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http://hub.abes.fr/acs/periodical/joceah/1994/volume_59/issue_17/101021jo00096a064/authorship/3
http://hub.abes.fr/acs/periodical/jmcmar/2007/volume_50/issue_5/101021jm0611509/authorship/10
http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_51/101021bi0349569/authorship/4
http://hub.abes.fr/acs/periodical/chreay/2006/volume_106/issue_8/101021cr050288g/authorship/2
http://hub.abes.fr/acs/periodical/crtoec/2006/volume_19/issue_9/101021tx060117m/authorship/5
http://hub.abes.fr/bmj/periodical/ard/2012/volume_71/issue_12/B3506C23F2014C7BE053120B220AB6A2/authorship/8
http://hub.abes.fr/oup/periodical/hmg/2004/volume_13/issue_18/101093hmgddh216/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2006/volume_45/issue_15/101021bi060163l/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2007/volume_46/issue_45/101021bi701378g/authorship/11
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_51/101021ja0779506/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_28/101021ja0532842/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2006/volume_45/issue_38/101021bi061122s/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2008/volume_47/issue_12/101021bi702530z/authorship/4
http://hub.abes.fr/acs/periodical/jmcmar/2005/volume_48/issue_6/101021jm049614v/authorship/13
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http://hub.abes.fr/acs/periodical/jacsat/2006/volume_128/issue_30/101021ja062999h/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_7/101021ja074138u/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_5/101021ja038441g/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_20/101021bi002578r/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_11/101021ja0506915/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_23/101021ja0724083/authorship/6
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_31/101021ja073650c/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2008/volume_47/issue_51/101021bi801786y/authorship/8
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_16/101021ja034490h/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2006/volume_45/issue_30/101021bi0608010/authorship/2
http://hub.abes.fr/acs/periodical/chreay/2008/volume_108/issue_5/101021cr0782067/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_45/101021bi0480335/authorship/6
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http://hub.abes.fr/acs/periodical/jmcmar/2007/volume_50/issue_14/101021jm061414r/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/1994/volume_116/issue_13/101021ja00092a080/authorship/1
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The Putative Endocannabinoid Transport Blocker LY2183240Is a Potent Inhibitor of FAAH and Several Other Brain SerineHydrolases
Characterization and Manipulation of the Acyl Chain Selectivity of Fatty AcidAmide Hydrolase
Mapping Enzyme Active Sites in Complex Proteomes
Inactivation of N-Acyl Phosphatidylethanolamine Phospholipase D Reveals MultipleMechanisms for the Biosynthesis of Endocannabinoids
Functional Proteomic and Structural Insights into Molecular Recognition in the Nitrilase Family Enzymes
Activity-Based Protein Profiling in Vivo Using a Copper(I)-CatalyzedAzide-Alkyne [3 + 2] Cycloaddition
Microarray Platform for Profiling Enzyme Activities in Complex Proteomes
Recombinant Expression, Purification, and Comparative Characterization of TorsinAand Its Torsion Dystonia-Associated Variant ΔE-TorsinA
Comparison of Anandamide Transport in FAAH Wild-Type and KnockoutNeurons: Evidence for Contributions by both FAAH and the CB1 Receptor toAnandamide Uptake
Mechanism-Based Profiling of Enzyme Families
Profiling Serine Hydrolase Activities in Complex Proteomes
Assignment of Endogenous Substrates to Enzymes by Global Metabolite Profiling
A FAAH-Regulated Class of N-Acyl Taurines That Activates TRP Ion Channels
Structure-Based Design of a FAAH Variant That Discriminates between the N-AcylEthanolamine and Taurine Families of Signaling Lipids
Novel Mechanistic Class of Fatty Acid Amide Hydrolase Inhibitors withRemarkable Selectivity
Reduced cellular expression and activity of the P129T mutant of human fatty acid amide hydrolase: evidence for a link between defects in the endocannabinoid system and problem drug use
Enzymatic Pathways That Regulate Endocannabinoid Signaling in the Nervous System
Microarray Platform for Profiling Enzyme Activities inComplex Proteomes [J. Am. Chem. Soc. 2004, 126,15640−15641].
Endocannabinoid Metabolism in the Absence of Fatty Acid Amide Hydrolase(FAAH): Discovery of Phosphorylcholine Derivatives of N-Acyl Ethanolamines
A Tandem Orthogonal Proteolysis Strategy for High-Content ChemicalProteomics
A Functional Proteomic Strategy to Discover Inhibitors for UncharacterizedHydrolases
Potent and Selective α-Ketoheterocycle-Based Inhibitors of the Anandamide and OleamideCatabolizing Enzyme, Fatty Acid Amide Hydrolase
Hydrolysis of Prostaglandin Glycerol Esters by the Endocannabinoid-HydrolyzingEnzymes, Monoacylglycerol Lipase and Fatty Acid Amide Hydrolase
Oxidative Metabolism of a Fatty Acid Amide Hydrolase-Regulated Lipid, Arachidonoyltaurine
Enrichment Tags for Enhanced-Resolution Profiling of the Polar Metabolome
Discovery of a Potent, Selective, and Efficacious Class of Reversibleα-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Effective asAnalgesics
Escherichia coli Signal Peptide Peptidase A Is a Serine-Lysine Protease with a Lysine Recruited to the Nonconserved Amino-Terminal Domain in the S49 Protease Family
Serine Hydrolase KIAA1363: Toxicological and Structural Featureswith Emphasis on Organophosphate Interactions
Tailored Glycoproteomics and Glycan Site Mapping UsingSaccharide-Selective Bioorthogonal Probes
Optimization of Activity-Based Probes for Proteomic Profilingof Histone Deacetylase Complexes
Structure−Activity Relationships of α-Ketooxazole Inhibitors of Fatty Acid Amide Hydrolase
Crossing Extreme Mechanistic Barriers by Antibody Catalysis: Syn Elimination to a Cis Olefin
Synthesis of a Functionalized Rigid Bicyclo[2.2.1]heptane: A Useful Hapten for Eliciting Catalytic Antibodies
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