Binding and Inactivation Mechanism of a Humanized Fatty Acid Amide Hydrolase by α-Ketoheterocycle Inhibitors Revealed from Cocrystal Structures-Reference-Cited by-同舟云学术

Binding and Inactivation Mechanism of a Humanized Fatty Acid Amide Hydrolase by α-Ketoheterocycle Inhibitors Revealed from Cocrystal Structures

Published:2009-07-08 Issue:30 Volume:131 Page:10497-10506
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Mileni Mauro¹,Garfunkle Joie¹,DeMartino Jessica K.¹,Cravatt Benjamin F.¹,Boger Dale L.¹,Stevens Raymond C.¹

Affiliation:

1. Departments of Molecular Biology, Chemistry, and Chemical Physiology, and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja902694n

Reference56 articles.

1. Isolation and Structure of a Brain Constituent That Binds to the Cannabinoid Receptor

2. 2-Arachidonoylgylcerol: A Possible Endogenous Cannabinoid Receptor Ligand in Brain

3. Control of pain initiation by endogenous cannabinoids

4. Fatty Acid Amide Hydrolase: From Characterization to Therapeutics

5. Cannabinoid Drugs and Enhancement of Endocannabinoid Responses: Strategies for a Wide Array of Disease States

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