메뉴 건너뛰기




Volumn 197, Issue , 2016, Pages 13-24

Monoglyceride lipase: Structure and inhibitors

Author keywords

2 Arachidonoyl sn glycerol (2 AG); Cysteines; Endocannabinoids; Inhibitors; Lid domain; Monoglyceride lipase (MGL)

Indexed keywords

2 ARACHIDONOYLGLYCEROL; 4 [BIS(1,3 BENZODIOXOL 5 YL)HYDROXYMETHYL] 1 PIPERIDINECARBOXYLIC ACID 4 NITROPHENYL ESTER; ACYLGLYCEROL LIPASE; ACYLGLYCEROL LIPASE INHIBITOR; BENZISOTHIAZOLINONE DERIVATIVE; BETA AMYRIN; CARBAMIC ACID DERIVATIVE; CL 6 A; COMP 21; CYSTEINE; DISULFIDE; DISULFIRAM; ENDOCANNABINOID; EUPHOL; ISOTHIAZOLINONE DERIVATIVE; JJKK 048; JW 651; JZL 195; KML 29; MALEIMIDE DERIVATIVE; MJN 110; O HEXAFLUOROISOPROPYLCARBAMATE DERIVATIVE; OCTHILINONE; PRISTIMERIN; SAR 127303; SERINE; TERPENOID DERIVATIVE; THIAZOLE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG; URB 602; ENZYME INHIBITOR;

EID: 84960815043     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2015.07.011     Document Type: Article
Times cited : (53)

References (100)
  • 6
    • 0034720298 scopus 로고    scopus 로고
    • Carrier-mediated and enzymatic hydrolysis of the endogenous cannabinoid 2-arachidonoylglycerol
    • M. Beltramo, and D. Piomelli Carrier-mediated and enzymatic hydrolysis of the endogenous cannabinoid 2-arachidonoylglycerol Neuroreport 11 2000 1231 1235
    • (2000) Neuroreport , vol.11 , pp. 1231-1235
    • Beltramo, M.1    Piomelli, D.2
  • 9
    • 37149013708 scopus 로고    scopus 로고
    • A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol
    • J.L. Blankman, G.M. Simon, and B.F. Cravatt A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol Chem. Biol. 14 2007 1347 1356
    • (2007) Chem. Biol. , vol.14 , pp. 1347-1356
    • Blankman, J.L.1    Simon, G.M.2    Cravatt, B.F.3
  • 10
    • 84872867557 scopus 로고    scopus 로고
    • ABHD12 controls brain lysophosphatidylserine pathways that are deregulated in a murine model of the neurodegenerative disease PHARC
    • J.L. Blankman, J.Z. Long, S.A. Trauger, G. Siuzdak, and B.F. Cravatt ABHD12 controls brain lysophosphatidylserine pathways that are deregulated in a murine model of the neurodegenerative disease PHARC Proc. Natl. Acad. Sci. U.S.A. 110 2013 1500 1505
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 1500-1505
    • Blankman, J.L.1    Long, J.Z.2    Trauger, S.A.3    Siuzdak, G.4    Cravatt, B.F.5
  • 12
    • 72849117351 scopus 로고    scopus 로고
    • Refined homology model of monoacylglycerol lipase: Toward a selective inhibitor
    • A.L. Bowman, and A. Makriyannis Refined homology model of monoacylglycerol lipase: toward a selective inhibitor J. Comput. Aided Mol. Des. 23 2009 799 806
    • (2009) J. Comput. Aided Mol. Des. , vol.23 , pp. 799-806
    • Bowman, A.L.1    Makriyannis, A.2
  • 14
    • 84867055620 scopus 로고    scopus 로고
    • Pretreatment with the monoacylglycerol lipase inhibitor URB602 protects from the long-term consequences of neonatal hypoxic-ischemic brain injury in rats
    • S. Carloni, D. Alonso-Alconada, S. Girelli, A. Duranti, A. Tontini, D. Piomelli, E. Hilario, A. Alvarez, and W. Balduini Pretreatment with the monoacylglycerol lipase inhibitor URB602 protects from the long-term consequences of neonatal hypoxic-ischemic brain injury in rats Pediatr. Res. 72 2012 400 406
    • (2012) Pediatr. Res. , vol.72 , pp. 400-406
    • Carloni, S.1    Alonso-Alconada, D.2    Girelli, S.3    Duranti, A.4    Tontini, A.5    Piomelli, D.6    Hilario, E.7    Alvarez, A.8    Balduini, W.9
  • 16
    • 84880517778 scopus 로고    scopus 로고
    • Proteome-wide reactivity profiling identifies diverse carbamate chemotypes tuned for serine hydrolase inhibition
    • J.W. Chang, A.B. Cognetta 3rd, M.J. Niphakis, and B.F. Cravatt Proteome-wide reactivity profiling identifies diverse carbamate chemotypes tuned for serine hydrolase inhibition ACS Chem. Biol. 8 2013 1590 1599
