Novel inhibitors of human glucose-6-phosphate dehydrogenase (HsG6PD) affect the activity and stability of the protein - Ramírez-Nava, Edson Jiovany; Hernández-Ochoa, Beatriz; Navarrete-Vázquez, Gabriel; Arreguín-Espinosa, Roberto; Ortega-Cuellar, Daniel; González-Valdez, Abigail; Martínez-Rosas, Víctor; Morales-Luna, Laura; Martínez-Miranda, Josué; Sierra-Palacios, Edgar; Rocha-Ramírez, Luz María; De Franceschi, Lucia; et al. (Biochimica et biophysica acta. General subjects, 2021)
Keywords: Catalytic Domain; circular dichroism spectroscopy; Enzyme Assays; Enzyme Inhibitors - chemistry; fluorescence emission spectroscopy; Gene Expression; Glucosephosphate Dehydrogenase - antagonists & inhibitors; Glucosephosphate Dehydrogenase - chemistry; Glucosephosphate Dehydrogenase - genetics; Glucosephosphate Dehydrogenase - metabolism; HsG6PD inhibition; Humans; Inhibition type; Kinetics; Molecular docking; Molecular Docking Simulation; NADP-glucose-6-phosphate dehydrogenase; neoplasms; pentose phosphate cycle; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Stability; Protein Structure, Tertiary; reaction kinetics; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Second-order inactivation constant; Small Molecule Libraries - chemistry; Structural perturbation; Structure-Activity Relationship; Substrate Specificity; thermal stability; Thermodynamics; Inhibition type; Second-order inactivation constant; HsG6PD inhibition; Molecular docking; Structural perturbation