Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions.
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Coronavirus particle assembly: primary structure requirements of the membrane protein.Novel approach to the development of effective H5N1 influenza A virus vaccines: use of M2 cytoplasmic tail mutants.The membrane-proximal stem region of vesicular stomatitis virus G protein confers efficient virus assembly.Influenza A virus can undergo multiple cycles of replication without M2 ion channel activity.The NB protein of influenza B virus is not necessary for virus replication in vitro.Immunogenicity of a recombinant influenza virus bearing both the CD4+ and CD8+ T cell epitopes of ovalbumin.Chimeric influenza A viruses with a functional influenza B virus neuraminidase or hemagglutinin.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.Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particlesAn internalization signal in the simian immunodeficiency virus transmembrane protein cytoplasmic domain modulates expression of envelope glycoproteins on the cell surfaceThe 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.Reverse genetics provides direct evidence for a correlation of hemagglutinin cleavability and virulence of an avian influenza A virus.The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.Mechanisms for enveloped virus budding: can some viruses do without an ESCRT?A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for buddingThe influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity.A single amino acid change in the cytoplasmic domain of the simian immunodeficiency virus transmembrane molecule increases envelope glycoprotein expression on infected cellsInfluenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein.Expression of a foreign protein by influenza A virus.Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope.Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza a virus neuraminidase in raft association and virus budding.The cytoplasmic domain of Marburg virus GP modulates early steps of viral infection.
P2860
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P2860
Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Mutations in the cytoplasmic t ...... ct incorporation into virions.
@ast
Mutations in the cytoplasmic t ...... ct incorporation into virions.
@en
type
label
Mutations in the cytoplasmic t ...... ct incorporation into virions.
@ast
Mutations in the cytoplasmic t ...... ct incorporation into virions.
@en
prefLabel
Mutations in the cytoplasmic t ...... ct incorporation into virions.
@ast
Mutations in the cytoplasmic t ...... ct incorporation into virions.
@en
P2093
P2860
P1433
P1476
Mutations in the cytoplasmic t ...... ct incorporation into virions.
@en
P2093
M R Castrucci
P2860
P304
P407
P577
1993-11-01T00:00:00Z