메뉴 건너뛰기




Volumn 203, Issue 1, 2013, Pages 231-237

Organophosphorus compound esterase profiles as predictors of therapeutic and toxic effects

Author keywords

Acetylcholinesterase (AChE); Butyrylcholinesterase (BChE); Carboxylesterase (CaE); Neuropathy target esterase (NTE); Organophosphorus compounds (OPCs); Quantitative structure activity relationships (QSAR)

Indexed keywords

ACETYLCHOLINESTERASE; CARBOXYLESTERASE; CHOLINESTERASE; NEUROTOXIC ESTERASE; ORGANOPHOSPHORUS COMPOUND; SERINE PROTEINASE;

EID: 84875813602     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2012.10.012     Document Type: Conference Paper
Times cited : (69)

References (49)
  • 1
    • 0346763979 scopus 로고    scopus 로고
    • "Esterase profiles" of O,O-dialkyl-O-dimethylchloroformimino phosphates in prediction of their toxic effects
    • G. Makhaeva, I. Filonenko, S. Fomicheva, and V. Malygin "Esterase profiles" of O,O-dialkyl-O-dimethylchloroformimino phosphates in prediction of their toxic effects Toxicol. Lett. 88 Suppl. 1 1996 25
    • (1996) Toxicol. Lett. , vol.88 , Issue.SUPPL. 1 , pp. 25
    • Makhaeva, G.1    Filonenko, I.2    Fomicheva, S.3    Malygin, V.4
  • 4
    • 84869424768 scopus 로고    scopus 로고
    • Combined QSAR studies of inhibitor properties of O-phosphorylated oximes toward serine esterases involved in neurotoxicity, drug metabolism and Alzheimer's disease
    • G.F. Makhaeva, E.V. Radchenko, I.I. Baskin, V.A. Palyulin, R.J. Richardson, and N.S. Zefirov Combined QSAR studies of inhibitor properties of O-phosphorylated oximes toward serine esterases involved in neurotoxicity, drug metabolism and Alzheimer's disease SAR QSAR Environ. Res. 23 2012 627 647
    • (2012) SAR QSAR Environ. Res. , vol.23 , pp. 627-647
    • Makhaeva, G.F.1    Radchenko, E.V.2    Baskin, I.I.3    Palyulin, V.A.4    Richardson, R.J.5    Zefirov, N.S.6
  • 5
    • 85012849914 scopus 로고    scopus 로고
    • Anticholinesterase insecticides
    • C.A. McQueen, Academic Press/Elsevier Oxford
    • R.J. Richardson Anticholinesterase insecticides C.A. McQueen, Comprehensive Toxicology vol. 13 2010 Academic Press/Elsevier Oxford 433 444
    • (2010) Comprehensive Toxicology , vol.13 VOL. , pp. 433-444
    • Richardson, R.J.1
  • 8
    • 0013300287 scopus 로고    scopus 로고
    • Carboxylesterase: Specificity and spontaneous reactivation of an endogenous scavenger for organophosphorus compounds
    • D.M. Maxwell, and K.M. Brecht Carboxylesterase: specificity and spontaneous reactivation of an endogenous scavenger for organophosphorus compounds J. Appl. Toxicol. 21 Suppl. 1 2001 S103 S107
    • (2001) J. Appl. Toxicol. , vol.21 , Issue.SUPPL. 1
    • Maxwell, D.M.1    Brecht, K.M.2
  • 9
    • 75549088598 scopus 로고    scopus 로고
    • Butyrylcholinesterase for protection from organophosphorus poisons: Catalytic complexities and hysteretic behavior
    • P. Masson, and O. Lockridge Butyrylcholinesterase for protection from organophosphorus poisons: catalytic complexities and hysteretic behavior Arch. Biochem. Biophys. 494 2010 107 120
