Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.
about
Viral Membrane Channels: Role and Function in the Virus Life CycleStructural basis for the function and inhibition of an influenza virus proton channelStructure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: The Role of Ser31 in Amantadine BindingStructure of the amantadine binding site of influenza M2 proton channels in lipid bilayersStructure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virusInsight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid BilayerHigh-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transductionStructure and inhibition of the SARS coronavirus envelope protein ion channelThe Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic ResonanceDrug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.Membrane protein structure and dynamics from NMR spectroscopy.G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.Structural basis for proton conduction and inhibition by the influenza M2 protein.Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR.Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.Discovery of spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A virus.Conformational heterogeneity of the M2 proton channel and a structural model for channel activationRetinal conformation and dynamics in activation of rhodopsin illuminated by solid-state H NMR spectroscopy.A theory for the proton transport of the influenza virus M2 protein: extensive test against conductance dataProton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH JumpDiffusion-Influenced Transport of Ions across a Transmembrane Channel with an Internal Binding Site.Aminoadamantanes with persistent in vitro efficacy against H1N1 (2009) influenza AWhere does amantadine bind to the influenza virus M2 proton channel?Proton and cation transport activity of the M2 proton channel from influenza A virus.Proton association constants of His 37 in the Influenza-A M218-60 dimer-of-dimers.Photoinduced electron transfer and fluorophore motion as a probe of the conformational dynamics of membrane proteins: application to the influenza a M2 proton channelViral miniproteinsInfluence of solubilizing environments on membrane protein structuresA pH-dependent conformational ensemble mediates proton transport through the influenza A/M2 proteinMechanism of influenza A M2 transmembrane domain assembly in lipid membranesSolid-supported membrane technology for the investigation of the influenza A virus M2 channel activityDynamic Short Hydrogen Bonds in Histidine Tetrad of Full-Length M2 Proton Channel Reveal Tetrameric Structural Heterogeneity and Functional MechanismAmantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel.Transmembrane helix uniformity examined by spectral mapping of torsion angles.Structural Influences: Cholesterol, Drug, and Proton Binding to Full-Length Influenza A M2 Protein.Transmembrane communication: general principles and lessons from the structure and function of the M2 proton channel, K⁺ channels, and integrin receptors.An amantadine-sensitive chimeric BM2 ion channel of influenza B virus has implications for the mechanism of drug inhibition.Acid activation mechanism of the influenza A M2 proton channel.Structure and function of the influenza A M2 proton channelFlu channel drug resistance: a tale of two sites.
P2860
Q27000898-782EA5BC-2629-423D-800D-11CEE1831316Q27649742-5F578A22-1C56-4E2C-AE00-D63F604D3295Q27653082-2E388DA2-8FC8-4BC6-92C4-57F3D5D0114AQ27659500-A381C4BE-D221-4880-8A63-F6592E41DACDQ27663887-98AD59C0-CD13-4F8C-8B91-2D0940F0F4B4Q27665298-A47AC95B-6283-4BCF-9639-543763705520Q28269976-1614FE18-9C06-402E-BADE-385D6EB5F949Q28475712-6F0F420D-8DA5-468D-BF34-3740FB270FB2Q28818506-6A05F81F-CF82-4309-A1BF-C0A255B81FE4Q30391763-B25D7483-CCF0-4839-A0A7-FC41D16A74F1Q30410205-E6D093AE-DAC1-47BA-ABD3-76C2EA96B073Q30427675-120FF04C-22AF-4FDB-9BF9-BDCB184B0F0AQ30570161-B99F3414-4360-4B46-B065-402429737AC4Q30646130-7EBE1F96-4895-46FB-B3AA-3E2271E19FCDQ30666144-9A0025D7-7D46-464F-8084-D79F7ABEEBBAQ33452730-5A504EFC-6EFF-4EF5-9814-07EBCE7CB976Q33487093-DCB6DA6F-8963-41BB-ABFC-7D6FA94890B4Q33807818-6E8E5C1C-3FBB-4F83-AFDD-72D5DB844839Q33820363-BCAEA1C8-4D8D-49F4-9991-21E26BE65CB4Q33902460-60694B77-5D27-4B63-9786-9FE672E8F29DQ33961874-086A00C0-0105-4F60-A906-51F0AEA6A83AQ34023430-38E8A78B-CF07-4D5E-BF7A-286B52128B59Q34057747-7FF9491B-CB8D-4D3D-99E7-E48BCA129F37Q34100507-28DF4D15-9638-4607-88A4-D1B97F648D2CQ34264872-1E8521B0-B02D-4804-8E1E-5F05AC1D2206Q34744629-4926DB49-B258-4F2D-93A1-F1D43A907212Q35151120-5DE476C0-5593-4E0C-A33E-DD7A6BF47523Q35180927-2EC7AB15-AEA5-4490-890F-13C82BD29056Q35187961-86D4BF97-A210-4D94-9B1D-86863816A574Q35865367-F01C1EEF-82AC-44E8-B4D8-7553AEB19AC1Q36193000-92F66B09-B8A2-41E7-806C-D2C9E58CE444Q36348835-1A82EE59-4CE4-4B22-9F26-D902D4C325C6Q36446338-E0CA6ACD-7FC6-405E-A9D0-699D2DBB19B5Q36731230-3D51584A-B5A9-4FF1-83A9-FCA1064FDE75Q36753703-4136BC03-6E1C-44B2-A8B0-1924A7F665AAQ37156475-6FCFABFA-9405-4E29-A10B-62396A5ACDA5Q37413585-574BD07E-761D-4429-A5C1-DE54B41755A4Q37417885-AF53FE28-56C6-456E-9EC3-FC93310F1EB7Q37550490-0B3AD054-8CBF-4BE9-8D99-60B4A067FB57Q37825830-EC789AF7-FFB4-4734-A4DB-AD93B232FCC0
P2860
Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Solid-state NMR characterizati ...... influenza A M2 proton channel.
@ast
Solid-state NMR characterizati ...... influenza A M2 proton channel.
@en
type
label
Solid-state NMR characterizati ...... influenza A M2 proton channel.
@ast
Solid-state NMR characterizati ...... influenza A M2 proton channel.
@en
prefLabel
Solid-state NMR characterizati ...... influenza A M2 proton channel.
@ast
Solid-state NMR characterizati ...... influenza A M2 proton channel.
@en
P2093
P2860
P1476
Solid-state NMR characterizati ...... influenza A M2 proton channel.
@en
P2093
Conggang Li
Fei Philip Gao
Huajun Qin
Timothy A Cross
P2860
P304
P356
10.1016/J.BBAMEM.2007.08.025
P407
P577
2007-09-08T00:00:00Z