메뉴 건너뛰기




Volumn 39, Issue 5, 2009, Pages 427-448

Model equations for the kinetics of covalent irreversible enzyme inhibition and spontaneous reactivation: Esterases and organophosphorus compounds

Author keywords

Acetylcholinesterase; Aging reaction; Carbamates; Dephosphorylation; Esterases; Inhibition; Kinetic; Model equation; Neuropathy target esterase; Ongoing inhibition; Organophosphorus; Phosphorylation; Reactivation

Indexed keywords

ACETYLCHOLINESTERASE; ESTERASE; NEUROTOXIC ESTERASE; ORGANOPHOSPHORUS COMPOUND; SERINE PEPTIDASE; UNCLASSIFIED DRUG; CHOLINESTERASE REACTIVATOR; ENZYME INHIBITOR;

EID: 68849112180     PISSN: 10408444     EISSN: 15476898     Source Type: Journal    
DOI: 10.1080/10408440802412309     Document Type: Review
Times cited : (45)

References (54)
  • 1
    • 76549233982 scopus 로고
    • Some properties of specifc cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analogues
    • Aldridge, W.N. (1950). Some properties of specifc cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analogues. Biochem. J. 46:451-460.
    • (1950) Biochem. J. , vol.46 , pp. 451-460
    • Aldridge, W.N.1
  • 2
    • 0003101123 scopus 로고
    • Te inhibition of erythrocyte cholinesterase by tri-esters of phosphoric acid. I. Diethyl p-nitrophenyl phosphate (E600) and analogues
    • Aldridge, W.N., and Davison, A.N. (1952). Te inhibition of erythrocyte cholinesterase by tri-esters of phosphoric acid. I. Diethyl p-nitrophenyl phosphate (E600) and analogues. Biochem. J. 51:62-70.
    • (1952) Biochem. J. , vol.51 , pp. 62-70
    • Aldridge, W.N.1    Davison, A.N.2
  • 4
    • 33745220989 scopus 로고    scopus 로고
    • Analysis of inhibition, reactivation and aging kinetics of highly toxic organophosphorus compounds with human and pig acetylcholinesterase
    • DOI 10.1016/j.tox.2006.04.030, PII S0300483X0600237X
    • Aurbek, N., Tiermann, H., Szinicz, L., Eyer, P., and Worek, F. (2006). Analysis of inhibition, reactivation and aging kinetics of highly toxic organophosphorus compounds with human and pig acetylcholinesterase. Toxicol 224:91-99. (Pubitemid 43912974)
    • (2006) Toxicology , vol.224 , Issue.1-2 , pp. 91-99
    • Aurbek, N.1    Thiermann, H.2    Szinicz, L.3    Eyer, P.4    Worek, F.5
  • 6
    • 33947685552 scopus 로고    scopus 로고
    • Enzyme-kinetic investigation of diferent sarin analogues reacting with human acetylcholinesterase and butyrylcholinesterase
    • Bartling, A., Worek, F., Szinicz, L., and Tiermann, H. (2007). Enzyme-kinetic investigation of diferent sarin analogues reacting with human acetylcholinesterase and butyrylcholinesterase. Toxicol. 233:166-172.
    • (2007) Toxicol. , vol.233 , pp. 166-172
    • Bartling, A.1    Worek, F.2    Szinicz, L.3    Tiermann, H.4
  • 7
    • 17144470883 scopus 로고    scopus 로고
    • Peripheral nerve soluble esterase are spontaneously reactivated after inhibition by paraoxon: Implication for a new defnition of neuropathy target esterase
    • Barril, J., Estévez, J., Escudero, M.A., Céspedes, M.V., Ñíguez, N., Sogorb, M.A., Monroy, A., and Vilanova, E. (1999). Peripheral nerve soluble esterase are spontaneously reactivated after inhibition by paraoxon: Implication for a new defnition of neuropathy target esterase. Chem. Biol. Interaction. 119-120: 541-550.