    • (2010) Arch. Biochem. Biophys. , vol.494 , pp. 107-120
    • Masson, P.1    Lockridge, O.2
  • 10
    • 33645958909 scopus 로고    scopus 로고
    • Carboxylesterases-detoxifying enzymes and targets for drug therapy
    • P.M. Potter, and R.M. Wadkins Carboxylesterases-detoxifying enzymes and targets for drug therapy Curr. Med. Chem. 13 2006 1045 1054
    • (2006) Curr. Med. Chem. , vol.13 , pp. 1045-1054
    • Potter, P.M.1    Wadkins, R.M.2
  • 12
    • 30344485665 scopus 로고    scopus 로고
    • Targeting acetylcholinesterase and butyrylcholinesterase in dementia
    • R.M. Lane, S.G. Potkin, and A. Enz Targeting acetylcholinesterase and butyrylcholinesterase in dementia Int. J. Neuropsychopharmacol. 9 2006 101 124
    • (2006) Int. J. Neuropsychopharmacol. , vol.9 , pp. 101-124
    • Lane, R.M.1    Potkin, S.G.2    Enz, A.3
  • 13
    • 40849092901 scopus 로고    scopus 로고
    • Modeling of the relationships between the structure of O-phosphorylated oximes and their anticholinesterase activity and selectivity using molecular field topology analysis (MFTA)
    • E.V. Radchenko, G.F. Makhaeva, V.V. Malygin, V.B. Sokolov, V.A. Palyulin, and N.S. Zefirov Modeling of the relationships between the structure of O-phosphorylated oximes and their anticholinesterase activity and selectivity using molecular field topology analysis (MFTA) Dokl. Biochem. Biophys. 418 2008 47 51
    • (2008) Dokl. Biochem. Biophys. , vol.418 , pp. 47-51
    • Radchenko, E.V.1    Makhaeva, G.F.2    Malygin, V.V.3    Sokolov, V.B.4    Palyulin, V.A.5    Zefirov, N.S.6
  • 14
    • 72249119078 scopus 로고    scopus 로고
    • Study of the structural determinants of acute and delayed neurotoxicity of O-phosphorylated oximes by molecular field topology analysis (MFTA)
    • E.V. Radchenko, G.F. Makhaeva, V.B. Sokolov, V.A. Palyulin, and N.S. Zefirov Study of the structural determinants of acute and delayed neurotoxicity of O-phosphorylated oximes by molecular field topology analysis (MFTA) Dokl. Biochem. Biophys. 429 2009 309 314
    • (2009) Dokl. Biochem. Biophys. , vol.429 , pp. 309-314
    • Radchenko, E.V.1    Makhaeva, G.F.2    Sokolov, V.B.3    Palyulin, V.A.4    Zefirov, N.S.5
  • 15
    • 0018076889 scopus 로고
    • Neurotoxicity of organophosphorus pesticides: Predictions can be based on in vitro studies with hen and human enzymes
    • M. Lotti, and M.K. Johnson Neurotoxicity of organophosphorus pesticides: predictions can be based on in vitro studies with hen and human enzymes Arch. Toxicol. 41 1978 215 221
    • (1978) Arch. Toxicol. , vol.41 , pp. 215-221
    • Lotti, M.1    Johnson, M.K.2
  • 16
    • 0037432753 scopus 로고    scopus 로고
    • Quantitative structure-activity relationships predict the delayed neurotoxicity potential of a series of O-alkyl-O-methylchloroformino phenylphosphonates
    • V.V. Malygin, V.B. Sokolov, R.J. Richardson, and G.F. Makhaeva Quantitative structure-activity relationships predict the delayed neurotoxicity potential of a series of O-alkyl-O-methylchloroformino phenylphosphonates J. Toxicol. Environ. Health, Part A 66 2003 611 625
