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

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

Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA

Pelletier, J., & Sonenberg, N. (1988) · Nature · doi:10.1038/334320a0 · Cited by 1,953

Transcription termination and 3′ processing: the end is in site!

Birnstiel, M. L., Busslinger, M., & Strub, K. (1985) · Cell · doi:10.1016/s0092-8674(85)80007-6 · Cited by 1,388

TRANSCRIPTION TERMINATION AND THE REGULATION OF GENE EXPRESSION

Platt, T. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.002011 · Cited by 793

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

Influences of mRNA secondary structure on initiation by eukaryotic ribosomes.

Kozak, M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.9.2850 · Cited by 687

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

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 633

Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency

Pelletier, J., & Sonenberg, N. (1985) · Cell · doi:10.1016/0092-8674(85)90200-4 · Cited by 610

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

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

Structural features in eukaryotic mRNAs that modulate the initiation of translation.

Kozak, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54860-2 · Cited by 1,826

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

Molecular mechanisms of translational control

Gebauer, F., & Hentze, M. W. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1488 · Cited by 991

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

CONTROL OF TRANSLATION INITIATION IN ANIMALS

Gray, N. K., & Wickens, M. (1998) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.14.1.399 · Cited by 500

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

Human erythroid 5‐aminolevulinate synthase: promoter analysis and identification of an iron‐responsive element in the mRNA.

Cox, T. C., Bawden, M. J., Martin, A., & May, B. K. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07715.x · Cited by 360

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

Post-transcriptional gene regulatory mechanisms in eukaryotes: an overview

Day, D., & Tuite, M. F. (1998) · Journal of Endocrinology · doi:10.1677/joe.0.1570361 · Cited by 304

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

Iron Regulates the Intracellular Degradation of Iron Regulatory Protein 2 by the Proteasome

Guo, B., Phillips, J. D., Yu, Y., & Leibold, E. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21645 · Cited by 287

Iron regulatory protein prevents binding of the 43S translation pre‐initiation complex to ferritin and eALAS mRNAs.

Gray, N. K., & Hentze, M. W. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06699.x · Cited by 276

Cap-dependent and cap-independent translation in eukaryotic systems

Merrick, W. C. (2004) · Gene · doi:10.1016/j.gene.2004.02.051 · Cited by 276

Signalling to eIF4E in cancer

Siddiqui, N., & Sonenberg, N. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150126 · Cited by 225

Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells.

Melefors, Ö., Goossen, B., Johansson, H. E., Stripecke, R., Gray, N. K., & Hentze, M. W. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53414-1 · Cited by 200

Iron regulatory elements (IREs): a family of mRNA non-coding sequences

Theil, E. C. (1994) · Biochemical Journal · doi:10.1042/bj3040001 · Cited by 192

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

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

Translation driven by an eIF4G core domain in vivo

Gregorio, E. D., Preiß, T., & Hentze, M. W. (1999) · The EMBO Journal · doi:10.1093/emboj/18.17.4865 · Cited by 169

Corticotropin releasing hormone receptors: two decades later

Aguilera, G., Nikodémová, M., WYNN, P. C., & Catt, K. J. (2004) · Peptides · doi:10.1016/j.peptides.2004.02.002 · Cited by 161

Proteins Binding to 5′ Untranslated Region Sites: a General Mechanism for Translational Regulation of mRNAs in Human and Yeast Cells

Stripecke, R., Oliveira, C. C., McCarthy, J. E. G., & Hentze, M. W. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.5898-5909.1994 · Cited by 153

Vertebrate mRNAs with a 5'-terminal pyrimidine tract are candidates for translational repression in quiescent cells: characterization of the translational cis-regulatory element.

Avni, D., Shama, S., Loreni, F., & Meyuhas, O. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.3822 · Cited by 149

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

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

Cap recap: The involvement of eIF-4F in regulating gene expression

Thach, R. E. (1992) · Cell · doi:10.1016/0092-8674(92)90461-k · Cited by 133

Translational regulation by mRNA/protein interactions in eukaryotic cells: Ferritin and beyond

Melefors, Ö., & Hentze, M. W. (1993) · BioEssays · doi:10.1002/bies.950150203 · Cited by 130

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

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

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

Iron-responsive element-binding protein. Phosphorylation by protein kinase C.

