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Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Open accessAbstract
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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“Two cytosolic iron sensors, the iron regulatory proteins (IRPs) IRP1 and IRP2 (panel; appendix), regulate iron metabolism post-transcriptionally.12”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [12]
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Cites
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
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
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
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
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- Laufberger, 1937, Sur la cristallisation de la ferritine, Bull. Soc. Chim. Biol., 19, 1575
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Items 101–200 of 287
Lagan, A. L., Melley, D. D., Evans, T. W., & Quinlan, G. J. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00169.2007 · Cited by 52
Direct Fe2+ Sensing by Iron-responsive Messenger RNA·Repressor Complexes Weakens Binding
Khan, M. A., Walden, W. E., Goss, D. J., & Theil, E. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.041061 · Cited by 51
Okazaki, F., Matsunaga, N., Okazaki, H., Azuma, H., Hamamura, K., Tsuruta, A., Tsurudome, Y., Ogino, T., Hara, Y., Suzuki, T., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.713412 · Cited by 53
The Role of Iron in Alcohol-Mediated Hepatocarcinogenesis
Mueller, S., & Rausch, V. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-09614-8_6 · Cited by 52
Cysteine Oxidation Regulates the RNA-Binding Activity of Iron Regulatory Protein 2
由幸, 松., 直人, 篠., Romney, S. J., & Leibold, E. A. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00004-09 · Cited by 52
Self-citationLiu, Y., & Wang, J. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs300 · Cited by 50
Romney, S. J., Thacker, C. M., & Leibold, E. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707043200 · Cited by 50
Self-citationSheftel, A. D., & Lill, R. (2008) · Annals of Medicine · doi:10.1080/07853890802322229 · Cited by 49
HSC20 interacts with frataxin and is involved in iron–sulfur cluster biogenesis and iron homeostasis
Shan, Y., & Cortopassi, G. A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr582 · Cited by 47
Chollangi, S., Thompson, J. W., Ruiz, J. C., Gardner, K. H., & Bruick, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.360404 · Cited by 46
Macková, E., Hrušková, K., Bendová, P., Jirkovská, A., Jansová, H., Hašková, P., Kovařı́ková, P., Vávrová, K., & Šimůnek, T. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.03.010 · Cited by 46
Poller, W. C., Pieber, M., Boehm‐Sturm, P., Ramberger, E., Karampelas, V., Möller, K., Schleicher, M., Wiekhorst, F., Löwa, N., Wagner, S., et al. (2018) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2018.07.013 · Cited by 42
Cell death induced by mitochondrial complex I inhibition is mediated by Iron Regulatory Protein 1
Urrutia, P. J., Aguirre, P., Tapia, V., Carrasco, C. M., Mena, N. P., & Núñez, M. T. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.05.015 · Cited by 44
Iron: Key player in cancer and cell cycle?
