Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.
about
Fusogenic pairings of vesicle-associated membrane proteins (VAMPs) and plasma membrane t-SNAREs--VAMP5 as the exceptionThe C terminus of the B5 receptor for herpes simplex virus contains a functional region important for infection.Viral and developmental cell fusion mechanisms: conservation and divergenceCell entry of enveloped virusesCell fusion activity of hepatitis C virus envelope proteinsFunctional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.Molecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein.Viral membrane fusionStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeCore structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolutionCrystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteinspH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMRMembrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.Fusion of Enveloped Viruses in Endosomes.Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structureThe anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA.Comprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.Interaction of synthetic HA2 influenza fusion peptide analog with model membranesIdentification of Influenza A/PR/8/34 Donor Viruses Imparting High Hemagglutinin Yields to Candidate Vaccine Viruses in EggsCrystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblyBiochemical characterization of nuclear pore complex protein gp210 oligomersFormation of a yeast SNARE complex is accompanied by significant structural changesVirus membrane-fusion proteins: more than one way to make a hairpinHemagglutinin 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 transitionViral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level.Membrane Fusion and Infection of the Influenza Hemagglutinin.Multiphasic effects of cholesterol on influenza fusion kinetics reflect multiple mechanistic roles.Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoproteinMembrane 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.Synchronized 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.Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusionpH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.
P2860
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P2860
Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.
description
1996 nî lūn-bûn
@nan
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Membrane fusion mediated by th ...... t three hemagglutinin trimers.
@ast
Membrane fusion mediated by th ...... t three hemagglutinin trimers.
@en
type
label
Membrane fusion mediated by th ...... t three hemagglutinin trimers.
@ast
Membrane fusion mediated by th ...... t three hemagglutinin trimers.
@en
prefLabel
Membrane fusion mediated by th ...... t three hemagglutinin trimers.
@ast
Membrane fusion mediated by th ...... t three hemagglutinin trimers.
@en
P2093
P2860
P356
P1476
Membrane fusion mediated by th ...... t three hemagglutinin trimers.
@en
P2093
S L Pelletier
P2860
P304
P356
10.1083/JCB.133.3.559
P407
P577
1996-05-01T00:00:00Z