-
1
-
-
0027318577
-
molecular and cellular biology of cholinesterases
-
Massoulié J., Pezzementi L., Bon S., Krejci E., and Vallette F.M. molecular and cellular biology of cholinesterases. Prog. Neurobiol. 41 (1993) 31-91
-
(1993)
Prog. Neurobiol.
, vol.41
, pp. 31-91
-
-
Massoulié, J.1
Pezzementi, L.2
Bon, S.3
Krejci, E.4
Vallette, F.M.5
-
2
-
-
0142039868
-
Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
-
Nicolet Y., Lockridge O., Masson P., Fontecilla-Camps J.C., and Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J. Biol. Chem. 278 (2003) 41141-41147
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 41141-41147
-
-
Nicolet, Y.1
Lockridge, O.2
Masson, P.3
Fontecilla-Camps, J.C.4
Nachon, F.5
-
5
-
-
0037375876
-
Cholinesterases: new roles in brain function and in Alzheimers's disease
-
Giacobini E. Cholinesterases: new roles in brain function and in Alzheimers's disease. Neurochem. Res. 28 (2003) 515-522
-
(2003)
Neurochem. Res.
, vol.28
, pp. 515-522
-
-
Giacobini, E.1
-
6
-
-
0037012468
-
Acetylcholinesterase knockouts establish central cholinergic pathway and can use butyrylcholinesterase to hydrolyze acetylcholine
-
Mesulam M.M., Guillozet A., Shaw P., Levey A., Duysen E.G., and Lockridge O. Acetylcholinesterase knockouts establish central cholinergic pathway and can use butyrylcholinesterase to hydrolyze acetylcholine. Neuroscience 110 (2003) 627-639
-
(2003)
Neuroscience
, vol.110
, pp. 627-639
-
-
Mesulam, M.M.1
Guillozet, A.2
Shaw, P.3
Levey, A.4
Duysen, E.G.5
Lockridge, O.6
-
7
-
-
0025294717
-
Genetic variants of human serum butyrylcholinesterase influence the metabolism of the muscle relaxant succinylcholine
-
Lockridge O. Genetic variants of human serum butyrylcholinesterase influence the metabolism of the muscle relaxant succinylcholine. Pharmac. Ther. 47 (1990) 35-60
-
(1990)
Pharmac. Ther.
, vol.47
, pp. 35-60
-
-
Lockridge, O.1
-
8
-
-
0036742363
-
Isosorbide-based aspirin prodrugs. II. Hydrolysis kinetics of isorsorbide diaspirinate
-
Gilmer G.F., Moriarty L.M., Lally M.N., and Clancy J.M. Isosorbide-based aspirin prodrugs. II. Hydrolysis kinetics of isorsorbide diaspirinate. Eur. J. Pharm. Sci. 16 (2002) 297-304
-
(2002)
Eur. J. Pharm. Sci.
, vol.16
, pp. 297-304
-
-
Gilmer, G.F.1
Moriarty, L.M.2
Lally, M.N.3
Clancy, J.M.4
-
9
-
-
2942551084
-
Interaction of human butyrylcholinesterase variants with bambuterol and terbutaline
-
Kovarik Z., and Simeon-Rudolf V. Interaction of human butyrylcholinesterase variants with bambuterol and terbutaline. J. Enz. Inhib. Med. Chem. 19 (2004) 113-117
-
(2004)
J. Enz. Inhib. Med. Chem.
, vol.19
, pp. 113-117
-
-
Kovarik, Z.1
Simeon-Rudolf, V.2
-
10
-
-
28044458963
-
Computational redesign of human butyrylcholinesterase for anticocaine medication
-
Pan Y., Gao D., Yang W., Cho H., Yang G., Tai H.-H., and Zhan C.-G. Computational redesign of human butyrylcholinesterase for anticocaine medication. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 16656-16661
-
(2005)
Proc. Natl. Acad. Sci. U. S. A.
, vol.102
, pp. 16656-16661
-
-
Pan, Y.1
Gao, D.2
Yang, W.3
Cho, H.4
Yang, G.5
Tai, H.-H.6
Zhan, C.-G.7
-
11
-
-
0018731624
-
Mode of action of anticholinesterases
-
Main A.R. Mode of action of anticholinesterases. Pharmac. Ther. 6 (1979) 579-628
-
(1979)
Pharmac. Ther.
, vol.6
, pp. 579-628
-
-
Main, A.R.1
-
12
-
-
0027281533
-
Organophosphate poisoning
-
Marrs T.C. Organophosphate poisoning. Pharmac. Ther. 58 (1993) 51-66
-
(1993)
Pharmac. Ther.
