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Showing 1–7 of 7 results
Advanced filters: Author: Alexander von Appen Clear advanced filters

  • Cardiac ryanodine receptors (RyR2) are critical for heart contraction. Here, the authors use 3D MINFLUX microscopy to image receptor subunits and RyR2 orientation with nanometre resolution, thereby providing a molecular view of the organisation and clustering of these cardiac muscle receptors.

    • Alexander H. Clowsley
    • Anna Meletiou
    • Christian Soeller
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-15

  • All cells are encapsulated by a membrane of complex lipidic composition, and understanding the roles of different lipids in membrane function is experimentally challenging to address. Here, Justice et al. present an approach to minimize and tune the membrane lipid composition in a ‘minimal’ bacterial cell, revealing that two lipid species can support life.

    • Isaac Justice
    • Petra Kiesel
    • James P. Saenz
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17

  • Human OPA1 embeds itself into cardiolipin-containing membranes through a lipid-binding paddle domain, and OPA1 oligomerization through multiple assembly interfaces promotes the helical assembly of a flexible OPA1 lattice on the membrane, driving mitochondrial fusion in cells.

    • Alexander von der Malsburg
    • Gracie M. Sapp
    • Halil Aydin
    Research
    Nature
    Volume: 620, P: 1101-1108

  • The most comprehensive architectural model to date of the nuclear pore complex reveals previously unknown local interactions, and a role for nucleoporin 358 in Y-complex oligomerization.

    • Alexander von Appen
    • Jan Kosinski
    • Martin Beck
    Research
    Nature
    Volume: 526, P: 140-143

  • TFIIIC is a RNA polymerase III-specific general transcription factor complex essential for tRNA synthesis. Here the authors combine chemical crosslinking/mass spectrometry and X-ray crystallography to define the architecture of TFIIIC and suggest a model for the assembly of pre-initiation complexes at tRNA genes.

    • Gary Male
    • Alexander von Appen
    • Christoph W. Müller
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-11

  • The Nup82–Nup159–Nsp1 complex, which plays a key role in mRNA export, is recruited late during the process of nuclear pore complex (NPC) assembly. Here the authors combine crosslinking mass spectrometry, biochemical reconstitution and molecular modeling to gain insights into the mechanism of Nup82 recruitment to the NPC.

    • Roman Teimer
    • Jan Kosinski
    • Ed Hurt
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11