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Showing 1–11 of 11 results
Advanced filters: Author: Joseph A. Mindell Clear advanced filters
  • The authors show cryo-electron microscopy structures of the human high-affinity sodium–dicarboxylate cotransporter, responsible for dicarboxylate import into the cell, in complex with various substrates and in different states establish the basis of substrate recognition, differentiation and release, as well as regulation of transport domain movement.

    • Yan Li
    • Jinmei Song
    • Da-Neng Wang
    Research
    Nature Structural & Molecular Biology
    Volume: 32, P: 502-512
  • This paper shows that ClC-7 is a Cl/H+ antiporter in lysosomal membranes, the activity of which maintains the correct membrane voltage during acidification of the organelle. This work reinforces the idea that plasma membrane CLCs are Cl channels whereas 'intracellular' CLCs are antiporters.

    • Austin R. Graves
    • Patricia K. Curran
    • Joseph A. Mindell
    Research
    Nature
    Volume: 453, P: 788-792
  • Structures of the human sodium-dependent citrate transporter NaCT in complexes with citrate or a small-molecule inhibitor reveal how the inhibitor—which binds to the same site as citrate—arrests the transport cycle of NaCT.

    • David B. Sauer
    • Jinmei Song
    • Da-Neng Wang
    Research
    Nature
    Volume: 591, P: 157-161
  • Membrane-bound protein channels that allow only urea to pass through are vital to the kidney's ability to conserve water. Crystal structures show that the channels select urea molecules by passing them through thin slots.

    • Mark A. Knepper
    • Joseph A. Mindell
    News & Views
    Nature
    Volume: 462, P: 733-734
  • All CLC proteins transport Cl across membranes. However, the family includes both Cl channels and Cl/H+ antiporters, proteins once thought to operate by dramatically different mechanisms. An apparent evolutionary relic, a proton-transport apparatus in a CLC channel, reveals deep intertwinings between channel and transporter mechanisms.

    • Joseph A Mindell
    News & Views
    Nature Structural & Molecular Biology
    Volume: 15, P: 781-783
  • ‘Repeat swap’ modeling of the outward-facing conformation and biochemical analyses show that the bacterial VcINDY symporter uses an elevator-type mechanism for substrate transport across the cell membrane.

    • Christopher Mulligan
    • Cristina Fenollar-Ferrer
    • Joseph A Mindell
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 256-263