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Showing 1–4 of 4 results
Advanced filters: Author: Omar E. Alvarenga Clear advanced filters

  • Feng, Alvarenga et al. use cryo-electron microscopy to visualize the activation of the transmembrane protein 16F channel and scramblase in liposomes to show that it adopts a conformation that forms separate pathways for ions and lipids, thereby rationalizing its dual activity.

    • Zhang Feng
    • Omar E. Alvarenga
    • Alessio Accardi
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 33, P: 664-676

  • Xkr4 apoptotic scramblase activation is thought to involve caspase cleavage and dimerization to expose phosphatidylserine on dying cells. The authors show that full-length Xkr4 is an active monomeric scramblase. CryoEM reveals a conformation that promotes membrane thinning and scrambling, enhancing understanding of hXkr4 activity.

    • Sayan Chakraborty
    • Zhang Feng
    • Alessio Accardi
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-18

  • The authors used cryo-EM to visualize the arrangement of lipids at the closed groove of a TMEM16 scramblase and to reveal that both the structures and distributions of the protein’s conformations depend on the lipid composition and nanodisc scaffold.

    • Zhang Feng
    • Omar E. Alvarenga
    • Alessio Accardi
    Research
    Nature Structural & Molecular Biology
    Volume: 31, P: 1468-1481

  • Lipid scrambling is required for many cellular processes but the lipid-protein interactions that occur during transport are unknown. Using cryoEM and biochemical assays the authors show that membrane thinning is critical for lipid flipping.

    • Maria E. Falzone
    • Zhang Feng
    • Alessio Accardi
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-14