Anshuman Dixit

TL;DR: The small molecule binding site in the Hsp90 C-terminal domain was revealed by protease fingerprinting and photoaffinity labeling utilizing LC-MS/MS and the resulting model for the bioactive conformation of NB bound to Hsp 90α is presented herein.

TL;DR: Docking studies revealed that hydrophobic interactions and hydrogen bond formation stabilize enzyme-inhibitor complex, and Benzo[d]thiazole derivatives exhibited the best inhibitory action.

TL;DR: Several Hsp90 modulators have been identified including the N-terminal ligand geldanamycin (GDA), the C-terminals ligand novobiocin (NB), and the co-chaperone disruptor celastrol as mentioned in this paper.

TL;DR: An integrated bioinformatics resource is developed, which consolidated and mapped all currently available information on genetic modifications in protein kinase genes with sequence, structure and functional data, and found that structurally conserved mutational hotspots can be shared by multiple kinases and are often enriched by cancer driver mutations with high oncogenic activity.

TL;DR: It is suggested that molecular mechanisms of activation by cancer mutations could mimic the activation process of the normal kinase, yet exploiting conserved structural catalysts to accelerate a conformational transition and the enhanced stabilization of the active kinase form.