Binding of a Cytosolic Protein to the Iron-Responsive Element of Human Ferritin Messenger RNA

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262 · see citing works

Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information

Zuker, M., & Stiegler, P. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.1.133 · Cited by 3,604 · see citing works

Iron-Responsive Elements: Regulatory RNA Sequences That Control mRNA Levels and Translation

Casey, J. L., Hentze, M. W., Koeller, D. M., Caughman, S. W., Rouault, T. A., Klausner, R. D., & Harford, J. B. (1988) · Science · doi:10.1126/science.2452485 · Cited by 709 · see citing works

Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs.

Leibold, E. A., & Munro, H. N. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.7.2171 · Cited by 671 · see citing works

Normal and mutant human β-globin pre-mRNAs are faithfully and efficiently spliced in vitro

Krainer, A. R., Maniatis, T., Ruskin, B., & Green, M. R. (1984) · Cell · doi:10.1016/0092-8674(84)90049-7 · Cited by 652 · see citing works

Identification of the iron-responsive element for the translational regulation of human ferritin mRNA

Hentze, 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 · see citing works

Novel mechanism for translational control in regulation of ferritin synthesis by iron.

Zähringer, J., Baliga, B. S., & Munro, H. N. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.3.857 · Cited by 318 · see citing works

A cis-acting element is necessary and sufficient for translational regulation of human ferritin expression in response to iron.

Hentze, M. W., Rouault, T. A., Caughman, S. W., Dancis, A., Harford, J. B., & Klausner, R. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6730 · Cited by 249 · see citing works

Translation of ferritin light and heavy subunit mRNAs is regulated by intracellular chelatable iron levels in rat hepatoma cells.

Rogers, J. T., & Munro, H. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.8.2277 · Cited by 162 · see citing works

Both subunits of rat liver ferritin are regulated at a translational level by iron induction

Aziz, N., & Munro, H. N. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.2.915 · Cited by 161 · see citing works

Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin. A comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed in amphibia.

Dickey, L. F., Sreedharan, S. P., Theil, E. C., Didsbury, J. R., Wang, Y.-H., & Kaufman, R. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47653-3 · Cited by 156 · see citing works

A model for the structure and functions of iron-responsive elements

Hentze, M. W., Caughman, S. W., Casey, J. L., Kodier, D. M., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1988) · Gene · doi:10.1016/0378-1119(88)90145-x · Cited by 116 · see citing works

Structure and expression of the chicken ferritin H-subunit gene.

Stevens, P. W., Dodgson, J. B., & Engel, J. D. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.5.1751 · Cited by 84 · see citing works

Influence of altered transcription on the translational control of human ferritin expression.

Rouault, T. A., Hentze, M. W., Dancis, A., Caughman, W., Harford, J. B., & Klausner, R. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.18.6335 · Cited by 62 · see citing works

Nucleoside and nucleotide inactivation of R17 coat protein: evidence for a transient covalent RNA-protein bond

Romaniuk, P. J., & Uhlenbeck, O. C. (1985) · Biochemistry · doi:10.1021/bi00336a064 · Cited by 53 · see citing works

Isolation of cDNA clones for the light subunit of rat liver ferritin: evidence that the light subunit is encoded by a multigene family.

Brown, A. J. P., Leibold, E. A., & Munro, H. N. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.5.1265 · Cited by 50 · see citing works

The scanning model for translation: an update.

Kozak, M. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.2.229 · Cited by 3,485 · see citing works

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 · see citing works

Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging

Que, E. L., Domaille, D. W., & Chang, C. J. (2008) · Chemical Reviews · doi:10.1021/cr078203u · Cited by 2,063 · see citing works

Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress.

Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292 · see citing works

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 · see citing works

Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury

Mori, K., Lee, H. T., Rapoport, D., Drexler, I. R., Foster, K., Yang, J., Schmidt-Ott, K. M., Chen, X., Li, J. Y., Weiss, S., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23056 · Cited by 954 · see citing works

Traits of fluorescent Pseudomonas spp. involved in suppression of plant root pathogens

O’Sullivan, D. J., & O’Gara, F. (1992) · Microbiological Reviews · doi:10.1128/mr.56.4.662-676.1992 · Cited by 743 · see citing works

Circumstances and Mechanisms of Inhibition of Translation by Secondary Structure in Eucaryotic mRNAs

Kozak, M. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.5134 · Cited by 630 · see citing works

Transition Metals in Control of Gene Expression

O’Halloran, T. V. (1993) · Science · doi:10.1126/science.8342038 · Cited by 626 · see citing works

Forging a field: the golden age of iron biology.

Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623 · see citing works

Intracellular iron transport and storage: from molecular mechanisms to health implications

Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526 · see citing works

A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA

Müllner, E. W., Neupert, B., & Kühn, L. C. (1989) · Cell · doi:10.1016/0092-8674(89)90851-9 · Cited by 497 · see citing works

Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues.

Leco, K. J., Khokha, R., Pavloff, N., Hawkes, S. P., & Edwards, D. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37115-6 · Cited by 480 · see citing works

Endotoxin-responsive sequences control cachectin/tumor necrosis factor biosynthesis at the translational level.

Han, J. S., Brown, T., & Beutler, B. (1990) · The Journal of Experimental Medicine · doi:10.1084/jem.171.2.465 · Cited by 477 · see citing works

HIV-1 structural gene expression requires binding of the Rev trans-activator to its RNA target sequence

Malim, M. H., Tiley, L. S., McCarn, D. F., Rusche, J. R., Hauber, J., & Cullen, B. R. (1990) · Cell · doi:10.1016/0092-8674(90)90670-a · Cited by 430 · see citing works

Biosynthesis of nitric oxide activates iron regulatory factor in macrophages.

Drapier, J. C., Hirling, H., Wietzerbin, J., Kaldy, P., & Kühn, L. C. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06038.x · Cited by 401 · see citing works

Translational regulation via iron‐responsive elements by the nitric oxide/NO‐synthase pathway.

Weiss, G., Goossen, B., Doppler, W., Fuchs, D., Pantopoulos, K., Werner‐Felmayer, G., Wachter, H., & Hentze, M. W. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06039.x · Cited by 389 · see citing works

RNA regulatory elements mediate control of Drosophila body pattern by the posterior morphogen nanos

Wharton, R. P., & Struhl, G. (1991) · Cell · doi:10.1016/0092-8674(91)90368-9 · Cited by 386 · see citing works

Autoregulation of human thymidylate synthase messenger RNA translation by thymidylate synthase.

Chu, E., Koeller, D. M., Casey, J. L., Drake, J. C., Chabner, B. A., Elwood, P. C., Zinn, S., & Allegra, C. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.20.8977 · Cited by 382 · see citing works

Oxidation-Reduction and the Molecular Mechanism of a Regulatory RNA-Protein Interaction

Hentze, M. W., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1989) · Science · doi:10.1126/science.2711187 · Cited by 377 · see citing works

Targeting iron metabolism in drug discovery and delivery

Crielaard, B. J., Lammers, T., & Rivella, S. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.248 · Cited by 352 · see citing works

Identification of a novel iron‐responsive element in murine and human erythroid delta‐aminolevulinic acid synthase mRNA.

Dandekar, T., Stripecke, R., Gray, N. K., Goossen, B., Constable, A., Johansson, H. E., & Hentze, M. W. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07716.x · Cited by 347 · see citing works

Control of mammalian translation by mRNA structure near caps

Babendure, J. R., Babendure, J. L., Ding, J.-H., & Tsien, R. Y. (2006) · RNA · doi:10.1261/rna.2309906 · Cited by 339 · see citing works

Iron regulation of transferrin receptor mRNA levels requires iron‐responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA.

Casey, J. L., Koeller, D. M., Ramin, V. C., Klausner, R. D., & Harford, J. B. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08544.x · Cited by 338 · see citing works

Regulation of ferritin and transferrin receptor mRNAs.

Theil, E. C. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34036-0 · Cited by 334 · see citing works

Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding.

Haile, D. J., Rouault, T. A., Harford, J. B., Kennedy, M. C., Blondin, G. A., Beinert, H., & Klausner, R. D. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11735 · Cited by 321 · see citing works

Contributions of heme and nonheme iron to human nutrition

Carpenter, C. E., & Mahoney, A. W. (1992) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408399209527576 · Cited by 317 · see citing works

Cis-Trans Models for Post-Transcriptional Gene Regulation

Klausner, R. D., & Harford, J. B. (1989) · Science · doi:10.1126/science.2683086 · Cited by 314 · see citing works

IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F.

