gsk3235025 has been researched along with Lymphoma* in 2 studies
2 other study(ies) available for gsk3235025 and Lymphoma
| Article | Year |
|---|---|
Discovery of new potent protein arginine methyltransferase 5 (PRMT5) inhibitors by assembly of key pharmacophores from known inhibitors.
Protein arginine methyltransferase 5 (PRMT5) is an epigenetics related enzyme that has been validated as a promising therapeutic target for human cancer. Up to now, two small molecule PRMT5 inhibitors has been put into phase I clinical trial. In the present study, a series of candidate molecules were designed by combining key pharmacophores of formerly reported PRMT5 inhibitors. The in vitro PRMT5 inhibitory testing of compound 4b14 revealed an IC Topics: Antineoplastic Agents; Cell Cycle Checkpoints; Cell Line, Tumor; Cell Proliferation; Drug Design; Drug Discovery; Enzyme Inhibitors; Humans; Isoquinolines; Leukemia; Lymphoma; Molecular Docking Simulation; Molecular Dynamics Simulation; Protein-Arginine N-Methyltransferases; Structure-Activity Relationship | 2018 |
Potent, Selective, and Cell Active Protein Arginine Methyltransferase 5 (PRMT5) Inhibitor Developed by Structure-Based Virtual Screening and Hit Optimization.
PRMT5 plays important roles in diverse cellular processes and is upregulated in several human malignancies. Besides, PRMT5 has been validated as an anticancer target in mantle cell lymphoma. In this study, we found a potent and selective PRMT5 inhibitor by performing structure-based virtual screening and hit optimization. The identified compound 17 (IC Topics: Acetanilides; Antineoplastic Agents; Benzimidazoles; Cell Line; Cell Line, Tumor; Cell Proliferation; Databases, Chemical; Drug Screening Assays, Antitumor; Humans; Kinetics; Leukemia; Lymphoma; Methylation; Models, Molecular; Molecular Docking Simulation; Protein Binding; Protein-Arginine N-Methyltransferases; snRNP Core Proteins; Structure-Activity Relationship | 2017 |