The oligomeric state of the active BM2 ion channel protein of influenza B virus (Q40036702)

16 September 2017

title

The oligomeric state of the active BM2 ion channel protein of influenza B virus (English)

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16 September 2017

influenza B virus

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Robert A Lamb

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16 September 2017

Lawrence H Pinto

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16 September 2017

Victoria Balannik

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16 September 2017

language of work or name

English

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publication date

11 December 2007

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Journal of Biological Chemistry

16 September 2017

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inferred from page(s)

published in

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16 September 2017

volume

283

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16 September 2017

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16 September 2017

page(s)

4895-4904

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

16 September 2017

cites work

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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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

Influenza B virus BM2 protein has ion channel activity that conducts protons across membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

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

21 January 2018

1 reference

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

21 January 2018

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

21 January 2018

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The M2 proton channels of influenza A and B viruses

21 January 2018

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Influenza virus M2 protein has ion channel activity

21 January 2018

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Controlling influenza virus replication by inhibiting its proton channel

21 January 2018

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Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel

21 January 2018

1 reference

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Oligomeric organization and strain-specific proteolytic modification of the virion M2 protein of influenza A H1N1 viruses

21 January 2018

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer.

21 January 2018

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

21 January 2018

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Design of the linkers which effectively separate domains of a bifunctional fusion protein.

21 January 2018

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Ion selectivity and activation of the M2 ion channel of influenza virus

21 January 2018

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Determination of the subunit stoichiometry of a voltage-activated potassium channel

21 January 2018

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21 January 2018

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Conformational Rearrangements Associated with the Gating of the G Protein-Coupled Potassium Channel Revealed by FRET Microscopy

21 January 2018

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Fluorescence measurements reveal stoichiometry of K+ channels formed by modulatory and delayed rectifier alpha-subunits

21 January 2018

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Issues in confocal microscopy for quantitative FRET analysis

21 January 2018

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Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser.

21 January 2018

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Quantitative fluorescence resonance energy transfer (FRET) measurement with acceptor photobleaching and spectral unmixing

21 January 2018

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Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching.

21 January 2018

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Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy

21 January 2018

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Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel

21 January 2018

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Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters

21 January 2018

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Topogenic signals in integral membrane proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

A functionally defined model for the M 2 proton channel of influenza A virus suggests a mechanism for its ion selectivity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

Analysis of the pore structure of the influenza A virus M(2) ion channel by the substituted-cysteine accessibility method

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M709433200

21 January 2018

Identifiers

DOI

10.1074/JBC.M709433200

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16 September 2017

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