Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamide
about
Supersensitivity to anandamide and enhanced endogenous cannabinoid signaling in mice lacking fatty acid amide hydrolaseAnandamide and vanilloid TRPV1 receptorsMechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymesStructure-guided inhibitor design for human FAAH by interspecies active site conversionDiscovery and Characterization of a Highly Selective FAAH Inhibitor that Reduces Inflammatory PainBinding 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 HydrolaseFluoride-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 AnalgesicsDiscovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH)Rational Design of Fatty Acid Amide Hydrolase Inhibitors That Act by Covalently Bonding to Two Active Site ResiduesInhibitors of Fatty Acid Amide Hydrolase and Monoacylglycerol Lipase: New Targets for Future AntidepressantsPreclinical Characterization of the FAAH Inhibitor JNJ-42165279Fatty acid amide hydrolase as a potential therapeutic target for the treatment of pain and CNS disordersLatest advances in the discovery of fatty acid amide hydrolase inhibitorsEffects of homologues and analogues of palmitoylethanolamide upon the inactivation of the endocannabinoid anandamideEnzymatic pathways that regulate endocannabinoid signaling in the nervous systemKeys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pocketsα-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).Assessment of the pharmacology and tolerability of PF-04457845, an irreversible inhibitor of fatty acid amide hydrolase-1, in healthy subjects.Discovery libraries targeting the major enzyme classes: the serine hydrolases.Mast cells promote fibroblast populated collagen lattice contraction through gap junction intercellular communication.Control of spasticity in a multiple sclerosis model is mediated by CB1, not CB2, cannabinoid receptors.A new class of inhibitors of 2-arachidonoylglycerol hydrolysis and invasion of prostate cancer cells.Endocannabinoid modulation by FAAH and monoacylglycerol lipase within the analgesic circuitry of the periaqueductal greyThe cannabinoid system: a role in both the homeostatic and hedonic control of eating?Actions of the FAAH inhibitor URB597 in neuropathic and inflammatory chronic pain models.Chemical strategies for activity-based proteomics.The endocannabinoid system: physiology and pharmacology.α-Ketoheterocycle-based Inhibitors of Fatty Acid Amide Hydrolase (FAAH).Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates.Clickable, photoreactive inhibitors to probe the active site microenvironment of fatty acid amide hydrolase().Changes of blood endocannabinoids during anaesthesia: a special case for fatty acid amide hydrolase inhibition by propofol?New targets for neuropathic pain therapeutics.Supraspinal modulation of pain by cannabinoids: the role of GABA and glutamateComprehensive Analysis of Structure-Activity Relationships of α-Ketoheterocycles as sn-1-Diacylglycerol Lipase α InhibitorsHemodynamic profile, responsiveness to anandamide, and baroreflex sensitivity of mice lacking fatty acid amide hydrolase.Pharmacological profile of the selective FAAH inhibitor KDS-4103 (URB597).Identification of N-acylethanolamines in Dictyostelium discoideum and confirmation of their hydrolysis by fatty acid amide hydrolase.
P2860
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P2860
Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamide
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Exceptionally potent inhibitor ...... genous oleamide and anandamide
@en
type
label
Exceptionally potent inhibitor ...... genous oleamide and anandamide
@en
prefLabel
Exceptionally potent inhibitor ...... genous oleamide and anandamide
@en
P2093
P2860
P921
P356
P1476
Exceptionally potent inhibitor ...... genous oleamide and anandamide
@en
P2093
A E Lerner
B F Cravatt
B J Austin
G D Wilkie
H Miyauchi
M P Hedrick
M P Patricelli
P2860
P304
P356
10.1073/PNAS.97.10.5044
P407
P577
2000-05-01T00:00:00Z