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Volumn 62, Issue , 2001, Pages 95-131

Proteins regulating the biosynthesis and inactivation of neuromodulatory fatty acid amides

Author keywords

[No Author keywords available]

Indexed keywords

AGENTS INTERACTING WITH TRANSMITTER, HORMONE OR DRUG RECEPTORS; AMIDASE; AMIDE; ENDOCANNABINOID; ETHANOLAMINE DERIVATIVE; FATTY ACID; FATTY ACID AMIDASE; FATTY-ACID AMIDE HYDROLASE; N ACYLETHANOLAMINES; N-ACYLETHANOLAMINES;

EID: 0035235117     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0083-6729(01)62002-8     Document Type: Review
Times cited : (78)

References (132)
  • 1
    • 0028246688 scopus 로고
    • (R)-methanandamide: A chiral novel anandamidepossessing higher potency and metabolic stability
    • V Abadji S Lin G Taha G Griffin L.A Stevenson R.G Pertwee A Makriyannis ( R )-methanandamide: A chiral novel anandamidepossessing higher potency and metabolic stability J. Med. Chem. 37 1994 1889 1893
    • (1994) J. Med. Chem. , vol.37 , pp. 1889-1893
    • Abadji, V1    Lin, S2    Taha, G3    Griffin, G4    Stevenson, L.A5    Pertwee, R.G6    Makriyannis, A7
  • 2
    • 0032854610 scopus 로고    scopus 로고
    • Membrane proteins implicated in long-chain fatty acid uptake by mammalian cells: CD36, FATP and FABPm
    • N Abumrad C Coburn A Ibrahimi Membrane proteins implicated in long-chain fatty acid uptake by mammalian cells: CD36, FATP and FABPm Biochim. Biophys. Acta 1441 1999 4 13
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 4-13
    • Abumrad, N1    Coburn, C2    Ibrahimi, A3
  • 3
    • 0031935011 scopus 로고    scopus 로고
    • Assessment of anandamide interaction with the cannabinoid brain receptor: SR 141716A antagonism studies in mice and autoradiographic analysis of receptor binding in rat brain
    • I.B Adams D.R Compton B.R Martin Assessment of anandamide interaction with the cannabinoid brain receptor: SR 141716A antagonism studies in mice and autoradiographic analysis of receptor binding in rat brain J. Pharmacol. Exp. Ther. 284 1998 1209 1217
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 1209-1217
    • Adams, I.B1    Compton, D.R2    Martin, B.R3
  • 5
    • 0030866539 scopus 로고    scopus 로고
    • The cloned rat hydrolytic enzyme responsible for the breakdown of anandamide also catalyzes its formation via the condensation of arachidonic acid and ethanolamine
    • G Arreaza W.A Devane R.L Omeir G Sajnani J Kunz B.F Cravatt D.G Deutsch The cloned rat hydrolytic enzyme responsible for the breakdown of anandamide also catalyzes its formation via the condensation of arachidonic acid and ethanolamine Neurosci Lett. 234 1997 59 62
    • (1997) Neurosci Lett. , vol.234 , pp. 59-62
    • Arreaza, G1    Devane, W.A2    Omeir, R.L3    Sajnani, G4    Kunz, J5    Cravatt, B.F6    Deutsch, D.G7
  • 6
    • 0032988751 scopus 로고    scopus 로고
    • Deletion of a proline-rich region and a transmembrane domain in fatty acid amide hydrolase
    • G Arreaza D.G Deutsch Deletion of a proline-rich region and a transmembrane domain in fatty acid amide hydrolase FEBS Lett. 454 1999 57 60
    • (1999) FEBS Lett. , vol.454 , pp. 57-60
    • Arreaza, G1    Deutsch, D.G2
  • 7
    • 0033528763 scopus 로고    scopus 로고
    • Characterization of the hypnotic properties of oleamide
    • A.S Basile L Hanus W.B Mendelson Characterization of the hypnotic properties of oleamide NeuroReport 10 1999 947 951
    • (1999) NeuroReport , vol.10 , pp. 947-951
    • Basile, A.S1    Hanus, L2    Mendelson, W.B3
  • 8
    • 0032902926 scopus 로고    scopus 로고
    • Anandamide transport inhibition by the vanilloid agonist olvanil
    • M Beltramo D Piomelli Anandamide transport inhibition by the vanilloid agonist olvanil Eur. J. Pharmacol. 364 1999 75 78
    • (1999) Eur. J. Pharmacol. , vol.364 , pp. 75-78
    • Beltramo, M1    Piomelli, D2
  • 9
    • 0031040788 scopus 로고    scopus 로고
    • Inhibition of anandamide hydrolysis in rat brain tissue by (E)-6-(bromomethylene) tetrahydro-3-(1-naphthalenyl)-2H-pyran-2-one
    • M Beltramo E di Tomaso D Piomelli Inhibition of anandamide hydrolysis in rat brain tissue by ( E )-6-(bromomethylene) tetrahydro-3-(1-naphthalenyl)-2H-pyran-2-one FEBS Lett. 403 1997 263 267
    • (1997) FEBS Lett. , vol.403 , pp. 263-267
    • Beltramo, M1    di Tomaso, E2    Piomelli, D3
  • 10
    • 0030865871 scopus 로고    scopus 로고
    • Functional role of high-affinity anandamide transport, as revealed by selective inhibition
    • M Beltramo N Stella A Calignano S.Y Lin A Makriyannis D Piomelli Functional role of high-affinity anandamide transport, as revealed by selective inhibition Science 277 1997 1094 1097
    • (1997) Science , vol.277 , pp. 1094-1097
    • Beltramo, M1    Stella, N2    Calignano, A3    Lin, S.Y4    Makriyannis, A5    Piomelli, D6
  • 11
    • 0012391128 scopus 로고
    • Spectrophotometric investigations of the mechanism of a-chymotrypsin catalyzed hydrolyses: Detection of the acyl enzyme intermediate
    • M.L Bender G.R Schonbaum B Zerner Spectrophotometric investigations of the mechanism of a-chymotrypsin catalyzed hydrolyses: Detection of the acyl enzyme intermediate J. Am. Chem. Soc. 84 1962 2540 2550
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 2540-2550
    • Bender, M.L1    Schonbaum, G.R2    Zerner, B3
  • 12
  • 13
    • 0031031557 scopus 로고    scopus 로고
    • Biosynthesis, uptake, and degradation of anandamide and palmitoylethanolamide in leukocytes
    • T Bisogno S Maurelli D Melck L De Petrocellis V Di Marzo Biosynthesis, uptake, and degradation of anandamide and palmitoylethanolamide in leukocytes J. Biol. Chem. 272 1997 3315 3323
    • (1997) J. Biol. Chem. , vol.272 , pp. 3315-3323
    • Bisogno, T1    Maurelli, S2    Melck, D3    De Petrocellis, L4    Di Marzo, V5
  • 15
    • 0031716079 scopus 로고    scopus 로고
    • Oleamide: An endogenous sleep-inducing lipid and prototypical member of a new class of biological signaling molecules
    • D.L Boger S.J Henriksen B.F Cravatt Oleamide: An endogenous sleep-inducing lipid and prototypical member of a new class of biological signaling molecules Curr. Pharm. Des. 4 1998 303 314
