메뉴 건너뛰기




Volumn 53, Issue 4, 2010, Pages 1830-1842

Characterization of tunable piperidine and piperazine carbamates as inhibitors of endocannabinoid hydrolases

Author keywords

[No Author keywords available]

Indexed keywords

1 BENZYL 4 (HYDROXYBIS(4 METHOXYPHENYL)METHYL)PYRROLIDIN 2 ONE; 4 (DIPHENYLMETHYLENE)PIPERADINE; 4 NITROPHENYL 2,2 DIPHENYL 1 OXA 6 AZASPIROL[2.5]OCTANE 6 CARBOXYLATE; 4 NITROPHENYL 3 (HYDROXYBIS(4 METHOXYPHENYL)METHYL)PYRROLIDINE 1 CARBOXYLATE; 4 NITROPHENYL 3,3 DIPHENYLPROPYL(ETHYL)CARBAMATE; 4 NITROPHENYL 4 (4 BENZYLOXY) 2 METHOXYBENZYL)PIPERAZINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (4 METHOXYBENZYL)PIPERAZINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (BIPHENYL 2 YLMETHYL)PIPERAZINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (BIS(3,4 DIMETHOXYPHENYL)(HYDROXY)METHYL)PIPERIDINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (BIS(4 CHLOROPHENYL)(HYDROXY)METHYL)PIPERIDINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (BIS(4 DIMETHYLAMINO)PHENYL)HYDROXY)METHYL)PIPERIDINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (DIPHENYLMETHYLENE)PIPERADINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (HYDROXYBIS(2 METHOXYPHENYL)METHYL)PIPERIDINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (HYDROXYBIS(3 METHOXYPHENYL)METHYL)PIPERIDINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (HYDROXYDINAPHTHALEN 2 YLMETHYL)PIPERIDINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (HYDROXYDIPHENYLMETHYL)PIPERADINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (NAPHTHALEN 2 YLMETHYL)PIPERAZINE 1 CARBOXYLATE; 4 NITROPHENYL 4 (QUINOLIN 2 YLMETHYL)PIPERAZINE 1 CARBOXYLATE; 4 NITROPHENYL 4 BENZYLPIPERAZINE 1 CARBOXYLATE; 4 NITROPHENYL 4 BIPHENYL 4 YLMETHYL)PIPERZINE 1 CARBOXYLATE; CARBAMIC ACID DERIVATIVE; ENDOCANNABINOID; HYDROLASE INHIBITOR; PIPERAZINE; PIPERIDINE; SERINE; TERT BUTYL 4 (4 METHOXYBENZYL)PIPERAZINE 1 CARBOXYLATE; TERT BUTYL 4 HYDROXYBIS(4 METHOXYPHENYL)METHYL)PIPERADINE 1 CARBOXYLATE; TERT BUTYL 4 NAPHTHALEN 2 YLMETHYL)PIPERAZINE 1 CARBOXYLATE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 77649198453     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm9016976     Document Type: Article
Times cited : (56)

References (45)
  • 1
    • 44849141696 scopus 로고    scopus 로고
    • Enzymatic pathways that regulate endocannabinoid signaling in the nervous system
    • DOI 10.1021/cr0782067
    • Ahn, K.; McKinney, M. K.; Cravatt, B. F. Enzymatic pathways that regulate endocannabinoid signaling in the nervous system. Chem, Rev. 2008, 108, 1687-1707. (Pubitemid 351796405)
    • (2008) Chemical Reviews , vol.108 , Issue.5 , pp. 1687-1707
    • Ahn, K.1    McKinney, M.K.2    Cravatt, B.F.3
  • 2
    • 0029904838 scopus 로고    scopus 로고
    • Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid, amides
    • Cravatt, B. F.; Giang, D. K.; Mayfield, S. P.; Boger, D. L.; Lerner, R. A.; Gilula, N. B. Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid, amides. Nature 1996, 384, 83-87.
