Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands
Nolte H-J, Rosenberry TL, Neumann E (1980)
Biochemistry 19(16): 3705-3711.
Zeitschriftenaufsatz
| Veröffentlicht | Englisch
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Autor*in
Nolte, Hans-Jürgen;
Rosenberry, Terrone L.;
Neumann, EberhardUniBi
Einrichtung
Stichworte
Molecular Biology;
Biochemistry
Erscheinungsjahr
1980
Zeitschriftentitel
Biochemistry
Band
19
Ausgabe
16
Seite(n)
3705-3711
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1774427
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Nolte H-J, Rosenberry TL, Neumann E. Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands. Biochemistry. 1980;19(16):3705-3711.
Nolte, H. - J., Rosenberry, T. L., & Neumann, E. (1980). Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands. Biochemistry, 19(16), 3705-3711. https://doi.org/10.1021/bi00557a011
Nolte, Hans-Jürgen, Rosenberry, Terrone L., and Neumann, Eberhard. 1980. “Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands”. Biochemistry 19 (16): 3705-3711.
Nolte, H. - J., Rosenberry, T. L., and Neumann, E. (1980). Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands. Biochemistry 19, 3705-3711.
Nolte, H.-J., Rosenberry, T.L., & Neumann, E., 1980. Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands. Biochemistry, 19(16), p 3705-3711.
H.-J. Nolte, T.L. Rosenberry, and E. Neumann, “Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands”, Biochemistry, vol. 19, 1980, pp. 3705-3711.
Nolte, H.-J., Rosenberry, T.L., Neumann, E.: Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands. Biochemistry. 19, 3705-3711 (1980).
Nolte, Hans-Jürgen, Rosenberry, Terrone L., and Neumann, Eberhard. “Effective charge on acetylcholinesterase active sites determined from the ionic strength dependence of association rate constants with cationic ligands”. Biochemistry 19.16 (1980): 3705-3711.
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PMID: 28869561
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PMID: 28869561
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PMID: 26547432
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Masson P, Lushchekina S, Schopfer LM, Lockridge O., Biochem J 454(3), 2013
PMID: 23782236
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PMID: 24053466
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PMID: 24053466
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Berg L, Andersson CD, Artursson E, Hörnberg A, Tunemalm AK, Linusson A, Ekström F., PLoS One 6(11), 2011
PMID: 22140425
Berg L, Andersson CD, Artursson E, Hörnberg A, Tunemalm AK, Linusson A, Ekström F., PLoS One 6(11), 2011
PMID: 22140425
Acetylcholinesterase: from 3D structure to function.
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PMID: 20138030
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PMID: 20138030
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Kamal MA, Klein P, Luo W, Li Y, Holloway HW, Tweedie D, Greig NH., Neurochem Res 33(5), 2008
PMID: 17985237
Kamal MA, Klein P, Luo W, Li Y, Holloway HW, Tweedie D, Greig NH., Neurochem Res 33(5), 2008
PMID: 17985237
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Zimmermann M, Grösgen S, Westwell MS, Greenfield SA., J Neurochem 104(1), 2008
PMID: 17986217
Zimmermann M, Grösgen S, Westwell MS, Greenfield SA., J Neurochem 104(1), 2008
PMID: 17986217
Acetylcholinesterase: mechanisms of covalent inhibition of H447I mutant determined by computational analyses.
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PMID: 18657802
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PMID: 18657802
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PMID: 17055616
Correa-Basurto J, Flores-Sandoval C, Marín-Cruz J, Rojo-Domínguez A, Espinoza-Fonseca LM, Trujillo-Ferrara JG., Eur J Med Chem 42(1), 2007
PMID: 17055616
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Cheng Y, Suen JK, Zhang D, Bond SD, Zhang Y, Song Y, Baker NA, Bajaj CL, Holst MJ, McCammon JA., Biophys J 92(10), 2007
PMID: 17307827
Cheng Y, Suen JK, Zhang D, Bond SD, Zhang Y, Song Y, Baker NA, Bajaj CL, Holst MJ, McCammon JA., Biophys J 92(10), 2007
PMID: 17307827
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PMID: 17847707
Wiesner J, Kriz Z, Kuca K, Jun D, Koca J., J Enzyme Inhib Med Chem 22(4), 2007
PMID: 17847707
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PMID: 16751247
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PMID: 16751247
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PMID: 16751249
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PMID: 16817854
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PMID: 16817854
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PMID: 15739192
