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Volumn 8, Issue 7, 2013, Pages 1590-1599

Proteome-wide reactivity profiling identifies diverse carbamate chemotypes tuned for serine hydrolase inhibition

Author keywords

[No Author keywords available]

Indexed keywords

ACYLGLYCEROL LIPASE; ALPHA BETA HYDROLASE 6; CARBAMIC ACID; CARBAMIC ACID DERIVATIVE; ENDOCANNABINOID; HYDROLASE; O ARYL CARBAMATE; O HEXAFLUOROISOPROPYL CARBAMATE; O N HYDROXYSUCCINIMIDYL CARBAMATE; PROTEOME; SERINE; UNCLASSIFIED DRUG;

EID: 84880517778     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb400261h     Document Type: Article
Times cited : (102)

References (61)
  • 1
    • 80054054097 scopus 로고    scopus 로고
    • The metabolic serine hydrolases and their functions in mammalian physiology and disease
    • Long, J. Z. and Cravatt, B. F. (2011) The metabolic serine hydrolases and their functions in mammalian physiology and disease Chem. Rev. 111, 6022-6063
    • (2011) Chem. Rev. , vol.111 , pp. 6022-6063
    • Long, J.Z.1    Cravatt, B.F.2
  • 2
    • 33746891446 scopus 로고    scopus 로고
    • Penicillin binding proteins: Key players in bacterial cell cycle and drug resistance processes
    • Macheboeuf, P., Contreras-Martel, C., Job, V., Dideberg, O., and Dessen, A. (2006) Penicillin binding proteins: key players in bacterial cell cycle and drug resistance processes FEMS Microbiol. Rev. 30, 673-691
    • (2006) FEMS Microbiol. Rev. , vol.30 , pp. 673-691
    • Macheboeuf, P.1    Contreras-Martel, C.2    Job, V.3    Dideberg, O.4    Dessen, A.5
  • 3
    • 80051687993 scopus 로고    scopus 로고
    • New hepatitis C therapies in clinical development
    • Vermehren, J. and Sarrazin, C. (2011) New hepatitis C therapies in clinical development Eur. J. Med. Res. 16, 303-314
    • (2011) Eur. J. Med. Res. , vol.16 , pp. 303-314
    • Vermehren, J.1    Sarrazin, C.2
  • 5
    • 33847736584 scopus 로고    scopus 로고
    • Human pancreatic digestive enzymes
    • Whitcomb, D. C. and Lowe, M. E. (2007) Human pancreatic digestive enzymes Dig. Dis. Sci. 52, 1-17
    • (2007) Dig. Dis. Sci. , vol.52 , pp. 1-17
    • Whitcomb, D.C.1    Lowe, M.E.2
  • 6
    • 0026704502 scopus 로고
    • Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs
    • Bongers, J., Lambros, T., Ahmad, M., and Heimer, E. P. (1992) Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs Biochim. Biophys. Acta 1122, 147-153
    • (1992) Biochim. Biophys. Acta , vol.1122 , pp. 147-153
    • Bongers, J.1    Lambros, T.2    Ahmad, M.3    Heimer, E.P.4
  • 7
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • Davie, E. W. and Ratnoff, O. D. (1964) Waterfall sequence for intrinsic blood clotting Science 145, 1310-1312
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 8
    • 30344485665 scopus 로고    scopus 로고
    • Targeting acetylcholinesterase and butyrylcholinesterase in dementia
    • Lane, R. M., Potkin, S. G., and Enz, A. (2006) Targeting acetylcholinesterase and butyrylcholinesterase in dementia Int. J. Neuropsychopharmacol. 9, 101-124
    • (2006) Int. J. Neuropsychopharmacol. , vol.9 , pp. 101-124
    • Lane, R.M.1    Potkin, S.G.2    Enz, A.3
  • 9
    • 44849141696 scopus 로고    scopus 로고
    • Enzymatic pathways that regulate endocannabinoid signaling in the nervous system
    • Ahn, K., McKinney, M. K., and Cravatt, B. F. (2008) Enzymatic pathways that regulate endocannabinoid signaling in the nervous system Chem. Rev. 108, 1687-1707
    • (2008) Chem. Rev. , vol.108 , pp. 1687-1707
    • Ahn, K.1    McKinney, M.K.2    Cravatt, B.F.3
  • 10
    • 28244502153 scopus 로고    scopus 로고
    • The use of orlistat in the treatment of obesity, dyslipidaemia, and Type 2 diabetes
    • Nelson, R. H. and Miles, J. M. (2005) The use of orlistat in the treatment of obesity, dyslipidaemia, and Type 2 diabetes Expert Opin. Pharmacother. 6, 2483-2491
    • (2005) Expert Opin. Pharmacother. , vol.6 , pp. 2483-2491
    • Nelson, R.H.1    Miles, J.M.2
  • 11
    • 33947690115 scopus 로고    scopus 로고
    • Discovery of JANUVIA (Sitagliptin), a selective dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes
    • Thornberry, N. A. and Weber, A. E. (2007) Discovery of JANUVIA (Sitagliptin), a selective dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes Curr. Top. Med. Chem. 7, 557-568
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 557-568
    • Thornberry, N.A.1    Weber, A.E.2
  • 12
    • 84859174317 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors for treatment of type 2 diabetes mellitus in the clinical setting: Systematic review and meta-analysis
    • 10.1136/bmj.e1369
    • Karagiannis, T., Paschos, P., Paletas, K., Matthews, D. R., and Tsapas, A. (2012) Dipeptidyl peptidase-4 inhibitors for treatment of type 2 diabetes mellitus in the clinical setting: systematic review and meta-analysis BMJ 344 10.1136/bmj.e1369
    • (2012) BMJ , vol.344
    • Karagiannis, T.1    Paschos, P.2    Paletas, K.3    Matthews, D.R.4    Tsapas, A.5
  • 13
    • 80053971718 scopus 로고    scopus 로고
    • Current and emerging drug treatment options for Alzheimer's disease: A systematic review
    • Herrmann, N., Chau, S. A., Kircanski, I., and Lanctoît, K. L. (2011) Current and emerging drug treatment options for Alzheimer's disease: A systematic review Drugs 71, 2031-2065
    • (2011) Drugs , vol.71 , pp. 2031-2065
    • Herrmann, N.1    Chau, S.A.2    Kircanski, I.3    Lanctoît, K.L.4
  • 14
    • 77952542136 scopus 로고    scopus 로고
    • Acylating drugs: Redesigning natural covalent inhibitors
    • Kluge, A. F. and Petter, R. C. (2010) Acylating drugs: Redesigning natural covalent inhibitors Curr. Opin. Chem. Biol. 14, 421-427
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 421-427
    • Kluge, A.F.1    Petter, R.C.2
  • 15
    • 84855414065 scopus 로고    scopus 로고
    • The pharmacological landscape and therapeutic potential of serine hydrolases
    • Bachovchin, D. A. and Cravatt, B. F. (2012) The pharmacological landscape and therapeutic potential of serine hydrolases Nat. Rev. Drug Discov. 11, 52-68
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 52-68
    • Bachovchin, D.A.1    Cravatt, B.F.2
  • 16
    • 84856402803 scopus 로고    scopus 로고
    • How chemoproteomics can enable drug discovery and development
    • Moellering, R. E. and Cravatt, B. F. (2012) How chemoproteomics can enable drug discovery and development Chem. Biol. 19, 11-22
    • (2012) Chem. Biol. , vol.19 , pp. 11-22
    • Moellering, R.E.1    Cravatt, B.F.2
  • 17
    • 77953631133 scopus 로고    scopus 로고
    • Strategies for discovering and derisking covalent, irreversible enzyme inhibitors
    • Johnson, D. S., Weerapana, E., and Cravatt, B. F. (2010) Strategies for discovering and derisking covalent, irreversible enzyme inhibitors Future Med. Chem. 2, 949-964
    • (2010) Future Med. Chem. , vol.2 , pp. 949-964
    • Johnson, D.S.1    Weerapana, E.2    Cravatt, B.F.3
  • 20
    • 11144245547 scopus 로고    scopus 로고
    • Activity-based protein profiling: Applications to biomarker discovery, in vivo imaging and drug discovery
    • Berger, A. B., Vitorino, P. M., and Bogyo, M. (2004) Activity-based protein profiling: Applications to biomarker discovery, in vivo imaging and drug discovery Am. J. PharmacoGenomics 4, 371-381
    • (2004) Am. J. PharmacoGenomics , vol.4 , pp. 371-381
    • Berger, A.B.1    Vitorino, P.M.2    Bogyo, M.3
  • 21
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt, B. F., Wright, A. T., and Kozarich, J. W. (2008) Activity-based protein profiling: From enzyme chemistry to proteomic chemistry Annu. Rev. Biochem. 77, 383-414
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 22
    • 84875428718 scopus 로고    scopus 로고
    • Determining target engagement in living systems
    • Simon, G. M., Niphakis, M. J., and Cravatt, B. F. (2013) Determining target engagement in living systems Nat. Chem. Biol. 9, 200-205
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 200-205
    • Simon, G.M.1    Niphakis, M.J.2    Cravatt, B.F.3
  • 23
    • 0032516463 scopus 로고    scopus 로고
    • Mechanism of inhibition of LDL phospholipase A(2) by monocyclic-beta- lactams. Burst kinetics and the effect of stereochemistry
    • Tew, D. G., Boyd, H. F., Ashman, S., Theobald, C., and Leach, C. A. (1998) Mechanism of inhibition of LDL phospholipase A(2) by monocyclic-beta- lactams. Burst kinetics and the effect of stereochemistry Biochemistry 37, 10087-10093