    • (1998) Curr. Pharm. Des. , vol.4 , pp. 303-314
    • Boger, D.L1    Henriksen, S.J2    Cravatt, B.F3
  • 16
    • 0032516022 scopus 로고    scopus 로고
    • Structural requirements for 5-HT2A and 5-HT1A serotonin receptor potentiation by the biologically active lipid oleamide
    • D.L Boger J.E Patterson Q Jin Structural requirements for 5-HT2A and 5-HT1A serotonin receptor potentiation by the biologically active lipid oleamide Proc. Natl. Acad. Sci. USA 95 1998 4102 4107
    • (1998) , pp. 4102-4107
    • Boger, D.L1    Patterson, J.E2    Jin, Q3
  • 17
    • 0033579908 scopus 로고    scopus 로고
    • Trifluoromethyl ketone inhibitors of fatty acid amide hydrolase: A probe of structural and conformational features contributing to inhibition
    • D.L Boger H Sato A.E Lerner B.J Austin J.E Patterson M.P Patricelli B.F Cravatt Trifluoromethyl ketone inhibitors of fatty acid amide hydrolase: A probe of structural and conformational features contributing to inhibition Bioorg. Med. Chem. Lett. 9 1999 265 270
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 265-270
    • Boger, D.L1    Sato, H2    Lerner, A.E3    Austin, B.J4    Patterson, J.E5    Patricelli, M.P6    Cravatt, B.F7
  • 18
    • 12944277105 scopus 로고    scopus 로고
    • Exceptionally potent inhibitors of fatty acid amide hydrolase: The enzyme responsible for the degradation of endogenous oleamide and anandamide
    • D.L Boger H Sato A.E Lerner M.P Hedrick R.A Fecik H Miyauchi G.D Wilkie B.J Austin M.P Patricelli B.F Cravatt Exceptionally potent inhibitors of fatty acid amide hydrolase: The enzyme responsible for the degradation of endogenous oleamide and anandamide Proc. Natl. Acad. Sci. USA 97 2000 5044 5049
    • (2000) , pp. 5044-5049
    • Boger, D.L1    Sato, H2    Lerner, A.E3    Hedrick, M.P4    Fecik, R.A5    Miyauchi, H6    Wilkie, G.D7    Austin, B.J8    Patricelli, M.P9    Cravatt, B.F10
  • 19
    • 0026694442 scopus 로고
    • Intramembrane helix-helix association in oligomerization and transmembrane signaling
    • B.J Bormann D.M Engelman Intramembrane helix-helix association in oligomerization and transmembrane signaling Annu. Rev. Biophys. Biomol. Struct. 21 1992 223 242
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 223-242
    • Bormann, B.J1    Engelman, D.M2
  • 20
    • 0031733645 scopus 로고    scopus 로고
    • Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis
    • H.I Boshoff V Mizrahi Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis J. Bacteriol. 180 1998 5809 5814
    • (1998) J. Bacteriol. , vol.180 , pp. 5809-5814
    • Boshoff, H.I1    Mizrahi, V2
  • 22
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • B Brosig D Langosch The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues Prot. Sci. 7 1998 1052 1056
    • (1998) Prot. Sci. , vol.7 , pp. 1052-1056
    • Brosig, B1    Langosch, D2
  • 23
    • 0030249478 scopus 로고    scopus 로고
    • Membrane localization of N-acylphosphatidylethanolamine in central neurons: Studies with exogenous phospholipases
    • H Cadas S Schinelli D Piomelli Membrane localization of N -acylphosphatidylethanolamine in central neurons: Studies with exogenous phospholipases J. Lipid. Mediat Cell Signal 14 1996 63 70
    • (1996) J. Lipid. Mediat Cell Signal , vol.14 , pp. 63-70
    • Cadas, H1    Schinelli, S2    Piomelli, D3
  • 24
    • 0031033841 scopus 로고    scopus 로고
    • Occurrence and biosynthesis of endogenous cannabinoid precursor, N-arachidonoylphosphatidylethanolamine, in rat brain
    • H Cadas E di Tomaso D Piomelli Occurrence and biosynthesis of endogenous cannabinoid precursor, N -arachidonoylphosphatidylethanolamine, in rat brain J. Neurosci. 17 1997 1226 1242
    • (1997) J. Neurosci. , vol.17 , pp. 1226-1242
    • Cadas, H1    di Tomaso, E2    Piomelli, D3
  • 25
    • 0032537734 scopus 로고    scopus 로고
    • Control of pain initiation by endogenous cannabinoids
    • A Calignano G La Rana A Giuffrida D Piomelli Control of pain initiation by endogenous cannabinoids Nature 394 1998 277 281
    • (1998) Nature , vol.394 , pp. 277-281
    • Calignano, A1    La Rana, G2    Giuffrida, A3    Piomelli, D4
  • 26
    • 1842331465 scopus 로고    scopus 로고
    • Direct interaction of the calcium sensor protein synaptotagmin I with a cytoplasmic domain of the alpha 1 A subunit of the P/Q-type calcium channel
    • N Charvin C L'Eveque D Walker F Berton C Raymond M Kataoka Y Shoji-Kasai M Takahashi Direct interaction of the calcium sensor protein synaptotagmin I with a cytoplasmic domain of the alpha 1 A subunit of the P/Q-type calcium channel EMBO J. 16 1997 4591 4596
    • (1997) EMBO J. , vol.16 , pp. 4591-4596
    • Charvin, N1    L'Eveque, C2    Walker, D3    Berton, F4    Raymond, C5    Kataoka, M6    Shoji-Kasai, Y7    Takahashi, M8
  • 28
    • 0033582418 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae FAT1 gene encodes an acyl-CoA synthetase that is required for maintenance of very long chain fatty acid levels
    • J.Y Choi C.E Martin The Saccharomyces cerevisiae FAT1 gene encodes an acyl-CoA synthetase that is required for maintenance of very long chain fatty acid levels J. Biol. Chem. 274 1999 4671 4683
    • (1999) J. Biol. Chem. , vol.274 , pp. 4671-4683
    • Choi, J.Y1    Martin, C.E2
  • 29
    • 0023275669 scopus 로고
    • The nucleotide sequence of the amdS gene of Aspergillus nidulans and the molecular characterization of 5′ mutations
    • C.M Corrick A.P Twomey M.J Hynes The nucleotide sequence of the amdS gene of Aspergillus nidulans and the molecular characterization of 5′ mutations Gene 53 1987 63 71
    • (1987) Gene , vol.53 , pp. 63-71
    • Corrick, C.M1    Twomey, A.P2    Hynes, M.J3
  • 31
    • 0029904838 scopus 로고    scopus 로고
    • Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
    • B.F Cravatt D.K Giang S.P Mayfield D.L Boger R.A Lerner N.B Gilula Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides Nature 384 1996 83 87
    • (1996) Nature , vol.384 , pp. 83-87
    • Cravatt, B.F1    Giang, D.K2    Mayfield, S.P3    Boger, D.L4    Lerner, R.A5    Gilula, N.B6
  • 32
    • 0027444977 scopus 로고
