Structure and function of fatty acid amide hydrolase.

By Michele K. McKinney, B. Cravatt. Annual Review of Biochemistry, 2005

658 citations recorded by the source corpus.

Subfields: Molecular Biology, Pharmacology, Surgery

View Paper: https://www.semanticscholar.org/paper/01578d96f165df8a83b155c534979c8fe6bbad81

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. B. Cravatt
2. G. Simon

In Pharmacology

1. B. Cravatt
2. P. Pacher
3. S. Batkai
4. George Kunos
5. G. Simon
6. Jacqueline L. Blankman

In Surgery

1. B. Cravatt
2. P. Pacher
3. S. Batkai
4. George Kunos

Citations in the corpus

• A Comprehensive Profile of Brain Enzymes that Hydrolyze the Endocannabinoid 2‐Arachidonoylglycerol (2007, background): “The hydrolysis of AEA to arachidonic acid and ethanolamine (Figure 1) is principally mediated by a single enzyme in the nervous system—the integral membrane enzyme fatty acid amide hydrolase (FAAH) [11, 12].”
• The Endocannabinoid System as an Emerging Target of Pharmacotherapy (2006, background): “In contrast to the unsettled status of anandamide transport and a putative transporter protein, the unique role of FAAH in the in vivo degradation of anandamide has been extensively documented (reviewed in McKinney and Cravatt, 2005).”