    • (1998) Biochemistry , vol.37 , pp. 10087-10093
    • Tew, D.G.1    Boyd, H.F.2    Ashman, S.3    Theobald, C.4    Leach, C.A.5
  • 25
    • 47149092981 scopus 로고    scopus 로고
    • Beta-lactones as privileged structures for the active-site labeling of versatile bacterial enzyme classes
    • Bottcher, T. and Sieber, S. A. (2008) Beta-lactones as privileged structures for the active-site labeling of versatile bacterial enzyme classes Angew. Chem., Int. Ed. Engl. 47, 4600-4603
    • (2008) Angew. Chem., Int. Ed. Engl. , vol.47 , pp. 4600-4603
    • Bottcher, T.1    Sieber, S.A.2
  • 30
    • 80053004364 scopus 로고    scopus 로고
    • Structural alert/reactive metabolite concept as applied in medicinal chemistry to mitigate the risk of idiosyncratic drug toxicity: A perspective based on the critical examination of trends in the top 200 drugs marketed in the United States
    • Stepan, A., Walker, D., Bauman, J., Price, D., Baillie, T., Kalgutkar, A., and Aleo, M. (2011) Structural alert/reactive metabolite concept as applied in medicinal chemistry to mitigate the risk of idiosyncratic drug toxicity: a perspective based on the critical examination of trends in the top 200 drugs marketed in the United States Chem. Res. Toxicol. 24, 1345-1755
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1345-1755
    • Stepan, A.1    Walker, D.2    Bauman, J.3    Price, D.4    Baillie, T.5    Kalgutkar, A.6    Aleo, M.7
  • 32
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • Kidd, D., Liu, Y., and Cravatt, B. F. (2001) Profiling serine hydrolase activities in complex proteomes Biochemistry 40, 4005-4015
    • (2001) Biochemistry , vol.40 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 33
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • Speers, A. E., Adam, G. C., and Cravatt, B. F. (2003) Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition J. Am. Chem. Soc. 125, 4686-4687
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 34
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A. E. and Cravatt, B. F. (2004) Profiling enzyme activities in vivo using click chemistry methods Chem. Biol. 11, 535-546
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 35
    • 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. and Cravatt, B. F. (2005) Mechanism of carbamate inactivation of FAAH: Implications for the design of covalent inhibitors and in vivo functional probes for enzymes Chem. Biol. 12, 1179-1187
    • (2005) Chem. Biol. , vol.12 , pp. 1179-1187
    • Alexander, J.P.1    Cravatt, B.F.2
  • 38
    • 84862091237 scopus 로고    scopus 로고
    • O-hydroxyacetamide carbamates as a highly potent and selective class of endocannabinoid hydrolase inhibitors
    • Niphakis, M. J., Johnson, D. S., Ballard, T. E., Stiff, C., and Cravatt, B. F. (2012) O-hydroxyacetamide carbamates as a highly potent and selective class of endocannabinoid hydrolase inhibitors ACS Chem. Neurosci. 3, 418-426
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 418-426
    • Niphakis, M.J.1    Johnson, D.S.2    Ballard, T.E.3    Stiff, C.4    Cravatt, B.F.5
  • 39
    • 84874652001 scopus 로고    scopus 로고
    • Therapeutic potential of monoacylglycerol lipase inhibitors
    • Mulvihill, M. M. and Nomura, D. K. (2012) Therapeutic potential of monoacylglycerol lipase inhibitors Life Sci. 92, 492-497
    • (2012) Life Sci. , vol.92 , pp. 492-497
    • Mulvihill, M.M.1    Nomura, D.K.2
  • 41
    • 84870412999 scopus 로고    scopus 로고
    • Monoacylglycerol lipase is a therapeutic target for Alzheimer's disease
    • Chen, R., Zhang, J., Wu, Y., Wang, D., Feng, G., Tang, Y.-P., Teng, Z., and Chen, C. (2012) Monoacylglycerol lipase is a therapeutic target for Alzheimer's disease Cell Rep. 2, 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
  • 43
    • 84862742406 scopus 로고    scopus 로고
    • Monoacylglycerol lipase - A target for drug development?
    • Fowler, C. J. (2012) Monoacylglycerol lipase-A target for drug development? Br. J. Pharmacol. 166, 1568-1585
    • (2012) Br. J. Pharmacol. , vol.166 , pp. 1568-1585
    • Fowler, C.J.1
  • 44