    • Anandamide, an endogenous ligand of the cannabinoid receptor, induces hypomotility and hypothermia in vivo in rodents
    • J.N Crawley R.L Corwin J.K Robinson C.C Felder W.A Devane J Axelrod Anandamide, an endogenous ligand of the cannabinoid receptor, induces hypomotility and hypothermia in vivo in rodents Pharmacol. Biochem. Behav. 46 1993 967 972
    • (1993) Pharmacol. Biochem. Behav. , vol.46 , pp. 967-972
    • Crawley, J.N1    Corwin, R.L2    Robinson, J.K3    Felder, C.C4    Devane, W.A5    Axelrod, J6
  • 33
    • 0030613553 scopus 로고    scopus 로고
    • Glu-tRNA Gln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
    • A.W Curnow K Hong R Yuan S Kim O Martins W Winkler T.M Henkin D Soll Glu-tRNA Gln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation Proc. Natl. Acad. Sci. USA 94 1997 11819 11826
    • (1997) , pp. 11819-11826
    • Curnow, A.W1    Hong, K2    Yuan, R3    Kim, S4    Martins, O5    Winkler, W6    Henkin, T.M7    Soll, D8
  • 34
    • 0019142217 scopus 로고
    • Uptake and metabolism of fatty acids by dispersed adult rat heart myocytes. I. Kinetics of homologous fatty acids
    • R.F DeGrella R.J Light Uptake and metabolism of fatty acids by dispersed adult rat heart myocytes. I. Kinetics of homologous fatty acids J. Biol. Chem. 255 1980 9731 9738
    • (1980) J. Biol. Chem. , vol.255 , pp. 9731-9738
    • DeGrella, R.F1    Light, R.J2
  • 35
    • 0019161021 scopus 로고
    • Uptake and metabolism of fatty acids by dispersed adult rat heart myocytes. II. Inhibition by albumin and fatty acid homologues, and the effect of temperature and metabolic reagents
    • R.F DeGrella R.J Light Uptake and metabolism of fatty acids by dispersed adult rat heart myocytes. II. Inhibition by albumin and fatty acid homologues, and the effect of temperature and metabolic reagents J. Biol. Chem. 255 1980 9739 9745
    • (1980) J. Biol. Chem. , vol.255 , pp. 9739-9745
    • DeGrella, R.F1    Light, R.J2
  • 36
    • 0028903996 scopus 로고
    • Anandamide amidohydrolase activity in rat brain microsomes: Identification and partial characterization
    • F Desarnaud H Cadas D Piomelli Anandamide amidohydrolase activity in rat brain microsomes: Identification and partial characterization J. Biol. Chem. 270 1995 6030 6035
    • (1995) J. Biol. Chem. , vol.270 , pp. 6030-6035
    • Desarnaud, F1    Cadas, H2    Piomelli, D3
  • 37
    • 0027180394 scopus 로고
    • Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist
    • D.G Deutsch S.A Chin Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist Biochem. Pharmacol. 46 1993 791 796
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 791-796
    • Deutsch, D.G1    Chin, S.A2
  • 40
    • 0032459475 scopus 로고    scopus 로고
    • Biochemistry of the endogenous ligands of cannabinoid receptors
    • V Di Marzo D.G Deutsch Biochemistry of the endogenous ligands of cannabinoid receptors Neurobiol. Dis. 5 1998 386 404
    • (1998) Neurobiol. Dis. , vol.5 , pp. 386-404
    • Di Marzo, V1    Deutsch, D.G2
  • 41
    • 0032784084 scopus 로고    scopus 로고
    • Cannabimimetic fatty acid derivatives: The anandamide family and other endocannabinoids
    • V Di Marzo T Bisogno L De Petrocellis D Melck B.R Martin Cannabimimetic fatty acid derivatives: The anandamide family and other endocannabinoids Curr. Med. Chem. 6 1999 721 744
    • (1999) Curr. Med. Chem. , vol.6 , pp. 721-744
    • Di Marzo, V1    Bisogno, T2    De Petrocellis, L3    Melck, D4    Martin, B.R5
  • 43
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • G Dodson A Wlodawer Catalytic triads and their relatives Trends Biochem. Sci. 23 1998 347 352
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G1    Wlodawer, A2
  • 44
    • 0032494704 scopus 로고    scopus 로고
    • A new perspective on cannabinoid signalling: Complementary localization of fatty acid amide hydrolase and the CB1 receptor in rat brain
    • M Egertova D.K Giang B.F Cravatt M.R Elphick A new perspective on cannabinoid signalling: Complementary localization of fatty acid amide hydrolase and the CB1 receptor in rat brain Proc. R. Soc. Lond. B Biol. Sci. 265 1998 2081 2085
    • (1998) , pp. 2081-2085
    • Egertova, M1    Giang, D.K2    Cravatt, B.F3    Elphick, M.R4
  • 45
    • 0026514908 scopus 로고
    • The biosynthesis of neuropeptides: Peptide alpha-amidation
    • B.A Eipper D.A Stoffers R.E Mains The biosynthesis of neuropeptides: Peptide alpha-amidation Annu. Rev. Neurosci. 15 1992 57 85
    • (1992) Annu. Rev. Neurosci. , vol.15 , pp. 57-85
    • Eipper, B.A1    Stoffers, D.A2    Mains, R.E3
  • 46
    • 0019308380 scopus 로고
    • Accumulation of N-acylethanolamine glycerophospholipids in infarcted myocardium
    • D.E Epps V Natarajan P.C Schmid H.O Schmid Accumulation of N -acylethanolamine glycerophospholipids in infarcted myocardium Biochim. Biophys. Acta 618 1980 420 430
    • (1980) Biochim. Biophys. Acta , vol.618 , pp. 420-430
    • Epps, D.E1    Natarajan, V2    Schmid, P.C3    Schmid, H.O4
  • 47
    • 0028984984 scopus 로고
    • The vitamin D3 hydroxylase-associated protein is a propionamide-metabolizing amidase enzyme
    • R.A Ettinger H.F DeLuca The vitamin D3 hydroxylase-associated protein is a propionamide-metabolizing amidase enzyme Arch. Biochem. Biophys. 316 1995 14 19
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 14-19
    • Ettinger, R.A1    DeLuca, H.F2
  • 48
    • 0028906566 scopus 로고
    • Mast cells express a peripheral cannabinoid receptor with differential sensitivity to anandamide and palmitoylethanolamide
    • L Facci R Dal Toso S Romanello A Buriani S.D Skaper A Leon Mast cells express a peripheral cannabinoid receptor with differential sensitivity to anandamide and palmitoylethanolamide Proc. Natl. Acad. Sci. USA 92 1995 3376 3380
    • (1995) , pp. 3376-3380
    • Facci, L1    Dal Toso, R2    Romanello, S3    Buriani, A4    Skaper, S.D5    Leon, A6
  • 49
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • S Feng J.K Chen H Yu J.A Simon S.L Schreiber Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions Science 266 1994 1241 1247
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S1    Chen, J.K2    Yu, H3    Simon, J.A4    Schreiber, S.L5
