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A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein

author

Jürgen A. Richt

published in: Virus Genes

date of publication: 2014-04-18

main subject: influenza A virus

Cites articles 28

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A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication

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2012-01-19

Human-like PB2 627K influenza virus polymerase activity is regulated by importin-α1 and -α7.

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Influenza virus assembly and budding

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Differential use of importin-α isoforms governs cell tropism and host adaptation of influenza virus

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Structural organization of a filamentous influenza A virus
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The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles

Dan Wang, Jing Jin
2010-11-16

Crucial role of the influenza virus NS2 (NEP) C-terminal domain in M1 binding and nuclear export of vRNP

Naoki Takizawa, Ken Watanabe
2008-08-13

The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding

Robert A. Lamb
2007-08-01

Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions

Paul Digard
2007-05-30

A mutation on influenza C virus M1 protein affects virion morphology by altering the membrane affinity of the protein
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Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly
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Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes

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The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation

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Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape

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Article - wd:Q33954072

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