    • 77649198453 scopus 로고    scopus 로고
    • Characterization of tunable piperidine and piperazine carbamates as inhibitors of endocannabinoid hydrolases
    • Long, J. Z., Jin, X., Adibekian, A., Li, W., and Cravatt, B. F. (2010) Characterization of tunable piperidine and piperazine carbamates as inhibitors of endocannabinoid hydrolases J. Med. Chem. 53, 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
  • 46
    • 0035469599 scopus 로고    scopus 로고
    • Direct visualization of serine hydrolase activities in complex proteome using fluorescent active site-directed probes
    • Patricelli, M. P., Giang, D. K., Stamp, L. M., and Burbaum, J. J. (2001) Direct visualization of serine hydrolase activities in complex proteome using fluorescent active site-directed probes Proteomics 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
  • 48
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • Rostovtsev, V. V., Green, J. G., Fokin, V. V., and Sharpless, K. B. (2002) A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes Angew. Chem., Int. Ed. Engl. 41, 2596-2599
    • (2002) Angew. Chem., Int. Ed. Engl. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, J.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 49
    • 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.-J., Long, J. Z., Arnold, A., Wager-Miller, J., Cravatt, B. F., and Mackie, K. (2009) Monoacylglycerol lipase limits the duration of endocannabinoid-mediated depolarization-induced suppression of excitation in autaptic hippocampal neurons Mol. Pharmacol. 76, 1220-1227
    • (2009) Mol. Pharmacol. , vol.76 , pp. 1220-1227
    • Straiker, A.1    Hu, S.S.-J.2    Long, J.Z.3    Arnold, A.4    Wager-Miller, J.5    Cravatt, B.F.6    Mackie, K.7
  • 51
    • 84856004739 scopus 로고    scopus 로고
    • An activity-based imaging probe for the integral membrane hydrolase KIAA1363
    • Chang, J. W., Moellering, R. E., and Cravatt, B. F. (2012) An activity-based imaging probe for the integral membrane hydrolase KIAA1363 Angew. Chem., Int. Ed. 51, 966-970
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 966-970
    • Chang, J.W.1    Moellering, R.E.2    Cravatt, B.F.3
  • 54
    • 84870373692 scopus 로고    scopus 로고
    • DAGLβ inhibition perturbs a lipid network involved in macrophage inflammatory responses
    • Hsu, K.-L., Tsuboi, K., Adibekian, A., Pugh, H., Masuda, K., and Cravatt, B. F. (2012) DAGLβ inhibition perturbs a lipid network involved in macrophage inflammatory responses Nat. Chem. Biol. 8, 999-1007
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 999-1007
    • Hsu, K.-L.1    Tsuboi, K.2    Adibekian, A.3    Pugh, H.4    Masuda, K.5    Cravatt, B.F.6
  • 55
    • 79960939546 scopus 로고    scopus 로고
    • Monoacylglycerol lipase exerts dual control over endocannabinoid and fatty acid pathways to support prostate cancer
    • Nomura, D. K., Lombardi, D. P., Chang, J. W., Niessen, S., Ward, A. M., Long, J. Z., Hoover, H. H., and Cravatt, B. F. (2011) Monoacylglycerol lipase exerts dual control over endocannabinoid and fatty acid pathways to support prostate cancer Chem. Biol. 18, 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
  • 57
    • 34548666006 scopus 로고    scopus 로고
    • Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes
    • Blum, G., von Degenfeld, G., Merchant, M. J., Blau, H. M., and Bogyo, M. (2007) Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes Nat. Chem. Biol. 3, 668-677
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 668-677
    • Blum, G.1    Von Degenfeld, G.2    Merchant, M.J.3    Blau, H.M.4    Bogyo, M.5
  • 61
    • 84867581006 scopus 로고    scopus 로고
    • Development and characterization of endocannabinoid hydrolases FAAH and MAGL inhibitors bearing a benzotriazol-1-yl carboxamide scaffold
    • Morera, L., Labar, G., Ortar, G., and Lambert, D. M. (2012) Development and characterization of endocannabinoid hydrolases FAAH and MAGL inhibitors bearing a benzotriazol-1-yl carboxamide scaffold Bioorg. Med. Chem. 20, 6260-6275
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 6260-6225
    • Morera, L.1    Labar, G.2    Ortar, G.3    Lambert, D.M.4


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