Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata

Heidmann T, Bernhardt J, Neumann E, Changeux JP (1983)
Biochemistry 22(23): 5452-5459.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Heidmann, Thierry; Bernhardt, Julius; Neumann, EberhardUniBi; Changeux, Jean Pierre
Stichworte
Molecular biology; Biochemistry
Erscheinungsjahr
1983
Zeitschriftentitel
Biochemistry
Band
22
Ausgabe
23
Seite(n)
5452-5459
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1774953

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Heidmann T, Bernhardt J, Neumann E, Changeux JP. Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata. Biochemistry. 1983;22(23):5452-5459.
Heidmann, T., Bernhardt, J., Neumann, E., & Changeux, J. P. (1983). Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata. Biochemistry, 22(23), 5452-5459. https://doi.org/10.1021/bi00292a029
Heidmann, Thierry, Bernhardt, Julius, Neumann, Eberhard, and Changeux, Jean Pierre. 1983. “Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata”. Biochemistry 22 (23): 5452-5459.
Heidmann, T., Bernhardt, J., Neumann, E., and Changeux, J. P. (1983). Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata. Biochemistry 22, 5452-5459.
Heidmann, T., et al., 1983. Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata. Biochemistry, 22(23), p 5452-5459.
T. Heidmann, et al., “Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata”, Biochemistry, vol. 22, 1983, pp. 5452-5459.
Heidmann, T., Bernhardt, J., Neumann, E., Changeux, J.P.: Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata. Biochemistry. 22, 5452-5459 (1983).
Heidmann, Thierry, Bernhardt, Julius, Neumann, Eberhard, and Changeux, Jean Pierre. “Rapid kinetics of agonist binding and permeability response analyzed in parallel on acetylcholine receptor rich membranes from Torpedo marmorata”. Biochemistry 22.23 (1983): 5452-5459.
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54 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

The nicotinic acetylcholine receptor: a typical 'allosteric machine'.
Changeux JP., Philos Trans R Soc Lond B Biol Sci 373(1749), 2018
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Agonists binding nicotinic receptors elicit specific channel-opening patterns at αγ and αδ sites.
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Hysteresis of ligand binding in CNGA2 ion channels.
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Increased agonist affinity at the μ-opioid receptor induced by prolonged agonist exposure.
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Allosteric receptors: from electric organ to cognition.
Changeux JP., Annu Rev Pharmacol Toxicol 50(), 2010
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Fluorescent agonists for the Torpedo nicotinic acetylcholine receptor.
Krieger F, Mourot A, Araoz R, Kotzyba-Hibert F, Molgó J, Bamberg E, Goeldner M., Chembiochem 9(7), 2008
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Electrostatic steering at acetylcholine binding sites.
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Karlin A., Nat Rev Neurosci 3(2), 2002
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Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints.
Martinez KL, Gohon Y, Corringer PJ, Tribet C, Mérola F, Changeux JP, Popot JL., FEBS Lett 528(1-3), 2002
PMID: 12297315
The nicotinic receptor ligand binding domain.
Sine SM., J Neurobiol 53(4), 2002
PMID: 12436411
Thermal imaging of receptor-activated heat production in single cells.
Zohar O, Ikeda M, Shinagawa H, Inoue H, Nakamura H, Elbaum D, Alkon DL, Yoshioka T., Biophys J 74(1), 1998
PMID: 9449312
The location of the gate in the acetylcholine receptor channel.
Wilson GG, Karlin A., Neuron 20(6), 1998
PMID: 9655513
Allosteric receptors after 30 years.
Changeux JP, Edelstein SJ., Neuron 21(5), 1998
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The initiation of the muscle action potential.
Neumann E, Weber J, Schürholz T., Arch Physiol Biochem 104(6), 1996
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Allosteric regulation of [3H]vinblastine binding to P-glycoprotein of MCF-7 ADR cells by dexniguldipine.
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Neuronal nicotinic receptors: molecular organization and regulations.
Galzi JL, Changeux JP., Neuropharmacology 34(6), 1995
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On allosteric mechanisms and acetylcholine receptors.
Changeux JP, Edelstein SJ., Trends Biochem Sci 19(10), 1994
PMID: 7817393
Functional architecture of the nicotinic acetylcholine receptor: a prototype of ligand-gated ion channels.
Devillers-Thiéry A, Galzi JL, Eiselé JL, Bertrand S, Bertrand D, Changeux JP., J Membr Biol 136(2), 1993
PMID: 7508983
Unconventional pharmacology of a neuronal nicotinic receptor mutated in the channel domain.
Bertrand D, Devillers-Thiéry A, Revah F, Galzi JL, Hussy N, Mulle C, Bertrand S, Ballivet M, Changeux JP., Proc Natl Acad Sci U S A 89(4), 1992
PMID: 1741378
The functional architecture of the acetylcholine nicotinic receptor explored by affinity labelling and site-directed mutagenesis.
Changeux JP, Galzi JL, Devillers-Thiéry A, Bertrand D., Q Rev Biophys 25(4), 1992
PMID: 1293635
Desensitization of central cholinergic mechanisms and neuroadaptation to nicotine.
Ochoa EL, Li L, McNamee MG., Mol Neurobiol 4(3-4), 1990
PMID: 2135395
Desensitization of the nicotinic acetylcholine receptor: molecular mechanisms and effect of modulators.
Ochoa EL, Chattopadhyay A, McNamee MG., Cell Mol Neurobiol 9(2), 1989
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Temperature effects on alpha 2-adrenergic receptor-Gi interactions.
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Functional domains of the nicotinic acetylcholine receptor.
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Acetylcholine receptor kinetics: chemical kinetics.
Udgaonkar JB, Hess GP., J Membr Biol 93(2), 1986
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Muscarinic cholinergic receptor in the human heart evidenced under physiological conditions by positron emission tomography.
Syrota A, Comar D, Paillotin G, Davy JM, Aumont MC, Stulzaft O, Maziere B., Proc Natl Acad Sci U S A 82(2), 1985
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Allosteric effects of diprobutine on acetylcholine receptors.
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