Amphipathic alpha-helices and putative cholesterol binding domains of the influenza virus matrix M1 protein are crucial for virion structure organisation-Reference-Cited by-同舟云学术

Amphipathic alpha-helices and putative cholesterol binding domains of the influenza virus matrix M1 protein are crucial for virion structure organisation

Published:2015-12 Issue: Volume:210 Page:114-118
ISSN:0168-1702
Container-title:Virus Research
language:en
Short-container-title:Virus Research

Author:

Tsfasman Tatyana,Kost Vladimir,Markushin Stanislav,Lotte Vera,Koptiaeva Irina,Bogacheva Elena,Baratova Ludmila,Radyukhin Victor

Funder

Russian Foundation for Basic Research

Ministry of Education and Science of Russian Federation

Publisher

Elsevier BV

Subject

Cancer Research,Infectious Diseases,Virology

Reference17 articles.

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3. Influenza A viruses with mutations in the M1 helix six domain display a wide variety of morphological phenotypes;Burleigh;J. Virol.,2005

4. Structural organization of a filamentous influenza A virus;Calder;Proc. Natl. Acad. Sci.,2010

5. Comparative analysis of seven nuclear export signals (NESs) reveals the crucial role of nuclear export mediated by the third NES consensus sequence of nucleoprotein (NP) in influenza A virus replication;Chutiwitoonchai;PLoS One,2014

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