Inhibition of Glutathione S Transferase Enzymes by NRF2 Activators: An off-target effect that may limit their therapeutic potential
Authors/Creators
- 1. Department of Biotechnology, Sharda School of Bio-Science and Technology, Sharda University, Greater Noida, India
- 2. Department of Medical Oncology, Jawaharlal Institute of Postgraduate Medical Education and Research (JIPMER), Puducherry, India
- 3. Cansearch Research Platform for Pediatric Oncology and Hematology, Department of Pediatrics, Gynecology, and Obstetrics, University of Geneva, Geneva, Switzerland
Description
This repository represents Version 2 of the NRF2-related computational dataset. Version 1 of the dataset contained the molecular dynamics (MD) simulation data and associated analyses. The present Version 2 extends the dataset by providing the molecular docking data for selected molecules against multiple glutathione S-transferase (GST) isoforms, thereby complementing the MD simulation results reported in Version 1.
Version 2 contains blind and direct molecular docking results for selected NRF2-related molecules against seven GST isoforms: GSTA1, GSTA2, GSTM1, GSTM2, GSTM5, GSTP1, and GSTT1. The dataset includes docking input and output structures, docking log files, docking result tables, control compounds, target-selection information, and supporting files associated with the selected molecules and docking analyses.
Together, Versions 1 and 2 provide complementary computational data, with Version 1 focusing on molecular dynamics simulations and Version 2 focusing on molecular docking and predicted ligand–GST interactions. These datasets are intended to support reproducibility, independent analysis, validation, and further computational investigation of the NRF2–GST regulatory axis.
The docking results represent computational predictions and should not be interpreted as experimental evidence of binding affinity, GST inhibition, or biological activity.