov, I., Mandel, S. A., Weinreb, O., Meyron‐Holtz, E. G., Iancu, T. C., & Youdim, M. B. H. (2012) · Journal of Neural Transmission · doi:10.1007/s00702-012-0795-x · Cited by 17
Louvel, H. ̈., Kanai, T., Atomi, H., & Reeve, J. N. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01594.x · Cited by 17
Cao, W., McMahon, M. E., Wang, B., O’Connor, R., & Clarkson, M. (2009) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2009.09.003 · Cited by 18
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Lorenzo, R. D., Marzetti, E., Coelho‐Júnior, H. J., Calvani, R., Pesce, V., Landi, F., Leeuwenburgh, C., & Picca, A. (2025) · Cells · doi:10.3390/cells14090672 · Cited by 18
Ma, Y., Dai, L., Qiu, B.-B., Zhou, Y. M., Zhao, Y. Q., Ran, Y., Zhang, K., & Zou, C. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009383 · Cited by 14
Hypobaric Hypoxia Regulates Brain Iron Homeostasis in Rats
Li, Y., Yu, P., Chang, S., Wu, Q., Yu, P., Xie, C., Wu, W., Zhao, B., Gao, G., & Chang, Y. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25822 · Cited by 16
Ye, S., Liang, Q., Li, Z., Xu, S., & Yao, C. (2017) · Tetrahedron · doi:10.1016/j.tet.2017.01.049 · Cited by 16
Martin, D., Nay, K., Robin, F., Rébillard, A., Orfila, L., Martin, B., Leroyer, P., Guggenbuhl, P., Dufresne, S., Noirez, P., et al. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12897 · Cited by 17
Lu, D., Chen, E. Y. T., Lee, P., Wang, Y.-C., Ching, W., Markey, C., Gulstrom, C., Chen, L.-C., Nguyen, T. H., & Chin, W. (2014) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2013.0725 · Cited by 17
Role of Hepcidin in Iron Metabolism and Potential Clinical Applications
Grimes, C. N., Giori, L., & Fry, M. M. (2012) · Veterinary Clinics of North America Small Animal Practice · doi:10.1016/j.cvsm.2011.10.002 · Cited by 16
Ferritin iron minerals are chelator targets, antioxidants, and coated, dietary iron
Theil, E. C. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05575.x · Cited by 16
Daghino, S., Vietro, L. D., Petiti, L., Martino, E. M. D., Dallabona, C., Lodi, T., & Perotto, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-43136-3 · Cited by 16
Khaladkar, M., Liu, J., Wen, D., Wang, J. T. L., & Tian, B. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-189 · Cited by 16
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Hayashi, M., Okazaki, K., Papgiannakopoulos, T., & Motohashi, H. (2024) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041546 · Cited by 16
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Koshizuka, K., Wu, X., Sato, K., Vo, P. T. T., Murawska, G. M., Ishikawa, T., Wang, Z., Molinolo, A., Dennis, E. A., Nathan, C. O., et al. (2025) · Cancer Research · doi:10.1158/0008-5472.can-24-3785 · Cited by 16
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Xiao, Z., Yang, H., Pan, Y., Meng, H., Qu, Z., Kong, B., Shuai, W., & Huang, H. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.08.021 · Cited by 15
Calla, J., Figueroa-Angulo, E. E., Ávila‐González, L., & Arroyo, R. (2014) · BioMed Research International · doi:10.1155/2014/424767 · Cited by 15
Kumari, N., Iordanskiy, S., Kovalskyy, D., Breuer, D., Niu, X., Lin, X., Xu, M., Gavrilenko, K. S., Kashanchi, F., Dhawan, S., et al. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02918-14 · Cited by 15
Russo, A., Putaggio, S., Tellone, E., Calderaro, A., Cirmi, S., Laganà, G., Ficarra, S., Barreca, D., & Patanè, G. T. (2025) · Molecules · doi:10.3390/molecules30061211 · Cited by 18
Guirola, M., Jiménez-Martí, E., & Atrian, S. (2014) · Metallomics · doi:10.1039/c3mt00360d · Cited by 14
Dopamine‑iron homeostasis interaction rescues mitochondrial fitness in Parkinson's disease
Buoso, C., Seifert, M., Lang, M., Griffith, C. M., Andújar, B. T., Rueda, M. P. C., Fischer, C., Doerrier, C., Talasz, H., Zanon, A., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106506 · Cited by 16
Kirchberg, J., Büttner, D., Thiemer, B., & Sawers, R. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034941 · Cited by 14
A novel coumarin-based fluorescence chemosensor for Fe3+
Wang, R., Wan, Q., Feng, F., & Bai, Y. (2014) · Chemical Research in Chinese Universities · doi:10.1007/s40242-014-3192-1 · Cited by 14
Ding, W., Zhang, H., Xu, J., Wen, Y., Zhang, J., Liu, H., Yao, Y., & Zhang, Z. (2016) · Journal of Polymer Science Part A Polymer Chemistry · doi:10.1002/pola.28262 · Cited by 14
A disease-modifying treatment for Alzheimer’s disease: focus on the trans-sulfuration pathway
Berry, T. M., Hamza, E. A., & Moustafa, A. A. (2019) · Reviews in the Neurosciences · doi:10.1515/revneuro-2019-0076 · Cited by 14