    • (1999) Chem. Biol. Interaction. , vol.119-120 , pp. 541-550
    • Barril, J.1    Estévez, J.2    Escudero, M.A.3    Céspedes, M.V.4    Ñíguez, N.5    Sogorb, M.A.6    Monroy, A.7    Vilanova, E.8
  • 8
    • 0030220635 scopus 로고    scopus 로고
    • Kinetic analysis of the in vitro inhibition, aging, and reactivation of brain acetylcholinesterase from rat and channel catfsh by paraoxon and chlorpyrifos-oxon
    • Carr, R.L., and Chambers, J.E. (1996). Kinetic analysis of the in vitro inhibition, aging, and reactivation of brain acetylcholinesterase from rat and channel catfsh by paraoxon and chlorpyrifos-oxon. Toxicol. Appl. Pharmacol. 139:365-373.
    • (1996) Toxicol. Appl. Pharmacol. , vol.139 , pp. 365-373
    • Carr, R.L.1    Chambers, J.E.2
  • 9
    • 0028348074 scopus 로고
    • In vivo inhibition of soluble and particulate forms of organophosphorus neuropathy target esterase NTE in hen sciatic nerve
    • Carrera, V, Díaz-Alejo, N., Sogorb, M.A., Vicedo, J.L., and Vilanova, E. (1994) In vivo inhibition of soluble and particulate forms of organophosphorus neuropathy target esterase NTE in hen sciatic nerve. Toxicol Lett. 71:47-51.
    • (1994) Toxicol Lett. , vol.71 , pp. 47-51
    • Carrera, V.1    Díaz-Alejo, N.2    Sogorb, M.A.3    Vicedo, J.L.4    Vilanova, E.5
  • 10
    • 0027161051 scopus 로고
    • Computerized analysis of covalent inhibition kinetics for identifcation of heart muscle cholinesterase and brain carboxylesterase isoenzymes. Design of diferential inhibition assays
    • Chemnitius, J.M., Dewald, K., Kreuzer, H., and Zech, R. (1993). Computerized analysis of covalent inhibition kinetics for identifcation of heart muscle cholinesterase and brain carboxylesterase isoenzymes. Design of diferential inhibition assays. Chem. Biol Interact. 87:239-244.
    • (1993) Chem. Biol Interact. , vol.87 , pp. 239-244
    • Chemnitius, J.M.1    Dewald, K.2    Kreuzer, H.3    Zech, R.4
  • 11
    • 0020623088 scopus 로고
    • Inhibition of brain carboxylesterases by neurotoxic and nonneurotoxic organophosphorus compounds
    • Chemnitius, J.M., and Zech, R. (1983). Inhibition of brain carboxylesterases by neurotoxic and nonneurotoxic organophosphorus compounds. Mol Pharmacol. 23:717-723.
    • (1983) Mol Pharmacol. , vol.23 , pp. 717-723
    • Chemnitius, J.M.1    Zech, R.2
  • 13
    • 0025081573 scopus 로고
    • Hen liver and plasma can metabolize O-hexyl, O-dichlorophenyl phosphoroamidate (Hexyl-DCP) at a rate comparable to that in rats
    • Díaz-Alejo, N., Vicedo, J.L., Pellín, M.C., and Vilanova E. (1990). Hen liver and plasma can metabolize O-hexyl, O-dichlorophenyl phosphoroamidate (Hexyl-DCP) at a rate comparable to that in rats. Neurotoxicol Teratol 12:615-618.
    • (1990) Neurotoxicol Teratol , vol.12 , pp. 615-618
    • Díaz-Alejo, N.1    Vicedo, J.L.2    Pellín, M.C.3    Vilanova, E.4
  • 14
    • 0030870227 scopus 로고    scopus 로고
    • Purifcation and characterization of naturally soluble neuropathy target esterase from chicken sciatic nerve by HPLC and Eastern Blot
    • Escudero, M.A., and Vilanova, E. (1997). Purifcation and characterization of naturally soluble neuropathy target esterase from chicken sciatic nerve by HPLC and Eastern Blot. J. Neurochem. 69:1975-1982.
