GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity.
about
A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2.The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionSynchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesGeranylgeranylated SNAREs are dominant inhibitors of membrane fusionSpecific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation.Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes.Tension of membranes expressing the hemagglutinin of influenza virus inhibits fusion.Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin.Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusionThe lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion poresBoth MHC class II and its GPI-anchored form undergo hop diffusion as observed by single-molecule trackingIminosugars: Promising therapeutics for influenza infection.Mutations in the fusion peptide and adjacent heptad repeat inhibit folding or activity of the Newcastle disease virus fusion proteinNegative potentials across biological membranes promote fusion by class II and class III viral proteinsMeta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin.Hemifusion between cells expressing hemagglutinin of influenza virus and planar membranes can precede the formation of fusion pores that subsequently fully enlargeDelay of influenza hemagglutinin refolding into a fusion-competent conformation by receptor binding: a hypothesisThe nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.Compensatory evolution of net-charge in influenza A virus hemagglutinin.Newcastle disease virus HN protein alters the conformation of the F protein at cell surfacesClass I and class II viral fusion protein structures reveal similar principles in membrane fusion.Evidence for mixed membrane topology of the newcastle disease virus fusion protein.Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusionAdvances in animal cell recombinant protein production: GS-NS0 expression system.Modifications of cysteine residues in the transmembrane and cytoplasmic domains of a recombinant hemagglutinin protein prevent cross-linked multimer formation and potency lossThiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.Truncation of the COOH-terminal region of the paramyxovirus SV5 fusion protein leads to hemifusion but not complete fusionAn early stage of membrane fusion mediated by the low pH conformation of influenza hemagglutinin depends upon membrane lipids.Uncoupled expression of Moloney murine leukemia virus envelope polypeptides SU and TM: a functional analysis of the role of TM domains in viral entry.Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein.P element insertion-dependent gene activation in the Drosophila eye.The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.Construction and characterization of secreted and chimeric transmembrane forms of Drosophila acetylcholinesterase: a large truncation of the C-terminal signal peptide does not eliminate glycoinositol phospholipid anchoring.GPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity.Hendra virus fusion protein transmembrane domain contributes to pre-fusion protein stability.Evidences for the existence of intermolecular disulfide-bonded oligomers in the H3 hemagglutinins expressed in insect cells.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.
P2860
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P2860
GPI- and transmembrane-anchored influenza hemagglutinin differ in structure and receptor binding activity.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
GPI- and transmembrane-anchore ...... and receptor binding activity.
@ast
GPI- and transmembrane-anchore ...... and receptor binding activity.
@en
type
label
GPI- and transmembrane-anchore ...... and receptor binding activity.
@ast
GPI- and transmembrane-anchore ...... and receptor binding activity.
@en
prefLabel
GPI- and transmembrane-anchore ...... and receptor binding activity.
@ast
GPI- and transmembrane-anchore ...... and receptor binding activity.
@en
P2860
P356
P1476
GPI- and transmembrane-anchore ...... and receptor binding activity
@en
P2093
P2860
P304
P356
10.1083/JCB.122.6.1253
P407
P50
P577
1993-09-01T00:00:00Z