Bridle, T. G., Kumarathasan, P., & Gailer, J. (2021) · Molecules · doi:10.3390/molecules26113408 · Cited by 14
Li, X., Yan, X. F., Wang, C., Ma, Y., Jiang, Y. H., Wang, R., Shi, D., Li, Z., Zhu, G., & Tan, B. (2022) · Microchemical Journal · doi:10.1016/j.microc.2022.108123 · Cited by 14
Ding, W., Zhang, G., Zhang, H., Xu, J., Wen, Y., & Zhang, J. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.06.082 · Cited by 14
Iron regulatory protein 2 is a suppressor of mutant p53 in tumorigenesis
Zhang, Y., Feng, X., Zhang, J., Chen, M., Huang, E. C., & Chen, X. (2019) · Oncogene · doi:10.1038/s41388-019-0876-5 · Cited by 17
Bayraktutan, T., Gür, B., & Onganer, Y. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.132448 · Cited by 14
Over-represented sequences located on 3' UTRs are potentially involved in regulatory functions
Yoon, K., Ko, D., Doderer, M. S., Livi, C. B., & Penalva, L. O. F. (2008) · RNA Biology · doi:10.4161/rna.7116 · Cited by 14
Regulation of transferrin receptor 2 in human cancer cell lines
Calzolari, A., Finisguerra, V., Oliviero, I., Deaglio, S., Mariani, G., Malavasi, F., & Testa, U. (2009) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2008.10.001 · Cited by 13
Hu, R., Li, G., Xu, Q., & Chen, L. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.925752 · Cited by 14
An Alternative Mechanism of Subcellular Iron Uptake Deficiency in Cardiomyocytes
Dai, Y., Ignatyeva, N., Xu, H., Wali, R., Toischer, K., Brandenburg, S., Lenz, C., Pronto, J. R. D., Fakuade, F. E., Sossalla, S. T., et al. (2023) · Circulation Research · doi:10.1161/circresaha.122.321157 · Cited by 13
Zhu, L., Chen, C., Cai, Y., Li, Y., Gong, L., Zhu, T., Kong, L., & Luo, J. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116250 · Cited by 14
Chen, C., Xing, Z., Zhang, W., Zheng, L., Zhao, H., Zhang, X., Ding, Y., Tong, Q. Z., Li, Y., Meyron‐Holtz, E. G., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321929121 · Cited by 13
Fujii, J. (2024) · Free Radical Research · doi:10.1080/10715762.2024.2407147 · Cited by 13
Parihar, S., Boricha, V. P., & Jadeja, R. N. (2014) · Luminescence · doi:10.1002/bio.2709 · Cited by 13
A Selective Fluorescence Sensor for Fe (III) Based on Phenanthroimidazole Imine Compound
Gülle, S., & Erbaş, S. Ç. (2017) · Journal of Fluorescence · doi:10.1007/s10895-017-2207-y · Cited by 13
Liu, L., Matsumoto, M., Watanabe‐Matsui, M., Ochiai, K., Callens, B. K. K., Nguyen, L. C., Kozuki, Y., Tanaka, M., Nishizawa, H., & Igarashi, K. (2022) · Antioxidants · doi:10.3390/antiox11081460 · Cited by 13
AIEgen-sensitized lanthanide nanocrystals as luminescent probes for intracellular Fe3+ monitoring
Liu, F., Zhou, W., Li, X., Li, Z., Lu, S., Shang, X., Tan, C. W., Hu, P., Chen, Z., & Chen, X. (2023) · Talanta · doi:10.1016/j.talanta.2023.124729 · Cited by 13
Muckenthaler, M. U., & Lill, R. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_2 · Cited by 13
Mackenzie, E. L., & Tsuji, Y. (2008) · Biochemical Journal · doi:10.1042/bj20071544 · Cited by 13
Karol, N., Brodski, C., Bibi, Y., Kaisman‐Elbaz, T., Forberg, M., Hershfinkel, M., Sekler, I., & Silverman, W. F. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22168 · Cited by 13
Cai, K., & Markley, J. L. (2018) · Molecules · doi:10.3390/molecules23092213 · Cited by 15
Metadata
- Authors
- Rouault, T. A.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Rouault, Tracey A
- ORCID
- Rouault, Tracey A
- Venue
- Nature Chemical Biology
- Published
- 2006-07-18
- Volume
- 2
- Issue
- 8
- Pages
- 406-414
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W1998351143
- Cited by
- 1,055
- References
- 108
- Citations by year
- 2026: 38 · 2025: 47 · 2024: 60 · 2023: 54 · 2022: 57 · 2021: 71 · 2020: 39 · 2019: 59 · 2018: 43 · 2017: 53 · 2016: 40 · 2015: 64 · 2014: 73 · 2013: 36 · 2012: 63
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- 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 regulatory proteins, iron regulatory protein 1, IRP2, iron homeostasis, iron-responsive element, post-transcriptional regulation, iron-sulfur clusters, aconitase, ubiquitin-proteasome degradation, iron deficiency, ferritin, transferrin receptor, hereditary hyperferritinemia-cataract syndrome, neurodegenerative diseases, anemia, embryonic lethality
- MeSH terms
- Iron Deficiencies, Animals, Cataract, Ferritins, Homeostasis, Humans, Iron, Mutation, Protein Conformation, RNA, Messenger, Syndrome, Iron Metabolism Disorders, Response Elements, Iron-Regulatory Proteins
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