Structure-guided inhibitor design for human FAAH by interspecies active site conversion - Test2 - elhamkhani - TriplyDB

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

http://www.wikidata.org/entity/Q27651822

about

sameAs

Marijuana, Spice 'herbal high', and early neural development: implications for rescheduling and legalization Discovery and Characterization of a Highly Selective FAAH Inhibitor that Reduces Inflammatory Pain Binding and Inactivation Mechanism of a Humanized Fatty Acid Amide Hydrolase by α-Ketoheterocycle Inhibitors Revealed from Cocrystal Structures X-ray Crystallographic Analysis of α-Ketoheterocycle Inhibitors Bound to a Humanized Variant of Fatty Acid Amide Hydrolase Crystal Structure of Fatty Acid Amide Hydrolase Bound to the Carbamate Inhibitor URB597: Discovery of a Deacylating Water Molecule and Insight into Enzyme Inactivation Fluoride-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 Hydrolase Reversible Competitive α-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Constraints in the Acyl Side Chain: Orally Active, Long-Acting Analgesics Discovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH)A Binding Site for Nonsteroidal Anti-inflammatory Drugs in Fatty Acid Amide Hydrolase Rational Design of Fatty Acid Amide Hydrolase Inhibitors That Act by Covalently Bonding to Two Active Site Residues Structure-Based Design of Irreversible Human KAT II Inhibitors: Discovery of New Potency-Enhancing Interactions Preclinical Characterization of the FAAH Inhibitor JNJ-42165279 Fatty acid amide hydrolase as a potential therapeutic target for the treatment of pain and CNS disorders Latest advances in the discovery of fatty acid amide hydrolase inhibitors Biochemical and mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase inhibition Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets Approximating protein flexibility through dynamic pharmacophore models: application to fatty acid amide hydrolase (FAAH)Biology-inspired microphysiological system approaches to solve the prediction dilemma of substance testing Strategies for discovering and derisking covalent, irreversible enzyme inhibitors.The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH).Discovery libraries targeting the major enzyme classes: the serine hydrolases.Discovery of MK-4409, a Novel Oxazole FAAH Inhibitor for the Treatment of Inflammatory and Neuropathic Pain.Mechanistic and pharmacological characterization of PF-04457845: a highly potent and selective fatty acid amide hydrolase inhibitor that reduces inflammatory and noninflammatory pain Discovery of PF-04457845: A Highly Potent, Orally Bioavailable, and Selective Urea FAAH Inhibitor.Fatty acid-binding proteins (FABPs) are intracellular carriers for Δ9-tetrahydrocannabinol (THC) and cannabidiol (CBD).Interaction of the N-(3-Methylpyridin-2-yl)amide Derivatives of Flurbiprofen and Ibuprofen with FAAH: Enantiomeric Selectivity and Binding Mode Luciferin Amides Enable in Vivo Bioluminescence Detection of Endogenous Fatty Acid Amide Hydrolase Activity.Clickable, photoreactive inhibitors to probe the active site microenvironment of fatty acid amide hydrolase().The synthesis and in vivo evaluation of [18F]PF-9811: a novel PET ligand for imaging brain fatty acid amide hydrolase (FAAH).A Personal Retrospective: Elevating Anandamide (AEA) by Targeting Fatty Acid Amide Hydrolase (FAAH) and the Fatty Acid Binding Proteins (FABPs).Measuring endocannabinoid hydrolysis: refining our tools and understanding Design, synthesis, and characterization of α-ketoheterocycles that additionally target the cytosolic port Cys269 of fatty acid amide hydrolase Synthesis of phenoxyacyl-ethanolamides and their effects on fatty acid amide hydrolase activity.Drug discovery for a new generation of covalent drugs.Recent advances in the discovery and evaluation of fatty acid amide hydrolase inhibitors.Membrane lipids are key modulators of the endocannabinoid-hydrolase FAAH.Fluorine NMR-based screening on cell membrane extracts.Application of EMBM to Structure-Based Design of Warheads for Protease Inhibitors.The endocannabinoid system in the baboon (Papio spp.) as a complex framework for developmental pharmacology.Aryl Piperazinyl Ureas as Inhibitors of Fatty Acid Amide Hydrolase (FAAH) in Rat, Dog, and Primate.

