The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles.
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Viral membrane scissionMulti-Omics Studies towards Novel Modulators of Influenza A Virus-Host InteractionSpecific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitroPhytochemicals attenuating aberrant activation of β-catenin in cancer cellsInvolvement of an Arginine Triplet in M1 Matrix Protein Interaction with Membranes and in M1 Recruitment into Virus-Like Particles of the Influenza A(H1N1)pdm09 Virus.Three-dimensional analysis of ribonucleoprotein complexes in influenza A virusInfluenza A virus uses intercellular connections to spread to neighboring cellsA crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domainAt low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane.Influenza virus assembly and budding.Structural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and MorphologyThe highly conserved arginine residues at positions 76 through 78 of influenza A virus matrix protein M1 play an important role in viral replication by affecting the intracellular localization of M1Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.pH-Dependent Formation and Disintegration of the Influenza A Virus Protein Scaffold To Provide Tension for Membrane FusionIn vitro and in vivo replication of influenza A H1N1 WSN33 viruses with different M1 proteins.The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particlesProtein-lipid interactions critical to replication of the influenza A virus.The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.Association of influenza virus proteins with membrane rafts.Selective incorporation of vRNP into influenza A virions determined by its specific interaction with M1 protein.A leucine residue in the C terminus of human parainfluenza virus type 3 matrix protein is essential for efficient virus-like particle and virion release.Interaction of influenza A virus matrix protein with RACK1 is required for virus release.Application of a split luciferase complementation assay for the detection of viral protein-protein interactionsBudding capability of the influenza virus neuraminidase can be modulated by tetherinUn-“ESCRT”-ed budding.Influenza A Virus Hemagglutinin is Required for the Assembly of Viral Components Including Bundled vRNPs at the Lipid Raft.Influenza A matrix protein M1 multimerizes upon binding to lipid membranes.Nuclear localization of influenza B polymerase proteins and their binary complexes.Alterations of membrane curvature during influenza virus budding.Co-evolution analysis to predict protein-protein interactions within influenza virus envelope.Intrinsic cytoskeleton-dependent clustering of influenza virus M2 protein with hemagglutinin assessed by FLIM-FRET.A Budding-Defective M2 Mutant Exhibits Reduced Membrane Interaction, Insensitivity to Cholesterol, and Perturbed Interdomain Coupling.Formation of virus-like particles from human cell lines exclusively expressing Influenza Neuraminidase.A Defect in Influenza A Virus Particle Assembly Specific to Primary Human Macrophages
P2860
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P2860
The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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name
The lack of an inherent membra ...... bud into virus-like particles.
@en
The lack of an inherent membra ...... for the failure of the matrix
@nl
type
label
The lack of an inherent membra ...... bud into virus-like particles.
@en
The lack of an inherent membra ...... for the failure of the matrix
@nl
prefLabel
The lack of an inherent membra ...... bud into virus-like particles.
@en
The lack of an inherent membra ...... for the failure of the matrix
@nl
P2093
P2860
P356
P1433
P1476
The lack of an inherent membra ...... bud into virus-like particles
@en
P2093
Aaron Harmon
David H Francis
Eric Nelson
Jane Christopher-Hennings
Ronald C Montelaro
P2860
P304
P356
10.1128/JVI.02306-09
P407
P577
2010-02-24T00:00:00Z