    • (1997) J. Neurochem. , vol.69 , pp. 1975-1982
    • Escudero, M.A.1    Vilanova, E.2
  • 15
    • 2942516233 scopus 로고    scopus 로고
    • Te inhibition of the high sensitive peripheral nerve soluble esterases by mipafox. A new mathematical processing for the kinetics of inhibition of esterases by organophosphorus compounds
    • Estevez, J., García-Pérez, A., Barril, J., Pellín, M.C., and Vilanova, E. (2004) Te inhibition of the high sensitive peripheral nerve soluble esterases by mipafox. A new mathematical processing for the kinetics of inhibition of esterases by organophosphorus compounds. Toxicol Lett. 151:243-249.
    • (2004) Toxicol Lett. , vol.151 , pp. 243-249
    • Estevez, J.1    García-Pérez, A.2    Barril, J.3    Pellín, M.C.4    Vilanova, E.5
  • 16
    • 0037473419 scopus 로고    scopus 로고
    • Properties of phenyl valerate esterase activities from chicken serum are comparable with soluble esterases of peripheral nerves in relation with organophosphorus compounds inhibition
    • Garcia-Pérez, A.G., Barril, J., Estévez, J., and Vilanova, E. (2003). Properties of phenyl valerate esterase activities from chicken serum are comparable with soluble esterases of peripheral nerves in relation with organophosphorus compounds inhibition. Toxicol Lett. 142:1-10.
    • (2003) Toxicol Lett. , vol.142 , pp. 1-10
    • Garcia-Pérez, A.G.1    Barril, J.2    Estévez, J.3    Vilanova, E.4
  • 19
    • 0017701182 scopus 로고
    • Spontaneous reactivation of acetylcholinesterase following organophosphate inhibition. I. An analysis of anomalous reactivation kinetics
    • Hovanec, J.W., Broomfeld, C.A., Steinberg, G.M., Lanks, K.W., and Lieske, C.N. (1977). Spontaneous reactivation of acetylcholinesterase following organophosphate inhibition. I. An analysis of anomalous reactivation kinetics. Biochim. Biophys. Acta 483:312-319.
    • (1977) Biochim. Biophys. Acta , vol.483 , pp. 312-319
    • Hovanec, J.W.1    Broomfeld, C.A.2    Steinberg, G.M.3    Lanks, K.W.4    Lieske, C.N.5
  • 20
    • 0005291238 scopus 로고
    • Te reversible inhibition of acetylesterase by diisopropyl fuorophosphate and tetraethyl pyrophosphate
    • Jansen, E.F., Fellows-Nutting, M.D., and Balls, A.K. (1948). Te reversible inhibition of acetylesterase by diisopropyl fuorophosphate and tetraethyl pyrophosphate. J. Biol Chem. 175:975-987.
    • (1948) J. Biol Chem. , vol.175 , pp. 975-987
    • Jansen, E.F.1    Fellows-Nutting, M.D.2    Balls, A.K.3
  • 21
    • 0033025563 scopus 로고    scopus 로고
    • Kinetic evidence for diferent mechanisms of acetylcholinesterase inhibition by (1R)- and (1S)-stereoisomers of isomalathion
    • Jianmongkol, S., Marable, B.R., Berkman, C.E., Talley, T.T., Tompson, CM., and Richardson, R.J. (1999). Kinetic evidence for diferent mechanisms of acetylcholinesterase inhibition by (1R)- and (1S)-stereoisomers of isomalathion. Toxicol. Appl. Pharmacol. 155:43-53.
    • (1999) Toxicol. Appl. Pharmacol. , vol.155 , pp. 43-53
    • Jianmongkol, S.1    Marable, B.R.2    Berkman, C.E.3    Talley, T.T.4    Tompson, C.M.5    Richardson, R.J.6
  • 22
    • 0026062669 scopus 로고
    • Anomalous biochemical responses in test of the delayed neuropathic potential of methamidophos (S-dimethyl phosphoramidates), its resolved isomers and of some higher O-alkyl homologues
    • Johnson, M.K., Vilanova, E., and Read, D.J. (1991). Anomalous biochemical responses in test of the delayed neuropathic potential of methamidophos (S-dimethyl phosphoramidates), its resolved isomers and of some higher O-alkyl homologues. Arch. Toxicol. 5:618-624.