P2860

2d60fc47e685c78255e6068adb2e5d5571e245cd

P248

Q27009287-ADCC8C72-89FE-403B-80CA-D50C2A95C238 Q27655121-30B75652-4DAC-46F7-B7BF-78867B60BCF3 Q27657268-B79E641D-F0E6-465E-BA7D-22E33BCC319A Q27658264-703192FC-1CB2-4954-BC64-063F99B0AEE0 Q27661834-C745D5D8-C721-42FB-8EE8-1B3EC38704C4 Q27667078-027FB58B-51BA-4E68-89C4-E698F4BFBA8F Q27667312-C7C881E4-3CF1-468C-B2D2-7E85ED92BDD7 Q27667550-CB4F84F2-3F8C-41A1-97F8-DE83E4F5A427 Q27675504-8230A4A9-611C-4993-A49B-35DC9CB2EA8F Q27677344-251CB331-5311-44C4-951D-374E80D4DB25 Q27684159-9C8AC532-86CC-4115-B605-6A08A99DCDE1 Q28271553-61BF4147-C963-47F4-AC07-503AFC39D4CA Q28285103-AEDFB667-5F6C-484A-A722-23B1A031C3EF Q28287173-F568E562-CB59-4548-80B6-1A4C5408D3FB Q28483214-B0F0E638-FC8D-4E27-9B1E-B5B09CC4B588 Q28548681-1E150D21-BF68-4C7B-8BC9-F62E25D24E20 Q28740837-A3D864CD-82B1-4905-82F6-143DF774F597 Q30358385-F68E8A69-AAF1-4C51-A155-86C8031B11AD Q34023143-9D2903DF-06EC-49CB-B158-3D4A8C35DFE2 Q34027721-DE3B4EA4-D11B-46FA-A45F-C6678BF14E50 Q34036280-764B4322-7B80-435D-B05A-47BAC6650E58 Q34041284-B06C86DD-AA39-4FA1-B270-C10CE2E54D31 Q34179408-6AEB7962-AC6A-40CD-B24B-41439CBB8B2D Q34191995-21D43927-5D70-4FDD-95DF-F1AA4B507B1A Q34461976-4E0F6DA4-BE01-462A-A8EC-A1DA4FE73E0A Q35840682-67BA6078-F05B-4E39-87C2-8EA9F7AEAE9A Q35866385-ECDCC5DC-33B4-43DF-91A5-E2C2533584B2 Q36041846-B276E154-1C8A-43D0-9F1B-D0062DA407FC Q36727793-9AA9C451-FDD8-4F90-A23F-F13217FA5261 Q37335452-0D282D67-F3FC-494B-A74F-C85D585C3E49 Q37474536-73F7620D-1886-4065-AC27-53ADF31F704E Q37613654-6150DB6E-8E72-4FE7-8EBD-77991E979926 Q37691667-9317BBDB-7611-42B8-A4DA-D9FFA4D224E9 Q38011256-3E54E826-F998-4D74-A7B8-1CE7CFA7733A Q38028659-471A8159-5681-469E-A146-E3E4FF5687D8 Q39064688-D73C2C53-1BDF-409E-AE2B-4FD0EDC05059 Q39294587-90947C13-E221-4B53-94D6-7881F35A4105 Q39531847-C402EF2F-6B24-41AA-8C4C-78C16DE469D3 Q39666956-AAE6EF71-7F71-4CE7-8308-966461D4D62E Q39736130-34B86012-6ED2-4ABC-9302-95FE9814AD75

