EC Number   |
Inhibitors |
Structure |
|---|
   1.8.98.2 | 1,9-pyrazoloanthrone |
- |
   |
| 1.8.98.2 | 4-(((4-(4-(2-chlorophenyl)piperazin-1-yl)-6-(2,4-dihydroxy-5-isopropylphenyl)pyrimidin-2-yl)thio)methyl)benzoic acid |
LMT-328, synthesis, a derivative of Jl4, more potent inhibitor than J14. The simulation, LMT-328 shows fast stabilization and tight binding with Srx. LMT-328 has a similar binding pose as the lead compound, J14, overview |
|
| 1.8.98.2 | 4-[[[4-[4-(2-chlorophenyl)-1-piperazinyl]-6-phenyl-2-pyrimidinyl]thio]methyl]-benzoic acid |
J14, synthesis, interferes with the antioxidant activity of Srx at the molecular level. Identification of two possible inhibition mechanisms of Srx by J14. Using molecular dynamics simulations and binding free energy calculations, it is confirmed that J14 binds to the ATP binding site, J14 acts as a competitive inhibitor of ATP. J14 can serve as a protein-protein interaction inhibitor that interferes with the binding between Prx and Srx |
|
| 1.8.98.2 | more |
screening for Srx inhibitors is carried out in an automated setup using 25000 chemicals |
|
| 1.8.98.2 | more |
analysis of the inhibition mechanism of sulfiredoxin using molecular modeling and development of its inhibitors. Protein-ligand docking simulation of J14 and LMT-328, molecular dynamics simulation and binding free energy calculation, elucidation of the Srx inhibition mechanism, detailed overview |
|
| 1.8.98.2 | N-acetylcysteine |
- |
|
| 1.8.98.2 | RNAi |
- |
|
| 1.8.98.2 | siRNA |
- |
|