    • (1996) Nature , vol.384 , pp. 83-87
    • Cravatt, B.F.1    Giang, D.K.2    Mayfield, S.P.3    Boger, D.L.4    Lerner, R.A.5    Gilula, N.B.6
  • 6
    • 37149013708 scopus 로고    scopus 로고
    • A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid. 2-arachidonoylglycerbl
    • Blankman, J. L.; Simon, G. M.; Cravatt, B. F. A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid. 2-arachidonoylglycerbl. Chem. Biol. 2007, 14, 1347-1356.
    • (2007) Chem. Biol. , vol.14 , pp. 1347-1356
    • Blankman, J.L.1    Simon, G.M.2    Cravatt, B.F.3
  • 8
    • 67651100845 scopus 로고    scopus 로고
    • Characterization of monoacylglycerol lipase inhibition reveals differences in central and peripheral endocannabinoid metabolism
    • Long, J. Z.; Nomura, D. K.; Cravatt, B. F. Characterization of monoacylglycerol lipase inhibition reveals differences in central and peripheral endocannabinoid metabolism. Chem. Biol. 2009, 16, 744-753.
    • (2009) Chem. Biol. , vol.16 , pp. 744-753
    • Long, J.Z.1    Nomura, D.K.2    Cravatt, B.F.3
  • 13
    • 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
    • Patricelli, M. P.; Lovato, M. A.; Cravatt, B. F. Chemical and mutagenic investigations of fatty acid, amide hydrolase: evidence for a family of serine hydrolases with, distinct catalytic properties. Biochemistry 1999, 38, 9804-9812. (Pubitemid 129515316)
    • (1999) Biochemistry , vol.38 , Issue.31 , pp. 9804-9812
    • Patricelli, M.P.1    Lovato, M.A.2    Cravatt, B.F.3
  • 14
    • 0030767295 scopus 로고    scopus 로고
    • CDNA cloning, tissue distribution, and identification of the catalytic triad, of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases. and haloperoxidases
    • Karlsson, M.; Contreras, J. A.; Hellman, U.; Tornqvist, H.; Holm, C. cDNA cloning, tissue distribution, and identification of the catalytic triad, of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases. and haloperoxidases. J. Biol. Chem. 1997, 272, 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
  • 16
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: The serine hydrolases
    • Liu, Y.; Patricelli, M. P.; Cravatt, B. F. Activity-based protein profiling: the serine hydrolases. Proc. Natl. U.S.A-1999, 96, 14694-14699.
    • (1999) Proc. Natl. U.S.A , vol.96 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 17
    • 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
    • Alexander, J. P.; Cravatt, B. F. Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes. Chem. Biol. 2005, 12, 1179-1187.
    • (2005) Chem. Biol. , vol.12 , pp. 1179-1187
    • Alexander, J.P.1    Cravatt, B.F.2
  • 18
    • 12444260741 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationships of alkylcarbamic acid aryl esters, a new class of fatty acid amide hydrolase inhibitors
    • Tarzia, G.; Duranti, A.; Tontini, A.; Piersanti, G.; Mor, M.; Rivara, S.; Plazzi, P. V.; Park, C.; Kathuria, S.; Piomelli, D. Design, synthesis, and structure-activity relationships of alkylcarbamic acid aryl esters, a new class of fatty acid amide hydrolase inhibitors. J. Med. Chem. 2003, 46, 2352-2360.
    • (2003) J. Med. Chem. , vol.46 , pp. 2352-2360
    • Tarzia, G.1    Duranti, A.2    Tontini, A.3    Piersanti, G.4    Mor, M.5    Rivara, S.6    Plazzi, P.V.7    Park, C.8    Kathuria, S.9    Piomelli, D.10
  • 19
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt, B. F.; Wright, A. T.; Kozarich, J. W. Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. "Annu, Rev. Biochem. 2008, 77, 383-414.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 20
    • 33748595526 scopus 로고    scopus 로고
    • Mechanism-based profiling of enzyme families
    • Evans, M. J.; Cravatt, B. F. Mechanism-based profiling of enzyme families. Chem. Rev. 2006, 106, 3279-3301.