    • (1991) Arch. Toxicol. , vol.5 , pp. 618-624
    • Johnson, M.K.1    Vilanova, E.2    Read, D.J.3
  • 23
    • 0029871481 scopus 로고    scopus 로고
    • Interaction of organophosphorus compounds with carboxylesterases in the rat
    • Jokanovic, M., Kosanovic, M., and Maksimovic, M. (1996) Interaction of organophosphorus compounds with carboxylesterases in the rat. Arch. Toxicol. 70:444-450.
    • (1996) Arch. Toxicol. , vol.70 , pp. 444-450
    • Jokanovic, M.1    Kosanovic, M.2    Maksimovic, M.3
  • 24
    • 33751171517 scopus 로고    scopus 로고
    • Current understanding of the application of pyridinium oximes as cholinesterase reactivators in treatment of organophosphate poisoning
    • Jokanovic, M., and Stojiljkovic, M.P. (2006) Current understanding of the application of pyridinium oximes as cholinesterase reactivators in treatment of organophosphate poisoning. Eur. J. Pharmacol 553:10-17.
    • (2006) Eur. J. Pharmacol , vol.553 , pp. 10-17
    • Jokanovic, M.1    Stojiljkovic, M.P.2
  • 25
    • 0033735721 scopus 로고    scopus 로고
    • Interactions of the organophosphates paraoxon and methyl paraoxon with mouse brain acetylcholinesterase
    • Kardos, S.A., and Sultatos, L.G. (2000). Interactions of the organophosphates paraoxon and methyl paraoxon with mouse brain acetylcholinesterase. Toxicol. Sci. 58(1):118-126.
    • (2000) Toxicol. Sci. , vol.58 , Issue.1 , pp. 118-126
    • Kardos, S.A.1    Sultatos, L.G.2
  • 26
    • 4344616457 scopus 로고    scopus 로고
    • Comparison of chlorpyrifos-oxon and paraoxon acetylcholinesterase inhibition dynamics: Potential role of a peripheral binding site
    • Kousba, A.A., Sultatos, L.G., Poet, T.S., and Timchalk, C. (2004). Comparison of chlorpyrifos-oxon and paraoxon acetylcholinesterase inhibition dynamics: Potential role of a peripheral binding site. Toxicol. Sci. 80:239-248.
    • (2004) Toxicol. Sci. , vol.80 , pp. 239-248
    • Kousba, A.A.1    Sultatos, L.G.2    Poet, T.S.3    Timchalk, C.4
  • 27
    • 34047272804 scopus 로고    scopus 로고
    • Mechanism of aging of mipafox-inhibited butyrylcholinesterase
    • Kropp, T.J., and Richardson, R.J. (2007). Mechanism of aging of mipafox-inhibited butyrylcholinesterase. Chem. Res. Toxicol. 20:504-510.
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 504-510
    • Kropp, T.J.1    Richardson, R.J.2
  • 28
    • 0001242480 scopus 로고
    • Afnity and phosphorylation constants for the inhibition of esterases by organophosphates
    • Main, A.R. (1964). Afnity and phosphorylation constants for the inhibition of esterases by organophosphates. Sci. 144:992-993.
    • (1964) Sci. , vol.144 , pp. 992-993
    • Main, A.R.1
  • 29
    • 0000169232 scopus 로고
    • An algorithm for least squares estimation of parameters
    • Marquardt, D.W. (1963). An algorithm for least squares estimation of parameters. J. Soc. Ind. Appl. Math. 11:431-441.
