Backbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A Virus-Reference-Cited by-同舟云学术

Backbone Structure of the Amantadine-Blocked Trans-Membrane Domain M2 Proton Channel from Influenza A Virus

Published:2007-06 Issue:12 Volume:92 Page:4335-4343
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Hu Jun,Asbury Tom,Achuthan Srisairam,Li Conggang,Bertram Richard,Quine Jack R.,Fu Riqiang,Cross Timothy A.

Publisher

Elsevier BV

Subject

Biophysics

Reference52 articles.

1. Ionic Channels of Excitable Membranes;Hille,2001

2. Morbidity and Mortality Weekly Report. 2006. High levels of adamantane resistance among Influenza A (H3N2) viruses and interim guidelines for use of antiviral agents. United States, 2005–06 Influenza season. Dispatch 55, January 26.

3. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block;Wang;J. Virol.,1993

4. Direct measurement of the influenza A virus protein ion channel activity in mammalian cells;Wang;Virology,1994

5. Proton conductance of Influenza virus M2 protein in planar bilayers;Vijayvergiya;Biophys. J.,2004

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