, vol.58
, pp. 51-66
-
-
Marrs, T.C.1
-
13
-
-
0346445341
-
-
Imperial College Press, London XXIV+485 pages
-
Karalliedde L., Feldman S., Henry J., and Marrs T. Organophosphates and health (2001), Imperial College Press, London XXIV+485 pages
-
(2001)
Organophosphates and health
-
-
Karalliedde, L.1
Feldman, S.2
Henry, J.3
Marrs, T.4
-
14
-
-
4043074138
-
Cholinesterase inhibitors: new roles and therapeutic alternatives
-
Giacobini E. Cholinesterase inhibitors: new roles and therapeutic alternatives. Pharmacol. Res. 50 (2004) 433-440
-
(2004)
Pharmacol. Res.
, vol.50
, pp. 433-440
-
-
Giacobini, E.1
-
15
-
-
1342288926
-
Estimation of the upper limit of human butyrylcholinesterase dose required for protection against organophosphate toxicity: a mathematically based toxicokinetic model
-
Ashani Y., and Pistinner S. Estimation of the upper limit of human butyrylcholinesterase dose required for protection against organophosphate toxicity: a mathematically based toxicokinetic model. Toxicol. Sci. 77 (2004) 358-367
-
(2004)
Toxicol. Sci.
, vol.77
, pp. 358-367
-
-
Ashani, Y.1
Pistinner, S.2
-
16
-
-
28744449011
-
Bioscavengers for the protection of humans against organophosphate toxicity
-
Doctor B.P., and Saxena A. Bioscavengers for the protection of humans against organophosphate toxicity. Chem.-Biol. Interact. 157-158C (2005) 167-171
-
(2005)
Chem.-Biol. Interact.
, vol.157-158 C
, pp. 167-171
-
-
Doctor, B.P.1
Saxena, A.2
-
17
-
-
21344437661
-
Mutants of human butyrylcholinesterase with organophosphate hydrolase activity; evidence that H117 is a general base catalyst for hydrolysis of echothiophate
-
Schopfer L.M., Ticu-Boeck A., Broomfield C.A., and Lockridge O. Mutants of human butyrylcholinesterase with organophosphate hydrolase activity; evidence that H117 is a general base catalyst for hydrolysis of echothiophate. J. Med. Chem. Def. 2 (2004) 1-21
-
(2004)
J. Med. Chem. Def.
, vol.2
, pp. 1-21
-
-
Schopfer, L.M.1
Ticu-Boeck, A.2
Broomfield, C.A.3
Lockridge, O.4
-
18
-
-
1942439688
-
Resistance to organophosphorus agent toxicity in transgenic mice expressing the G117H mutant of human butyrylcholinesterase
-
Wang Y., Boeck A.T., Duysen E.G., Saunders T.L., van Keuren M., and Lockridge O. Resistance to organophosphorus agent toxicity in transgenic mice expressing the G117H mutant of human butyrylcholinesterase. Tox. Appl. Pharmacol. 196 (2004) 356-366
-
(2004)
Tox. Appl. Pharmacol.
, vol.196
, pp. 356-366
-
-
Wang, Y.1
Boeck, A.T.2
Duysen, E.G.3
Saunders, T.L.4
van Keuren, M.5
Lockridge, O.6
-
19
-
-
33845282579
-
Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states
-
Quinn D.M. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem. Rev. 87 (1987) 955-979
-
(1987)
Chem. Rev.
, vol.87
, pp. 955-979
-
-
Quinn, D.M.1
-
20
-
-
0001585830
-
Acetylcholinesterase: mechanism of catalysis and inhibition
-
Tougu V. Acetylcholinesterase: mechanism of catalysis and inhibition. Curr. Med. Chem. 1 (2001) 155-170
-
(2001)
Curr. Med. Chem.
, vol.1
, pp. 155-170
-
-
Tougu, V.1
-
21
-
-
0021126688
-
Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine
-
Froede H.C., and Wilson I.B. Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine. J. Biol. Chem. 259 (1984) 11010-11013
-
(1984)
