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.
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
“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
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 999
Crooks, D. R., Maio, N., Lane, A. N., Jarník, M., Higashi, R. M., Haller, R. G., Yang, Y., Fan, T. W. ‐., Linehan, W. M., & Rouault, T. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001885 · Cited by 102
Mitochondrial iron metabolism and its role in diseases
Gao, J., Zhou, Q., Wu, D., & Chen, L. (2020) · Clinica Chimica Acta · doi:10.1016/j.cca.2020.12.005 · Cited by 111
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 family of iron responsive RNA structures regulated by changes in cellular iron and oxygen
Leipuvienė, R., & Theil, E. C. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7198-4 · Cited by 106
Iron–Sulfur Clusters: Biogenesis, Molecular Mechanisms, and Their Functional Significance
Xu, X. M., & Møller, S. G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3259 · Cited by 102
Iron homeostasis imbalance and ferroptosis in brain diseases
Long, H., Zhu, W., Wei, L., & Zhao, J. (2023) · MedComm · doi:10.1002/mco2.298 · Cited by 108
miR-20a regulates expression of the iron exporter ferroportin in lung cancer
Babu, K. R., & Muckenthaler, M. U. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-015-1362-3 · Cited by 101
Ripa, R., Dolfi, L., Terrigno, M., Pandolfini, L., Savino, A., Arcucci, V., Groth, M., Tozzini, E. T., Baumgart, M., & Cellerino, A. (2017) · BMC Biology · doi:10.1186/s12915-017-0354-x · Cited by 109
Long, L., Zhou, L., Wang, L., Meng, S., Gong, A., & Chi Zhang, A. (2014) · Analytica Chimica Acta · doi:10.1016/j.aca.2013.12.024 · Cited by 101
Iron-Dependent RNA-Binding Activity of Mycobacterium tuberculosis Aconitase
Banerjee, S., Nandyala, A. K., Raviprasad, P., Ahmed, N., & Hasnain, S. E. (2007) · Journal of Bacteriology · doi:10.1128/jb.00026-07 · Cited by 98
Iron‐induced NCOA4 condensation regulates ferritin fate and iron homeostasis
Kuno, S., Fujita, H., Tanaka, Y., Ogra, Y., & Iwaï, K. (2022) · EMBO Reports · doi:10.15252/embr.202154278 · Cited by 102
Singh, P., Arpita, Kumar, S., Kumar, P., Kataria, N., Bhankar, V., Kumar, K., Kumar, R., Hsieh, C., & Khoo, K. S. (2023) · Nanoscale · doi:10.1039/d3nr01966g · Cited by 99
Understanding Anthracycline Cardiotoxicity From Mitochondrial Aspect
Huang, J., Wu, R., Chen, L., Yang, Z., Yan, D., & Li, M. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.811406 · Cited by 102
Mitochondrial ferritin in the regulation of brain iron homeostasis and neurodegenerative diseases
Gao, G., & Chang, Y. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00019 · Cited by 95
In vivo magnetic resonance imaging of ferritin-based reporter visualizes native neuroblast migration
Iordanova, B. E., & Ahrens, E. T. (2011) · NeuroImage · doi:10.1016/j.neuroimage.2011.08.068 · Cited by 97
Zeng, L., Zhou, J., Wang, X., Zhang, Y., Wang, M., & Su, P. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.09.028 · Cited by 96
Ceruloplasmin Protects Injured Spinal Cord from Iron-Mediated Oxidative Damage
Rathore, K. I., Kerr, B. J., Redensek, A., López‐Vales, R., Jeong, S. Y., Ponka, P., & David, S. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3649-08.2008 · Cited by 98
Abnormal erythropoiesis and the pathophysiology of chronic anemia
Koury, M. J. (2014) · Blood Reviews · doi:10.1016/j.blre.2014.01.002 · Cited by 98
Chereddy, N. R., Thennarasu, S., & Mandal, A. B. (2013) · The Analyst · doi:10.1039/c3an36577h · Cited by 93
Petroutsos, D., Terauchi, A. M., Busch, A., Hirschmann, I., Merchant, S., Finazzi, G., & Hippler, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.050468 · Cited by 94
Iron Uptake Mediated by Binding of H-Ferritin to the TIM-2 Receptor in Mouse Cells
