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Showing 1–6 of 6 results
Advanced filters: Author: Marcel P. Goldschen-Ohm Clear advanced filters

  • In outwardly rectifying potassium channels, depolarization initiates conformational changes in voltage-sensing domains. Goldschen-Ohmet al. find that movement of three specific domains correlates with conductance levels, and rearrangements of a fourth domain results in preinactivation subconductance states.

    • Marcel P. Goldschen-Ohm
    • Deborah L. Capes
    • Baron Chanda
    ResearchOpen Access
    Nature Communications
    Volume: 4, P: 1-10

  • The authors identify a single main-chain hydrogen bond required to keep GABAA receptors closed in the absence of neurotransmitter. Electrophysiology and molecular dynamics simulations suggest disruption of this bond is a key component of channel opening during inhibitory synaptic signaling in the brain.

    • Cecilia M. Borghese
    • Jason D. Galpin
    • Marcel P. Goldschen-Ohm
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-10

  • Here the authors use nanovesicles, microfluidics and single-molecule methods to observe individual ligand binding events that stimulate activation of CNG ion channels. They find that binding is followed by a conformational change of either independent or weakly cooperative binding domains.

    • Vishal R. Patel
    • Arturo M. Salinas
    • Marcel P. Goldschen-Ohm
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13

  • Pioneering studies in voltage-gated potassium channels have described movement of the voltage-sensing domain (VSD) S4 helix across the membrane electric field in molecular detail, but much less is known regarding opening of the intrinsic proton pore within VSDs of voltage-dependent proton channels. By systematically probing local kinematics, a new study reveals that movements in helix S1 correlate with pore opening and are distinct from voltage-sensing movements of the charged S4 segment.

    • Marcel P Goldschen-Ohm
    • Baron Chanda
    News & Views
    Nature Structural & Molecular Biology
    Volume: 22, P: 277-278

  • The location of the activation gate in voltage-gated sodium channels is not clear. Here, the authors report that a conserved intracellular gate consisting of a ring of hydrophobic residues regulates access to the pore.

    • Kevin Oelstrom
    • Marcel P. Goldschen-Ohm
    • Baron Chanda
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-9

  • A nanodisc-based approach reveals that the fusion pores formed during neurotransmitter exocytosis are hybrid structures composed of both membrane lipids and SNARE proteins.

    • Huan Bao
    • Marcel Goldschen-Ohm
    • Edwin R Chapman
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 67-73