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Showing 1–9 of 9 results
Advanced filters: Author: Jens Lykke-Andersen Clear advanced filters

  • Jens Lykke-Andersen, Frank Baas, Joseph Gleeson and colleagues report that mutations in the 3′ exonuclease TOE1 cause pontocerebellar hypoplasia type 7. They further show that these mutations result in the accumulation of incompletely processed small nuclear RNAs, leading to severe, early-onset neurodegeneration.

    • Rea M Lardelli
    • Ashleigh E Schaffer
    • Joseph G Gleeson
    Research
    Nature Genetics
    Volume: 49, P: 457-464

  • In this Review, Dowdle and Lykke-Andersen discuss advances in our understanding of the machinery and mechanisms involved in the control of cytoplasmic mRNA decay and comment on implications for the design of therapeutic mRNAs.

    • Megan E. Dowdle
    • Jens Lykke-Andersen
    Reviews
    Nature Reviews Genetics
    Volume: 26, P: 463-478

  • A new study reports the hUpf2-hUpf3b interaction domain structure and provides the first structural insight into the core of the nonsense-mediated decay pathway. Surprisingly, the RNA-recognition motif of hUpf3b, a domain typically involved in RNA binding, constitutes instead an interaction surface for hUpf2.

    • Jens Lykke-Andersen
    News & Views
    Nature Structural & Molecular Biology
    Volume: 11, P: 305-306

  • A recent study describes a novel mRNA-surveillance pathway called 'no-go decay' that triggers the endonucleolytic cleavage of yeast mRNAs with translation-elongation stalls. This adds to the repertoire of mRNA-decay processes in which abnormal translation may activate mRNA degradation through proteins recruited to the ribosomal A site.

    • Sandra L Clement
    • Jens Lykke-Andersen
    News & Views
    Nature Structural & Molecular Biology
    Volume: 13, P: 299-301

  • Determining which covalent binding events impact protein function is challenging. Now, a strategy has been reported that integrates base editing and chemical proteomics to infer the functionality of ligandable cysteines in cancer dependency proteins by quantifying the impact of their missense mutation on cancer cell proliferation.

    • Haoxin Li
    • Tiantai Ma
    • Benjamin F. Cravatt
    Research
    Nature Chemical Biology
    Volume: 19, P: 1320-1330

  • Gene expression is regulated by a range of mechanisms, including post-translational modifications such as phosphorylation. Here the authors present evidence for a feedback mechanism whereby hyperphosphorylation of UPF1 in response to delays in nonsense-mediated decay enhances recruitment of mRNA decay machinery.

    • Sébastien Durand
    • Tobias M. Franks
    • Jens Lykke-Andersen
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-12

  • It has been suggested that nonsense-mediated mRNA decay (NMD) is restricted to a pioneer round of translation initiated on mRNAs associated with the cap-binding complex (CBC), whereas the exchange of the CBC for the eIF4F translation initiation complex renders mRNAs immune to NMD. However, multiple lines of evidence now suggest that eIF4F-associated mRNAs are not immune to NMD.

    • Sébastien Durand
    • Jens Lykke-Andersen
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 702-709

  • Mass-spectrometry-based proteomics led to the identification of NoBody, a microprotein translated from LINC01420 RNA, which interacts with enhancer of decapping 4 (EDC4) and negatively regulates 5′-to-3′ mRNA decay.

    • Nadia G D'Lima
    • Jiao Ma
    • Sarah A Slavoff
    Research
    Nature Chemical Biology
    Volume: 13, P: 174-180

  • How the nuclear exosome is targeted to nuclear RNA substrates is poorly understood. An affinity-capture MS approach and functional analyses now demonstrate a physical and functional connection between the human exosome and the cap-binding complex (CBC). A CBC-containing complex was found to promote transcription termination of several RNA types, thus suggesting a direct link to exosomal RNA degradation.

    • Peter Refsing Andersen
    • Michal Domanski
    • Torben Heick Jensen
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1367-1376