Eisenstein, R. S., Tuazon, P. T., Schalinske, K. L., Anderson, S. A., & Traugh, J. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74258-6 · Cited by 122

Inhibition of translation by RNA–small molecule interactions

Harvey, I., Garneau, P., & Pelletier, J. (2002) · RNA · doi:10.1017/s135583820202633x · Cited by 116

Coordmation of cellular iron metabolism by post-transcriptional gene regulation

Kühn, L. C., & Hentze, M. W. (1992) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(92)84064-t · Cited by 115

Determinants and regulation of cytoplasmic mRNA stability in eukaryotic cells

Hentze, M. W. (1991) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(91)90191-n · Cited by 115

Autoregulation of poly(A)-binding protein synthesisin vitro

Neto, O. P. D. M., Standart, N., & de, C. M. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.12.2198 · Cited by 111

Ferritin mRNA: interactions of iron regulatory element with translational regulator protein P-90 and the effect on base-paired flanking regions.

Harrell, C. M., McKenzie, A. R., Patiño, M. M., Walden, W. E., & Theil, E. C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4166 · Cited by 96

An iron-sulfur cluster plays a novel regulatory role in the iron-responsive element binding protein

Rouault, T. A., Haile, D. J., Downey, W. E., Philpott, C. C., Tang, C. K., Samaniego, F., Chin, J., Paul, I. A., Orloff, D. G., Harford, J. B., et al. (1992) · BioMetals · doi:10.1007/bf01061319 · Cited by 91

Iron regulatory factor expressed from recombinant baculovirus: conversion between the RNA-binding apoprotein and Fe-S cluster containing aconitase

Emery-Goodman, A., Hirling, H., Scarpellino, L., Henderson, B. R., & Kühn, L. C. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.6.1457 · Cited by 89

Heat shock protein 27 downregulates the transferrin receptor 1-mediated iron uptake

Chen, H., Zheng, C., Zhang, Y., Chang, Y., Qian, Z., & Shen, X. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.02.006 · Cited by 90

Identification of a C-terminal Poly(A)-binding Protein (PABP)-PABP Interaction Domain

Melo, E. O., Dhália, R., de, C. M., Standart, N., & Neto, O. P. D. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307624200 · Cited by 87

Iron feeding induces ferroportin 1 and hephaestin migration and interaction in rat duodenal epithelium

Yeh, K., YEH, M. K. Y., Mims, L., & Glass, J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90298.2008 · Cited by 85

Translational Repressor Activity Is Equivalent and Is Quantitatively Predicted by in Vitro RNA Binding for Two Iron-responsive Element-binding Proteins, IRP1 and IRP2

Kim, H., Klausner, R. D., & Rouault, T. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.4983 · Cited by 81

Targeting the eIF4A RNA helicase as an anti-neoplastic approach

Chu, J., & Pelletier, J. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.09.006 · Cited by 81

Global Analysis of Pub1p Targets Reveals a Coordinate Control of Gene Expression through Modulation of Binding and Stability

Duttagupta, R., Tian, B., Wilusz, C. J., Khounh, D. T., Soteropoulos, P., Ouyang, M., Dougherty, J. P., & Peltz, S. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5499-5513.2005 · Cited by 79

The iron-responsive element binding protein: a target for synaptic actions of nitric oxide.

Jaffrey, S. R., Cohen, N. A., Rouault, T. A., Klausner, R. D., & Snyder, S. H. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12994 · Cited by 78

Differential regulation of IRP1 and IRP2 by nitric oxide in rat hepatoma cells

Phillips, J., Kinikini, D., Yu, Y., Guo, B., & Leibold, E. E. (1996) · Blood · doi:10.1182/blood.v87.7.2983.bloodjournal8772983 · Cited by 72

Converse Modulation of IRP1 and IRP2 by Immunological Stimuli in Murine RAW 264.7 Macrophages

Bouton, C., Oliveira, L., & Drapier, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9403 · Cited by 71

Perturbation of Iron Metabolism by Cisplatin through Inhibition of Iron Regulatory Protein 2

Miyazawa, M., Bogdan, A. R., & Tsuji, Y. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.10.009 · Cited by 71

Expression of active iron regulatory factor from a full length human cDNA byin vitrotranscription/translation

