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Showing 1–10 of 10 results
Advanced filters: Author: Vera Moiseenkova-Bell Clear advanced filters

  • TRPV5 ion channels play pivotal roles in epithelial physiology. Here, the authors describe that the common compound menthol acts as a pore blocker on these channels and provide a functional and structural picture of its mechanism of action.

    • Angélica Méndez-Reséndiz
    • José J. De Jesús-Pérez
    • León D. Islas
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-13

  • Lysosomes are vital for cellular health and linked to many diseases. Here, authors use cryo-ET to image intact lysosomes and resolve lysosomal protein structures, providing a platform to advance the study of lysosome biology.

    • Bridget M. McVeigh
    • José J. De Jesús-Pérez
    • Vera Y. Moiseenkova-Bell
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • The authors reveal that probenecid, an FDA-approved drug, uniquely modulates TRPV2 through an intracellular pocket. Probenecid drives the channel into an activated conformation, providing insights into potential therapeutic applications.

    • Julia A. Rocereta
    • Toni Sturhahn
    • Vera Moiseenkova-Bell
    Research
    Nature Structural & Molecular Biology
    Volume: 32, P: 1019-1029

  • Long-chain acyl-Coenzyme-A is a metabolic intermediate with important signaling functions. Here the authors show that it activates the Ca2+ selective ion channels TRPV5 and TRPV6 and elucidate the structural basis of TRPV5 activation using CryoEM.

    • Bo-Hyun Lee
    • José J. De Jesús Pérez
    • Tibor Rohacs
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • A non-selective calcium channel transient receptor potential vanilloid 2 (TRPV2) is a potential drug target. Here, the authors employ cryo-electron microscopy, in silico docking, and electrophysiology to identify a binding site for an activator 2-aminoethoxydiphenyl borate (2-APB) in this channel.

    • Ruth A. Pumroy
    • Anna D. Protopopova
    • Vera Y. Moiseenkova-Bell
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • Transient receptor potential (TRP) proteins are Ca2+-permeable cation channels activated by a range of chemical and physical stimuli. Here the authors describe a cryo-EM structure of the full-length TRPV2 channel that provides insight into the regulation of the TRPV subfamily of channels.

    • Kevin W. Huynh
    • Matthew R. Cohen
    • Vera Y. Moiseenkova-Bell
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-8

  • Serotonin receptor (5-HT3AR), a pentameric ligand-gated ion channel, regulates numerous gastrointestinal functions. Here the authors provide a cryo-electron microscopic structure from the full-length 5-HT3AR in the apo-state which corresponds to a resting conformation of the channel.

    • Sandip Basak
    • Yvonne Gicheru
    • Sudha Chakrapani
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10

  • TRPV5 is a kidney specific transient receptor potential (TRP) channel with an important role in calcium reabsorption. Here the authors provide mechanistic insights into TRPV5 modulation by determining the phosphatidylinositol 4,5-bisphosphate and calmodulin bound TRPV5 cryo-EM structures.

    • Taylor E. T. Hughes
    • Ruth A. Pumroy
    • Vera Y. Moiseenkova-Bell
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-11

  • The cryo-EM structure of the full-length TRPV5 channel in complex with inhibitor econazole reveals a domain-swapped architecture and provides insights into mechanisms of inhibition.

    • Taylor E. T. Hughes
    • David T. Lodowski
    • Vera Y. Moiseenkova-Bell
    Research
    Nature Structural & Molecular Biology
    Volume: 25, P: 53-60

  • High-speed AFM enables visualization of intrinsically disordered regions (IDRs) in TRP ion channels and shows that IDRs may mediate protein-protein interactions with adjacent TRP molecules.

    • Raghavendar R. Sanganna Gari
    • Grigory Tagiltsev
    • Simon Scheuring
    ResearchOpen Access
    Communications Biology
    Volume: 6, P: 1-10