  • 50
    • 0027467421 scopus 로고
    • Pharmacological activity of the cannabinoid receptor agonist, anandamide, a brain constituent
    • E Fride R Mechoulam Pharmacological activity of the cannabinoid receptor agonist, anandamide, a brain constituent Eur. J. Pharmacol. 231 1993 313 314
    • (1993) Eur. J. Pharmacol. , vol.231 , pp. 313-314
    • Fride, E1    Mechoulam, R2
  • 51
    • 0026281199 scopus 로고
    • The urea amidolyase (DUR1,2) gene of Saccharomyces cerevisiae
    • F.S Genbauffe T.G Cooper The urea amidolyase (DUR1,2) gene of Saccharomyces cerevisiae DNA Seq. 2 1991 19 32
    • (1991) DNA Seq. , vol.2 , pp. 19-32
    • Genbauffe, F.S1    Cooper, T.G2
  • 52
    • 0030903752 scopus 로고    scopus 로고
    • Molecular characterization of human and mouse fatty acid amide hydrolases
    • D.K Giang B.F Cravatt Molecular characterization of human and mouse fatty acid amide hydrolases Proc. Natl. Acad. Sci. USA 94 1997 2238 2242
    • (1997) , pp. 2238-2242
    • Giang, D.K1    Cravatt, B.F2
  • 54
    • 0032883310 scopus 로고    scopus 로고
    • Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression and site-directed mutagenesis(1)
    • S.K Goparaju Y Kurahashi H Suzuki N Ueda S Yamamoto Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression and site-directed mutagenesis(1) Biochim. Biophys. Acta 1441 1999 77 84
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 77-84
    • Goparaju, S.K1    Kurahashi, Y2    Suzuki, H3    Ueda, N4    Yamamoto, S5
  • 55
    • 0032559369 scopus 로고    scopus 로고
    • Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand
    • S.K Goparaju N Ueda H Yamaguchi S Yamamoto Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand FEBS Lett. 422 1998 69 73
    • (1998) FEBS Lett. , vol.422 , pp. 69-73
    • Goparaju, S.K1    Ueda, N2    Yamaguchi, H3    Yamamoto, S4
  • 56
    • 0022632821 scopus 로고
    • Acyl-CoA: Glycine N-acyltransferase: In vitro studies on the glycine conjugation of straight- and branched-chained acyl-CoA esters in human liver
    • N Gregersen S Kolvraa P.B Mortensen Acyl-CoA: Glycine N -acyltransferase: In vitro studies on the glycine conjugation of straight- and branched-chained acyl-CoA esters in human liver Biochem. Med. Metab. Biol. 35 1986 210 218
    • (1986) Biochem. Med. Metab. Biol. , vol.35 , pp. 210-218
    • Gregersen, N1    Kolvraa, S2    Mortensen, P.B3
  • 57
    • 0031921236 scopus 로고    scopus 로고
    • Fatty acid transport: Difficult or easy?
    • J.A Hamilton Fatty acid transport: Difficult or easy? J. Lipid Res. 39 1998 467 481
    • (1998) J. Lipid Res. , vol.39 , pp. 467-481
    • Hamilton, J.A1
  • 58
    • 0033511647 scopus 로고    scopus 로고
    • How are free fatty acids transported in membranes? Is it by proteins or by free diffusion through the lipids?
    • J.A Hamilton F Kamp How are free fatty acids transported in membranes? Is it by proteins or by free diffusion through the lipids? Diabetes 48 1999 2255 2269
    • (1999) Diabetes , vol.48 , pp. 2255-2269
    • Hamilton, J.A1    Kamp, F2
  • 59
    • 0032520747 scopus 로고    scopus 로고
    • Formation of N-acylphosphatidylethanolamines and N-acetylethanolamines: Proposed role in neurotoxicity
    • H.S Hansen L Lauritzen B Moesgaard A.M Strand H.H Hansen Formation of N -acylphosphatidylethanolamines and N -acetylethanolamines: Proposed role in neurotoxicity Biochem. Pharmacol. 55 1998 719 725
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 719-725
    • Hansen, H.S1    Lauritzen, L2    Moesgaard, B3    Strand, A.M4    Hansen, H.H5
  • 60
    • 0030838502 scopus 로고    scopus 로고
    • Characterization of glutamate-induced formation of N-acylphosphatidylethanolamine and N-acylethanolamine in cultured neocortical neurons
    • H.S Hansen L Lauritzen A.M Strand A.M Vinggaard A Frandsen A Schousboe Characterization of glutamate-induced formation of N -acylphosphatidylethanolamine and N -acylethanolamine in cultured neocortical neurons J. Neurochem. 69 1997 753 761
    • (1997) J. Neurochem. , vol.69 , pp. 753-761
    • Hansen, H.S1    Lauritzen, L2    Strand, A.M3    Vinggaard, A.M4    Frandsen, A5    Schousboe, A6
  • 61
    • 0029666267 scopus 로고    scopus 로고
    • A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation
    • T.E Hebert S Moffett J.P Morello T.P Loisel D.G Bichet C Barret M Bouvier A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation J. Biol. Chem. 271 1996 16,384 16,392
    • (1996) J. Biol. Chem. , vol.271
    • Hebert, T.E1    Moffett, S2    Morello, J.P3    Loisel, T.P4    Bichet, D.G5    Barret, C6    Bouvier, M7
  • 62
    • 0032702510 scopus 로고    scopus 로고
    • Allosteric regulation by oleamide of the binding properties of 5-hydroxytryptamine7 receptors
    • P.B Hedlund M.J Carson J.G Sutcliffe E.A Thomas Allosteric regulation by oleamide of the binding properties of 5-hydroxytryptamine7 receptors Biochem. Pharmacol. 58 1999 1807 1813
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 1807-1813
    • Hedlund, P.B1    Carson, M.J2    Sutcliffe, J.G3    Thomas, E.A4
  • 63
    • 0029133671 scopus 로고
    • Characterization of the kinetics and distribution of N-arachidonylethanolamine (anandamide) hydrolysis by rat brain
    • C.J Hillard D.M Wilkison W.S Edgemond W.B Campbell Characterization of the kinetics and distribution of N -arachidonylethanolamine (anandamide) hydrolysis by rat brain Biochim. Biophys. Acta 1257 1995 249 256
    • (1995) Biochim. Biophys. Acta , vol.1257 , pp. 249-256
    • Hillard, C.J1    Wilkison, D.M2    Edgemond, W.S3    Campbell, W.B4
  • 64
    • 0030852614 scopus 로고    scopus 로고
    • Accumulation of N-arachidonoylethanolamine (anandamide) into cerebellar granule cells occurs via facilitated diffusion
    • C.J Hillard W.S Edgemond A Jarrahian W.B Campbell Accumulation of N -arachidonoylethanolamine (anandamide) into cerebellar granule cells occurs via facilitated diffusion J. Neurochem. 69 1997 631 638
    • (1997) J. Neurochem. , vol.69 , pp. 631-638
    • Hillard, C.J1    Edgemond, W.S2    Jarrahian, A3    Campbell, W.B4
  • 65
    • 0029836767 scopus 로고    scopus 로고