Muckenthaler, M., Gray, N. K., & Hentze, M. W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80282-8 · Cited by 297 · see citing works

Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: Functional implications

Rouault, T. A., Stout, C. D., Kaptain, S., Harford, J. B., & Klausner, R. D. (1991) · Cell · doi:10.1016/0092-8674(91)90312-m · Cited by 296 · see citing works

Iron sensing and signalling

Evstatiev, R., & Gasché, C. (2011) · Gut · doi:10.1136/gut.2010.214312 · Cited by 292 · see citing works

Molecular control of vertebrate iron homeostasis by iron regulatory proteins

Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287 · see citing works

Coordinate Transcriptional and Translational Regulation of Ferritin in Response to Oxidative Stress

Tsuji, Y., Ayaki, H., Whitman, S. P., Morrow, C. S., Torti, S. V., & Torti, F. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5818-5827.2000 · Cited by 285 · see citing works

Sucrose‐specific signalling represses translation of the Arabidopsis ATB2 bZIP transcription factor gene

Rook, F., Gerrits, N., Kortstee, A. J., van Kampen, M. D., Borrias, M., Weisbeek, P. J., & SMEEKENS, S. C. M. (1998) · The Plant Journal · doi:10.1046/j.1365-313x.1998.00205.x · Cited by 279 · see citing works

Metabolic Enzymes Enjoying New Partnerships as RNA-Binding Proteins

Castelló, A., Hentze, M. W., & Preiß, T. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.012 · Cited by 274 · see citing works

Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster.

Haile, D. J., Rouault, T. A., Tang, C., Chin, J., Harford, J. B., & Klausner, R. D. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7536 · Cited by 270 · see citing works

Living with Iron (and Oxygen): Questions and Answers about Iron Homeostasis

Theil, E. C., & Goss, D. J. (2009) · Chemical Reviews · doi:10.1021/cr900052g · Cited by 265 · see citing works

Translational control during the acute phase response. Ferritin synthesis in response to interleukin-1.

Rogers, J. T., Bridges, K. R., Durmowicz, G. P., Glass, J., Auron, P. E., & Munro, H. N. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77341-9 · Cited by 260 · see citing works

Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity.

Guo, B., Yu, Y., & Leibold, E. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51075-4 · Cited by 257 · see citing works

Iron regulatory proteins and their role in controlling iron metabolism

Kühn, L. C. (2015) · Metallomics · doi:10.1039/c4mt00164h · Cited by 242 · see citing works

A cytosolic protein binds to structural elements within the iron regulatory region of the transferrin receptor mRNA.

Koeller, D. M., Casey, J. L., Hentze, M. W., Gerhardt, E. M., Chan, L.-N. L., Klausner, R. D., & Harford, J. B. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3574 · Cited by 242 · see citing works

Regulation of Iron Metabolism in Eukaryotes

Rouault, T. A., & Klausner, R. D. (1997) · Current topics in cellular regulation · doi:10.1016/s0070-2137(97)80001-5 · Cited by 239 · see citing works

Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation.

Samaniego, F., Chin, J., Iwaï, K., Rouault, T. A., & Klausner, R. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47367-x · Cited by 219 · see citing works

Iron-independent induction of ferritin H chain by tumor necrosis factor

Miller, L. L., Miller, S. C., Torti, S. V., Tsuji, Y., & Torti, F. M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4946 · Cited by 213 · see citing works

Negative regulatory sequences in the lin-14 3'-untranslated region are necessary to generate a temporal switch during Caenorhabditis elegans development.Preprint

Wightman, B., Bürglin, T. R., Gatto, J., Arasu, P., & Ruvkun, G. (1991) · Genes & Development · doi:10.1101/gad.5.10.1813 · Cited by 210 · see citing works

Cloning of the cDNA encoding an RNA regulatory protein--the human iron-responsive element-binding protein.

Rouault, T. A., Tang, C., Kaptain, S., Burgess, W. H., Haile, D. J., Samaniego, F., McBride, O. W., Harford, J. B., & Klausner, R. D. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.20.7958 · Cited by 203 · see citing works

Nuclear and chloroplast mutations affect the synthesis or stability of the chloroplast psbC gene product in Chlamydomonas reinhardtii.

Rochaix, J.-D., Kuchka, M. R., Mayfield, S. P., Schirmer-Rahire, M., Girard‐Bascou, J., & Bennoun, P. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03468.x · Cited by 199 · see citing works

A regulated RNA binding protein also possesses aconitase activity.

Kaptain, S., Downey, W. E., Tang, C., Philpott, C. M., Haile, D. J., Orloff, D. G., Harford, J. B., Rouault, T. A., & Klausner, R. D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10109 · Cited by 201 · see citing works

Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes identifies a family of RNA-binding proteins.