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1590-1599
    • Chang, J.W.1    Cognetta, A.B.2    Niphakis, M.J.3    Cravatt, B.F.4
  • 17
    • 84870412999 scopus 로고    scopus 로고
    • Monoacylglycerol lipase is a therapeutic target for Alzheimer's disease
    • R. Chen, J. Zhang, Y. Wu, D. Wang, G. Feng, Y.P. Tang, Z. Teng, and C. Chen Monoacylglycerol lipase is a therapeutic target for Alzheimer's disease Cell Rep. 2 2012 1329 1339
    • (2012) Cell Rep. , vol.2 , pp. 1329-1339
    • Chen, R.1    Zhang, J.2    Wu, Y.3    Wang, D.4    Feng, G.5    Tang, Y.P.6    Teng, Z.7    Chen, C.8
  • 18
    • 84867386846 scopus 로고    scopus 로고
    • The antinociceptive triterpene β-amyrin inhibits 2-arachidonoylglycerol (2-AG) hydrolysis without directly targeting cannabinoid receptors
    • A. Chicca, J. Marazzi, and J. Gertsch The antinociceptive triterpene β-amyrin inhibits 2-arachidonoylglycerol (2-AG) hydrolysis without directly targeting cannabinoid receptors Br. J. Pharmacol. 167 2012 1596 1608
    • (2012) Br. J. Pharmacol. , vol.167 , pp. 1596-1608
    • Chicca, A.1    Marazzi, J.2    Gertsch, J.3
  • 20
    • 35648973242 scopus 로고    scopus 로고
    • The inhibition of monoacylglycerol lipase by URB602 showed an anti-inflammatory and anti-nociceptive effect in a murine model of acute inflammation
    • F. Comelli, G. Giagnoni, I. Bettoni, M. Colleoni, and B. Costa The inhibition of monoacylglycerol lipase by URB602 showed an anti-inflammatory and anti-nociceptive effect in a murine model of acute inflammation Br. J. Pharmacol. 152 2007 787 794
    • (2007) Br. J. Pharmacol. , vol.152 , pp. 787-794
    • Comelli, F.1    Giagnoni, G.2    Bettoni, I.3    Colleoni, M.4    Costa, B.5
  • 21
    • 33644989300 scopus 로고    scopus 로고
    • Role of the basolateral nucleus of the amygdala in endocannabinoid-mediated stress-induced analgesia
    • K. Connell, N. Bolton, D. Olsen, D. Piomelli, and A.G. Hohmann Role of the basolateral nucleus of the amygdala in endocannabinoid-mediated stress-induced analgesia Neurosci. Lett. 397 2006 180 184
    • (2006) Neurosci. Lett. , vol.397 , pp. 180-184
    • Connell, K.1    Bolton, N.2    Olsen, D.3    Piomelli, D.4    Hohmann, A.G.5
  • 22
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • B.F. Cravatt, A.T. Wright, and J.W. Kozarich Activity-based protein profiling: from enzyme chemistry to proteomic chemistry Annu. Rev. Biochem. 77 2008 383 414
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 23
    • 84924860926 scopus 로고    scopus 로고
    • Combined inhibition of monoacylglycerol lipase and cyclooxygenases synergistically reduces neuropathic pain in mice
    • M.S. Crowe, E. Leishman, M.L. Banks, R. Gujjar, A. Mahadevan, H.B. Bradshaw, and S.G. Kinsey Combined inhibition of monoacylglycerol lipase and cyclooxygenases synergistically reduces neuropathic pain in mice Br. J. Pharmacol. 172 2015 1700 1712
    • (2015) Br. J. Pharmacol. , vol.172 , pp. 1700-1712
    • Crowe, M.S.1    Leishman, E.2    Banks, M.L.3    Gujjar, R.4    Mahadevan, A.5    Bradshaw, H.B.6    Kinsey, S.G.7
  • 24
    • 57349137829 scopus 로고    scopus 로고
    • Modulation of the anti-nociceptive effects of 2-arachidonoyl glycerol by peripherally administered FAAH and MGL inhibitors in a neuropathic pain model
    • J. Desroches, J. Guindon, C. Lambert, and P. Beaulieu Modulation of the anti-nociceptive effects of 2-arachidonoyl glycerol by peripherally administered FAAH and MGL inhibitors in a neuropathic pain model Br. J. Pharmacol. 155 2008 913 924
    • (2008) Br. J. Pharmacol. , vol.155 , pp. 913-924
    • Desroches, J.1    Guindon, J.2    Lambert, C.3    Beaulieu, P.4
  • 28
    • 0037207088 scopus 로고    scopus 로고
