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Showing 1–6 of 6 results
Advanced filters: Author: Rasmus Kock Flygaard Clear advanced filters

  • Mitochondrial ATP synthases are involved in shaping the mitochondrial cristae. The cryo-EM structure of type III ATP synthase reveals the architecture of the unusual, asymmetrical, U-shaped dimer and offers insights into the interaction with the natural inhibitor IF1 and membrane lipids. The structure of the enzyme tetramer suggests the mechanism of membrane curvature generation.

    • Rasmus Kock Flygaard
    • Alexander Mühleip
    • Alexey Amunts
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Structural and functional analysis of mitochondria from the human parasite Toxoplasma gondii reveals that its ATP synthase assembles into cyclic hexamers, arranged together in a form of pentagonal pyramids required for maintenance of cristae morphology in Apicomplexa.

    • Alexander Mühleip
    • Rasmus Kock Flygaard
    • Alexey Amunts
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13

  • Asymmetric phospholipid distribution in cell membranes is vital for cellular function. Here, authors reveal how ATP8B1, a P4-ATPase, can transport different lipids, including phosphatidylinositol.

    • Thibaud Dieudonné
    • Felix Kümmerer
    • Poul Nissen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • During stress conditions bacterial ribosomes dimerize and form inactive but stable hibernating 100S particles, a process that is facilitated by the hibernation-promoting factor (HPF). Here the authors analyze 100S dimer formation as a function of HPF protein concentration and present the Thermus thermophilus 100S ribosome cryo-EM structure.

    • Rasmus Kock Flygaard
    • Niels Boegholm
    • Lasse B. Jenner
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-12