Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.
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The C terminus of the B5 receptor for herpes simplex virus contains a functional region important for infection.Attenuation of Murray Valley encephalitis virus by site-directed mutagenesis of the hinge and putative receptor-binding regions of the envelope protein.Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeInteractions between HIV-1 gp41 core and detergents and their implications for membrane fusionStructural Characterization of an Early Fusion Intermediate of Influenza Virus HemagglutininMembrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p.Comprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.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 transitionMutagenesis studies of the H5 influenza hemagglutinin stem loop region.A Potent Anti-influenza Compound Blocks Fusion through Stabilization of the Prefusion Conformation of the Hemagglutinin ProteinpH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.New insights into the spring-loaded conformational change of influenza virus hemagglutinin.Conformational intermediates and fusion activity of influenza virus hemagglutinin.Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1.SNARE motif: a common motif used by pathogens to manipulate membrane fusionSpring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore.Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion.Membrane fusion mediated by coiled coils: a hypothesis.Stochastic simulation of hemagglutinin-mediated fusion pore formation.Functional motions of influenza virus hemagglutinin: a structure-based analytical approach.Protonation and stability of the globular domain of influenza virus hemagglutinin.Molecular dynamics simulation of the evolution of hydrophobic defects in one monolayer of a phosphatidylcholine bilayer: relevance for membrane fusion mechanisms.Dynamic changes during acid-induced activation of influenza hemagglutinin.Structure of influenza haemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy.Lysolipids do not inhibit influenza virus fusion by interaction with hemagglutinin.Rotation-Activated and Cooperative Zipping Characterize Class I Viral Fusion Protein Dynamics.
P2860
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P2860
Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Specific single or double prol ...... lish membrane fusion activity.
@ast
Specific single or double prol ...... lish membrane fusion activity.
@en
type
label
Specific single or double prol ...... lish membrane fusion activity.
@ast
Specific single or double prol ...... lish membrane fusion activity.
@en
prefLabel
Specific single or double prol ...... lish membrane fusion activity.
@ast
Specific single or double prol ...... lish membrane fusion activity.
@en
P2093
P2860
P356
P1476
Specific single or double prol ...... lish membrane fusion activity.
@en
P2093
P2860
P304
P356
10.1083/JCB.141.6.1335
P407
P577
1998-06-01T00:00:00Z