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Showing 1–4 of 4 results
Advanced filters: Author: Anne-Laure Blayo Clear advanced filters

  • The repressive states of peroxisome proliferator-activated receptor γ (PPARγ) are ill-defined, despite nuclear receptors being a major drug target. Here authors demonstrate multiple structurally distinct repressive states, providing a structural rationale for ligand bias in a nuclear receptor.

    • Zahra Heidari
    • Ian M. Chrisman
    • Travis S. Hughes
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • The nuclear receptor PPARγ regulates insulin sensitivity and is the molecular target of anti-diabetic drugs. Here, Hughes et al. show demonstrate binding of synthetic PPARγ agonists to a previously unknown binding site within PPARγ and show this affects structure and function of the receptor.

    • Travis S. Hughes
    • Pankaj Kumar Giri
    • Douglas J. Kojetin
    Research
    Nature Communications
    Volume: 5, P: 1-13

  • Peroxisome proliferator-activated receptor gamma (PPARγ) is a nuclear receptor. Here the authors provide insights into PPARγ activation by combining fluorine (19F) NMR and molecular dynamics simulations to characterize the nuclear receptor conformational ensemble in solution and the response of this ensemble to ligand and coregulatory peptide binding.

    • Ian M. Chrisman
    • Michelle D. Nemetchek
    • Travis S. Hughes
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-16

  • Peroxisome proliferator-activated receptor gamma (PPARγ) is a target for insulin sensitizing drugs. Here the authors combine NMR, X-ray crystallography and MD simulations and report a structural mechanism for eliciting PPARγ inverse agonism, where coactivator binding is inhibited and corepressor binding promoted, which causes PPARγ repression.

    • Richard Brust
    • Jinsai Shang
    • Douglas J. Kojetin
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-14