    • (2003) J. Toxicol. Environ. Health, Part A , vol.66 , pp. 611-625
    • Malygin, V.V.1    Sokolov, V.B.2    Richardson, R.J.3    Makhaeva, G.F.4
  • 17
    • 14644422580 scopus 로고    scopus 로고
    • Mammalian carboxylesterases: From drug targets to protein therapeutics
    • M.R. Redinbo, and P.M. Potter Mammalian carboxylesterases: from drug targets to protein therapeutics Drug Discovery Today 10 2005 313 325
    • (2005) Drug Discovery Today , vol.10 , pp. 313-325
    • Redinbo, M.R.1    Potter, P.M.2
  • 19
    • 0033040546 scopus 로고    scopus 로고
    • A stable preparation of hen brain neuropathy target esterase for rapid biochemical assessment of neurotoxic potential of organophosphates
    • G.F. Makhaeva, and V.V. Malygin A stable preparation of hen brain neuropathy target esterase for rapid biochemical assessment of neurotoxic potential of organophosphates Chem. Biol. Interact. 119-120 1999 551 557
    • (1999) Chem. Biol. Interact. , vol.119-120 , pp. 551-557
    • Makhaeva, G.F.1    Malygin, V.V.2
  • 21
    • 0026000701 scopus 로고
    • The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26
    • P.W. Allderdice, H.A.R. Gardner, D. Galutira, O. Lockridge, and B.N. LaDu The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26 Genomics 11 1991 452 454
    • (1991) Genomics , vol.11 , pp. 452-454
    • Allderdice, P.W.1    Gardner, H.A.R.2    Galutira, D.3    Lockridge, O.4    Ladu, B.N.5
  • 22
    • 84860642795 scopus 로고    scopus 로고
    • NTE and non-NTE esterases in brain membrane: Kinetic characterization with organophosphates
    • I. Mangas, E. Vilanova, and J. Estévez NTE and non-NTE esterases in brain membrane: kinetic characterization with organophosphates Toxicology 297 2012 17 25
    • (2012) Toxicology , vol.297 , pp. 17-25
    • Mangas, I.1    Vilanova, E.2    Estévez, J.3
  • 23
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: From molecules to functions
    • T. Satoh, and M. Hosokawa The mammalian carboxylesterases: from molecules to functions Annu. Rev. Pharmacol. Toxicol. 38 1998 257 288
    • (1998) Annu. Rev. Pharmacol. Toxicol. , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 24
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
    • B. Li, M. Sedlacek, I. Manoharan, R. Boopathy, E.G. Duysen, P. Masson, and O. Lockridge Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma Biochem. Pharmacol. 70 2005 1673 1684
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 1673-1684
    • Li, B.1    Sedlacek, M.2    Manoharan, I.3    Boopathy, R.4    Duysen, E.G.5    Masson, P.6    Lockridge, O.7
  • 26
    • 84875805371 scopus 로고    scopus 로고
    • A biochemical model in mice for assessment of neuropathic potential of organophosphorus compounds
    • (in press) (Russian)
    • E.V. Rudakova, O.G. Serebryakova, N.P. Boltneva, T.G. Galenko, G.F. Makhaeva, A biochemical model in mice for assessment of neuropathic potential of organophosphorus compounds, Toxicol. Rev. (in press) (Russian).
    • Toxicol. Rev.