Khan, A., Singh, P., & Srivastava, A. (2020) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2020.126582 · Cited by 41
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Salahudeen, A. A., & Bruick, R. K. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05038.x · Cited by 41
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Liu, Y., & Wang, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7686956 · Cited by 40
Ovariectomy and estrogen treatment modulate iron metabolism in rat adipose tissue
Raso, G. M., Irace, C., Esposito, E., Maffettone, C., Iacono, A., Pascale, A. D., Santamaria, R., Colonna, A., & Meli, R. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.05.034 · Cited by 40
Ghio, A. J., Soukup, J. M., Dailey, L. A., & Madden, M. C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.007 · Cited by 39
Guan, P., & Wang, N. (2014) · Nutrition · doi:10.1016/j.nut.2013.12.016 · Cited by 38
Mathematical modeling of the dynamic storage of iron in ferritin
Salgado, J. C., Olivera‐Nappa, Á., Gerdtzen, Z. P., Tapia, V., Theil, E. C., Conca, C., & Núñez, M. T. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-147 · Cited by 36
Valerio, L. G. (2007) · Toxicology Mechanisms and Methods · doi:10.1080/15376510701556690 · Cited by 38
Lee, Y.-K., Lau, Y., Ng, K., Lai, W., Ho, S., Tse, H., Siu, C., & Ho, P. W. (2015) · International Journal of Cardiology · doi:10.1016/j.ijcard.2015.11.101 · Cited by 43
Núñez, M. T. (2010) · BioFactors · doi:10.1002/biof.84 · Cited by 36
Advanced Techniques in Biology & Medicine
Arika, W. M., Ogola, P. E., Nyamai, D. W., Mawia, A. M., Wambua, F. K., Kiboi, N. G., Wambani, J. R., Njagi, S. M., Rachuonyo, H. O., Emmah, K. O., et al. (2018) · Advanced Techniques in Biology & Medicine · doi:10.4172/2379-1764 · Cited by 35
Zhang, H.-Y., Song, N., Jiang, H. F., Bi, M., & Xie, J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.010 · Cited by 35
Liu, C., Zhang, C., Lo, S. Q., Ang, S. T., Chew, K. C. M., Yu, D., Chai, B. H., Tan, B. C. Y., Tsang, F., Tai, Y. K., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.3262-17.2018 · Cited by 34
Triad role of hepcidin, ferroportin, and Nrf2 in cardiac iron metabolism: From health to disease
Jayakumar, D., Narasimhan, K. K. S., & Kalaiselvi, P. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126882 · Cited by 34
Ostareck‐Lederer, A., & Ostareck, D. H. (2012) · Current Protein and Peptide Science · doi:10.2174/138920312801619484 · Cited by 34
Krenn, M. A., Schürz, M., Teufl, B., Uchida, K., Eckl, P., & Bresgen, N. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.12.007 · Cited by 34
Deck, K. M., Vasanthakumar, A., Anderson, S. A., Goforth, J. B., Kennedy, M. C., Antholine, W. E., & Eisenstein, R. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807717200 · Cited by 33
Self-citationSchreinemachers, D. M., & Ghio, A. J. (2016) · Environmental Health Insights · doi:10.4137/ehi.s36225 · Cited by 32
Khan, M. A., Walden, W. E., Theil, E. C., & Goss, D. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-09093-5 · Cited by 33
Davis, M. R., Shawron, K., Rendina-Ruedy, E., Peterson, S., Lucas, E. A., Smith, B. J., & Clarke, S. L. (2011) · Journal of Nutrition · doi:10.3945/jn.111.144105 · Cited by 30
Garré, E., Pelechano, V., del Pino, M. M. S., Alepuz, P. M., & Sunnerhagen, P. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007563 · Cited by 33
Santamaria, R., Fiorito, F., Irace, C., Martino, L. D., Maffettone, C., Granato, G. E., Pascale, A. D., Iovane, V., Pagnini, U., & Colonna, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.02.003 · Cited by 31
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da Silva, I. S., Rausch, V., Seitz, H. K., & Mueller, S. (2017) · Cancers · doi:10.3390/cancers9110145 · Cited by 31
Differential regulation of estrogen in iron metabolism in astrocytes and neurons
Xu, M., Tan, X., Li, N., Wu, H., Wang, Y., Xie, J., & Wang, J. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27188 · Cited by 31
Redox control of iron regulatory protein 2 stability
Hausmann, A., Lee, J., & Pantopoulos, K. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.036 · Cited by 29
Matsuo, S., Ogawa, M., Muckenthaler, M. U., Mizui, Y., Sasaki, S., Fujimura, T., Takizawa, M., Ariga, N., Ozaki, H., Sakaguchi, M., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.694414 · Cited by 30