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PMID: 15739192
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PMID: 15994894
Ramos AS, Techert S., Biophys J 89(3), 2005
PMID: 15994894
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PMID: 15041644
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PMID: 14501022
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Nunes-Tavares N, Nery da Matta A, Batista e Silva CM, Araújo GM, Louro SR, Hassón-Voloch A., Int J Biochem Cell Biol 34(9), 2002
PMID: 12009302
Nunes-Tavares N, Nery da Matta A, Batista e Silva CM, Araújo GM, Louro SR, Hassón-Voloch A., Int J Biochem Cell Biol 34(9), 2002
PMID: 12009302
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PMID: 10692319
Song XZ, Pedersen SE., Biophys J 78(3), 2000
PMID: 10692319
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Van Belle D, De Maria L, Iurcu G, Wodak SJ., J Mol Biol 298(4), 2000
PMID: 10788331
Van Belle D, De Maria L, Iurcu G, Wodak SJ., J Mol Biol 298(4), 2000
PMID: 10788331
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Malany S, Baker N, Verweyst M, Medhekar R, Quinn DM, Velan B, Kronman C, Shafferman A., Chem Biol Interact 119-120(), 1999
PMID: 10421443
Malany S, Baker N, Verweyst M, Medhekar R, Quinn DM, Velan B, Kronman C, Shafferman A., Chem Biol Interact 119-120(), 1999
PMID: 10421443
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PMID: 10423544
Tara S, Helms V, Straatsma TP, McCammon JA., Biopolymers 50(4), 1999
PMID: 10423544
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Botti SA, Felder CE, Lifson S, Sussman JL, Silman I., Biophys J 77(5), 1999
PMID: 10545346
Botti SA, Felder CE, Lifson S, Sussman JL, Silman I., Biophys J 77(5), 1999
PMID: 10545346
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PMID: 10631970
Arnon R, Silman I, Tarrab-Hazdai R., Protein Sci 8(12), 1999
PMID: 10631970
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Zhou HX, Wlodek ST, McCammon JA., Proc Natl Acad Sci U S A 95(16), 1998
PMID: 9689071
Zhou HX, Wlodek ST, McCammon JA., Proc Natl Acad Sci U S A 95(16), 1998
PMID: 9689071
Rapid binding of a cationic active site inhibitor to wild type and mutant mouse acetylcholinesterase: Brownian dynamics simulation including diffusion in the active site gorge.
Tara S, Elcock AH, Kirchhoff PD, Briggs JM, Radic Z, Taylor P, McCammon JA., Biopolymers 46(7), 1998
PMID: 9838872
Tara S, Elcock AH, Kirchhoff PD, Briggs JM, Radic Z, Taylor P, McCammon JA., Biopolymers 46(7), 1998
PMID: 9838872
Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.
Ledvina PS, Tsai AL, Wang Z, Koehl E, Quiocho FA., Protein Sci 7(12), 1998
PMID: 9865949
Ledvina PS, Tsai AL, Wang Z, Koehl E, Quiocho FA., Protein Sci 7(12), 1998
PMID: 9865949
Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin.
Radić Z, Kirchhoff PD, Quinn DM, McCammon JA, Taylor P., J Biol Chem 272(37), 1997
PMID: 9287336
Radić Z, Kirchhoff PD, Quinn DM, McCammon JA, Taylor P., J Biol Chem 272(37), 1997
PMID: 9287336
External and internal electrostatic potentials of cholinesterase models.
Felder CE, Botti SA, Lifson S, Silman I, Sussman JL., J Mol Graph Model 15(5), 1997
PMID: 9640563
Felder CE, Botti SA, Lifson S, Silman I, Sussman JL., J Mol Graph Model 15(5), 1997
PMID: 9640563
Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase.
Porschke D, Créminon C, Cousin X, Bon C, Sussman J, Silman I., Biophys J 70(4), 1996
PMID: 8785319
Porschke D, Créminon C, Cousin X, Bon C, Sussman J, Silman I., Biophys J 70(4), 1996
PMID: 8785319
Electrostatic interactions of the butyrylcholinesterase dimer of mucosal cells of rat intestine with glycosaminoglycans.
Sine JP, Colas B., Int J Biochem Cell Biol 28(5), 1996
PMID: 8697103
Sine JP, Colas B., Int J Biochem Cell Biol 28(5), 1996
PMID: 8697103
Acetylcholinesterase: role of the enzyme's charge distribution in steering charged ligands toward the active site.
Antosiewicz J, Wlodek ST, McCammon JA., Biopolymers 39(1), 1996
PMID: 8924629
Antosiewicz J, Wlodek ST, McCammon JA., Biopolymers 39(1), 1996
PMID: 8924629
Fasciculin 2 binds to the peripheral site on acetylcholinesterase and inhibits substrate hydrolysis by slowing a step involving proton transfer during enzyme acylation.
Eastman J, Wilson EJ, Cerveñansky C, Rosenberry TL., J Biol Chem 270(34), 1995
PMID: 7649979
Eastman J, Wilson EJ, Cerveñansky C, Rosenberry TL., J Biol Chem 270(34), 1995
PMID: 7649979
Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL., Structure 3(12), 1995
PMID: 8747462
Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL., Structure 3(12), 1995
PMID: 8747462
Efficient product clearance through exit channels in substrate hydrolysis by acetylcholinesterase.
