A unified mechanism for NR4A–RXR activation
Our eLife study examines ligand-dependent activation of NR4A–RXR heterodimers.
Douglas Kojetin promoted to Professor of Biochemistry
The Vanderbilt Institute of Chemical Biology announces Douglas Kojetin’s promotion to Professor of Biochemistry.
Conformational ensembles and PPARγ inhibitor efficacy
Our eLife study connects a shift toward a transcriptionally repressive PPARγ ensemble with improved covalent inhibitor efficacy.
Structural insights into IMP2 dimerization and RNA binding
A collaborative study in the Journal of Structural Biology examines IMP2 dimerization and RNA binding.
The structural basis of PPARγ repression by FX-909
Our study of the covalent inverse agonist FX-909 is published in the Journal of Medicinal Chemistry. The work examines the structural basis of PPARγ-mediated transcriptional repression.
A tethering mechanism for Pin1 catalysis
Our PNAS study examines how a tethering mechanism supports Pin1-catalyzed proline cis–trans isomerization at a noncanonical site.
Ligand efficacy and receptor conformational ensembles
Our Nature Communications study connects ligand efficacy with shifts between transcriptionally active and repressive nuclear receptor conformations.