Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
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Coronavirus particle assembly: primary structure requirements of the membrane protein.The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatusGPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes.Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA.Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape.Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.Quantitative measurement of paramyxovirus fusion: differences in requirements of glycoproteins between simian virus 5 and human parainfluenza virus 3 or Newcastle disease virus.Differences in the role of the cytoplasmic domain of human parainfluenza virus fusion proteins.Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions.Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivityTruncation of the COOH-terminal region of the paramyxovirus SV5 fusion protein leads to hemifusion but not complete fusionPostassembly cleavage of a retroviral glycoprotein cytoplasmic domain removes a necessary incorporation signal and activates fusion activity.Influenza virus M2 protein ion channel activity stabilizes the native form of fowl plague virus hemagglutinin during intracellular transportAn influenza A (H1N1) virus, closely related to swine influenza virus, responsible for a fatal case of human influenzaBasis for selective incorporation of glycoproteins into the influenza virus envelopeMutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions.Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivityEffects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutininThe influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity.Influenza A virus hemagglutinin and neuraminidase mutually accelerate their apical targeting through clustering of lipid rafts.Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro.The YXXL sequences of a transmembrane protein of bovine leukemia virus are required for viral entry and incorporation of viral envelope protein into virions.Fusion 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.Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.Importance of the cytoplasmic tails of the measles virus glycoproteins for fusogenic activity and the generation of recombinant measles viruses.Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation.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.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.
P2860
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P2860
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
@ast
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
@en
type
label
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
@ast
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
@en
prefLabel
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
@ast
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
@en
P2860
P1433
P1476
Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity.
@en
P2093
D A Simpson
P2860
P304
P407
P577
1992-02-01T00:00:00Z