Thioflavin S (NSC71948) interferes with Bcl-2-associated athanogene (BAG-1)-mediated protein-protein interactions.

@article{Sharp2009ThioflavinS,
  title={Thioflavin S (NSC71948) interferes with Bcl-2-associated athanogene (BAG-1)-mediated protein-protein interactions.},
  author={Adam Sharp and Simon J Crabb and Peter W. M. Johnson and Angela C. Hague and Ramsey I. Cutress and Paul A. Townsend and Aparna Ganesan and Graham Packham},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={2009},
  volume={331 2},
  pages={680-9}
}
The C-terminal BAG domain is thought to play a key role in BAG-1-induced survival and proliferation by mediating protein-protein interactions, for example, with heat shock proteins HSC70 and HSP70, and with RAF-1 kinase. Here, we have identified thioflavin S (NSC71948) as a potential small-molecule chemical inhibitor of these interactions. NSC71948 inhibited the interaction of BAG-1 and HSC70 in vitro and decreased BAG-1:HSC70 and BAG-1:HSP70 binding in intact cells. NSC71948 also reduced… CONTINUE READING

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