    • Rudakova, E.V.1    Serebryakova, O.G.2    Boltneva, N.P.3    Galenko, T.G.4    Makhaeva, G.F.5
  • 29
    • 0031690145 scopus 로고    scopus 로고
    • Comparative studies of O,O-dialkyl-O-chloromethylchloroformimino phosphates: Interaction with neuropathy target esterase and acetylcholinesterase
    • G.F. Makhaeva, I.V. Filonenko, V.L. Yankovskaya, S.B. Fomicheva, and V.V. Malygin Comparative studies of O,O-dialkyl-O-chloromethylchloroformimino phosphates: interaction with neuropathy target esterase and acetylcholinesterase Neurotoxicology 19 1998 623 628
    • (1998) Neurotoxicology , vol.19 , pp. 623-628
    • Makhaeva, G.F.1    Filonenko, I.V.2    Yankovskaya, V.L.3    Fomicheva, S.B.4    Malygin, V.V.5
  • 32
    • 34249970757 scopus 로고
    • Synthesis and antiesteratic activity of O,O-dialkyl-S- carboethoxychloromethylthiol phosphates
    • (Translated from Izvestiya Akademii Nauk SSSR, Seriya Khimicheskaya, No. 12, pp. 2741-2746, 1989)
    • B.A. Khaskin, G.F. Makhaeva, N.A. Torgasheva, A.S. Ishmuratov, V.L. Yankovskaya, V.I. Fetisov, V.V. Malygin, and I.V. Martynov Synthesis and antiesteratic activity of O,O-dialkyl-S-carboethoxychloromethylthiol phosphates Russ. Chem. Bull. 38 1989 2508 2512 (Translated from Izvestiya Akademii Nauk SSSR, Seriya Khimicheskaya, No. 12, pp. 2741-2746, 1989)
    • (1989) Russ. Chem. Bull. , vol.38 , pp. 2508-2512
    • Khaskin, B.A.1    Makhaeva, G.F.2    Torgasheva, N.A.3    Ishmuratov, A.S.4    Yankovskaya, V.L.5    Fetisov, V.I.6    Malygin, V.V.7    Martynov, I.V.8
  • 33
    • 27544436925 scopus 로고
    • Reaction of dialkoxyphosphoryl- and thiophosphorylsulfenyl bromides with diazo compounds
    • (Russian), 989-993 (Engl)
    • B.A. Khaskin, N.A. Torgasheva, and A.S. Ishmuratov Reaction of dialkoxyphosphoryl- and thiophosphorylsulfenyl bromides with diazo compounds J. Gen. Chem. USSR (Engl. Transl.) 61 1991 1090 1095 (Russian), 989-993 (Engl)
    • (1991) J. Gen. Chem. USSR (Engl. Transl.) , vol.61 , pp. 1090-1095
    • Khaskin, B.A.1    Torgasheva, N.A.2    Ishmuratov, A.S.3
  • 34
    • 69949107722 scopus 로고    scopus 로고
    • Synthesis of organophosphates with fluorine-containing leaving groups as serine esterase inhibitors with potential for Alzheimer disease therapeutics
    • G.F. Makhaeva, A.Y. Aksinenko, V.B. Sokolov, O.G. Serebryakova, and R.J. Richardson Synthesis of organophosphates with fluorine-containing leaving groups as serine esterase inhibitors with potential for Alzheimer disease therapeutics Bioorg. Med. Chem. Lett. 19 2009 5528 5530
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5528-5530
    • Makhaeva, G.F.1    Aksinenko, A.Y.2    Sokolov, V.B.3    Serebryakova, O.G.4    Richardson, R.J.5
  • 35
    • 77955903675 scopus 로고    scopus 로고
    • Synthesis of O-phosphorylated 1-substituted 2,2,2-trifluoroethanols, serine hydrolase inhibitors
    • A.Yu. Aksinenko, V.B. Sokolov, T.V. Goreva, and G.F. Makhaeva Synthesis of O-phosphorylated 1-substituted 2,2,2-trifluoroethanols, serine hydrolase inhibitors Russ. Chem. Bull. 59 2010 102 106
    • (2010) Russ. Chem. Bull. , vol.59 , pp. 102-106
    • Aksinenko, A.Yu.1    Sokolov, V.B.2    Goreva, T.V.3    Makhaeva, G.F.4
  • 39
    • 0001358063 scopus 로고    scopus 로고
    • Molecular Field Topology Analysis method in QSAR studies of organic compounds
