Publications by authors named "V G Upadhyay"
Inspired by our previous efforts in the semisynthetic modification of naturally occurring pyranoacridones, we report the targeted design and semisynthesis of dual inhibitors of HDAC and topoisomerase II α (Topo II α) derived from des--methylacronycine () and noracronycine () pyranoacridone alkaloids. Designed from the clinically approved SAHA, the cytotoxic pyranoacridone nuclei from the alkaloids served as the capping group, while a hydroxamic acid moiety functioned as the zinc-binding group. Out of 16 compounds evaluated in an cytotoxicity assay, KT32 () with noracronycine () as the capping group and five-carbon linker hydroxamic acid side chains showed good cytotoxic activity with IC values of 1.
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- The text discusses a new method for activating distal C-H bonds to create benzofulvenes, which are compounds formed through a [3 + 2] reaction involving palladium catalysis, overcoming traditional bond activation challenges.
- This innovative approach involves concurrent activation of both β-C(benzylic)-H and δ-C(aryl)-H bonds and leads to the formation of novel chemical entities with promising anticancer properties.
- In studies, these new compounds were found to effectively target oral squamous cell carcinoma (OSCC) by arresting the cell cycle at the S-phase and activating various apoptosis pathways, indicating their potential as effective chemotherapy options.
Despite extensive research, strategies to effectively combat breast cancer stemness and achieve a definitive cure remains elusive. CD44, a well-defined cancer stem cell (CSC) marker is reported to promote breast cancer tumorigenesis, metastasis, and chemoresistance. However, mechanisms leading to its enhanced expression and function is poorly understood.
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- Duchenne muscular dystrophy (DMD) is caused by a mutation in the dystrophin gene, leading to a lack of functional dystrophin protein, resulting in muscle degeneration, and although some targeted therapies exist, they have limited effectiveness and are expensive.
- The structure and function of the C-terminal (CT) domain of dystrophin, which interacts with dystrobrevin to stabilize muscle cell membranes, are not well understood, posing challenges for treatment development.
- Research indicates that the CT domain is non-globular and interacts differently with two isoforms of dystrobrevin, revealing how variations in their amino acid composition can affect the stability of the dystrophin-associated glycoprotein