Influenza B virus BM2 protein is an oligomeric integral membrane protein expressed at the cell surface. (Q40666124)

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1 November 2019

title

Influenza B virus BM2 protein is an oligomeric integral membrane protein expressed at the cell surface (English)

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1 November 2019

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Influenza B virus

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2

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1 November 2019

4

Lawrence H Pinto

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1 November 2019

author name string

Reay G Paterson

series ordinal

1

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1 November 2019

Yuki Ohigashi

series ordinal

3

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1 November 2019

Robert A Lamb

series ordinal

5

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1 November 2019

language of work or name

English

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publication date

1 February 2003

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1 November 2019

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22 September 2017

306

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1 November 2019

issue

1

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1 November 2019

page(s)

7-17

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Sequence of RNA segment 7 of the influenza B virus genome: Partial amino acid homology between the membrane proteins (M1) of Influenza A and B viruses and conservation of a second open reading frame

1 November 2019

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Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells.

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The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers

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Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds

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Eukaryotic coupled translation of tandem cistrons: identification of the influenza B virus BM2 polypeptide.

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Identification of a second protein (M2) encoded by RNA segment 7 of influenza virus

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Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: colinear and interrupted mRNAs code for overlapping proteins

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Do Vpu and Vpr of human immunodeficiency virus type 1 and NB of influenza B virus have ion channel activities in the viral life cycles?

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Influenza virus M2 protein is an integral membrane protein expressed on the infected-cell surface

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Definitive assignment of proton selectivity and attoampere unitary current to the M2 ion channel protein of influenza A virus

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Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains

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Permeation and activation of the M2 ion channel of influenza A virus.

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Mechanism for proton conduction of the M(2) ion channel of influenza A virus

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Efficient selection for high-expression transfectants with a novel eukaryotic vector

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The BM2 protein of influenza B virus is synthesized in the late phase of infection and incorporated into virions as a subviral component

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Transposition of domains between the M2 and HN viral membrane proteins results in polypeptides which can adopt more than one membrane orientation

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Topology of eukaryotic type II membrane proteins: importance of N-terminal positively charged residues flanking the hydrophobic domain

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Ability of the hydrophobic fusion-related external domain of a paramyxovirus F protein to act as a membrane anchor

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7 January 2021

Influenza virus M2 protein has ion channel activity

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7 January 2021

Studies with cross-linking reagents on the oligomeric form of the paramyxovirus fusion protein

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The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatus

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Ion channels formed by NB, an influenza B virus protein

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7 January 2021

The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue

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Activation of the M2 ion channel of influenza virus: a role for the transmembrane domain histidine residue

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Determination of the orientation of an integral membrane protein and sites of glycosylation by oligonucleotide-directed mutagenesis: influenza B virus NB glycoprotein lacks a cleavable signal sequence and has an extracellular NH2-terminal region

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Cell surface expression and orientation in membranes of the 44-amino-acid SH protein of simian virus 5.

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Effect of cytoplasmic tail truncations on the activity of the M(2) ion channel of influenza A virus.

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12620792%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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