Nanosecond dynamics of influenza A/M2TM and an amantadine resistant mutant probed by time-dependent red shifts of a native tryptophan
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Reference49 articles.
1. The molecular basis of the specific anti-influenza action of amantadine.
2. Influenza virus M2 protein has ion channel activity
3. The M2 Proton Channels of Influenza A and B Viruses
4. Total Chemical Synthesis of the Integral Membrane Protein Influenza A Virus M2: Role of Its C-Terminal Domain in Tetramer Assembly
5. pH-Dependent Tetramerization and Amantadine Binding of the Transmembrane Helix of M2 from the Influenza A Virus
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1. Dissecting Nanosecond Dynamics in Membrane Proteins with Dipolar Relaxation upon Tryptophan Photoexcitation;The Journal of Physical Chemistry Letters;2018-04-13
2. Role of Cationic Side Chains in the Antimicrobial Activity of C18G;Molecules;2018-02-04
3. Proton Transport Mechanism of M2 Proton Channel Studied by Laser-Induced pH Jump;Journal of the American Chemical Society;2017-05-08
4. Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel;Physical Chemistry Chemical Physics;2016
5. Functional characterization of a melittin analog containing a non-natural tryptophan analog;Biopolymers;2015-07
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