Real-time tracking of drug binding to influenza A M2 reveals a high energy barrier
Author:
Funder
Deutsche Forschungsgemeinschaft
Max-Planck-Gesellschaft
Publisher
Elsevier BV
Subject
Structural Biology
Reference55 articles.
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2. Magic angle spinning NMR investigation of influenza A M2(18–60): support for an allosteric mechanism of inhibition;Andreas;J. Am. Chem. Soc.,2010
3. Dynamic nuclear polarization study of inhibitor binding to the M2(18–60) proton transporter from influenza A;Andreas;Biochemistry,2013
4. Structure and mechanism of the influenza A M218–60 dimer of dimers;Andreas;J. Am. Chem. Soc.,2015
5. Design and pharmacological characterization of inhibitors of amantadine-resistant mutants of the M2 ion channel of influenza A virus;Balannik;Biochemistry,2009
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1. 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
2. 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
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