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Showing 1–17 of 17 results
Advanced filters: Author: Douglas J. Kojetin Clear advanced filters

  • Some nuclear receptors dimerize with retinoid X receptor to allow ligand-dependent signalling. Here, Kojetin et al.use structural and biophysical techniques to identify structural changes that guide these complex signalling networks.

    • Douglas J. Kojetin
    • Edna Matta-Camacho
    • Kendall W. Nettles
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-14

  • Central to the lineage commitment of multipotent mesenchymal stem cells is the nuclear receptor PPARγ, the master regulator of adipogenesis. Here the authors use a variety of structural approaches to rationally design PPARγ inverse agonist SR2595, and demonstrate its ability to promote osteogenesis.

    • David P. Marciano
    • Dana S. Kuruvilla
    • Patrick R. Griffin
    Research
    Nature Communications
    Volume: 6, P: 1-7

  • Progesterone receptor membrane component 2 is required to transport haem from the mitochondria to the nucleus, where, in adipose tissue, it has roles in regulation of thermogenesis and glucose metabolism.

    • Andrea Galmozzi
    • Bernard P. Kok
    • Enrique Saez
    Research
    Nature
    Volume: 576, P: 138-142

  • Structural studies of nuclear receptor transcription factors revealed that nearly all nuclear receptors share a conserved helix 12 dependent transcriptional activation mechanism. Here the authors present two crystal structures of peroxisome proliferator-activated receptor gamma (PPARγ) in an inverse agonist/corepressor-bound transcriptionally repressive conformation, where helix 12 is located within the orthosteric ligand-binding pocket instead, and discuss mechanistic implications.

    • Jinsai Shang
    • Sarah A. Mosure
    • Douglas J. Kojetin
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-14

  • A systems-based approach to profile glucocorticoid (GC) receptor ligands in a broad range of assays representing different phenotypic responses linked these to transcriptional profiles and led to separation of GC therapeutic effects from side effects.

    • Nelson E. Bruno
    • Jerome C. Nwachukwu
    • Kendall W. Nettles
    Research
    Nature Chemical Biology
    Volume: 17, P: 307-316

  • The abundant IincRNA growth arrest-specific 5 (Gas5) inhibits the transcriptional activity of steroid hormone receptors (SRs) through direct competition for DNA binding. Here the authors use X-ray crystallography, NMR and complementary biochemical approaches to elucidate the molecular and evolutionary mechanisms that guide Gas5 binding to SRs.

    • William H. Hudson
    • Mark R. Pickard
    • Eric A. Ortlund
    Research
    Nature Communications
    Volume: 5, P: 1-13

  • Synthetic REV-ERB agonists can alter the circadian expression of core clock genes in the hypothalami of mice, which changes the expression of metabolic genes in liver, skeletal muscle and adipose tissue, and results in increased energy expenditure.

    • Laura A. Solt
    • Yongjun Wang
    • Thomas P. Burris
    Research
    Nature
    Volume: 485, P: 62-68

  • 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 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

  • Glucocorticoid receptor (GR) regulates immunity and inflammation but the mechanisms by which GR represses proinflammatory genes are still being debated. Here the authors use a multidisciplinary approach and show that GR binds to a cryptic site within genome-wide NFκB DNA response elements to repress pro-inflammatory genes.

    • William H. Hudson
    • Ian Mitchelle S. de Vera
    • Eric A. Ortlund
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13

  • A comprehensive HDX analysis of the vitamin D receptor–retinoid X receptor (VDR-RXR) reveals extensive allosteric communication within the same polypeptide where DNA or ligand can induce alterations in distant domains of the receptors. The work also shows communication between subunits in the heterodimer.

    • Jun Zhang
    • Michael J Chalmers
    • Patrick R Griffin
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 556-563

  • 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

  • Constrained ligands activate a canonical ER pathway via a common structural mechanism, whereas dynamic ligands rewire the canonical pathway; DBD-dependent activity interferes with canonical ER proliferative signals and associates with a strong anti-inflammatory effect.

    • Sathish Srinivasan
    • Jerome C Nwachukwu
    • Kendall W Nettles
    Research
    Nature Chemical Biology
    Volume: 9, P: 326-332

  • This Review highlights recent progress in the development of ligands to target two classes of nuclear receptors — the REV-ERBs and retinoic acid receptor-related orphan receptors (RORs) — and describes how such ligands might be useful for treating disorders related to metabolism, immune function and the circadian rhythm.

    • Douglas J. Kojetin
    • Thomas P. Burris
    Reviews
    Nature Reviews Drug Discovery
    Volume: 13, P: 197-216