    • (2006) Chem. Rev. , vol.106 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 21
    • 0035469599 scopus 로고    scopus 로고
    • Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes
    • Patricelli, M. P.; Giang, D. K.; Stamp, L. M.; Burbaum, J. J. Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes. Proteomics 2001, 1, 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
  • 23
    • 34547789923 scopus 로고    scopus 로고
    • A functional proteomic strategy to discover inhibitors for uncharacterized hydrolases
    • Li, W.; Blankman, J. L.; Cravatt, B. F. A functional proteomic strategy to discover inhibitors for uncharacterized hydrolases. J Am, Chem, Soc. 2007, 129, 9594-9595.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9594-9595
    • Li, W.1    Blankman, J.L.2    Cravatt, B.F.3
  • 24
    • 55249111745 scopus 로고    scopus 로고
    • Selectivity of inhibitors of endocannabinoid biosynthesis evaluated by activity-based, protein profiling
    • Hoover, H. S.; Blankman, J. L.; Niessen, S.; Cravatt, B. F. Selectivity of inhibitors of endocannabinoid biosynthesis evaluated by activity-based, protein profiling. Bioorg. Med, Chem, Lett. 2008, 18, 5838-5841.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5838-5841
    • Hoover, H.S.1    Blankman, J.L.2    Niessen, S.3    Cravatt, B.F.4
  • 25
    • 0038361307 scopus 로고    scopus 로고
    • Discovering potent and selective reversible inhibitors of enzymes in complex proteomes
    • Leung, D.; Hardouin, C.; Boger, D. L.; Cravatt, B. F. Discovering potent and selective reversible inhibitors of enzymes in complex proteomes. Nat. Biotechnol. 2003, 21, 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
    • 64349085775 scopus 로고    scopus 로고
    • Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes
    • Bachovchin, D. A.; Brown, S. J.; Rosen, H.; Cravatt, B. F. Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes. Nat. Biotechnol. 2009, 27, 387-394.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 387-394
    • Bachovchin, D.A.1    Brown, S.J.2    Rosen, H.3    Cravatt, B.F.4
  • 27
    • 2242490907 scopus 로고    scopus 로고
    • Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling
    • Bracey, M. H.; Hanson, M. A.; Masuda, K. R.; Stevens, R. C.; Cravatt, B. F. Structural adaptations in a membrane enzyme that terminates endocannabinoid. signaling. Science 2002, 298, 1793-1796.
    • (2002) Science , vol.298 , pp. 1793-1796
    • Bracey, M.H.1    Hanson, M.A.2    Masuda, K.R.3    Stevens, R.C.4    Cravatt, B.F.5
  • 28
    • 27144449695 scopus 로고    scopus 로고
    • Designed multiple ligands. An emerging drug discovery paradigm
    • DOI 10.1021/jm058225d
    • Morphy, R.; Rankovic, Z. Designed multiple ligands. An emerging drug discovery paradigm. J. Med, Chem- 2005, 48, 6523-6543. (Pubitemid 41504710)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.21 , pp. 6523-6543
    • Morphy, R.1    Rankovic, Z.2
  • 30
    • 0028142231 scopus 로고
    • Synthesis and characterization of a biotinylated organophosphorus ester for detection and affinity purification of a brain serine esterase: Neuropathy target esterase
    • Glynn, P.; Read, D. J.; Guo, R.; Wylie, S.; Johnson, M. K. Synthesis and characterization of a biotinylated organophosphorus ester for detection and affinity purification of a brain serine esterase: neuropathy target esterase. Biochem, J. 1994, 301 (Part 2), 551-556.
