The polybasic region is not essential for membrane binding of the matrix protein M1 of influenza virus. (Q45388763)

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17 January 2020

title

The polybasic region is not essential for membrane binding of the matrix protein M1 of influenza virus (English)

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17 January 2020

1

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17 January 2020

author name string

Andreas Herrmann

series ordinal

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19004463%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

Michael Veit

series ordinal

3

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17 January 2020

language of work or name

English

0 references

publication date

12 November 2008

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17 January 2020

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19004463%20AND%20SRC:MED&resulttype=core&format=json

17 January 2020

volume

383

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17 January 2020

issue

1

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17 January 2020

page(s)

150-155

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Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)

17 January 2020

cites work

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Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer

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CRM1 is responsible for intracellular transport mediated by the nuclear export signal

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The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1

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Influenza A virus M1 protein structure probed by in situ limited proteolysis with bromelain.

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Membrane association of influenza virus matrix protein does not require specific hydrophobic domains or the viral glycoproteins

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Introduction of a temperature-sensitive phenotype into influenza A/WSN/33 virus by altering the basic amino acid domain of influenza virus matrix protein

7 January 2021

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Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1

7 January 2021

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