Hirling, H., Emery-Goodman, A., Thompson, N. A., Neupert, B., Seiser, C., & Kühn, L. C. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.1.33 · Cited by 69

Gene Expression during Spermatogenesis

Eddy, E. M., Welch, J. E., & O’Brien, D. A. (1993) · Elsevier eBooks · doi:10.1016/b978-0-08-091764-1.50010-6 · Cited by 66

Hippuristanol - A potent steroid inhibitor of eukaryotic initiation factor 4A

Cencic, R., & Pelletier, J. (2016) · Translation · doi:10.1080/21690731.2015.1137381 · Cited by 63

Translational Regulation of Human Neuronal Nitric-oxide Synthase by an Alternatively Spliced 5′-Untranslated Region Leader Exon

Newton, D. C., Bevan, S. C., Choi, S., Robb, G. B., Millar, A. C., Wang, Y., & Marsden, P. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209988200 · Cited by 63

The iron regulatory region of ferritin mRNA is also a positive control element for iron-independent translation

Dix, D. J., Lin, P. C., Kimata, Y., & Theil, E. C. (1992) · Biochemistry · doi:10.1021/bi00125a024 · Cited by 63

Translation of a Testis-Specific Cu/Zn Superoxide Dismutase (SOD-1) mRNA Is Regulated by a 65-Kilodalton Protein Which Binds to Its 5′ Untranslated Region

Gu, W., & Hecht, N. B. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4535 · Cited by 59

Bacteriophage and spliceosomal proteins function as position-dependentcis/transrepressors of mRNA translationin vitro

Stripecke, R., & Hentze, M. W. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.21.5555 · Cited by 59

Ascorbic Acid Enhances Ferritin mRNA Translation by an IRP/Aconitase Switch

Tóth, I., & Bridges, K. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.33.19540 · Cited by 58

Cloning of a functional cDNA for the rabbit ferritin mRNA repressor protein. Demonstration of a tissue-specific pattern of expression.

Patiño, M. M., & Walden, W. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)37061-9 · Cited by 57

Ribosomal Pausing and Scanning Arrest as Mechanisms of Translational Regulation from Cap-Distal Iron-Responsive Elements

Paraskeva, E., Gray, N. K., Schläger, B., Wehr, K., & Hentze, M. W. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.807 · Cited by 56

Translational enhancement of H-ferritin mRNA by interleukin-1β acts through 5′ leader sequences distinct from the iron responsive element

Rogers, J. T., Andriotakis, J., Lacroix, L., Durmowicz, G. P., Kasschau, K., & Bridges, K. R. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.13.2678 · Cited by 55

A cluster of four genes selectively expressed in the male germ line of Drosophila melanogaster

Kuhn, R., Kühn, C., Börsch, D., Glätzer, K. H., Schäfer, U., & Schäfer, M. (1991) · Mechanisms of Development · doi:10.1016/0925-4773(91)90064-d · Cited by 54

Translational Regulation of mRNAs with Distinct IRE Sequences by Iron Regulatory Proteins 1 and 2

Menotti, E., Henderson, B. R., & Kühn, L. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1821 · Cited by 54

Prostate-specific transcription factor hPSE is translated only in normal prostate epithelial cells.

Nozawa, M., Yomogida, K., Kanno, N., Nonomura, N., Miki, T., Okuyama, Ä., Nishimune, Y., & Nozaki, M. (2000) · PubMed · Cited by 53

Modulation of Ferritin Η-Chain Expression in Friend Erythroleukemia Cells: Transcriptional and Translational Regulation by Hemin

Coccia, E. M., Profita, V., Fiorucci, G., Romeo, G., Affabris, E., Testa, U., Hentze, M. W., & Battistini, A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.7.3015-3022.1992 · Cited by 54

Translational Control of Poly(A)‐Binding Protein Expression

Bag, J., & Wu, J. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0143n.x · Cited by 51

High density lipoproteins stimulate the production and secretion of endothelin-1 from cultured bovine aortic endothelial cells.