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Walden, W. E., Selezneva, A. I., & Volz, K. W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.11.018 · Cited by 29
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Figueroa-Angulo, E. E., Calla, J., Mancilla-Olea, M. I., & Arroyo, R. (2015) · Biomolecules · doi:10.3390/biom5043354 · Cited by 28
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Goss, D. J., & Theil, E. C. (2011) · Accounts of Chemical Research · doi:10.1021/ar2001149 · Cited by 28
Khan, M. A., Ma, J., Walden, W. E., Merrick, W. C., Theil, E. C., & Goss, D. J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku248 · Cited by 27
Defects in the rice aconitase-encoding OsACO1 gene alter iron homeostasis
Senoura, T., Kobayashi, T., An, G., Nakanishi, H., & Nishizawa, N. K. (2020) · Plant Molecular Biology · doi:10.1007/s11103-020-01065-0 · Cited by 28
Siderophore-mediated iron trafficking in humans is regulated by iron
Liu, Z., Lanford, R. E., Mueller, S., Gerhard, G. S., Luscieti, S., Sánchez, M., & Devireddy, L. R. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0899-7 · Cited by 27
Ulaş, M., & Çay, M. (2010) · Biological Trace Element Research · doi:10.1007/s12011-010-8669-2 · Cited by 27
AtHO1 is Involved in Iron Homeostasis in an NO-Dependent Manner
Li, H., Song, J. B., Zhao, W. T., & Yang, Z. M. (2013) · Plant and Cell Physiology · doi:10.1093/pcp/pct063 · Cited by 27
Jiang, S., Wang, C., Lan, L., & Zhao, D. (2011) · Nutrition · doi:10.1016/j.nut.2011.08.015 · Cited by 27
Air pollution particles and iron homeostasis
Ghio, A. J., Soukup, J. M., & Dailey, L. A. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.05.026 · Cited by 27
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Zhang, J., Huang, W., Xu, F., Cao, Z., Jia, F., & Li, Y. (2019) · Biological Trace Element Research · doi:10.1007/s12011-019-02008-7 · Cited by 27
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Carota, G., Ronsisvalle, S., Panarello, F., Tibullo, D., Nicolosi, A., & Volti, G. L. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10112306 · Cited by 26
Expression of iron‐related proteins during infection by bovine herpes virus type‐1
Maffettone, C., Martino, L. D., Irace, C., Santamaria, R., Pagnini, U., Iovane, G., & Colonna, A. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21618 · Cited by 25
Damasceno, F. C., Condeles, A. L., Lopes, A. K. B., Facci, R. R., Linares, E., Truzzi, D. R., Augusto, O., & Toledo, J. C. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000883 · Cited by 25
Iron endowment at birth: maternal iron status and other influences
Viteri, F. E. (2011) · Nutrition Reviews · doi:10.1111/j.1753-4887.2011.00449.x · Cited by 26
Rouault, T. A. (2009) · Science · doi:10.1126/science.1181938 · Cited by 25
Kumfu, S., Chattipakorn, S. C., Fucharoen, S., & Chattipakorn, N. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.02.082 · Cited by 24
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Carbajo, C. G., Cornell, L., Madbouly, Y., Lai, Z., Yates, P. A., Tinti, M., & Tiengwe, C. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009696 · Cited by 24
Dycke, C., Bougault, C., Gaillard, J., Andrieu, J., Pantopoulos, K., & Moulis, J. (2007) · Biochemical Journal · doi:10.1042/bj20070983 · Cited by 25
Suo, N., Zhou, Z., Xu, J. H., Cao, D., Wu, B.-F., Zhang, H.-Y., Xu, P., & Zhao, Z. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.907944 · Cited by 23
Werner, T., Hörmannsperger, G., Schuemann, K., Hoelzlwimmer, G., Tsuji, S., & Haller, D. (2009) · Journal of Proteome Research · doi:10.1021/pr800772b · Cited by 23
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Orang, F. N., & Shadbad, M. A. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06732-4 · Cited by 25
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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
Self-citationDoulias, P.-T., Vlachou, C., Boudouri, C., Kanavaros, P., Siamopoulos, K. C., & Galaris, D. (2008) · Free Radical Research · doi:10.1080/10715760801911649 · Cited by 21
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
Myoglobin production in emperor penguins
Ponganis, P. J., Welch, T. J., Welch, L. S., & Stockard, T. K. (2010) · Journal of Experimental Biology · doi:10.1242/jeb.042093 · Cited by 21
Watt, R. K. (2013) · ChemBioChem · doi:10.1002/cbic.201200783 · Cited by 20
