메뉴 건너뛰기




Volumn 100, Issue 1, 2007, Pages 136-145

Aging pathways for organophosphate-inhibited human butyrylcholinesterase, including novel pathways for isomalathion, resolved by mass spectrometry

Author keywords

Aging; Butyrylcholinesterase; Mass spectrometry; Organophosphate

Indexed keywords

CHOLINESTERASE; CYCLOSARIN; DICHLORVOS; DIISOPROPYL FLUOROPHOSPHATASE; ECOTHIOPATE; MALATHION; METHYLPHOSPHONOTHIOIC ACID S (2 DIISOPROPYLAMINOETHYL) O ETHYL ESTER; ORGANOPHOSPHATE; SARIN; SOMAN;

EID: 35448956936     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kfm215     Document Type: Article
Times cited : (60)

References (29)
  • 1
    • 33745220989 scopus 로고    scopus 로고
    • Analysis of inhibition, reactivation and aging kinetics of highly toxic organophosphorus compounds with human and pig acetylcholinesterase
    • Aurbek, N., Thiermann, 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. Toxicology 224, 91-99.
    • (2006) Toxicology , vol.224 , pp. 91-99
    • Aurbek, N.1    Thiermann, H.2    Szinicz, L.3    Eyer, P.4    Worek, F.5
  • 4
    • 0027533119 scopus 로고
    • Kinetics of the postinhibitory reactions of acetylcholinesterase poisoned by chiral isomalathion: A surprising nonreactivation induced by the RP stereoisomers
    • Berkman, C. E., Ryu, S., Quinn, D. A., and Thompson, C. M. (1993a). Kinetics of the postinhibitory reactions of acetylcholinesterase poisoned by chiral isomalathion: A surprising nonreactivation induced by the RP stereoisomers. Chem. Res. Toxicol. 6, 28-32.
    • (1993) Chem. Res. Toxicol , vol.6 , pp. 28-32
    • Berkman, C.E.1    Ryu, S.2    Quinn, D.A.3    Thompson, C.M.4
  • 5
    • 0027377453 scopus 로고
    • Synthesis, absolute configuration, and analysis of malathion, malaoxon, and isomalathion enantiomers
    • Berkman, C. E., Thompson, C. M., and Perrin, S. R. (1993b). Synthesis, absolute configuration, and analysis of malathion, malaoxon, and isomalathion enantiomers. Chem. Res. Toxicol. 6, 718-723.
    • (1993) Chem. Res. Toxicol , vol.6 , pp. 718-723
    • Berkman, C.E.1    Thompson, C.M.2    Perrin, S.R.3
  • 6
    • 4243148518 scopus 로고    scopus 로고
    • Organophosphate toxicology: Safety aspects of nonacetylcholinesterase secondary targets
    • Casida, J. E., and Quistad, G. B. (2004). Organophosphate toxicology: Safety aspects of nonacetylcholinesterase secondary targets. Chem. Res. Toxicol. 17, 983-998.
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 983-998
    • Casida, J.E.1    Quistad, G.B.2
  • 7
    • 0034764279 scopus 로고    scopus 로고
    • Identification of butyrylcholinesterase adducts after inhibition with isomalathion using mass spectrometry: Difference in mechanism between (1R)- and (1S)-stereoisomers
    • Doorn, J. A., Schall, M., Gage, D. A., Talley, T. T., Thompson, C. M., and Richardson, R. J. (2001a). Identification of butyrylcholinesterase adducts after inhibition with isomalathion using mass spectrometry: Difference in mechanism between (1R)- and (1S)-stereoisomers. Toxicol. Appl. Pharmacol. 176, 73-80.
    • (2001) Toxicol. Appl. Pharmacol , vol.176 , pp. 73-80
    • Doorn, J.A.1    Schall, M.2    Gage, D.A.3    Talley, T.T.4    Thompson, C.M.5    Richardson, R.J.6
  • 8
    • 0034946676 scopus 로고    scopus 로고
    • Probing the active sites of butyrylcholinesterase and cholesterol esterase with isomalathion: Conserved stereoselective inactivation of serine hydrolases structurally related to acetylcholinesterase
    • Doorn, J. A., Talley, T. T., Thompson, C. M., and Richardson, R. J. (2001b). Probing the active sites of butyrylcholinesterase and cholesterol esterase with isomalathion: Conserved stereoselective inactivation of serine hydrolases structurally related to acetylcholinesterase. Chem. Res. Toxicol. 14, 807-813.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 807-813
