PUBLICATION
The development of highly potent inhibitors for porcupine
- Authors
- 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., and Chen, C.
- ID
- ZDB-PUB-130403-2
- Date
- 2013
- Source
- Journal of medicinal chemistry 56(6): 2700-2704 (Journal)
- Registered Authors
- Amatruda, James F., Moon, Jesung
- Keywords
- none
- MeSH Terms
-
- Drug Discovery*
- Enzyme Inhibitors/chemistry*
- Enzyme Inhibitors/pharmacology*
- Membrane Proteins/antagonists & inhibitors*
- Small Molecule Libraries/chemistry*
- Small Molecule Libraries/pharmacology*
- Structure-Activity Relationship
- PubMed
- 23477365 Full text @ J. Med. Chem.
Citation
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., and Chen, C. (2013) The development of highly potent inhibitors for porcupine. Journal of medicinal chemistry. 56(6):2700-2704.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping