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Volumn 119-120, Issue , 1999, Pages 119-128

Reversible inhibition of acetylcholinesterase and butyrylcholinesterase by 4,4'-bipyridine and by a coumarin derivative

Author keywords

4,4' Bipyridine; Acetylcholinesterase; Butyrylcholinesterase; Coumarin derivative; Molecular modelling; Reversible inhibition

Indexed keywords

3 CHLORO 7 HYDROXY 4 METHYLCOUMARIN; 4,4' BIPYRIDINE; ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; CHOLINESTERASE; COUMARIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0033002757     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(99)00020-4     Document Type: Conference Paper
Times cited : (31)

References (18)
  • 1
    • 0014597797 scopus 로고
    • Acetylcholinesterase. Two types of inhibition by an organophosphorus compound: One the formation of phosphorylated enzyme and the other analogous to inhibition by substrate
    • Aldridge W.N., Reiner E. Acetylcholinesterase. Two types of inhibition by an organophosphorus compound: one the formation of phosphorylated enzyme and the other analogous to inhibition by substrate. Biochem. J. 115:1969;147-162.
    • (1969) Biochem. J. , vol.115 , pp. 147-162
    • Aldridge, W.N.1    Reiner, E.2
  • 2
    • 0345135891 scopus 로고
    • Inhibition of acetylcholinesterase by 4,4′-bipyridine and its effect upon phosphylation of the enzyme
    • Reiner E. Inhibition of acetylcholinesterase by 4,4′-bipyridine and its effect upon phosphylation of the enzyme. Croat. Chem. Acta. 59:1986;925-931.
    • (1986) Croat. Chem. Acta , vol.59 , pp. 925-931
    • Reiner, E.1
  • 3
    • 0026031111 scopus 로고
    • Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives
    • Radić Z., Reiner E., Taylor P. Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives. Mol. Pharmacol. 39:1991;98-104.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 98-104
    • Radić, Z.1    Reiner, E.2    Taylor, P.3
  • 4
    • 0029847351 scopus 로고    scopus 로고
    • Binding sites on acetylcholinesterase and butyrylcholinesterase for pyridinium and imidazolium oximes, and other reversible ligands
    • Reiner E., Škrinjarić-Špoljar M., Simeon-Rudolf V. Binding sites on acetylcholinesterase and butyrylcholinesterase for pyridinium and imidazolium oximes, and other reversible ligands. Period. Biol. 98:1996;325-329.
    • (1996) Period. Biol. , vol.98 , pp. 325-329
    • Reiner, E.1    Škrinjarić-Špoljar, M.2    Simeon-Rudolf, V.3
  • 5
    • 0010365058 scopus 로고
    • Kinetic study of the effect of substrates on reversible inhibition of cholinesterase and acetylcholinesterase by two coumarin derivatives
    • Reiner E., Simeon V. Kinetic study of the effect of substrates on reversible inhibition of cholinesterase and acetylcholinesterase by two coumarin derivatives. Croat. Chem. Acta. 47:1975;321-331.
    • (1975) Croat. Chem. Acta , vol.47 , pp. 321-331
    • Reiner, E.1    Simeon, V.2
  • 7
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- And butyrylcholinesterase inhibitors
    • Radić Z., Pickering N.A., Vellom D.C., Camp S., Taylor P. Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry. 32:1993;12074-12084.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radić, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 10
    • 0023605724 scopus 로고
    • Horse serum butyrylcholinesterase kinetics: A molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium
    • Cauet G., Friboulet A., Thomas D. Horse serum butyrylcholinesterase kinetics: a molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium. Biochem. Cell. Biol. 65:1987;529-535.
    • (1987) Biochem. Cell. Biol. , vol.65 , pp. 529-535
    • Cauet, G.1    Friboulet, A.2    Thomas, D.3
  • 11
    • 0027273738 scopus 로고
    • Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant
    • Masson P., Adkins S., Gouet P., Lockridge O. Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant. J. Biol. Chem. 268:1993;14329-14341.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14329-14341
    • Masson, P.1    Adkins, S.2    Gouet, P.3    Lockridge, O.4
  • 12
    • 0028908608 scopus 로고
    • Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by mono- And bisquaternary oximes
    • Ashani Y., Radić Z., Tsigelny I., Vellom D.C., Pickering N.A., Quinn D.M., Doctor B.P., Taylor P. Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by mono- and bisquaternary oximes. J. Biol. Chem. 270:1995;6370-6380.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6370-6380
    • Ashani, Y.1    Radić, Z.2    Tsigelny, I.3    Vellom, D.C.4    Pickering, N.A.5    Quinn, D.M.6    Doctor, B.P.7    Taylor, P.8
  • 13
    • 85058248664 scopus 로고    scopus 로고
    • Catalytic parameters for the hydrolysis of butyrylthiocholine by human serum butyrylcholinesterase variants
    • this volume
    • V. Simeon-Rudolf, E. Reiner, R.T. Evans, P.M. George, H.C. Potter, Catalytic parameters for the hydrolysis of butyrylthiocholine by human serum butyrylcholinesterase variants. Chem.-Biol. Interact., this volume.
    • Chem.-Biol. Interact.
    • Simeon-Rudolf, V.1    Reiner, E.2    Evans, R.T.3    George, P.M.4    Potter, H.C.5
  • 14
    • 0016823110 scopus 로고
    • Interaction of fluorescent probes with acetylcholinesterase: The site and specificity of propidium binding
    • Taylor P., Lappi S. Interaction of fluorescent probes with acetylcholinesterase: the site and specificity of propidium binding. Biochemistry. 14:1975;1989-1997.
    • (1975) Biochemistry , vol.14 , pp. 1989-1997
    • Taylor, P.1    Lappi, S.2
  • 15
    • 0008145786 scopus 로고
    • Michaelis constants and substrate inhibition constants for the reaction of acetylthiocholine with acetylcholinesterase and cholinesterase
    • Simeon V. Michaelis constants and substrate inhibition constants for the reaction of acetylthiocholine with acetylcholinesterase and cholinesterase. Croat. Chem. Acta. 46:1974;137-144.
    • (1974) Croat. Chem. Acta , vol.46 , pp. 137-144
    • Simeon, V.1
  • 16
    • 0029781839 scopus 로고    scopus 로고
    • Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates
    • Hosea N.A., Radić Z., Tsigelny I., Berman H.A., Quinn D.M., Taylor P. Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates. Biochemistry. 35:1996;10995-11004.
    • (1996) Biochemistry , vol.35 , pp. 10995-11004
    • Hosea, N.A.1    Radić, Z.2    Tsigelny, I.3    Berman, H.A.4    Quinn, D.M.5    Taylor, P.6
  • 17
    • 0029611091 scopus 로고
    • Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera
    • Reiner E., Simeon-Rudolf V., Škrinjarić-Špoljar M. Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera. Toxicol. Lett. 82/83:1995;447-452.
    • (1995) Toxicol. Lett. , vol.8283 , pp. 447-452
    • Reiner, E.1    Simeon-Rudolf, V.2    Škrinjarić-Špoljar, M.3
  • 18
    • 0021322057 scopus 로고
    • Binding sites on acetylcholinesterase for reversible ligands and phosphorylating agents
    • Radić Z., Reiner E., Simeon V. Binding sites on acetylcholinesterase for reversible ligands and phosphorylating agents. Biochem. Pharmacol. 33:1984;671-677.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 671-677
    • Radić, Z.1    Reiner, E.2    Simeon, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.