    • Doorn, J.A.1    Talley, T.T.2    Thompson, C.M.3    Richardson, R.J.4
  • 9
    • 30144445702 scopus 로고    scopus 로고
    • Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase
    • Ekstrom, F., Akfur, C., Tunemalm, A. K., and Lundberg, S. (2006). Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase. Biochemistry 45, 74-81.
    • (2006) Biochemistry , vol.45 , pp. 74-81
    • Ekstrom, F.1    Akfur, C.2    Tunemalm, A.K.3    Lundberg, S.4
  • 11
    • 0030451745 scopus 로고    scopus 로고
    • Deglycosylation of proteins for crystallization using recombinant fusion protein glycosidases
    • Grueninger-Leitch, F., D'Arcy, A., D'Arcy, B., and Chene, C. (1996). Deglycosylation of proteins for crystallization using recombinant fusion protein glycosidases. Protein Sci. 5, 2617-2622.
    • (1996) Protein Sci , vol.5 , pp. 2617-2622
    • Grueninger-Leitch, F.1    D'Arcy, A.2    D'Arcy, B.3    Chene, C.4
  • 12
    • 0014024404 scopus 로고
    • Dealkylation and loss of capacity for reactivation of cholinesterase inhibited by sarin
    • Harris, L. W., Fleisher, J. H., Clark, J., and Cliff, W. J. (1966). Dealkylation and loss of capacity for reactivation of cholinesterase inhibited by sarin. Science 154, 404-407.
    • (1966) Science , vol.154 , pp. 404-407
    • Harris, L.W.1    Fleisher, J.H.2    Clark, J.3    Cliff, W.J.4
  • 13
    • 0141542697 scopus 로고    scopus 로고
    • Direct analysis of the kinetic profiles of organophosphate-acetylcholinesterase adducts by MALDI-TOF mass spectrometry
    • Jennings, L. L., Malecki, M., Komives, E. A., and Taylor, P. (2003). Direct analysis of the kinetic profiles of organophosphate-acetylcholinesterase adducts by MALDI-TOF mass spectrometry. Biochemistry 42, 11083-11091.
    • (2003) Biochemistry , vol.42 , pp. 11083-11091
    • Jennings, L.L.1    Malecki, M.2    Komives, E.A.3    Taylor, P.4
  • 14
    • 0033025563 scopus 로고    scopus 로고
    • Kinetic evidence for different mechanisms of acetylcholinesterase inhibition by (1R)- and (1S)- stereoisomers of isomalathion
    • Jianmongkol, S., Marable, B. R., Berkman, C. E., Talley, T. T., Thompson, C. M., and Richardson, R. J. (1999). Kinetic evidence for different 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    Thompson, C.M.5    Richardson, R.J.6
  • 16
    • 0034009408 scopus 로고    scopus 로고
    • Pesticides and susceptible populations: People with butyrylcholinesterase genetic variants may be at risk
    • Lockridge, O., and Masson, P. (2000). Pesticides and susceptible populations: People with butyrylcholinesterase genetic variants may be at risk. Neurotoxicology 21, 113-126.
    • (2000) Neurotoxicology , vol.21 , pp. 113-126
    • Lockridge, O.1    Masson, P.2
  • 17
    • 27544478065 scopus 로고    scopus 로고
    • Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys; a potential new therapeutic for protection against cocaine and nerve agent toxicity
    • online
    • Lockridge, O., Schopfer, L. M., Winger, G., and Woods, G. H. (2005). Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys; a potential new therapeutic for protection against cocaine and nerve agent toxicity. J. Med, CBR. Def. 3, online.
    • (2005) J. Med, CBR. Def , vol.3
    • Lockridge, O.1    Schopfer, L.M.2    Winger, G.3    Woods, G.H.4
  • 18
    • 0027365801 scopus 로고
    • Aging and spontaneous reactivation of human plasma cholinesterase activity after inhibition by organophosphorus pesticides
    • Mason, H. J., Waine, E., Stevenson, A., and Wilson, H. K. (1993). Aging and spontaneous reactivation of human plasma cholinesterase activity after inhibition by organophosphorus pesticides. Hum. Exp. Toxicol. 12, 497-503.
    • (1993) Hum. Exp. Toxicol , vol.12 , pp. 497-503
