scispace - formally typeset
B

Benjamin F. Cravatt

Researcher at Scripps Research Institute

Publications -  698
Citations -  69790

Benjamin F. Cravatt is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Fatty acid amide hydrolase & Anandamide. The author has an hindex of 131, co-authored 666 publications receiving 61932 citations. Previous affiliations of Benjamin F. Cravatt include Pfizer & Indiana University.

Papers
More filters
Journal ArticleDOI

Chemical genetic screen identifies Toxoplasma DJ-1 as a regulator of parasite secretion, attachment, and invasion

Carolyn I. Hall, +12 more
- 28 Jun 2011 - 
TL;DR: A screen to identify small molecules that block the process of host cell invasion by the T. gondii parasite was described and suggested that TgDJ-1 plays an important role that is likely downstream of the calcium flux required for microneme secretion, parasite motility, and subsequent invasion of host cells.
Journal ArticleDOI

Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids

Jonathan Z. Long, +7 more
- 01 Nov 2011 - 
TL;DR: A general cell-based screen for enzyme substrate discovery by untargeted metabolomics and its application to identify α/β-hydrolase domain-containing 3 (ABHD3) as a lipase that selectively cleaves medium-chain and oxidatively-truncated phospholipids is described.
Journal ArticleDOI

An endogenous sleep-inducing compound is a novel competitive inhibitor of fatty acid amide hydrolase

Matthew P. Patricelli, +3 more
- 17 Mar 1998 - 
TL;DR: The possibility that O gamma Br may be a physiological regulator of FAAH activity and fatty acid amide levels in vivo is supported and the characterization of gamma-halo beta-keto esters as powerful FAAH inhibitors near physiological pH may aid in future studies of the enzymology and biological properties of FAAh.
Journal ArticleDOI

Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase.

Matthew P. Patricelli, +1 more
- 28 Apr 2001 - 
TL;DR: The significant changes in substrate selectivity achieved by single amino acid changes suggest that FAAH possesses a rather malleable substrate binding domain and may serve, along with other AS enzymes, as a template for the engineering of amidases with novel and/or tailored specificities.
Journal ArticleDOI

Discovery and Optimization of Sulfonyl Acrylonitriles as Selective, Covalent Inhibitors of Protein Phosphatase Methylesterase-1

Daniel A. Bachovchin, +7 more
- 28 Jul 2011 - 
TL;DR: The optimized compound, 28 (AMZ30), selectively inactivates PME-1 and reduces the demethylated form of protein phosphatase 2A in living cells, providing a valuable set of pharmacological probes to study the role of methylation in regulating PP2A function.