The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particles
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Viral Membrane Channels: Role and Function in the Virus Life CycleIdentification of Influenza A/PR/8/34 Donor Viruses Imparting High Hemagglutinin Yields to Candidate Vaccine Viruses in EggsChemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domainViral miniproteinsInvestigation of a recent rise of dual amantadine-resistance mutations in the influenza A M2 sequence.Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and MorphologySelective Degradation of Host RNA Polymerase II Transcripts by Influenza A Virus PA-X Host Shutoff Protein.Cholesterol-Dependent Conformational Exchange of the C-Terminal Domain of the Influenza A M2 Protein.Structural Influences: Cholesterol, Drug, and Proton Binding to Full-Length Influenza A M2 Protein.Protein-lipid interactions critical to replication of the influenza A virus.Acid activation mechanism of the influenza A M2 proton channel.Host Cell Copper Transporters CTR1 and ATP7A are important for Influenza A virus replication.XFEL structures of the influenza M2 proton channel: Room temperature water networks and insights into proton conduction.Lateral Organization of Influenza Virus Proteins in the Budozone Region of the Plasma Membrane.From Variation of Influenza Viral Proteins to Vaccine Development.Abnormal Morphological Vesicles in Influenza A Virus Exposed to Acid pH.The Molecular Switch of Telomere Phages: High Binding Specificity of the PY54 Cro Lytic Repressor to a Single Operator Site.C-terminal juxtamembrane region of full-length M2 protein forms a membrane surface associated amphipathic helix.Acylation and cholesterol binding are not required for targeting of influenza A virus M2 protein to the hemagglutinin-defined budozone.Influenza A Virus M2 Protein: Roles from Ingress to Egress.Mutations in the Influenza A virus M1 protein enhance virus budding to complement lethal mutations in the M2 cytoplasmic tail.RNA structure interactions and ribonucleoprotein processes of the influenza A virus.A Budding-Defective M2 Mutant Exhibits Reduced Membrane Interaction, Insensitivity to Cholesterol, and Perturbed Interdomain Coupling.Structural analysis of influenza vaccine virus-like particles reveals a multicomponent organization.A Defect in Influenza A Virus Particle Assembly Specific to Primary Human Macrophages
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P2860
The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particles
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 10 July 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The amphipathic helix of influ ...... entous and spherical particles
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The amphipathic helix of influ ...... ntous and spherical particles.
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type
label
The amphipathic helix of influ ...... entous and spherical particles
@en
The amphipathic helix of influ ...... ntous and spherical particles.
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prefLabel
The amphipathic helix of influ ...... entous and spherical particles
@en
The amphipathic helix of influ ...... ntous and spherical particles.
@nl
P2093
P2860
P356
P1433
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The amphipathic helix of influ ...... entous and spherical particles
@en
P2093
Chunlong Ma
George P Leser
Kari L Roberts
Robert A Lamb
P2860
P304
P356
10.1128/JVI.01363-13
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P577
2013-07-10T00:00:00Z