    • A role for monoglyceride lipase in 2-arachidonoylglycerol inactivation
    • T.P. Dinh, T.F. Freund, and D. Piomelli A role for monoglyceride lipase in 2-arachidonoylglycerol inactivation Chem. Phys. Lipids 121 2002 149 158
    • (2002) Chem. Phys. Lipids , vol.121 , pp. 149-158
    • Dinh, T.P.1    Freund, T.F.2    Piomelli, D.3
  • 29
    • 6944247598 scopus 로고    scopus 로고
    • RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of 2-arachidonoylglycerol
    • T.P. Dinh, S. Kathuria, and D. Piomelli RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of 2-arachidonoylglycerol Mol. Pharmacol. 66 2004 1260 1264
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1260-1264
    • Dinh, T.P.1    Kathuria, S.2    Piomelli, D.3
  • 35
    • 84926231211 scopus 로고    scopus 로고
    • Peripheral antinociceptive effects of inhibitors of monoacylglycerol lipase in a rat model of inflammatory pain
    • J. Guindon, A. Guijarro, D. Piomelli, and A.G. Hohmann Peripheral antinociceptive effects of inhibitors of monoacylglycerol lipase in a rat model of inflammatory pain Br. J. Pharmacol. 163 2011 1464 1478
    • (2011) Br. J. Pharmacol. , vol.163 , pp. 1464-1478
    • Guindon, J.1    Guijarro, A.2    Piomelli, D.3    Hohmann, A.G.4
  • 36
    • 84870915147 scopus 로고    scopus 로고
    • Alterations in endocannabinoid tone following chemotherapy-induced peripheral neuropathy: Effects of endocannabinoid deactivation inhibitors targeting fatty-acid amide hydrolase and monoacylglycerol lipase in comparison to reference analgesics following cisplatin treatment
    • J. Guindon, Y. Lai, S.M. Takacs, H.B. Bradshaw, and A.G. Hohmann Alterations in endocannabinoid tone following chemotherapy-induced peripheral neuropathy: effects of endocannabinoid deactivation inhibitors targeting fatty-acid amide hydrolase and monoacylglycerol lipase in comparison to reference analgesics following cisplatin treatment Pharmacol. Res. 67 2013 94 109
    • (2013) Pharmacol. Res. , vol.67 , pp. 94-109
    • Guindon, J.1    Lai, Y.2    Takacs, S.M.3    Bradshaw, H.B.4    Hohmann, A.G.5
  • 37
    • 3242751838 scopus 로고    scopus 로고
    • Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala
    • A.I. Gulyas, B.F. Cravatt, M.H. Bracey, T.P. Dinh, D. Pomelli, F. Boscia, and T.F. Freund Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala Eur. J. Neurosci. 20 2004 441 458
    • (2004) Eur. J. Neurosci. , vol.20 , pp. 441-458
    • Gulyas, A.I.1    Cravatt, B.F.2    Bracey, M.H.3    Dinh, T.P.4    Pomelli, D.5    Boscia, F.6    Freund, T.F.7
  • 39
    • 84903384432 scopus 로고    scopus 로고
    • Substrate-selective COX-2 inhibition as a novel strategy for therapeutic endocannabinoid augmentation
    • D.J. Hermanson, J.C. Gamble-George, L.J. Marnett, and S. Patel Substrate-selective COX-2 inhibition as a novel strategy for therapeutic endocannabinoid augmentation Trends Pharmacol. Sci. 35 2014 358 367
    • (2014) Trends Pharmacol. Sci. , vol.35 , pp. 358-367
    • Hermanson, D.J.1    Gamble-George, J.C.2    Marnett, L.J.3    Patel, S.4
  • 41
    • 84878358316 scopus 로고    scopus 로고
    • Differential modulation of nociceptive versus non-nociceptive synapses by endocannabinoids
    • A. Higgins, S. Yuan, Y. Wang, and B.D. Burrell Differential modulation of nociceptive versus non-nociceptive synapses by endocannabinoids Mol. Pain 9 2013 26
    • (2013) Mol. Pain , vol.9 , pp. 26
    • Higgins, A.1    Yuan, S.2    Wang, Y.3    Burrell, B.D.4
  • 44
    • 41649118003 scopus 로고    scopus 로고
    • Prostaglandin E2 glycerol ester, an endogenous COX-2 metabolite of 2-arachidonoylglycerol, induces hyperalgesia and modulates NFjB activity