J. Biol. Chem.
, vol.259
, pp. 11010-11013
-
-
Froede, H.C.1
Wilson, I.B.2
-
22
-
-
1642458106
-
Damped oscillatory hysteretic behaviour of butyrylcholinesterase with benzoylcholine as substrate
-
Masson P., Goldstein B.N., Debouzy J.C., Froment M.-T., Lockridge O., and Schopfer L.M. Damped oscillatory hysteretic behaviour of butyrylcholinesterase with benzoylcholine as substrate. Eur. J. Biochem. 271 (2004) 220-234
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 220-234
-
-
Masson, P.1
Goldstein, B.N.2
Debouzy, J.C.3
Froment, M.-T.4
Lockridge, O.5
Schopfer, L.M.6
-
23
-
-
2442713750
-
Rate-determining step of butyrylcholinesterase-catalyzed hydrolysis of benzoylcholine and benzoylthiocholine
-
Masson P., Bec N., Froment M.-T., Nachon F., Balny C., Lockridge O., and Schopfer L.M. Rate-determining step of butyrylcholinesterase-catalyzed hydrolysis of benzoylcholine and benzoylthiocholine. Eur. J. Biochem. 271 (2004) 1980-1990
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 1980-1990
-
-
Masson, P.1
Bec, N.2
Froment, M.-T.3
Nachon, F.4
Balny, C.5
Lockridge, O.6
Schopfer, L.M.7
-
24
-
-
0031043533
-
Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase
-
Masson P., Legrand P., Bartels C.F., Froment M.-T., Schopfer L.M., and Lockridge O. Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry 36 (1997) 2266-2277
-
(1997)
Biochemistry
, vol.36
, pp. 2266-2277
-
-
Masson, P.1
Legrand, P.2
Bartels, C.F.3
Froment, M.-T.4
Schopfer, L.M.5
Lockridge, O.6
-
25
-
-
0028845803
-
Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite
-
Barak D., Ordentlich A., Bromberg A., Kronman C., Marcus D., Lazar A., Ariel N., Velan B., and Shafferman A. Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite. Biochemistry 34 (1995) 15444-15452
-
(1995)
Biochemistry
, vol.34
, pp. 15444-15452
-
-
Barak, D.1
Ordentlich, A.2
Bromberg, A.3
Kronman, C.4
Marcus, D.5
Lazar, A.6
Ariel, N.7
Velan, B.8
Shafferman, A.9
-
26
-
-
0032774638
-
Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates
-
Masson P., Xie W.-H., Froment M.-T., Levitsky V., Fortier P.-L., Albaret C., and Lockridge O. Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates. Biochim. Biophys. Acta 1433 (1999) 281-293
-
(1999)
Biochim. Biophys. Acta
, vol.1433
, pp. 281-293
-
-
Masson, P.1
Xie, W.-H.2
Froment, M.-T.3
Levitsky, V.4
Fortier, P.-L.5
Albaret, C.6
Lockridge, O.7
-
27
-
-
0035968202
-
Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and the acylation sites
-
De Ferrari G.V., Mallender W.D., Inestrosa N.C., and Rosenberry T.L. Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and the acylation sites. J. Biol. Chem. 276 (2001) 23282-23287
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 23282-23287
-
-
De Ferrari, G.V.1
Mallender, W.D.2
Inestrosa, N.C.3
Rosenberry, T.L.4
-
28
-
-
0032946621
-
Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant
-
Levitsky V., Xie W., Froment M.-T., Lockridge O., and Masson P. Polyol-induced activation by excess substrate of the D70G butyrylcholinesterase mutant. Biochim. Biophys. Acta 1429 (1999) 422-430
-
(1999)
Biochim. Biophys. Acta
, vol.1429
, pp. 422-430
-
-
Levitsky, V.1
Xie, W.2
Froment, M.-T.3
Lockridge, O.4
Masson, P.5
-
29
-
-
0037060466
-
Substrate activation in acetylcholinesterase induced by low pH or mutation in the π-cation subsite
-
Masson P., Schopfer L.M., Bartels C.F., Froment M.-T., Ribes F., Nachon F., and Lockridge O. Substrate activation in acetylcholinesterase induced by low pH or mutation in the π-cation subsite. Biochim. Biophys. Acta 1594 (2002) 313-324
-
(2002)
Biochim. Biophys. Acta
, vol.1594
, pp. 313-324
-
-
Masson, P.1
Schopfer, L.M.2
Bartels, C.F.3
Froment, M.-T.4
Ribes, F.5
Nachon, F.6
Lockridge, O.7
-
30
-
-
0037238060
-
High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine
-
Masson P., Nachon F., Bartels C.F., Froment M.-T., Ribes F., Matthews C., and Lockridge O. High activity of human butyrylcholinesterase at low pH in the presence of excess butyrylthiocholine. Eur. J. Biochem. 270 (2003) 315-324
-
(2003)
Eur. J. Biochem.
