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Showing 1–12 of 12 results
Advanced filters: Author: Daniel J. A. Roderer Clear advanced filters

  • Our understanding of how post-translational modification—protein phosphorylation—impacts the complexity of eukaryotic signalling pathways is continuously expanding. Now, protein oligophosphorylation has been characterized as an additional phosphorylation mode. Structural and mass spectrometry methods revealed that NME1 catalysed its own oligophosphorylation, leading to altered protein–protein interactions.

    • Arif Celik
    • Felix Schöpf
    • Dorothea Fiedler
    ResearchOpen Access
    Nature Chemistry
    Volume: 17, P: 1757-1767

  • A high-resolution cryo-electron microscopy structure of a complete Tc holotoxin complex reveals the precise mechanism of Tc toxin assembly, gate opening and release of the cytotoxic enzyme into the translocation channel.

    • Christos Gatsogiannis
    • Felipe Merino
    • Stefan Raunser
    Research
    Nature
    Volume: 563, P: 209-213

  • A genome-wide CRISPR–Cas9-mediated knockout screen in Drosophila cells identifies Visgun as a proteinaceous receptor for toxin complex toxins, demonstrating the utility of this approach for investigating insecticidal toxins and pathogens.

    • Ying Xu
    • Raghuvir Viswanatha
    • Min Dong
    Research
    Nature
    Volume: 610, P: 349-355

  • Pore-forming toxins are expressed as monomers and assemble into multimeric pores. Here, Benke et al. follow the kinetics of pore formation for the bacterial toxin ClyA with single-molecule methods and show that pore formation progresses through the assembly of oligomeric intermediates, rather than by the addition of monomers to a nascent pore.

    • Stephan Benke
    • Daniel Roderer
    • Benjamin Schuler
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-15

  • Entomopathogenic bacteria used for pest control secrete potent Tc toxins. Here, the authors combine biochemistry, solution and solid-state NMR spectroscopy and cryo-EM to show in atomic detail how the toxin disrupts the host cell cytoskeleton and kills the target cell.

    • Alexander Belyy
    • Florian Lindemann
    • Stefan Raunser
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • A cryo-EM structure of toxin component TcdA1 embedded in lipid nanodiscs reveals details of the mechanism used by this bacterial toxin to insert into the host cell membrane.

    • Christos Gatsogiannis
    • Felipe Merino
    • Stefan Raunser
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 884-890

  • Non-enveloped viruses such as SV40 are transported from the extracellular space into the host cell nucleus through a pathway involving endocytosis, trafficking to the endoplasmic reticulum (ER) lumen, transport across the ER membrane to the cytoplasm, and subsequent nuclear import. Helenius and colleagues provide insight into how SV40 escapes from the ER by showing that viral proteins interact with components of the host ER-associated degradation machinery (ERAD). These interactions are crucial for translocation of SV40 into the cytoplasm and infectivity.

    • Roger Geiger
    • Daniel Andritschke
    • Ari Helenius
    Research
    Nature Cell Biology
    Volume: 13, P: 1305-1314

  • Thorsten Wagner et al. present SPHIRE-crYOLO, a particle picking software for selecting particles from digital micrographs in cryoEM data. After training, the method automatically recognizes particles with high recall and precision, simplifying data pre-processing.

    • Thorsten Wagner
    • Felipe Merino
    • Stefan Raunser
    ResearchOpen Access
    Communications Biology
    Volume: 2, P: 1-13