Murray, M. T., Schiller, D. L., & Franke, W. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.1.11 · Cited by 201 · see citing works

Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements.

Gray, N. K., Pantopoulos, K., Dandekar, T., Ackrell, B. A. C., & Hentze, M. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4925 · Cited by 187 · see citing works

Specific Interaction between RNA Phage Coat Proteins and RNA

Witherell, G. W., Gott, J. M., & Uhlenbeck, O. C. (1991) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60842-9 · Cited by 182 · see citing works

A redox switch and phosphorylation are involved in the post-translational up-regulation of the adenosine-uridine binding factor by phorbol ester and ionophore.

Malter, J. S., & Hong, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49969-3 · Cited by 181 · see citing works

Mutational analysis of the [4Fe‐4S]‐cluster converting iron regulatory factor from its RNA‐binding form to cytoplasmic aconitase.

Hirling, H., Henderson, B. R., & Kühn, L. C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06280.x · Cited by 175 · see citing works

Norrie disease is caused by mutations in an extracellular protein resembling C–terminal globular domain of mucins

Meindl, A., Berger, W., Meitinger, T., van de Pol, D., Achatz, H., Doerner, C., Haasemann, M., Hellebrand, H., Gal, A., Cremers, F. P. M., et al. (1992) · Nature Genetics · doi:10.1038/ng1092-139 · Cited by 172 · see citing works

Regulation of Interaction of the Iron-Responsive Element Binding Protein with Iron-Responsive RNA Elements

Haile, D. J., Hentze, M. W., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.5055-5061.1989 · Cited by 172 · see citing works

Characterization of a second RNA-binding protein in rodents with specificity for iron-responsive elements.

Henderson, B. R., Seiser, C., & Kühn, L. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74253-7 · Cited by 162 · see citing works

Iron and the pathophysiology of diabetes

Harrison, A. V., Lorenzo, F. R., & McClain, D. A. (2023) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022522-102832 · Cited by 161 · see citing works

The Ferritin Family of Iron Storage Proteins

Theil, E. C. (1990) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123096.ch7 · Cited by 160 · see citing works

Function of plastid mRNA 3′ inverted repeats

Stern, D. B., Jones, H. B., & Gruissem, W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51530-1 · Cited by 158 · see citing works

Regulation of rat ornithine decarboxylase mRNA translation by its 5'-untranslated region.

Manzella, J. M., & Blackshear, P. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38471-6 · Cited by 154 · see citing works

Optimal sequence and structure of iron-responsive elements. Selection of RNA stem-loops with high affinity for iron regulatory factor

Henderson, B. R., Menotti, E., Bonnard, C., & Kühn, L. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32466-3 · Cited by 151 · see citing works

Regulation of transferrin receptor expression and ferritin content in human mononuclear phagocytes. Coordinate upregulation by iron transferrin and downregulation by interferon gamma.

Byrd, T. F., & Horwitz, M. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116318 · Cited by 149 · see citing works

Haploid spermatids exhibit translationally repressed mRNAs

Steger, K. (2001) · Anatomy and Embryology · doi:10.1007/s004290100176 · Cited by 148 · see citing works

Position Is the Critical Determinant for Function of Iron-Responsive Elements as Translational Regulators

Goossen, B., & Hentze, M. W. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.1959-1966.1992 · Cited by 145 · see citing works

Translational repression by a complex between the iron‐responsive element of ferritin mRNA and its specific cytoplasmic binding protein is position‐dependent in vivo.

Goossen, B., Caughman, S. W., Harford, J. B., Klausner, R. D., & Hentze, M. W. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07635.x · Cited by 144 · see citing works

The iron-responsive element binding protein: a method for the affinity purification of a regulatory RNA-binding protein.

Rouault, T. A., Hentze, M. W., Haile, D. J., Harford, J. B., & Klausner, R. D. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5768 · Cited by 142 · see citing works

Cytoplasmic protein binding to highly conserved sequences in the 3' untranslated region of mouse protamine 2 mRNA, a translationally regulated transcript of male germ cells.