    • (1994) Biochem. J. , vol.301 , Issue.PART 2 , pp. 551-556
    • Glynn, P.1    Read, D.J.2    Guo, R.3    Wylie, S.4    Johnson, M.K.5
  • 31
    • 0032524552 scopus 로고    scopus 로고
    • Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man
    • Lush, M. J.; Li, Y.; Read, D. J.; Willis, A. C.; Glynn, P. Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from, bacteria to man. Biochem. J. 1998, 332 (Part 1), 1-4. (Pubitemid 28239311)
    • (1998) Biochemical Journal , vol.332 , Issue.1 , pp. 1-4
    • Lush, M.J.1    Li, Y.2    Read, D.J.3    Willis, A.C.4    Glynn, P.5
  • 32
    • 32644447214 scopus 로고    scopus 로고
    • A mechanism for organophosphate-induced delayed, neuropathy
    • Glynn, P. A mechanism for organophosphate-induced delayed, neuropathy. Toxjcol, Lett. 2006, 162, 94-97.
    • (2006) Toxjcol. Lett. , vol.162 , pp. 94-97
    • Glynn, P.1
  • 33
    • 50649099682 scopus 로고    scopus 로고
    • Organophosphate-sensitive lipases modulate brain lysophospholipids, ether lipids and endocannabinoids
    • Casida, J. E.; Nomura, D. K.; Vose, S. C.; Fujioka, K. Organophosphate-sensitive lipases modulate brain lysophospholipids, ether lipids and endocannabinoids. Chem.-Biol. Interact. 2008, 175, 355-364.
    • (2008) Chem.Biol. Interact. , vol.175 , pp. 355-364
    • Casida, J.E.1    Nomura, D.K.2    Vose, S.C.3    Fujioka, K.4
  • 34
    • 0029557343 scopus 로고
    • Neuropathy target esterase (NTE) and organophosphorus-induced delayed polyneuropathy (OPIDP): Recent advances
    • DOI 10.1016/0378-4274(95)03495-1
    • Johnson, M. K.; Glynn, P. Neuropathy target esterase (NTE) and organophosphorus-induced delayed polyneuropathy (OPIDP): recent advances. Toxicol. Lett. 1995, 82-83, 459-463. (Pubitemid 26054736)
    • (1995) Toxicology Letters , vol.82-83 , pp. 459-463
    • Johnson, M.K.1    Glynn, P.2
  • 35
    • 70350455918 scopus 로고    scopus 로고
    • Blockade of 2-arachidonoylglycerol hydrolysis by selective monoacylglycerol lipase inhibitor 4-nitrophenyl 4-(dibenzo[d][1, 3]dioxol-5-yl(hydroxy)methyl)piperidine-1-carboxylate (JZL184) enhances retrograde endocannabinoid signaling
    • Pan, B.; Wang, W.; Long, J. Z.; Sun, D.; Hillard, C. J.; Cravatt, B. F.; Liu, Q. S. Blockade of 2-arachidonoylglycerol hydrolysis by selective monoacylglycerol lipase inhibitor 4-nitrophenyl 4-(dibenzo[d][1, 3]dioxol-5-yl(hydroxy)methyl)piperidine-1-carboxylate (JZL184) enhances retrograde endocannabinoid signaling. J. Pharmacol. Exp,Ther- 2009, 331, 591-597.
    • (2009) J. Pharmacol. Exp. Ther. , vol.331 , pp. 591-597
    • Pan, B.1    Wang, W.2    Long, J.Z.3    Sun, D.4    Hillard, C.J.5    Cravatt, B.F.6    Liu, Q.S.7
  • 36
    • 68249133858 scopus 로고    scopus 로고
    • Inhibitors of endocannabinoid-metabolizing enzymes reduce precipitated, withdrawal responses in THC-dependent mice
    • Schlosburg, J. E.; Carlson, B. L.; Ramesh, D.; Abdullah, R. A.; Long, J. Z.; Cravatt, B. F.; Lichtman, A. H. Inhibitors of endocannabinoid-metabolizing enzymes reduce precipitated, withdrawal responses in THC-dependent mice. AAPS J 2009, 11, 342-352.