    • Brain lipids that induce sleep are novel modulators of 5-hydroxytrypamine receptors
    • J.P Huidobro-Toro R.A Harris Brain lipids that induce sleep are novel modulators of 5-hydroxytrypamine receptors Proc. Natl. Acad. Sci. USA 93 1996 8078 8082
    • (1996) , pp. 8078-8082
    • Huidobro-Toro, J.P1    Harris, R.A2
  • 66
    • 0031776783 scopus 로고    scopus 로고
    • The anti-hyperalgesic actions of the cannabinoid anandamide and the putative CB2 receptor agonist palmitoyl ethanolamide in visceral and somatic inflammatory pain
    • S.I Jaggar F.S Hasnie S Sellaturay A.S Rice The anti-hyperalgesic actions of the cannabinoid anandamide and the putative CB2 receptor agonist palmitoyl ethanolamide in visceral and somatic inflammatory pain Pain 76 1998 189 199
    • (1998) Pain , vol.76 , pp. 189-199
    • Jaggar, S.I1    Hasnie, F.S2    Sellaturay, S3    Rice, A.S4
  • 67
    • 0032829859 scopus 로고    scopus 로고
    • Equilibrium in the hydrolysis and synthesis of cannabimimetic anandamide demonstrated by a purified enzyme
    • K Katayama N Ueda I Katoh S Yamamoto Equilibrium in the hydrolysis and synthesis of cannabimimetic anandamide demonstrated by a purified enzyme Biochim. Biophys. Acta 1440 1999 205 214
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 205-214
    • Katayama, K1    Ueda, N2    Katoh, I3    Yamamoto, S4
  • 68
    • 0027618423 scopus 로고
    • Isolation and characterization of mitochondrial acyl-CoA-Glycine N-acyltransferases from kidney
    • M Kelley D.A Vessey Isolation and characterization of mitochondrial acyl-CoA-Glycine N -acyltransferases from kidney J. Biochem. Toxicol. 8 1993 63 69
    • (1993) J. Biochem. Toxicol. , vol.8 , pp. 63-69
    • Kelley, M1    Vessey, D.A2
  • 69
    • 0345125820 scopus 로고
    • Nucleotide sequence of the tms genes of the pTiA6NC octopine Ti plasmid: Two gene products involved in plant tumorigenesis
    • H Klee A Montoya F Horodyski C Lichtenstein D Garfinkel S Fuller C Flores J Peschon Nucleotide sequence of the tms genes of the pTiA6NC octopine Ti plasmid: Two gene products involved in plant tumorigenesis Proc. Natl. Acad. Sci. USA 81 1984 1728 1732
    • (1984) , pp. 1728-1732
    • Klee, H1    Montoya, A2    Horodyski, F3    Lichtenstein, C4    Garfinkel, D5    Fuller, S6    Flores, C7    Peschon, J8
  • 70
    • 0032474456 scopus 로고    scopus 로고
    • Transport of long-chain native fatty acids across human erythrocyte ghost membranes
    • A.M Kleinfeld S Storms M Watts Transport of long-chain native fatty acids across human erythrocyte ghost membranes Biochemistry 37 1998 8011 8019
    • (1998) Biochemistry , vol.37 , pp. 8011-8019
    • Kleinfeld, A.M1    Storms, S2    Watts, M3
  • 71
    • 0027488920 scopus 로고
    • Amidase coupled with low-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1. Sequencing and expression of the gene and purification and characterization of the gene product
    • M Kobayashi H Komeda T Nagasawa M Nishiyama S Horinouchi T Beppu H Yamada S Shimizu Amidase coupled with low-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1. Sequencing and expression of the gene and purification and characterization of the gene product Eur. J. Biochem. 217 1993 327 336
    • (1993) Eur. J. Biochem. , vol.217 , pp. 327-336
    • Kobayashi, M1    Komeda, H2    Nagasawa, T3    Nishiyama, M4    Horinouchi, S5    Beppu, T6    Yamada, H7    Shimizu, S8
  • 72
    • 0031589532 scopus 로고    scopus 로고
    • Reversible hydrolysis and synthesis of anandamide demonstrated by recombinant rat fatty-acid amide hydrolase
    • Y Kurahashi N Ueda H Suzuki M Suzuki S Yamamoto Reversible hydrolysis and synthesis of anandamide demonstrated by recombinant rat fatty-acid amide hydrolase Biochem. Biophys. Res. Commun. 237 1997 512 515
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 512-515
    • Kurahashi, Y1    Ueda, N2    Suzuki, H3    Suzuki, M4    Yamamoto, S5
  • 74
    • 0031864409 scopus 로고    scopus 로고
    • Modulation of GABA(A) receptors and inhibitory synaptic currents by the endogenous CNS sleep regulator cis-9, 10-octadecenoamide (cOA)
    • G Lees M.D Edwards A.A Hassoni C.R Ganellin D Galanakis Modulation of GABA(A) receptors and inhibitory synaptic currents by the endogenous CNS sleep regulator cis-9, 10-octadecenoamide (cOA) Br. J. Pharmacol. 124 1998 873 882
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 873-882
    • Lees, G1    Edwards, M.D2    Hassoni, A.A3    Ganellin, C.R4    Galanakis, D5
  • 76
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • K.R MacKenzie J.H Prestegard D.M Engelman A transmembrane helix dimer: Structure and implications Science 276 1997 131 133
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R1    Prestegard, J.H2    Engelman, D.M3
  • 77
    • 0032459476 scopus 로고    scopus 로고
    • Cannabinoid transmission and pain perception
    • B.R Martin A.H Lichtman Cannabinoid transmission and pain perception Neurobiol. Dis. 5 1998 447 461
    • (1998) Neurobiol. Dis. , vol.5 , pp. 447-461
    • Martin, B.R1    Lichtman, A.H2
  • 78
    • 0029619298 scopus 로고
    • Two novel classes of neuroactive fatty acid amides are substrates for mouse neuroblastoma ‘anandamide amidohydrolase’
    • S Maurelli T Bisogno L De Petrocellis A Di Luccia G Marino V Di Marzo Two novel classes of neuroactive fatty acid amides are substrates for mouse neuroblastoma ‘anandamide amidohydrolase’ FEBS Lett. 377 1995 82 86
    • (1995) FEBS Lett. , vol.377 , pp. 82-86
    • Maurelli, S1    Bisogno, T2    De Petrocellis, L3    Di Luccia, A4    Marino, G5    Di Marzo, V6
  • 79
    • 0028658378 scopus 로고
    • Purification to homogeneity of mitochondrial acyl-CoA:glycine N-acyltransferase from human liver
    • Y.R Mawal I.A Qureshi Purification to homogeneity of mitochondrial acyl-CoA:glycine N -acyltransferase from human liver Biochem. Biophys. Res. Commun. 205 1994 1373 1379
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1373-1379
    • Mawal, Y.R1    Qureshi, I.A2
  • 80
    • 0025604503 scopus 로고
    • Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: Structural evidence for genetic coupling with nitrile hydratase.