Ye, M., Nan, Y.-L., Ding, M., Hu, J.-B., Liu, Q., Wei, W., & Yang, S. (2016) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2016.01.011 · Cited by 20
Asthma as a disruption in iron homeostasis
Ghio, A. J. (2016) · BioMetals · doi:10.1007/s10534-016-9948-y · Cited by 21
Yin, X., Chen, N., Mu, L., Bai, H., Wu, H., Qi, W., Huang, Y., Jian, J., Wang, A., & Ye, J. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.737317 · Cited by 20
Jung, W. H., & Kronstad, J. W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.09.025 · Cited by 19
Chen, S.-C., & Olsthoorn, R. C. L. (2019) · Gene · doi:10.1016/j.gene.2019.06.012 · Cited by 19
Hepcidin treatment in Hfe−/− mice diminishes plasma iron without affecting erythropoiesis
Morán‐Jiménez, M., Méndez, M., Santiago, B., Rodríguez‐García, M. E., Moreno‐Carralero, M., Sánchez‐Lucío, A., Grau, M., & de Salamanca, R. E. (2010) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2010.02291.x · Cited by 19
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Cardona, C. J., & Montgomery, M. R. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1229710 · Cited by 21
Fiorito, F., Irace, C., Pascale, A. D., Colonna, A., Iovane, G., Pagnini, U., Santamaria, R., & Martino, L. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058845 · Cited by 19
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
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
Theil, E. C. (2014) · Metallomics · doi:10.1039/c4mt00136b · Cited by 17
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
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
HOIL-1 is not required for iron-mediated IRP2 degradation in HEK293 cells
Zumbrennen‐Bullough, K. B., Hanson, E. S., & Leibold, E. A. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.07.010 · Cited by 15
Self-citationInfluence of multistrain probiotic and iron supplementation on iron status in rats
Skrypnik, K., Bogdański, P., Sobieska, M., SCHMIDT, M. T., & Suliburska, J. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126849 · Cited by 14
Ovaries of estrogen receptor 1-deficient mice show iron overload and signs of aging
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Suganuma, T., Swanson, S. K., Florens, L. A., Washburn, M. P., & Workman, J. L. (2015) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjv070 · 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
Interaction of ferritin iron responsive element (IRE) mRNA with translation initiation factor eIF4F
Khan, M. A., Malik, A., Domashevskiy, A., San, A., & Khan, J. M. (2020) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2020.118776 · 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
Muckenthaler, M. U., & Lill, R. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_2 · Cited by 13
Skrypnik, K., Bogdański, P., Sobieska, M., & Suliburska, J. (2020) · Molecules · doi:10.3390/molecules25071674 · Cited by 13
He, F., Ma, L., Wang, H., Shen, Z., & Li, M. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9162-z · Cited by 13
Ferroptosis: Regulatory mechanisms and potential targets for bone metabolism: A review
Zhang, Y., Hu, K., Shang, Z., Yang, X., & Cao, L. X. (2024) · Medicine · doi:10.1097/md.0000000000039158 · Cited by 12
Iron nitrosyl complexes are formed from nitrite in the human placenta
Mukosera, G. T., Principe, P., Mata‐Greenwood, E., Liu, T., Schroeder, H. J., Parast, M. M., & Blood, A. B. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102078 · Cited by 11
Iron: Physiology, Dietary Sources, and Requirements
Lönnerdal, B., & Hernell, O. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-375083-9.00164-1 · Cited by 12
Zhang, L., Xiao, S., Kang, X., Sun, T., Zhou, C., Xu, Z., Du, M., Zhang, Y., Wang, G., Liu, Y., et al. (2021) · International Journal of Nanomedicine · doi:10.2147/ijn.s289707 · Cited by 12
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ASS1 deficiency is associated with impaired neuronal differentiation in zebrafish larvae
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The Crosstalk between Micro RNA and Iron Homeostasis
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Metadata
- 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.
- 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)
- 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
- 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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