The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Translational repression by a complex between the iron‐responsive element of ferritin mRNA and its specific cytoplasmic binding protein is position‐dependent in vivo.
Open accessAbstract
The interaction of ferritin mRNA is regulated by iron via the interaction of a cytoplasmic binding protein (IRE-BP) with a specific stem-loop structure in the 5' untranslated region (UTR), referred to as the iron-responsive element (IRE). A high affinity RNA-protein complex between the IRE and the IRE-BP functions as a repressor of translation in vivo. Translational repression appears to depend upon the position of the IRE in the 5' UTR of the mRNA. IREs located in the 5' untranslated region 67 nucleotides or more downstream of the 5' terminus of the mRNA fail to mediate iron-dependent translational regulation and give rise to constitutively derepressed transcripts. A model is proposed in which translational regulation of protein biosynthesis involves a position-dependent interference of the IRE/IRE-BP complex with one of the initial steps in translation initiation.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The text we found for this paper looks like another document, so the self-check wasn’t run.
Citations
Cites
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
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
Self-citationInfluences 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
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
Pelletier, J., & Sonenberg, N. (1985) · Cell · doi:10.1016/0092-8674(85)90200-4 · Cited by 610
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
Self-citation
Cited by
Sorted by citations
Items 101–144 of 144
mRNA translation is not a prerequisite for small interfering RNA-mediated mRNA cleavage
Sen, G. L., Wehrman, T. S., & Blau, H. M. (2005) · Differentiation · doi:10.1111/j.1432-0436.2005.00029.x · Cited by 18
Shemesh, J., & Ehrlich, R. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82313-4 · Cited by 18
Molecular Cloning and Expression of Ferritin mRNA in Heavy Metal-Poisoned Xenopus laevis Cells
Muller, J. P., Vedel, M., Monnot, M. J., TOUZET, N., & Wegnez, M. R. (1991) · DNA and Cell Biology · doi:10.1089/dna.1991.10.571 · Cited by 17
Chin, D. J. (1992) · Journal of Virology · doi:10.1128/jvi.66.1.600-607.1992 · Cited by 17
Pantopoulos, K., Johansson, H. E., & Hentze, M. W. (1994) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60856-9 · Cited by 17
Self-citationExpert, D., Sauvage, C., & Neilands, J. B. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb01373.x · Cited by 17
Muckenthaler, M. U., & Hentze, M. W. (1997) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-60471-3_5 · Cited by 16
Self-citationEclectic mechanisms of heme regulation of hematopoiesis
Abraham, N. G., Levere, R. D., & Lutton, J. D. (1991) · The International Journal Of Cell Cloning · doi:10.1002/stem.5530090304 · Cited by 16
Henderson, B. R., & Kühn, L. C. (1997) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-60471-3_6 · Cited by 15
Wang, Y.-H., Lin, P. C., Sczekan, S. R., McKenzie, R. A., & Theil, E. C. (1991) · BioMetals · doi:10.1007/bf01135558 · Cited by 13
Posch, M., Sutterlüty, H., Skern, T., & Seiser, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16611 · Cited by 13
Nichol, H., & Winzerling, J. J. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00110-8 · Cited by 12
Modulation of iron metabolism by new chemicals interacting with the iron regulatory system
Tsuji, Y., Ninomiya‐Tsuji, J., Shen, M. Y. F., & DiFrancesco, B. R. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103444 · Cited by 11
Developing anti-neoplastic biotherapeutics against eIF4F
Steinberger, J., Chu, J., Maïga, R. I., Sleiman, K., & Pelletier, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2430-8 · Cited by 11
RNA-binding protein-mediated translational repression of transgene expression in plants
Cerny, R. E., Qi, Y., Aydt, C. M., Huang, S., Listello, J. J., Fabbri, B. J., Conner, T. W., Crossland, L., & Huang, J. (2003) · Plant Molecular Biology · doi:10.1023/a:1023953130574 · Cited by 11
Effects of the Ferritin Open Reading Frame on Translational Induction by iron
Mascotti, D. P., Goessling, L. S., Rup, D., & Thach, R. E. (1996) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60191-9 · Cited by 11
Translational Control by Iron-Responsive Elements
Hentze, M. W. (1994) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-2554-7_13 · Cited by 10
Self-citationWang, W., Song, N., Zhang, H., Xie, J., & Wang, J. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.07.018 · Cited by 9
The cap-proximal RNA secondary structure inhibits preinitiation complex formation on HAC1 mRNA
Uppala, J. K., Sathe, L., Chakraborty, A., Bhattacharjee, S., Pulvino, A., & Dey, M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101648 · Cited by 7
Transcriptional modulation of foreign gene expression in engineered somatic tissues
Bohl, D., & Heard, J. (1998) · Cell Biology and Toxicology · doi:10.1023/a:1007480419685 · Cited by 6