Han, J., Seaman, W. E., Di, X., Wang, W., Willingham, M. C., Torti, F. M., & Torti, S. V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023800 · Cited by 93
Ferric iron reductases and their contribution to unicellular ferrous iron uptake
Cain, T. J., & Smith, A. T. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111407 · Cited by 92
Ghosh, M. C., Tong, W.-H., Zhang, D., Ollivierre, H., Singh, A., Krishna, M. C., Mitchell, J. B., & Rouault, T. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805361105 · Cited by 91
Coenzyme A corrects pathological defects in human neurons of PANK2‐associated neurodegeneration
Orellana, D. I., Santambrogio, P., Rubio, A., Yekhlef, L., Cancellieri, C., Dusi, S., Giannelli, S. G., Venco, P., Mazzara, P. G., Cozzi, A., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606391 · Cited by 93
The role of ferroptosis in intervertebral disc degeneration
Fan, C., Chu, G., Yu, Z., Ji, Z., Kong, F., Yao, L., Wang, J., Geng, D., Wu, X., & Mao, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1219840 · Cited by 94
MicroRNA-152-mediated dysregulation of hepatic transferrin receptor 1 in liver carcinogenesis
Kindrat, I., Tryndyak, V., de Conti, A., Shpyleva, S., Mudalige, T., Kobets, T., Еrstenyuk, H. M., Beland, F. A., & Pogribny, I. P. (2015) · Oncotarget · doi:10.18632/oncotarget.6004 · Cited by 92
Uhrigshardt, H., Singh, A., Kovtunovych, G., Ghosh, M. C., & Rouault, T. A. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq301 · Cited by 93
Hereditary Sideroblastic Anemias: Pathophysiology, Diagnosis, and Treatment
Camaschella, C. (2009) · Seminars in Hematology · doi:10.1053/j.seminhematol.2009.07.001 · Cited by 92
Jackson, K. A., Helston, R. M., McKay, J. A., O'Neill, E. D., Mathers, J. C., & Ford, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610535200 · Cited by 91
Qiu, L., Zhu, C., Chen, H., Hu, M., He, W., & Guo, Z. (2014) · Chemical Communications · doi:10.1039/c3cc49482a · Cited by 90
Reciprocal Regulation of Endocytosis and Metabolism
Antonescu, C. N., McGraw, T. E., & Klip, A. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016964 · Cited by 104
Sato, T., Chang, H., Bayeva, M., Shapiro, J. S., Ramos-Alonso, L., Kouzu, H., Jiang, X., Liu, T., Yar, S., Sawicki, K. T., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804701115 · Cited by 87
Berndt, A., Leme, A. S., & Shapiro, S. D. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100627 · Cited by 89
Lakhal‐Littleton, S., Crosby, A., Frise, M. C., Mohammad, G. H., Carr, C. A., Loick, P., & Robbins, P. A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1822010116 · Cited by 86
Soliman, A. T., Sanctis, V. D., & Kalra, S. (2014) · Indian Journal of Endocrinology and Metabolism · doi:10.4103/2230-8210.145038 · Cited by 86
Iron and the heart: A paradigm shift from systemic to cardiomyocyte abnormalities
Paterek, A., Mackiewicz, U., & Ma̧czewski, M. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28820 · Cited by 88
Iron Dysregulation in Mitochondrial Dysfunction and Alzheimer’s Disease
Onukwufor, J. O., Dirksen, R. T., & Wojtovich, A. P. (2022) · Antioxidants · doi:10.3390/antiox11040692 · Cited by 85
SIRT3 regulates cellular iron metabolism and cancer growth by repressing iron regulatory protein 1
Jeong, S. M., Lee, J. J., Finley, L. W. S., Schmidt, P. J., Fleming, M. D., & Haigis, M. C. (2014) · Oncogene · doi:10.1038/onc.2014.124 · Cited by 87
Ba, Q., Zhou, N., Duan, J., Chen, T., Hao, M., Yang, X., Li, J., Yin, J., Chu, R., & Wang, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042703 · Cited by 84
Arnaud, N., Ravet, K., Borlotti, A., Touraine, B., Boucherez, J., Fizames, C., Briat, J., Cellier, F., & Gaymard, F. (2007) · Biochemical Journal · doi:10.1042/bj20061874 · Cited by 83
Could Alzheimer’s Disease Originate in the Periphery and If So How So?
