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Volumn 57, Issue 6, 2000, Pages 1243-1248

Inactivation studies of acetylcholinesterase with phenylmethylsulfonyl fluoride

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; BENZENESULFONIC ACID DERIVATIVE; BENZYLSULFONYL FLUORIDE;

EID: 0034121307     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (42)

References (16)
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  • 2
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    • Inactivation of Electrophorus electricus acetylcholinesterase by benzenemethane sulfonyl fluoride
    • Barnett P and Rosenberry T (1978) Inactivation of Electrophorus electricus acetylcholinesterase by benzenemethane sulfonyl fluoride. Arch Biochem Biophys 190: 202-205.
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  • 3
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    • Crystal structure of mouse acetylcholinesterase: A peripheral site-occluding loop in a tetrameric assembly
    • Bourne Y, Taylor P, Bougis PE and Marchot P (1999) Crystal structure of mouse acetylcholinesterase: A peripheral site-occluding loop in a tetrameric assembly. J Biol Chem. 274:2963-2970.
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    • Bourne, Y.1    Taylor, P.2    Bougis, P.E.3    Marchot, P.4
  • 4
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • Ellman G, Courtney KD, Andres JV and Featherstone R (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:88-95.
    • (1961) Biochem Pharmacol , vol.7 , pp. 88-95
    • Ellman, G.1    Courtney, K.D.2    Andres, J.V.3    Featherstone, R.4
  • 5
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    • Sulfonyl fluorides as inhibitors of esterases. I. Rates of reaction with acetylcholinesterase, α-chymotrypsin, and trypsin
    • Fahrney D and Gold A (1963) Sulfonyl fluorides as inhibitors of esterases. I. Rates of reaction with acetylcholinesterase, α-chymotrypsin, and trypsin. J Am Chem Soc 85:997-1000.
    • (1963) J Am Chem Soc , vol.85 , pp. 997-1000
    • Fahrney, D.1    Gold, A.2
  • 7
    • 0015789712 scopus 로고
    • Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate
    • Hart GJ and O'Brien RD (1973) Recording spectrophotometric method for determination of dissociation and phosphorylation constants for the inhibition of acetylcholinesterase by organophosphates in the presence of substrate. Biochemistry 12:2940-2945.
    • (1973) Biochemistry , vol.12 , pp. 2940-2945
    • Hart, G.J.1    O'Brien, R.D.2
  • 8
    • 0028957265 scopus 로고
    • Anticholinesterases: Medical applications of neurochemical principles
    • Millard CB and Broomfield CA (1995) Anticholinesterases: Medical applications of neurochemical principles. J Neurochem 64:1909-1918.
    • (1995) J Neurochem , vol.64 , pp. 1909-1918
    • Millard, C.B.1    Broomfield, C.A.2
  • 10
    • 0018107843 scopus 로고
    • Kinetic analyses of differences in brain acetylcholinesterase from fish or mammalian sources
    • Moss D and Fahrney D (1978) Kinetic analyses of differences in brain acetylcholinesterase from fish or mammalian sources. Biochem Pharmacol 27:2693-2698.
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    • Moss, D.1    Fahrney, D.2
  • 11
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl-and butyryl-cholinesterase inhibitors
    • Radic Z, Pickering NA, Vellom DC, Camp S and Taylor P (1993) Three distinct domains in the cholinesterase molecule confer selectivity for acetyl-and butyryl-cholinesterase inhibitors. Biochemistry 32:12074-12084.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radic, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 13
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    • Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L and Silman I (1991) Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein. Science (Washington DC) 253:872-878.
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    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 14
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  • 15
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    • (1993) Biochemistry , vol.32 , pp. 12-17
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.