    • S.S. Hu, H.B. Bradshaw, J.S. Chen, B. Tan, and J.M. Walker Prostaglandin E2 glycerol ester, an endogenous COX-2 metabolite of 2-arachidonoylglycerol, induces hyperalgesia and modulates NFjB activity Br. J. Pharmacol. 153 2008 1538 1549
    • (2008) Br. J. Pharmacol. , vol.153 , pp. 1538-1549
    • Hu, S.S.1    Bradshaw, H.B.2    Chen, J.S.3    Tan, B.4    Walker, J.M.5
  • 45
    • 84855909190 scopus 로고    scopus 로고
    • NMDA receptors, mGluR5, and endocannabinoids are involved in a cascade leading to hippocampal long-term depression
    • Y. Izumi, and C.F. Zorumski NMDA receptors, mGluR5, and endocannabinoids are involved in a cascade leading to hippocampal long-term depression Neuropsychopharmacology 37 2012 609 617
    • (2012) Neuropsychopharmacology , vol.37 , pp. 609-617
    • Izumi, Y.1    Zorumski, C.F.2
  • 46
    • 45849106100 scopus 로고    scopus 로고
    • Inhibition of fatty acid amide hydrolase and cyclooxygenase-2 increases levels of endocannabinoid related molecules and produces analgesia via peroxisome proliferator-activated receptor-alpha in a model of inflammatory pain
    • M.D. Jhaveri, D. Richardson, I. Robinson, M.J. Garle, A. Patel, Y. Sun, D.R. Sagar, A.J. Bennett, S.P. Alexander, D.A. Kendall, and V. Chapman Inhibition of fatty acid amide hydrolase and cyclooxygenase-2 increases levels of endocannabinoid related molecules and produces analgesia via peroxisome proliferator-activated receptor-alpha in a model of inflammatory pain Neuropharmacology 55 2008 85 93
    • (2008) Neuropharmacology , vol.55 , pp. 85-93
    • Jhaveri, M.D.1    Richardson, D.2    Robinson, I.3    Garle, M.J.4    Patel, A.5    Sun, Y.6    Sagar, D.R.7    Bennett, A.J.8    Alexander, S.P.9    Kendall, D.A.10    Chapman, V.11
  • 47
    • 70949084728 scopus 로고    scopus 로고
    • Bis(dialkylaminethiocarbonyl)disulfides as potent and selective monoglyceride lipase inhibitors
    • C.N. Kapanda, G.G. Muccioli, G. Labar, J.H. Poupaert, and D.M. Lambert Bis(dialkylaminethiocarbonyl)disulfides as potent and selective monoglyceride lipase inhibitors J. Med. Chem. 52 2009 7310 7314
    • (2009) J. Med. Chem. , vol.52 , pp. 7310-7314
    • Kapanda, C.N.1    Muccioli, G.G.2    Labar, G.3    Poupaert, J.H.4    Lambert, D.M.5
  • 48
    • 0030767295 scopus 로고    scopus 로고
    • CDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase
    • M. Karlsson, J.A. Contreras, U. Hellman, H. Tornqvist, and C. Holm cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase J. Biol. Chem. 272 1997 27218 27223
    • (1997) J. Biol. Chem. , vol.272 , pp. 27218-27223
    • Karlsson, M.1    Contreras, J.A.2    Hellman, U.3    Tornqvist, H.4    Holm, C.5
  • 49
    • 84878526504 scopus 로고    scopus 로고
    • 1,3,4-Oxadiazol-2-ones as fatty-acid amide hydrolase and monoacylglycerol lipase inhibitors: Synthesis, in vitro evaluation and insight into potency and selectivity determinants by molecular modelling
    • H. Käsnänen, A. Minkkilä, S. Taupila, J.Z. Patel, T. Parkkari, M. Lahtela-Kakkonen, S.M. Saario, T. Nevalainen, and A. Poso 1,3,4-Oxadiazol-2-ones as fatty-acid amide hydrolase and monoacylglycerol lipase inhibitors: synthesis, in vitro evaluation and insight into potency and selectivity determinants by molecular modelling Eur. J. Pharm. Sci. 49 2013 423 433
    • (2013) Eur. J. Pharm. Sci. , vol.49 , pp. 423-433
    • Käsnänen, H.1    Minkkilä, A.2    Taupila, S.3    Patel, J.Z.4    Parkkari, T.5    Lahtela-Kakkonen, M.6    Saario, S.M.7    Nevalainen, T.8    Poso, A.9
  • 51
    • 3042785976 scopus 로고    scopus 로고
    • Inhibition of cyclooxygenase-2 potentiates retrograde endocannabinoid effects in hippocampus
    • J. Kim, and B.E. Alger Inhibition of cyclooxygenase-2 potentiates retrograde endocannabinoid effects in hippocampus Nat. Neurosci. 7 2004 697 698
    • (2004) Nat. Neurosci. , vol.7 , pp. 697-698
