Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus.
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Fusion of Rous sarcoma virus with host cells does not require exposure to low pHThe central proline of an internal viral fusion peptide serves two important rolesEntry and uncoating of enveloped virusesMutational Evidence for an Internal Fusion Peptide in Flavivirus Envelope Protein EA fusion-defective mutant of the vesicular stomatitis virus glycoproteinMutagenesis of the putative fusion domain of the Semliki Forest virus spike proteinConformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatmentThe complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interfaceInsight into Highly Conserved H1 Subtype-Specific Epitopes in Influenza Virus HemagglutininStudies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.Implicit solvent model studies of the interactions of the influenza hemagglutinin fusion peptide with lipid bilayers.Interaction of synthetic HA2 influenza fusion peptide analog with model membranesCharacterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopyA specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotypeMembrane Fusion and Infection of the Influenza Hemagglutinin.Structural basis of influenza virus neutralization.Passive immune neutralization strategies for prevention and control of influenza A infections.Cell-based analysis of Chikungunya virus E1 protein in membrane fusion.Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.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.Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity.Activation of a retroviral membrane fusion protein: soluble receptor-induced liposome binding of the ALSV envelope glycoprotein.Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers.Mutational analysis of the candidate internal fusion peptide of the avian leukosis and sarcoma virus subgroup A envelope glycoprotein.Properties and structures of the influenza and HIV fusion peptides on lipid membranes: implications for a role in fusionThe amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH. Oligomerization and the conformational flexibility.A Moloney murine leukemia virus-based retroviral vector pseudotyped by the insect retroviral gypsy envelope can infect Drosophila cells.Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike proteinHelical hairpin structure of influenza hemagglutinin fusion peptide stabilized by charge-dipole interactions between the N-terminal amino group and the second helix.Mutational analysis of the putative fusion domain of Ebola virus glycoprotein.Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement.Interaction of the influenza hemagglutinin fusion peptide with lipid bilayers: area expansion and permeation.The influenza hemagglutinin precursor as an acid-sensitive probe of the biosynthetic pathway.Order and disorder control the functional rearrangement of influenza hemagglutinin.Analyzing the fusion process of influenza hemagglutinin by mutagenesis and molecular modeling.Micropipette manipulation technique for the monitoring of pH-dependent membrane lysis as induced by the fusion peptide of influenza virus
P2860
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P2860
Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Studies on the mechanism of me ...... agglutinin of influenza virus.
@ast
Studies on the mechanism of me ...... agglutinin of influenza virus.
@en
type
label
Studies on the mechanism of me ...... agglutinin of influenza virus.
@ast
Studies on the mechanism of me ...... agglutinin of influenza virus.
@en
prefLabel
Studies on the mechanism of me ...... agglutinin of influenza virus.
@ast
Studies on the mechanism of me ...... agglutinin of influenza virus.
@en
P2093
P2860
P356
P1476
Studies on the mechanism of me ...... agglutinin of influenza virus.
@en
P2093
P2860
P356
10.1083/JCB.102.1.11
P407
P577
1986-01-01T00:00:00Z