Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism
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Brain monoglyceride lipase participating in endocannabinoid inactivationChemical probes of endocannabinoid metabolismBinding and Inactivation Mechanism of a Humanized Fatty Acid Amide Hydrolase by α-Ketoheterocycle Inhibitors Revealed from Cocrystal StructuresX-ray Crystallographic Analysis of α-Ketoheterocycle Inhibitors Bound to a Humanized Variant of Fatty Acid Amide HydrolaseCrystal Structure of Fatty Acid Amide Hydrolase Bound to the Carbamate Inhibitor URB597: Discovery of a Deacylating Water Molecule and Insight into Enzyme InactivationFluoride-Mediated Capture of a Noncovalent Bound State of a Reversible Covalent Enzyme Inhibitor: X-ray Crystallographic Analysis of an Exceptionally Potent α-Ketoheterocycle Inhibitor of Fatty Acid Amide HydrolaseReversible Competitive α-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Constraints in the Acyl Side Chain: Orally Active, Long-Acting AnalgesicsRational Design of Fatty Acid Amide Hydrolase Inhibitors That Act by Covalently Bonding to Two Active Site ResiduesFatty acid amide hydrolase as a potential therapeutic target for the treatment of pain and CNS disordersUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationEnzymatic pathways that regulate endocannabinoid signaling in the nervous systemEvidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolaseα-Ketoheterocycle inhibitors of fatty acid amide hydrolase: exploration of conformational constraints in the acyl side chain.The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH).Discovery libraries targeting the major enzyme classes: the serine hydrolases.Discovery of PF-04457845: A Highly Potent, Orally Bioavailable, and Selective Urea FAAH Inhibitor.Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633.A catalytically silent FAAH-1 variant drives anandamide transport in neurons.Luciferin Amides Enable in Vivo Bioluminescence Detection of Endogenous Fatty Acid Amide Hydrolase Activity.α-Ketoheterocycle-based Inhibitors of Fatty Acid Amide Hydrolase (FAAH).A facile hybrid 'flow and batch' access to substituted 3,4-dihydro-2H-benzo[b][1,4]oxazinones.Activity-based protein profiling: the serine hydrolasesDiscovery of a potent, selective, and efficacious class of reversible alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase effective as analgesicsPotent and selective alpha-ketoheterocycle-based inhibitors of the anandamide and oleamide catabolizing enzyme, fatty acid amide hydrolaseStructure-activity relationships of alpha-ketooxazole inhibitors of fatty acid amide hydrolaseOptimization of the central heterocycle of alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase.Therapeutic potential of endocannabinoid-hydrolysing enzyme inhibitors.Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamideOptimization of alpha-ketooxazole inhibitors of fatty acid amide hydrolase.Design, synthesis, and characterization of α-ketoheterocycles that additionally target the cytosolic port Cys269 of fatty acid amide hydrolaseFatty acid amide signaling molecules.Recent advances in the discovery and evaluation of fatty acid amide hydrolase inhibitors.N-Acylethanolamines: lipid metabolites with functions in plant growth and development.Endocannabinoid signaling and its regulation by nutrients.Directed evolution of Pseudomonas aeruginosa lipase for improved amide-hydrolyzing activity.Improving the antitumor activity of squalenoyl-paclitaxel conjugate nanoassemblies by manipulating the linker between paclitaxel and squalene.Aryl Piperazinyl Ureas as Inhibitors of Fatty Acid Amide Hydrolase (FAAH) in Rat, Dog, and Primate.Oxidation of endogenous N-arachidonoylserotonin by human cytochrome P450 2U1.Clarifying the catalytic roles of conserved residues in the amidase signature family.Mutations in Arabidopsis fatty acid amide hydrolase reveal that catalytic activity influences growth but not sensitivity to abscisic acid or pathogens.
P2860
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P2860
Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@ast
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@en
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@nl
type
label
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@ast
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@en
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@nl
prefLabel
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@ast
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@en
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@nl
P356
P1433
P1476
Fatty acid amide hydrolase com ...... nventional catalytic mechanism
@en
P2093
B F Cravatt
M P Patricelli
P304
P356
10.1021/BI991876P
P407
P577
1999-10-26T00:00:00Z