Number and locations of agonist binding sites required to activate homomeric Cys-loop receptors
about
End-plate acetylcholine receptor: structure, mechanism, pharmacology, and diseaseLigand Activation of the Prokaryotic Pentameric Ligand-Gated Ion Channel ELICInhibition of the Prokaryotic Pentameric Ligand-Gated Ion Channel ELIC by Divalent CationsPrinciples of agonist recognition in Cys-loop receptorsStructural and functional studies of the modulator NS9283 reveal agonist-like mechanism of action at α4β2 nicotinic acetylcholine receptorsA membrane-embedded pathway delivers general anesthetics to two interacting binding sites in the Gloeobacter violaceus ion channel.β Subunit M2-M3 loop conformational changes are uncoupled from α1 β glycine receptor channel gating: implications for human hereditary hyperekplexia.The novel α7β2-nicotinic acetylcholine receptor subtype is expressed in mouse and human basal forebrain: biochemical and pharmacological characterization.Specificity determinants of allosteric modulation in the neuronal nicotinic acetylcholine receptor: a fine line between inhibition and potentiationThe effective opening of nicotinic acetylcholine receptors with single agonist binding sitesIn glycine and GABA(A) channels, different subunits contribute asymmetrically to channel conductance via residues in the extracellular domain.An Accessory Agonist Binding Site Promotes Activation of α4β2* Nicotinic Acetylcholine Receptors.Transcriptome Analysis of the Central and Peripheral Nervous Systems of the Spider Cupiennius salei Reveals Multiple Putative Cys-Loop Ligand Gated Ion Channel Subunits and an Acetylcholine Binding Protein.α7-Containing and non-α7-containing nicotinic receptors respond differently to spillover of acetylcholine.Stoichiometry for α-bungarotoxin block of α7 acetylcholine receptors.A Novel α2/α4 Subtype-selective Positive Allosteric Modulator of Nicotinic Acetylcholine Receptors Acting from the C-tail of an α SubunitActivation of α7 nicotinic receptors by orthosteric and allosteric agonists: influence on single-channel kinetics and conductanceAsymmetric ligand binding facilitates conformational transitions in pentameric ligand-gated ion channels.Stoichiometry for drug potentiation of a pentameric ion channelPropofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activationAn ER-resident membrane protein complex regulates nicotinic acetylcholine receptor subunit composition at the synapse.Single-channel kinetic analysis for activation and desensitization of homomeric 5-HT(3)A receptors.The unique α4+/-α4 agonist binding site in (α4)3(β2)2 subtype nicotinic acetylcholine receptors permits differential agonist desensitization pharmacology versus the (α4)2(β2)3 subtypeStoichiometry for activation of neuronal α7 nicotinic receptors.Functional relationships between agonist binding sites and coupling regions of homomeric Cys-loop receptorsComplex between α-bungarotoxin and an α7 nicotinic receptor ligand-binding domain chimaera.What single-channel analysis tells us of the activation mechanism of ligand-gated channels: the case of the glycine receptor.Differential Contribution of Subunit Interfaces to α9α10 Nicotinic Acetylcholine Receptor Function.Intra-subunit flexibility underlies activation and allosteric modulation of neuronal nicotinic acetylcholine receptors.The structural basis of function in Cys-loop receptors.The structural mechanism of the Cys-loop receptor desensitization.Additional acetylcholine (ACh) binding site at alpha4/alpha4 interface of (alpha4beta2)2alpha4 nicotinic receptor influences agonist sensitivity.Cysteine modification reveals which subunits form the ligand binding site in human heteromeric 5-HT3AB receptors.Understanding the Bases of Function and Modulation of α7 Nicotinic Receptors: Implications for Drug Discovery.Structural mechanisms of activation and desensitization in neurotransmitter-gated ion channels.Orthosteric and allosteric potentiation of heteromeric neuronal nicotinic acetylcholine receptors.Nicotinic acetylcholine receptors at the single-channel level.Probing pore constriction in a ligand-gated ion channel by trapping a metal ion in the pore upon agonist dissociation.Molecular dissection of Cl--selective Cys-loop receptor points to components that are dispensable or essential for channel activity.5-HT3 Receptor Brain-Type B-Subunits are Differentially Expressed in Heterologous Systems.