    • V.A. Palyulin, E.V. Radchenko, and N.S. Zefirov Molecular Field Topology Analysis method in QSAR studies of organic compounds J. Chem. Inf. Comp. Sci. 40 2000 659 667
    • (2000) J. Chem. Inf. Comp. Sci. , vol.40 , pp. 659-667
    • Palyulin, V.A.1    Radchenko, E.V.2    Zefirov, N.S.3
  • 40
  • 41
    • 84856559059 scopus 로고    scopus 로고
    • Comparative analysis of esterase activities of human, mouse, and rat blood
    • E.V. Rudakova, N.P. Boltneva, and G.F. Makhaeva Comparative analysis of esterase activities of human, mouse, and rat blood Bull. Exp. Biol. Med. 152 2011 73 75
    • (2011) Bull. Exp. Biol. Med. , vol.152 , pp. 73-75
    • Rudakova, E.V.1    Boltneva, N.P.2    Makhaeva, G.F.3
  • 42
    • 80051822924 scopus 로고    scopus 로고
    • Evolution of and perspectives on therapeutic approaches to nerve agent poisoning
    • P. Masson Evolution of and perspectives on therapeutic approaches to nerve agent poisoning Toxicol. Lett. 206 2011 5 13
    • (2011) Toxicol. Lett. , vol.206 , pp. 5-13
    • Masson, P.1
  • 43
    • 0016815842 scopus 로고
    • Organophosphorus esters causing delayed neurotoxic effects: Mechanism of action and structure activity studies
    • M.K. Johnson Organophosphorus esters causing delayed neurotoxic effects: mechanism of action and structure activity studies Arch. Toxicol. 34 1975 259 288
    • (1975) Arch. Toxicol. , vol.34 , pp. 259-288
    • Johnson, M.K.1
  • 44
    • 0345314143 scopus 로고
    • Organophosphorus pesticides induced delayed neurotoxicity (Review)
    • G.F. Makhaeva, V.V. Malygin, and I.V. Martynov Organophosphorus pesticides induced delayed neurotoxicity (Review) Agrokhimiya No. 12 1987 103 123
    • (1987) Agrokhimiya , vol.12 NO. , pp. 103-123
    • Makhaeva, G.F.1    Malygin, V.V.2    Martynov, I.V.3
  • 47
    • 34548399893 scopus 로고    scopus 로고
    • Generation of chemical structures on the basis of QSAR Models of Molecular Field Topology Analysis
    • A.A. Melnikov, V.A. Palyulin, E.V. Radchenko, and N.S. Zefirov Generation of chemical structures on the basis of QSAR Models of Molecular Field Topology Analysis Dokl. Chem. 415 2007 196 199
    • (2007) Dokl. Chem. , vol.415 , pp. 196-199
    • Melnikov, A.A.1    Palyulin, V.A.2    Radchenko, E.V.3    Zefirov, N.S.4
  • 48
    • 79953874196 scopus 로고    scopus 로고
    • Activity-based protein profiling of organophosphorus and thiocarbamate pesticides reveals multiple serine hydrolase targets in mouse brain
    • D.K. Nomura, and J.E. Casida Activity-based protein profiling of organophosphorus and thiocarbamate pesticides reveals multiple serine hydrolase targets in mouse brain J. Agric. Food Chem. 59 2011 2808 2815
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 2808-2815
    • Nomura, D.K.1    Casida, J.E.2
  • 49
    • 68849112180 scopus 로고    scopus 로고
    • Model equations for the kinetics of covalent irreversible enzyme inhibition and spontaneous reactivation: Esterases and organophosphorus compounds
    • J. Estevez, and E. Vilanova Model equations for the kinetics of covalent irreversible enzyme inhibition and spontaneous reactivation: esterases and organophosphorus compounds Crit. Rev. Toxicol. 39 2009 427 448
    • (2009) Crit. Rev. Toxicol. , vol.39 , pp. 427-448
    • Estevez, J.1    Vilanova, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.