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. Author manuscript; available in PMC: 2025 Mar 24.
Published in final edited form as: J Med Chem. 2025 Feb 7;68(4):4829–4847. doi: 10.1021/acs.jmedchem.4c03104

Figure 1. Nurr1 agonism of 37.

Figure 1

(a) Isothermal titration calorimetry (ITC) demonstrated high affinity (Kd 0.12 μM) binding of 37 to the recombinant Nurr1 LBD. The fitting of the heat of binding is shown and the isotherm at 25°C is shown as inset. (b) 37 activated full-length human Nurr1 on the response elements for the monomer (NBRE, EC50 0.07±0.02 μM), homodimer (NurRE, EC50 0.027±0.008 μM) and RXR heterodimer (DR5, EC50 0.014±0.006 μM) with consistently low nanomolar potency. Data are the mean±S.E.M., n≥4.