Chemical characterization of a family of brain lipids that induce sleep
about
Cannabinoid-hypocretin cross-talk in the central nervous system: what we know so farMolecular characterization of human and mouse fatty acid amide hydrolasesStructure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in natureSupersensitivity to anandamide and enhanced endogenous cannabinoid signaling in mice lacking fatty acid amide hydrolaseA hypothesis about the endogenous analogue of general anesthesiaThe endocannabinoid system as an emerging target of pharmacotherapyMechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymesAn adaptogenic role for omega-3 fatty acids in stress; a randomised placebo controlled double blind intervention study (pilot) [ISRCTN22569553]Lipidomic Analysis of Endocannabinoid Signaling: Targeted Metabolite Identification and QuantificationChemical probes of endocannabinoid metabolismCannabinoids as therapeutic agents in cancer: current status and future implicationsAmygdala FAAH and anandamide: mediating protection and recovery from stressStructure-guided inhibitor design for human FAAH by interspecies active site conversionBinding 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 ResiduesEndozepinesFatty 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 inhibitorsEnzymatic pathways that regulate endocannabinoid signaling in the nervous systemSimultaneously hermaphroditic shrimp use lipophilic cuticular hydrocarbons as contact sex pheromonesEvidence of high expression of peptidylglycine alpha-amidating monooxygenase in the rat uterus: estrogen regulationLiquid chromatography quadrupole time-of-flight mass spectrometry characterization of metabolites guided by the METLIN databaseEffect of social isolation on CB1 and D2 receptor and fatty acid amide hydrolase expression in rats.The extended phenotypes of marine symbioses: ecological and evolutionary consequences of intraspecific genetic diversity in coral-algal associations.Mass spectrometry techniques in the survey of steroid metabolites as potential disease biomarkers: a review.Drosophila melanogaster as a model system to study long-chain fatty acid amide metabolism.α-Ketoheterocycle inhibitors of fatty acid amide hydrolase: exploration of conformational constraints in the acyl side chain.Unique allosteric regulation of 5-hydroxytryptamine receptor-mediated signal transduction by oleamide.Evaluation and evidence of natural gangliosides with two unsaturated bonds in the ceramide structure obtained by a combination of MALDI-MS and NMR spectroscopy.The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH).Discovery libraries targeting the major enzyme classes: the serine hydrolases.Anticonvulsant activity of N-palmitoylethanolamide, a putative endocannabinoid, in mice.Mechanistic and pharmacological characterization of PF-04457845: a highly potent and selective fatty acid amide hydrolase inhibitor that reduces inflammatory and noninflammatory painNo hypothermic response to serotonin in 5-HT7 receptor knockout mice.Functional disassociation of the central and peripheral fatty acid amide signaling systems.Sulfonyl fluoride inhibitors of fatty acid amide hydrolase.
P2860
Q21090468-BF460F8E-6930-4CF9-85B0-E91DFD38F88DQ24317261-B913348A-8BC4-4680-A031-6E5E2BBB4B1EQ24536561-6936FB8C-F668-4743-9FFC-AB13A2FF6D4DQ24555807-42B5BBCF-EE5C-4FF9-A8D1-6708EFF44D57Q24601737-35543355-43FB-47EF-9936-39AB1C6F0792Q24648473-3EE743BA-3C6E-44F9-BCBE-80D3529D2960Q24680869-9C58024A-E6EC-4C65-9F37-F8A7A4A91922Q24808700-D994B5B7-20DA-496F-A292-E4F14EB655F2Q26769959-82030454-2806-4648-A66F-71390F1C7AD3Q26863202-F179D789-D57A-47CF-B1A7-19CD89860C9CQ26866298-F2DEB2C2-ACB2-4813-9BA9-C16D122BDCABQ27026443-84160834-0A06-438A-8274-93AF961376F6Q27651822-B4BC7E40-2351-4F9B-A854-25B73F5E73C7Q27657268-042E2D81-312E-443D-94FC-143B2E918137Q27658264-FC0591D7-A91A-4379-8762-4DB9C1E4D89FQ27667078-61D3C703-EB11-43B1-A929-0D4DDEE1412AQ27667312-FF041C00-BFB5-44EE-ADDD-BB1165D45E20Q27667550-1DB6D4F9-768F-4DC0-B825-95DC11FFA489Q27677344-4D0B2085-EAF2-488C-B262-E1FB9BDAC78DQ28082983-48CB0C89-66DB-49FC-926B-9307C9579076Q28285103-A33BD6C3-8D9E-4A11-B02B-BC91F0FA5BEBQ28287173-6EA6F0D8-7E05-4ECA-A3BE-4D12A962E29FQ28390932-B7703B18-BCFB-4FC8-B331-39CB0345D333Q28477832-0B83E750-EBE8-41EE-9917-0541A16479B9Q28582376-BAC52AFB-207A-49D7-870A-4E93520B808EQ28686521-B8993604-56F3-404C-AB48-3B1938F963B2Q30489165-657660B3-9104-4BEA-9FDD-74810CCB5799Q30848939-C553E5AB-1F3E-4C8B-8903-88241C496F68Q33457880-9A813B49-0A42-4435-9F80-B2E8920CD61EQ33622202-36CD3042-F5B3-48AB-98D7-8FF56A38182AQ33644120-39630589-C838-4854-B377-A097E25E4AF3Q33748149-049FC0F9-96CA-439E-9B0C-E6CB075215AAQ33890989-2A269712-EDC6-4FA7-9753-B484BCE181A5Q34027721-6C83E8F2-2112-4940-99A3-E92CB832DBC3Q34036280-7B5FB144-737C-46C1-A018-B19459DD0A2EQ34083248-578ED6C0-6936-4CB2-AF0D-B64A14666B23Q34179408-60599DC3-29ED-4D29-827D-16C3EC8476B6Q34331037-E1148DAC-B03F-400E-AAA5-F529AAFE7B0CQ34332678-4BEC3A4B-C379-4E7F-A54F-F1487A48D5DAQ34452685-4EB15C3A-AC2B-4D64-9C0B-DC261C64E62A
P2860
Chemical characterization of a family of brain lipids that induce sleep
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Chemical characterization of a family of brain lipids that induce sleep
@ast
Chemical characterization of a family of brain lipids that induce sleep
@en
Chemical characterization of a family of brain lipids that induce sleep
@nl
type
label
Chemical characterization of a family of brain lipids that induce sleep
@ast
Chemical characterization of a family of brain lipids that induce sleep
@en
Chemical characterization of a family of brain lipids that induce sleep
@nl
prefLabel
Chemical characterization of a family of brain lipids that induce sleep
@ast
Chemical characterization of a family of brain lipids that induce sleep
@en
Chemical characterization of a family of brain lipids that induce sleep
@nl
P2093
P921
P3181
P356
P1433
P1476
Chemical characterization of a family of brain lipids that induce sleep
@en
P2093
B F Cravatt
N B Gilula
O Prospero-Garcia
R A Lerner
S J Henriksen
P304
P3181
P356
10.1126/SCIENCE.7770779
P407
P577
1995-06-09T00:00:00Z