, vol.270
, pp. 315-324
-
-
Masson, P.1
Nachon, F.2
Bartels, C.F.3
Froment, M.-T.4
Ribes, F.5
Matthews, C.6
Lockridge, O.7
-
31
-
-
0038219567
-
Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate
-
Johnson J.L., Cusack B., Davies M.P., Fauq A., and Rosenberry T.L. Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate. Biochemistry 42 (2003) 5438-5452
-
(2003)
Biochemistry
, vol.42
, pp. 5438-5452
-
-
Johnson, J.L.1
Cusack, B.2
Davies, M.P.3
Fauq, A.4
Rosenberry, T.L.5
-
32
-
-
1942520265
-
Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate
-
Stojan J., Brochier L., Alies C., Colletier J.P., and Fournier D. Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate. Eur. J. Biochem. 271 (2004) 1364-1371
-
(2004)
Eur. J. Biochem.
, vol.271
, pp. 1364-1371
-
-
Stojan, J.1
Brochier, L.2
Alies, C.3
Colletier, J.P.4
Fournier, D.5
-
33
-
-
0027517144
-
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
-
Radic Z., Pickering N.A., Vellom D.C., Camp S., and 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
-
-
Radic, Z.1
Pickering, N.A.2
Vellom, D.C.3
Camp, S.4
Taylor, P.5
-
34
-
-
33845995644
-
Hydrolysis of carboxylic acid esters of thiocholine and its analogues. 3. Hydrolysis catalysed by acetylcholine esterase and butyrylcholine esterase
-
Heilbronn E. Hydrolysis of carboxylic acid esters of thiocholine and its analogues. 3. Hydrolysis catalysed by acetylcholine esterase and butyrylcholine esterase. Acta Chem. Scand. 13 (1959) 1547-1560
-
(1959)
Acta Chem. Scand.
, vol.13
, pp. 1547-1560
-
-
Heilbronn, E.1
-
35
-
-
0034607435
-
Transition state structure and rate determination for the acylation stage of acetylcholinesterase-catalyzed hydrolysis of (acetylthio)choline
-
Malany S., Sawai M., Sikorski R.S., Seravalli J., Quinn D.M., Radic Z., Taylor P., Kronman C., Velan B., and Shafferman A. Transition state structure and rate determination for the acylation stage of acetylcholinesterase-catalyzed hydrolysis of (acetylthio)choline. J. Am. Chem. Soc. 122 (2000) 2981-2987
-
(2000)
J. Am. Chem. Soc.
, vol.122
, pp. 2981-2987
-
-
Malany, S.1
Sawai, M.2
Sikorski, R.S.3
Seravalli, J.4
Quinn, D.M.5
Radic, Z.6
Taylor, P.7
Kronman, C.8
Velan, B.9
Shafferman, A.10
-
36
-
-
0001277102
-
The histochemical differentiation of types of cholinesterases and their localizations in tissues of the cat
-
Koelle G.B. The histochemical differentiation of types of cholinesterases and their localizations in tissues of the cat. J. Pharm. Exptl. Ther. 100 (1950) 158-179
-
(1950)
J. Pharm. Exptl. Ther.
, vol.100
, pp. 158-179
-
-
Koelle, G.B.1
-
38
-
-
15844422678
-
The X-ray structure of a transition state analog complex reveals the molecular origin of the catalytic power and substrate specificity of acetylcholinesterase
-
Harel M., Quinn D.M., Nair H.K., Silman I., and Sussman J.L. The X-ray structure of a transition state analog complex reveals the molecular origin of the catalytic power and substrate specificity of acetylcholinesterase. J. Am. Chem. Soc. 118 (1996) 2340-2346
-
(1996)
J. Am. Chem. Soc.
, vol.118
, pp. 2340-2346
-
-
Harel, M.1
Quinn, D.M.2
Nair, H.K.3
Silman, I.4
Sussman, J.L.5
-
39
-
-
0032584583
-
Functional characteristics of the oxyanion hole in human acetylcholinesterase
-
Ordentlich A., Barak D., Kronman C., Ariel N., Segall Y., Velan B., and Shafferman A. Functional characteristics of the oxyanion hole in human acetylcholinesterase. J. Biol. Chem. 273 (1998) 19509-19517
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 19509-19517
-
-
Ordentlich, A.1
Barak, D.2
Kronman, C.3
Ariel, N.4
Segall, Y.5
Velan, B.6
Shafferman, A.7
-
40
-
-
0037019547
-
Pole of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: an ab initio QM/MM study
-
Zhang Y., Kua J., and McCammon J.A. Pole of the catalytic triad and oxyanion hole in acetylcholinesterase catalysis: an ab initio QM/MM study. J. Chem. Soc. 124 (2002) 10572-10577
-
(2002)
