The development of highly potent inhibitors for porcupine.


Porcupine is a member of the membrane-bound O-acyltransferase family of proteins. It catalyzes the palmitoylation of Wnt proteins, a process required for their secretion and activity. We recently disclosed a class of small molecules (IWPs) as the first reported Porcn inhibitors. We now describe the structure-activity relationship studies and the identification of subnanomolar inhibitors. We also report herein the effects of IWPs on Wnt-dependent developmental processes, including zebrafish posterior axis formation and kidney tubule formation.

DOI: 10.1021/jm400159c
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@article{Wang2013TheDO, title={The development of highly potent inhibitors for porcupine.}, author={Xu Wang and Jesung Moon and Michael E. Dodge and Xinchao Pan and Lishu Zhang and Jordan M Hanson and Rubina Tuladhar and Zhiqiang Ma and He Shi and Noelle Sevilir Williams and James F. Amatruda and Thomas J Carroll and Lawrence Lum and Chuo Chen}, journal={Journal of medicinal chemistry}, year={2013}, volume={56 6}, pages={2700-4} }