메뉴 건너뛰기




Volumn 231, Issue 2, 2008, Pages 157-164

A structure-activity analysis of the variation in oxime efficacy against nerve agents

Author keywords

Acetylcholinesterase; Organophosphorus nerve agents; Oxime; Steric hindrance

Indexed keywords

1 (4 CARBAMOYLPYRIDINIO) 1' (2 HYDROXYIMINOMETHYLPYRIDINIO)DIMETHYL ETHER; ACETYLCHOLINESTERASE; ATROPINE; CYCLOSARIN; ICD 585; ISONICOTINAMIDE; METHYLPHOSPHONOTHIOIC ACID S (2 DIISOPROPYLAMINOETHYL) O ETHYL ESTER; O ISOBUTYL S [2 (DIETHYLAMINO)ETHYL]METHYLPHOSPHONOTHIOATE; OBIDOXIME; ORGANOPHOSPHORUS COMPOUND; OXIME DERIVATIVE; PHOSPHONIC ACID DERIVATIVE; PRALIDOXIME; SARIN; UNCLASSIFIED DRUG;

EID: 49549113611     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2008.04.007     Document Type: Article
Times cited : (59)

References (52)
  • 1
    • 3042825350 scopus 로고    scopus 로고
    • Future considerations for the medical management of nerve agent intoxication
    • Aas P. Future considerations for the medical management of nerve agent intoxication. Prehosp. Disaster Med. 18 (2003) 208-216
    • (2003) Prehosp. Disaster Med. , vol.18 , pp. 208-216
    • Aas, P.1
  • 2
    • 0028908608 scopus 로고
    • Amino acid residues controlling reactivation of organophosphonyl conjugates of acetycholinesterase by mono- and bis-quaternary oximes
    • Ashani Y., Radic Z., Tsigelny I., Vellom D.C., Pickering N.A., Quinn D.M., Doctor B.P., and Taylor P. Amino acid residues controlling reactivation of organophosphonyl conjugates of acetycholinesterase by mono- and bis-quaternary oximes. J. Biol. Chem. 270 (1995) 6370-6380
    • (1995) J. Biol. Chem. , vol.270 , pp. 6370-6380
    • Ashani, Y.1    Radic, Z.2    Tsigelny, I.3    Vellom, D.C.4    Pickering, N.A.5    Quinn, D.M.6    Doctor, B.P.7    Taylor, P.8
  • 3
    • 0001861650 scopus 로고
    • Overview of the biological and clinical aspects of organophosphates and carbamates
    • Ballantyne B., and Marrs T.C. (Eds), Butterworth-Heinemann, Oxford
    • Ballantyne B., and Marrs T.C. Overview of the biological and clinical aspects of organophosphates and carbamates. In: Ballantyne B., and Marrs T.C. (Eds). Clinical and Experimental Toxicology of Organophosphates and Carbamates (1992), Butterworth-Heinemann, Oxford 3-14
    • (1992) Clinical and Experimental Toxicology of Organophosphates and Carbamates , pp. 3-14
    • Ballantyne, B.1    Marrs, T.C.2
  • 5
    • 0000976597 scopus 로고
    • On the mechanism of ageing of phosphonylated cholinesterases
    • Benschop H.P., and Keijer J.H. On the mechanism of ageing of phosphonylated cholinesterases. Biochim. Biophys. Acta 128 (1966) 586-588
    • (1966) Biochim. Biophys. Acta , vol.128 , pp. 586-588
    • Benschop, H.P.1    Keijer, J.H.2
  • 6
    • 31044442395 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of pyridinium oximes: mode of interaction with acetylcholinesterase, effect on tabun- and soman-poisoned mice and their cytotoxicity
    • Calic M., Vrdoljak A.L., Radic B., Jelic D., Jun D., Kuca K., and Kovarik Z. In vitro and in vivo evaluation of pyridinium oximes: mode of interaction with acetylcholinesterase, effect on tabun- and soman-poisoned mice and their cytotoxicity. Toxicology. 219 (2006) 85-96
    • (2006) Toxicology. , vol.219 , pp. 85-96
    • Calic, M.1    Vrdoljak, A.L.2    Radic, B.3    Jelic, D.4    Jun, D.5    Kuca, K.6    Kovarik, Z.7
  • 7
    • 33845377446 scopus 로고
    • Computation of molecular volume
