Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
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A conserved proline in the last transmembrane segment of Gaa1 is required for glycosylphosphatidylinositol (GPI) recognition by GPI transamidaseTransmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion.Lipid-anchored SNAREs lacking transmembrane regions fully support membrane fusion during neurotransmitter releaseHerpesvirus gB: A Finely Tuned Fusion MachineEntry and uncoating of enveloped virusesCharacterization of a Structural Intermediate of Flavivirus Membrane FusionTransmembrane Domains of Hepatitis C Virus Envelope Glycoproteins: Residues Involved in E1E2 Heterodimerization and Involvement of These Domains in Virus EntryA Virus-Encoded Cell–Cell Fusion Machine Dependent on Surrogate AdhesinsViral membrane fusionStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeFunctional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane FusionCrystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteinsStructure of the dengue virus envelope protein after membrane fusionMolecular mechanism of the synaptotagmin–SNARE interaction in Ca2+-triggered vesicle fusionThe complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interfaceMembrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.Hemifusion in SNARE-mediated membrane fusion.Viral membrane fusion.The anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA.Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.Interaction of synthetic HA2 influenza fusion peptide analog with model membranesBiochemical reconstitution of hemorrhagic-fever arenavirus envelope glycoprotein-mediated membrane fusionEvidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusionMolecular and cellular aspects of rhabdovirus entryHemagglutinin Spatial Distribution Shifts in Response to Cholesterol in the Influenza Viral Envelope.A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotypeThe transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionRecombinant influenza A H3N2 viruses with mutations of HA transmembrane cysteines exhibited altered virological characteristics.Membrane Fusion and Infection of the Influenza Hemagglutinin.Multiphasic effects of cholesterol on influenza fusion kinetics reflect multiple mechanistic roles.The transmembrane domain and acidic lipid flip-flop regulates voltage-dependent fusion mediated by class II and III viral proteins.Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational modelsViral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41.Raft protein clustering alters N-Ras membrane interactions and activation pattern.A bundling of viral fusion mechanisms.Emerging antiviral strategies to interfere with influenza virus entry.Reevaluating herpes simplex virus hemifusion.Different domains regulate homomeric and heteromeric complex formation among type I and type II transforming growth factor-beta receptors.Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.
P2860
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P2860
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh-hant
name
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
@en
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
@nl
type
label
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
@en
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
@nl
prefLabel
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
@en
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
@nl
P2093
P1433
P1476
Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion.
@en
P2093
P304
P356
10.1016/0092-8674(94)90344-1
P407
P577
1994-01-01T00:00:00Z