Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.
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Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStudies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.Reovirus FAST Proteins Drive Pore Formation and Syncytiogenesis Using a Novel Helix-Loop-Helix Fusion-Inducing Lipid Packing SensorSequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoproteinFUS1 regulates the opening and expansion of fusion pores between mating yeast.Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement.Kinetically differentiating influenza hemagglutinin fusion and hemifusion machines.Murine leukemia virus R Peptide inhibits influenza virus hemagglutinin-induced membrane fusion.Rational site-directed mutations of the LLP-1 and LLP-2 lentivirus lytic peptide domains in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41 indicate common functions in cell-cell fusion but distinct roles in virion envelope incThe final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusionProgressive truncations C terminal to the membrane-spanning domain of simian immunodeficiency virus Env reduce fusogenicity and increase concentration dependence of Env for fusion.Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.Lipid interaction of the C terminus and association of the transmembrane segments facilitate atlastin-mediated homotypic endoplasmic reticulum fusion.Class II fusion protein of alphaviruses drives membrane fusion through the same pathway as class I proteins.Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation.The 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.Intrinsic temperature sensitivity of influenza C virus hemagglutinin-esterase-fusion protein.Evidences for the existence of intermolecular disulfide-bonded oligomers in the H3 hemagglutinins expressed in insect cells.Helix-destabilizing, beta-branched, and polar residues in the baboon reovirus p15 transmembrane domain influence the modularity of FAST proteins.Varicella-zoster Virus gB and gE coexpression, but not gB or gE alone, leads to abundant fusion and syncytium formation equivalent to those from gH and gL coexpression.Fatty acids on the A/USSR/77 influenza virus hemagglutinin facilitate the transition from hemifusion to fusion pore formation.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.A histidine residue of the influenza virus hemagglutinin controls the pH dependence of the conformational change mediating membrane fusion.Multifaceted sequence-dependent and -independent roles for reovirus FAST protein cytoplasmic tails in fusion pore formation and syncytiogenesis.Influence of additional acylation site(s) of influenza B virus hemagglutinin on syncytium formation.Peptide mimics of the vesicular stomatitis virus G-protein transmembrane segment drive membrane fusion in vitro.
P2860
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P2860
Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.
description
2000 nî lūn-bûn
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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name
Modification of the cytoplasmi ...... nlargement of the fusion pore.
@en
Modification of the cytoplasmi ...... nlargement of the fusion pore.
@nl
type
label
Modification of the cytoplasmi ...... nlargement of the fusion pore.
@en
Modification of the cytoplasmi ...... nlargement of the fusion pore.
@nl
prefLabel
Modification of the cytoplasmi ...... nlargement of the fusion pore.
@en
Modification of the cytoplasmi ...... nlargement of the fusion pore.
@nl
P2093
P2860
P1433
P1476
Modification of the cytoplasmi ...... nlargement of the fusion pore.
@en
P2093
Herrmann A
Kozerski C
Ponimaskin E
Schmidt MF
Schroth-Diez B
P2860
P304
P356
10.1128/JVI.74.16.7529-7537.2000
P407
P577
2000-08-01T00:00:00Z