    • Kim, J.1    Alger, B.E.2
  • 53
    • 70350339817 scopus 로고    scopus 로고
    • A critical cysteine residue in monoacylglycerol lipase is targeted by a new class of isothiazolinone-based enzyme inhibitors
    • A.R. King, A. Lodola, C. Carmi, J. Fu, M. Mor, and D. Piomelli A critical cysteine residue in monoacylglycerol lipase is targeted by a new class of isothiazolinone-based enzyme inhibitors Br. J. Pharmacol. 157 2009 974 983
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 974-983
    • King, A.R.1    Lodola, A.2    Carmi, C.3    Fu, J.4    Mor, M.5    Piomelli, D.6
  • 55
    • 84878069411 scopus 로고    scopus 로고
    • Repeated low-dose administration of the monoacylglycerol lipase inhibitor JZL184 retains cannabinoid receptor type 1-mediated antinociceptive and gastroprotective effects
    • S.G. Kinsey, L.E. Wise, D. Ramesh, R. Abdullah, D.E. Selley, B.F. Cravatt, and A.H. Lichtman Repeated low-dose administration of the monoacylglycerol lipase inhibitor JZL184 retains cannabinoid receptor type 1-mediated antinociceptive and gastroprotective effects J. Pharmacol. Exp. Ther. 345 2013 492 501
    • (2013) J. Pharmacol. Exp. Ther. , vol.345 , pp. 492-501
    • Kinsey, S.G.1    Wise, L.E.2    Ramesh, D.3    Abdullah, R.4    Selley, D.E.5    Cravatt, B.F.6    Lichtman, A.H.7
  • 56
    • 0035839520 scopus 로고    scopus 로고
    • Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol
    • K.R. Kozak, J.J. Prusakiewicz, S.W. Rowlinson, C. Schneider, and L.J. Marnett Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol J. Biol. Chem. 276 2001 30072 30077
    • (2001) J. Biol. Chem. , vol.276 , pp. 30072-30077
    • Kozak, K.R.1    Prusakiewicz, J.J.2    Rowlinson, S.W.3    Schneider, C.4    Marnett, L.J.5
  • 57
    • 0034721794 scopus 로고    scopus 로고
    • Oxygenation of the endocannabinoid, 2-arachidonylglycerol, to glyceryl prostaglandins by cyclooxygenase-2
    • K.R. Kozak, S.W. Rowlinson, and L.J. Marnett Oxygenation of the endocannabinoid, 2-arachidonylglycerol, to glyceryl prostaglandins by cyclooxygenase-2 J. Biol. Chem. 275 2000 33744 33749
    • (2000) J. Biol. Chem. , vol.275 , pp. 33744-33749
    • Kozak, K.R.1    Rowlinson, S.W.2    Marnett, L.J.3
  • 58
    • 62149143788 scopus 로고    scopus 로고
    • 2-Arachidonoylglycerol elicits neuroprotective effects on excitotoxically lesioned dentate gyrus granule cells via abnormal-cannabidiol-sensitive receptors on microglial cells
    • S. Kreutz, M. Koch, C. Böttger, C. Ghadban, H.W. Korf, and F. Dehghani 2-Arachidonoylglycerol elicits neuroprotective effects on excitotoxically lesioned dentate gyrus granule cells via abnormal-cannabidiol-sensitive receptors on microglial cells Glia 57 2009 286 294
    • (2009) Glia , vol.57 , pp. 286-294
    • Kreutz, S.1    Koch, M.2    Böttger, C.3    Ghadban, C.4    Korf, H.W.5    Dehghani, F.6
  • 59
    • 34547483026 scopus 로고    scopus 로고
    • Disulfiram is an inhibitor of human purified monoacylglycerol lipase, the enzyme regulating 2-arachidonoylglycerol signaling
    • G. Labar, C. Bauvois, G.G. Muccioli, J. Wouters, and D.M. Lambert Disulfiram is an inhibitor of human purified monoacylglycerol lipase, the enzyme regulating 2-arachidonoylglycerol signaling ChemBioChem 8 2007 1293 1297
    • (2007) ChemBioChem , vol.8 , pp. 1293-1297
    • Labar, G.1    Bauvois, C.2    Muccioli, G.G.3    Wouters, J.4    Lambert, D.M.5
  • 60
    • 76649126721 scopus 로고    scopus 로고
    • Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling
    • G. Labar, C. Bauvois, F. Borel, J.L. Ferrer, J. Wouters, and D.M. Lambert Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling ChemBioChem 11 2010 218 227
    • (2010) ChemBioChem , vol.11 , pp. 218-227
    • Labar, G.1    Bauvois, C.2    Borel, F.3    Ferrer, J.L.4    Wouters, J.5    Lambert, D.M.6
