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Showing 1–4 of 4 results
Advanced filters: Author: Elise Delaforge Clear advanced filters

  • This study reveals how the intrinsically disordered protein POSH undergoes stepwise folding upon binding to the GTPase Rac1. Each folding step is dependent on the successful completion of the previous one, revealing a hierarchical folding mechanism.

    • Lenette F. Kjaer
    • Francesco S. Ielasi
    • Malene Ringkjøbing Jensen
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12

  • Studies on protein–protein interactions using proteins containing d- or l-amino acids show that stereoselectivity of binding varies with the degree of disorder within the complex.

    • Estella A. Newcombe
    • Amanda D. Due
    • Birthe B. Kragelund
    ResearchOpen Access
    Nature
    Volume: 636, P: 762-768

  • Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Here, the authors use NMR spectroscopy and quantitative ensemble modelling to describe the highly dynamic assemblies formed by the human-adapted or avian-adapted C-terminal domains with the respective ANP32A host proteins.

    • Aldo R. Camacho-Zarco
    • Sissy Kalayil
    • Martin Blackledge
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • Replication of Nipah virus, which causes human encephalitis, requires delivery of viral nucleoprotein N to the viral genome by phosphoprotein chaperone, P. The crystal structure of the N0–P core complex now reveals how the chaperone prevents premature N assembly on RNA and identifies a potential target for antiviral drugs.

    • Filip Yabukarski
    • Philip Lawrence
    • Marc Jamin
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 754-759