J. Chem. Soc.
, vol.124
, pp. 10572-10577
-
-
Zhang, Y.1
Kua, J.2
McCammon, J.A.3
-
41
-
-
33745143582
-
A computational study of the deacylation mechanism of human butyrylcholinesterase
-
Suarez D., Diaz N., Fontecilla-Camps J., and Field M.J. A computational study of the deacylation mechanism of human butyrylcholinesterase. Biochemistry 45 (2006) 7529-7543
-
(2006)
Biochemistry
, vol.45
, pp. 7529-7543
-
-
Suarez, D.1
Diaz, N.2
Fontecilla-Camps, J.3
Field, M.J.4
-
43
-
-
0032497424
-
Butyrylcholinesterase-catalysed hydrolysis of aspirin, a negatively charged ester, and aspirin-related neutral esters
-
Masson P., Froment M.-T., Fortier P.-L., Visicchio J.-E., Bartels C.F., and Lockridge O. Butyrylcholinesterase-catalysed hydrolysis of aspirin, a negatively charged ester, and aspirin-related neutral esters. Biochim. Biophys. Acta 1387 (1998) 41-52
-
(1998)
Biochim. Biophys. Acta
, vol.1387
, pp. 41-52
-
-
Masson, P.1
Froment, M.-T.2
Fortier, P.-L.3
Visicchio, J.-E.4
Bartels, C.F.5
Lockridge, O.6
-
44
-
-
0023241821
-
Kinetic evidence for thermally induced conformational change of butyrylcholinesterase
-
Ferro A., and Masson P. Kinetic evidence for thermally induced conformational change of butyrylcholinesterase. Biochim. Biophys. Acta 916 (1987) 193-199
-
(1987)
Biochim. Biophys. Acta
, vol.916
, pp. 193-199
-
-
Ferro, A.1
Masson, P.2
-
46
-
-
0031713093
-
Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon
-
Amitai G., Moorad D., Adani R., and Doctor B.P. Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon. Biochem. Pharmacol. 56 (1998) 293-299
-
(1998)
Biochem. Pharmacol.
, vol.56
, pp. 293-299
-
-
Amitai, G.1
Moorad, D.2
Adani, R.3
Doctor, B.P.4
-
47
-
-
11644261806
-
Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
-
Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., and Olson A.J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19 (1998) 1639-1662
-
(1998)
J. Comput. Chem.
, vol.19
, pp. 1639-1662
-
-
Morris, G.M.1
Goodsell, D.S.2
Halliday, R.S.3
Huey, R.4
Hart, W.E.5
Belew, R.K.6
Olson, A.J.7
-
48
-
-
33845986579
-
-
http://www.webmo.net (WebMO, LCC all rights reserved).
-
-
-
-
49
-
-
0031473847
-
SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
-
Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
-
(1997)
Electrophoresis
, vol.18
, pp. 2714-2723
-
-
Guex, N.1
Peitsch, M.C.2
-
50
-
-
28744450737
-
Hysteresis of butyrylcholinesterase in the approach to steady-state
-
Masson P., Schopfer L.M., Froment M.-T., Debouzy J.C., Nachon F., Gillon E., Lockridge O., Hrabovska A., and Goldstein B.N. Hysteresis of butyrylcholinesterase in the approach to steady-state. Chem.-Biol. Interact. 157-158C (2005) 143-152
-
(2005)
Chem.-Biol. Interact.
, vol.157-158 C
, pp. 143-152
-
-
Masson, P.1
Schopfer, L.M.2
Froment, M.-T.3
Debouzy, J.C.4
Nachon, F.5
Gillon, E.6
Lockridge, O.7
Hrabovska, A.8
Goldstein, B.N.9
-
51
-
-
0014332140
-
Kinetics of hydrolysis of the phenyl analog of acetylcholine under the action of horse serum cholinesterase and bovine erythrocyte acetylcholinesterase
-
Brestkin A.P., Brik I.L., and Teplov N.E. Kinetics of hydrolysis of the phenyl analog of acetylcholine under the action of horse serum cholinesterase and bovine erythrocyte acetylcholinesterase. Biokhimiya 33 (1968) 1059-1068
-
(1968)
Biokhimiya
, vol.33
, pp. 1059-1068
-
-
Brestkin, A.P.1
Brik, I.L.2
Teplov, N.E.3
-
52
-
-
0022493194
-
Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase
-
Bazelyansky M., Robey E., and Kirsh J.F. Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. Biochemistry 25 (1986) 125-130
-
(1986)
Biochemistry
, vol.25
, pp. 125-130
-
-
Bazelyansky, M.1
Robey, E.2
Kirsh, J.F.3
-
53
-
-
0033837738
-
A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases
-
Ayala Y.M., and Di Cera E. A simple method for the determination of individual rate constants for substrate hydrolysis by serine proteases. Prot. Sci. 9 (2000) 1589-1593
-
(2000)
Prot. Sci.
