An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors.
about
The Intracellular Loop of the Glycine Receptor: It's not all about the SizeNMR structure of the transmembrane domain of the n-acetylcholine receptor β2 subunitOpen-channel structures of the human glycine receptor α1 full-length transmembrane domain.Characterization of SLCO5A1/OATP5A1, a solute carrier transport protein with non-classical functionThe Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-SheetsGenome-wide Membrane Protein Structure Prediction.Glycine receptor mutants of the mouse: what are possible routes of inhibitory compensation?Efficient expression of acetylcholine-binding protein from Aplysia californica in Bac-to-Bac systemStructure-function study of the fourth transmembrane segment of the GABAρ1 receptor.Atomistic insights into human Cys-loop receptors by solution NMR.Linking of Glycine Receptor Transmembrane Segments Three and Four Allows Assignment of Intrasubunit-Facing Residues.Disturbed neuronal ER-Golgi sorting of unassembled glycine receptors suggests altered subcellular processing is a cause of human hyperekplexia.Control of ethanol sensitivity of the glycine receptor α3 subunit by transmembrane 2, the intracellular splice cassette and C-terminal domains.Inhibitory glycine receptors: an update.Thermal unfolding of a mammalian pentameric ligand-gated ion channel proceeds at consecutive, distinct stepsNovel missense mutations in the glycine receptor β subunit gene (GLRB) in startle diseasePentameric quaternary structure of the intracellular domain of serotonin type 3A receptors.Role of the Fourth Transmembrane α Helix in the Allosteric Modulation of Pentameric Ligand-Gated Ion Channels.Structural sensitivity of a prokaryotic pentameric ligand-gated ion channel to its membrane environment.New hyperekplexia mutations provide insight into glycine receptor assembly, trafficking, and activation mechanisms.Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activationThe structural basis of function in Cys-loop receptors.Assembly of nicotinic and other Cys-loop receptors.Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Homodimeric anoctamin-1, but not homodimeric anoctamin-6, is activated by calcium increases mediated by the P2Y1 and P2X7 receptors.The M4 Transmembrane α-Helix Contributes Differently to Both the Maturation and Function of Two Prokaryotic Pentameric Ligand-gated Ion Channels.The importance of TM3-4 loop subdomains for functional reconstitution of glycine receptors by independent domains.Intramembrane aromatic interactions influence the lipid sensitivities of pentameric ligand-gated ion channels.Pentameric ligand-gated ion channels exhibit distinct transmembrane domain archetypes for folding/expression and function.A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and crystallization.Single expressed glycine receptor domains reconstitute functional ion channels without subunit-specific desensitization behavior.A distinct mechanism for activating uncoupled nicotinic acetylcholine receptors.The role of charged residues in independent glycine receptor folding domains for intermolecular interactions and ion channel function.Structure/Function Studies of the α4 Subunit Reveal Evolutionary Loss of a GlyR Subtype Involved in Startle and Escape Responses.An allosteric link connecting the lipid-protein interface to the gating of the nicotinic acetylcholine receptor.Impaired Glycine Receptor Trafficking in Neurological DiseasesThe roles of aromatic residues in the glycine receptor transmembrane domain
P2860
Q26743781-7E1AD9E2-49AF-4015-A612-62C29B00BFCAQ27661310-CA7165D9-8774-44F5-A0B0-32FC2CCCF5D8Q27679842-FA3508C0-3E1A-4D9D-BAD1-3FF63124D04EQ28537862-BD148376-F522-46BA-8C66-77A9D6A764B9Q30155071-FD61A28B-4A7A-4D26-A2C3-630600F004B0Q30357668-D6F5FB33-AE5F-4182-B631-85B74F297CD8Q30461478-E8B865A4-88CF-484D-A874-52B4DD3309B8Q34022402-0EB977BE-55F6-48ED-980A-53711825EC9FQ34199810-2A8C9FFE-A14B-4CA6-AF43-8109E980755BQ34257782-2C2DDF5C-A84C-4BA3-93FD-7DD136E9D9B7Q34572493-34D4AE7E-3422-4C1A-AC5A-EBAFE87034D0Q34869853-E2320E4C-D3CF-4263-B373-1F15F0DDCB64Q35197866-EB4017CA-09CA-4CCC-AD94-FDAAC2E26DDAQ36418772-BAE0A3F0-D5B6-4260-91C1-4243AF58BC99Q36636020-B2116924-016E-449A-8CAF-3947BEBBBB91Q36636926-B54CDC73-615E-44A1-AD5E-76D5886134E6Q36764827-801AF966-9A2A-40D3-A03D-A3CA18ED7BDDQ36777831-BB55B1FC-E626-48D3-AD77-E78CE3612356Q36779466-F0320781-F0AD-4827-B8A7-F3391988EE2CQ37333728-44FF2CDF-0D03-4DD1-91E0-50BFB247FAB0Q37334375-B195273E-41E5-43F9-A5E2-8E23F2AB3BC0Q37789790-DD2C7F5C-0F29-4815-98AF-D33E078EDF7BQ37826784-A4701016-904F-4A9E-AEA7-642A29AE0966Q38273638-38465D29-7727-4D3E-8E62-811EEADF19A9Q38919495-283BA6A1-8D54-4B2D-8F30-795ABFDEC2F9Q40595431-6C412FDC-F737-48F6-ADDC-4C8D40CA4581Q41308485-F81733B7-A541-49FF-BFBA-C233B9A310A6Q41675967-88623347-3794-4D1D-A944-FDDB42EE707CQ41921413-6670B075-8478-4EEE-A1D1-41C432C01CA1Q41949216-2AF416FE-A351-45E3-9AA1-C857C164521DQ42117968-BB5B35F4-41A6-40F6-9EC2-A2F463AF19DAQ43750212-C1EED4BB-A860-4B29-85D8-2314BEA67915Q48250089-E6AB53F7-D0E4-47AB-BD2C-5E8C1F1ECEB0Q49489241-E307DB71-0392-4C99-90D4-28DC2F9AC9AFQ53840266-792B52D6-BB18-4B97-9CD6-D5AAC40956F3Q58728657-D66B14CA-76F0-4DFD-BB45-B2EF402C7A5FQ58761747-53CB6A3E-A3F0-4661-A1DA-B6C68418ECD9
P2860
An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors.
@en
type
label
An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors.
@en
prefLabel
An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors.
@en
P2093
P2860
P356
P1476
An intramembrane aromatic network determines pentameric assembly of Cys-loop receptors.
@en
P2093
Bodo Laube
Günther Schmalzing
Heinrich Betz
Michael Kilb
Niklas Lang
Silvia Detro-Dassen
Svenja Haeger
Victor Tsetlin
P2860
P2888
P356
10.1038/NSMB.1721
P577
2009-12-20T00:00:00Z