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Showing 1–7 of 7 results
Advanced filters: Author: Paul G. DeCaen Clear advanced filters

  • Voltage-gated sodium (Nav) channels are crucial for action potential initiation in excitable cells. Here the authors present the complete structure of prokaryotic NavMs in a fully open state, providing structural insight into the opening and closure of the channel's intracellular gate.

    • Altin Sula
    • Jennifer Booker
    • B. A. Wallace
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-9

  • Prokaryotic voltage-gated sodium channels possess dynamically disordered cytoplasmic C-terminal domains. Bagnéris et al. present the structure of the Magnetococcus marinusNavMs pore and C-terminal domain and reveal its role in coupling channel inactivation and opening.

    • Claire Bagnéris
    • Paul G. DeCaen
    • B. A. Wallace
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-10

  • Primary cilia are known as specialized calcium signalling compartments on the cell surface, but the ionic permeability and other physiological properties of these protrusions are unknown—this is one of two studies identifying the ion channels that densely populate primary cilia, with direct measurements revealing cilia as a unique, functionally independent calcium signalling compartment that modulates hedgehog signalling pathways.

    • Paul G. DeCaen
    • Markus Delling
    • David E. Clapham
    Research
    Nature
    Volume: 504, P: 315-318

  • Primary cilia are known as specialized calcium signalling compartments on the cell surface, but the ionic permeability and other physiological properties of these protrusions are unknown—this is one of two studies identifying the ion channels that densely populate primary cilia, with direct measurements revealing cilia as a unique, functionally independent calcium signalling compartment that modulates hedgehog signalling pathways.

    • Markus Delling
    • Paul G. DeCaen
    • David E. Clapham
    Research
    Nature
    Volume: 504, P: 311-314

  • The crystal structure of NavRh, a NaChBac orthologue from the marine Rickettsiales sp. HIMB114, defines an ion binding site within the selectivity filter, and reveals several conformational rearrangements that may underlie the electromechanical coupling mechanism.

    • Xu Zhang
    • Wenlin Ren
    • Nieng Yan
    Research
    Nature
    Volume: 486, P: 130-134