, vol.9
, pp. 1589-1593
-
-
Ayala, Y.M.1
Di Cera, E.2
-
54
-
-
1242338790
-
The condition for pseudo-first-order kinetics in enzymatic reactions is independent of the initial enzyme concentration
-
Schnell S., and Mendoza C. The condition for pseudo-first-order kinetics in enzymatic reactions is independent of the initial enzyme concentration. Biophys. Chem. 107 (2004) 165-174
-
(2004)
Biophys. Chem.
, vol.107
, pp. 165-174
-
-
Schnell, S.1
Mendoza, C.2
-
55
-
-
0032518976
-
Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration
-
Marcel V., Gagnoux-Palacios L., Pertuy C., Masson P., and Fournier D. Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration. Biochem. J. 329 (1998) 329-334
-
(1998)
Biochem. J.
, vol.329
, pp. 329-334
-
-
Marcel, V.1
Gagnoux-Palacios, L.2
Pertuy, C.3
Masson, P.4
Fournier, D.5
-
56
-
-
0016157081
-
A steady-state kinetic model of butyrylcholinesterase from horse plasma
-
Augustinson K.B., Bartfai T., and Mannervik B. A steady-state kinetic model of butyrylcholinesterase from horse plasma. Biochem. J. 141 (1974) 825-834
-
(1974)
Biochem. J.
, vol.141
, pp. 825-834
-
-
Augustinson, K.B.1
Bartfai, T.2
Mannervik, B.3
-
57
-
-
0019321441
-
Resolution and purification of two monomeric butyrylcholinesterases from rabbit liver
-
Rush R.S., Main A.R., Miller S.K., and Kilpatrick B.F. Resolution and purification of two monomeric butyrylcholinesterases from rabbit liver. J. Biol. Chem. 255 (1980) 7155-7160
-
(1980)
J. Biol. Chem.
, vol.255
, pp. 7155-7160
-
-
Rush, R.S.1
Main, A.R.2
Miller, S.K.3
Kilpatrick, B.F.4
-
59
-
-
0014152148
-
Kinetic of enzymatic hydrolysis of phenylacetate
-
Volkova R.I. Kinetic of enzymatic hydrolysis of phenylacetate. Biokhimiya 32 (1967) 1253-1259
-
(1967)
Biokhimiya
, vol.32
, pp. 1253-1259
-
-
Volkova, R.I.1
-
60
-
-
0015425090
-
Acetylcholinesterase substrates: acetoxymethylpyridines and benzyl acetate
-
Steinberg G.M., Thomas N.C., Mednick M.L., and Amshey J.W. Acetylcholinesterase substrates: acetoxymethylpyridines and benzyl acetate. J. Pharm. Sci. 61 (1972) 1735-1738
-
(1972)
J. Pharm. Sci.
, vol.61
, pp. 1735-1738
-
-
Steinberg, G.M.1
Thomas, N.C.2
Mednick, M.L.3
Amshey, J.W.4
-
61
-
-
0017076526
-
Structure-activity relationships in acetylcholinesterase reactions
-
Jarv J., Kesvatera T., and Aaviksaar A. Structure-activity relationships in acetylcholinesterase reactions. Eur. J. Biochem. 67 (1976) 315-322
-
(1976)
Eur. J. Biochem.
, vol.67
, pp. 315-322
-
-
Jarv, J.1
Kesvatera, T.2
Aaviksaar, A.3
-
62
-
-
0027273738
-
Recombinant human butyrylcholinesterase G390, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant
-
Masson P., Adkins S., Gouet P., and Lockridge O. Recombinant human butyrylcholinesterase G390, 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
-
63
-
-
0032944436
-
An improved cocaine hydrolase: the A328Y mutant of human butyrylcholinesterase
-
Xie W., Varkey-Altamirano C., Bartels C.F., Speirs R.J., Cashman J.R., and Lockridge O. An improved cocaine hydrolase: the A328Y mutant of human butyrylcholinesterase. Mol. Pharmacol. 55 (1999) 83-91
-
(1999)
Mol. Pharmacol.
