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Showing 1–6 of 6 results
Advanced filters: Author: Leela Shrestha Clear advanced filters

  • ELOVLs are membrane-embedded enzymes that elongate very long chain fatty acids, precursors of sphingolipids and ceramides. The first crystal structure of a human ELOVL reveals an unexpected reaction mechanism, suggesting potential approaches for inhibition in disease.

    • Laiyin Nie
    • Tomas C. Pascoa
    • Elisabeth P. Carpenter
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 512-520

  • The X-ray crystal structure of the potassium channel TASK-1 reveals the presence of an X-gate, which traps small-molecule inhibitors in the intramembrane vestibule and explains their low washout rates from the channel.

    • Karin E. J. Rödström
    • Aytuğ K. Kiper
    • Elisabeth P. Carpenter
    Research
    Nature
    Volume: 582, P: 443-447

  • TMEM16K is a member of the TMEM16 family of integral membrane proteins that are either lipid scramblases or chloride channels. Here the authors combine cell biology, electrophysiology measurements, X-ray crystallography, cryo-EM and MD simulations to structurally characterize TMEM16K and show that it is an ER-resident lipid scramblase.

    • Simon R. Bushell
    • Ashley C. W. Pike
    • Elisabeth P. Carpenter
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-16

  • The cryo-EM structure of human polycystin-2 (PC2) in a closed conformation reveals a domain located above the pore filter, forming an upper vestibule and making contacts with the pore and voltage-sensor-like domains.

    • Mariana Grieben
    • Ashley C W Pike
    • Elisabeth P Carpenter
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 114-122