Morris, G., Berk, M., Maes, M. H. J., & Puri, B. K. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1092-y · Cited by 86
Irp2 regulates insulin production through iron-mediated Cdkal1-catalyzed tRNA modification
Ferreira, M. C., Anderson, C. P., Neschen, S., Zumbrennen‐Bullough, K. B., Romney, S. J., Kahle, M., Rathkolb, B., Gailus‐Durner, V., Fuchs, H., Wolf, E., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14004-5 · Cited by 85
Zarruk, J. G., Berard, J. L., dos Santos, R. P., Kroner, A., Lee, J., Arosio, P., & David, S. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.001 · Cited by 79
Iron Homeostasis and Its Interaction with Prolyl Hydroxylases
Mole, D. R. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2790 · Cited by 80
Yeast aconitase binds and provides metabolically coupled protection to mitochondrial DNA
Chen, X. J., Wang, X., & Butow, R. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703078104 · Cited by 81
Iron metabolism: a double-edged sword in the resistance of glioblastoma to therapies
Legendre, C., & Garcion, E. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.03.008 · Cited by 78
Aminoxy-linked rhodamine hydroxamate as fluorescent chemosensor for Fe3+ in aqueous media
Moon, K., Yang, Y., Ji, S., & Tae, J. (2010) · Tetrahedron Letters · doi:10.1016/j.tetlet.2010.04.068 · Cited by 80
Significance of Programmed Cell Death Pathways in Neurodegenerative Diseases
Guo, D., Liu, Z., Zhou, J., Ke, C., & Li, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189947 · Cited by 83
Das, N. K., Biswas, S., Solanki, S., & Mukhopadhyay, C. K. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01241.x · Cited by 80
Iron Homeostasis and Nutritional Iron Deficiency1–3
Theil, E. C. (2011) · Journal of Nutrition · doi:10.3945/jn.110.127639 · Cited by 81
Hickok, J. R., Sahni, S., Mikhed, Y., Bonini, M. G., & Thomas, D. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287052 · Cited by 80
Shu, W., Baumann, B. H., Song, Y., Liu, Y., Wu, X., & Dunaief, J. L. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101469 · Cited by 77
Karim, W., Kleibert, A., Hartfelder, U., Balan, A., Gobrecht, J., van Bokhoven, J. A., & Ekinci, Y. (2016) · Scientific Reports · doi:10.1038/srep18818 · Cited by 78
NRF2 and Hypoxia-Inducible Factors: Key Players in the Redox Control of Systemic Iron Homeostasis
Duarte, T. L., Talbot, N. P., & Drakesmith, H. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8148 · Cited by 77
Ferroptosis: an important player in the inflammatory response in diabetic nephropathy
Li, J., Li, L., Zhang, Z., Chen, P., Shu, H., Yang, C., Chu, Y., & Liu, J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1294317 · Cited by 82
Recent advances in the understanding of inherited sideroblastic anaemia
Camaschella, C. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07290.x · Cited by 79
A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis
Song, D., & Lee, F. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708077200 · Cited by 79
Mechanisms of endonuclease‐mediated mRNA decay
Schoenberg, D. R. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.78 · Cited by 75
Iron Deprivation Suppresses Hepatocellular Carcinoma Growth in Experimental Studies
Ba, Q., Hao, M., Huang, H., Hou, J., Ge, S., Zhang, Z., Yin, J., Chu, R., Jiang, H., Wang, F., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-3099 · Cited by 75
Basiri, S., Mehdinia, A., & Jabbari, A. (2018) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2018.02.053 · Cited by 75
Romney, S. J., Newman, B. S., Thacker, C. M., & Leibold, E. A. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002394 · Cited by 76