    • Connolly M.L. Computation of molecular volume. J. Am. Chem. Soc. 107 (1985) 1118-1124
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 1118-1124
    • Connolly, M.L.1
  • 8
    • 0028132872 scopus 로고
    • Review of oximes available for treatment of nerve agent poisoning
    • Dawson R.M. Review of oximes available for treatment of nerve agent poisoning. J. Appl. Toxicol. 14 (1994) 317-331
    • (1994) J. Appl. Toxicol. , vol.14 , pp. 317-331
    • Dawson, R.M.1
  • 9
    • 50549175610 scopus 로고
    • The preparation and chemical characterization of hemoglobin-free ghosts of human erythrocytes
    • Dodge J.T., Mitchell C., and Hanahan D.J. The preparation and chemical characterization of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 100 (1963) 119-130
    • (1963) Arch. Biochem. Biophys. , vol.100 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 11
    • 84890132026 scopus 로고    scopus 로고
    • Oximes
    • Marrs T.C., Maynard R.L., and Sidell F.R. (Eds), John Wiley, New York
    • Eyer P., and Worek F. Oximes. In: Marrs T.C., Maynard R.L., and Sidell F.R. (Eds). Chemical Warfare Agents: Toxicology and Treatment (2007), John Wiley, New York 305-329
    • (2007) Chemical Warfare Agents: Toxicology and Treatment , pp. 305-329
    • Eyer, P.1    Worek, F.2
  • 12
    • 0026063178 scopus 로고
    • Statistical analysis of dose-response experiments by maximum likelihood analysis and iteratively reweighted nonlinear least squares techniques
    • Feder P.I., Olson C.T., Hobson D.W., and Matthews M.C. Statistical analysis of dose-response experiments by maximum likelihood analysis and iteratively reweighted nonlinear least squares techniques. Drug Info. J. 25 (1991) 323-334
    • (1991) Drug Info. J. , vol.25 , pp. 323-334
    • Feder, P.I.1    Olson, C.T.2    Hobson, D.W.3    Matthews, M.C.4
  • 16
    • 3543013633 scopus 로고
    • Reactivation of phosphorylated acetylcholinesterase
    • Koelle G.B. (Ed), Springer-Verlag, Berlin
    • Hobbiger F. Reactivation of phosphorylated acetylcholinesterase. In: Koelle G.B. (Ed). Cholinesterases and Anticholinesterase Agents (1963), Springer-Verlag, Berlin 921-988
    • (1963) Cholinesterases and Anticholinesterase Agents , pp. 921-988
    • Hobbiger, F.1
  • 17
    • 34247550159 scopus 로고    scopus 로고
    • Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state
    • Hornberg A., Tunemalm A.K., and Ekstrom F. Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state. Biochemistry 46 (2007) 4815-4825
    • (2007) Biochemistry , vol.46 , pp. 4815-4825
    • Hornberg, A.1    Tunemalm, A.K.2    Ekstrom, F.3
  • 18
    • 0020577156 scopus 로고
    • The efficacy of bispyridinium derivatives in the treatment of organophosphonate poisoning in the guinea pig
    • Inns R.H., and Leadbeater L. The efficacy of bispyridinium derivatives in the treatment of organophosphonate poisoning in the guinea pig. J. Pharm. Pharmacol. 35 (1983) 427-433
    • (1983) J. Pharm. Pharmacol. , vol.35 , pp. 427-433
    • Inns, R.H.1    Leadbeater, L.2
  • 19
    • 33751171517 scopus 로고    scopus 로고
    • Current understanding of the application of pyridinium oximes as cholinesterase reactivators in treatment of organophosphate poisoning
    • Jokanovic M., and Stojilkovic M.P. Current understanding of the application of pyridinium oximes as cholinesterase reactivators in treatment of organophosphate poisoning. Eur. J. Pharmacol. 553 (2006) 10-17
    • (2006) Eur. J. Pharmacol. , vol.553 , pp. 10-17
