Molecular dynamics calculations suggest a conduction mechanism for the M2 proton channel from influenza A virus
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference39 articles.
1. pH-Dependent Tetramerization and Amantadine Binding of the Transmembrane Helix of M2 from the Influenza A Virus
2. The Closed State of a H+ Channel Helical Bundle Combining Precise Orientational and Distance Restraints from Solid State NMR
3. Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity
4. Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel
5. Solid-State 19F NMR Spectroscopy Reveals That Trp41 Participates in the Gating Mechanism of the M2 Proton Channel of Influenza A Virus
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3. Corrigendum: A Study of the Activity of Adamantyl Amines against Mutant Influenza A M2 Channels Identified a Polycyclic Cage Amine Triple Blocker, Explored by Molecular Dynamics Simulations and Solid‐State NMR;ChemMedChem;2023-09-04
4. A Study of the Activity of Adamantyl Amines against Mutant Influenza A M2 Channels Identified a Polycyclic Cage Amine Triple Blocker, Explored by Molecular Dynamics Simulations and Solid‐State NMR**;ChemMedChem;2023-07-25
5. Transient water wires mediate selective proton transport in designed channel proteins;Nature Chemistry;2023-06-12
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