Gamma-aminobutyric acid increases the water accessibility of M3 membrane-spanning segment residues in gamma-aminobutyric acid type A receptors
about
Structural mechanisms underlying benzodiazepine modulation of the GABA(A) receptorA locally closed conformation of a bacterial pentameric proton-gated ion channelMethionine 286 in transmembrane domain 3 of the GABAA receptor beta subunit controls a binding cavity for propofol and other alkylphenol general anestheticsMutations affecting GABAergic signaling in seizures and epilepsy.Molecular targets and mechanisms for ethanol action in glycine receptorsSpecific binding sites for alcohols and anesthetics on ligand-gated ion channels.Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.Hydrocarbon molar water solubility predicts NMDA vs. GABAA receptor modulation.Structure of the M2 transmembrane segment of GLIC, a prokaryotic Cys loop receptor homologue from Gloeobacter violaceus, probed by substituted cysteine accessibility.Anesthetic sites and allosteric mechanisms of action on Cys-loop ligand-gated ion channels.Tryptophan scanning mutagenesis in TM2 of the GABA(A) receptor alpha subunit: effects on channel gating and regulation by ethanol.Discrete M3-M4 intracellular loop subdomains control specific aspects of γ-aminobutyric acid type A receptor function.Gating-induced conformational rearrangement of the γ-aminobutyric acid type A receptor β-α subunit interface in the membrane-spanning domainThe location of a closed channel gate in the GABAA receptor channel.Identification of amino acid residues lining the pore of a gap junction channelModulating inhibitory ligand-gated ion channels.Tryptophan mutations at azi-etomidate photo-incorporation sites on alpha1 or beta2 subunits enhance GABAA receptor gating and reduce etomidate modulation.A novel, rapid, inhibitory effect of insulin on alpha1beta2gamma2s gamma-aminobutyric acid type A receptors.Probing protein packing surrounding the residues in and flanking the nicotinic acetylcholine receptor M2M3 loop.GABA-induced intersubunit conformational movement in the GABAA receptor alpha 1M1-beta 2M3 transmembrane subunit interface: experimental basis for homology modeling of an intravenous anesthetic binding site.The structural basis of function in Cys-loop receptors.Spontaneous mobility of GABAA receptor M2 extracellular half relative to noncompetitive antagonist action.EPR Studies of Gating Mechanisms in Ion Channels.A mutant residue in the third transmembrane region of the GABA(A) alpha1 subunit causes increased agonistic neurosteroid responses.A proton-mediated conformational shift identifies a mobile pore-lining cysteine residue (Cys-561) in human concentrative nucleoside transporter 3.RNA editing of the GABA(A) receptor alpha3 subunit alters the functional properties of recombinant receptors.Functional interactions of alcohol-sensitive sites in the N-methyl-D-aspartate receptor M3 and M4 domainsThe alpha 1 and alpha 6 subunit subtypes of the mammalian GABA(A) receptor confer distinct channel gating kinetics.Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC).Conformational transitions underlying pore opening and desensitization in membrane-embedded Gloeobacter violaceus ligand-gated ion channel (GLIC)Loose protein packing around the extracellular half of the GABA(A) receptor beta1 subunit M2 channel-lining segment.Channel gating of the glycine receptor changes accessibility to residues implicated in receptor potentiation by alcohols and anesthetics.Structural and electrostatic properties of the 5-HT3 receptor pore revealed by substituted cysteine accessibility mutagenesis.Effects of ethanol on adenosine 5'-triphosphate-gated purinergic and 5-hydroxytryptamine receptors.Identification of a novel residue within the second transmembrane domain that confers use-facilitated block by picrotoxin in glycine alpha 1 receptors.Application of SCAM (substituted cysteine accessibility method) to gap junction intercellular channels.GABA(A) receptor M2-M3 loop secondary structure and changes in accessibility during channel gating.Evidence that the TM1-TM2 loop contributes to the rho1 GABA receptor pore.Inhibitory effects of insulin on GABAA currents modulated by the GABAA alpha subunit.Functional and structural analysis of the GABAA receptor alpha 1 subunit during channel gating and alcohol modulation.
