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Showing 1–6 of 6 results
Advanced filters: Author: Philipp A. M. Schmidpeter Clear advanced filters

  • Thon et al. showed that the signaling lipid PIP2 inhibits a bacterial homolog of cyclic nucleotide-gated ion channels by binding between the voltage-sensing and pore domains of adjacent subunits and stabilizing a resting channel state.

    • Oliver Thon
    • Zhihan Wang
    • Crina M. Nimigean
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-10

  • Schmidpeter and colleagues showed that anionic lipids bind to pacemaker ion channels and increase their activity by acting like keys that unlock salt bridges at the channel gates.

    • Philipp A. M. Schmidpeter
    • Di Wu
    • Crina M. Nimigean
    Research
    Nature Structural & Molecular Biology
    Volume: 29, P: 1092-1100

  • Using atomic force microscopy, Pan et al. show that cyclic nucleotide-gated ion channel SthK, which can be differentially activated by cAMP and cGMP, binds both cyclic nucleotides but only cAMP can access a deep-bound state that could be essential for cAMP-dependent channel activation.

    • Yangang Pan
    • Emmi Pohjolainen
    • Simon Scheuring
    Research
    Nature Structural & Molecular Biology
    Volume: 30, P: 512-520

  • Tandem pore (K2P) potassium channels set the cellular resting membrane potential in tissues throughout the body. Here, authors show how the composition of phospholipid within the bilayer may directly alter gating in this family of ion channels.

    • Philipp A. M. Schmidpeter
    • John T. Petroff II
    • Paul M. Riegelhaupt
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • SthK, a cyclic nucleotide-gated ion channel from Spirochaeta thermophila activates slowly upon cAMP increase. Here, authors investigate cAMP-induced activation in purified SthK channels using stopped-flow assays and enzymatic catalysis and reveal that the cis/trans conformation of a conserved proline in the cyclic nucleotide-binding domain determines the activation kinetics of SthK.

    • Philipp A. M. Schmidpeter
    • Jan Rheinberger
    • Crina M. Nimigean
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12