Identification of the pore-lining residues of the BM2 ion channel protein of influenza B virus.
about
Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channelSolution structure and functional analysis of the influenza B proton channelStructure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virusVoltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) familySolid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton ChannelDrug sensitivity, drug-resistant mutations, and structures of three conductance domains of viral porins.A photon-free approach to transmembrane protein structure determination.Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes.Flu BM2 structure and function.The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particlesMolecular dynamics simulations of homo-oligomeric bundles embedded within a lipid bilayerIdentification of the functional core of the influenza A virus A/M2 proton-selective ion channelAn amantadine-sensitive chimeric BM2 ion channel of influenza B virus has implications for the mechanism of drug inhibition.Exploring the size limit of templates for inhibitors of the M2 ion channel of influenza A virus.Influenza A Virus Nucleoprotein: A Highly Conserved Multi-Functional Viral Protein as a Hot Antiviral Drug Target.A Review of Functional Motifs Utilized by Viruses.Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR.Slow but Steady Wins the Race: Dissimilarities among New Dual Inhibitors of the Wild-Type and the V27A Mutant M2 Channels of Influenza A Virus.3-Azatetracyclo[5.2.1.1(5,8).0(1,5)]undecane derivatives: from wild-type inhibitors of the M2 ion channel of influenza A virus to derivatives with potent activity against the V27A mutant.Easily accessible polycyclic amines that inhibit the wild-type and amantadine-resistant mutants of the M2 channel of influenza A virus.Synthesis of benzopolycyclic cage amines: NMDA receptor antagonist, trypanocidal and antiviral activities.Functional studies reveal the similarities and differences between AM2 and BM2 proton channels from influenza viruses.Engineering a Chemical Switch into the Light-driven Proton Pump Proteorhodopsin by Cysteine Mutagenesis and Thiol Modification.Chemical synthesis of membrane proteins: a model study on the influenza virus B proton channel.
P2860
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P2860
Identification of the pore-lining residues of the BM2 ion channel protein of influenza B virus.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Identification of the pore-lin ...... protein of influenza B virus.
@en
type
label
Identification of the pore-lin ...... protein of influenza B virus.
@en
prefLabel
Identification of the pore-lin ...... protein of influenza B virus.
@en
P2093
P2860
P356
P1476
Identification of the pore-lin ...... protein of influenza B virus.
@en
P2093
Albert Taylor
Brett Glawe
Chunlong Ma
Cinque S Soto
Lawrence H Pinto
Maria K Udo
Robert A Lamb
Vasilios Bournas
William F Degrado
Yuki Ohigashi
P2860
P304
15921-15931
P356
10.1074/JBC.M710302200
P407
P577
2008-04-11T00:00:00Z