Comment
doi: 10.1016/j.chembiol.2005.11.001.
Design of on-target FAAH inhibitors
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- PMID: 16298293
- DOI: 10.1016/j.chembiol.2005.11.001
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Comment
Design of on-target FAAH inhibitors
Chem Biol.
2005 Nov.
Abstract
In this issue of Chemistry & Biology, Alexander and Cravatt propose a model for the binding of carbamate inhibitors to fatty acid amide hydrolase (FAAH), the enzyme that breaks down signaling lipids. Using competitive activity-based protein profiling and click chemistry, they designed potent and selective FAAH inhibitors and characterized their off-target reactions.
Comment on
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Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes.Chem Biol. 2005 Nov;12(11):1179-87. doi: 10.1016/j.chembiol.2005.08.011. Chem Biol. 2005. PMID: 16298297 Free PMC article.
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