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  • 1
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    Protein synthesis. Believe it or not-translation in the nucleus (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1058-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany. hentze@embl-heidelberg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11498567" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Fractionation ; Cell Nucleus/*genetics/metabolism ; Cytoplasm/metabolism ; Fluorescence ; HeLa Cells ; Humans ; Lysine/metabolism ; *Protein Biosynthesis ; Protein Transport ; Proteins/metabolism ; RNA, Messenger/*genetics/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: The human ferritin H chain messenger RNA contains a specific iron-responsive element (IRE) in its 5' untranslated region, which mediates regulation by iron of ferritin translation. An RNA gel retardation assay was used to demonstrate the affinity of a specific cytosolic binding protein for the IRE. A single-base deletion in the IRE eliminated both the interaction of the cytoplasmic protein with the IRE and translational regulation. Thus, the regulatory potential of the IRE correlates with its capacity to specifically interact with proteins. Titration curves of binding activity after treatment of cells with an iron chelator suggest that the factor acts as a repressor of ferritin translation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rouault, T A -- Hentze, M W -- Caughman, S W -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1207-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413484" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Binding, Competitive ; Carrier Proteins/*metabolism ; Cytosol/analysis ; Deferoxamine/pharmacology ; Ferritins/*genetics ; Globins/genetics ; Humans ; Iron/*pharmacology ; Liver/analysis ; *Nucleocytoplasmic Transport Proteins ; Protein Biosynthesis/drug effects ; RNA, Messenger/*metabolism ; *RNA-Binding Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-21
    Description: Iron-responsive elements (IREs) are RNA motifs that have been identified within the 5' untranslated region of ferritin messenger RNA and the 3' untranslated region of transferrin receptor mRNA. A single IRE mediates iron-dependent control of ferritin translation, whereas multiple IREs are found in the region of the transferrin receptor mRNA responsible for iron-dependent control of mRNA stability. A cytosolic protein binds in vitro to the IREs of both mRNAs. The IRE-binding protein (IRE-BP) is shown to require free sulfhydryl groups for its specific interaction with the IRE. Treatment of lysates with reducing agents increases the binding activity, whereas agents that block sulfhydryls inhibit binding. Iron starvation, leading to decreased ferritin translation, results in increased binding activity, which is explained by an increase in the fraction of the IRE-BP that is in a fully reduced state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- Rouault, T A -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1989 Apr 21;244(4902):357-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2711187" target="_blank"〉PubMed〈/a〉
    Keywords: Cytosol/metabolism ; DNA-Binding Proteins/*metabolism ; Disulfides/metabolism ; Dithiothreitol/pharmacology ; Ethylmaleimide/pharmacology ; Ferritins/*genetics ; Humans ; Iron/*pharmacology ; Leukemia, Erythroblastic, Acute ; Mercaptoethanol/pharmacology ; Oxidation-Reduction ; Protein Biosynthesis/drug effects ; RNA, Messenger/genetics/*metabolism ; Receptors, Transferrin/*genetics ; Regulatory Sequences, Nucleic Acid ; Sulfhydryl Compounds/metabolism ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    eIF4G: a multipurpose ribosome adapter? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- New York, N.Y. -- Science. 1997 Jan 24;275(5299):500-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Programme, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany. matthias.hentze@EMBL-Heidelberg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9019810" target="_blank"〉PubMed〈/a〉
    Keywords: Eukaryotic Initiation Factor-3 ; Eukaryotic Initiation Factor-4E ; Eukaryotic Initiation Factor-4G ; *Peptide Chain Initiation, Translational ; Peptide Initiation Factors/*metabolism ; Picornaviridae/genetics/metabolism ; Poly(A)-Binding Proteins ; RNA Caps/metabolism ; RNA, Messenger/*metabolism ; RNA, Viral/metabolism ; RNA-Binding Proteins/metabolism ; Ribosomes/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Genetics. IRES unplugged (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-01-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gebauer, Fatima -- Hentze, Matthias W -- New York, N.Y. -- Science. 2016 Jan 15;351(6270):228. doi: 10.1126/science.aad8540.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Regulation, Stem Cells and Cancer Programme, Centre for Genomic Regulation, Barcelona Institute of Science and Technology, 08003 Barcelona, Spain. Universitat Pompeu Fabra, 08003 Barcelona, Spain. ; European Molecular Biology Laboratory, 69117 Heidelberg, Germany. hentze@embl.de.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26816364" target="_blank"〉PubMed〈/a〉
