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Showing 1–9 of 9 results
Advanced filters: Author: Elisabetta Boeri Erba 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

  • Authors demonstrate that four distinct heterodimeric complexes catalyze chondroitin sulfate chain polymerization in humans. The synthase proteins possess catalytic activity, while the polymerization factors are essential for complex formation.

    • Poushalee Dutta
    • Rosa L. Cordeiro
    • Rebekka Wild
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Dubiez and colleagues present a cryo-EM structure of the complex responsible for nuclear export of pre-small nuclear RNAs, comprising CBC–PHAX–CRM1–RanGTP. The structure provides insights into the complex architecture, assembly and target RNA recognition.

    • Etienne Dubiez
    • William Garland
    • Stephen Cusack
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1555-1566

  • On the basis of the known crystallographic structures of 5000 'homo-oligomeric' complexes, this study derives plausible pathways for the emergence of ever more complex such assemblies during evolution. Using electrospray mass spectrometry, it is observed that the same pathways are followed on the shorter time-scale of protein assembly in vitro.

    • Emmanuel D. Levy
    • Elisabetta Boeri Erba
    • Sarah A. Teichmann
    Research
    Nature
    Volume: 453, P: 1262-1265

  • A number of disease-causing human transthyretin (TTR) mutations are known to lead to amyloid formation. Here the authors combine neutron crystallography, native mass spectrometry and modelling studies to characterize the T119M and S52P-TTR mutants, providing mechanistic insights into TTR amyloidosis.

    • Ai Woon Yee
    • Matteo Aldeghi
    • V. Trevor Forsyth
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • Bacillus thuringiensis israelensis (Bti) produces the naturally-crystalline proteinaceous toxin Cyt1Aa that is toxic to mosquito larvae. Here the authors grow recombinant nanocrystals of the Cyt1Aa protoxin in vivo and use serial femtosecond crystallography to determine its structure at different redox and pH conditions and by combining their structural data with further biochemical, toxicological and biophysical analyses provide mechanistic insights into the Cyt1Aa bioactivation cascade.

    • Guillaume Tetreau
    • Anne-Sophie Banneville
    • Jacques-Philippe Colletier
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16

  • Vps4 is a AAA+ family protein involved in the disassembly of ESCRT-III polymers during membrane fission events such as occur during HIV budding. Here the authors propose a structure-based model of how the conformational flexibility of Vps4 can be translated into mechanical forces to disassemble ESCRT-III during membrane fission.

    • Christophe Caillat
    • Pauline Macheboeuf
    • Patricia Renesto
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-12