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Showing 1–3 of 3 results
Advanced filters: Author: Alexander Krah Clear advanced filters

  • The membrane-embedded c-ring allows the passage of protons to power the synthesis of ATP by the FoF1 ATPase. Previous structural data have shown the proton acceptor-donor sites in a closed, ion-locked conformation. Structural and computational data now reveal the open conformation of the yeast mitochondrial c10 ring.

    • Jindrich Symersky
    • Vijayakanth Pagadala
    • David M Mueller
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 485-491

  • Free-energy molecular dynamics simulations and high-resolution structural analysis of the c-ring of the F1Fo ATPase rotary motor, which mediates ion translocation, suggest conformational flexibility and reversible ion binding in the c-subunits, in an environment mimicking the a-subunit.

    • Denys Pogoryelov
    • Alexander Krah
    • Thomas Meier
    Research
    Nature Chemical Biology
    Volume: 6, P: 891-899

  • ATP-binding cassette transporter ABCB1 is known to be involved in drug resistance in cancer treatment, however, current ABCB1 inhibitors have not been successful in clinical trials due to their potential cytotoxicity. Here, the authors hypothesize that potential ABCB1 substrates in bats could act as competitive inhibitors against ABCB1 in humans, and identify the tryptophan structure as a promising lead structure for the development of non-toxic ABCB1 inhibitors.

    • Javier Yu Peng Koh
    • Yoko Itahana
    • Koji Itahana
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-17