    • J.F Mayaux E Cerebelaud F Soubrier D Faucher D Petre Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: Structural evidence for genetic coupling with nitrile hydratase. J. Bacteriol. 172 1990 6764 6773
    • (1990) J. Bacteriol. , vol.172 , pp. 6764-6773
    • Mayaux, J.F1    Cerebelaud, E2    Soubrier, F3    Faucher, D4    Petre, D5
  • 84
    • 0032724357 scopus 로고    scopus 로고
    • The hypnotic actions of oleamide are blocked by a cannabinoid receptor antagonist
    • W.B Mendelson A.S Basile The hypnotic actions of oleamide are blocked by a cannabinoid receptor antagonist NeuroReport 10 1999 3237 3239
    • (1999) NeuroReport , vol.10 , pp. 3237-3239
    • Mendelson, W.B1    Basile, A.S2
  • 85
    • 0030008554 scopus 로고    scopus 로고
    • Fatty acid amide biosynthesis: A possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A:glycine N-acyltransferase
    • D.J Merkler K.A Merkler W Stern F.F Fleming Fatty acid amide biosynthesis: A possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A:glycine N -acyltransferase Arch. Biochem. Biophys. 330 1996 430 434
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 430-434
    • Merkler, D.J1    Merkler, K.A2    Stern, W3    Fleming, F.F4
  • 87
    • 0019867747 scopus 로고
    • On the biosynthesis and metabolism of N-acylethanolamine phospholipids in infarcted dog heart
    • V Natarajan P.V Reddy P.C Schmid H.H Schmid On the biosynthesis and metabolism of N -acylethanolamine phospholipids in infarcted dog heart Biochim. Biophys. Acta 664 1981 445 448
    • (1981) Biochim. Biophys. Acta , vol.664 , pp. 445-448
    • Natarajan, V1    Reddy, P.V2    Schmid, P.C3    Schmid, H.H4
  • 88
    • 0028674857 scopus 로고
    • Genes galore: A summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones
    • T Newman F.J de Bruijn P Green K Keegstra H Kende L McIntosh J Ohlrogge N Raikhel Genes galore: A summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones Plant Physiol. 106 1994 1241 1255
    • (1994) Plant Physiol. , vol.106 , pp. 1241-1255
    • Newman, T1    de Bruijn, F.J2    Green, P3    Keegstra, K4    Kende, H5    McIntosh, L6    Ohlrogge, J7    Raikhel, N8
  • 89
    • 0033595722 scopus 로고    scopus 로고
    • Identification of two serine residues involved in catalysis by fatty acid amide hydrolase
    • R.L Omeir G Arreaza D.G Deutsch Identification of two serine residues involved in catalysis by fatty acid amide hydrolase Biochem. Biophys. Res. Commun. 264 1999 316 320
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 316-320
    • Omeir, R.L1    Arreaza, G2    Deutsch, D.G3
  • 90
    • 0033607236 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism
    • M.P Patricelli B.F Cravatt Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism Biochemistry 38 1999 14,125 14,130
    • (1999) Biochemistry , vol.38
    • Patricelli, M.P1    Cravatt, B.F2
  • 91
    • 0034705440 scopus 로고    scopus 로고
    • Clarifying the catalytic roles of conserved residues in the amidase signature family
    • M.P Patricelli B.F Cravatt Clarifying the catalytic roles of conserved residues in the amidase signature family J. Biol. Chem. 275 2000 19,177 19,184
    • (2000) J. Biol. Chem. , vol.275
    • Patricelli, M.P1    Cravatt, B.F2
  • 92
    • 0032573124 scopus 로고    scopus 로고
    • Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: Identification of the transmembrane domain as a site for oligomerization
    • M.P Patricelli H.A Lashuel D.K Giang J.W Kelly B.F Cravatt Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: Identification of the transmembrane domain as a site for oligomerization Biochemistry 37 1998 15,177 15,187
    • (1998) Biochemistry , vol.37
    • Patricelli, M.P1    Lashuel, H.A2    Giang, D.K3    Kelly, J.W4    Cravatt, B.F5
  • 93
    • 0033520099 scopus 로고    scopus 로고
    • Chemical and mutagenic investigations of fatty acid amide hydrolase: Evidence for a family of serine hydrolases with distinct catalytic properties
    • M.P Patricelli M.A Lovato B.F Cravatt Chemical and mutagenic investigations of fatty acid amide hydrolase: Evidence for a family of serine hydrolases with distinct catalytic properties Biochemistry 38 1999 9804 9812
    • (1999) Biochemistry , vol.38 , pp. 9804-9812
    • Patricelli, M.P1    Lovato, M.A2    Cravatt, B.F3
  • 94
    • 0030037917 scopus 로고    scopus 로고
    • Inhibition of oleamide hydrolase catalyzed hydrolysis of the endogenous sleep-inducing lipid cis-9-octadecenamide
    • J.E Patterson I.R Ollman B.F Cravatt D.L Boger C.H Wong R.A Lerner Inhibition of oleamide hydrolase catalyzed hydrolysis of the endogenous sleep-inducing lipid cis-9-octadecenamide J. Am. Chem. Soc. 118 1996 5938 5945
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5938-5945
    • Patterson, J.E1    Ollman, I.R2    Cravatt, B.F3    Boger, D.L4    Wong, C.H5    Lerner, R.A6
  • 95
    • 0033063326 scopus 로고    scopus 로고
    • N-acylphosphatidylethanolamine-hydrolyzing phospholipase D lacks the ability to transphosphatidlyate
    • G Petersen H.S Hansen N -acylphosphatidylethanolamine-hydrolyzing phospholipase D lacks the ability to transphosphatidlyate FEBS Lett. 455 1999 41 44
    • (1999) FEBS Lett. , vol.455 , pp. 41-44
    • Petersen, G1    Hansen, H.S2
  • 96
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • D Picot P.J Loll R.M Garavito The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1 Nature 367 1994 243 249
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D1    Loll, P.J2    Garavito, R.M3
  • 98
    • 0033545991 scopus 로고    scopus 로고
    • Structural determinants for recognition and translocation by the anandamide transporter
    • D Piomelli M Beltramo S Glasnapp S.Y Lin A Goutopoulos X.Q Xie A Makriyannis Structural determinants for recognition and translocation by the anandamide transporter Proc. Natl. Acad. Sci. USA 96 1999 5802 5807
    • (1999) , pp. 5802-5807
    • Piomelli, D1    Beltramo, M2    Glasnapp, S3    Lin, S.Y4    Goutopoulos, A5    Xie, X.Q6    Makriyannis, A7
  • 100
    • 0031779305 scopus 로고    scopus 로고
    • Cannabinoids reduce hyperalgesia and inflammation via interaction with peripheral CB1 receptors
    • J.D Richardson S Kilo K.M Hargreaves Cannabinoids reduce hyperalgesia and inflammation via interaction with peripheral CB1 receptors Pain 75 1998 111 119
    • (1998) Pain , vol.75 , pp. 111-119
    • Richardson, J.D1    Kilo, S2    Hargreaves, K.M3
  • 101