Hu, R., Chuang, M.-Y., Prins, B. A., Kashyap, M. L., Frank, H. J. L., Pedram, A., & Levin, E. R. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117055 · Cited by 50

MicroReview Control of translation initiation in Saccharomyces cerevisiae

Yoon, H., & Donahue, T. F. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb00861.x · Cited by 50

Expression and Βiochemical Characterization of Iron Regulatory Proteins 1 and 2 in Saccharomyces cerevisiae

Phillips, J. D., Guo, B., Yu, Y., Brown, F. M., & Leibold, E. A. (1996) · Biochemistry · doi:10.1021/bi960653l · Cited by 45

Human ribosomal protein L7 inhibits cell-free translation in reticulocyte lysates and affects the expression of nuclear proteins upon stable transfection into Jurkat T-lymphoma cells

Neumann, F., Hemmerich, P. H., von Mikecz, A. H., Peter, H. H., & Krawinkel, U. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.2.195 · Cited by 49

Role of RNA secondary structure of the iron-responsive element in translational regulation of ferritin synthesis

Kikinis, Z., Eisenstein, R. S., Bettany, A. J. E., & Munro, H. N. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.20.4190 · Cited by 43

Post-transcriptional control via iron-responsive elements: the impact of aberrations in hereditary disease

Mikulits, W., Schranzhofer, M., Beug, H., & Müllner, E. W. (1999) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(99)00085-x · Cited by 40

A translational repression assay procedure (TRAP) for RNA–protein interactions in vivo

Paraskeva, E., Atzberger, A., & Hentze, M. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.951 · Cited by 39

Thyrotropin-releasing Hormone and Epidermal Growth Factor Regulate Iron-regulatory Protein Binding in Pituitary Cells via Protein Kinase C-dependent and -independent Signaling Pathways

Thomson, A. M., Rogers, J. T., & Leedman, P. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002354200 · Cited by 38

The molecular machinery of translational control in malaria parasites

Bennink, S., & Pradel, G. (2019) · Molecular Microbiology · doi:10.1111/mmi.14388 · Cited by 38

Translationaj repression by the human iron-regulatory factor (IRF) in Saccharomyces cerevisiae

Oliveira, C. C., Goossen, B., Zanchin, N. I. T., McCarthy, J. E. G., Hentze, M. W., & Stripecke, R. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.23.5316 · Cited by 38

1 Molecular regulation of iron proteins

Kühn, L. C. (1994) · Baillière s Clinical Haematology · doi:10.1016/s0950-3536(05)80123-4 · Cited by 37

RNA-binding properties of a translational activator, the adenovirus L4 100-kilodalton protein

Riley, D., & Flint, S. J. (1993) · Journal of Virology · doi:10.1128/jvi.67.6.3586-3595.1993 · Cited by 36

Effect of iron and retinoic acid on the control of transferrin receptor and ferritin in the human promonocytic cell line U937

Iturralde, M., Vass, J. K., Oria, R., & Brock, J. H. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(92)90043-b · Cited by 35

Multiple Sites of Control of Type-1 Corticotropin Releasing Hormone Receptor Levels in the Pituitary

Nikodémová, M., Rabadan‐Diehl, C., & Aguilera, G. (2002) · Archives of Physiology and Biochemistry · doi:10.1076/apab.110.1.123.901 · Cited by 32

Vertebrate mRNAs with a 5′-Terminal Pyrimidine Tract Are Candidates for Translational Repression in Quiescent Cells: Characterization of the Translational cis -Regulatory Element

Avni, D., Shama, S., Loreni, F., & Meyuhas, O. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.3822-3833.1994 · Cited by 31

Ferritin synthesis is controlled by iron-dependent translational derepression and by changes in synthesis/transport of nuclear ferritin RNAs.

Coulson, R., & Cleveland, D. W. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7613 · Cited by 30

Interleukin-6 regulates iron-related proteins through c-Jun N-terminal kinase activation in BV2 microglial cell lines

Zhou, S.-D., Du, X., Xie, J.-X., & Wang, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180464 · Cited by 31

Visualizing mRNA Localization and Local Protein Translation in Neurons

Dahm, R., Zeitelhofer, M., Götze, B., Kiebler, M. A., & Macchi, P. (2008) · Methods in cell biology · doi:10.1016/s0091-679x(08)85013-3 · Cited by 30

Eukaryotic Initiation Factor 4F: A Vulnerability of Tumor Cells

Lee, T., & Pelletier, J. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.150 · Cited by 27

Conservation in the Iron Responsive Element Family

Volz, K. W. (2021) · Genes · doi:10.3390/genes12091365 · Cited by 26

Post-transcriptional Regulation by 3′ UTRs Can Be Masked by Regulatory Elements in 5′ UTRs

