메뉴 건너뛰기




Volumn 19, Issue 5, 2012, Pages 579-588

Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates

Author keywords

[No Author keywords available]

Indexed keywords

CARBAMIC ACID; ENDOCANNABINOID; ENZYME INHIBITOR; HYDROLASE INHIBITOR; JZL 184; KML 29; MONOACYLGLYCEROL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 84861635055     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.03.009     Document Type: Article
Times cited : (154)

References (40)
  • 1
    • 44849141696 scopus 로고    scopus 로고
    • Enzymatic pathways that regulate endocannabinoid signaling in the nervous system
    • K. Ahn, M.K. McKinney, and B.F. Cravatt Enzymatic pathways that regulate endocannabinoid signaling in the nervous system Chem. Rev. 108 2008 1687 1707
    • (2008) Chem. Rev. , vol.108 , pp. 1687-1707
    • Ahn, K.1    McKinney, M.K.2    Cravatt, B.F.3
  • 3
    • 27744466783 scopus 로고    scopus 로고
    • Mechanism of carbamate inactivation of FAAH: Implications for the design of covalent inhibitors and in vivo functional probes for enzymes
    • J.P. Alexander, and B.F. Cravatt Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes Chem. Biol. 12 2005 1179 1187
    • (2005) Chem. Biol. , vol.12 , pp. 1179-1187
    • Alexander, J.P.1    Cravatt, B.F.2
  • 6
    • 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
  • 9
    • 79955396596 scopus 로고    scopus 로고
    • A potent and selective inhibitor of KIAA1363/AADACL1 that impairs prostate cancer pathogenesis
    • J.W. Chang, D.K. Nomura, and B.F. Cravatt A potent and selective inhibitor of KIAA1363/AADACL1 that impairs prostate cancer pathogenesis Chem. Biol. 18 2011 476 484
    • (2011) Chem. Biol. , vol.18 , pp. 476-484
    • Chang, J.W.1    Nomura, D.K.2    Cravatt, B.F.3
  • 11
    • 58149094776 scopus 로고    scopus 로고
    • RosettaLigand docking with full ligand and receptor flexibility
    • I.W. Davis, and D. Baker RosettaLigand docking with full ligand and receptor flexibility J. Mol. Biol. 385 2009 381 392
    • (2009) J. Mol. Biol. , vol.385 , pp. 381-392
    • Davis, I.W.1    Baker, D.2
  • 12
    • 61749096176 scopus 로고    scopus 로고
    • An introduction to the endocannabinoid system: From the early to the latest concepts
    • L. De Petrocellis, and V. Di Marzo An introduction to the endocannabinoid system: from the early to the latest concepts Best Pract. Res. Clin. Endocrinol. Metab. 23 2009 1 15
    • (2009) Best Pract. Res. Clin. Endocrinol. Metab. , vol.23 , pp. 1-15
    • De Petrocellis, L.1    Di Marzo, V.2
  • 13
    • 43249100162 scopus 로고    scopus 로고
    • Targeting the endocannabinoid system: To enhance or reduce?
    • V. Di Marzo Targeting the endocannabinoid system: to enhance or reduce? Nat. Rev. Drug Discov. 7 2008 438 455
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 438-455
    • Di Marzo, V.1
  • 14
    • 67449119913 scopus 로고    scopus 로고
    • The endocannabinoid system: Its general strategy of action, tools for its pharmacological manipulation and potential therapeutic exploitation
    • V. Di Marzo The endocannabinoid system: its general strategy of action, tools for its pharmacological manipulation and potential therapeutic exploitation Pharmacol. Res. 60 2009 77 84
    • (2009) Pharmacol. Res. , vol.60 , pp. 77-84
    • Di Marzo, V.1
  • 16
    • 52949149368 scopus 로고    scopus 로고
    • "The tools of the trade" - An overview of the pharmacology of the endocannabinoid system
    • C.J. Fowler "The tools of the trade" - an overview of the pharmacology of the endocannabinoid system Curr. Pharm. Des. 14 2008 2254 2265
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 2254-2265
    • Fowler, C.J.1
  • 17
    • 63849237026 scopus 로고    scopus 로고
    • Cannabinoid receptors: A brief history and "what's hot"
    • E.S. Graham, J.C. Ashton, and M. Glass Cannabinoid receptors: a brief history and "what's hot" Front. Biosci. 14 2009 944 957
    • (2009) Front. Biosci. , vol.14 , pp. 944-957
    • Graham, E.S.1    Ashton, J.C.2    Glass, M.3
  • 18
    • 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
  • 20
    • 0035845011 scopus 로고    scopus 로고
    • Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene
    • M. Karlsson, K. Reue, Y.-R. Xia, A.J. Lusis, D. Langin, H. Tornqvist, and C. Holm Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene Gene 272 2001 11 18
    • (2001) Gene , vol.272 , pp. 11-18
    • Karlsson, M.1    Reue, K.2    Xia, Y.-R.3    Lusis, A.J.4    Langin, D.5    Tornqvist, H.6    Holm, C.7
  • 23
    • 0031767182 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and differential expression pattern of mouse lung surfactant convertase
    • S. Krishnasamy, A.L. Teng, R. Dhand, R.M. Schultz, and N.J. Gross Molecular cloning, characterization, and differential expression pattern of mouse lung surfactant convertase Am. J. Physiol. 275 1998 L969 L975
    • (1998) Am. J. Physiol. , vol.275
    • Krishnasamy, S.1    Teng, A.L.2    Dhand, R.3    Schultz, R.M.4    Gross, N.J.5
  • 25
    • 0038361307 scopus 로고    scopus 로고
    • Discovering potent and selective reversible inhibitors of enzymes in complex proteomes
    • D. Leung, C. Hardouin, D.L. Boger, and B.F. Cravatt Discovering potent and selective reversible inhibitors of enzymes in complex proteomes Nat. Biotechnol. 21 2003 687 691
    • (2003) Nat. Biotechnol. , vol.21 , pp. 687-691
    • Leung, D.1    Hardouin, C.2    Boger, D.L.3    Cravatt, B.F.4
  • 26
    • 34547789923 scopus 로고    scopus 로고
    • A functional proteomic strategy to discover inhibitors for uncharacterized hydrolases
    • W. Li, J.L. Blankman, and B.F. Cravatt A functional proteomic strategy to discover inhibitors for uncharacterized hydrolases J. Am. Chem. Soc. 129 2007 9594 9595
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9594-9595
    • Li, W.1    Blankman, J.L.2    Cravatt, B.F.3
  • 27
    • 2442510225 scopus 로고    scopus 로고
    • Mice lacking fatty acid amide hydrolase exhibit a cannabinoid receptor-mediated phenotypic hypoalgesia
    • A.H. Lichtman, C.C. Shelton, T. Advani, and B.F. Cravatt Mice lacking fatty acid amide hydrolase exhibit a cannabinoid receptor-mediated phenotypic hypoalgesia Pain 109 2004 319 327
    • (2004) Pain , vol.109 , pp. 319-327
    • Lichtman, A.H.1    Shelton, C.C.2    Advani, T.3    Cravatt, B.F.4
  • 28
    • 67649886200 scopus 로고    scopus 로고
    • From endocannabinoid profiling to 'endocannabinoid therapeutics'
    • A. Ligresti, S. Petrosino, and V. Di Marzo From endocannabinoid profiling to 'endocannabinoid therapeutics' Curr. Opin. Chem. Biol. 13 2009 321 331
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 321-331
    • Ligresti, A.1    Petrosino, S.2    Di Marzo, V.3
  • 30
    • 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
  • 32
    • 77649198453 scopus 로고    scopus 로고
    • Characterization of tunable piperidine and piperazine carbamates as inhibitors of endocannabinoid hydrolases
    • J.Z. Long, X. Jin, A. Adibekian, W. Li, and B.F. Cravatt Characterization of tunable piperidine and piperazine carbamates as inhibitors of endocannabinoid hydrolases J. Med. Chem. 53 2010 1830 1842
    • (2010) J. Med. Chem. , vol.53 , pp. 1830-1842
    • Long, J.Z.1    Jin, X.2    Adibekian, A.3    Li, W.4    Cravatt, B.F.5
  • 34
    • 84856402803 scopus 로고    scopus 로고
    • How chemoproteomics can enable drug discovery and development
    • R.E. Moellering, and B.F. Cravatt How chemoproteomics can enable drug discovery and development Chem. Biol. 19 2012 11 22
    • (2012) Chem. Biol. , vol.19 , pp. 11-22
    • Moellering, R.E.1    Cravatt, B.F.2
  • 35
    • 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.S. Hoover, S.W. 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.S.4    Ng, S.W.5    Cravatt, B.F.6
  • 36
  • 38
    • 0035469599 scopus 로고    scopus 로고
    • Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes
    • M.P. Patricelli, D.K. Giang, L.M. Stamp, and J.J. Burbaum Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes Proteomics 1 2001 1067 1071
    • (2001) Proteomics , vol.1 , pp. 1067-1071
    • Patricelli, M.P.1    Giang, D.K.2    Stamp, L.M.3    Burbaum, J.J.4
  • 40
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.