Kwon, Y. K., & Hecht, N. B. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.3584 · Cited by 142 · see citing works

Adiponectin translation is increased by the PPARγ agonists pioglitazone and ω-3 fatty acids

Banga, A., Ünal, R., Tripathi, P., Pokrovskaya, I. D., Owens, R. J., Kern, P. A., & Ranganathan, G. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90892.2008 · Cited by 139 · see citing works

Recombinant iron‐regulatory factor functions as an iron‐responsive‐element‐binding protein, a translational repressor and an aconitase

Gray, N. K., QUICK, S., Goossen, B., Constable, A., Hirling, H., Kühn, L. C., & Hentze, M. W. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18420.x · Cited by 140 · see citing works

IRP2 Regulates Breast Tumor Growth

Wang, W., Deng, Z., Hatcher, H., Miller, L. D., Di, X., Tesfay, L., Sui, G., D'Agostino, R. B., Torti, F. M., & Torti, S. V. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1224 · Cited by 137 · see citing works

Purification of a Specific Repressor of Ferritin mRNA Translation from Rabbit Liver

Walden, W. E., Patiño, M. M., & Gaffield, L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80066-7 · Cited by 134 · see citing works

Iron in the Brain: An Important Contributor in Normal and Diseased States

Piñero, D. J., & Connor, J. R. (2000) · The Neuroscientist · doi:10.1177/107385840000600607 · Cited by 131 · see citing works

Characterization and Expression of Iron Regulatory Protein 2 (IRP2)

Guo, B., Brown, F. M., Phillips, J. D., Yu, Y., & Leibold, E. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16529 · Cited by 129 · see citing works

Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: switching between enzymatic and genetic function?

Constable, A., Quick, S., Gray, N. K., & Hentze, M. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4554 · Cited by 127 · see citing works

Iron-regulatory proteins: molecular biology and pathophysiological implications

Cairo, G., & Recalcati, S. (2007) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399407000531 · Cited by 124 · see citing works

Iron-Responsive miR-485-3p Regulates Cellular Iron Homeostasis by Targeting Ferroportin

Sangokoya, C., Doss, J. F., & Chi, J. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003408 · Cited by 122 · see citing works

Regulation of Cellular Iron Metabolism by Erythropoietin: Activation of Iron-Regulatory Protein and Upregulation of Transferrin Receptor Expression in Erythroid Cells

Weiß, G., Houston, T. E., Kastner, S., Jöhrer, K., Grünewald, K., & Brock, J. H. (1997) · Blood · doi:10.1182/blood.v89.2.680 · Cited by 123 · see citing works

The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution

Rothenberger, S., Müllner, E. W., & Kühn, L. C. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.5.1175 · Cited by 123 · see citing works

Two mechanisms of iron uptake from transferrin by melanoma cells. The effect of desferrioxamine and ferric ammonium citrate.

Richardson, D. R., & Baker, E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49665-8 · Cited by 118 · see citing works

Structure and expression of the gene encoding the periplasmic arylsulfatase of Chlamydomonas reinhardtii

de Hostos, E. L., Schilling, J., & Grossman, A. R. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00331273 · Cited by 116 · see citing works

Derepression of Ferritin Mmessenger RNA Translation by Hemin in Vitro

Lin, J.-J., Daniels-McQueen, S., Patiño, M. M., Gaffield, L., Walden, W. E., & Thach, R. E. (1990) · Science · doi:10.1126/science.2294594 · Cited by 116 · see citing works

Probing Structure-Function Relations In Ferritin And Bacterioferritin

Harrison, P. M., Andrews, S. C., Artymiuk, P. J., Ford, G. C., Guest, J. R., Hirzmann, J., Lawson, D. M., Livingstone, J. C., Smith, J. M., Treffry, A., et al. (1991) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60046-x · Cited by 114 · see citing works

Hemin-Mediated Regulation of an Antioxidant-Responsive Element of the Human Ferritin H Gene and Role of Ref-1 during Erythroid Differentiation of K562 Cells

Iwasaki, K., MacKenzie, E. L., Hailemariam, K., Sakamoto, K., & Tsuji, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2845-2856.2006 · Cited by 112 · see citing works

Iron Regulatory Proteins 1 and 2 Bind Distinct Sets of RNA Target Sequences

Henderson, B. R., Menotti, E., & Kühn, L. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.4900 · Cited by 112 · see citing works

Structural requirements of iron-responsive elements for binding of the protein involved in both transferrin receptor and ferritin mRNA post-transcriptional regulation

Leibold, E. A., Laudano, A. P., & Yu, Y. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.7.1819 · Cited by 112 · see citing works

Sendai Virus Y Proteins Are Initiated by a Ribosomal Shunt

Latorre, P., Kolakofsky, D., & Curran, J. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.9.5021 · Cited by 110 · see citing works

5 Iron metabolism in inflammation

Konijn, A. M. (1994) · Baillière s Clinical Haematology · doi:10.1016/s0950-3536(05)80127-1 · Cited by 108 · see citing works