  • 62
    • 0036089489 scopus 로고    scopus 로고
    • Pharmacological activity of fatty acid amides is regulated, but not mediated, by fatty acid amide hydrolase in vivo
    • A.H. Lichtman, E.G. Hawkins, G. Griffin, and B.F. Cravatt Pharmacological activity of fatty acid amides is regulated, but not mediated, by fatty acid amide hydrolase in vivo J. Pharmacol. Exp. Ther. 302 2002 73 79
    • (2002) J. Pharmacol. Exp. Ther. , vol.302 , pp. 73-79
    • Lichtman, A.H.1    Hawkins, E.G.2    Griffin, G.3    Cravatt, B.F.4
  • 64
    • 67651100845 scopus 로고    scopus 로고
    • Characterization of monoacylglycerol lipase inhibition reveals differences in central and peripheral endocannabinoid metabolism
    • J.Z. Long, D.K. Nomura, and B.F. Cravatt Characterization of monoacylglycerol lipase inhibition reveals differences in central and peripheral endocannabinoid metabolism Chem. Biol. 16 2009 744 753
    • (2009) Chem. Biol. , vol.16 , pp. 744-753
    • Long, J.Z.1    Nomura, D.K.2    Cravatt, B.F.3
  • 68
    • 72249083920 scopus 로고    scopus 로고
    • Synthesis and in vivo evaluation of N-substituted maleimide derivatives as selective monoglyceride lipase inhibitors
    • N. Matuszak, G.G. Muccioli, G. Labar, and D.M. Lambert Synthesis and in vivo evaluation of N-substituted maleimide derivatives as selective monoglyceride lipase inhibitors J. Med. Chem. 52 2009 7410 7420
    • (2009) J. Med. Chem. , vol.52 , pp. 7410-7420
    • Matuszak, N.1    Muccioli, G.G.2    Labar, G.3    Lambert, D.M.4
  • 69
    • 81255209307 scopus 로고    scopus 로고
    • Benzisothiazolinone as a useful template for the design of new monoacylglycerol lipase inhibitors: Investigation of the target residues and comparison with octhilinone
    • N. Matuszak, B. Es Saadi, G. Labar, J. Marchan-Brynaert, and D.M. Lambert Benzisothiazolinone as a useful template for the design of new monoacylglycerol lipase inhibitors: investigation of the target residues and comparison with octhilinone Bioorg. Med. Chem. Lett. 21 2011 7321 7324
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 7321-7324
    • Matuszak, N.1    Es Saadi, B.2    Labar, G.3    Marchan-Brynaert, J.4    Lambert, D.M.5
  • 73
    • 73149109062 scopus 로고    scopus 로고
    • Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
    • D.K. Nomura, J.Z. Long, S. Niessen, H.H. Hoover, S. Ng, and B.F. Cravatt Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis Cell 140 2010 49 61
    • (2010) Cell , vol.140 , pp. 49-61
    • Nomura, D.K.1    Long, J.Z.2    Niessen, S.3    Hoover, H.H.4    Ng, S.5    Cravatt, B.F.6
  • 75
    • 79960939546 scopus 로고    scopus 로고
    • Monoacylglycerol lipase exerts dual control over the endocannabinoid and fatty acid pathways to support prostate cancer
    • D.K. Nomura, D.P. Lombardi, J.W. Chang, S. Niessen, A.M. Ward, J.Z. Long, H.H. Hoover, and B.F. Cravatt Monoacylglycerol lipase exerts dual control over the endocannabinoid and fatty acid pathways to support prostate cancer Chem. Biol. 18 2011 846 856
    • (2011) Chem. Biol. , vol.18 , pp. 846-856
    • Nomura, D.K.1    Lombardi, D.P.2    Chang, J.W.3    Niessen, S.4    Ward, A.M.5    Long, J.Z.6    Hoover, H.H.7    Cravatt, B.F.8
  • 77
    • 79952771931 scopus 로고    scopus 로고
    • Endocannabinoids regulate the migration of subventricular zone-derived neuroblast in the postnatal brain
    • M.J. Oudin, S. Gajendra, G. Williams, C. Hobbs, G. Lalli, and P. Doherty Endocannabinoids regulate the migration of subventricular zone-derived neuroblast in the postnatal brain J. Neurosci. 31 2011 4000 4011
    • (2011) J. Neurosci. , vol.31 , pp. 4000-4011
    • Oudin, M.J.1    Gajendra, S.2    Williams, G.3    Hobbs, C.4    Lalli, G.5    Doherty, P.6
  • 78