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 30
    • 34848896346 scopus 로고    scopus 로고
    • Comparative hydrolysis of O-hexyl O-2,5-dichlorophenyl phosphoramidate and paraoxon in diferent tissues of vertebrates
    • Monroy-Noyola, A., Rojas, P., Vilanova, E., and Sogorb, M.A. (2007). Comparative hydrolysis of O-hexyl O-2,5-dichlorophenyl phosphoramidate and paraoxon in diferent tissues of vertebrates. Arch. Toxicol. 81:689-695.
    • (2007) Arch. Toxicol. , vol.81 , pp. 689-695
    • Monroy-Noyola, A.1    Rojas, P.2    Vilanova, E.3    Sogorb, M.A.4
  • 33
    • 33846185545 scopus 로고    scopus 로고
    • Over-expression of neuropathy target esterase activity in bovine chromafn cell cultures by adenovirus-mediated gene transfer
    • Quesada, E., Castell, J.V. , Vilanova, E., and Carrera, V. (2007). Over-expression of neuropathy target esterase activity in bovine chromafn cell cultures by adenovirus-mediated gene transfer. Toxicol. Lett. 168:286-291.
    • (2007) Toxicol. Lett. , vol.168 , pp. 286-291
    • Quesada, E.1    Castell, J.V.2    Vilanova, E.3    Carrera, V.4
  • 34
    • 0036838112 scopus 로고    scopus 로고
    • Lizard cholinesterases as biomarkers of pesticide exposure: Enzymological characterization
    • Sanchez-Hernandez, J.C., and Moreno-Sanchez, B. (2002) Lizard cholinesterases as biomarkers of pesticide exposure: enzymological characterization. Environ. Toxicol. Chem. 21:2319-2325.
    • (2002) Environ. Toxicol. Chem. , vol.21 , pp. 2319-2325
    • Sanchez-Hernandez, J.C.1    Moreno-Sanchez, B.2
  • 35
    • 4644235743 scopus 로고    scopus 로고
    • Methyl-paraoxon comparative inhibition kinetics for acetylcholinesterases from brain of neotropical fshes
    • Silva Filho, M.V., Oliveira, M.M., Salles, J.B., Bastos, V.L., Cassano, V.P., and Bastos, J.C. (2004). Methyl-paraoxon comparative inhibition kinetics for acetylcholinesterases from brain of neotropical fshes. Toxicol. Lett. 153(2):247-254.
    • (2004) Toxicol. Lett. , vol.153 , Issue.2 , pp. 247-254
    • Silva Filho, M.V.1    Oliveira, M.M.2    Salles, J.B.3    Bastos, V.L.4    Cassano, V.P.5    Bastos, J.C.6
  • 36
    • 0015796473 scopus 로고
    • Spontaneous reactivation and aging of dimethylphosphorylated acetylcholinesterase and cholinesterase
    • Skrinjaric-Spoljar, M., Simeon, V., and Reiner, E. (1973). Spontaneous reactivation and aging of dimethylphosphorylated acetylcholinesterase and cholinesterase. Biochim. Biophys. Acta 315:363-369.
    • (1973) Biochim. Biophys. Acta , vol.315 , pp. 363-369
    • Skrinjaric-Spoljar, M.1    Simeon, V.2    Reiner, E.3
  • 37
    • 33846818304 scopus 로고    scopus 로고
    • An in vitro approach for demonstrating the critical role of serum albumin in the detoxication of the carbamate carbaryl at in vivo toxicologically relevant concetrations
    • Sogorb, M.A., Álvarez-Escalante, C., Carrera, V., and Vilanova, E. (2007). An in vitro approach for demonstrating the critical role of serum albumin in the detoxication of the carbamate carbaryl at in vivo toxicologically relevant concetrations. Arch. Toxicol. 81:113-119.
    • (2007) Arch. Toxicol. , vol.81 , pp. 113-119
    • Sogorb, M.A.1    Álvarez-Escalante, C.2    Carrera, V.3    Vilanova, E.4
  • 38
    • 2942549125 scopus 로고    scopus 로고
    • Future applications of phosphotriesterases in the prophylaxis and treatment of organophosphorus insecticide and nerve agent poisonings
    • Sogorb, M.A., Carrera, V., and Vilanova, E. (2004). Future applications of phosphotriesterases in the prophylaxis and treatment of organophosphorus insecticide and nerve agent poisonings. Toxicol. Lett. 151(1):219-233.
