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Showing 1–5 of 5 results
Advanced filters: Author: Nasrollah Rezaei-Ghaleh Clear advanced filters

  • Protein aggregation plays a crucial role in several neurodegenerative diseases. Here the authors demonstrate that phosphorylation of β-amyloid aggregates—the pathological hallmark of Alzheimer's disease—can change the molecular properties of aggregates, suggesting how phosphorylation contributes to disease progression.

    • Nasrollah Rezaei-Ghaleh
    • Mehriar Amininasab
    • Markus Zweckstetter
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-9

  • The authors demonstrate a proof-of-principle example of an NH-π hydrogen bond on the surface of an intrinsically disordered protein through detection of weak scalar couplings by NMR, supported by Molecular Dynamics simulation and DFT calculations.

    • Luigi Russo
    • Dipendu Dhar
    • Nasrollah Rezaei-Ghaleh
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-11

  • Processing bodies (P-bodies) are non-membrane-bound protein/RNA granules in the cytosol. Here the authors combine bioinformatics, NMR and cell based assays and find that lysine is enriched in the disordered regions of P-body-associated proteins and show that lysine-rich polypeptides form highly dynamic lysine/RNA-coacervates and lysine acetylation reverses liquid-liquid phase separation.

    • Tina Ukmar-Godec
    • Saskia Hutten
    • Markus Zweckstetter
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-15