Theil, K., Herzog, M., & Rajewsky, N. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.094 · Cited by 27

A GFP-based System to Uncouple mRNA Transport from Translation in a Single Living Neuron

Macchi, P., Hemraj, I., Goetze, B., Grunewald, B., Mallardo, M., & Kiebler, M. A. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-08-0505 · Cited by 26

Coupling the Iron-Responsive Element to GFP--An Inducible System to Study Translation in a Single Living Cell

Goetze, B., Grunewald, B., Kiebler, M. A., & Macchi, P. (2003) · Science s STKE · doi:10.1126/stke.2003.204.pl12 · Cited by 26

Cis-acting sequences in the 5'-untranslated region of the ribosomal protein A1 mRNA mediate its translational regulation during early embryogenesis of Drosophila.

Patel, R. C., & Jacobs‐Lorena, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48409-8 · Cited by 26

Adenosine‐rich elements present in the 5′‐untranslated region of PABP mRNA can selectively reduce the abundance and translation of CAT mRNAs in vivo

Melo, E. O., Neto, O. P. D. M., & de, C. M. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00620-3 · Cited by 25

Chronic regulation of the renal Na + /H + exchanger NHE3 by dopamine: translational and posttranslational mechanisms

Hu, M. C., Sole, F. D., Zhang, J., McLeroy, P., & Moe, O. W. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00630.2012 · Cited by 25

Ferritin mRNAs in Schistosoma Mansoni do not have Iron‐Responsive Elements for Post‐Transcriptional Regulation

Schüßler, P., Pötters, E., Winnen, R., Michel, A., Bottke, W., & Kunz, W. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0064t.x · Cited by 24

Construction of regulatable picornavirus IRESes as a test of current models of the mechanism of internal translation initiation

Pöyry, T. A. A., Hentze, M. W., & Jackson, R. J. (2001) · RNA · doi:10.1017/s1355838201001911 · Cited by 24

Heterogeneity in the 5′ untranslated region of mouse cytochrome cTmRNAs leads to altered translational status of the mRNAs

Yiu, G. K., Gu, W., & Hecht, N. B. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4599 · Cited by 24

Regulation of ferritin H-chain expression in differentiating Friend leukemia cells

Coccia, E. M., Stellacci, E., Orsatti, R., Testa, U., & Battistini, A. (1995) · Blood · doi:10.1182/blood.v86.4.1570.bloodjournal8641570 · Cited by 23

Optimization of Biotinylated RNA or DNA Pull-Down Assays for Detection of Binding Proteins: Examples of IRP1, IRP2, HuR, AUF1, and Nrf2

Tsuji, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043604 · Cited by 24

Proximity between the cap and 5′ ε stem–loop structure is critical for the suppression of pgRNA translation by the hepatitis B viral polymerase

Ryu, D.-K., Ahn, B.-Y., & Ryu, W. (2010) · Virology · doi:10.1016/j.virol.2010.07.005 · Cited by 22

Identification and mapping of the promoter for the gene encoding the ferritin heavy-chain homologue of the yellow fever mosquito Aedes aegypti

Pham, D. Q. ‐., Shaffer, J. J., Chavez, C. A., & Douglass, P. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00167-4 · Cited by 21

Synthetic RNA-based post-transcriptional expression control methods and genetic circuits

Pardi, M. L., Wu, J., Kawasaki, S., & Saito, H. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114196 · Cited by 20

Forced engagement of a RNA/protein complex by a chemical inducer of dimerization to modulate gene expression

Harvey, I., Garneau, P., & Pelletier, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042693399 · Cited by 20

A novel method to identify nucleic acid binding sites in protiens by scanning mutagenesis: application to iron regulatory protein

Neupert, B., Menotti, E., & Kühn, L. C. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.14.2579 · Cited by 20

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

12 Translational Control of FerritinPreprint

Rouault, T. A., Klausner, R. D., & Harford, J. B. (1996) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969458.30.335 · Cited by 25

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

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

The iron regulatory region of ferritin mRNA is also a positive control element for iron-independent translation

Dix, D. J., Lin, P. C., Kimata, Y., & Theil, E. C. (1992) · Biochemistry · doi:10.1021/bi00125a024 · Cited by 63