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Showing 1–8 of 8 results
Advanced filters: Author: Ina Vorberg Clear advanced filters

  • Pathologic protein aggregates associated with neurodegenerative diseases have the ability to transmit to unaffected cells via extracellular vesicles or direct cell-to-cell contact. Here, Liu et al. show that viral glycoproteins can contribute to intercellular proteopathic seed transmission via both routes.

    • Shu Liu
    • André Hossinger
    • Ina M. Vorberg
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • Endogenous retroviruses, or genomic relics of ancient viral infection, have been associated with certain neurodegenerative diseases. Here, Liu et al. report a pathway by which reactivated viral gene products contribute to intercellular protein aggregate spreading.

    • Shu Liu
    • Stefanie-Elisabeth Heumüller
    • Ina M. Vorberg
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • The authors show that acetylation enhances the aggregation of 3R tau, while blocking the aggregation of 4R tau, providing a molecular basis for disease- and isoform-specific tau deposition.

    • Pijush Chakraborty
    • Gwladys Rivière
    • Markus Zweckstetter
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-13

  • The authors present a method for the conversion of full-length tau protein into seeding-competent amyloid fibrils without heparin or other negatively charged co-factors, which could be useful for studying the effects of post-translational modifications on Tau aggregation as well as to identify potential inhibitors of tau aggregation. Biochemical experiments and solid-state NMR spectroscopy measurements show that these co-factor-free tau fibrils have similar properties as amyloid fibrils isolated from brain tissue but differ from those of commonly used heparin-induced tau fibrils.

    • Pijush Chakraborty
    • Gwladys Rivière
    • Markus Zweckstetter
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Some human amyloid proteins have been shown to interact with viral proteins, suggesting that they may have potential as therapeutic agents. Here the authors design synthetic amyloids specific for influenza A and Zika virus proteins, respectively, and show that they can inhibit viral replication.

    • Emiel Michiels
    • Kenny Roose
    • Joost Schymkowitz
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13