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English
Flu channel drug resistance: a tale of two sites.
scientific article published on 23 February 2010
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Europe PubMed Central
PMCID
4875082
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
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19 January 2020
review article
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title
Flu channel drug resistance: a tale of two sites
(English)
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Europe PubMed Central
PMCID
4875082
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
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19 January 2020
author
James J Chou
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2
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Europe PubMed Central
PMCID
4875082
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
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19 January 2020
author name string
Rafal M Pielak
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1
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Europe PubMed Central
PMCID
4875082
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
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19 January 2020
publication date
23 February 2010
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4875082
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retrieved
19 January 2020
published in
Protein & Cell
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4875082
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19 January 2020
volume
1
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Europe PubMed Central
PMCID
4875082
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19 January 2020
issue
3
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Europe PubMed Central
PMCID
4875082
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
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19 January 2020
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246-258
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Europe PubMed Central
PMCID
4875082
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19 January 2020
exact match
https://scigraph.springernature.com/pub.10.1007/s13238-010-0025-y
0 references
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An amantadine-sensitive chimeric BM2 ion channel of influenza B virus has implications for the mechanism of drug inhibition
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Mechanism of drug inhibition and drug resistance of influenza A M2 channel
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Structure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: The Role of Ser31 in Amantadine Binding
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The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding
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Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel
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A secondary gate as a mechanism for inhibition of the M2 proton channel by amantadine.
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Cytoplasmic domain of influenza B virus BM2 protein plays critical roles in production of infectious virus
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Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel
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Crystallographic study of the tetrabutylammonium block to the KcsA K+ channel
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Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus production
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Influenza B virus BM2 protein is a crucial component for incorporation of viral ribonucleoprotein complex into virions during virus assembly
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The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue
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6 September 2017
Structure of the transmembrane region of the M2 protein H+ channel
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Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein
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A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity
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Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block
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Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins
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14 September 2017
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23 June 2018
Energetic analysis of the two controversial drug binding sites of the M2 proton channel in influenza A virus
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1 September 2018
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Adamantane resistance among influenza A viruses isolated early during the 2005-2006 influenza season in the United States
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1 September 2018
ANTIVIRAL ACTIVITY OF 1-ADAMANTANAMINE (AMANTADINE).
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4875082
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1 September 2018
Influenza B virus BM2 protein has ion channel activity that conducts protons across membranes
1 reference
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1 September 2018
Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property
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1 September 2018
Cu(II) inhibition of the proton translocation machinery of the influenza A virus M2 protein
1 reference
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1 September 2018
Experimentally based orientational refinement of membrane protein models: A structure for the Influenza A M2 H+ channel
1 reference
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4875082
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1 September 2018
Influenza virus M2 protein: a molecular modelling study of the ion channel.
1 reference
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4875082
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1 September 2018
Neutron diffraction reveals the site of amantadine blockade in the influenza A M2 ion channel.
1 reference
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PubMed Central
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4875082
retrieved
1 September 2018
Identifiers
DOI
10.1007/S13238-010-0025-Y
1 reference
stated in
Europe PubMed Central
PMCID
4875082
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
retrieved
19 January 2020
PMCID
4875082
1 reference
stated in
Europe PubMed Central
PMCID
4875082
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
retrieved
19 January 2020
PubMed ID
21203971
1 reference
stated in
Europe PubMed Central
PMCID
4875082
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21203971%20AND%20SRC:MED&resulttype=core&format=json
retrieved
19 January 2020
ResearchGate publication ID
49726761
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