The iron cycle and oxidative stress in the lung

Turi, J. L., Yang, F., Garrick, M. D., Piantadosi, C. A., & Ghio, A. J. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.12.008 · Cited by 108 · see citing works

Control of Start Codon Choice on a Plant Viral RNA Encoding Overlapping Genes

Dinesh-Kumar, S. P., & Miller, W. A. (1993) · The Plant Cell · doi:10.1105/tpc.5.6.679 · Cited by 107 · see citing works

The 5′-Untranslated Region of Picornaviral Genomes

Agol, V. I. (1991) · Advances in virus research · doi:10.1016/s0065-3527(08)60278-x · Cited by 104 · see citing works

Tumor necrosis factor-alpha and interleukin 1-alpha regulate transferrin receptor in human diploid fibroblasts. Relationship to the induction of ferritin heavy chain.

Tsuji, Y., Miller, L. L., Miller, S. C., Torti, S. V., & Torti, F. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89638-0 · Cited by 103 · see citing works

Increased Expression of Iron-Regulating Genes in Monkey and Human Glaucoma

Farkas, R. H. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0872 · Cited by 101 · see citing works

An RNA hairpin at the extreme 5' end of the poliovirus RNA genome modulates viral translation in human cells

SIMOES, E. A. F., & Sarnow, P. (1991) · Journal of Virology · doi:10.1128/jvi.65.2.913-921.1991 · Cited by 100 · see citing works

Genetics of iron regulation and the possible role of iron in Parkinson's disease

Rhodes, S. L., & Ritz, B. R. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.07.001 · Cited by 99 · see citing works

Tumor Cell Cytotoxicity of a Novel Metal Chelator

Torti, S. V., Torti, F. M., Whitman, S. P., Brechbiel, M. W., Park, G., & Planalp, R. P. (1998) · Blood · doi:10.1182/blood.v92.4.1384 · Cited by 98 · see citing works

Age-Dependent Retinal Iron Accumulation and Degeneration in Hepcidin Knockout Mice

Hadziahmetovic, M., Song, Y., Ponnuru, P., Iacovelli, J., Hunter, A. A., Haddad, N., Beard, J., Connor, J. R., Vaulont, S., & Dunaief, J. L. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-6113 · Cited by 98 · see citing works

Differential Modulation of the RNA-binding Proteins IRP-1 and IRP-2 in Response to Iron

Henderson, B. R., & Kühn, L. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.35.20509 · Cited by 95 · see citing works

Interleukin-2-dependent transcriptional and post-transcriptional regulation of transferrin receptor mRNA

Seiser, C., Teixeira, S. M. R., & Kühn, L. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38621-1 · Cited by 92 · see citing works

Hypoxia Alters Iron-regulatory Protein-1 Binding Capacity and Modulates Cellular Iron Homeostasis in Human Hepatoma and Erythroleukemia Cells

Toth, I., Yuan, L., Rogers, J. T., Boyce, H., & Bridges, K. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4467 · Cited by 91 · see citing works

Positive and negative control of translation by the leader sequence of cauliflower mosaic virus pregenomic 35S RNA.

Fütterer, J., Gordon, K. H. J., Sanfaçon, H., Bonneville, J., & Höhn, T. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08293.x · Cited by 91 · see citing works

The iron-responsive element is the single element responsible for iron-dependent translational regulation of ferritin biosynthesis: evidence for function as the binding site for a translational repressor.

Caughman, S. W., Hentze, M. W., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37387-3 · Cited by 85 · see citing works

Identification of the iron-responsive element for the translational regulation of human ferritin mRNA

Hentze, 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 · see citing works

Translational repression by a complex between the iron‐responsive element of ferritin mRNA and its specific cytoplasmic binding protein is position‐dependent in vivo.

Goossen, B., Caughman, S. W., Harford, J. B., Klausner, R. D., & Hentze, M. W. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07635.x · Cited by 144 · see citing works

Determinants of the interaction between the iron-responsive element-binding protein and its binding site in rat L-ferritin mRNA.

Barton, H. A., Eisenstein, R. S., Bomford, A. B., & Munro, H. N. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39250-6 · Cited by 111 · see citing works

Coordinate Post-Transcriptional Regulation of Ferritin and Transferrin Receptor Expression: The Role of Regulated RNA-Protein Interaction

Harford, J. B., & Klausner, R. D. (2017) · Enzyme · doi:10.1159/000468745 · Cited by 87 · see citing works