    • Jokanovic, M.1    Stojilkovic, M.P.2
  • 20
    • 37649006683 scopus 로고    scopus 로고
    • Potency of novel oximes to reactivate sarin inhibited human cholinesterases
    • Jun D., Kuca K., Picha J., Koleckar V., and Marek J. Potency of novel oximes to reactivate sarin inhibited human cholinesterases. Drug Chem. Toxicol. 31 (2008) 1-9
    • (2008) Drug Chem. Toxicol. , vol.31 , pp. 1-9
    • Jun, D.1    Kuca, K.2    Picha, J.3    Koleckar, V.4    Marek, J.5
  • 21
    • 0026702496 scopus 로고
    • Esterase-1: developmental expression in the mouse and distribution of related proteins in other species
    • Kadner S.S., Katz J., and Finlay T.H. Esterase-1: developmental expression in the mouse and distribution of related proteins in other species. Arch. Biochem. Biophys. 296 (1992) 435-441
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 435-441
    • Kadner, S.S.1    Katz, J.2    Finlay, T.H.3
  • 22
    • 0036447187 scopus 로고    scopus 로고
    • Review of oximes in the antidotal treatment of poisoning by organophosphorus nerve agents
    • Kassa J. Review of oximes in the antidotal treatment of poisoning by organophosphorus nerve agents. J. Toxicol. Clin. Toxicol. 40 (2002) 803-816
    • (2002) J. Toxicol. Clin. Toxicol. , vol.40 , pp. 803-816
    • Kassa, J.1
  • 23
    • 33751160026 scopus 로고    scopus 로고
    • The role of oximes in the antidotal treatment of chemical casualties exposed to nerve agents
    • Monov A., and Dishovsky C. (Eds), Union of Scientists in Bulgaria, Sofia available at http://www.jmedchemdef.org/archives.html
    • Kassa J. The role of oximes in the antidotal treatment of chemical casualties exposed to nerve agents. In: Monov A., and Dishovsky C. (Eds). Medical Aspects of Chemical and Biological Terrorism: Chemical Terrorism and Traumatism (2005), Union of Scientists in Bulgaria, Sofia 193-208. http://www.jmedchemdef.org/archives.html available at http://www.jmedchemdef.org/archives.html
    • (2005) Medical Aspects of Chemical and Biological Terrorism: Chemical Terrorism and Traumatism , pp. 193-208
    • Kassa, J.1
  • 24
    • 0013805620 scopus 로고
    • Activity-structure relationships in the reactivation of diethylphosphoryl acetylcholinesterase by phenyl-1-methyl pyridinium ketoximes
    • Kitz R.J., Ginsburg S., and Wilson I.B. Activity-structure relationships in the reactivation of diethylphosphoryl acetylcholinesterase by phenyl-1-methyl pyridinium ketoximes. Biochem. Pharmacol. 14 (1965) 1471-1477
    • (1965) Biochem. Pharmacol. , vol.14 , pp. 1471-1477
    • Kitz, R.J.1    Ginsburg, S.2    Wilson, I.B.3
  • 25
    • 49549119648 scopus 로고    scopus 로고
    • Cholinesterase blockers as potential agents for chemical terrorism and contemporary approaches to therapy of acute poisonings induced by anti-cholinesterase neuroparalytic substances
    • Monov A., and Dishovsky C. (Eds), Union of Scientists in Bulgaria, Sofia available at http://www.jmedchemdef.org/archives.html
    • Kokshareva N., Prodanchuk N., Zhminko P., and Krivenchuk V. Cholinesterase blockers as potential agents for chemical terrorism and contemporary approaches to therapy of acute poisonings induced by anti-cholinesterase neuroparalytic substances. In: Monov A., and Dishovsky C. (Eds). Medical Aspects of Chemical and Biological Terrorism: Chemical Terrorism and Traumatism (2005), Union of Scientists in Bulgaria, Sofia 153-182. http://www.jmedchemdef.org/archives.html available at http://www.jmedchemdef.org/archives.html