, vol.55
, pp. 83-91
-
-
Xie, W.1
Varkey-Altamirano, C.2
Bartels, C.F.3
Speirs, R.J.4
Cashman, J.R.5
Lockridge, O.6
-
64
-
-
0031868426
-
Cocaine benzoyl thioester: synthesis, kinetics of base hydrolysis, and application to the assay of cocaine esterases
-
Cashman J.R., Berkman C.E., Underiner G., Kolly C.A., and Hunter A.D. Cocaine benzoyl thioester: synthesis, kinetics of base hydrolysis, and application to the assay of cocaine esterases. Chem. Res. Toxicol. 11 (1998) 895-901
-
(1998)
Chem. Res. Toxicol.
, vol.11
, pp. 895-901
-
-
Cashman, J.R.1
Berkman, C.E.2
Underiner, G.3
Kolly, C.A.4
Hunter, A.D.5
-
65
-
-
0242669341
-
Fundamental reaction mechanism for cocaine hydrolysis in human butyrylcholinesterase
-
Zhan C.-G., Zheng F., and Landrey D.W. Fundamental reaction mechanism for cocaine hydrolysis in human butyrylcholinesterase. J. Am. Chem. Soc. 125 (2003) 2462-2474
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 2462-2474
-
-
Zhan, C.-G.1
Zheng, F.2
Landrey, D.W.3
-
66
-
-
0000736637
-
The catalysis of the hydrolysis of phenylacetates by imidazole
-
Bruice T.C., and Schmir G.L. The catalysis of the hydrolysis of phenylacetates by imidazole. J. Am. Chem. Soc. 79 (1957) 1663-1667
-
(1957)
J. Am. Chem. Soc.
, vol.79
, pp. 1663-1667
-
-
Bruice, T.C.1
Schmir, G.L.2
-
67
-
-
0001471822
-
Parallel mechanism in acetylcholinesterase-catalyzed hydrolysis of choline esters
-
Selwood T., Feaster S.R., States M.J., Pryor A.N., and Quinn D.M. Parallel mechanism in acetylcholinesterase-catalyzed hydrolysis of choline esters. J. Am. Chem. Soc. 115 (1993) 10477-10482
-
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 10477-10482
-
-
Selwood, T.1
Feaster, S.R.2
States, M.J.3
Pryor, A.N.4
Quinn, D.M.5
-
68
-
-
0014270409
-
Trialkylphosphate and phosphorothiolate anticholinesterases. I. Amiton analogs
-
Bracha P., and O'Brien R.D. Trialkylphosphate and phosphorothiolate anticholinesterases. I. Amiton analogs. Biochemistry 7 (1968) 1545-1554
-
(1968)
Biochemistry
, vol.7
, pp. 1545-1554
-
-
Bracha, P.1
O'Brien, R.D.2
-
69
-
-
0035823872
-
Understanding the relative acyl-transfer reactivity of oxoesters and thioesters: computational analysis of transition state delocalization effects
-
Yang W., and Drueckhammer D.G. Understanding the relative acyl-transfer reactivity of oxoesters and thioesters: computational analysis of transition state delocalization effects. J. Am. Chem. Soc. 123 (2001) 11004-11009
-
(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 11004-11009
-
-
Yang, W.1
Drueckhammer, D.G.2
-
70
-
-
0014959666
-
Hydrolysis of electronically and sterically defined substrates of acetylcholinesterase
-
Hillman G.R., and Mautner H.G. Hydrolysis of electronically and sterically defined substrates of acetylcholinesterase. Biochemistry 9 (1970) 2633-2638
-
(1970)
Biochemistry
, vol.9
, pp. 2633-2638
-
-
Hillman, G.R.1
Mautner, H.G.2
-
72
-
-
0014553523
-
Acetylcholine and its thiolester and selenoester analogs: conformation, electron distribution, and biological activity
-
Shefter E., and Mautner H.G. Acetylcholine and its thiolester and selenoester analogs: conformation, electron distribution, and biological activity. Proc. Natl. Acad. Sci. U. S. A. 63 (1969) 1253-1260
-
(1969)
Proc. Natl. Acad. Sci. U. S. A.
, vol.63
, pp. 1253-1260
-
-
Shefter, E.1
Mautner, H.G.2
-
73
-
-
0015344197
-
On the conformation of acetylcholine and acetylthiocholine
-
Pullman B., and Courriere P. On the conformation of acetylcholine and acetylthiocholine. Mol. Pharmacol. 8 (1972) 371-373
-
(1972)
Mol. Pharmacol.
