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Volumn 206, Issue 1, 2011, Pages 24-28

In vitro detoxification of cyclosarin in human blood pre-incubated ex vivo with recombinant serum paraoxonases

Author keywords

Cholinesterase; Cyclosarin; Detoxification; Nerve agent; Paraoxonase; Protection

Indexed keywords

ACETYLCHOLINESTERASE; ARYLDIALKYLPHOSPHATASE 1; CALCIUM ION; CHOLINESTERASE; CYCLOSARIN; ORGANOPHOSPHORUS COMPOUND;

EID: 80051814341     PISSN: 03784274     EISSN: 18793169     Source Type: Journal    
DOI: 10.1016/j.toxlet.2011.07.017     Document Type: Article
Times cited : (19)

References (16)
  • 1
    • 0015504318 scopus 로고
    • The inhibition of cholinesterase by diethylphosphorochloridate
    • Ashani Y., Wins P., Wilson I.B. The inhibition of cholinesterase by diethylphosphorochloridate. Biochim. Biophys. Acta 1972, 284:427-434.
    • (1972) Biochim. Biophys. Acta , vol.284 , pp. 427-434
    • Ashani, Y.1    Wins, P.2    Wilson, I.B.3
  • 2
    • 1342288926 scopus 로고    scopus 로고
    • Estimation of the upper limit of human butyrylcholinesterase dose required for protection against organophosphates toxicity: a mathematically based toxicokinetic model
    • Ashani Y., Pistinner S. Estimation of the upper limit of human butyrylcholinesterase dose required for protection against organophosphates toxicity: a mathematically based toxicokinetic model. Toxicol. Sci. 2004, 77:358-367.
    • (2004) Toxicol. Sci. , vol.77 , pp. 358-367
    • Ashani, Y.1    Pistinner, S.2
  • 3
    • 77955518989 scopus 로고    scopus 로고
    • Stereo-specific synthesis of analogs of nerve agents and their utilization for selection and characterization of paraoxonase (PON1) catalytic scavengers
    • Ashani Y., Gupta R.D., Goldsmith M., Silman I., Sussman J.L., Tawfik D.S., Leader H. Stereo-specific synthesis of analogs of nerve agents and their utilization for selection and characterization of paraoxonase (PON1) catalytic scavengers. Chem. Biol. Interact. 2010, 187:362-369.
    • (2010) Chem. Biol. Interact. , vol.187 , pp. 362-369
    • Ashani, Y.1    Gupta, R.D.2    Goldsmith, M.3    Silman, I.4    Sussman, J.L.5    Tawfik, D.S.6    Leader, H.7
  • 4
    • 79952484251 scopus 로고    scopus 로고
    • Adenovirus-mediated human paraoxonase1 gene transfer to provide protection against the toxicity of the organophosphorus pesticide toxicant diazoxon
    • Duysen E.G., Parikh K., Aleti V., Manne V., Lockridge O., Chilukuri N. Adenovirus-mediated human paraoxonase1 gene transfer to provide protection against the toxicity of the organophosphorus pesticide toxicant diazoxon. Gene Ther. 2011, 18:250-257.
    • (2011) Gene Ther. , vol.18 , pp. 250-257
    • Duysen, E.G.1    Parikh, K.2    Aleti, V.3    Manne, V.4    Lockridge, O.5    Chilukuri, N.6
  • 8
    • 33646373929 scopus 로고    scopus 로고
    • The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases
    • Khersonsky O., Tawfik D.S. The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases. J. Biol. Chem. 2006, 281:7649-7656.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7649-7656
    • Khersonsky, O.1    Tawfik, D.S.2
  • 9
    • 0028958850 scopus 로고
    • Paraoxonase protects against chlorpyrifos toxicity in mice
    • Li W.F., Furlong C.E., Costa L.G. Paraoxonase protects against chlorpyrifos toxicity in mice. Toxicol. Lett. 1995, 76:219-226.
    • (1995) Toxicol. Lett. , vol.76 , pp. 219-226
    • Li, W.F.1    Furlong, C.E.2    Costa, L.G.3
  • 10
    • 48549098997 scopus 로고    scopus 로고
    • HDL subfraction distribution of paraoxonase-1 and its relevance to enzyme activity and resistance to oxidative stress
    • Moren X., Deakin S., Liu M.L., Taskinen M.R., James R.W. HDL subfraction distribution of paraoxonase-1 and its relevance to enzyme activity and resistance to oxidative stress. J. Lipid Res. 2008, 49:1246-1253.
    • (2008) J. Lipid Res. , vol.49 , pp. 1246-1253
    • Moren, X.1    Deakin, S.2    Liu, M.L.3    Taskinen, M.R.4    James, R.W.5
  • 11
    • 33947177549 scopus 로고    scopus 로고
    • Effect of metal ions and calcium on purified PON1 and PON3 from rat liver
    • Pla A., Rodrigo L., Hernández A.F., Gil F., Lopez O. Effect of metal ions and calcium on purified PON1 and PON3 from rat liver. Chem. Biol. Interact. 2007, 167:63-70.
    • (2007) Chem. Biol. Interact. , vol.167 , pp. 63-70
    • Pla, A.1    Rodrigo, L.2    Hernández, A.F.3    Gil, F.4    Lopez, O.5
  • 12
    • 0032877947 scopus 로고    scopus 로고
    • Human serum paraoxonase/arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: apolipoprotein A-I stabilizes activity
    • Sorenson R.C., Bisgaier C.L., Aviram M., Hsu C., Billecke S., La Du B.N. Human serum paraoxonase/arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: apolipoprotein A-I stabilizes activity. Arterioscler. Thromb. Vasc. Biol. 1999, 19:2214-2225.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 2214-2225
    • Sorenson, R.C.1    Bisgaier, C.L.2    Aviram, M.3    Hsu, C.4    Billecke, S.5    La Du, B.N.6
  • 13
    • 0024279312 scopus 로고
    • Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C
    • Sussman J.L., Harel M., Frolow F., Varon L., Toker L., Futerman A.H., Silman I. Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C. J. Mol. Biol. 1988, 203:821-823.
    • (1988) J. Mol. Biol. , vol.203 , pp. 821-823
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Varon, L.4    Toker, L.5    Futerman, A.H.6    Silman, I.7
  • 15
    • 0031694251 scopus 로고    scopus 로고
    • Inhibition, reactivation and aging kinetics of cyclohexylmethylphosphonofluoridate-inhibited human cholinesterases
    • Worek F., Eyer P., Szinicz L. Inhibition, reactivation and aging kinetics of cyclohexylmethylphosphonofluoridate-inhibited human cholinesterases. Arch. Toxicol. 1998, 72:580-587.
    • (1998) Arch. Toxicol. , vol.72 , pp. 580-587
    • Worek, F.1    Eyer, P.2    Szinicz, L.3
  • 16
    • 0032842978 scopus 로고    scopus 로고
    • Improved determination of acetylcholinesterase activity in human whole blood
    • Worek F., Mast U., Kiderlen D., Diepold C., Eyer P. Improved determination of acetylcholinesterase activity in human whole blood. Clin. Chim. Acta 1999, 288:73-90.
    • (1999) Clin. Chim. Acta , vol.288 , pp. 73-90
    • Worek, F.1    Mast, U.2    Kiderlen, D.3    Diepold, C.4    Eyer, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.