    • (2005) Medical Aspects of Chemical and Biological Terrorism: Chemical Terrorism and Traumatism , pp. 153-182
    • Kokshareva, N.1    Prodanchuk, N.2    Zhminko, P.3    Krivenchuk, V.4
  • 26
    • 1542533645 scopus 로고    scopus 로고
    • Mutant cholinesterases possessing enhanced capacity for reactivation of their phosphonylated conjugates
    • Kovarik Z., Radic Z., Berman H.A., Simeon-Rudolf V., Reiner E., and Taylor P. Mutant cholinesterases possessing enhanced capacity for reactivation of their phosphonylated conjugates. Biochemistry 43 (2004) 3222-3229
    • (2004) Biochemistry , vol.43 , pp. 3222-3229
    • Kovarik, Z.1    Radic, Z.2    Berman, H.A.3    Simeon-Rudolf, V.4    Reiner, E.5    Taylor, P.6
  • 27
    • 10744232850 scopus 로고    scopus 로고
    • Reactivation of cyclosarin-inhibited rat brain acetylcholinesterase by pyridinium oximes
    • Kuca K., and Patocka J. Reactivation of cyclosarin-inhibited rat brain acetylcholinesterase by pyridinium oximes. J. Enzym. Inhib. Med. Chem. 19 (2004) 39-43
    • (2004) J. Enzym. Inhib. Med. Chem. , vol.19 , pp. 39-43
    • Kuca, K.1    Patocka, J.2
  • 28
    • 33646056667 scopus 로고    scopus 로고
    • Structural requirements of acetylcholinesterase reactivators
    • Kuca K., Jun D., and Musilek K. Structural requirements of acetylcholinesterase reactivators. Mini Rev. Med. Chem. 6 (2006) 269-277
    • (2006) Mini Rev. Med. Chem. , vol.6 , pp. 269-277
    • Kuca, K.1    Jun, D.2    Musilek, K.3
  • 29
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
    • Li B., Sedlacek M., Manoharan I., Boopathy R., Duysen E.G., Masson P., and Lockridge O. 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
  • 30
    • 0026568340 scopus 로고
    • Comparison of several oximes against poisoning by soman, tabun and GF
    • Lundy P.M., Hansen A.S., Hand B.T., and Boulet C.A. Comparison of several oximes against poisoning by soman, tabun and GF. Toxicology 72 (1992) 99-105
    • (1992) Toxicology , vol.72 , pp. 99-105
    • Lundy, P.M.1    Hansen, A.S.2    Hand, B.T.3    Boulet, C.A.4
  • 31
    • 0026639319 scopus 로고
    • The specificity of carboxylesterase protection against the toxicity of organophosphorus compounds
    • Maxwell D.M. The specificity of carboxylesterase protection against the toxicity of organophosphorus compounds. Toxicol. Appl. Pharmacol. 114 (1992) 306-312
    • (1992) Toxicol. Appl. Pharmacol. , vol.114 , pp. 306-312
    • Maxwell, D.M.1
  • 32
    • 0025870153 scopus 로고
    • The role of carboxylesterase in species variation of oxime protection against soman
    • Maxwell D.M., and Brecht K.M. The role of carboxylesterase in species variation of oxime protection against soman. Neurosci. Biobehav. Rev. 15 (1991) 135-139
    • (1991) Neurosci. Biobehav. Rev. , vol.15 , pp. 135-139
    • Maxwell, D.M.1    Brecht, K.M.2
  • 33
    • 0023633188 scopus 로고
    • The effect of carboxylesterase inhibition on interspecies differences in soman toxicity
    • Maxwell D.M., Brecht K.M., and ONeill B.L. The effect of carboxylesterase inhibition on interspecies differences in soman toxicity. Toxicol. Lett. 39 (1987) 35-42
    • (1987) Toxicol. Lett. , vol.39 , pp. 35-42
    • Maxwell, D.M.1    Brecht, K.M.2    ONeill, B.L.3
  • 34
    • 33751416601 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibition: does it explain the toxicity of organophosphorus compounds?
