ArticleBiochimica et biophysica acta2007
Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.
Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed.
- Molecular biophysics and inhibition mechanism of influenza virus A M2 viroporin by adamantane-based drugs - Challenges in designing antiviral agents.Journal of structural biology: X · 2025Article
- Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025Article
- Multiscale Simulation of an Influenza A M2 Channel Mutant Reveals Key Features of Its Markedly Different Proton Transport Behavior.Journal of the American Chemical Society · 2022Article
- Influenza A M2 Inhibitor Binding Understood through Mechanisms of Excess Proton Stabilization and Channel Dynamics.Journal of the American Chemical Society · 2020Article
- Cholesterol Alters the Orientation and Activity of the Influenza Virus M2 Amphipathic Helix in the Membrane.The journal of physical chemistry. B · 2020Article
- X-ray Crystal Structure of the Influenza A M2 Proton Channel S31N Mutant in Two Conformational States: An Open and Shut Case.Journal of the American Chemical Society · 2019Article
- Proton-Induced Conformational and Hydration Dynamics in the Influenza A M2 Channel.Journal of the American Chemical Society · 2019Article
- Viroporins in the Influenza Virus.Cells · 2019Review
- Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR.Journal of structural biology · 2019Article
- Structural Variability in the RLR-MAVS Pathway and Sensitive Detection of Viral RNAs.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2019Review
- Inhibitors of the M2 Proton Channel Engage and Disrupt Transmembrane Networks of Hydrogen-Bonded Waters.Journal of the American Chemical Society · 2018Article
- Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR.Journal of the American Chemical Society · 2018Article
- XFEL structures of the influenza M2 proton channel: Room temperature water networks and insights into proton conduction.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Influenza A Virus M2 Protein: Roles from Ingress to Egress.International journal of molecular sciences · 2017Review
- Structural Basis for Asymmetric Conductance of the Influenza M2 Proton Channel Investigated by Solid-State NMR Spectroscopy.Journal of molecular biology · 2017Article
- Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH Jump.Journal of the American Chemical Society · 2017Article
- Activation pH and Gating Dynamics of Influenza A M2 Proton Channel Revealed by Single-Molecule Spectroscopy.Angewandte Chemie (International ed. in English) · 2017Article
- Binding and Proton Blockage by Amantadine Variants of the Influenza M2Journal of medicinal chemistry · 2017Article
- Acid activation mechanism of the influenza A M2 proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State Nuclear Magnetic Resonance.Biochemistry · 2016Article
10 more citing papers are in PubMed but not listed here.
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4 authors.
Funding
Abstract
Membrane protein function within the membrane interstices is achieved by mechanisms that are not typically available to water-soluble proteins. The whole balance of molecular interactions that stabilize three-dimensional structure in the membrane environment is different from that in an aqueous environment. As a result interhelical interactions are often dominated by non-specific van der Waals interactions permitting dynamics and conformational heterogeneity in these interfaces. Here, solid-state NMR data of the transmembrane domain of the M2 protein from influenza A virus are used to exemplify such conformational plasticity in a tetrameric helical bundle. Such data lead to very high resolution structural restraints that can identify both subtle and substantial structural differences associated with various states of the protein. Spectra from samples using two different preparation protocols, samples prepared in the presence and absence of amantadine, and spectra as a function of pH are used to illustrate conformational plasticity.
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