P2860

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

http://www.wikidata.org/entity/Q27651822

description

2008 nî lūn-bûn

@nan

2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@ast

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@en

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@nl

type

label

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@ast

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@en

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@nl

prefLabel

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@ast

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@en

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@nl

P1433

Q27651822-85114C93-2BEE-43EA-93A6-3C73336C0580

P1476

Q27651822-0ABA7986-5ABB-44BE-ACF1-02647ED41E86

P2093

Q27651822-1D44BDFE-82C4-4BAA-8658-F7F18BC454FC

Q27651822-2AE6B14E-2518-4CBF-B3A0-7B3D5AB1870B

Q27651822-3BB33615-3112-4482-8283-FB2C9D603A33

Q27651822-554A52C1-16F3-43CD-A7F8-34E7F45CD7D2

Q27651822-61EB30D4-BCCE-472D-8370-8A7E2B30982A

Q27651822-74B5A3DB-2247-46E7-BF65-85D30283B4FD

Q27651822-A9DE86F2-BAE8-46B7-A3BB-AD947C6BBFC8

Q27651822-DE5C766A-C3A8-49E9-BF6A-311B52DFD6DD

Q27651822-E52BCDE1-B50F-4BF4-9D0D-8C1F16A9AC37

Q27651822-F75F37A1-CF60-41D4-9A25-628C9062A23E

P2860

Q27651822-10BDE847-4FA8-41F9-A6A2-F06759BB340C

Q27651822-12F2BE08-B111-467C-94DF-43B8BEF9B3F4

Q27651822-1BD8946A-5627-46E0-A083-6739AC6D6858

Q27651822-1DD5D031-D1DB-48F1-A9EC-34984E0C2CDD

Q27651822-223A54F8-F54B-4085-8FCF-B87E4C48A7CF

Q27651822-291B8D23-6649-4425-B809-BF6EA683404A

Q27651822-2E7A1565-7EA9-4288-AA34-8AF5A9FD8094

Q27651822-3903CAD0-F3DB-4F8C-960B-6071ED2CF396

Q27651822-3CB9574D-AC4A-4AD6-A6E4-F1F6D5A57A82

Q27651822-3DBC8045-B152-45EF-A2AC-91AE48A3D6AD

P304

Q27651822-E26D8297-6E19-4F51-99E4-8EB6B6513B64

P31

Q27651822-46A46536-BA62-45A9-8054-B8309B5961B4

P3181

Q27651822-B8DAAA20-9F6B-422C-B564-9017ACBFB126

P356

Q27651822-B19F2A06-362C-4A27-886C-AE73250AF4D7

P407

Q27651822-8F0F20E0-D100-4B7D-A4BC-4C996E02CDC9

P433

Q27651822-2681C0D4-D053-4170-957D-AB94146335D6

P478

Q27651822-9F6C954A-76A9-49B4-B9CA-10C65A67E913

P50

Q27651822-0E005279-7054-4264-B1EB-7C33C90BAF87

Q27651822-85EA5CED-BA23-4803-B17C-064CD4F704F5

P577

Q27651822-6CFF4054-5580-4458-9BF5-80B6E2C7098C

P5875

Q27651822-088A05F2-44A2-4160-B869-A2A88972B56B

P698

Q27651822-488C9DA8-F17A-45FB-9AD7-734E0705CE81

P932

Q27651822-EEDF15D1-FDC2-4191-8924-3CABF3B6B01E

P3181

P356

PNAS.0806121105

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

@en

P2093

Brandon Pabst

http://www.w3.org/2001/XMLSchema#string

Daniel S Everdeen

http://www.w3.org/2001/XMLSchema#string

Douglas S Johnson

http://www.w3.org/2001/XMLSchema#string

Kay Ahn

http://www.w3.org/2001/XMLSchema#string

Keshab Bhattacharya

http://www.w3.org/2001/XMLSchema#string

Mauro Mileni

http://www.w3.org/2001/XMLSchema#string

Raymond C Stevens

http://www.w3.org/2001/XMLSchema#string

Richard A Nugent

http://www.w3.org/2001/XMLSchema#string

Satwik Kamtekar

http://www.w3.org/2001/XMLSchema#string

Zhigang Wang

http://www.w3.org/2001/XMLSchema#string

P2860

Development of highly sensitive fluorescent assays for fatty acid amide hydrolase

Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature

Supersensitivity to anandamide and enhanced endogenous cannabinoid signaling in mice lacking fatty acid amide hydrolase

Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes

Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling

Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity

Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides

The fatty acid amide hydrolase inhibitor URB597 (cyclohexylcarbamic acid 3'-carbamoylbiphenyl-3-yl ester) reduces neuropathic pain after oral administration in mice

Chemical characterization of a family of brain lipids that induce sleep

Methyl arachidonyl fluorophosphonate: a potent irreversible inhibitor of anandamide amidase

P304

12820-4

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2991193

http://www.w3.org/2001/XMLSchema#string

P356

10.1073/PNAS.0806121105

http://www.w3.org/2001/XMLSchema#string

P407

P433

35

http://www.w3.org/2001/XMLSchema#string

P478

105

http://www.w3.org/2001/XMLSchema#string

P50

Benjamin Cravatt III

P577

2008-09-02T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

23220099

http://www.w3.org/2001/XMLSchema#string

P698

18753625

http://www.w3.org/2001/XMLSchema#string

P932

2529035

http://www.w3.org/2001/XMLSchema#string