    • Maxwell D.M., Brecht K.M., Koplovitz I., and Sweeney R.E. Acetylcholinesterase inhibition: does it explain the toxicity of organophosphorus compounds?. ArchToxicol. 80 (2006) 756-760
    • (2006) ArchToxicol. , vol.80 , pp. 756-760
    • Maxwell, D.M.1    Brecht, K.M.2    Koplovitz, I.3    Sweeney, R.E.4
  • 35
    • 0014910328 scopus 로고
    • Antidotal effects of pyridinium and imidazolium salts on soman and paraoxon poisoning in mice
    • Oldiges H., and Schoene K. Antidotal effects of pyridinium and imidazolium salts on soman and paraoxon poisoning in mice. Arch. Toxikol. 26 (1970) 293-305
    • (1970) Arch. Toxikol. , vol.26 , pp. 293-305
    • Oldiges, H.1    Schoene, K.2
  • 36
    • 21544471553 scopus 로고    scopus 로고
    • Pre-junctional effects of oximes on [3H]-acetylcholine release in rat hippocampal slices during soman intoxication
    • Oydvin O.K., Tanso R., and Aas P. Pre-junctional effects of oximes on [3H]-acetylcholine release in rat hippocampal slices during soman intoxication. Eur. J. Pharmacol. 516 (2005) 227-234
    • (2005) Eur. J. Pharmacol. , vol.516 , pp. 227-234
    • Oydvin, O.K.1    Tanso, R.2    Aas, P.3
  • 38
    • 0019249604 scopus 로고
    • Pyridinium salts as organophosphate antagonists
    • Schoene K. Pyridinium salts as organophosphate antagonists. Monogr. Neural Sci. 7 (1980) 85-98
    • (1980) Monogr. Neural Sci. , vol.7 , pp. 85-98
    • Schoene, K.1
  • 39
    • 0020586611 scopus 로고
    • Reactivation of soman-inhibited acetylcholinesterase in vitro and protection against soman in vivo by bispyridinium-2-aldoximes
    • Schoene K., Steinhanses J., and Oldiges H. Reactivation of soman-inhibited acetylcholinesterase in vitro and protection against soman in vivo by bispyridinium-2-aldoximes. Biochem. Pharmacol. 32 (1983) 1649-1651
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 1649-1651
    • Schoene, K.1    Steinhanses, J.2    Oldiges, H.3
  • 40
    • 0034040340 scopus 로고    scopus 로고
    • Efficacy of biperiden and atropine as anticonvulsant treatment for organophosphorus nerve agent intoxication
    • Shih T.-M., and McDonough J.H. Efficacy of biperiden and atropine as anticonvulsant treatment for organophosphorus nerve agent intoxication. Arch. Toxicol. 74 (2000) 165-172
    • (2000) Arch. Toxicol. , vol.74 , pp. 165-172
    • Shih, T.-M.1    McDonough, J.H.2
  • 41
    • 0021085681 scopus 로고
    • Quantitative structure-activity relationships and possible mechanisms of action of bis-pyridinium oximes as antidotes against pinacolyl methylphosphonofluoridate
    • Su C.T., Tang C.P., Ma C., Shih Y.S., Liu C.Y., and Wu M.T. Quantitative structure-activity relationships and possible mechanisms of action of bis-pyridinium oximes as antidotes against pinacolyl methylphosphonofluoridate. Fundam. Appl. Toxicol. 3 (1983) 271-277
    • (1983) Fundam. Appl. Toxicol. , vol.3 , pp. 271-277
    • Su, C.T.1    Tang, C.P.2    Ma, C.3    Shih, Y.S.4    Liu, C.Y.5    Wu, M.T.6
  • 42
    • 58149193064 scopus 로고
    • Kinetic studies and structure-activity relationships of bispyridinium oximes as reactivators of acetylcholinesterase inhibited by organophosphorus compounds
    • Su C.T., Wang P.H., Liu R.F., Shih J.H., Ma C., Lin C.H., Liu C.Y., and Wu M.T. Kinetic studies and structure-activity relationships of bispyridinium oximes as reactivators of acetylcholinesterase inhibited by organophosphorus compounds. Fundam. Appl. Toxicol. 6 (1986) 506-514
    • (1986) Fundam. Appl. Toxicol. , vol.6 , pp. 506-514
    • Su, C.T.1    Wang, P.H.2    Liu, R.F.3    Shih, J.H.4    Ma, C.5    Lin, C.H.6    Liu, C.Y.7    Wu, M.T.8
  • 43
    • 0027481819 scopus 로고
    • Ion channel blockade by oximes and recovery of diaphragm muscle from soman poisoning in vitro
    • Tattersall J.E. Ion channel blockade by oximes and recovery of diaphragm muscle from soman poisoning in vitro. Br. J. Pharmacol. 108 (1993) 1006-1015
    • (1993) Br. J. Pharmacol. , vol.108 , pp. 1006-1015
    • Tattersall, J.E.1