    • (2004) Toxicol. Lett. , vol.151 , Issue.1 , pp. 219-233
    • Sogorb, M.A.1    Carrera, V.2    Vilanova, E.3
  • 39
    • 0031967954 scopus 로고    scopus 로고
    • Phosphotriesterase activity identifed in purifed serum albumins
    • Sogorb, M.A., Diaz-Alejo, N., Escudero, M.A., and Vilanova, E. (1997). Phosphotriesterase activity identifed in purifed serum albumins. Arch. Toxicol. 72:219-226.
    • (1997) Arch. Toxicol. , vol.72 , pp. 219-226
    • Sogorb, M.A.1    Diaz-Alejo, N.2    Escudero, M.A.3    Vilanova, E.4
  • 41
    • 70350477296 scopus 로고
    • Partial characterization of neuropathy target esterase and related phenyl valerate esterases from bovine adrenal medulla
    • Sogorb, M.A., Viniegra, S., Reig, J.A., and Vilanova, E. (1994). Partial characterization of neuropathy target esterase and related phenyl valerate esterases from bovine adrenal medulla. Toxicol. Lett. 74(Suppl 1):S80.
    • (1994) Toxicol. Lett. , vol.74 , Issue.SUPPL 1
    • Sogorb, M.A.1    Viniegra, S.2    Reig, J.A.3    Vilanova, E.4
  • 42
    • 0037051175 scopus 로고    scopus 로고
    • Enzymes involved in the detoxifcation of organophosphorus, carbamate and pyrethroid insecticides through hydrolysis
    • Sogorb, M.A., and Vilanova, E. (2002). Enzymes involved in the detoxifcation of organophosphorus, carbamate and pyrethroid insecticides through hydrolysis. Toxicol. Lett. 128:215-228.
    • (2002) Toxicol. Lett. , vol.128 , pp. 215-228
    • Sogorb, M.A.1    Vilanova, E.2
  • 43
    • 0027325864 scopus 로고
    • Te kinetics of o hexyo 2-5-dichlorophenyl phosphoramidate hydrolysing activity
    • Sogorb, M.A., Vilanova, E., and Díaz Alejo, N., (1993). Te kinetics of o hexyo 2-5-dichlorophenyl phosphoramidate hydrolysing activity. Chem. Biol. Interact. 87:117-125.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 117-125
    • Sogorb, M.A.1    Vilanova, E.2    Alejo, D.N.3
  • 44
    • 0029960552 scopus 로고    scopus 로고
    • Las esterasas que hidrolizan compuestos organofosforados: Un mecanismo efcaz de detoxifcación
    • Sogorb, M.A., Plá, A., and Vandilanova, E. (1996). Las esterasas que hidrolizan compuestos organofosforados: Un mecanismo efcaz de detoxifcación. Rev. Toxicol. 13:43-48.
    • (1996) Rev. Toxicol. , vol.13 , pp. 43-48
    • Sogorb, M.A.1    Plá, A.2    Vandilanova, E.3
  • 45
    • 0036071561 scopus 로고    scopus 로고
    • Importancia de la hidrólisis estereoespecífca en la evaluación de riesgos tóxicos de insecticidas fosforamidatos
    • Sogorb, M.A., Monroy-Noyola, A., and Vilanova, E. (2002). Importancia de la hidrólisis estereoespecífca en la evaluación de riesgos tóxicos de insecticidas fosforamidatos. Rev. Toxicol. 19:61-68.
    • (2002) Rev. Toxicol. , vol.19 , pp. 61-68
    • Sogorb, M.A.1    Monroy-Noyola, A.2    Vilanova, E.3
  • 46
    • 0014814578 scopus 로고
    • Regression with linear constraints: An extension of the magnifed diagonal method
    • Shrager, R.I. (1970). Regression with linear constraints: An extension of the magnifed diagonal method. J. ACM 17:446-452.
