Rational Design of Fatty Acid Amide Hydrolase Inhibitors that Act by Covalently Bonding to Two Active Site Residues

The design and characterization of α-ketoheterocycle fatty acid amide hydrolase (FAAH) inhibitors are disclosed that additionally and irreversibly target a cysteine (Cys269) found in the enzyme cytosolic port while maintaining the reversible covalent Ser241 attachment responsible for their rapid and...

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Bibliographische Detailangaben
Hauptverfasser: Otrubova, Katerina, Brown, Monica, McCormick, Michael S., Han, Gye W., O’Neal, Scott T., Cravatt, Benjamin F., Stevens, Raymond C., Lichtman, Aron H., Boger, Dale L.
Format: Artigo
Sprache:Inglês
Veröffentlicht: 2013
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Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3678763/
https://ncbi.nlm.nih.gov/pubmed/23581831
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja4014997
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