Rausa, M., Pagani, A., Nai, A., Campanella, A., Gilberti, M. E., Apostoli, P., Camaschella, C., & Silvestri, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122696 · Cited by 80
Roles of Fe–S proteins: from cofactor synthesis to iron homeostasis to protein synthesis
Pain, D., & Dancis, A. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.03.006 · Cited by 72
Mechanisms of cardiac iron homeostasis and their importance to heart function
Lakhal‐Littleton, S. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.010 · Cited by 74
Shrivas, K. K., Monisha, M., Kant, T., Karbhal, I., Kurrey, R., Sahu, B., Sinha, D., Patra, G. K., Deb, M. K., & Pervez, S. (2020) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-019-02385-x · Cited by 74
A Quantitative and Predictive Model for RNA Binding by Human Pumilio Proteins
Jarmoskaite, I., Denny, S. K., Vaidyanathan, P. P., Becker, W. R., Andreasson, J. O. L., Layton, C. J., Kappel, K., Shivashankar, V., Sreenivasan, R., Das, R., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.04.012 · Cited by 76
Dornelles, A. D. S., Garcia, V. A., de Lima, M. N. M., Vedana, G., Alcalde, L. A., Bogo, M. R., & Schröder, N. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0100-z · Cited by 74
Apoferritin Applications in Nanomedicine
Heger, Z., Skalíčková, S., Zítka, O., Adam, V., & Kizek, R. (2014) · Nanomedicine · doi:10.2217/nnm.14.119 · Cited by 73
Elucidating the Molecular Function of Human BOLA2 in GRX3-Dependent Anamorsin Maturation Pathway
Banci, L., Camponeschi, F., Ciofi‐Baffoni, S., & Muzzioli, R. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10592 · Cited by 73
Thompson, J. W., Salahudeen, A. A., Chollangi, S., Ruiz, J. C., Brautigam, C. A., Makris, T. M., Lipscomb, J. D., Tomchick, D. R., & Bruick, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308684 · Cited by 71
Tetraphenylethene functionalized rhodamine chemosensor for Fe3+ and Cu2+ ions in aqueous media
Yang, Y., Gao, C., Zhang, N., & Dong, D. (2015) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2015.08.125 · Cited by 72
Iron-Dependent Degradation of Apo-IRP1 by the Ubiquitin-Proteasome Pathway
Wang, J., Fillebeen, C., Chen, G., Biederbick, A., Lill, R., & Pantopoulos, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01111-06 · Cited by 72
Iron and Neurodegeneration: From Cellular Homeostasis to Disease
Batista-Nascimento, L. S., Pimentel, C., Menezes, R., & Rodrigues‐Pousada, C. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/128647 · Cited by 74
Ma, J., Haldar, S., Khan, M. A., Sharma, S. D., Merrick, W. C., Theil, E. C., & Goss, D. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120045109 · Cited by 72
Decreasing TfR1 expression reverses anemia and hepcidin suppression in β-thalassemic mice
Li, H., Choesang, T., Bao, W., Chen, H., Feola, M., Garcia‐Santos, D., Li, J., Sun, S., Follenzi, A., Pham, P., et al. (2017) · Blood · doi:10.1182/blood-2016-09-742387 · Cited by 72
Shen, B., & Qian, Y. (2018) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2017.12.146 · Cited by 70
Age-Related Changes and Sex-Related Differences in Brain Iron Metabolism
Kezele, T. G., & Ćurko‐Cofek, B. (2020) · Nutrients · doi:10.3390/nu12092601 · Cited by 78
Fighting Iron-Deficiency Anemia: Innovations in Food Fortificants and Biofortification Strategies
Liberal, Â., Pinela, J., Quintana, A. M. V., Ferreira, I. C. F. R., & Barros, L. (2020) · Foods · doi:10.3390/foods9121871 · Cited by 83
Mitochondrial Iron Metabolism: The Crucial Actors in Diseases
Duan, G., Li, J., Duan, Y., Zheng, C., Guo, Q., Li, F., Zheng, J., Yu, J., Zhang, P., Wan, M., et al. (2022) · Molecules · doi:10.3390/molecules28010029 · Cited by 74
Maffettone, C., Chen, G., Drozdov, I. A., Ouzounis, C. A., & Pantopoulos, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010163 · Cited by 68
RNA decay modulates gene expression and controls its fidelity
Ghosh, S., & Jacobson, A. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.25 · Cited by 70
Aging-related changes in the iron status of skeletal muscle
DeRuisseau, K. C., Park, Y.-M., DeRuisseau, L. R., Cowley, P. M., Fazen, C. H., & Doyle, R. P. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.08.011 · Cited by 69
Mechanisms of mammalian zinc-regulated gene expression
Jackson, K. A., Valentine, R. A., Coneyworth, L. J., Mathers, J. C., & Ford, D. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361262 · Cited by 72
Xu, J., Hou, Y., Ma, Q., Wu, X.-F., & Wei, X. (2013) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2013.04.044 · Cited by 69
Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin
Condò, I., Malisan, F., Guccini, I., Serio, D., Rufini, A., & Testi, R. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddp592 · Cited by 68
Ganesan, J. S., Murugesan, S., Ashokkumar, B., & Siva, A. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117993 · Cited by 66
Pedro-Segura, E., Vergara, S. V., Rodríguez‐Navarro, S., Parker, R., Thiele, D. J., & Puig, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804910200 · Cited by 72
Iron Homeostasis Regulates the Activity of the MicroRNA Pathway through Poly(C)-Binding Protein 2
Li, Y., Lin, L., Li, Z., Ye, X., Xiong, K., Aryal, B., Xu, Z., Paroo, Z., Liu, Q., He, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.021 · Cited by 66
Portable and selective colorimetric film and digital image colorimetry for detection of iron
Choodum, A., Sriprom, W., & Wongniramaikul, W. (2018) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2018.09.062 · Cited by 69
Iron homeostasis: new players, newer insights
Edison, E. S., Bajel, A. R., & Chandy, M. (2008) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2008.01143.x · Cited by 71
Yang, L., Yang, W., Xu, D., Zhang, Z., & Liu, A. (2012) · Dyes and Pigments · doi:10.1016/j.dyepig.2012.12.016 · Cited by 66
Heterogeneity of nervous system mitochondria: Location, location, location!
Dubinsky, J. M. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.020 · Cited by 67
Zhang, S., Cao, Y., & Yang, Q. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008682 · Cited by 64
From Iron Metabolism to Ferroptosis: Pathologic Changes in Coronary Heart Disease
Fan, X., Li, A., Yan, Z., Geng, X., Lian, L., Lv, H., Gao, D., & Zhang, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/6291889 · Cited by 68
Mitoferrin, Cellular and Mitochondrial Iron Homeostasis
Ali, M. Y., Oliva, C. R., Flor, S., & Griguer, C. E. (2022) · Cells · doi:10.3390/cells11213464 · Cited by 66
Mehta, V. N., Kailasa, S. K., & Wu, H. (2013) · New Journal of Chemistry · doi:10.1039/c3nj01468a · Cited by 65
Fetal regulation of iron transport during pregnancy
Gambling, L., Lang, C., & McArdle, H. J. (2011) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.000885 · Cited by 65
The critical role of ferritinophagy in human disease
Liu, M., Kong, N., Zhang, G., Xu, Q. L., Xu, Y. Y., Ke, P., & Liu, C. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.933732 · Cited by 64
Ferroptosis inhibitor improves outcome after early and delayed treatment in mild spinal cord injury
Ryan, F., Blex, C., Ngo, T. D., Kopp, M. A., Michalke, B., Venkataramani, V., Curran, L., Schwab, J. M., Ruprecht, K., Otto, C., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02758-2 · Cited by 68
Iron-sulfur proteins hiding in plain sight
Rouault, T. A. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1843 · Cited by 64
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
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