pH-Dependent Tetramerization and Amantadine Binding of the Transmembrane Helix of M2 from the Influenza A Virus
Author:
Affiliation:
1. Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine of the University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi001799u
Reference42 articles.
Cited by 152 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Accurate calculation of affinity changes to the close state of influenza A M2 transmembrane domain in response to subtle structural changes of adamantyl amines using free energy perturbation methods in different lipid bilayers;Biochimica et Biophysica Acta (BBA) - Biomembranes;2024-02
2. 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
3. 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
4. Channel activity of SARS-CoV-2 viroporin ORF3a inhibited by adamantanes and phenolic plant metabolites;Scientific Reports;2023-04-01
5. SARS-CoV-2 Envelope Protein Forms Clustered Pentamers in Lipid Bilayers;Biochemistry;2022-10-11
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