Basis for selective incorporation of glycoproteins into the influenza virus envelope
about
Chimeric measles viruses with a foreign envelopeCoronavirus particle assembly: primary structure requirements of the membrane protein.Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusionThe 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.The membrane-proximal stem region of vesicular stomatitis virus G protein confers efficient virus assembly.Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 proteinMeasles viruses with altered envelope protein cytoplasmic tails gain cell fusion competence.Measles virus matrix protein specifies apical virus release and glycoprotein sorting in epithelial cells.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.Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivityAssociation of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells.An internalization signal in the simian immunodeficiency virus transmembrane protein cytoplasmic domain modulates expression of envelope glycoproteins on the cell surfaceMutations at palmitylation sites of the influenza virus hemagglutinin affect virus formationMutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions.Attenuated measles virus as a vaccine vector.Membrane-tethered ligands are effective probes for exploring class B1 G protein-coupled receptor function.The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity.Use of a mammalian internal ribosomal entry site element for expression of a foreign protein by a transfectant influenza virus.Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein.Plasmid-driven formation of influenza virus-like particles.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.Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope.
P2860
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P2860
Basis for selective incorporation of glycoproteins into the influenza virus envelope
description
1993 nî lūn-bûn
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1993年の論文
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1993年論文
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1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
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1993年论文
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1993年论文
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1993年论文
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name
Basis for selective incorporation of glycoproteins into the influenza virus envelope
@ast
Basis for selective incorporation of glycoproteins into the influenza virus envelope
@en
type
label
Basis for selective incorporation of glycoproteins into the influenza virus envelope
@ast
Basis for selective incorporation of glycoproteins into the influenza virus envelope
@en
prefLabel
Basis for selective incorporation of glycoproteins into the influenza virus envelope
@ast
Basis for selective incorporation of glycoproteins into the influenza virus envelope
@en
P2860
P1433
P1476
Basis for selective incorporation of glycoproteins into the influenza virus envelope
@en
P2093
P2860
P304
P407
P577
1993-08-01T00:00:00Z