bi-78d3 has been researched along with Diabetes-Mellitus--Type-2* in 2 studies
2 other study(ies) available for bi-78d3 and Diabetes-Mellitus--Type-2
| Article | Year |
|---|---|
Novel compounds reducing IRS-1 serine phosphorylation for treatment of diabetes.
Activation of various interacting stress kinases, particularly the c-Jun N-terminal kinases (JNK), and a concomitant phosphorylation of insulin receptor substrate 1 (IRS-1) at serine 307 play a central role both in insulin resistance and in β-cell dysfunction. IRS-1 phosphorylation is stimulated by elevated free fatty acid levels through different pathways in obesity. A series of novel pyrido[2,3-d]pyrimidin-7-one derivatives were synthesized as potential antidiabetic agents, preventing IRS-1 phosphorylation at serine 307 in a cellular model of lipotoxicity and type 2 diabetes. Topics: Diabetes Mellitus, Type 2; HEK293 Cells; Humans; Hypoglycemic Agents; Insulin Receptor Substrate Proteins; JNK Mitogen-Activated Protein Kinases; Phosphorylation; Pyrimidines; Serine | 2016 |
Design, synthesis, and structure-activity relationship of substrate competitive, selective, and in vivo active triazole and thiadiazole inhibitors of the c-Jun N-terminal kinase.
We report comprehensive structure-activity relationship studies on a novel series of c-Jun N-terminal kinase (JNK) inhibitors. The compounds are substrate competitive inhibitors that bind to the docking site of the kinase. The reported medicinal chemistry and structure-based optimizations studies resulted in the discovery of selective and potent thiadiazole JNK inhibitors that display promising in vivo activity in mouse models of insulin insensitivity. Topics: Activating Transcription Factor 2; Animals; Binding Sites; Diabetes Mellitus, Type 2; Drug Design; HeLa Cells; Humans; Hypoglycemic Agents; Insulin Resistance; JNK Mitogen-Activated Protein Kinases; Male; Mice; Phosphorylation; Protein Binding; Structure-Activity Relationship; Substrate Specificity; Thiadiazoles; Thiazoles; Triazoles | 2009 |