Kovach IM, Qian N, Bencsura A., FEBS Lett 349(1), 1994
PMID: 8045303
Kovach IM, Qian N, Bencsura A., FEBS Lett 349(1), 1994
PMID: 8045303
Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase.
Shafferman A, Ordentlich A, Barak D, Kronman C, Ber R, Bino T, Ariel N, Osman R, Velan B., EMBO J 13(15), 1994
PMID: 8062821
Shafferman A, Ordentlich A, Barak D, Kronman C, Ber R, Bino T, Ariel N, Osman R, Velan B., EMBO J 13(15), 1994
PMID: 8062821
An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase.
Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL., Proc Natl Acad Sci U S A 90(11), 1993
PMID: 8506359
Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL., Proc Natl Acad Sci U S A 90(11), 1993
PMID: 8506359
Molecular and cellular biology of cholinesterases.
Massoulié J, Pezzementi L, Bon S, Krejci E, Vallette FM., Prog Neurobiol 41(1), 1993
PMID: 8321908
Massoulié J, Pezzementi L, Bon S, Krejci E, Vallette FM., Prog Neurobiol 41(1), 1993
PMID: 8321908
Structure-function relationship studies in human cholinesterases reveal genomic origins for individual variations in cholinergic drug responses.
Loewenstein Y, Gnatt A, Neville LF, Zakut H, Soreq H., Prog Neuropsychopharmacol Biol Psychiatry 17(6), 1993
PMID: 8278601
Loewenstein Y, Gnatt A, Neville LF, Zakut H, Soreq H., Prog Neuropsychopharmacol Biol Psychiatry 17(6), 1993
PMID: 8278601
Intramolecular relationships in cholinesterases revealed by oocyte expression of site-directed and natural variants of human BCHE.
Neville LF, Gnatt A, Loewenstein Y, Seidman S, Ehrlich G, Soreq H., EMBO J 11(4), 1992
PMID: 1373381
Neville LF, Gnatt A, Loewenstein Y, Seidman S, Ehrlich G, Soreq H., EMBO J 11(4), 1992
PMID: 1373381
Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I., Science 253(5022), 1991
PMID: 1678899
Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I., Science 253(5022), 1991
PMID: 1678899
Substrate-binding sites in acetylcholinesterase.
Hucho F, Järv J, Weise C., Trends Pharmacol Sci 12(11), 1991
PMID: 1796496
Hucho F, Järv J, Weise C., Trends Pharmacol Sci 12(11), 1991
PMID: 1796496
Anionic subsites of the acetylcholinesterase from Torpedo californica: affinity labelling with the cationic reagent N,N-dimethyl-2-phenyl-aziridinium.
Weise C, Kreienkamp HJ, Raba R, Pedak A, Aaviksaar A, Hucho F., EMBO J 9(12), 1990
PMID: 2249655
Weise C, Kreienkamp HJ, Raba R, Pedak A, Aaviksaar A, Hucho F., EMBO J 9(12), 1990
PMID: 2249655
Reflections on the kinetics of substrate binding.
Gutfreund H., Biophys Chem 26(2-3), 1987
PMID: 3607224
Gutfreund H., Biophys Chem 26(2-3), 1987
PMID: 3607224
Acetylcholinesterase as polyelectrolyte in reaction with cationic substrates.
Tóugu V, Pedak A, Kesvatera T, Aaviksaar A., FEBS Lett 225(1-2), 1987
PMID: 3691807
Tóugu V, Pedak A, Kesvatera T, Aaviksaar A., FEBS Lett 225(1-2), 1987
PMID: 3691807
Chemical electric field effects in biological macromolecules.
Neumann E., Prog Biophys Mol Biol 47(3), 1986
PMID: 3544052
Neumann E., Prog Biophys Mol Biol 47(3), 1986
PMID: 3544052
Ionic strength dependence of the inhibition of acetylcholinesterase activity by Al3+.
Sharp TR, Rosenberry TL., Biophys Chem 21(3-4), 1985
PMID: 3986284
Sharp TR, Rosenberry TL., Biophys Chem 21(3-4), 1985
PMID: 3986284
Detergent-soluble form of acetylcholinesterase in the electric organ of electric rays. Its isolation, characterization and monoclonal antibodies.
Sakai M, Saisu H, Koshigoe N, Abe T., Eur J Biochem 148(1), 1985
PMID: 3979394
Sakai M, Saisu H, Koshigoe N, Abe T., Eur J Biochem 148(1), 1985
PMID: 3979394
Chemical representation of ion flux gating in excitable biomembranes.
Neumann E., Neurochem Int 2C(), 1980
PMID: 20487768
Neumann E., Neurochem Int 2C(), 1980
PMID: 20487768
Electric-field induced effects in acetylcholinesterase.
Fringeli UP, Hofer P., Neurochem Int 2C(), 1980
PMID: 20487782
Fringeli UP, Hofer P., Neurochem Int 2C(), 1980
PMID: 20487782
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