Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin.
about
Chemoenzymatic site-specific labeling of influenza glycoproteins as a tool to observe virus budding in real timeAmino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusionRole of the cytoplasmic tail of ecotropic moloney murine leukemia virus Env protein in fusion pore formation.Mutations in the cytoplasmic tail of murine leukemia virus envelope protein suppress fusion inhibition by R peptide.Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement.Mutations in the cytoplasmic domain of a paramyxovirus fusion glycoprotein rescue syncytium formation and eliminate the hemagglutinin-neuraminidase protein requirement for membrane fusionThe baculovirus GP64 protein mediates highly stable infectivity of a human respiratory syncytial virus lacking its homologous transmembrane glycoproteinsMurine leukemia virus R Peptide inhibits influenza virus hemagglutinin-induced membrane fusion.Activation of fusion by the SER virus F protein: a low-pH-dependent paramyxovirus entry process.Effect of extension of the cytoplasmic domain of human immunodeficiency type 1 virus transmembrane protein gp41 on virus replication.Tight binding of influenza virus hemagglutinin to its receptor interferes with fusion pore dilationModification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.C-terminal tyrosine residues modulate the fusion activity of the Hendra virus fusion protein.Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore 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.Multifaceted sequence-dependent and -independent roles for reovirus FAST protein cytoplasmic tails in fusion pore formation and syncytiogenesis.A chimeric respiratory syncytial virus fusion protein functionally replaces the F and HN glycoproteins in recombinant Sendai virus.
P2860
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P2860
Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Elongation of the cytoplasmic ...... influenza virus hemagglutinin.
@en
Elongation of the cytoplasmic ...... influenza virus hemagglutinin.
@nl
type
label
Elongation of the cytoplasmic ...... influenza virus hemagglutinin.
@en
Elongation of the cytoplasmic ...... influenza virus hemagglutinin.
@nl
prefLabel
Elongation of the cytoplasmic ...... influenza virus hemagglutinin.
@en
Elongation of the cytoplasmic ...... influenza virus hemagglutinin.
@nl
P2093
P2860
P1433
P1476
Elongation of the cytoplasmic ...... influenza virus hemagglutinin.
@en
P2093
P2860
P304
P407
P577
1998-05-01T00:00:00Z