Key roles of hydrophobic rings of TM2 in gating of the α9α10 nicotinic cholinergic receptor
暂无分享,去创建一个
C. Bouzat | M. Verbitsky | N. Weisstaub | A. Elgoyhen | P. Plazas | M. E. Gómez-Casati | E. Katz | M. J. Rosa
[1] C. Bouzat,et al. Molecular Basis of the Differential Sensitivity of Nematode and Mammalian Muscle to the Anthelmintic Agent Levamisole* , 2004, Journal of Biological Chemistry.
[2] Y. Fujiyoshi,et al. Structure and gating mechanism of the acetylcholine receptor pore , 2003, Nature.
[3] J. Changeux,et al. The diversity of subunit composition in nAChRs: evolutionary origins, physiologic and pharmacologic consequences. , 2002, Journal of neurobiology.
[4] N. Weisstaub,et al. The α9α10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations , 2002, Hearing Research.
[5] A. Auerbach,et al. Structure of the transition state of gating in the acetylcholine receptor channel pore: a phi-value analysis. , 2002, Biochemistry.
[6] S. Sine,et al. Subunit-selective contribution to channel gating of the M4 domain of the nicotinic receptor. , 2002, Biophysical journal.
[7] S. Panicker,et al. Evidence for a Centrally Located Gate in the Pore of a Serotonin-Gated Ion Channel , 2002, The Journal of Neuroscience.
[8] S. Heinemann,et al. α10: A determinant of nicotinic cholinergic receptor function in mammalian vestibular and cochlear mechanosensory hair cells , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[9] M. Verbitsky,et al. Mixed nicotinic–muscarinic properties of the α9 nicotinic cholinergic receptor , 2000, Neuropharmacology.
[10] S. Heinemann,et al. High calcium permeability and calcium block of the α9 nicotinic acetylcholine receptor , 2000, Hearing Research.
[11] D. S. Weiss,et al. Allosteric Activation Mechanism of the α1β2γ2 γ-Aminobutyric Acid Type A Receptor Revealed by Mutation of the Conserved M2 Leucine , 1999 .
[12] J. Spafford,et al. The effects of level of expression of a jellyfish Shaker potassium channel: a positive potassium feedback mechanism , 1999, The Journal of physiology.
[13] J. Changeux,et al. Mutational Analysis of the Charge Selectivity Filter of the α7 Nicotinic Acetylcholine Receptor , 1999, Neuron.
[14] H. Lester,et al. Backbone Mutations in Transmembrane Domains of a Ligand-Gated Ion Channel Implications for the Mechanism of Gating , 1999, Cell.
[15] D. Colquhoun,et al. Binding, gating, affinity and efficacy: The interpretation of structure‐activity relationships for agonists and of the effects of mutating receptors , 1998, British journal of pharmacology.
[16] A. Karlin,et al. The Location of the Gate in the Acetylcholine Receptor Channel , 1998, Neuron.
[17] D. S. Weiss,et al. Substitutions of the highly conserved M2 leucine create spontaneously opening rho1 gamma-aminobutyric acid receptors. , 1998 .
[18] J. Changeux,et al. Paradoxical allosteric effects of competitive inhibitors on neuronal α7 nicotinic receptor mutants , 1997, Neuroreport.
[19] J P Changeux,et al. Identification of calcium binding sites that regulate potentiation of a neuronal nicotinic acetylcholine receptor. , 1996, The EMBO journal.
[20] R. Papke,et al. An evaluation of neuronal nicotinic acetylcholine receptor activation by quaternary nitrogen compounds indicates that choline is selective for the α7 subtype , 1996, Neuroscience Letters.
[21] L. Ebihara. Xenopus connexin38 forms hemi-gap-junctional channels in the nonjunctional plasma membrane of Xenopus oocytes. , 1996, Biophysical journal.
[22] J. Changeux,et al. The multiple phenotypes of allosteric receptor mutants. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[23] A. Karlin,et al. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins , 1995, Neuron.
[24] G N Filatov,et al. The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating. , 1995, Molecular pharmacology.
[25] Lixin Tang,et al. Channel gating governed symmetrically by conserved leucine residues in the M2 domain of nicotinic receptors , 1995, Nature.
[26] R. Miledi,et al. A monovalent cationic conductance that is blocked by extracellular divalent cations in Xenopus oocytes. , 1995, The Journal of physiology.
[27] J. Changeux,et al. Molecular evolution of the nicotinic acetylcholine receptor: An example of multigene family in excitable cells , 1995, Journal of Molecular Evolution.
[28] S. Sine,et al. Structural basis of the different gating kinetics of fetal and adult acetylcholine receptors , 1994, Neuron.
[29] S. Heinemann,et al. α9: An acetylcholine receptor with novel pharmacological properties expressed in rat cochlear hair cells , 1994, Cell.
[30] A. Karlin,et al. Identification of acetylcholine receptor channel-lining residues in the entire M2 segment of the α subunit , 1994, Neuron.
[31] J. Changeux,et al. Stratification of the channel domain in neurotransmitter receptors. , 1993, Current opinion in cell biology.
[32] Jean-Luc Galzi,et al. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic , 1992, Nature.
[33] J P Changeux,et al. Unconventional pharmacology of a neuronal nicotinic receptor mutated in the channel domain. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[34] J. Changeux,et al. Mutations in the channel domain alter desensitization of a neuronal nicotinic receptor , 1991, Nature.
[35] V. Taglietti,et al. A study of stretch‐activated channels in the membrane of frog oocytes: interactions with Ca2+ ions. , 1988, The Journal of physiology.
[36] B. Sakmann,et al. Multiple conductance states of single acetylcholine receptor channels in embryonic muscle cells , 1981, Nature.
[37] N. Weisstaub,et al. The alpha9alpha10 nicotinic acetylcholine receptor is permeable to and is modulated by divalent cations. , 2002, Hearing research.
[38] D. S. Weiss,et al. Allosteric activation mechanism of the alpha 1 beta 2 gamma 2 gamma-aminobutyric acid type A receptor revealed by mutation of the conserved M2 leucine. , 1999, Biophysical journal.