P2860
Q24645323-3C2259CE-405F-44C9-9BFB-71CC8CEAB3C1Q27679065-54E384A5-3B4F-49A3-B10E-51A1371C1AA4Q28366642-C33DE887-025A-47CF-AD2E-383FBE8366F4Q33912426-770ADB78-C65E-4D20-BA28-781299EFFF66Q33936421-65F53030-F0FE-4F7D-919D-0129B30E718DQ34509821-7D4AE28D-BD3C-401F-9D25-987A753EC54FQ34572493-1F14FCE2-0EB3-4278-9212-F6930F93AFBCQ34587545-9C0B1C7E-FB19-467F-B6E6-4B861AB39559Q34800089-9C175F93-DA0B-4236-B33B-92255673179FQ35024917-8DCE8C90-A1CA-4751-8434-D31D4F3B0EAEQ35042675-43593A12-056E-471A-A2E6-4648B6D730E6Q35515794-B9FD2B20-CC26-4306-B88C-D54485972847Q36201884-A5E7E930-3DB6-4394-BE24-967CE375BB9DQ36299672-1249A63E-15E2-4637-A247-B14283878A21Q36323688-12BF67E4-6BDA-4A8C-96E8-CF2CDE362BDEQ36516836-BE1E4238-4AB3-4EC6-BAF7-35AA8BB53C32Q37000978-B71CFB5C-4A80-4654-B105-27C845B4EF61Q37003433-65B19892-98B4-47A1-A0F8-50C9A6C0D0A9Q37124675-1BED268F-63BA-495F-97CC-1EF364CBC35CQ37181047-627E9D10-2181-4003-A03A-A96973FBEF0CQ37789790-B4038752-6DF4-46F9-8FD3-141D9F3A0BA9Q38308422-80B044D6-6287-471D-84A9-D63F4AD9E4D2Q38464421-627CC8C7-3055-4E14-9129-4E282B76BB37Q38498708-96BBB3B7-B618-4DDC-BA01-D21F63F35193Q38923874-1663BF86-EE94-40ED-9E24-D3BC25B56AA4Q39860889-93EAA2FD-4835-4EFB-A0FA-E24CA136231BQ40022351-39C3DBC0-D1FD-4274-9278-BA71C230DDC1Q40484829-5E5283B8-CEC8-4BB6-B51E-1806BD13C05AQ41903108-683A2A56-AB9F-468C-8524-0196AB6EACC0Q42404119-4DB456EB-2A0C-4ECF-97E2-443B4AE508F9Q42616990-606BC498-D949-4DC8-B8BF-3A00E146AF12Q42628316-10528D02-37B0-44E5-AE0E-255846C7A993Q42659707-34CE04FC-84E2-4B05-B190-948FF2EBC6E8Q42911114-A3D27C1D-B589-4326-85F5-5C58C343455EQ43823925-C2785772-3C04-4442-B9AB-364A5EA0B04DQ44027821-1F9B06BD-93D7-45CC-8207-22CD8D97E2C7Q44133863-E3FFFD54-8EB9-40B6-855C-A374C133F898Q44790627-AA2E7019-BF48-442C-AF7A-C573A6D9EA2AQ45134796-83CD7B95-87E9-4803-905A-C71B6A019760Q45136842-F546FAF5-74E7-4AA9-A322-160EA16FF7E1
P2860
Gamma-aminobutyric acid increases the water accessibility of M3 membrane-spanning segment residues in gamma-aminobutyric acid type A receptors
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@ast
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@en
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@nl
type
label
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@ast
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@en
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@nl
prefLabel
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@ast
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@en
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@nl
P2860
P1433
P1476
Gamma-aminobutyric acid increa ...... obutyric acid type A receptors
@en
P2093
D B Williams
P2860
P304
P356
10.1016/S0006-3495(99)77091-8
P407
P577
1999-11-01T00:00:00Z