    • (1970) J. ACM , vol.17 , pp. 446-452
    • Shrager, R.I.1
  • 47
    • 0015280101 scopus 로고
    • Quadratic programming for nonlinear regression
    • Shrager, R.I. (1972). Quadratic programming for nonlinear regression. Commun. ACM 15:41-45.
    • (1972) Commun. ACM , vol.15 , pp. 41-45
    • Shrager, R.I.1
  • 48
    • 0032963556 scopus 로고    scopus 로고
    • Te role of phosphotriesterases in the detoxication of organophosphorus compounds
    • Vilanova, E., and Sogorb, M.A. (1999). Te role of phosphotriesterases in the detoxication of organophosphorus compounds. Crit. Rev. Toxicol. 29:21-57.
    • (1999) Crit. Rev. Toxicol. , vol.29 , pp. 21-57
    • Vilanova, E.1    Sogorb, M.A.2
  • 49
    • 0023195693 scopus 로고
    • Te interaction of some unsubstituted phosphoramidates analogues of methamidophos O, S-dimethyl phosphorothioamidate with acetylcholinesterase and neuropathy target esterase of hen brain
    • Vilanova, E., Johnson, M.K., and Vicedo, J.L. (1987) Te interaction of some unsubstituted phosphoramidates analogues of methamidophos O, S-dimethyl phosphorothioamidate with acetylcholinesterase and neuropathy target esterase of hen brain. Pestic. Biochem. Physiol. 28:224-238
    • (1987) Pestic. Biochem. Physiol. , vol.28 , pp. 224-238
    • Vilanova, E.1    Johnson, M.K.2    Vicedo, J.L.3
  • 50
    • 34247165881 scopus 로고    scopus 로고
    • Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by diferent phosphoramidates
    • Worek, F., Aurbek, N., Koller, M., Becker, C., Eyer, P., and Tiermann, H. (2007). Kinetic analysis of reactivation and aging of human acetylcholinesterase inhibited by diferent phosphoramidates. Biochem. Pharmacol. 73:1807-1817.
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 1807-1817
    • Worek, F.1    Aurbek, N.2    Koller, M.3    Becker, C.4    Eyer, P.5    Tiermann, H.6
  • 51
    • 0032892487 scopus 로고    scopus 로고
    • Dimethylphosphoryl-inhibited human cholinesterases: Inhibition, reactivation, and aging kinetics
    • Worek, F., Diepold, C., and Eyer, P. (1999). Dimethylphosphoryl-inhibited human cholinesterases: inhibition, reactivation, and aging kinetics. Arch. Toxicol. 73:7-14.
    • (1999) Arch. Toxicol. , vol.73 , pp. 7-14
    • Worek, F.1    Diepold, C.2    Eyer, P.3
  • 52
    • 28244473567 scopus 로고    scopus 로고
    • Evaluation of oxime efcacy in nerve agent poisoning: Development of a kinetic-based dynamic model
    • Worek, F., Szinicza, L., Eyerb P., and Tiermann, H. (2005). Evaluation of oxime efcacy in nerve agent poisoning: Development of a kinetic-based dynamic model. Toxicol. Appl. Pharmacol. 209:193-202.
    • (2005) Toxicol. Appl. Pharmacol. , vol.209 , pp. 193-202
    • Worek, F.1    Szinicza, L.2    Eyerb, P.3    Tiermann, H.4
  • 53
    • 7444221716 scopus 로고    scopus 로고
    • Kinetic analysis of interactions between human acetylcholinesterase, structurally diferent organophosphorus compounds and oximes
    • Worek, F., Tiermann, H., Szinicz, L., and Eyer, P. (2004). Kinetic analysis of interactions between human acetylcholinesterase, structurally diferent organophosphorus compounds and oximes. Biochem. Pharmacol. 68:2237-2248.
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 2237-2248
    • Worek, F.1    Tiermann, H.2    Szinicz, L.3    Eyer, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.