    • (2009) AAPS J , vol.11 , pp. 342-352
    • Schlosburg, J.E.1    Carlson, B.L.2    Ramesh, D.3    Abdullah, R.A.4    Long, J.Z.5    Cravatt, B.F.6    Lichtman, A.H.7
  • 38
    • 73149104901 scopus 로고    scopus 로고
    • Monoacylglycerol lipase limits the duration of endocannabinoid-mediated depolarization-induced suppression of excitation in autaptic hippocampal neurons
    • Straiker, A.; Hu, S. S.; Long, J. Z.; Arnold, A.; Wager-Miller, J.; Cravatt, B. F.; Mackie, K. Monoacylglycerol lipase limits the duration of endocannabinoid-mediated depolarization-induced suppression of excitation in autaptic hippocampal neurons. MoI. Pharmacol, 2009, 76, 1220-1227.
    • (2009) MoI. Pharmacol , vol.76 , pp. 1220-1227
    • Straiker, A.1    Hu, S.S.2    Long, J.Z.3    Arnold, A.4    Wager-Miller, J.5    Cravatt, B.F.6    Mackie, K.7
  • 39
    • 73149109062 scopus 로고    scopus 로고
    • Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
    • Nomura, D. K.; Long, J. Z.; Niessen, S.; Hoover, H. S.; Ng, S.-W.; Cravatt, B. F. Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis. Cell 2010, 140, 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
  • 40
    • 76649126721 scopus 로고    scopus 로고
    • Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling
    • DOI:10.1002/cbic.200900621
    • Labar, G.; Bauvois, C.; Borel, F.; Ferrer, J. L.; Wouters, J.; Lambert, D. M. Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling. ChemBioChem 2009, DOI:10.1002/cbic.200900621.
    • (2009) ChemBioChem
    • Labar, G.1    Bauvois, C.2    Borel, F.3    Ferrer, J.L.4    Wouters, J.5    Lambert, D.M.6
  • 42
    • 71749101672 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of piperazinyl carbamates and ureas as fatty acid amide hydrolase (FAAH) and, transient receptor potential (TRP) channel dual ligands
    • Morera, E.; De Petrocelhs, L.; Morera, L.; Moriello, A. S.; Ligresti, A.; Nalli, M.; Woodward, D. F.; Di Marzo, V.; Ortar, G. Synthesis and biological evaluation of piperazinyl carbamates and ureas as fatty acid amide hydrolase (FAAH) and, transient receptor potential (TRP) channel dual ligands. Bioorz. Med. Chem. Lett. 2009, 19, 6806-6809.
    • (2009) Bioorz. Med. Chem. Lett. , vol.19 , pp. 6806-6809
    • Morera, E.1    De Petrocelhs, L.2    Morera, L.3    Moriello, A.S.4    Ligresti, A.5    Nalli, M.6    Woodward, D.F.7    Di Marzo, V.8    Ortar, G.9
  • 44
    • 33746657575 scopus 로고    scopus 로고
    • A FAAH-regulated class Class of N- Acyl taurines that activates TRP ion channels
    • Saghatelian, A.; McKinney, M. K.; Bandell, M.; Patapoutian, A.; Cravatt, B. F. A. FAAH-regulated class Class of N- acyl taurines that activates TRP ion channels. Biochemistry 2006, 45, 9007-9015.
    • (2006) Biochemistry , vol.45 , pp. 9007-9015
    • Saghatelian, A.1    McKinney, M.K.2    Bandell, M.3    Patapoutian, A.4    Cravatt, B.F.5
  • 45
    • 0035845011 scopus 로고    scopus 로고
    • Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene
    • DOI 10.1016/S0378-1119(01)00559-5, PII S0378111901005595
    • Karlsson, M.; Reue, K.; Xia, Y. R.; Lusis, A. J.; Langin, D.; Tornqvist, H.; Holm, C. Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene. Gene 2001, 272, 11-18. (Pubitemid 32695393)
    • (2001) Gene , vol.272 , Issue.1-2 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.