  • 44
    • 33847129496 scopus 로고    scopus 로고
    • Anticholinesterase agents
    • Brunton L.L., Lazo J.S., and Parker K.L. (Eds), McGraw-Hill, New York
    • Taylor P. Anticholinesterase agents. In: Brunton L.L., Lazo J.S., and Parker K.L. (Eds). Goodman and Gilman's Pharmacological Basis of Therapeutics (2006), McGraw-Hill, New York 201-216
    • (2006) Goodman and Gilman's Pharmacological Basis of Therapeutics , pp. 201-216
    • Taylor, P.1
  • 45
    • 33947630408 scopus 로고    scopus 로고
    • Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure
    • Taylor P., Kovarik Z., Reiner E., and Radic Z. Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure. Toxicology 233 (2007) 70-78
    • (2007) Toxicology , vol.233 , pp. 70-78
    • Taylor, P.1    Kovarik, Z.2    Reiner, E.3    Radic, Z.4
  • 46
    • 0014198558 scopus 로고
    • Oxime reactivation of diethylphosphoryl human serum cholinesterase
    • Wang E.I.C., and Braid P.E. Oxime reactivation of diethylphosphoryl human serum cholinesterase. J. Biol. Chem. 242 (1967) 2683-2687
    • (1967) J. Biol. Chem. , vol.242 , pp. 2683-2687
    • Wang, E.I.C.1    Braid, P.E.2
  • 47
    • 19544368045 scopus 로고
    • A powerful reactivator of alkylphosphate-inhibited acetylcholinesterase
    • Wilson I.B., and Ginsburg S. A powerful reactivator of alkylphosphate-inhibited acetylcholinesterase. Biochim. Biophys. Acta 18 (1955) 168-170
    • (1955) Biochim. Biophys. Acta , vol.18 , pp. 168-170
    • Wilson, I.B.1    Ginsburg, S.2
  • 48
    • 0003042077 scopus 로고
    • Reactivation of organophosphorus inhibited AChE with oximes
    • Chambers J.E., and Levi P.E. (Eds), Academic Press, San Diego
    • Wilson B.W., Hooper M.J., Hensen M.E., and Neiberg P.S. Reactivation of organophosphorus inhibited AChE with oximes. In: Chambers J.E., and Levi P.E. (Eds). Organophosphates: Chemistry, Fate and Metabolism (1992), Academic Press, San Diego 107-137
    • (1992) Organophosphates: Chemistry, Fate and Metabolism , pp. 107-137
    • Wilson, B.W.1    Hooper, M.J.2    Hensen, M.E.3    Neiberg, P.S.4
  • 49
    • 0034673934 scopus 로고    scopus 로고
    • Mechanism of oxime reactivation of acetylcholinesterase analyzed by chirality and mutagenesis
    • Wong L., Radic Z., Bruggemann J.M., Hosea N., Berman H.A., and Taylor P. Mechanism of oxime reactivation of acetylcholinesterase analyzed by chirality and mutagenesis. Biochemistry. 39 (2000) 5750-5757
    • (2000) Biochemistry. , vol.39 , pp. 5750-5757
    • Wong, L.1    Radic, Z.2    Bruggemann, J.M.3    Hosea, N.4    Berman, H.A.5    Taylor, P.6
  • 50
    • 0032892487 scopus 로고    scopus 로고
    • Dimethylphosphoryl-inhibited human cholinesterases: inhibition, reactivation, and aging kinetics
    • Worek F., Diepold C., and Eyer P. Dimethylphosphoryl-inhibited human cholinesterases: inhibition, reactivation, and aging kinetics. Arch. Toxicol. 73 (1999) 7-14
    • (1999) Arch. Toxicol. , vol.73 , pp. 7-14
    • Worek, F.1    Diepold, C.2    Eyer, P.3
  • 51
    • 0036381465 scopus 로고    scopus 로고
    • Reactivation kinetics of acetylcholinesterase from different species inhibited by highly toxic organophosphates
    • Worek F., Reiter G., Eyer P., and Szinicz L. Reactivation kinetics of acetylcholinesterase from different species inhibited by highly toxic organophosphates. Arch. Toxicol. 76 (2002) 523-529
    • (2002) Arch. Toxicol. , vol.76 , pp. 523-529
    • Worek, F.1    Reiter, G.2    Eyer, P.3    Szinicz, L.4
  • 52
    • 7444221716 scopus 로고    scopus 로고
    • Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes
    • Worek F., Thiermann H., Szinicz L., and Eyer P. Kinetic analysis of interactions between human acetylcholinesterase, structurally different organophosphorus compounds and oximes. Biochem. Pharmacol. 68 (2004) 2237-2248
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 2237-2248
    • Worek, F.1    Thiermann, H.2    Szinicz, L.3    Eyer, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.