    Keywords: Genome, Human/*genetics ; Genome, Viral/*genetics ; Humans ; Protein Biosynthesis/*genetics ; RNA Caps/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Identification of the iron-responsive element for the translational regulation of human ferritin mRNA (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-12-11
    Description: Regulated translation of messenger RNA offers an important mechanism for the control of gene expression. The biosynthesis of the intracellular iron storage protein ferritin is translationally regulated by iron. A cis-acting element that is both necessary and sufficient for this translational regulation is present within the 5' nontranslated leader region of the human ferritin H-chain messenger RNA. In this report the iron-responsive element (IRE) was identified by deletional analysis. Moreover, a synthetic oligodeoxynucleotide was shown to be able to transfer iron regulation to a construct that would otherwise not be able to respond to iron. The IRE has been highly conserved and predates the evolutionary segregation between amphibians, birds, and man. The IRE may prove to be useful for the design of translationally regulated expression systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hentze, M W -- Caughman, S W -- Rouault, T A -- Barriocanal, J G -- Dancis, A -- Harford, J B -- Klausner, R D -- New York, N.Y. -- Science. 1987 Dec 11;238(4833):1570-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685996" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromosome Deletion ; Ferritins/*genetics ; *Gene Expression Regulation ; Genes ; Humans ; Iron/*pharmacology ; Molecular Sequence Data ; Plasmids ; Promoter Regions, Genetic/*drug effects ; *Protein Biosynthesis ; RNA, Messenger/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-05-13
    Description: The biosynthetic rates for both the transferrin receptor (TfR) and ferritin are regulated by iron. An iron-responsive element (IRE) in the 5' untranslated portion of the ferritin messenger RNA (mRNA) mediates iron-dependent control of its translation. In this report the 3' untranslated region of the mRNA for the human TfR was shown to be necessary and sufficient for iron-dependent control of mRNA levels. Deletion studies identified a 678-nucleotide fragment of the TfR complementary DNA that is critical for this iron regulation. Five potential stem-loops that resemble the ferritin IRE are contained within the region critical for TfR regulation. Each of two of the five TfR elements was independently inserted into the 5' untranslated region of an indicator gene transcript. In this location they conferred iron regulation of translation. Thus, an mRNA element has been implicated in the mediation of distinct regulatory phenomena dependent on the context of the element within the transcript.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Casey, J L -- Hentze, M W -- Koeller, D M -- Caughman, S W -- Rouault, T A -- Klausner, R D -- Harford, J B -- New York, N.Y. -- Science. 1988 May 13;240(4854):924-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2452485" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; DNA/genetics ; DNA, Recombinant ; Ferritins/biosynthesis/*genetics ; Growth Hormone/genetics ; Humans ; Iron/*pharmacology ; Mice ; Plasmids ; Protein Biosynthesis/*drug effects ; RNA/*genetics ; RNA, Messenger/*genetics ; Receptors, Transferrin/biosynthesis/*genetics ; *Regulatory Sequences, Nucleic Acid ; Transcription, Genetic ; Transfection ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Nitric oxide signaling to iron-regulatory protein: direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. (1995)
    National Academy of Sciences
    Details
    Publication Date: 1995-02-28
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: switching between enzymatic and genetic function? (1992)
    National Academy of Sciences
    Details
    Publication Date: 1992-05-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    A translational repression assay procedure (TRAP) for RNA-protein interactions in vivo (1998)
    National Academy of Sciences
    Details
    Publication Date: 1998-02-03
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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