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Showing 1–9 of 9 results
Advanced filters: Author: Florian Wilfling Clear advanced filters

  • The large and small subunits of the ribosome are synthesized independently within the nucleolus — a membrane-less compartment within the nucleus — before being exported into the cytoplasm. Here, the authors use in situ cryo-ET to observe ribosome maturation and reveal the native organization of the nucleolus.

    • Philipp S. Erdmann
    • Zhen Hou
    • Wolfgang Baumeister
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-9

  • A global network of researchers was formed to investigate the role of human genetics in SARS-CoV-2 infection and COVID-19 severity; this paper reports 13 genome-wide significant loci and potentially actionable mechanisms in response to infection.

    • Mari E. K. Niemi
    • Juha Karjalainen
    • Chloe Donohue
    ResearchOpen Access
    Nature
    Volume: 600, P: 472-477

  • Hoyer et al. establish that selective autophagy mechanisms are needed to remodel the ER and its proteome during in vitro neurogenesis across neuronal subcompartments and decode the substrate selectivity of ER-phagy receptors.

    • Melissa J. Hoyer
    • Cristina Capitanio
    • J. Wade Harper
    ResearchOpen Access
    Nature Cell Biology
    Volume: 26, P: 378-392

  • Lee et al. show that, after nitrogen starvation and genetic interference with the architecture of nuclear pore complexes, nucleoporins are degraded by autophagy, constituting a quality-control step at the nuclear envelope.

    • Chia-Wei Lee
    • Florian Wilfling
    • Boris Pfander
    Research
    Nature Cell Biology
    Volume: 22, P: 159-166

  • In-cell structural studies in Saccharomyces cerevisiae reveal that the configuration of the Nup159 complex is a key determinant of the mRNA export function of the nuclear pore complex, and suggest a model in which nuclear pore complexes are degraded via the autophagy machinery.

    • Matteo Allegretti
    • Christian E. Zimmerli
    • Martin Beck
    Research
    Nature
    Volume: 586, P: 796-800