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Showing 1–4 of 4 results
Advanced filters: Author: Jacqueline M. Gulbis Clear advanced filters

  • The transition between conducting and non-conducting states of K+ channels has been explained by conformational changes at the intracellular entrance to the conduction pathway. Here authors demonstrate that control over K+ currents in Kir channels is not explained by the canonical pore-gating model, as conduction is not impaired by a constricted inner helix bundle.

    • Katrina A. Black
    • Sitong He
    • Jacqueline M. Gulbis
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • The Kir potassium channels are known to operate and gate without a major conformational change. Here, the authors identify the permeation gate of Kir channels as a steric plug within the conduction pathway, describing how tightly associated anionic lipids pushing into fenestrations in the pore walls engage with the plug to operate the gate.

    • Ruitao Jin
    • Sitong He
    • Jacqueline M. Gulbis
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-11

  • Crystal structures of BAK core domain dimers suggest a mechanism by which lipids contribute to the oligomerization of BAK, which is essential for BAK-mediated permeabilization of the mitochondrial outer membrane.

    • Angus D. Cowan
    • Nicholas A. Smith
    • Peter E. Czabotar
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 1024-1031