    • 84921023711 scopus 로고    scopus 로고
    • Comparative biochemical characterization of the monoacylglycerol lipase inhibitor KML29 in brain, spinal cord, liver, spleen, fat and muscle tissue
    • N. Pasquarelli, C. Porazik, J. Hanselmann, P. Weydt, B. Ferger, and A. Witting Comparative biochemical characterization of the monoacylglycerol lipase inhibitor KML29 in brain, spinal cord, liver, spleen, fat and muscle tissue Neuropharmacology 91 2015 148 156
    • (2015) Neuropharmacology , vol.91 , pp. 148-156
    • Pasquarelli, N.1    Porazik, C.2    Hanselmann, J.3    Weydt, P.4    Ferger, B.5    Witting, A.6
  • 82
    • 84887072489 scopus 로고    scopus 로고
    • More surprises lying ahead. the endocannabinoids keep us guessing
    • D. Piomelli More surprises lying ahead. The endocannabinoids keep us guessing Neuropharmacology 76 2014 228 234
    • (2014) Neuropharmacology , vol.76 , pp. 228-234
    • Piomelli, D.1
  • 84
    • 24944508307 scopus 로고    scopus 로고
    • Characterization of the sulfhydryl-sensitive site in the enzyme responsible for hydrolysis of 2-arachidonoyl-glycerol in rat cerebellar membranes
    • S.M. Saario, O.M.H. Salo, T. Nevalainen, A. Poso, J.T. Laitinen, T. Järivinen, and R. Niemi Characterization of the sulfhydryl-sensitive site in the enzyme responsible for hydrolysis of 2-arachidonoyl-glycerol in rat cerebellar membranes Chem. Biol. 12 2005 649 656
    • (2005) Chem. Biol. , vol.12 , pp. 649-656
    • Saario, S.M.1    Salo, O.M.H.2    Nevalainen, T.3    Poso, A.4    Laitinen, J.T.5    Järivinen, T.6    Niemi, R.7
  • 88
    • 79959977058 scopus 로고    scopus 로고
    • Enhancement of endocannabinoid signaling with JZL184, an inhibitor of the 2-arachidonoylglycerol hydrolyzing enzyme monoacylglycerol lipase, produces anxiolytic effects under conditions of high environmental aversiveness in rats
    • N.R. Sciolino, W. Zhou, and A.G. Hohmann Enhancement of endocannabinoid signaling with JZL184, an inhibitor of the 2-arachidonoylglycerol hydrolyzing enzyme monoacylglycerol lipase, produces anxiolytic effects under conditions of high environmental aversiveness in rats Pharmacol. Res. 64 2011 226 234
    • (2011) Pharmacol. Res. , vol.64 , pp. 226-234
    • Sciolino, N.R.1    Zhou, W.2    Hohmann, A.G.3
  • 89
    • 0030870722 scopus 로고    scopus 로고
    • A second endogenous cannabinoid that modulates long-term potentiation
    • N. Stella, P. Schweitzer, and D. Piomelli A second endogenous cannabinoid that modulates long-term potentiation Nature 388 1997 773 777
    • (1997) Nature , vol.388 , pp. 773-777
    • Stella, N.1    Schweitzer, P.2    Piomelli, D.3
  • 91
    • 80054728036 scopus 로고    scopus 로고
    • The design, synthesis and biological evaluation of novel URB602 analogues as potential monoacylglycerol lipase inhibitors
    • M. Szabo, M. Agostino, D.T. Malone, E. Yuriev, and B. Capuano The design, synthesis and biological evaluation of novel URB602 analogues as potential monoacylglycerol lipase inhibitors Bioorg. Med. Chem. Lett. 21 2011 6782 6787
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 6782-6787
    • Szabo, M.1    Agostino, M.2    Malone, D.T.3    Yuriev, E.4    Capuano, B.5
  • 92
    • 0017295234 scopus 로고
    • Purification and some properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose tissue
    • H. Tornqvist, and P. Belfrage Purification and some properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose tissue J. Biol. Chem. 251 1976 813 819
    • (1976) J. Biol. Chem. , vol.251 , pp. 813-819
    • Tornqvist, H.1    Belfrage, P.2
  • 94
    • 84876951107 scopus 로고    scopus 로고
    • Metabolism of endocannabinoids and related N-acylethanolamines: Canonical and alternative pathways
