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Showing 1–7 of 7 results
Advanced filters: Author: Robert Buschauer Clear advanced filters

  • Identification of SDD1 mRNA from Saccharomyces cerevisiae as an endogenous RQC substrate allows analysis of the mechanism underlying translational stalling and Hel2-dependent polyubiquitination of collided ribosomes to provide insight into ribosome dissociation.

    • Yoshitaka Matsuo
    • Petr Tesina
    • Toshifumi Inada
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 323-332

  • The structure of the assembly-competent 5S RNP was elucidated by cryo-EM. These findings provide molecular insight into how this module incorporates into the nascent pre-60S ribosome and how it can affect the MDM2–p53 pathway in human cells.

    • Nestor Miguel Castillo Duque de Estrada
    • Matthias Thoms
    • Ed Hurt
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1119-1131

  • Tigecycline is widely used to treat complex bacterial infections. Here, authors present cryo-EM structures of tigecycline-bound eukaryotic ribosomes, revealing how it also targets the human mitoribosome with distinct binding properties.

    • Xiang Li
    • Mengjiao Wang
    • Jingdong Cheng
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-12

  • Structural and biochemical analysis reveal that tetracenomycin X acts as an inhibitor of protein synthesis by binding within the exit tunnel in a large ribosomal unit to prevent the prolongation of the nascent polypeptide chain.

    • Ilya A. Osterman
    • Maximiliane Wieland
    • Petr V. Sergiev
    Research
    Nature Chemical Biology
    Volume: 16, P: 1071-1077

  • Otu2-driven deubiquitylation of ribosomal protein eS7 impacts translational efficiency. Here, the authors provide the molecular basis for recognition of monoubiquitinated eS7 on 40S and give mechanistic insights into Otu2’s role in translation reset.

    • Ken Ikeuchi
    • Nives Ivic
    • Roland Beckmann
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-15

  • The cryo-EM structure of the Saccharomyces cerevisiae 80S ribosome–Xrn1 nuclease complex reveals how the conserved core of Xrn1 allows binding at the mRNA exit channel of the ribosome, ensuring efficient degradation of mRNA after the final round of translation.

    • Petr Tesina
    • Elisabeth Heckel
    • Roland Beckmann
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 275-280