Waithaka, A., Maiakovska, O., Grimm, D., do Nascimento, L. M., & CLAYTON, C. E. (2022) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0010876 · Cited by 6
Testa, U. (2001) · CRC Press eBooks · doi:10.1201/b14262-9 · Cited by 4
[24] Frameshifting assay to characterize RNA-protein Interactions in eukaryotic cells
Kollmus, H., & Häuser, H. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)18063-2 · Cited by 5
The Iron Responsive Element (IRE), the Iron Regulatory Protein (IRP), and Cytosolic Aconitase
Eisenstein, R. S., Kennedy, M. C., & Beinert, H. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5993-1_7 · Cited by 5
Exploring the dynamics of messenger ribonucleoprotein-mediated translation repression
Meyer, J., Payr, M., Duss, O., & Hennig, J. (2024) · Biochemical Society Transactions · doi:10.1042/bst20231240 · Cited by 4
Goetze, B., Grunewald, B., Kiebler, M. A., & Macchi, P. (2003) · Science Signaling · doi:10.1126/scisignal.2042003pl12 · Cited by 4
Translation and Posttranslational Processing of Gastrointestinal Peptides
Gariepy, C. E., & Dickinson, C. J. (2006) · Elsevier eBooks · doi:10.1016/b978-012088394-3/50005-2 · Cited by 2
The Structure and Function of Iron Regulatory Factor
Kühn, L. C., Hirling, H., Henderson, B. R., Emery-Goodman, A., Neupert, B., & Kaldy, P. (1994) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-2554-7_11 · Cited by 3
Repressor-Mediated Translational Control
Walden, W. E. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2894-4_15 · Cited by 3
Engineering and standardization of posttranscriptional biocircuitry inSaccharomyces cerevisiae
McCarthy, J. E. G. (2021) · Integrative Biology · doi:10.1093/intbio/zyab013 · Cited by 1
Regulation of iron metabolism in higher eukaryotes: iron–sulfur centers as genetic switches
Pantopoulos, K., & Hentze, M. W. (1999) · Wiley eBooks · doi:10.1002/9783527613700.ch08 · Cited by 1
Self-citationIron and Heme Transport and Trafficking
Yien, Y. Y., & Paw, B. H. (2004) · Wiley eBooks · doi:10.1002/9781119951438.eibc2117 · Cited by 1
Current and Emerging Therapies Targeting Translation
Galicia-Vázquez, G., & Pelletier, J. (2014) · Springer eBooks · doi:10.1007/978-94-017-9078-9_14
[13] Translational control of gene expression using retroviral vectors with iron response elements
Davis, J. L., Gross, P. R., & Danos, O. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)06015-2
Iron metabolism in cultured cytotrophoblasts : a model of the maternal-fetal interphase
Starreveld, J. S. (1994) · RePub (Erasmus University Rotterdam)
Application of Tetracycline Regulatable Systems for Gene Therapy
Bohl, D., & Heard, J. (1998) · Springer eBooks · doi:10.1007/978-3-642-72160-1_5
Natalin, P. (2009) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00008939
Post-Transcriptional Regulation of Gene Expression by Iron
Hentze, M. W. (1995) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4684-6840-3_8
Self-citationYeh, K., YEH, M. K. Y., Mims, L., & Glass, J. (2016)
Translational Regulation in the Early Drosophila Embryo
Nelson, M. R. (2008) · TSpace (University of Toronto)
Genomweite Annotation von Translationsinitiationsstellen in der humanen Monozyten-Zelllinie THP-1
Fritsch, C. (2013) · Multimedialen Archiv und Publikationsserver der Christian-Albrechts-Universität zu Kiel (Christian-Albrechts-Universität zu Kiel)
Modulation of Iron Metabolism by New Chemicals Interacting with the Iron Regulatory SystemPreprint
Tsuji, Y., Ninomiya‐Tsuji, J., Shen, M. Y. F., & DiFrancesco, B. R. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4960121
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 Control in Eukaryotic Cells: Principles Learned from the IRE/IRF System
Hentze, M. W. (1996) · Springer eBooks · doi:10.1007/978-3-642-60929-9_11
Self-citation
Metadata
- Authors
- Goossen, B., Caughman, S. W., Harford, J. B., Klausner, R. D., & Hentze, M. W.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Venue
- The EMBO Journal
- Published
- 1990-12-01
- Volume
- 9
- Issue
- 12
- Pages
- 4127-4133
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC552186
- OpenAlex
- W979668760
- Cited by
- 144
- References
- 49
- Citations by year
- 2024: 3 · 2023: 1 · 2022: 3 · 2021: 2 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 3 · 2015: 1 · 2014: 2 · 2013: 2 · 2012: 1
- FWCI
- 8.98
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- protein synthesis inhibition, iron-responsive element, ferritin mRNA, iron-responsive element-binding protein, 5' untranslated region, protein-RNA complex, translation initiation, stem-loop structure
- MeSH terms
- Animals, Base Sequence, Binding Sites, Carrier Proteins, Cell Line, Cytoplasm, Ferritins, Gene Expression Regulation, Molecular Sequence Data, Nucleic Acid Conformation, Plasmids, RNA, RNA, Messenger, Transcription, Genetic, Transfection, Protein Biosynthesis, Blotting, Northern, Restriction Mapping, Oligonucleotide Probes, Mutagenesis, Insertional, Iron-Regulatory Proteins, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review