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Showing 1–8 of 8 results
Advanced filters: Author: Jonas Barandun Clear advanced filters

  • A proteomics approach using MS2 as an RNA tag is used to provide snapshots of nascent preribosomal particles from budding yeast, thus allowing the determination of the stage-specific order in which 70 ribosome-assembly factors associate with pre-rRNA domains.

    • Malik Chaker-Margot
    • Mirjam Hunziker
    • Sebastian Klinge
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 920-923

  • Pupylation is a bacterial posttranslational modification pathway with functional analogies to ubiquitination. Here, Özceliket al.report the structures of the Pup Ligase, PafA and the Depupylase, Dop. Mutational analysis revealed residues required for catalysis and for the interaction with Pup.

    • Dennis Özcelik
    • Jonas Barandun
    • Eilika Weber-Ban
    Research
    Nature Communications
    Volume: 3, P: 1-10

  • Eukaryotic ribosome biogenesis involves a large number of maturations factors which are responsible for the stepwise assembly of the ribosomal subunits. Here the authors use an array of biochemical and structural biology methods to investigate the function of the UtpA and UtpB complexes as part of the small subunit processome.

    • Mirjam Hunziker
    • Jonas Barandun
    • Sebastian Klinge
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-10

  • The cryo-electron microscopy structure of the ribosome from the microsporidium Vairimorpha necatrix reveals that, despite extreme genome compaction reducing the ribosomal RNA to a functionally conserved core, most ribosomal proteins are retained and adapt to form the minimized protein synthesis machinery in these eukaryotic parasites.

    • Jonas Barandun
    • Mirjam Hunziker
    • Sebastian Klinge
    Research
    Nature Microbiology
    Volume: 4, P: 1798-1804

  • Deep mutational scanning revealed the drug efflux activity profile of more than 1,430 single variants, enabling the identification of critical residues that regulate the activity of the bacterial drug efflux pump EfrCD in response to different drugs.

    • Gianmarco Meier
    • Sujani Thavarasah
    • Markus A. Seeger
    Research
    Nature Chemical Biology
    Volume: 19, P: 440-450

  • The 3.8-Å cryo-EM structure of the Saccharomyces cerevisiae small-subunit processome in a state that precedes pre-rRNA cleavage at site A1 provides an essentially complete near-atomic model of this assembly.

    • Jonas Barandun
    • Malik Chaker-Margot
    • Sebastian Klinge
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 944-953

  • Cryo-electron microscopy structures of multiple states along the assembly pathway of the nucleolar pre-60S ribosomal subunit suggest that folding of the pre-ribosomal RNA and sequential binding of transient assembly factors are regulated by steric hindrance among these factors.

    • Zahra Assur Sanghai
    • Linamarie Miller
    • Sebastian Klinge
    Research
    Nature
    Volume: 556, P: 126-129