Douglas J. Kojetin

The paper shows that ileitis disrupts bile acid (BA) pool balance, altering immune regulation by affecting BA receptor interactions and Th17 cell function.

The paper investigates how covalent inhibitors of PPARγ shift its conformational state, affecting ligand binding and inhibitor efficacy.

This study determines the structural properties of full-length IMP2, revealing its dimeric conformation and RNA-induced changes, which may inform drug design.

This study compares FX-909 to other covalent PPARγ inverse agonists, showing improved corepressor-selective inverse agonism and stabilization of a repressive conformation.

This paper identifies a tethering mechanism by which Pin1 catalyzes proline cis-trans isomerization at a noncanonical site in the PPARγ AF-1 domain.

This paper investigates the activation mechanism of NR4A-RXR heterodimers using a diverse RXR ligand set, revealing both classical and non-classical activation pathways.

This study identifies a PPARγ ligand series that shifts the receptor's conformational ensemble between active and repressive states, revealing how subtle chemical changes influence its function.

This study reveals that covalent PPARgamma inhibitors like GW9662 and T0070907 weaken but do not block binding of other synthetic ligands through an allosteric mechanism, altering the receptor's conformation and ligand binding affinity.

The paper resolves conflicting findings on heme's role in REV-ERBβ-NCoR binding by showing heme directly enhances their interaction through structural and biochemical analyses.