, vol.8
, pp. 371-373
-
-
Pullman, B.1
Courriere, P.2
-
74
-
-
0017780677
-
CNDO/2 conformational analysis of acetylselenocholine
-
Chidichimo G., Lelj F., and Russo N. CNDO/2 conformational analysis of acetylselenocholine. J. Theor. Biol. 66 (1977) 811-814
-
(1977)
J. Theor. Biol.
, vol.66
, pp. 811-814
-
-
Chidichimo, G.1
Lelj, F.2
Russo, N.3
-
75
-
-
33947296738
-
A study of the effects of replacing either of the oxygens of the ester group by sulfur and selenium
-
Wallmark I., Krachov M.H., Chu S.H., and Mautner H.G. A study of the effects of replacing either of the oxygens of the ester group by sulfur and selenium. J. Am. Chem. Soc. 92 (1970) 4447-4450
-
(1970)
J. Am. Chem. Soc.
, vol.92
, pp. 4447-4450
-
-
Wallmark, I.1
Krachov, M.H.2
Chu, S.H.3
Mautner, H.G.4
-
76
-
-
17044457879
-
Structural basis for selectivity of butyrylcholinesterase towards enantiomeric quinuclidin-3-yl benzoates: a quantum chemical study
-
Primozic I., Hrenar T., Tomic S., and Meic Z. Structural basis for selectivity of butyrylcholinesterase towards enantiomeric quinuclidin-3-yl benzoates: a quantum chemical study. Croat. Chem. Acta 76 (2003) 93-99
-
(2003)
Croat. Chem. Acta
, vol.76
, pp. 93-99
-
-
Primozic, I.1
Hrenar, T.2
Tomic, S.3
Meic, Z.4
-
77
-
-
0014320575
-
The importance of steric and stereochemical features in serum cholinesterase substrates
-
Beckett A.H., Mitchard M., and Clitherow J.W. The importance of steric and stereochemical features in serum cholinesterase substrates. Biochem. Pharmacol. 17 (1968) 1601-1607
-
(1968)
Biochem. Pharmacol.
, vol.17
, pp. 1601-1607
-
-
Beckett, A.H.1
Mitchard, M.2
Clitherow, J.W.3
-
78
-
-
0002232722
-
Dialkoxy-phosphorylthiocholines, alkoxy-methyl phosphoryl thiocholines and analogous choline esters
-
Tammelin L.E. Dialkoxy-phosphorylthiocholines, alkoxy-methyl phosphoryl thiocholines and analogous choline esters. Acta Chem. Scand. 11 (1957) 1340-1349
-
(1957)
Acta Chem. Scand.
, vol.11
, pp. 1340-1349
-
-
Tammelin, L.E.1
-
79
-
-
0029142579
-
Specificity and orientation of trigonal carboxyl esters and tetrahedral alkylphosphonyl esters in cholinesterases
-
Hosea N.A., Berman H.A., and Taylor P. Specificity and orientation of trigonal carboxyl esters and tetrahedral alkylphosphonyl esters in cholinesterases. Biochemistry 34 (1995) 11528-11536
-
(1995)
Biochemistry
, vol.34
, pp. 11528-11536
-
-
Hosea, N.A.1
Berman, H.A.2
Taylor, P.3
-
80
-
-
27144551946
-
The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetraehedral intermediate
-
Tormos J.R., Wiley K.L., Seravalli J., Nachon F., Masson P., Nicolet Y., and Quinn D.M. The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetraehedral intermediate. J. Am. Chem. Soc. 127 (2005) 14538-14539
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 14538-14539
-
-
Tormos, J.R.1
Wiley, K.L.2
Seravalli, J.3
Nachon, F.4
Masson, P.5
Nicolet, Y.6
Quinn, D.M.7
-
81
-
-
28444433108
-
Catalytic mechanism and energy barriers for butyrylcholinesterase-catalyzed hydrolysis of cocaine
-
Zhan C.-G., and Gao D. Catalytic mechanism and energy barriers for butyrylcholinesterase-catalyzed hydrolysis of cocaine. Biophys. J. 89 (2005) 3863-3872
-
(2005)
Biophys. J.
, vol.89
, pp. 3863-3872
-
-
Zhan, C.-G.1
Gao, D.2
-
82
-
-
0022994346
-
Acetylcholinesterase inhibition by sulphur and selenium heterosubstituted isomers of N,N-diethylcarbamyl choline and carbaryl
-
Lindgren B., Lindgren G., Artursson E., and Puu G. Acetylcholinesterase inhibition by sulphur and selenium heterosubstituted isomers of N,N-diethylcarbamyl choline and carbaryl. J. Enz. Inhib. 1 (1985) 1-11
-
(1985)
J. Enz. Inhib.
, vol.1
, pp. 1-11
-
-
Lindgren, B.1
Lindgren, G.2
Artursson, E.3
Puu, G.4
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