Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity
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Adaptive mutations in Sindbis virus E2 and Ross River virus E1 that allow efficient budding of chimeric virusesStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeInfluenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.Formation of raft-like assemblies within clusters of influenza hemagglutinin observed by MD simulationsProtein intrinsic disorder toolbox for comparative analysis of viral proteins.Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins.Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 proteinInfluenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.Palmitoylations on murine coronavirus spike proteins are essential for virion assembly and infectivity.Modifications of cysteine residues in the transmembrane and cytoplasmic domains of a recombinant hemagglutinin protein prevent cross-linked multimer formation and potency lossHeterogeneity of early intermediates in cell-liposome fusion mediated by influenza hemagglutinin.Recombinant parainfluenza virus 5 (PIV5) expressing the influenza A virus hemagglutinin provides immunity in mice to influenza A virus challengeInfluence of calcium on lipid mixing mediated by influenza hemagglutininTruncation of the COOH-terminal region of the paramyxovirus SV5 fusion protein leads to hemifusion but not complete fusionFusion activity of transmembrane and cytoplasmic domain chimeras of the influenza virus glycoprotein hemagglutinin.Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin.Measles virus fusion protein is palmitoylated on transmembrane-intracytoplasmic cysteine residues which participate in cell fusion.Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein.Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation.Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein.A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein.Receptor-like Molecules on Human Intestinal Epithelial Cells Interact with an Adhesion Factor from Lactobacillus reuteri.Palmitoylation, membrane-proximal basic residues, and transmembrane glycine residues in the reovirus p10 protein are essential for syncytium formation.Influence of acylation sites of influenza B virus hemagglutinin on fusion pore formation and dilation.Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity.The carboxy-terminal domain of glycoprotein N of human cytomegalovirus is required for virion morphogenesis.Recombinant influenza H9N2 virus with a substitution of H3 hemagglutinin transmembrane domain showed enhanced immunogenicity in mice and chicken.
P2860
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P2860
Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity
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
Palmitylation of the influenza ...... virus assembly or infectivity
@ast
Palmitylation of the influenza ...... virus assembly or infectivity
@en
type
label
Palmitylation of the influenza ...... virus assembly or infectivity
@ast
Palmitylation of the influenza ...... virus assembly or infectivity
@en
prefLabel
Palmitylation of the influenza ...... virus assembly or infectivity
@ast
Palmitylation of the influenza ...... virus assembly or infectivity
@en
P2093
P2860
P1433
P1476
Palmitylation of the influenza ...... virus assembly or infectivity
@en
P2093
P2860
P304
P407
P577
1996-03-01T00:00:00Z