    • 0034685030 scopus 로고    scopus 로고
    • Induction of peptidylglycine alpha-amidating monooxygenase in N(18)TG(2) cells: A model for studying oleamide biosynthesis
    • K.J Ritenour-Rodgers W.J Driscoll K.A Merkler D.J Merkler G.P Mueller Induction of peptidylglycine alpha-amidating monooxygenase in N(18)TG(2) cells: A model for studying oleamide biosynthesis Biochem. Biophys. Res. Commun. 267 2000 521 526
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 521-526
    • Ritenour-Rodgers, K.J1    Driscoll, W.J2    Merkler, K.A3    Merkler, D.J4    Mueller, G.P5
  • 102
    • 0342832962 scopus 로고    scopus 로고
    • Extrapyramidal effects of methanandamide, an analog of anandamide, the endogenous CB1 receptor ligand
    • J Romero E Garcia-Palomero S.Y Lin J.A Ramos A Makriyannis J.J Fernandez-Ruiz Extrapyramidal effects of methanandamide, an analog of anandamide, the endogenous CB1 receptor ligand Life Sci. 58 1996 1249 1257
    • (1996) Life Sci. , vol.58 , pp. 1249-1257
    • Romero, J1    Garcia-Palomero, E2    Lin, S.Y3    Ramos, J.A4    Makriyannis, A5    Fernandez-Ruiz, J.J6
  • 103
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • W.P Russ D.M Engelman The GxxxG motif: A framework for transmembrane helix-helix association J. Mol. Biol. 296 2000 911 919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P1    Engelman, D.M2
  • 104
    • 0029826916 scopus 로고    scopus 로고
    • Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C
    • Y Sako N Nomura A Uchida Y Ishida H Morii Y Koga T Hoaki T Maruyama Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C Int. J. Syst. Bacteriol. 46 1996 1070 1077
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 1070-1077
    • Sako, Y1    Nomura, N2    Uchida, A3    Ishida, Y4    Morii, H5    Koga, Y6    Hoaki, T7    Maruyama, T8
  • 105
    • 0028837562 scopus 로고
    • Occurrence and postmortem generation of anandamide and other longchain N-acylethanolamines in mammalian brain
    • P.C Schmid R.J Krebsbach S.R Perry T.M Dettmer J.L Maason H.H Schmid Occurrence and postmortem generation of anandamide and other longchain N -acylethanolamines in mammalian brain FEBS Lett. 375 1995 117 120
    • (1995) FEBS Lett. , vol.375 , pp. 117-120
    • Schmid, P.C1    Krebsbach, R.J2    Perry, S.R3    Dettmer, T.M4    Maason, J.L5    Schmid, H.H6
  • 106
    • 0021099820 scopus 로고
    • Metabolism of N-acylethanolamine phospholipids by a mammalian phosphodiesterase of the phospholipase D type
    • P.C Schmid P.V Reddy V Natarajan H.H Schmid Metabolism of N -acylethanolamine phospholipids by a mammalian phosphodiesterase of the phospholipase D type J. Biol. Chem. 258 1983 9302 9306
    • (1983) J. Biol. Chem. , vol.258 , pp. 9302-9306
    • Schmid, P.C1    Reddy, P.V2    Natarajan, V3    Schmid, H.H4
  • 107
  • 108
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • A Senes M Gerstein D.M Engelman Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions J. Mol. Biol. 296 2000 921 936
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A1    Gerstein, M2    Engelman, D.M3
  • 109
    • 0033988703 scopus 로고    scopus 로고
    • Endocannabinoids protect cerebral cortical neurons from in vitro ischemia in rats
    • A.D Sinor S.M Irvin D.A Greenberg Endocannabinoids protect cerebral cortical neurons from in vitro ischemia in rats Neurosci. Lett. 278 2000 157 160
    • (2000) Neurosci. Lett. , vol.278 , pp. 157-160
    • Sinor, A.D1    Irvin, S.M2    Greenberg, D.A3
  • 110
    • 0029870716 scopus 로고    scopus 로고
    • The ALIAmide palmitoylethanolamide and cannabinoids, but not anandamide, are protective in a delayed postglutamate paradigm of excitotoxic death in cerebellar granule neurons
    • S.D Skaper A Buriani R Dal Toso L Petrelli S Romanello L Facci A Leon The ALIAmide palmitoylethanolamide and cannabinoids, but not anandamide, are protective in a delayed postglutamate paradigm of excitotoxic death in cerebellar granule neurons Proc. Natl. Acad. Sci. USA 93 1996 3984 3989
    • (1996) , pp. 3984-3989
    • Skaper, S.D1    Buriani, A2    Dal Toso, R3    Petrelli, L4    Romanello, S5    Facci, L6    Leon, A7
  • 112
    • 0030222771 scopus 로고    scopus 로고
    • Synaptotagmins: C2-domain proteins that regulate membrane traffic
    • T.C Sudhof J Rizo Synaptotagmins: C2-domain proteins that regulate membrane traffic Neuron 17 1996 379 388
    • (1996) Neuron , vol.17 , pp. 379-388
    • Sudhof, T.C1    Rizo, J2
  • 114
    • 0029860393 scopus 로고    scopus 로고
    • Enzymatic synthesis of oleamide (cis-9, 10-octadecenoamide), an endogenous sleep-inducing lipid, by rat brain microsomes
    • T Sugiura S Kondo T Kodaka T Tonegawa S Nakane A Yamashita Y Ishima K Waku Enzymatic synthesis of oleamide (cis-9, 10-octadecenoamide), an endogenous sleep-inducing lipid, by rat brain microsomes Biochem. Mol. Biol. Int. 40 1996 931 938
    • (1996) Biochem. Mol. Biol. Int. , vol.40 , pp. 931-938
    • Sugiura, T1    Kondo, S2    Kodaka, T3    Tonegawa, T4    Nakane, S5    Yamashita, A6    Ishima, Y7    Waku, K8
  • 115
    • 0029798721 scopus 로고    scopus 로고
    • Transacylase-mediated and phosphodiesterase-mediated synthesis of N-arachidonoylethanolamine, an endogenous cannabinoid-receptor ligand, in rat brain microsomes: Comparison with synthesis from free arachidonic acid and ethanolamine
    • T Sugiura S Kondo A Sukagawa T Tonegawa S Nakane A Yamashita Y Ishima K Waku Transacylase-mediated and phosphodiesterase-mediated synthesis of N -arachidonoylethanolamine, an endogenous cannabinoid-receptor ligand, in rat brain microsomes: Comparison with synthesis from free arachidonic acid and ethanolamine Eur. J. Biochem. 240 1996 53 62
    • (1996) Eur. J. Biochem. , vol.240 , pp. 53-62
    • Sugiura, T1    Kondo, S2    Sukagawa, A3    Tonegawa, T4    Nakane, S5    Yamashita, A6    Ishima, Y7    Waku, K8
  • 116
    • 0030066244 scopus 로고    scopus 로고
    • Enzymatic synthesis of anandamide, an endogenous cannabinoid receptor ligand, through N-acylphosphatidylethanolamine pathway in testis: Involvement of Ca(2+)-dependent transacylase and phosphodiesterase activities
    • T Sugiura S Kondo A Sukagawa T Tonegawa S Nakane A Yamashita K Waku Enzymatic synthesis of anandamide, an endogenous cannabinoid receptor ligand, through N -acylphosphatidylethanolamine pathway in testis: Involvement of Ca(2+)-dependent transacylase and phosphodiesterase activities Biochem. Biophys. Res. Commun. 218 1996 113 117