    • N. Ueda, K. Tsuboi, and T. Uyama Metabolism of endocannabinoids and related N-acylethanolamines: canonical and alternative pathways FEBS J. 280 2013 1874 1894
    • (2013) FEBS J. , vol.280 , pp. 1874-1894
    • Ueda, N.1    Tsuboi, K.2    Uyama, T.3
  • 95
    • 84887495462 scopus 로고    scopus 로고
    • The inhibition of 2-arachidonoyl-glycerol (2-AG) biosynthesis, rather than enhancing striatal damage, protects striatal neurons from malonate-induced death: A potential role of cyclooxygenase-2-dependent metabolism of 2-AG
    • S. Valdeolivas, M.R. Pazos, T. Bisogno, F. Piscitelli, F.A. Iannotti, M. Allarà, O. Sagredo, V. Di Marzo, and J. Fernández-Ruiz The inhibition of 2-arachidonoyl-glycerol (2-AG) biosynthesis, rather than enhancing striatal damage, protects striatal neurons from malonate-induced death: a potential role of cyclooxygenase-2-dependent metabolism of 2-AG Cell Death Dis. 17 4 2013 e862
    • (2013) Cell Death Dis. , vol.17 , Issue.4 , pp. e862
    • Valdeolivas, S.1    Pazos, M.R.2    Bisogno, T.3    Piscitelli, F.4    Iannotti, F.A.5    Allarà, M.6    Sagredo, O.7    Di Marzo, V.8    Fernández-Ruiz, J.9
  • 96
    • 84924933470 scopus 로고    scopus 로고
    • Endocannabinoids in synaptic plasticity and neuroprotection
    • Y.J. Xu, and C. Chen Endocannabinoids in synaptic plasticity and neuroprotection Neuroscientist 21 2 2015 152 168
    • (2015) Neuroscientist , vol.21 , Issue.2 , pp. 152-168
    • Xu, Y.J.1    Chen, C.2
  • 97
    • 79957510037 scopus 로고    scopus 로고
    • Monoacylglycerol lipase (MAGL) knockdown inhibits tumor cells growth in colorectal cancer
    • L. Ye, B. Zhang, E.G. Seviour, K. Tao, X. Liu, Y. Ling, J. Chen, and G. Wang Monoacylglycerol lipase (MAGL) knockdown inhibits tumor cells growth in colorectal cancer Cancer Lett. 307 2011 6 17
    • (2011) Cancer Lett. , vol.307 , pp. 6-17
    • Ye, L.1    Zhang, B.2    Seviour, E.G.3    Tao, K.4    Liu, X.5    Ling, Y.6    Chen, J.7    Wang, G.8
  • 98
    • 84908556265 scopus 로고    scopus 로고
    • Synaptic and cognitive improvements by inhibition of 2-AG metabolism are through upregulation of microRNA-188-3p in a mouse model of Alzheimer's disease
    • J. Zhang, M. Hu, Z. Teng, Y.P. Tang, and C. Chen Synaptic and cognitive improvements by inhibition of 2-AG metabolism are through upregulation of microRNA-188-3p in a mouse model of Alzheimer's disease J. Neurosci. 34 2014 14919 14933
    • (2014) J. Neurosci. , vol.34 , pp. 14919-14933
    • Zhang, J.1    Hu, M.2    Teng, Z.3    Tang, Y.P.4    Chen, C.5
  • 99
    • 49449086026 scopus 로고    scopus 로고
    • Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification
    • N. Zvonok, J. Williams, M. Johnston, L. Pandarinathan, D.R. Janero, J. Li, S.C. Krishnan, and A. Makriyannis Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification J. Proteome Res. 7 2008 2158 2164
    • (2008) J. Proteome Res. , vol.7 , pp. 2158-2164
    • Zvonok, N.1    Williams, J.2    Johnston, M.3    Pandarinathan, L.4    Janero, D.R.5    Li, J.6    Krishnan, S.C.7    Makriyannis, A.8
  • 100
    • 49449092396 scopus 로고    scopus 로고
    • Covalent inhibitors of human monoacylglycerol lipase: Ligand-assisted characterization of the catalytic site by mass spectrometry and mutational analysis
    • N. Zvonok, L. Pandarinathan, J. Williams, M. Johnston, I. Karageorgos, D.R. Janero, S.C. Krishnan, and A. Makryiannis Covalent inhibitors of human monoacylglycerol lipase: ligand-assisted characterization of the catalytic site by mass spectrometry and mutational analysis Chem. Biol. 15 2008 854 862
    • (2008) Chem. Biol. , vol.15 , pp. 854-862
    • Zvonok, N.1    Pandarinathan, L.2    Williams, J.3    Johnston, M.4    Karageorgos, I.5    Janero, D.R.6    Krishnan, S.C.7    Makryiannis, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.