Differences in conductance of M2 proton channels of two influenza viruses at low and high pH (Q78793311)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12527729%20AND%20SRC:MED&resulttype=core&format=json

16 December 2019

title

Differences in conductance of M2 proton channels of two influenza viruses at low and high pH (English)

1 reference

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16 December 2019

4

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16 December 2019

author name string

I V Chizhmakov

1

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16 December 2019

D C Ogden

2

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16 December 2019

F M Geraghty

3

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16 December 2019

A Skinner

5

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16 December 2019

T Betakova

6

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16 December 2019

A J Hay

7

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16 December 2019

publication date

1 January 2003

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16 December 2019

published in

Journal of Physiology

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16 December 2019

volume

546

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16 December 2019

issue

Pt 2

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16 December 2019

page(s)

427-438

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The voltage-activated hydrogen ion conductance in rat alveolar epithelial cells is determined by the pH gradient.

16 December 2019

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Cu(II) inhibition of the proton translocation machinery of the influenza A virus M2 protein

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Influence of amantadine resistance mutations on the pH regulatory function of the M2 protein of influenza A viruses

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

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Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation

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Conformational mobility of His-64 in the Thr-200----Ser mutant of human carbonic anhydrase II

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A receptor for protons in the nerve cell membrane

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Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza a virus

21 January 2018

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Noncontact dipole effects on channel permeation. III. Anomalous proton conductance effects in gramicidin

21 January 2018

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A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity

21 January 2018

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

21 January 2018

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pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus

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

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Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesicles

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

21 January 2018

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

21 January 2018

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Structure of the transmembrane region of the M2 protein H+ channel

21 January 2018

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The molecular basis of the specific anti-influenza action of amantadine

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/12527729

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Specific structural alteration of the influenza haemagglutinin by amantadine

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12527729

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12527729