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 113-117
    • Sugiura, T1    Kondo, S2    Sukagawa, A3    Tonegawa, T4    Nakane, S5    Yamashita, A6    Waku, K7
  • 117
    • 0028811599 scopus 로고
    • Inhibition of long-term potentiation in rat hippocampal slices by anandamide and WIN55212-2: Reversal by SR141716 A, a selective antagonist of CB 1 cannabinoid receptors
    • J.P Terranova J.C Michaud G Le Fur P Soubrie Inhibition of long-term potentiation in rat hippocampal slices by anandamide and WIN55212-2: Reversal by SR141716 A, a selective antagonist of CB 1 cannabinoid receptors Naunyn Schmiedebergs Arch. Pharmacol. 352 1995 576 579
    • (1995) Naunyn Schmiedebergs Arch. Pharmacol. , vol.352 , pp. 576-579
    • Terranova, J.P1    Michaud, J.C2    Le Fur, G3    Soubrie, P4
  • 118
    • 0032417599 scopus 로고    scopus 로고
    • Oleamide-induced modulation of 5-hydroxytryptamine receptor-mediated signaling
    • E.A Thomas M.J Carson J.G Sutcliffe Oleamide-induced modulation of 5-hydroxytryptamine receptor-mediated signaling Ann. NY Acad. Sci. 861 1998 183 189
    • (1998) Ann. NY Acad. Sci. , vol.861 , pp. 183-189
    • Thomas, E.A1    Carson, M.J2    Sutcliffe, J.G3
  • 119
    • 0031469972 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase, the degradative enzyme for anandamide and oleamide, has selective distribution in neurons within the rat central nervous system
    • E.A Thomas B.F Cravatt P.E Danielson N.B Gilula J.G Sutcliffe Fatty acid amide hydrolase, the degradative enzyme for anandamide and oleamide, has selective distribution in neurons within the rat central nervous system J. Neurosci. Res. 50 1997 1047 1052
    • (1997) J. Neurosci. Res. , vol.50 , pp. 1047-1052
    • Thomas, E.A1    Cravatt, B.F2    Danielson, P.E3    Gilula, N.B4    Sutcliffe, J.G5
  • 120
    • 0033013899 scopus 로고    scopus 로고
    • The endogenous lipid oleamide activates serotonin 5-HT7 neurons in mouse thalamus and hypothalamus
    • E.A Thomas B.F Cravatt J.G Sutcliffe The endogenous lipid oleamide activates serotonin 5-HT7 neurons in mouse thalamus and hypothalamus J. Neurochem. 72 1999 2370 2378
    • (1999) J. Neurochem. , vol.72 , pp. 2370-2378
    • Thomas, E.A1    Cravatt, B.F2    Sutcliffe, J.G3
  • 121
    • 0032476070 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase is located preferentially in large neurons in the rat central nervous system as revealed by immunohistochemistry
    • K Tsou M.I Nogueron S Muthian M.C Sanudo-Pena C.J Hillard D.G Deutsch J.M Walker Fatty acid amide hydrolase is located preferentially in large neurons in the rat central nervous system as revealed by immunohistochemistry Neurosci. Lett. 254 1998 137 140
    • (1998) Neurosci. Lett. , vol.254 , pp. 137-140
    • Tsou, K1    Nogueron, M.I2    Muthian, S3    Sanudo-Pena, M.C4    Hillard, C.J5    Deutsch, D.G6    Walker, J.M7
  • 122
    • 0032192487 scopus 로고    scopus 로고
    • Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors
    • J.C Tu B Xiao J.P Yuan A.A Lanahan K Leoffert M Li D.J Linden P.F Worley Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors Neuron 21 1998 717 726
    • (1998) Neuron , vol.21 , pp. 717-726
    • Tu, J.C1    Xiao, B2    Yuan, J.P3    Lanahan, A.A4    Leoffert, K5    Li, M6    Linden, D.J7    Worley, P.F8
  • 123
    • 0028787812 scopus 로고
    • Partial purification and characterization of the porcine brain enzyme hydrolyzing and synthesizing anandamide
    • N Ueda Y Kurahashi S Yamamoto T Tokunaga Partial purification and characterization of the porcine brain enzyme hydrolyzing and synthesizing anandamide J. Biol. Chem. 270 1995 23823 23827
    • (1995) J. Biol. Chem. , vol.270 , pp. 23823-23827
    • Ueda, N1    Kurahashi, Y2    Yamamoto, S3    Tokunaga, T4
  • 124
    • 0027315816 scopus 로고
    • Anandamide, a brain endogenous compound, interacts specifically with cannabinoid receptors and inhibits adenylate cyclase
    • Z Vogel J.L Barg R Levy D Saya E Heldman R Mechoulam Anandamide, a brain endogenous compound, interacts specifically with cannabinoid receptors and inhibits adenylate cyclase J. Neurochem. 61 1993 352 355
    • (1993) J. Neurochem. , vol.61 , pp. 352-355
    • Vogel, Z1    Barg, J.L2    Levy, R3    Saya, D4    Heldman, E5    Mechoulam, R6
  • 125
    • 0032716177 scopus 로고    scopus 로고
    • Pain modulation by release of the endogenous cannabinoid anandamide
    • J.M Walker S.M Huang N.M Strangman K Tsou M.C Sanudo-Pena Pain modulation by release of the endogenous cannabinoid anandamide Proc. Natl. Acad. Sci. USA 96 1999 12198 12203
    • (1999) , pp. 12198-12203
    • Walker, J.M1    Huang, S.M2    Strangman, N.M3    Tsou, K4    Sanudo-Pena, M.C5
  • 126
    • 0004135644 scopus 로고
    • Enzymatic Reaction Mechanisms
    • C Walsh Enzymatic Reaction Mechanisms 1979 Freeman New York
    • (1979)
    • Walsh, C1
  • 127
    • 0030769202 scopus 로고    scopus 로고
    • Structure and function of a squalene cyclase
    • K.U Wendt K Poralla G.E Schulz Structure and function of a squalene cyclase Science 277 1997 1811 1815
    • (1997) Science , vol.277 , pp. 1811-1815
    • Wendt, K.U1    Poralla, K2    Schulz, G.E3
  • 130
    • 0033048369 scopus 로고    scopus 로고
    • GC/MS analysis of anandamide and quantification of N-arachidonoylphosphatidylethanolamides in various brain regions, spinal cord, testis, and spleen of the rat
    • H.Y Yang F Karoum C Felder H Badger T.C Wang S.P Markey GC/MS analysis of anandamide and quantification of N -arachidonoylphosphatidylethanolamides in various brain regions, spinal cord, testis, and spleen of the rat J. Neurochem. 72 1999 1959 1968
    • (1999) J. Neurochem. , vol.72 , pp. 1959-1968
    • Yang, H.Y1    Karoum, F2    Felder, C3    Badger, H4    Wang, T.C5    Markey, S.P6
  • 131
    • 0031811635 scopus 로고    scopus 로고
    • Oleamide potentiates benzodiazepine-sensitive gamma-aminobutyric acid receptor activity but does not alter minimum alveolar anesthetic concentration
    • C.S Yost A.J Hampson D Leonoudakis D.D Koblin L.M Bornheim A.T Gray Oleamide potentiates benzodiazepine-sensitive gamma-aminobutyric acid receptor activity but does not alter minimum alveolar anesthetic concentration Anesth. Analg. 86 1998 1294 1300
    • (1998) Anesth. Analg. , vol.86 , pp. 1294-1300
    • Yost, C.S1    Hampson, A.J2    Leonoudakis, D3    Koblin, D.D4    Bornheim, L.M5    Gray, A.T6


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