P2860
Q24618824-AD73F5FE-3814-42BC-BE62-30A220E48F99Q27670592-BA681DD0-9783-44C9-A35E-5538443C951EQ27675268-B34F9649-7139-409F-BB75-A6BC49A97EC7Q28239408-2E2E7C7E-B0EA-4855-94C3-B478D1E57ECFQ28655994-6120A753-2894-494F-8B3D-58941488F48AQ33781359-FBC64CF1-3473-4671-85AE-715AD6F68278Q34088145-28F5443D-ECA0-4B2D-ADB7-D7AFAD59B99EQ34125225-434E603D-6C7F-4621-A042-2FD5AAC7FCD2Q34230674-81B91AC0-7E93-4EFA-8F1E-52ABAC695AD7Q34745010-7F09B1B5-89D1-415E-B08F-F1E17CAB5288Q34787233-599F62CF-5F5E-447B-A9EF-3F87DF09990BQ35662305-943FDC5D-2018-4F8F-AA6C-924021845C06Q35774453-FD3B448E-F7F4-46D7-B6BA-6C2468A7BD63Q35929504-48500D06-86B6-435F-8BFC-C6A1B873578BQ35981924-055D6EE4-A6DA-40AA-BBCA-B0C620C3BAB9Q36323450-31F76A81-6764-49B6-9EF3-BD93EA4CA88DQ36335581-FC04C709-AC9D-4304-8350-37427F2EEB14Q36638888-793DC4B4-2508-43FE-A146-EDB9CAD983F9Q36781949-0E7BD49F-4FF8-490A-AD89-DE8BE3623F60Q37334375-8CB36455-C671-4CD4-BF07-63A498615CE1Q37334917-E3B40600-3B54-48D7-8E8D-103687BFB4ECQ37359381-08D1C12B-3D0D-412D-99EB-80AB00939713Q37405338-40295C5B-9D29-4F7F-AE5B-4EB3E684B8D8Q37409428-0A506019-4294-494B-9AB0-C6A7DDE8E423Q37533114-F6C9FD93-3E21-4439-87B1-D11A05BF5DD6Q37577016-7376B0A7-10B0-4B0A-BF2E-6DE160FDDE88Q37601095-DD90E811-67E2-42A7-9F63-A9E3804C4E80Q37664769-1B53C6A7-9038-40E2-88CB-339A85591619Q37674639-D61D11B3-A66B-495B-AC51-BC96720AE898Q37789790-C2DB9800-1426-4139-B18B-3F0FC36C8396Q38080450-50176F50-4971-4E01-A424-EDED9DF5C0ACQ38264151-8ABCACAA-252E-480B-B13B-AA848EF39FACQ38566791-B26954F5-2D71-4DA9-8E42-DCA3FE020CC9Q38837028-9B226BDB-4B36-43E0-A445-2E1E556D0FDEQ38858502-EB8C0739-646F-4E54-AE7D-C5C342F2ABD8Q39136644-67CE595A-F235-4D1B-9F33-BE21FDA50339Q39162936-21194FD7-8024-45D5-8485-E63580ADE318Q39704220-9F7192A1-7679-4C59-86C6-C32F1895AA3FQ39936711-2FC96FD7-A998-4FD8-8903-0736A6A7B7C0Q40964899-2D25F1FE-AD96-4E94-8F67-4C0CC49932E9
P2860
Number and locations of agonist binding sites required to activate homomeric Cys-loop receptors
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Number and locations of agonis ...... e homomeric Cys-loop receptors
@en
Number and locations of agonis ...... homomeric Cys-loop receptors.
@nl
type
label
Number and locations of agonis ...... e homomeric Cys-loop receptors
@en
Number and locations of agonis ...... homomeric Cys-loop receptors.
@nl
prefLabel
Number and locations of agonis ...... e homomeric Cys-loop receptors
@en
Number and locations of agonis ...... homomeric Cys-loop receptors.
@nl
P2093
P2860
P1476
Number and locations of agonis ...... e homomeric Cys-loop receptors
@en
P2093
Cecilia Bouzat
Diego Rayes
Steven M Sine
P2860
P304
P356
10.1523/JNEUROSCI.0627-09.2009
P407
P577
2009-05-01T00:00:00Z