The development of highly potent inhibitors for porcupine

Xiaolei Wang, Jesung Moon, Michael E. Dodge, Xinchao Pan, Lishu Zhang, Jordan M. Hanson, Rubina Tuladhar, Zhiqiang Ma, Heping Shi, Noelle S. Williams, James F. Amatruda, Thomas J. Carroll, Lawrence Lum, Chuo Chen

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2700-2704
Number of pages5
JournalJournal of Medicinal Chemistry
Volume56
Issue number6
DOIs
StatePublished - Mar 28 2013

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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    Wang, X., Moon, J., Dodge, M. E., Pan, X., Zhang, L., Hanson, J. M., Tuladhar, R., Ma, Z., Shi, H., Williams, N. S., Amatruda, J. F., Carroll, T. J., Lum, L., & Chen, C. (2013). The development of highly potent inhibitors for porcupine. Journal of Medicinal Chemistry, 56(6), 2700-2704. https://doi.org/10.1021/jm400159c