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    1. Neuroscience

    Enhanced excitability of cortical neurons in low-divalent solutions is primarily mediated by altered voltage-dependence of voltage-gated sodium channels

    Briana J Martiszus, Timur Tsintsadze ... Stephen M Smith
    External calcium regulates neuronal excitability via its actions on voltage-gated sodium channels but not by regulating NALCN via the calcium-sensing receptor.
    1. Structural Biology and Molecular Biophysics

    High temperature sensitivity is intrinsic to voltage-gated potassium channels

    Fan Yang, Jie Zheng
    Highly temperature-sensitive behavior of voltage-gated potassium channels provides a mechanistic model for how heat-activated TRP channels serve as temperature and pain sensors.
    1. Structural Biology and Molecular Biophysics

    Structural dynamics determine voltage and pH gating in human voltage-gated proton channel

    Shuo Han, Sophia Peng ... Shizhen Wang
    Visualization of the real-time conformational transitions of the human voltage-gated proton channel hHv1 provided novel insights into how voltage and pH gradients modify the dynamic behaviors of channel structures to control proton flow across membrane.
    1. Structural Biology and Molecular Biophysics

    Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state

    Keenan C Taylor, Po Wei Kang ... Charles R Sanders
    The intermediate state conformation of the human KCNQ1 potassium channel voltage sensor domain was determined, validated, and shown to be conductive under physiological conditions.
    1. Structural Biology and Molecular Biophysics

    Helix breaking transition in the S4 of HCN channel is critical for hyperpolarization-dependent gating

    Marina A Kasimova, Debanjan Tewari ... Baron Chanda
    The gating polarity of a voltage-gated ion channel is primarily determined by turn propensity of residues at a critical position in the middle of the S4 voltage-sensing helix.
    1. Structural Biology and Molecular Biophysics

    Distinctive mechanisms of epilepsy-causing mutants discovered by measuring S4 movement in KCNQ2 channels

    Michaela A Edmond, Andy Hinojo-Perez ... Rene Barro-Soria
    Because voltage-gated KCNQ2 channels are central to physiological and pathophysiological events, understanding how disease-causing mutations in different channel regions disrupt function will help future development of mutation-specific antiepileptic therapies.
    1. Structural Biology and Molecular Biophysics

    Aromatic interactions with membrane modulate human BK channel activation

    Mahdieh Yazdani, Guohui Zhang ... Jianhan Chen
    Computation and experiment together demonstrate that nonspecific membrane–protein interactions could regulate transmembrane protein function and suggest that covalent linkers can be an integral component of the sensing apparatus.
    1. Structural Biology and Molecular Biophysics

    ML277 specifically enhances the fully activated open state of KCNQ1 by modulating VSD-pore coupling

    Panpan Hou, Jingyi Shi ... Jianmin Cui
    ML277 exclusively enhances the AO state voltage-sensing domain (VSD)-pore coupling of KCNQ1 channels, providing an effective tool to investigate the voltge-dependent gating and new strategies for treating long QT syndrome.
    1. Structural Biology and Molecular Biophysics
    2. Neuroscience

    Single-molecule fluorimetry and gating currents inspire an improved optical voltage indicator

    Jeremy S Treger, Michael F Priest, Francisco Bezanilla
    ArcLight, a popular optogenetic reporter of voltage, is studied at both single-molecule and macroscopic levels, which leads to new mechanistic understanding and to the rational design of a faster reporter.
    1. Structural Biology and Molecular Biophysics

    The HCN domain couples voltage gating and cAMP response in hyperpolarization-activated cyclic nucleotide-gated channels

    Alessandro Porro, Andrea Saponaro ... Anna Moroni
    Experimental and computational approaches reveal how ligand binding is coupled to voltage sensing in a HCN channels.