    • Mason, H.J.1    Waine, E.2    Stevenson, A.3    Wilson, H.K.4
  • 20
    • 0030764030 scopus 로고    scopus 로고
    • Importance of aspartate-70 in organophosphate inhibition, oxime re-activation and aging of human butyrylcholinesterase
    • Masson, P., Froment, M. T., Bartels, C. F., and Lockridge, O. (1997b). Importance of aspartate-70 in organophosphate inhibition, oxime re-activation and aging of human butyrylcholinesterase. Biochem. J. 325(Pt. 1), 53-61.
    • (1997) Biochem. J , vol.325 , Issue.PART. 1 , pp. 53-61
    • Masson, P.1    Froment, M.T.2    Bartels, C.F.3    Lockridge, O.4
  • 23
    • 13444261934 scopus 로고    scopus 로고
    • Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: The crystal structure suggests two alternative mechanisms of aging
    • Nachon, F., Asojo, O. A., Borgstahl, G. E., Masson, P., and Lockridge, O. (2005). Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: The crystal structure suggests two alternative mechanisms of aging. Biochemistry 44, 1154-1162.
    • (2005) Biochemistry , vol.44 , pp. 1154-1162
    • Nachon, F.1    Asojo, O.A.2    Borgstahl, G.E.3    Masson, P.4    Lockridge, O.5
  • 25
    • 0029742777 scopus 로고    scopus 로고
    • Aging of phosphylated human acetylcholinesterase: Catalytic processes mediated by aromatic and polar residues of the active centre
    • Shafferman, A., Ordentlich, A., Barak, D., Stein, D., Ariel, N., and Velan, B. (1996). Aging of phosphylated human acetylcholinesterase: Catalytic processes mediated by aromatic and polar residues of the active centre. Biochem. J. 318(Pt. 3), 833-840.
    • (1996) Biochem. J , vol.318 , Issue.PART. 3 , pp. 833-840
    • Shafferman, A.1    Ordentlich, A.2    Barak, D.3    Stein, D.4    Ariel, N.5    Velan, B.6
  • 26
    • 0015964160 scopus 로고
    • The reactivatibility of cholinesterase inhibited by VX and sarin in man
    • Sidell, F. R., and Groff, W. A. (1974). The reactivatibility of cholinesterase inhibited by VX and sarin in man. Toxicol. Appl. Pharmacol 27, 241-252.
    • (1974) Toxicol. Appl. Pharmacol , vol.27 , pp. 241-252
    • Sidell, F.R.1    Groff, W.A.2
  • 27
    • 5344245964 scopus 로고    scopus 로고
    • Retrospective detection of exposure to nerve agents: Analysis of phosphofluoridates originating from fluoride-induced reactivation of phosphylated BuChE
    • van der Schans, M. J., Polhuijs, M., Yan Dijk, C., Degenhardt, C. E., Pleijsier, K., Langenberg, J. P., and Benschop, H. P. (2004). Retrospective detection of exposure to nerve agents: Analysis of phosphofluoridates originating from fluoride-induced reactivation of phosphylated BuChE. Arch. Toxicol. 78, 508-524.
    • (2004) Arch. Toxicol , vol.78 , pp. 508-524
    • van der Schans, M.J.1    Polhuijs, M.2    Yan Dijk, C.3    Degenhardt, C.E.4    Pleijsier, K.5    Langenberg, J.P.6    Benschop, H.P.7
  • 28
    • 0030833798 scopus 로고    scopus 로고
    • Unique push-pull mechanism of dealkylation in soman-inhibited cholinesterases
    • Viragh, C., Akhmetshin, R., Kovach, I. M., and Broomfield, C. (1997). Unique push-pull mechanism of dealkylation in soman-inhibited cholinesterases. Biochemistry 36, 8243-8252.
    • (1997) Biochemistry , vol.36 , pp. 8243-8252
    • Viragh, C.1    Akhmetshin, R.2    Kovach, I.M.3    Broomfield, C.4
  • 29
    • 0040962825 scopus 로고    scopus 로고
    • Small molecular products of dealkylation in soman-inhibited electric eel acetylcholinesterase
    • Viragh, C., Kovach, I. M., and Pannell, L. (1999). Small molecular products of dealkylation in soman-inhibited electric eel acetylcholinesterase. Biochemistry 38, 9557-9561.
    • (1999) Biochemistry , vol.38 , pp. 9557-9561
    • Viragh, C.1    Kovach, I.M.2    Pannell, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.