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

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

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

Mechanism and regulation of eukaryotic protein synthesis

Merrick, W. C. (1992) · Microbiological Reviews · doi:10.1128/mr.56.2.291-315.1992 · Cited by 650

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 Mechanism by which Cycloheximide and Related Glutarimide Antibiotics Inhibit Peptide Synthesis on Reticulocyte Ribosomes

Obrig, T. G., Culp, W. J., McKeehan, W. L., & Hardesty, B. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62546-3 · Cited by 513

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

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

Iron regulates ferritin mRNA translation through a segment of its 5′-untranslated region.

Aziz, N., & Munro, H. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8478 · Cited by 368

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

Oligopyrimidine tract at the 5' end of mammalian ribosomal protein mRNAs is required for their translational control.

Levy, S., Avni, D., Hariharan, N., Perry, R. P., & Meyuhas, O. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3319 · Cited by 344

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

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

Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA.

Scherly, D., Boelens, W. C., VENROOIJ, W. J. V., Dathan, N. A., Hamm, J., & Mattaj, I. W. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08601.x · Cited by 309

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

Cap-Binding Proteins of Eukaryotic Messenger RNA: Functions in Initiation and Control of Translation

Sonenberg, N. (1988) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60614-5 · Cited by 259

Translation of 15‐lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region.

Ostareck‐Lederer, A., Ostareck, D. H., Standart, N., & Thiele, B. J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06402.x · Cited by 257

Cap recognition and the entry of mRNA into the protein synthesis initiation cycle

Rhoads, R. E. (1988) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(88)90028-x · Cited by 256

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

Initiation of encephalomyocarditis virus RNA translation: the authentic initiation site is not selected by a scanning mechanism.

Kaminski, A., Howell, M. T., & Jackson, R. J. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07588.x · Cited by 203

Migration of 40 S ribosomal subunits on messenger RNA in the presence of edeine.

Kozak, M., & Shatkin, A. J. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)46969-x · Cited by 202

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

Identification of an RNA binding site for human thymidylate synthase.

Chu, E., Voeller, D. M., Koeller, D. M., Drake, J. C., Takimoto, C. H. M., Maley, G. F., Maley, F., & Allegra, C. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.2.517 · Cited by 178

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

Role of ATP in binding and migration of 40S ribosomal subunits

Kozak, M. (1980) · Cell · doi:10.1016/0092-8674(80)90356-6 · Cited by 153

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

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

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

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

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

Effects of long 5' leader sequences on initiation by eukaryotic ribosomes in vitro.

Kozak, M. (1991) · PubMed · Cited by 127

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 protein synthesis by mRNA structure

Gray, N. K., & Hentze, M. W. (1994) · Molecular Biology Reports · doi:10.1007/bf00986961 · Cited by 114

Translational repression in eukaryotes: partial purification and characterization of a repressor of ferritin mRNA translation.

Walden, W. E., Daniels-McQueen, S., Brown, P. H., Gaffield, L., Russell, D. A., Bielser, D., Bailey, L. C., & Thach, R. E. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.24.9503 · Cited by 108

Probing the function of the eucaryotic 5′ cap structure by using a monoclonal antibody directed against cap-binding proteins

Sonenberg, N., Guertin, D., Cleveland, D., & Trachsel, H. (1981) · Cell · doi:10.1016/0092-8674(81)90398-6 · Cited by 103

Internal initiation of translation of picornavirus RNAs

Jackson, R. J., Hunt, S. L., Gibbs, C. L., & Kaminski, A. (1994) · Molecular Biology Reports · doi:10.1007/bf00986957 · Cited by 98

Analysis of 40 S and 80 S complexes with mRNA as measured by sucrose density gradients and primer extension inhibition.

Anthony, D. D., & Merrick, W. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45981-9 · Cited by 98

Ribosomal protein L32 of Saccharomyces cerevisiae regulates both splicing and translation of its own transcript.

Dabeva, M. D., & Warner, J. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36568-8 · Cited by 92

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

A competitive inhibitor of the GTP reaction in protein synthesis

Hershey, J. W. B., & Monro, R. E. (1966) · Journal of Molecular Biology · doi:10.1016/s0022-2836(66)80077-3 · Cited by 87

Sequences mediating the translation of mouse S16 ribosomal protein mRNA during myoblast differentiation and in vitro and possible control points for the in vitro translation.Preprint

Hammond, M. L., Merrick, W. C., & Bowman, L. (1991) · Genes & Development · doi:10.1101/gad.5.9.1723 · Cited by 62

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

Picornavirus RNA translation continues to surprise

Sonenberg, N. (1991) · Trends in Genetics · doi:10.1016/0168-9525(91)90440-2 · Cited by 49

Nitric oxide and the post-transcriptional control of cellular iron traffic

Pantopoulos, K., WEISS, G., & Hentze, M. W. (1994) · Trends in Cell Biology · doi:10.1016/0962-8924(94)90179-1 · Cited by 46

Gene regulation: translational initiation by internal ribosome binding

Oh, S.-K., & Sarnow, P. (1993) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(93)90037-p · Cited by 42

Gene regulation in Drosophila spermatogenesis: Analysis of protein binding at the translational control element TCE

Kempe, E., Muhs, B., & Schäfer, M. (1993) · Developmental Genetics · doi:10.1002/dvg.1020140606 · Cited by 37

Characteristics of the interaction of the ferritin repressor protein with the iron-responsive element

Swenson, G. R., Patiño, M. M., Beck, M. M., Gaffield, L., & Walden, W. E. (1991) · BioMetals · doi:10.1007/bf01135557 · Cited by 25

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

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

Functional 5′ UTR mRNA structures in eukaryotic translation regulation and how to find them

Leppek, K., Das, R., & Barna, M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.103 · Cited by 949

Initiation of Protein Synthesis in Eukaryotic Cells

Pain, V. M. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00747.x · Cited by 718

Mechanisms for Induction and Rerepression of Ferritin Synthesis

Mascotti, D. P., Goessling, L. S., Rup, D., & Thach, R. E. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5993-1_8

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

The Mechanism of Translational Repression by Iron Regulatory Protein

Gray, N. K. (1994) · Enlighten: Theses (The University of Glasgow) · Cited by 2

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

The IRE (iron regulatory element) family: structures which regulate mRNA translation or stability.

Theil, E. C. (1993) · PubMed · Cited by 57