The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication.
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Coronavirus particle assembly: primary structure requirements of the membrane protein.The packaging signal of influenza viral RNA molecules.The M segment of the 2009 pandemic influenza virus confers increased neuraminidase activity, filamentous morphology, and efficient contact transmissibility to A/Puerto Rico/8/1934-based reassortant virusesThe M2 ectodomain is important for its incorporation into influenza A virions.Cytoplasmic domain of Sendai virus HN protein contains a specific sequence required for its incorporation into virions.Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins.Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus.Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 proteinVirus maturation by budding.Measles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence.Requirements for budding of paramyxovirus simian virus 5 virus-like particles.Ebola virus VP40 drives the formation of virus-like filamentous particles along with GPRoles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5.Type II transmembrane domain hydrophobicity dictates the cotranslational dependence for inversion.Filament-producing mutants of influenza A/Puerto Rico/8/1934 (H1N1) virus have higher neuraminidase activities than the spherical wild-type.NP body domain and PB2 contribute to increased virulence of H5N1 highly pathogenic avian influenza viruses in chickens.The cytoplasmic tail of the influenza A virus M2 protein plays a role in viral assembly.Conserved elements of the RAM signaling pathway establish cell polarity in the basidiomycete Cryptococcus neoformans in a divergent fashion from other fungi.Selecting vaccine strains for H3N2 human influenza A virus.Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells.Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particlesHost cell dependence of viral morphology.The cytoplasmic tail domain of influenza B virus hemagglutinin is important for its incorporation into virions but is not essential for virus replication in cell culture in the presence of compensatory mutations.Cytoplasmic domain of influenza B virus BM2 protein plays critical roles in production of infectious virus.Molecular mechanisms underlying oseltamivir resistance mediated by an I117V substitution in the neuraminidase of subtype H5N1 avian influenza A viruses.Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site.The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.An eight-segment swine influenza virus harboring H1 and H3 hemagglutinins is attenuated and protective against H1N1 and H3N2 subtypes in pigs.Mapping the sequence mutations of the 2009 H1N1 influenza A virus neuraminidase relative to drug and antibody binding sites.Molecular determinants within the surface proteins involved in the pathogenicity of H5N1 influenza viruses in chickens.Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics.Lateral Organization of Influenza Virus Proteins in the Budozone Region of the Plasma Membrane.Filamentous influenza viruses.A Perspective on the Structural and Functional Constraints for Immune Evasion: Insights from Influenza Virus.Plasmid-driven formation of influenza virus-like particles.Influenza virus matrix protein is the major driving force in virus budding.Lipid rafts and pseudotyping.Budding capability of the influenza virus neuraminidase can be modulated by tetherin
P2860
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P2860
The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
The cytoplasmic tail of influe ...... sential for virus replication.
@ast
The cytoplasmic tail of influe ...... sential for virus replication.
@en
type
label
The cytoplasmic tail of influe ...... sential for virus replication.
@ast
The cytoplasmic tail of influe ...... sential for virus replication.
@en
prefLabel
The cytoplasmic tail of influe ...... sential for virus replication.
@ast
The cytoplasmic tail of influe ...... sential for virus replication.
@en
P2093
P2860
P1433
P1476
The cytoplasmic tail of influe ...... ssential for virus replication
@en
P2093
L J Mitnaul
M R Castrucci
P2860
P304
P407
P577
1996-02-01T00:00:00Z