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Showing 1–7 of 7 results
Advanced filters: Author: Rajaa Boujemaa-Paterski Clear advanced filters
  • Vinculin binding to talin is a key event in focal adhesion dynamics; yet, how vinculin is activated to recruit actin remains unknown. Here, the authors use a multiscale approach to reveal that talin activates vinculin through an intricate allosteric mechanism tightly regulated by force.

    • Florian Franz
    • Rafael Tapia-Rojo
    • Frauke Gräter
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-16
  • Wang, Kronenberg-Tenga, Rosti and colleagues use several structural approaches to analyze the distribution of nucleosomes at the lamin–chromatin interface, test the impact of lamins on nucleosome density and identify a lamin A nucleosome-binding motif.

    • Baihui Wang
    • Rafael Kronenberg-Tenga
    • Ohad Medalia
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 1999-2011
  • Protrusive cellular structures contain a heterogeneous density of actin, but whether this influences motility is not known. Using an in vitro system and modelling, here the authors show that local actin monomer depletion and network architecture can tune the rate of network growth to impose steering during motility.

    • Rajaa Boujemaa-Paterski
    • Cristian Suarez
    • Laurent Blanchoin
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13
  • Actin filaments are a principal component of the cell cytoskeleton. Using micropatterning methods, physical influences on the growth of highly ordered actin structures are investigated. The spatial organization of actin nucleation sites is discovered to play an important role in establishing the architecture of actin networks.

    • Anne-Cécile Reymann
    • Jean-Louis Martiel
    • Manuel Théry
    Research
    Nature Materials
    Volume: 9, P: 827-832
  • Using cryo-electron microscopy and integrative modeling, the authors defined the structure of vimentin intermediate filaments, revealing a helical tube built of five protofibrils that enclose a fiber of low-complexity N-terminal domains.

    • Matthias Eibauer
    • Miriam S. Weber
    • Ohad Medalia
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 939-949